DrugMAP Full Data Download File Title - DrugMAP drug therapeutic target (DTT) information in raw format Version 1.01 (2022.07.20) Provided by Lab of Innovative Drug Reasearch and Bioinformatics (IDRB) College of Pharmaceutical Sciences Zhejiang University https://idrblab.org/ Any question about data provided here, please contact with: Dr. Li (lifengcheng@zju.edu.cn) and Dr. Yin (yinjiayi@zju.edu.cn) ID: DTT_ID TN: DTT_Name UP: Uniprot_ID UC: Uniprot_ID_HUMAN BC: BioChemical_Class SN: Synonyms GN: Gene_Name FC: Function EC: EC_Number PD: PDB_Structure SQ: Sequence TT: DTT_type FM: Family KE: KEGG_pathway RC: Reactome TTGKNB4 ID TTGKNB4 TTGKNB4 TN Epidermal growth factor receptor (EGFR) TTGKNB4 UP P00533 TTGKNB4 UC EGFR_HUMAN TTGKNB4 BC Kinase TTGKNB4 SN Receptor tyrosine-protein kinase erbB-1; Proto-oncogene c-ErbB-1; HER1; ERBB1; ERBB TTGKNB4 GN EGFR TTGKNB4 FC Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Plays a role in enhancing learning and memory performance (By similarity). TTGKNB4 EC EC 2.7.10.1 TTGKNB4 PD 6D8E; 6B3S; 6ARU; 5ZWJ; 5YU9 TTGKNB4 SQ MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA TTGKNB4 TT Successful TTGKNB4 FM Kinase TTGKNB4 KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04320:Dorso-ventral axis formation; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04540:Gap junction; hsa04810:Regulation of actin cytoskeleton; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05160:Hepatitis C; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTGKNB4 RC R-HSA-1236382:Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1250196:SHC1 events in ERBB2 signaling; R-HSA-1251932:PLCG1 events in ERBB2 signaling; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-179812:GRB2 events in EGFR signaling; R-HSA-180292:GAB1 signalosome; R-HSA-180336:SHC1 events in EGFR signaling; R-HSA-182971:EGFR downregulation; R-HSA-1963640:GRB2 events in ERBB2 signaling; R-HSA-1963642:PI3K events in ERBB2 signaling; R-HSA-2179392:EGFR Transactivation by Gastrin; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5637810:Constitutive Signaling by EGFRvIII; R-HSA-5673001:RAF/MAP kinase cascade TTRLW2X ID TTRLW2X TTRLW2X TN Fibroblast growth factor receptor 1 (FGFR1) TTRLW2X UP P11362 TTRLW2X UC FGFR1_HUMAN TTRLW2X BC Kinase TTRLW2X SN c-fgr; bFGF-R-1; bFGF-R; N-sam; HBGFR; Fms-like tyrosine kinase 2; FLT2; FLT-2; FLG; FGFR-1; FGFBR; CEK; CD331 antigen; CD331; Basic fibroblast growth factor receptor 1; BFGFR TTRLW2X GN FGFR1 TTRLW2X FC Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation. Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. TTRLW2X EC EC 2.7.10.1 TTRLW2X PD 6MZW; 6MZQ; 6C1O; 6C1C; 6C1B TTRLW2X SQ MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLKRR TTRLW2X TT Successful TTRLW2X FM Kinase TTRLW2X KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04520:Adherens junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05230:Central carbon metabolism in cancer TT9SL3Q ID TT9SL3Q TT9SL3Q TN Polypeptide deformylase (PDF) TT9SL3Q UP Q9HBH1 TT9SL3Q UC DEFM_HUMAN TT9SL3Q BC CH-NH donor oxidoreductase TT9SL3Q SN PDF TT9SL3Q GN PDF TT9SL3Q FC Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP. TT9SL3Q EC EC 3.5.1.88 TT9SL3Q PD 3G5P; 3G5K TT9SL3Q SQ MARLWGALSLWPLWAAVPWGGAAAVGVRACSSTAAPDGVEGPALRRSYWRHLRRLVLGPPEPPFSHVCQVGDPVLRGVAAPVERAQLGGPELQRLTQRLVQVMRRRRCVGLSAPQLGVPRQVLALELPEALCRECPPRQRALRQMEPFPLRVFVNPSLRVLDSRLVTFPEGCESVAGFLACVPRFQAVQISGLDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSRTFTNVYWMKVND TT9SL3Q TT Successful TT9SL3Q RC R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-1474151:Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation; R-HSA-196757:Metabolism of folate and pterines; R-HSA-69205:G1/S-Specific Transcription TT1D53B ID TT1D53B TT1D53B TN COVID-19 3C-like protease (3CLpro) TT1D53B UP P0DTD1 (3264-3569) TT1D53B UC R1AB_SARS2 (3264-3569) TT1D53B BC Coronaviruses polyprotein 1ab family TT1D53B SN COVID-19 3CL-PRO; COVID-19 3CLp; COVID-19 nsp5 TT1D53B GN COVID-19 rep TT1D53B FC Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). TT1D53B EC EC 3.4.22.69 TT1D53B PD 5R7Y; 5R7Z; 5R80; 5R81; 5R82 TT1D53B SQ SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ TTNHMO8 ID TTNHMO8 TTNHMO8 TN COVID-19 papain-like proteinase (PL-PRO) TTNHMO8 UP P0DTD1 (819-2763) TTNHMO8 UC R1AB_SARS2 (819-2763) TTNHMO8 BC Coronaviruses polyprotein 1ab family TTNHMO8 SN COVID-19 papain-like proteinase; COVID-19 PL2-PRO; COVID-19 PL-PRO; COVID-19 main proteinase; COVID-19 non-structural protein 3 TTNHMO8 GN COVID-19 rep; COVID-19 1a-1b TTNHMO8 FC Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. TTNHMO8 EC EC 3.4.19.12 TTNHMO8 PD 5R7Y; 5R7Z; 5R80; 5R81; 5R82 TTNHMO8 SQ APTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVIKTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPLEFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVEQKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLKKDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSIISNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLNDLNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPYPNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNKATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPANNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRCLNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCLGSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTAFGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHVVDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVYYSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQGFVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPF TTV1095 ID TTV1095 TTV1095 TN COVID-19 RNA-directed RNA polymerase (RdRp) TTV1095 UP P0DTD1 (4393-5324) TTV1095 UC R1AB_SARS2 (4393-5324) TTV1095 BC Coronaviruses polyprotein 1ab family TTV1095 SN COVID-19 Pol; COVID-19 nsp12 TTV1095 GN COVID-19 rep; COVID-19 1a-1b TTV1095 FC Responsible for replication and transcription of the viral RNA genome. TTV1095 EC EC 2.7.7.48 TTV1095 PD 5R7Y; 5R7Z; 5R80; 5R81; 5R82 TTV1095 SQ SADAQSFLNRVCGVSAARLTPCGTGTSTDVVYRAFDIYNDKVAGFAKFLKTNCCRFQEKDEDDNLIDSYFVVKRHTFSNYQHEETIYNLLKDCPAVAKHDFFKFRIDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQALLKTVQFCDAMRNAGIVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDSYYSLLMPILTLTRALTAESHVDTDLTKPYIKWDLLKYDFTEERLKLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASLVLARKHTTCCSLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDTDFVNEFYAYLRKHFSMMILSDDAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQ TTN9A16 ID TTN9A16 TTN9A16 TN HUMAN adaptor-associated kinase 1 (AAK1) TTN9A16 UP Q2M2I8 TTN9A16 UC AAK1_HUMAN TTN9A16 BC Kinase TTN9A16 SN Adaptor-associated kinase 1 TTN9A16 GN AAK1 TTN9A16 FC Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity. TTN9A16 EC EC 2.7.11.1 TTN9A16 PD 5TE0; 5L4Q; 4WSQ TTN9A16 SQ MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKPQAPPSQPLPQTQAKQPQAPPTPQQTPSTQAQGLPAQAQATPQHQQQLFLKQQQQQQQPPPAQQQPAGTFYQQQQAQTQQFQAVHPATQKPAIAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQQQLATALHQQQLMTQQAALQQKPTMAAGQQPQPQPAAAPQPAPAQEPAIQAPVRQQPKVQTTPPPAVQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRTSQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQSTQGDAFATTSFSAGTAEKRKGGQTVDSGLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLLDCSLLSNPTTDLLEEFAPTAISAPVHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL TTGFNPD ID TTGFNPD TTGFNPD TN HUMAN angiotensin-converting enzyme (ACE) TTGFNPD UP P12821 TTGFNPD UC ACE_HUMAN TTGFNPD BC Glycosylase TTGFNPD SN Kininase II; Dipeptidyl carboxypeptidase I; DCP1; DCP; CD143 antigen; CD143; ACE TTGFNPD GN SLC33A1 TTGFNPD FC Able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. TTGFNPD EC EC 3.2.1.- TTGFNPD PD 6QS1; 6H5X; 6H5W; 6F9V; 6F9U TTGFNPD SQ MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSADEAGAQLFAQSYNSSAEQVLFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQAGSSRPWQEVLKDMVGLDALDAQPLLKYFQPVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQARVGQWLLLFLGIALLVATLGLSQRLFSIRHRSLHRHSHGPQFGSEVELRHS TTGFNPD FM Peptidase TT0AGBL ID TT0AGBL TT0AGBL TN HUMAN cyclin G-associated kinase (GAK) TT0AGBL UP O14976 TT0AGBL UC GAK_HUMAN TT0AGBL BC Ser/Thr protein kinase family TT0AGBL SN cyclin G associated kinase TT0AGBL GN GAK TT0AGBL FC Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1. TT0AGBL EC EC 2.7.11.1 TT0AGBL PD 4C57; 4C58; 4C59; 4Y8D; 5Y7Z TT0AGBL SQ MSLLQSALDFLAGPGSLGGASGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDVGSGREYALKRLLSNEEEKNRAIIQEVCFMKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEITRNTTPMYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAARNVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYMCDMVAEEPITPHSKPILVRAVVMTPVPLFSKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSREAPPWENSSMRGLNPKILFSSREEQQDILSKFGKPELPRQPGSTAQYDAGAGSPEAEPTDSDSPPSSSADASRFLHTLDWQEEKEAETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQEDGVDLLGLHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAWTETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPDPFADLGDLSSGLQGSPAGFPPGGFIPKTATTPKGSSSWQTSRPPAQGASWPPQAKPPPKACTQPRPNYASNFSVIGAREERGVRAPSFAQKPKVSENDFEDLLSNQGFSSRSDKKGPKTIAEMRKQDLAKDTDPLKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVGMADLVAPEQVKKHYRRAVLAVHPDKAAGQPYEQHAKMIFMELNDAWSEFENQGSRPLF TTF928K ID TTF928K TTF928K TN HUMAN dipeptidyl peptidase 4 (DPP-4) TTF928K UP P27487 TTF928K UC DPP4_HUMAN TTF928K BC Peptidase TTF928K SN Tcell activation antigen CD26; TP103; T-cell activation antigen CD26; Dipeptidyl peptidase IV; Dipeptidyl peptidase 4 soluble form; DPP-IV; DPP IV; DPP 4; CD26; Adenosine deaminase complexing protein-2; Adenosine deaminase complexing protein 2; ADCP2; ADCP-2; ADABP TTF928K GN DPP4 TTF928K FC Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. TTF928K EC EC 3.4.14.5 TTF928K PD 6B1O; 6B1E; 5ZID; 5Y7K; 5Y7J TTF928K SQ MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP TTF928K FM Peptidase TTWKB01 ID TTWKB01 TTWKB01 TN HUMAN janus kinase 1 (JAK-1) TTWKB01 UP P23458 TTWKB01 UC JAK1_HUMAN TTWKB01 BC Kinase TTWKB01 SN Tyrosine-protein kinase JAK1; JAK1B; JAK1A TTWKB01 GN JAK1 TTWKB01 FC Kinase partner for the interleukin (IL)-2 receptor as well as interleukin (IL)-10 receptor. Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. TTWKB01 EC EC 2.7.10.2 TTWKB01 PD 6N7D; 6N7C; 6N7B; 6N7A; 6N79 TTWKB01 SQ MQYLNIKEDCNAMAFCAKMRSSKKTEVNLEAPEPGVEVIFYLSDREPLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKKIPDATPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLENKHKKDEEKNKIREEWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKGRYSLHGSDRSFPSLGDLMSHLKKQILRTDNISFMLKRCCQPKPREISNLLVATKKAQEWQPVYPMSQLSFDRILKKDLVQGEHLGRGTRTHIYSGTLMDYKDDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDPGIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK TT0F5HE ID TT0F5HE TT0F5HE TN HUMAN janus kinase 2 (JAK-2) TT0F5HE UP O60674 TT0F5HE UC JAK2_HUMAN TT0F5HE BC Kinase TT0F5HE SN Tyrosine-protein kinase JAK2 TT0F5HE GN JAK2 TT0F5HE FC Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin. Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. TT0F5HE EC EC 2.7.10.2 TT0F5HE PD 6M9H; 6E2Q; 6E2P; 6DRW; 6BSS TT0F5HE SQ MGMACLTMTEMEGTSTSSIYQNGDISGNANSMKQIDPVLQVYLYHSLGKSEADYLTFPSGEYVAEEICIAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHNVLYRIRFYFPRWYCSGSNRAYRHGISRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKENDQTPLAIYNSISYKTFLPKCIRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEKFEVKEPGSGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPNIIDVSIKQANQEGSNESRVVTIHKQDGKNLEIELSSLREALSFVSLIDGYYRLTADAHHYLCKEVAPPAVLENIQSNCHGPISMDFAISKLKKAGNQTGLYVLRCSPKDFNKYFLTFAVERENVIEYKHCLITKNENEEYNLSGTKKNFSSLKDLLNCYQMETVRSDNIIFQFTKCCPPKPKDKSNLLVFRTNGVSDVPTSPTLQRPTHMNQMVFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSKLSHKHLVLNYGVCVCGDENILVQEFVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEENTLIHGNVCAKNILLIREEDRKTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWAELANLINNCMDYEPDFRPSFRAIIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG TTRYFSB ID TTRYFSB TTRYFSB TN HUMAN phosphodiesterase type 5 (PDE5) TTRYFSB UP O76074 TTRYFSB UC PDE5A_HUMAN TTRYFSB BC Phosphoric diester hydrolase TTRYFSB SN cGMP-specific 3',5'-cyclic phosphodiesterase; PDE5A; CGMP-binding cGMP-specific phosphodiesterase; CGB-PDE TTRYFSB GN PDE5A TTRYFSB FC Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP. TTRYFSB EC EC 3.1.4.35 TTRYFSB PD 6ACB; 5ZZ2; 5JO3; 4OEX; 4OEW TTRYFSB SQ MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN TTPZGYX ID TTPZGYX TTPZGYX TN HUMAN colony-stimulating factor (GM-CSF) TTPZGYX UP P04141 TTPZGYX UC CSF2_HUMAN TTPZGYX BC Growth factor TTPZGYX SN Sargramostim; Molgramostin; GM-CSF; Colony-stimulating factor; CSF2; CSF TTPZGYX GN CSF2 TTPZGYX FC Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. TTPZGYX PD 6BFS; 6BFQ; 5D72; 5D71; 5D70 TTPZGYX SQ MWLQSLLLLGTVACSISAPARSPSPSTQPWEHVNAIQEARRLLNLSRDTAAEMNETVEVISEMFDLQEPTCLQTRLELYKQGLRGSLTKLKGPLTMMASHYKQHCPPTPETSCATQIITFESFKENLKDFLLVIPFDCWEPVQE TTJH4Y5 ID TTJH4Y5 TTJH4Y5 TN HUMAN interleukin 6 (IL6) TTJH4Y5 UP P05231 TTJH4Y5 UC IL6_HUMAN TTJH4Y5 BC Cytokine: interleukin TTJH4Y5 SN Interferon beta-2; IL-6; IFNB2; IFN-beta-2; Hybridoma growth factor; CTL differentiation factor; CDF; BSF-2; B-cell stimulatory factor 2 TTJH4Y5 GN IL6 TTJH4Y5 FC It is a potent inducer of the acute phase response. Plays an essential role in the final differentiation of B-cells into Ig-secreting cells Involved in lymphocyte and monocyte differentiation. Acts on B-cells, T-cells, hepatocytes, hematopoietic progenitor cells and cells of the CNS. Required for the generation of T(H)17 cells. Also acts as a myokine. It is discharged into the bloodstream after muscle contraction and acts to increase the breakdown of fats and to improve insulin resistance. It induces myeloma and plasmacytoma growth and induces nerve cells differentiation. Cytokine with a wide variety of biological functions. TTJH4Y5 PD 5FUC; 4ZS7; 4O9H; 4NI9; 4NI7 TTJH4Y5 SQ MNSFSTSAFGPVAFSLGLLLVLPAAFPAPVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM TTJH4Y5 FM Interleukin TTT7FOP ID TTT7FOP TTT7FOP TN HUMAN interleukin-1 receptor 1 (IL1R1) TTT7FOP UP P14778 TTT7FOP UC IL1R1_HUMAN TTT7FOP BC Cytokine receptor TTT7FOP SN p80; Interleukin-1 receptor type I; Interleukin-1 receptor type 1; Interleukin-1 receptor alpha; IL1RT1; IL1RA; IL1R; IL-1RT1; IL-1RT-1; IL-1R-alpha; IL-1R-1; CD121a; CD121 antigen-like family member A TTT7FOP GN IL1R1 TTT7FOP FC Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the coreceptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. Involved in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells. TTT7FOP PD 4GAF; 4DEP; 1ITB; 1IRA; 1G0Y TTT7FOP SQ MKVLLRLICFIALLISSLEADKCKEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKISAKFVENEPNLCYNAQAIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPTRPVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRFYKHPFTCFAKNTHGIDAAYIQLIYPVTNFQKHMIGICVTLTVIIVCSVFIYKIFKIDIVLWYRDSCYDFLPIKASDGKTYDAYILYPKTVGEGSTSDCDIFVFKVLPEVLEKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSWLGGSSEEQIAMYNALVQDGIKVVLLELEKIQDYEKMPESIKFIKQKHGAIRWSGDFTQGPQSAKTRFWKNVRYHMPVQRRSPSSKHQLLSPATKEKLQREAHVPLG TTPKMXQ ID TTPKMXQ TTPKMXQ TN HUMAN type-1 angiotensin II receptor (AGTR1) TTPKMXQ UP P30556 TTPKMXQ UC AGTR1_HUMAN TTPKMXQ BC GPCR rhodopsin TTPKMXQ SN Type-1 angiotensin II receptor; Angiotensin II type-1 receptor; Angiotensin II receptor 1; Angiotensin 1 receptor; AT2R1B; AT2R1; AT1BR; AT1AR; AT1; AGTR1B; AGTR1A TTPKMXQ GN AGTR1 TTPKMXQ FC Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Receptor for angiotensin II. TTPKMXQ PD 6DO1; 4ZUD; 4YAY; 1ZV0 TTPKMXQ SQ MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPAPCFEVE TTPKMXQ FM GPCR rhodopsin TTN0GJ5 ID TTN0GJ5 TTN0GJ5 TN HUMAN complement C5 protein (C5) TTN0GJ5 UP P01031 TTN0GJ5 UC CO5_HUMAN TTN0GJ5 BC Complement system TTN0GJ5 SN C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4 TTN0GJ5 GN C5 TTN0GJ5 FC Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled. Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes (PubMed:8182049). C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation. TTN0GJ5 SQ MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC TTDVAKP ID TTDVAKP TTDVAKP TN HUMAN interleukin-6 receptor (IL6R) TTDVAKP UP P08887; P40189 TTDVAKP UC IL6RA_HUMAN; IL6RB_HUMAN TTDVAKP BC Cytokine receptor TTDVAKP SN Membrane glycoprotein; Interleukin-6 receptor; IL-6R; IL-6 receptor TTDVAKP GN IL6R; IL6ST TTDVAKP FC Low concentration of a soluble form of IL6 receptor acts as an agonist of IL6 activity. TTDVAKP SQ MLAVGCALLAALLAAPGAALAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGSHPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQLSCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPPANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWMVKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESRSPPAENEVSTPMQALTTNKDDDNILFRDSANATSLPVQDSSSVPLPTFLVAGGSLAFGTLLCIAIVLRFKKTWKLRALKEGKTSMHPPYSLGQLVPERPRPTPVLVPLISPPVSPSSLGSDNTSSHNRPDARDPRSPYDISNTDYFFPR TT1RS9F ID TT1RS9F TT1RS9F TN Acetylcholinesterase (AChE) TT1RS9F UP P22303 TT1RS9F UC ACES_HUMAN TT1RS9F BC Carboxylic ester hydrolase TT1RS9F SN YT; N-ACHE; ARACHE TT1RS9F GN ACHE TT1RS9F FC Role in neuronal apoptosis. Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. TT1RS9F EC EC 3.1.1.7 TT1RS9F PD 6O69; 6F25; 6CQZ; 6CQY; 6CQX TT1RS9F SQ MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL TT1RS9F TT Successful TT1RS9F FM Carboxylic ester hydrolase TT1RS9F KE hsa00564:Glycerophospholipid metabolism; hsa04725:Cholinergic synapse TTMXGCW ID TTMXGCW TTMXGCW TN Adrenergic receptor beta-3 (ADRB3) TTMXGCW UP P13945 TTMXGCW UC ADRB3_HUMAN TTMXGCW BC GPCR rhodopsin TTMXGCW SN Beta3AR; Beta3-AR; Beta-3 adrenoreceptor; Beta-3 adrenoceptor; Beta-3 adrenergic receptor; B3AR; ADRB3R TTMXGCW GN ADRB3 TTMXGCW FC Beta-3 is involved in the regulation of lipolysis and thermogenesis. Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. TTMXGCW PD 2CDW TTMXGCW SQ MAPWPHENSSLAPWPDLPTLAPNTANTSGLPGVPWEAALAGALLALAVLATVGGNLLVIVAIAWTPRLQTMTNVFVTSLAAADLVMGLLVVPPAATLALTGHWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRCARTAVVLVWVVSAAVSFAPIMSQWWRVGADAEAQRCHSNPRCCAFASNMPYVLLSSSVSFYLPLLVMLFVYARVFVVATRQLRLLRGELGRFPPEESPPAPSRSLAPAPVGTCAPPEGVPACGRRPARLLPLREHRALCTLGLIMGTFTLCWLPFFLANVLRALGGPSLVPGPAFLALNWLGYANSAFNPLIYCRSPDFRSAFRRLLCRCGRRLPPEPCAAARPALFPSGVPAARSSPAQPRLCQRLDGASWGVS TTMXGCW TT Successful TTMXGCW KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04144:Endocytosis; hsa04970:Salivary secretion TTMXGCW RC R-HSA-390696:Adrenoceptors; R-HSA-418555:G alpha (s) signalling events TTFBNVI ID TTFBNVI TTFBNVI TN Aldose reductase (AKR1B1) TTFBNVI UP P15121 TTFBNVI UC ALDR_HUMAN TTFBNVI BC Short-chain dehydrogenases reductase TTFBNVI SN Aldehyde reductase; AKR1B1 TTFBNVI GN AKR1B1 TTFBNVI FC Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. TTFBNVI EC EC 1.1.1.300 TTFBNVI PD 6F8O; 6F84; 6F82; 6F81; 6F7R TTFBNVI SQ MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF TTFBNVI TT Successful TTFBNVI KE hsa00040:Pentose and glucuronate interconversions; hsa00051:Fructose and mannose metabolism; hsa00052:Galactose metabolism; hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways TT2J34L ID TT2J34L TT2J34L TN Arachidonate 5-lipoxygenase (5-LOX) TT2J34L UP P09917 TT2J34L UC LOX5_HUMAN TT2J34L BC Oxygenase TT2J34L SN LOG5; 5-lipoxygenase; 5-LO TT2J34L GN ALOX5 TT2J34L FC Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. TT2J34L EC EC 1.13.11.34 TT2J34L PD 3V99; 3V98; 3V92; 3O8Y; 2ABV TT2J34L SQ MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGCNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECGLFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWEAIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLTVVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPYYYLSPDRIPNSVAI TT2J34L TT Successful TT2J34L FM Single donor oxidoreductase TT2J34L KE hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse; hsa04913:Ovarian steroidogenesis; hsa05145:Toxoplasmosis TTHQPL7 ID TTHQPL7 TTHQPL7 TN Carbonic anhydrase I (CA-I) TTHQPL7 UP P00915 TTHQPL7 UC CAH1_HUMAN TTHQPL7 BC Alpha-carbonic anhydrase TTHQPL7 SN Carbonic anhydrase B; Carbonic anhydrase 1; Carbonate dehydratase I; CAB TTHQPL7 GN CA1 TTHQPL7 FC Can hydrates cyanamide to urea. Reversible hydration of carbon dioxide. TTHQPL7 EC EC 4.2.1.1 TTHQPL7 PD 6HWZ; 6G3V; 6FAG; 6FAF; 6F3B TTHQPL7 SQ MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF TTHQPL7 TT Successful TTHQPL7 FM Carbon oxygen lyase TTHQPL7 KE hsa00910:Nitrogen metabolism TTHQPL7 RC R-HSA-1237044:Erythrocytes take up carbon dioxide and release oxygen; R-HSA-1247673:Erythrocytes take up oxygen and release carbon dioxide; R-HSA-1475029:Reversible hydration of carbon dioxide TTANPDJ ID TTANPDJ TTANPDJ TN Carbonic anhydrase II (CA-II) TTANPDJ UP P00918 TTANPDJ UC CAH2_HUMAN TTANPDJ BC Alpha-carbonic anhydrase TTANPDJ SN Carbonic anhydrase C; Carbonic anhydrase 2; Carbonate dehydratase II; CAC TTANPDJ GN CA2 TTANPDJ FC Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6. Essential for bone resorption and osteoclast differentiation. TTANPDJ EC EC 4.2.1.1 TTANPDJ PD 9CA2; 8CA2; 7CA2; 6QEB; 6MBY TTANPDJ SQ MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK TTANPDJ TT Successful TTANPDJ FM Carbon oxygen lyase TTANPDJ KE hsa00910:Nitrogen metabolism; hsa04964:Proximal tubule bicarbonate reclamation; hsa04966:Collecting duct acid secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04976:Bile secretion TTANPDJ RC R-HSA-1237044:Erythrocytes take up carbon dioxide and release oxygen; R-HSA-1247673:Erythrocytes take up oxygen and release carbon dioxide; R-HSA-1475029:Reversible hydration of carbon dioxide TTZHA0O ID TTZHA0O TTZHA0O TN Carbonic anhydrase IV (CA-IV) TTZHA0O UP P22748 TTZHA0O UC CAH4_HUMAN TTZHA0O BC Alpha-carbonic anhydrase TTZHA0O SN Carbonic anhydrase 4; Carbonate dehydratase IV; CAIV TTZHA0O GN CA4 TTZHA0O FC May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid. Reversible hydration of carbon dioxide. TTZHA0O EC EC 4.2.1.1 TTZHA0O PD 5KU6; 5JNC; 5JNA; 5JN9; 5JN8 TTZHA0O SQ MRMLLALLALSAARPSASAESHWCYEVQAESSNYPCLVPVKWGGNCQKDRQSPINIVTTKAKVDKKLGRFFFSGYDKKQTWTVQNNGHSVMMLLENKASISGGGLPAPYQAKQLHLHWSDLPYKGSEHSLDGEHFAMEMHIVHEKEKGTSRNVKEAQDPEDEIAVLAFLVEAGTQVNEGFQPLVEALSNIPKPEMSTTMAESSLLDLLPKEEKLRHYFRYLGSLTTPTCDEKVVWTVFREPIQLHREQILAFSQKLYYDKEQTVSMKDNVRPLQQLGQRTVIKSGAPGRPLPWALPALLGPMLACLLAGFLR TTZHA0O TT Successful TTZHA0O KE hsa00910:Nitrogen metabolism; hsa04964:Proximal tubule bicarbonate reclamation TTZHA0O RC R-HSA-1237044:Erythrocytes take up carbon dioxide and release oxygen; R-HSA-1247673:Erythrocytes take up oxygen and release carbon dioxide; R-HSA-1475029:Reversible hydration of carbon dioxide TT6EO5L ID TT6EO5L TT6EO5L TN Erbb2 tyrosine kinase receptor (HER2) TT6EO5L UP P04626 TT6EO5L UC ERBB2_HUMAN TT6EO5L BC Kinase TT6EO5L SN p185erbB2; Tyrosine kinase-type cell surface receptor HER2; Receptor tyrosine-protein kinase erbB-2; Proto-oncogene c-ErbB-2; Proto-oncogene Neu; NGL; NEU; Metastatic lymph node gene 19 protein; MLN19; MLN 19; HER2; CD340 TT6EO5L GN ERBB2 TT6EO5L FC Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization. TT6EO5L EC EC 2.7.10.1 TT6EO5L PD 6OGE; 6J71; 6BGT; 6ATT; 5TQS TT6EO5L SQ MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV TT6EO5L TT Successful TT6EO5L FM Kinase TT6EO5L KE hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05215:Prostate cancer; hsa05219:Bladder cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer TT6EO5L RC R-HSA-1250196:SHC1 events in ERBB2 signaling; R-HSA-1251932:PLCG1 events in ERBB2 signaling; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1963640:GRB2 events in ERBB2 signaling; R-HSA-1963642:PI3K events in ERBB2 signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-416572:Sema4D induced cell migration and growth-cone collapse; R-HSA-5673001:RAF/MAP kinase cascade TT0JESD ID TT0JESD TT0JESD TN Erbb4 tyrosine kinase receptor (Erbb-4) TT0JESD UP Q15303 TT0JESD UC ERBB4_HUMAN TT0JESD BC Kinase TT0JESD SN Tyrosine kinase-type cell surface receptor HER4; Receptor tyrosine-protein kinase erbB-4; Proto-oncogene-like protein c-ErbB-4; P180erbB4; HER4 TT0JESD GN ERBB4 TT0JESD FC Required for normal cardiac muscle differentiation during embryonic development, and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system, especially for normal neural crest cell migration and normal axon guidance. Required for mammary gland differentiation, induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1, NRG2, NRG3 and NRG4 and the EGF family members BTC, EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alternative splicing, proteolytic processing, and by the formation of heterodimers with other ERBB family members, thereby creating multiple combinations of intracellular phosphotyrosines that trigger ligand- and context-specific cellular responses. Mediates phosphorylation of SHC1 and activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Isoform JM-A CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the activation of phosphatidylinositol 3-kinase and AKT1 and protect cells against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate reorganization of the actin cytoskeleton and promote cell migration in response to NRG1. Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the phosphotyrosine that mediates interaction with PIK3R1, and hence do not phosphorylate PIK3R1, do not protect cells against apoptosis, and do not promote reorganization of the actin cytoskeleton and cell migration. Proteolytic processing of isoform JM-A CYT-1 and isoform JM-A CYT-2 gives rise to the corresponding soluble intracellular domains (4ICD) that translocate to the nucleus, promote nuclear import of STAT5A, activation of STAT5A, mammary epithelium differentiation, cell proliferation and activation of gene expression. The ERBB4 soluble intracellular domains (4ICD) colocalize with STAT5A at the CSN2 promoter to regulate transcription of milk proteins during lactation. The ERBB4 soluble intracellular domains can also translocate to mitochondria and promote apoptosis. Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart, the central nervous system and the mammary gland, gene transcription, cell proliferation, differentiation, migration and apoptosis. TT0JESD EC EC 2.7.10.1 TT0JESD PD 3U9U; 3U7U; 3U2P; 3BCE; 3BBW TT0JESD SQ MKPATGLWVWVSLLVAAGTVQPSDSQSVCAGTENKLSSLSDLEQQYRALRKYYENCEVVMGNLEITSIEHNRDLSFLRSVREVTGYVLVALNQFRYLPLENLRIIRGTKLYEDRYALAIFLNYRKDGNFGLQELGLKNLTEILNGGVYVDQNKFLCYADTIHWQDIVRNPWPSNLTLVSTNGSSGCGRCHKSCTGRCWGPTENHCQTLTRTVCAEQCDGRCYGPYVSDCCHRECAGGCSGPKDTDCFACMNFNDSGACVTQCPQTFVYNPTTFQLEHNFNAKYTYGAFCVKKCPHNFVVDSSSCVRACPSSKMEVEENGIKMCKPCTDICPKACDGIGTGSLMSAQTVDSSNIDKFINCTKINGNLIFLVTGIHGDPYNAIEAIDPEKLNVFRTVREITGFLNIQSWPPNMTDFSVFSNLVTIGGRVLYSGLSLLILKQQGITSLQFQSLKEISAGNIYITDNSNLCYYHTINWTTLFSTINQRIVIRDNRKAENCTAEGMVCNHLCSSDGCWGPGPDQCLSCRRFSRGRICIESCNLYDGEFREFENGSICVECDPQCEKMEDGLLTCHGPGPDNCTKCSHFKDGPNCVEKCPDGLQGANSFIFKYADPDRECHPCHPNCTQGCNGPTSHDCIYYPWTGHSTLPQHARTPLIAAGVIGGLFILVIVGLTFAVYVRRKSIKKKRALRRFLETELVEPLTPSGTAPNQAQLRILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVTQLMPHGCLLEYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYLVIQGDDRMKLPSPNDSKFFQNLLDEEDLEDMMDAEEYLVPQAFNIPPPIYTSRARIDSNRSEIGHSPPPAYTPMSGNQFVYRDGGFAAEQGVSVPYRAPTSTIPEAPVAQGATAEIFDDSCCNGTLRKPVAPHVQEDSSTQRYSADPTVFAPERSPRGELDEEGYMTPMRDKPKQEYLNPVEENPFVSRRKNGDLQALDNPEYHNASNGPPKAEDEYVNEPLYLNTFANTLGKAEYLKNNILSMPEKAKKAFDNPDYWNHSLPPRSTLQHPDYLQEYSTKYFYKQNGRIRPIVAENPEYLSEFSLKPGTVLPPPPYRHRNTVV TT0JESD TT Successful TT0JESD FM Kinase TT0JESD KE hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04144:Endocytosis; hsa05205:Proteoglycans in cancer TTZAYWL ID TTZAYWL TTZAYWL TN Estrogen receptor (ESR) TTZAYWL UP P03372 TTZAYWL UC ESR1_HUMAN TTZAYWL BC Nuclear hormone receptor TTZAYWL SN Nuclear receptor subfamily 3 group A member 1; NR3A1; Estradiol receptor; ESR; ER-alpha; ER TTZAYWL GN ESR1 TTZAYWL FC Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full-length receptor. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3. Isoform 3 can bind to ERE and inhibit isoform 1. TTZAYWL PD 6IAR; 6HMU; 6HKF; 6HKB; 6HHP TTZAYWL SQ MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV TTZAYWL TT Successful TTZAYWL FM Zinc finger TTZAYWL KE hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04961:Endocrine and other factor-regulated calcium reabsorption; hsa05205:Proteoglycans in cancer TTZAYWL RC R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-383280:Nuclear Receptor transcription pathway TTGJVQM ID TTGJVQM TTGJVQM TN Fibroblast growth factor receptor 2 (FGFR2) TTGJVQM UP P21802 TTGJVQM UC FGFR2_HUMAN TTGJVQM BC Kinase TTGJVQM SN Keratinocyte growth factor receptor 2; Keratinocyte growth factor receptor; KSAM; KGFR; K-sam; FGFR-2; FGF-2 receptor; CD332; BEK TTGJVQM GN FGFR2 TTGJVQM FC Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1. Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. TTGJVQM EC EC 2.7.10.1 TTGJVQM PD 5UI0; 5UHN; 5UGX; 5UGL; 5EG3 TTGJVQM SQ MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT TTGJVQM TT Successful TTGJVQM FM Kinase TTGJVQM KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer; hsa05215:Prostate cancer; hsa05230:Central carbon metabolism in cancer TTGJVQM RC R-HSA-2033519:Activated point mutants of FGFR2 TTGJCWZ ID TTGJCWZ TTGJCWZ TN Fms-like tyrosine kinase 3 (FLT-3) TTGJCWZ UP P36888 TTGJCWZ UC FLT3_HUMAN TTGJCWZ BC Kinase TTGJCWZ SN Stem cell tyrosine kinase 1; STK1; STK-1; Receptor-type tyrosine-protein kinase FLT3; Fetal liver kinase-2; FLT-3; FLK2; FLK-2; FL cytokine receptor; CD135 TTGJCWZ GN FLT3 TTGJCWZ FC Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine FLT3LG and regulates differentiation, proliferation and survival of hematopoietic progenitor cells and of dendritic cells. Promotes phosphorylation of SHC1 and AKT1, and activation of the downstream effector MTOR. Promotes activation of RAS signaling and phosphorylation of downstream kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation of FES, FER, PTPN6/SHP, PTPN11/SHP-2, PLCG1, and STAT5A and/or STAT5B. Activation of wild-type FLT3 causes only marginal activation of STAT5A or STAT5B. Mutations that cause constitutive kinase activity promote cell proliferation and resistance to apoptosis via the activation of multiple signaling pathways. TTGJCWZ EC EC 2.7.10.1 TTGJCWZ PD 6IL3; 5X02; 4XUF; 4RT7; 3QS9 TTGJCWZ SQ MPALARDGGQLPLLVVFSAMIFGTITNQDLPVIKCVLINHKNNDSSVGKSSSYPMVSESPEDLGCALRPQSSGTVYEAAAVEVDVSASITLQVLVDAPGNISCLWVFKHSSLNCQPHFDLQNRGVVSMVILKMTETQAGEYLLFIQSEATNYTILFTVSIRNTLLYTLRRPYFRKMENQDALVCISESVPEPIVEWVLCDSQGESCKEESPAVVKKEEKVLHELFGTDIRCCARNELGRECTRLFTIDLNQTPQTTLPQLFLKVGEPLWIRCKAVHVNHGFGLTWELENKALEEGNYFEMSTYSTNRTMIRILFAFVSSVARNDTGYYTCSSSKHPSQSALVTIVEKGFINATNSSEDYEIDQYEEFCFSVRFKAYPQIRCTWTFSRKSFPCEQKGLDNGYSISKFCNHKHQPGEYIFHAENDDAQFTKMFTLNIRRKPQVLAEASASQASCFSDGYPLPSWTWKKCSDKSPNCTEEITEGVWNRKANRKVFGQWVSSSTLNMSEAIKGFLVKCCAYNSLGTSCETILLNSPGPFPFIQDNISFYATIGVCLLFIVVLTLLICHKYKKQFRYESQLQMVQVTGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFHRTWTEIFKEHNFSFYPTFQSHPNSSMPGSREVQIHPDSDQISGLHGNSFHSEDEIEYENQKRLEEEEDLNVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQLADAEEAMYQNVDGRVSECPHTYQNRRPFSREMDLGLLSPQAQVEDS TTGJCWZ TT Successful TTGJCWZ FM Kinase TTGJCWZ KE hsa04060:Cytokine-cytokine receptor interaction; hsa04640:Hematopoietic cell lineage; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05221:Acute myeloid leukemia; hsa05230:Central carbon metabolism in cancer TT6R7JZ ID TT6R7JZ TT6R7JZ TN Histone deacetylase 1 (HDAC1) TT6R7JZ UP Q13547 TT6R7JZ UC HDAC1_HUMAN TT6R7JZ BC Carbon-nitrogen hydrolase TT6R7JZ SN RPD3L1; HD1 TT6R7JZ GN HDAC1 TT6R7JZ FC Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). TT6R7JZ EC EC 3.5.1.98 TT6R7JZ PD 5ICN; 4BKX; 1TYI TT6R7JZ SQ MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA TT6R7JZ TT Successful TT6R7JZ FM Carbon nitrogen hydrolase TT6R7JZ KE hsa04110:Cell cycle; hsa04330:Notch signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05016:Huntington's disease; hsa05031:Amphetamine addiction; hsa05034:Alcoholism; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05203:Viral carcinogenesis; hsa05206:MicroRNAs in cancer; hsa05220:Chronic myeloid leukemia TT6R7JZ RC R-HSA-1538133:G0 and Early G1; R-HSA-193670:p75NTR negatively regulates cell cycle via SC1; R-HSA-201722:Formation of the beta-catenin:TCF transactivating complex; R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2173796:SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-3214815:HDACs deacetylate histones; R-HSA-3769402:Deactivation of the beta-catenin transactivating complex; R-HSA-427413:NoRC negatively regulates rRNA expression; R-HSA-73762:RNA Polymerase I Transcription Initiation; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTPADOQ ID TTPADOQ TTPADOQ TN HMG-CoA reductase (HMGCR) TTPADOQ UP P04035 TTPADOQ UC HMDH_HUMAN TTPADOQ BC CH-OH donor oxidoreductase TTPADOQ SN 3-hydroxy-3-methylglutaryl-coenzyme A reductase TTPADOQ GN HMGCR TTPADOQ FC Transmembrane glycoprotein that is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including ubiquinone and geranylgeranyl proteins. TTPADOQ EC EC 1.1.1.34 TTPADOQ PD 3CDB; 3CDA; 3CD7; 3CD5; 3CD0 TTPADOQ SQ MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVTQKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNSSLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA TTPADOQ TT Successful TTPADOQ FM CH OH donor oxidoreductase TTPADOQ KE hsa00900:Terpenoid backbone biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa04152:AMPK signaling pathway; hsa04976:Bile secretion TTCBFJO ID TTCBFJO TTCBFJO TN Insulin receptor (INSR) TTCBFJO UP P06213 TTCBFJO UC INSR_HUMAN TTCBFJO BC Kinase TTCBFJO SN IR; CD220 antigen; CD220 TTCBFJO GN INSR TTCBFJO FC Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosine residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti-apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K-AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). Isoform Short has a higher affinity for IGFII binding. When present in a hybrid receptor with IGF1R, binds IGF1. shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin. Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. TTCBFJO EC EC 2.7.10.1 TTCBFJO PD 6HN5; 6HN4; 5U1M; 5KQV; 5J3H TTCBFJO SQ MATGGRRGAAAAPLLVAVAALLLGAAGHLYPGEVCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDICPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHSECLGNCSQPDDPTKCVACRNFYLDGRCVETCPPPYYHFQDWRCVNFSFCQDLHHKCKNSRRQGCHQYVIHNNKCIPECPSGYTMNSSNLLCTPCLGPCPKVCHLLEGEKTIDSVTSAQELRGCTVINGSLIINIRGGNNLAAELEANLGLIEEISGYLKIRRSYALVSLSFFRKLRLIRGETLEIGNYSFYALDNQNLRQLWDWSKHNLTITQGKLFFHYNPKLCLSEIHKMEEVSGTKGRQERNDIALKTNGDQASCENELLKFSYIRTSFDKILLRWEPYWPPDFRDLLGFMLFYKEAPYQNVTEFDGQDACGSNSWTVVDIDPPLRSNDPKSQNHPGWLMRGLKPWTQYAIFVKTLVTFSDERRTYGAKSDIIYVQTDATNPSVPLDPISVSNSSSQIILKWKPPSDPNGNITHYLVFWERQAEDSELFELDYCLKGLKLPSRTWSPPFESEDSQKHNQSEYEDSAGECCSCPKTDSQILKELEESSFRKTFEDYLHNVVFVPRKTSSGTGAEDPRPSRKRRSLGDVGNVTVAVPTVAAFPNTSSTSVPTSPEEHRPFEKVVNKESLVISGLRHFTGYRIELQACNQDTPEERCSVAAYVSARTMPEAKADDIVGPVTHEIFENNVVHLMWQEPKEPNGLIVLYEVSYRRYGDEELHLCVSRKHFALERGCRLRGLSPGNYSVRIRATSLAGNGSWTEPTYFYVTDYLDVPSNIAKIIIGPLIFVFLFSVVIGSIYLFLRKRQPDGPLGPLYASSNPEYLSASDVFPCSVYVPDEWEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPSFPEVSFFHSEENKAPESEELEMEFEDMENVPLDRSSHCQREEAGGRDGGSSLGFKRSYEEHIPYTHMNGGKKNGRILTLPRSNPS TTCBFJO TT Successful TTCBFJO FM Kinase TTCBFJO KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04520:Adherens junction; hsa04910:Insulin signaling pathway; hsa04913:Ovarian steroidogenesis; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04960:Aldosterone-regulated sodium reabsorption TTCBFJO RC R-HSA-74713:IRS activation; R-HSA-74749:Signal attenuation; R-HSA-74751:Insulin receptor signalling cascade; R-HSA-77387:Insulin receptor recycling TTRMX3V ID TTRMX3V TTRMX3V TN Janus kinase 2 (JAK-2) TTRMX3V UP O60674 TTRMX3V UC JAK2_HUMAN TTRMX3V BC Kinase TTRMX3V SN Tyrosine-protein kinase JAK2 TTRMX3V GN JAK2 TTRMX3V FC Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin. Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. TTRMX3V EC EC 2.7.10.2 TTRMX3V PD 6M9H; 6E2Q; 6E2P; 6DRW; 6BSS TTRMX3V SQ MGMACLTMTEMEGTSTSSIYQNGDISGNANSMKQIDPVLQVYLYHSLGKSEADYLTFPSGEYVAEEICIAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHNVLYRIRFYFPRWYCSGSNRAYRHGISRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKENDQTPLAIYNSISYKTFLPKCIRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEKFEVKEPGSGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPNIIDVSIKQANQEGSNESRVVTIHKQDGKNLEIELSSLREALSFVSLIDGYYRLTADAHHYLCKEVAPPAVLENIQSNCHGPISMDFAISKLKKAGNQTGLYVLRCSPKDFNKYFLTFAVERENVIEYKHCLITKNENEEYNLSGTKKNFSSLKDLLNCYQMETVRSDNIIFQFTKCCPPKPKDKSNLLVFRTNGVSDVPTSPTLQRPTHMNQMVFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSKLSHKHLVLNYGVCVCGDENILVQEFVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEENTLIHGNVCAKNILLIREEDRKTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWAELANLINNCMDYEPDFRPSFRAIIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG TTRMX3V TT Successful TTRMX3V FM Kinase TTRMX3V KE hsa04062:Chemokine signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04630:Jak-STAT signaling pathway; hsa04725:Cholinergic synapse; hsa04917:Prolactin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa05140:Leishmaniasis; hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection TTRMX3V RC R-HSA-1059683:Interleukin-6 signaling; R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-112411:MAPK1 (ERK2) activation; R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1170546:Prolactin receptor signaling; R-HSA-3214858:RMTs methylate histone arginines; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-5673000:RAF activation; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-877300:Interferon gamma signaling; R-HSA-877312:Regulation of IFNG signaling; R-HSA-912526:Interleukin receptor SHC signaling; R-HSA-982772:Growth hormone receptor signaling; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TT860QF ID TT860QF TT860QF TN LCK tyrosine protein kinase (LCK) TT860QF UP P06239 TT860QF UC LCK_HUMAN TT860QF BC Kinase TT860QF SN p56-LCK; Tyrosine-protein kinase Lck; T cell-specific protein-tyrosine kinase; Proto-oncogene tyrosine-protein kinase LCK; Proto-oncogene Lck; Protein YT16; Lymphocyte cell-specific protein-tyrosine kinase; Leukocyte C-terminal Src kinase; LSK; LCK p59-Fyn; LCK Protooncogene Syn TT860QF GN LCK TT860QF FC Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP. Interacts with FYB2. Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. TT860QF EC EC 2.7.10.2 TT860QF PD 6H6A; 5MTN; 5MTM; 4D8K; 4C3F TT860QF SQ MGCGCSSHPEDDWMENIDVCENCHYPIVPLDGKGTLLIRNGSEVRDPLVTYEGSNPPASPLQDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEELYQLMRLCWKERPEDRPTFDYLRSVLEDFFTATEGQYQPQP TT860QF TT Successful TT860QF FM Kinase TT860QF KE hsa04064:NF-kappa B signaling pathway; hsa04380:Osteoclast differentiation; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa05166:HTLV-I infection; hsa05340:Primary immunodeficiency TT860QF RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1433559:Regulation of KIT signaling; R-HSA-202427:Phosphorylation of CD3 and TCR zeta chains; R-HSA-202430:Translocation of ZAP-70 to Immunological synapse; R-HSA-202433:Generation of second messenger molecules; R-HSA-210990:PECAM1 interactions; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-2424491:DAP12 signaling; R-HSA-389356:CD28 co-stimulation; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389359:CD28 dependent Vav1 pathway; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-389948:PD-1 signaling; R-HSA-451927:Interleukin-2 signaling TTMX39J ID TTMX39J TTMX39J TN Matrix metalloproteinase-1 (MMP-1) TTMX39J UP P03956 TTMX39J UC MMP1_HUMAN TTMX39J BC Peptidase TTMX39J SN Interstitial collagenase; Fibroblast collagenase; CLG TTMX39J GN MMP1 TTMX39J FC Cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity. Cleaves collagens of types I, II, and III at one site in the helical domain. TTMX39J EC EC 3.4.24.7 TTMX39J PD 966C; 4AYK; 4AUO; 3SHI; 3AYK TTMX39J SQ MHSFPPLLLLLFWGVVSHSFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN TTMX39J TT Successful TTMX39J FM Peptidase TTMX39J KE hsa03320:PPAR signaling pathway; hsa05200:Pathways in cancer; hsa05219:Bladder cancer; hsa05323:Rheumatoid arthritis TTMX39J RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-210991:Basigin interactions; R-HSA-381426:Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) TTLM12X ID TTLM12X TTLM12X TN Matrix metalloproteinase-2 (MMP-2) TTLM12X UP P08253 TTLM12X UC MMP2_HUMAN TTLM12X BC Peptidase TTLM12X SN TBE-1; Matrix metalloproteinase 2; CLG4A; 72 kDa type IV collagenase; 72 kDa gelatinase TTLM12X GN MMP2 TTLM12X FC As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14. Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. TTLM12X EC EC 3.4.24.24 TTLM12X PD 3AYU; 1RTG; 1QIB; 1KS0; 1J7M TTLM12X SQ MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC TTLM12X TT Successful TTLM12X FM Peptidase TTLM12X KE hsa04670:Leukocyte transendothelial migration; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05219:Bladder cancer TTLM12X RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-381426:Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-3928665:EPH-ephrin mediated repulsion of cells TT3WG5C ID TT3WG5C TT3WG5C TN Monoamine oxidase type A (MAO-A) TT3WG5C UP P21397 TT3WG5C UC AOFA_HUMAN TT3WG5C BC CH-NH(2) donor oxidoreductase TT3WG5C SN Monoamine oxidase A; Amine oxidase [flavin-containing] A TT3WG5C GN MAOA TT3WG5C FC MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine. Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. TT3WG5C EC EC 1.4.3.4 TT3WG5C PD 2Z5Y; 2Z5X; 2BXS; 2BXR; 1H8Q TT3WG5C SQ MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKDVPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS TT3WG5C TT Successful TT3WG5C FM CH NH2 donor oxidoreductase TT3WG5C KE hsa00260:Glycine, serine and threonine metabolism; hsa00330:Arginine and proline metabolism; hsa00340:Histidine metabolism; hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism; hsa00380:Tryptophan metabolism; hsa00982:Drug metabolism - cytochrome P450; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse; hsa04728:Dopaminergic synapse; hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05034:Alcoholism TT3WG5C RC R-HSA-181430:Norepinephrine Neurotransmitter Release Cycle TTJ0IQB ID TTJ0IQB TTJ0IQB TN Phosphodiesterase 5A (PDE5A) TTJ0IQB UP O76074 TTJ0IQB UC PDE5A_HUMAN TTJ0IQB BC Phosphoric diester hydrolase TTJ0IQB SN cGMP-specific 3',5'-cyclic phosphodiesterase; PDE5A; CGMP-binding cGMP-specific phosphodiesterase; CGB-PDE TTJ0IQB GN PDE5A TTJ0IQB FC Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP. TTJ0IQB EC EC 3.1.4.35 TTJ0IQB PD 6ACB; 5ZZ2; 5JO3; 4OEX; 4OEW TTJ0IQB SQ MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN TTJ0IQB TT Successful TTJ0IQB KE hsa00230:Purine metabolism; hsa04022:cGMP-PKG signaling pathway TTJ0IQB RC R-HSA-418457:cGMP effects TT3PQ2Y ID TT3PQ2Y TT3PQ2Y TN Plasmodium Dihydroorotate dehydrogenase (Malaria DHOdehase) TT3PQ2Y UP Q08210 TT3PQ2Y UC PYRD_PLAF7 TT3PQ2Y BC CH-CH donor oxidoreductase TT3PQ2Y SN PFF0160c; Mitochondrially bound dihydroorotate-ubiqui oxidoreductase; Dihydroorotate oxidase of Plasmodium falciparum; Dihydroorotate dehydrogenase of Plasmodium falciparum; DHOdehase of Plasmodium falciparum; DHODase; DHODH of Plasmodium falciparum; DHOD TT3PQ2Y GN Malaria DHOdehase TT3PQ2Y FC Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. TT3PQ2Y EC EC 1.3.5.2 TT3PQ2Y PD 6GJG; 6E0B; 5TBO; 5FI8; 5DEL TT3PQ2Y SQ MISKLKPQFMFLPKKHILSYCRKDVLNLFEQKFYYTSKRKESNNMKNESLLRLINYNRYYNKIDSNNYYNGGKILSNDRQYIYSPLCEYKKKINDISSYVSVPFKINIRNLGTSNFVNNKKDVLDNDYIYENIKKEKSKHKKIIFLLFVSLFGLYGFFESYNPEFFLYDIFLKFCLKYIDGEICHDLFLLLGKYNILPYDTSNDSIYACTNIKHLDFINPFGVAAGFDKNGVCIDSILKLGFSFIEIGTITPRGQTGNAKPRIFRDVESRSIINSCGFNNMGCDKVTENLILFRKRQEEDKLLSKHIVGVSIGKNKDTVNIVDDLKYCINKIGRYADYIAINVSSPNTPGLRDNQEAGKLKNIILSVKEEIDNLEKNNIMNDESTYNEDNKIVEKKNNFNKNNSHMMKDAKDNFLWFNTTKKKPLVFVKLAPDLNQEQKKEIADVLLETNIDGMIISNTTTQINDIKSFENKKGGVSGAKLKDISTKFICEMYNYTNKQIPIIASGGIFSGLDALEKIEAGASVCQLYSCLVFNGMKSAVQIKRELNHLLYQRGYYNLKEAIGRKHSKS TT3PQ2Y TT Successful TT3PQ2Y KE hsa00240:Pyrimidine metabolism; hsa01100:Metabolic pathways TT3PQ2Y RC R-HSA-500753:Pyrimidine biosynthesis TT8FYO9 ID TT8FYO9 TT8FYO9 TN Platelet-derived growth factor receptor alpha (PDGFRA) TT8FYO9 UP P16234 TT8FYO9 UC PGFRA_HUMAN TT8FYO9 BC Kinase TT8FYO9 SN RHEPDGFRA; Platelet-derived growth factor receptor 2; Platelet-derived growth factor alpha receptor; PDGFR2; PDGFR-alpha; PDGFR-2; PDGF-R-alpha; CD140a antigen; CD140a; CD140 antigen-like family member A; Alpha-type platelet-derived growth factor receptor; Alpha platelet-derived growth factor receptor TT8FYO9 GN PDGFRA TT8FYO9 FC Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. TT8FYO9 EC EC 2.7.10.1 TT8FYO9 PD 5K5X; 5GRN; 1GQ5 TT8FYO9 SQ MGTSHPAFLVLGCLLTGLSLILCQLSLPSILPNENEKVVQLNSSFSLRCFGESEVSWQYPMSEEESSDVEIRNEENNSGLFVTVLEVSSASAAHTGLYTCYYNHTQTEENELEGRHIYIYVPDPDVAFVPLGMTDYLVIVEDDDSAIIPCRTTDPETPVTLHNSEGVVPASYDSRQGFNGTFTVGPYICEATVKGKKFQTIPFNVYALKATSELDLEMEALKTVYKSGETIVVTCAVFNNEVVDLQWTYPGEVKGKGITMLEEIKVPSIKLVYTLTVPEATVKDSGDYECAARQATREVKEMKKVTISVHEKGFIEIKPTFSQLEAVNLHEVKHFVVEVRAYPPPRISWLKNNLTLIENLTEITTDVEKIQEIRYRSKLKLIRAKEEDSGHYTIVAQNEDAVKSYTFELLTQVPSSILDLVDDHHGSTGGQTVRCTAEGTPLPDIEWMICKDIKKCNNETSWTILANNVSNIITEIHSRDRSTVEGRVTFAKVEETIAVRCLAKNLLGAENRELKLVAPTLRSELTVAAAVLVLLVIVIISLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRVLGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFLSHHPEKPKKELDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDNSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL TT8FYO9 TT Successful TT8FYO9 FM Kinase TT8FYO9 KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04540:Gap junction; hsa04810:Regulation of actin cytoskeleton; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TT8FYO9 RC R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5673001:RAF/MAP kinase cascade TT4DXQT ID TT4DXQT TT4DXQT TN Proto-oncogene c-Ret (RET) TT4DXQT UP P07949 TT4DXQT UC RET_HUMAN TT4DXQT BC Kinase TT4DXQT SN RET51; RET receptor tyrosine kinase; RET mutant Y791F; RET mutant V804M; RET mutant V804L; RET mutant S891A; RET mutant M918T; RET mutant G691S; Proto-oncogene tyrosine-protein kinase receptor Ret; PTC; Cadherin family member 12; CDHR16; CDHF12; C-ret TT4DXQT GN RET TT4DXQT FC Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e. g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration. Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways. Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL. Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. TT4DXQT EC EC 2.7.10.1 TT4DXQT PD 6FEK; 5FM3; 5FM2; 5AMN; 4UX8 TT4DXQT SQ MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNRNLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPRGIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCRTVIAAAVLFSFIVSVLLSAFCIHCYHKFAHKPPISSAEMTFRRPAQAFPVSYSSSGARRPSLDSMENQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPSDSLIYDDGLSEEETPLVDCNNAPLPRALPSTWIENKLYGMSDPNWPGESPVPLTRADGTNTGFPRYPNDSVYANWMLSPSAAKLMDTFDS TT4DXQT TT Successful TT4DXQT FM Kinase TT4DXQT KE hsa04144:Endocytosis; hsa05200:Pathways in cancer; hsa05216:Thyroid cancer; hsa05230:Central carbon metabolism in cancer TT6PKBN ID TT6PKBN TT6PKBN TN Proto-oncogene c-Src (SRC) TT6PKBN UP P12931 TT6PKBN UC SRC_HUMAN TT6PKBN BC Kinase TT6PKBN SN pp60c-src; Tyrosine kinase (pp60(src)); Src tyrosine kinase; SRC1; Proto-oncogene tyrosine-protein kinase Src; Pp60(src); P60-Src; C-src TK; C-Src TT6PKBN GN SRC TT6PKBN FC Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-128'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Involved in anchorage-independent cell growth. Required for podosome formation. Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. TT6PKBN EC EC 2.7.10.2 TT6PKBN PD 6EHJ; 6C4S; 6ATE; 4MXZ; 4MXY TT6PKBN SQ MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL TT6PKBN TT Successful TT6PKBN FM Kinase TT6PKBN KE hsa04012:ErbB signaling pathway; hsa04015:Rap1 signaling pathway; hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa04370:VEGF signaling pathway; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04530:Tight junction; hsa04540:Gap junction; hsa04611:Platelet activation; hsa04727:GABAergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04810:Regulation of actin cytoskeleton; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05100:Bacterial invasion of epithelial cells; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer TTWCGQT ID TTWCGQT TTWCGQT TN Serine/threonine-protein kinase B-raf (BRAF) TTWCGQT UP P15056 TTWCGQT UC BRAF_HUMAN TTWCGQT BC Kinase TTWCGQT SN V-Raf murine sarcoma viral oncogene homolog B1; RAFB1; Proto-oncogene B-Raf; P94; BRAF1; BRAF(V599E); BRAF serine/threonine kinase; B-raf protein; B-Raf TTWCGQT GN BRAF TTWCGQT FC May play a role in the postsynaptic responses of hippocampal neuron. Phosphorylates MAP2K1, and thereby contributes to the MAP kinase signal transduction pathway. Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus. TTWCGQT EC EC 2.7.11.1 TTWCGQT PD 6CAD; 6B8U; 5VYK; 5VR3; 5VAM TTWCGQT SQ MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH TTWCGQT TT Successful TTWCGQT FM Kinase TTWCGQT KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04015:Rap1 signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04068:FoxO signaling pathway; hsa04150:mTOR signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04510:Focal adhesion; hsa04650:Natural killer cell mediated cytotoxicity; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa05034:Alcoholism; hsa05160:Hepatitis C; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer TTWCGQT RC R-HSA-1295596:Spry regulation of FGF signaling; R-HSA-170968:Frs2-mediated activation; R-HSA-170984:ARMS-mediated activation; R-HSA-442742:CREB phosphorylation through the activation of Ras; R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5674499:Negative feedback regulation of MAPK pathway; R-HSA-5675221:Negative regulation of MAPK pathway TTCJG29 ID TTCJG29 TTCJG29 TN Serine/threonine-protein kinase mTOR (mTOR) TTCJG29 UP P42345 TTCJG29 UC MTOR_HUMAN TTCJG29 BC Kinase TTCJG29 SN Target of rapamycin; TOR kinase; Rapamycin target protein 1; Rapamycin target protein; Rapamycin and FKBP12 target 1; RAPT1; RAFT1; Mechanistic target of rapamycin; Mammalian target of rapamycin; FRAP2; FRAP1; FRAP; FKBP12-rapamycin complex-associated protein; FKBP-rapamycin associated protein; FK506-binding protein 12-rapamycin complex-associated protein 1 TTCJG29 GN MTOR TTCJG29 FC MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4. Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor. In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1. To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A. mTORC1 also negatively regulates autophagy through phosphorylation of ULK1. Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1. Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP. Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions. mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor. Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules. As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton. Plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1. mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B. mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422'. Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms. Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks. Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. TTCJG29 EC EC 2.7.11.1 TTCJG29 PD 6BCX; 6BCU; 5ZCS; 5WBY; 5WBU TTCJG29 SQ MLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFW TTCJG29 TT Successful TTCJG29 FM Kinase TTCJG29 KE hsa04012:ErbB signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04910:Insulin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04930:Type II diabetes mellitus; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05221:Acute myeloid leukemia; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTCJG29 RC R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1632852:Macroautophagy; R-HSA-166208:mTORC1-mediated signalling; R-HSA-3371571:HSF1-dependent transactivation; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-5218920:VEGFR2 mediated vascular permeability; R-HSA-5628897:TP53 Regulates Metabolic Genes; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer TTE14XG ID TTE14XG TTE14XG TN Squalene monooxygenase (SQLE) TTE14XG UP Q14534 TTE14XG UC ERG1_HUMAN TTE14XG BC Paired donor oxygen oxidoreductase TTE14XG SN Squalene epoxidase; SQLE; SE; Oxidosqaulene cyclase TTE14XG GN SQLE TTE14XG FC Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway. TTE14XG EC EC 1.14.14.17 TTE14XG PD 6C6R; 6C6P; 6C6N TTE14XG SQ MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQQSGSQFALFSDILSGLPFIGFFWAKSPPESENKEQLEARRRRKGTNISETSLIGTAACTSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDIRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYDDAAIFEAKKSFYWARKTSHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALLSSGAVLYKACSVIFPLIYSEMKYMVH TTE14XG TT Successful TTE14XG KE sce00100:Steroid biosynthesis; sce00909:Sesquiterpenoid and triterpenoid biosynthesis; sce01100:Metabolic pathways; sce01110:Biosynthesis of secondary metabolites; sce01130:Biosynthesis of antibiotics TTE14XG RC R-HSA-191273:Cholesterol biosynthesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP) TTTDVOJ ID TTTDVOJ TTTDVOJ TN Tropomyosin-related kinase A (TrkA) TTTDVOJ UP P04629 TTTDVOJ UC NTRK1_HUMAN TTTDVOJ BC Kinase TTTDVOJ SN gp140trk; Tyrosine kinase receptor A; Tyrosine kinase receptor; Trk-A; TRKA; TRK1-transforming tyrosine kinase protein; TRK1 transforming tyrosinekinase protein; TRK; P140-TrkA; Neurotrophic tyrosine kinase receptor type 1; NGF-trk receptor type A; MTC; High affinity nerve growth factor receptor TTTDVOJ GN NTRK1 TTTDVOJ FC High affinity receptor for NGF which is its primary ligand. Can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival. Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors. Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. TTTDVOJ EC EC 2.7.10.1 TTTDVOJ PD 6NSS; 6NSP; 6NPT; 6DKW; 6DKI TTTDVOJ SQ MLRGGRRGQLGWHSWAAGPGSLLAWLILASAGAAPCPDACCPHGSSGLRCTRDGALDSLHHLPGAENLTELYIENQQHLQHLELRDLRGLGELRNLTIVKSGLRFVAPDAFHFTPRLSRLNLSFNALESLSWKTVQGLSLQELVLSGNPLHCSCALRWLQRWEEEGLGGVPEQKLQCHGQGPLAHMPNASCGVPTLKVQVPNASVDVGDDVLLRCQVEGRGLEQAGWILTELEQSATVMKSGGLPSLGLTLANVTSDLNRKNVTCWAENDVGRAEVSVQVNVSFPASVQLHTAVEMHHWCIPFSVDGQPAPSLRWLFNGSVLNETSFIFTEFLEPAANETVRHGCLRLNQPTHVNNGNYTLLAANPFGQASASIMAAFMDNPFEFNPEDPIPVSFSPVDTNSTSGDPVEKKDETPFGVSVAVGLAVFACLFLSTLLLVLNKCGRRNKFGINRPAVLAPEDGLAMSLHFMTLGGSSLSPTEGKGSGLQGHIIENPQYFSDACVHHIKRRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKEASESARQDFQREAELLTMLQHQHIVRFFGVCTEGRPLLMVFEYMRHGDLNRFLRSHGPDAKLLAGGEDVAPGPLGLGQLLAVASQVAAGMVYLAGLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWYQLSNTEAIDCITQGRELERPRACPPEVYAIMRGCWQREPQQRHSIKDVHARLQALAQAPPVYLDVLG TTTDVOJ TT Successful TTTDVOJ FM Kinase TTTDVOJ KE hsa04010:MAPK signaling pathway; hsa04144:Endocytosis; hsa04210:Apoptosis; hsa04722:Neurotrophin signaling pathway; hsa04750:Inflammatory mediator regulation of TRP channels; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05216:Thyroid cancer; hsa05230:Central carbon metabolism in cancer TTTDVOJ RC R-HSA-170968:Frs2-mediated activation; R-HSA-170984:ARMS-mediated activation; R-HSA-187024:NGF-independant TRKA activation; R-HSA-198203:PI3K/AKT activation TT3PJMV ID TT3PJMV TT3PJMV TN Tyrosine-protein kinase ABL1 (ABL) TT3PJMV UP P00519 TT3PJMV UC ABL1_HUMAN TT3PJMV BC Kinase TT3PJMV SN p150; Proto-oncogene tyrosine-protein kinase ABL1; Proto-oncogene c-Abl; JTK7; C-ABL; Abl; Abelson tyrosine-protein kinase 1; Abelson murine leukemia viral oncogene homolog 1 TT3PJMV GN ABL1 TT3PJMV FC Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717'. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E. coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H. pylori, or AnkA (ankyrin repeat-containing protein A) of A. phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner. Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity. Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. TT3PJMV EC EC 2.7.10.2 TT3PJMV PD 6NPV; 6NPU; 6NPE; 6BL8; 6AMW TT3PJMV SQ MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR TT3PJMV TT Successful TT3PJMV FM Kinase TT3PJMV KE hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04110:Cell cycle; hsa04360:Axon guidance; hsa04722:Neurotrophin signaling pathway; hsa05130:Pathogenic Escherichia coli infection; hsa05131:Shigellosis; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05220:Chronic myeloid leukemia; hsa05416:Viral myocarditis TT3PJMV RC R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-375170:CDO in myogenesis; R-HSA-5663213:RHO GTPases Activate WASPs and WAVEs; R-HSA-5685938:HDR through Single Strand Annealing (SSA); R-HSA-5693565:Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTGM6VW ID TTGM6VW TTGM6VW TN Tyrosine-protein kinase BTK (ATK) TTGM6VW UP Q06187 TTGM6VW UC BTK_HUMAN TTGM6VW BC Kinase TTGM6VW SN Bruton's tyrosine kinase; Bruton tyrosine kinase; BPK; B-cell progenitor kinase; B cell progenitor kinase; Agammaglobulinemia tyrosine kinase; Agammaglobulinaemia tyrosine kinase; AGMX1 TTGM6VW GN BTK TTGM6VW FC Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis. Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. TTGM6VW EC EC 2.7.10.2 TTGM6VW PD 6O8I; 6NFI; 6NFH; 6N9P; 6HRT TTGM6VW SQ MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPAAAPVSTSELKKVVALYDYMPMNANDLQLRKGDEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSTGDPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLISRLKYPVSQQNKNAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNILDVMDEES TTGM6VW TT Successful TTGM6VW FM Kinase TTGM6VW KE hsa04064:NF-kappa B signaling pathway; hsa04380:Osteoclast differentiation; hsa04611:Platelet activation; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa05340:Primary immunodeficiency TTGM6VW RC R-HSA-166058:MyD88:Mal cascade initiated on plasma membrane; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-2424491:DAP12 signaling; R-HSA-2871809:FCERI mediated Ca+2 mobilization; R-HSA-5602498:MyD88 deficiency (TLR2/4); R-HSA-5603041:IRAK4 deficiency (TLR2/4); R-HSA-5663213:RHO GTPases Activate WASPs and WAVEs; R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTX41N9 ID TTX41N9 TTX41N9 TN Tyrosine-protein kinase Kit (KIT) TTX41N9 UP P10721 TTX41N9 UC KIT_HUMAN TTX41N9 BC Kinase TTX41N9 SN v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog; p145 c-kit; Proto-oncogene tyrosine-protein kinase Kit; Proto-oncogene c-Kit; Piebald trait protein; PBT; Mast/stem cell growth factor receptor Kit; CD117 antigen; CD117; C-kit TTX41N9 GN KIT TTX41N9 FC In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1. Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. TTX41N9 EC EC 2.7.10.1 TTX41N9 PD 6GQM; 6GQL; 6GQK; 6GQJ; 4U0I TTX41N9 SQ MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWEDYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDSSAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSVGSTASSSQPLLVHDDV TTX41N9 TT Successful TTX41N9 FM Kinase TTX41N9 KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04916:Melanogenesis; hsa05200:Pathways in cancer; hsa05221:Acute myeloid leukemia; hsa05230:Central carbon metabolism in cancer TTX41N9 RC R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1433559:Regulation of KIT signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5673001:RAF/MAP kinase cascade TTUTJGQ ID TTUTJGQ TTUTJGQ TN Vascular endothelial growth factor receptor 2 (KDR) TTUTJGQ UP P35968 TTUTJGQ UC VGFR2_HUMAN TTUTJGQ BC Kinase TTUTJGQ SN VEGFR2; VEGFR-2; VEGF-2 receptor; Protein-tyrosine kinase receptor flk-1; Kinase insert domain receptor; Fetal liver kinase 1; FLK1; FLK-1; CD309 TTUTJGQ GN KDR TTUTJGQ FC Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC. Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. TTUTJGQ EC EC 2.7.10.1 TTUTJGQ PD 6GQQ; 6GQP; 6GQO; 5OYJ; 5EW3 TTUTJGQ SQ MQSKVLLAVALWLCVETRAASVGLPSVSLDLPRLSIQKDILTIKANTTLQITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGAYKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRSDQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRIPAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVILTNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAIPPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVNKNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRGPEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPTPVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTKKRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIIEGAQEKTNLEIIILVGTAVIAMFFWLLLVIILRTVKRANGGELKTGYLSIVMDPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYKTKGARFRQGKDYVGAIPVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEAPEDLYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQDGKDYIVLPISETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISQYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDDNQTDSGMVLASEELKTLEDRTKLSPSFGGMVPSKSRESVASEGSNQTSGYQSGYHSDDTDTTVYSSEEAELLKLIEIGVQTGSTAQILQPDSGTTLSSPPV TTUTJGQ TT Successful TTUTJGQ FM Kinase TTUTJGQ KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04370:VEGF signaling pathway; hsa04510:Focal adhesion; hsa05205:Proteoglycans in cancer TTUTJGQ RC R-HSA-194306:Neurophilin interactions with VEGF and VEGFR; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization; R-HSA-216083:Integrin cell surface interactions; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5218921:VEGFR2 mediated cell proliferation TTYRG7F ID TTYRG7F TTYRG7F TN HUMAN angiotensin-converting enzyme 2 (ACE2) TTYRG7F UP Q9BYF1 TTYRG7F UC ACE2_HUMAN TTYRG7F BC Peptidase TTYRG7F SN Processed angiotensinconverting enzyme 2; Metalloprotease MPROT15; Angiotensinconverting enzyme homolog; Angiotensinconverting enzyme 2; ACErelated carboxypeptidase; ACEH; ACE2 TTYRG7F GN ACE2 TTYRG7F FC Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin- 13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses. TTYRG7F EC EC 3.4.17.23 TTYRG7F PD 6CS2; 6ACK; 6ACJ; 6ACG; 3SCL TTYRG7F SQ MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKGENNPGFQNTDDVQTSF TTOWPER ID TTOWPER TTOWPER TN HUMAN bruton tyrosine kinase (BTK) TTOWPER UP Q06187 TTOWPER UC BTK_HUMAN TTOWPER BC Kinase TTOWPER SN Bruton's tyrosine kinase; Bruton tyrosine kinase; BPK; B-cell progenitor kinase; B cell progenitor kinase; Agammaglobulinemia tyrosine kinase; Agammaglobulinaemia tyrosine kinase; AGMX1 TTOWPER GN BTK TTOWPER FC Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis. Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. TTOWPER EC EC 2.7.10.2 TTOWPER PD 6O8I; 6NFI; 6NFH; 6N9P; 6HRT TTOWPER SQ MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPAAAPVSTSELKKVVALYDYMPMNANDLQLRKGDEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSTGDPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLISRLKYPVSQQNKNAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNILDVMDEES TT3UY29 ID TT3UY29 TT3UY29 TN HUMAN dihydroorotate dehydrogenase (DHODH) TT3UY29 UP Q02127 TT3UY29 UC PYRD_HUMAN TT3UY29 BC CH-CH donor oxidoreductase TT3UY29 SN Dihydroorotate oxidase; Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOdehase; DHODH TT3UY29 GN DHODH TT3UY29 FC Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. TT3UY29 EC EC 1.3.5.2 TT3UY29 PD 6FMD; 6ET4; 6CJG; 6CJF; 5ZFB TT3UY29 SQ MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR TT7HQAF ID TT7HQAF TT7HQAF TN HUMAN mammalian target of rapamycin (mTOR) TT7HQAF UP P42345 TT7HQAF UC MTOR_HUMAN TT7HQAF BC Kinase TT7HQAF SN Target of rapamycin; TOR kinase; Rapamycin target protein 1; Rapamycin target protein; Rapamycin and FKBP12 target 1; RAPT1; RAFT1; Mechanistic target of rapamycin; Mammalian target of rapamycin; FRAP2; FRAP1; FRAP; FKBP12-rapamycin complex-associated protein; FKBP-rapamycin associated protein; FK506-binding protein 12-rapamycin complex-associated protein 1 TT7HQAF GN MTOR TT7HQAF FC MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4. Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor. In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1. To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A. mTORC1 also negatively regulates autophagy through phosphorylation of ULK1. Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1. Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP. Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions. mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor. Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules. As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton. Plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1. mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B. mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422'. Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms. Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks. Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. TT7HQAF EC EC 2.7.11.1 TT7HQAF PD 6BCX; 6BCU; 5ZCS; 5WBY; 5WBU TT7HQAF SQ MLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFW TT7HQAF FM Kinase TTK5FVJ ID TTK5FVJ TTK5FVJ TN HUMAN PI3-kinase delta (PIK3CD) TTK5FVJ UP O00329 TTK5FVJ UC PK3CD_HUMAN TTK5FVJ BC Kinase TTK5FVJ SN PtdIns-3-kinase subunit p110-delta; PtdIns-3-kinase subunit delta; Phosphoinositide 3-kinase delta; Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, delta isoform; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform; Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta; PI3Kdelta; PI3K-delta; PI3-kinase subunit delta; PI3-kinase p110 subunit delta; P110delta TTK5FVJ GN PIK3CD TTK5FVJ FC Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Have a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Have important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function. Isoform 2 may be involved in stabilizing total RAS levels, resulting in increased ERK phosphorylation and increased PI3K activity. TTK5FVJ EC EC 2.7.1.153 TTK5FVJ PD 6G6W; 5VLR; 5UBT; 5T8F; 5M6U TTK5FVJ SQ MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ TTHXGLJ ID TTHXGLJ TTHXGLJ TN HUMAN PI3-kinase gamma (PIK3CG) TTHXGLJ UP P48736 TTHXGLJ UC PK3CG_HUMAN TTHXGLJ BC Kinase TTHXGLJ SN p120-PI3K; p110gamma; Serine/threonine protein kinase PIK3CG; PtdIns-3-kinase subunit p110-gamma; PtdIns-3-kinase subunit gamma; PtdIns-3-kinase p110; Phosphoinositol-3 kinase; Phosphoinositide-3-kinase catalytic gamma polypeptide; Phosphoinositide 3-Kinase gamma; Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, gamma isoform; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform; Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma; PI3Kgamma; PI3K-gamma; PI3K; PI3-kinase subunit gamma; PI3-kinase p110 subunit gamma TTHXGLJ GN PIK3CG TTHXGLJ FC Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Together with PIK3CD participates in T-lymphocyte development. Required for B-lymphocyte development and signaling. Together with PIK3CD participates in neutrophil respiratory burst. Together with PIK3CD is involved in neutrophil chemotaxis and extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to GRK2 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contributes to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis. TTHXGLJ EC EC 2.7.1.153 TTHXGLJ PD 6GQ7; 6FH5; 6C1S; 6AUD; 5T23 TTHXGLJ SQ MELENYKQPVVLREDNCRRRRRMKPRSAAASLSSMELIPIEFVLPTSQRKCKSPETALLHVAGHGNVEQMKAQVWLRALETSVAADFYHRLGPHHFLLLYQKKGQWYEIYDKYQVVQTLDCLRYWKATHRSPGQIHLVQRHPPSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGLVTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDTPGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNGEEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRKFRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKIKDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEYVLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEGDRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQQEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYLLQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAYLRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGWTVQFNWFLHLVLGIKQGEKHSA TT0APVH ID TT0APVH TT0APVH TN HUMAN angiopoietin-2 (ANG-2) TT0APVH UP O15123 TT0APVH UC ANGP2_HUMAN TT0APVH BC Fibrinogen protein TT0APVH SN ANG-2 TT0APVH GN ANGPT2 TT0APVH FC Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal. Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. TT0APVH PD 4ZFG; 4JZC; 2GY7; 1Z3U; 1Z3S TT0APVH SQ MWQIVFFTLSCDLVLAAAYNNFRKSMDSIGKKQYQVQHGSCSYTFLLPEMDNCRSSSSPYVSNAVQRDAPLEYDDSVQRLQVLENIMENNTQWLMKLENYIQDNMKKEMVEIQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEINKLQDKNSFLEKKVLAMEDKHIIQLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVNNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQISFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGGGWTIIQRREDGSVDFQRTWKEYKVGFGNPSGEYWLGNEFVSQLTNQQRYVLKIHLKDWEGNEAYSLYEHFYLSSEELNYRIHLKGLTGTAGKISSISQPGNDFSTKDGDNDKCICKCSQMLTGGWWFDACGPSNLNGMYYPQRQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF TTQLO2H ID TTQLO2H TTQLO2H TN HUMAN C5a receptor (C5aR) TTQLO2H UP P21730 TTQLO2H UC C5AR1_HUMAN TTQLO2H BC GPCR rhodopsin TTQLO2H SN CD88; C5aR; C5a-R; C5a anaphylatoxin chemotactic receptor 1; C5R1 TTQLO2H GN C5AR1 TTQLO2H FC The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production. Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a. TTQLO2H PD 6C1R; 6C1Q; 5O9H TTQLO2H SQ MDSFNYTTPDYGHYDDKDTLDLNTPVDKTSNTLRVPDILALVIFAVVFLVGVLGNALVVWVTAFEAKRTINAIWFLNLAVADFLSCLALPILFTSIVQHHHWPFGGAACSILPSLILLNMYASILLLATISADRFLLVFKPIWCQNFRGAGLAWIACAVAWGLALLLTIPSFLYRVVREEYFPPKVLCGVDYSHDKRRERAVAIVRLVLGFLWPLLTLTICYTFILLRTWSRRATRSTKTLKVVVAVVASFFIFWLPYQVTGIMMSFLEPSSPTFLLLKKLDSLCVSFAYINCCINPIIYVVAGQGFQGRLRKSLPSLLRNVLTEESVVRESKSFTRSTVDTMAQKTQAV TTH91NV ID TTH91NV TTH91NV TN HUMAN C-C chemokine receptor 5 (CCR5) TTH91NV UP P51681 TTH91NV UC CCR5_HUMAN TTH91NV BC GPCR rhodopsin TTH91NV SN HIV-1 fusion coreceptor; HIV-1 fusion co-receptor; Chemokine receptor CCR5; CMKBR5; CHEMR13; CD195 antigen; CD195; CCR-5; CC-CKR-5; C-C CKR-5 TTH91NV GN CCR5 TTH91NV FC May play a role in the control of granulocytic lineage proliferation or differentiation. Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. TTH91NV PD 6MET; 6MEO; 6FGP; 5YY4; 5YD5 TTH91NV SQ MDYQVSSPIYDINYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNMLVILILINCKRLKSMTDIYLLNLAISDLFFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAVVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQKEGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQEISVGL TTR10KI ID TTR10KI TTR10KI TN HUMAN interferon gamma (IFNG) TTR10KI UP P01579 TTR10KI UC IFNG_HUMAN TTR10KI BC Cytokine: interferon TTR10KI SN Interferon gamma; Immune interferon; IFN-gamma TTR10KI GN IFNG TTR10KI FC Produced by lymphocytes activated by specific antigens or mitogens. IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions. It is a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. TTR10KI PD 6E3L; 6E3K; 3BES; 1HIG; 1FYH TTR10KI SQ MKYTSYILAFQLCIVLGSLGCYCQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ TT3JF7X ID TT3JF7X TT3JF7X TN HUMAN interleukin 8 (IL8) TT3JF7X UP P10145 TT3JF7X UC IL8_HUMAN TT3JF7X BC Cytokine: interleukin TT3JF7X SN T-cell chemotactic factor; Protein 3-10C; Neutrophil-activating protein 1; NAP-1; Monocyte-derived neutrophil-activating peptide; Monocyte-derived neutrophil chemotactic factor; MONAP; MDNCF; IL8; IL-8; Granulocyte chemotactic protein 1; GCP-1; Emoctakin; Chemokine (C-X-C motif) ligand 8; C-X-C motif chemokine 8 TT3JF7X GN CXCL8 TT3JF7X FC IL-8 is a chemotactic factor that attracts neutrophils, basophils, and T-cells, but not monocytes. It is also involved in neutrophil activation. It is released from several cell types in response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold higher activity on neutrophil activation, IL-8(5-77) has increased activity on neutrophil activation and IL-8(7-77) has a higher affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77), respectively. TT3JF7X PD 5WDZ; 5D14; 4XDX; 3IL8; 2IL8 TT3JF7X SQ MTSKLAVALLAAFLISAALCEGAVLPRSAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS TTAVUMS ID TTAVUMS TTAVUMS TN HUMAN toll-like receptor 2 (TLR2) TTAVUMS UP O60603 TTAVUMS UC TLR2_HUMAN TTAVUMS BC Toll-like receptor TTAVUMS SN Toll/interleukin-1 receptor-like protein 4; TIL4; CD282 TTAVUMS GN TLR2 TTAVUMS FC Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also activate immune cells and promote apoptosis in response to the lipid moiety of lipoproteins. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B. burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6. Stimulation of monocytes in vitro with M. tuberculosis PstS1 induces p38 MAPK and ERK1/2 activation primarily via this receptor, but also partially via TLR4. MAPK activation in response to bacterial peptidoglycan also occurs via this receptor. Acts as a receptor for M. tuberculosis lipoproteins LprA, LprG, LpqH and PstS1, some lipoproteins are dependent on other coreceptors (TLR1, CD14 and/or CD36); the lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen. M. tuberculosis HSP70 (dnaK) but not HSP65 (groEL-2) acts via this protein to stimulate NF-kappa-B expression. Recognizes M. tuberculosis major T-antigen EsxA (ESAT-6) which inhibits downstream MYD88-dependent signaling (shown in mouse). Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides. Required for normal uptake of M. tuberculosis, a process that is inhibited by M. tuberculosis LppM. Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. TTAVUMS PD 6NIG; 2Z80; 2Z7X; 1O77; 1FYX TTAVUMS SQ MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLMVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNIDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS TTLSU52 ID TTLSU52 TTLSU52 TN HUMAN toll-like receptor 6 (TLR6) TTLSU52 UP Q9Y2C9 TTLSU52 UC TLR6_HUMAN TTLSU52 BC Toll-like receptor TTLSU52 SN CD286 TTLSU52 GN TLR6 TTLSU52 FC Specifically recognizes diacylated and, to a lesser extent, triacylated lipopeptides. In response to diacylated lipopeptides, forms the activation cluster TLR2:TLR6:CD14:CD36, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B. burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR2. In complex with TLR4, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. Participates in the innate immune response to Gram-positive bacteria and fungi. TTLSU52 PD 4OM7 TTLSU52 SQ MTKDKEPIVKSFHFVCLMIIIVGTRIQFSDGNEFAVDKSKRGLIHVPKDLPLKTKVLDMSQNYIAELQVSDMSFLSELTVLRLSHNRIQLLDLSVFKFNQDLEYLDLSHNQLQKISCHPIVSFRHLDLSFNDFKALPICKEFGNLSQLNFLGLSAMKLQKLDLLPIAHLHLSYILLDLRNYYIKENETESLQILNAKTLHLVFHPTSLFAIQVNISVNTLGCLQLTNIKLNDDNCQVFIKFLSELTRGSTLLNFTLNHIETTWKCLVRVFQFLWPKPVEYLNIYNLTIIESIREEDFTYSKTTLKALTIEHITNQVFLFSQTALYTVFSEMNIMMLTISDTPFIHMLCPHAPSTFKFLNFTQNVFTDSIFEKCSTLVKLETLILQKNGLKDLFKVGLMTKDMPSLEILDVSWNSLESGRHKENCTWVESIVVLNLSSNMLTDSVFRCLPPRIKVLDLHSNKIKSVPKQVVKLEALQELNVAFNSLTDLPGCGSFSSLSVLIIDHNSVSHPSADFFQSCQKMRSIKAGDNPFQCTCELREFVKNIDQVSSEVLEGWPDSYKCDYPESYRGSPLKDFHMSELSCNITLLIVTIGATMLVLAVTVTSLCIYLDLPWYLRMVCQWTQTRRRARNIPLEELQRNLQFHAFISYSEHDSAWVKSELVPYLEKEDIQICLHERNFVPGKSIVENIINCIEKSYKSIFVLSPNFVQSEWCHYELYFAHHNLFHEGSNNLILILLEPIPQNSIPNKYHKLKALMTQRTYLQWPKEKSKRGLFWANIRAAFNMKLTLVTENNDVKS TT3FDB1 ID TT3FDB1 TT3FDB1 TN HUMAN transmembrane protease serine 2 (TMPRSS2) TT3FDB1 UP O15393 TT3FDB1 UC TMPS2_HUMAN TT3FDB1 BC Peptidase TT3FDB1 SN TMPRSS2 protease; TMPRSS2 TT3FDB1 GN TMPRSS2 TT3FDB1 FC Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus- cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike glycoprotein which activates the glycoprotein for cathepsin L- independent host cell entry. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity. TT3FDB1 EC EC 3.4.21.- TT3FDB1 SQ MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG TTWOH4Q ID TTWOH4Q TTWOH4Q TN MERS-CoV 3C-like proteinase (3CLpro) TTWOH4Q UP K9N7C7 (3248-3553) TTWOH4Q UC R1AB_CVEMC (3248-3553) TTWOH4Q BC Coronaviruses polyprotein 1ab family TTWOH4Q SN MERS-CoV 3C-like proteinase; MERS-CoV 3CLp; MERS-CoV 3CL-PRO; MERS-CoV 3CLpro TTWOH4Q GN MERS-CoV rep; MERS-CoV 1a-1b TTWOH4Q FC Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). TTWOH4Q EC EC 3.4.22.- TTWOH4Q SQ SGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLDNTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGAAFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQVHQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLYTGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQ TTZ3COY ID TTZ3COY TTZ3COY TN COVID-19 spike glycoprotein (S) TTZ3COY UP P0DTC2 TTZ3COY UC SPIKE_SARS2 TTZ3COY BC Betacoronaviruses spike protein family TTZ3COY SN COVID-19 S glycoprotein; COVID-19 E2; COVID-19 Peplomer protein TTZ3COY GN COVID-19 S TTZ3COY FC Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. TTZ3COY PD 6LVN; 6LXT; 6M0J; 6M17; 6VSB TTRJ91Q ID TTRJ91Q TTRJ91Q TN HUMAN complement C5 alpha (C5A) TTRJ91Q UP P01031 (678-1676) TTRJ91Q UC CO5_HUMAN (678-1676) TTRJ91Q BC Complement system TTRJ91Q SN Complement C5 alpha chain TTRJ91Q GN C5 TTRJ91Q FC Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes. C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation. TTRJ91Q SQ TLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC TT2LBCR ID TT2LBCR TT2LBCR TN HUMAN toll-like receptor 9 (TLR9) TT2LBCR UP Q9NR96 TT2LBCR UC TLR9_HUMAN TT2LBCR BC Toll-like receptor TT2LBCR SN UNQ5798/PRO19605; TLR-9; CD289 TT2LBCR GN TLR9 TT2LBCR FC Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR9 is a nucleotide-sensing TLR which is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Controls lymphocyte response to Helicobacter infection. Upon CpG stimulation, induces B-cell proliferation, activation, survival and antibody production. TT2LBCR SQ MGFCRSALHPLSLLVQAIMLAMTLALGTLPAFLPCELQPHGLVNCNWLFLKSVPHFSMAAPRGNVTSLSLSSNRIHHLHDSDFAHLPSLRHLNLKWNCPPVGLSPMHFPCHMTIEPSTFLAVPTLEELNLSYNNIMTVPALPKSLISLSLSHTNILMLDSASLAGLHALRFLFMDGNCYYKNPCRQALEVAPGALLGLGNLTHLSLKYNNLTVVPRNLPSSLEYLLLSYNRIVKLAPEDLANLTALRVLDVGGNCRRCDHAPNPCMECPRHFPQLHPDTFSHLSRLEGLVLKDSSLSWLNASWFRGLGNLRVLDLSENFLYKCITKTKAFQGLTQLRKLNLSFNYQKRVSFAHLSLAPSFGSLVALKELDMHGIFFRSLDETTLRPLARLPMLQTLRLQMNFINQAQLGIFRAFPGLRYVDLSDNRISGASELTATMGEADGGEKVWLQPGDLAPAPVDTPSSEDFRPNCSTLNFTLDLSRNNLVTVQPEMFAQLSHLQCLRLSHNCISQAVNGSQFLPLTGLQVLDLSHNKLDLYHEHSFTELPRLEALDLSYNSQPFGMQGVGHNFSFVAHLRTLRHLSLAHNNIHSQVSQQLCSTSLRALDFSGNALGHMWAEGDLYLHFFQGLSGLIWLDLSQNRLHTLLPQTLRNLPKSLQVLRLRDNYLAFFKWWSLHFLPKLEVLDLAGNQLKALTNGSLPAGTRLRRLDVSCNSISFVAPGFFSKAKELRELNLSANALKTVDHSWFGPLASALQILDVSANPLHCACGAAFMDFLLEVQAAVPGLPSRVKCGSPGQLQGLSIFAQDLRLCLDEALSWDCFALSLLAVALGLGVPMLHHLCGWDLWYCFHLCLAWLPWRGRQSGRDEDALPYDAFVVFDKTQSAVADWVYNELRGQLEECRGRWALRLCLEERDWLPGKTLFENLWASVYGSRKTLFVLAHTDRVSGLLRASFLLAQQRLLEDRKDVVVLVILSPDGRRSRYVRLRQRLCRQSVLLWPHQPSGQRSFWAQLGMALTRDNHHFYNRNFCQGPTAE TTHQJ2Y ID TTHQJ2Y TTHQJ2Y TN HUMAN two pore channel subtype 2 (TPC2) TTHQJ2Y UP Q8NHX9 TTHQJ2Y UC TPC2_HUMAN TTHQJ2Y SN Voltage-dependent calcium channel protein TPC2; TPC2 TTHQJ2Y GN TPCN2 TTHQJ2Y FC Nicotinic acid adenine dinucleotide phosphate (NAADP) receptor that may function as one of the major voltage-gated Ca(2+) channels (VDCC) across the lysosomal membrane. May be involved in smooth muscle contraction. TTHQJ2Y PD 6NQ2; 6NQ1; 6NQ0 TTHQJ2Y SQ MAEPQAESEPLLGGARGGGGDWPAGLTTYRSIQVGPGAAARWDLCIDQAVVFIEDAIQYRSINHRVDASSMWLYRRYYSNVCQRTLSFTIFLILFLAFIETPSSLTSTADVRYRAAPWEPPCGLTESVEVLCLLVFAADLSVKGYLFGWAHFQKNLWLLGYLVVLVVSLVDWTVSLSLVCHEPLRIRRLLRPFFLLQNSSMMKKTLKCIRWSLPEMASVGLLLAIHLCLFTMFGMLLFAGGKQDDGQDRERLTYFQNLPESLTSLLVLLTTANNPDVMIPAYSKNRAYAIFFIVFTVIGSLFLMNLLTAIIYSQFRGYLMKSLQTSLFRRRLGTRAAFEVLSSMVGEGGAFPQAVGVKPQNLLQVLQKVQLDSSHKQAMMEKVRSYGSVLLSAEEFQKLFNELDRSVVKEHPPRPEYQSPFLQSAQFLFGHYYFDYLGNLIALANLVSICVFLVLDADVLPAERDDFILGILNCVFIVYYLLEMLLKVFALGLRGYLSYPSNVFDGLLTVVLLVLEISTLAVYRLPHPGWRPEMVGLLSLWDMTRMLNMLIVFRFLRIIPSMKLMAVVASTVLGLVQNMRAFGGILVVVYYVFAIIGINLFRGVIVALPGNSSLAPANGSAPCGSFEQLEYWANNFDDFAAALVTLWNLMVVNNWQVFLDAYRRYSGPWSKIYFVLWWLVSSVIWVNLFLALILENFLHKWDPRSHLQPLAGTPEATYQMTVELLFRDILEEPGEDELTERLSQHPHLWLCR TT45V0U ID TT45V0U TT45V0U TN HUMAN calpain-1/calpain small subunit 1 heterodimer (CAPN1/CAPNS1) TT45V0U UP P07384/P04632 TT45V0U UC CAN1_HUMAN/CPNS1_HUMAN TT45V0U BC Peptidase C2 family TT45V0U SN Calpain-1 large subunit/calpain small subunit 1 dimer TT45V0U FC Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. TT45V0U SQ MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA TTO361H ID TTO361H TTO361H TN HUMAN calpain-2/calpain small subunit 1 heterodimer (CAPN2/CAPNS1) TTO361H UP P17655/P04632 TTO361H UC CAN2_HUMAN/CPNS1_HUMAN TTO361H BC Peptidase C2 family TTO361H SN Calpain-2 large subunit/calpain small subunit 1 dimer TTO361H FC Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'. Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs. TTO361H SQ MAGIAAKLAKDREAAEGLGSHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDNCPSWNTIDPEERERLTRRHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELSGQTNIHLSKNFFLTNRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL TT6RIOV ID TT6RIOV TT6RIOV TN Acyl-CoA desaturase (SCD) TT6RIOV UP O00767 TT6RIOV UC ACOD_HUMAN TT6RIOV BC Paired donor oxygen oxidoreductase TT6RIOV SN hSCD1; Stearoyl-coenzyme A (Delta9) desaturase; Stearoyl-CoA desaturase; Membrane-bound 9 desaturase; Fatty acid desaturase; DesA3; Des A3; Delta-9-stearoyl desaturase; Delta-9 desaturase; Delta(9)-desaturase; 9 stearoyl-desaturase TT6RIOV GN SCD TT6RIOV FC Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation. Plays an important role in body energy homeostasis. Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides. Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. TT6RIOV EC EC 1.14.19.1 TT6RIOV PD 4ZYO TT6RIOV SQ MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYKDKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAHRLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGETFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNYHHSFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAILARIKRTGDGNYKSG TT6RIOV TT Successful TT6RIOV FM Oxidoreductases acting on paired donors TT6RIOV KE mtc01100:Metabolic pathways TTK25J1 ID TTK25J1 TTK25J1 TN Adenosine A1 receptor (ADORA1) TTK25J1 UP P30542 TTK25J1 UC AA1R_HUMAN TTK25J1 BC GPCR rhodopsin TTK25J1 SN Adenosine receptor A1; A(1) adenosine receptor TTK25J1 GN ADORA1 TTK25J1 FC The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Receptor for adenosine. TTK25J1 PD 6D9H; 5UEN; 5N2S TTK25J1 SQ MPPSISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGALVIPLAILINIGPQTYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKMVVTPRRAAVAIAGCWILSFVVGLTPMFGWNNLSAVERAWAANGSMGEPVIKCEFEKVISMEYMVYFNFFVWVLPPLLLMVLIYLEVFYLIRKQLNKKVSASSGDPQKYYGKELKIAKSLALILFLFALSWLPLHILNCITLFCPSCHKPSILTYIAIFLTHGNSAMNPIVYAFRIQKFRVTFLKIWNDHFRCQPAPPIDEDLPEERPDD TTK25J1 TT Successful TTK25J1 FM GPCR rhodopsin TTK25J1 KE hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa05032:Morphine addiction TTK25J1 RC R-HSA-417973:Adenosine P1 receptors; R-HSA-418594:G alpha (i) signalling events TTPMQSO ID TTPMQSO TTPMQSO TN ALK tyrosine kinase receptor (ALK) TTPMQSO UP Q9UM73 TTPMQSO UC ALK_HUMAN TTPMQSO BC Kinase TTPMQSO SN CD246; Anaplastic lymphoma kinase TTPMQSO GN ALK TTPMQSO FC Transduces signals from ligands at the cell surface, through specific activation of the mitogen-activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif. Following activation by ligand, ALK induces tyrosine phosphorylation of CBL, FRS2, IRS1 and SHC1, as well as of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Acts as a receptor for ligands pleiotrophin (PTN), a secreted growth factor, and midkine (MDK), a PTN-related factor, thus participating in PTN and MDK signal transduction. PTN-binding induces MAPK pathway activation, which is important for the anti-apoptotic signaling of PTN and regulation of cell proliferation. MDK-binding induces phosphorylation of the ALK target insulin receptor substrate (IRS1), activates mitogen-activated protein kinases (MAPKs) and PI3-kinase, resulting also in cell proliferation induction. Drives NF-kappa-B activation, probably through IRS1 and the activation of the AKT serine/threonine kinase. Recruitment of IRS1 to activated ALK and the activation of NF-kappa-B are essential for the autocrine growth and survival signaling of MDK. Neuronal receptor tyrosine kinase that is essentially and transiently expressed in specific regions of the central and peripheral nervous systems and plays an important role in the genesis and differentiation of the nervous system. TTPMQSO EC EC 2.7.10.1 TTPMQSO PD 6MX8; 6EDL; 6EBW; 6E0R; 6CDT TTPMQSO SQ MGAIGLLWLLPLLLSTAAVGSGMGTGQRAGSPAAGPPLQPREPLSYSRLQRKSLAVDFVVPSLFRVYARDLLLPPSSSELKAGRPEARGSLALDCAPLLRLLGPAPGVSWTAGSPAPAEARTLSRVLKGGSVRKLRRAKQLVLELGEEAILEGCVGPPGEAAVGLLQFNLSELFSWWIRQGEGRLRIRLMPEKKASEVGREGRLSAAIRASQPRLLFQIFGTGHSSLESPTNMPSPSPDYFTWNLTWIMKDSFPFLSHRSRYGLECSFDFPCELEYSPPLHDLRNQSWSWRRIPSEEASQMDLLDGPGAERSKEMPRGSFLLLNTSADSKHTILSPWMRSSSEHCTLAVSVHRHLQPSGRYIAQLLPHNEAAREILLMPTPGKHGWTVLQGRIGRPDNPFRVALEYISSGNRSLSAVDFFALKNCSEGTSPGSKMALQSSFTCWNGTVLQLGQACDFHQDCAQGEDESQMCRKLPVGFYCNFEDGFCGWTQGTLSPHTPQWQVRTLKDARFQDHQDHALLLSTTDVPASESATVTSATFPAPIKSSPCELRMSWLIRGVLRGNVSLVLVENKTGKEQGRMVWHVAAYEGLSLWQWMVLPLLDVSDRFWLQMVAWWGQGSRAIVAFDNISISLDCYLTISGEDKILQNTAPKSRNLFERNPNKELKPGENSPRQTPIFDPTVHWLFTTCGASGPHGPTQAQCNNAYQNSNLSVEVGSEGPLKGIQIWKVPATDTYSISGYGAAGGKGGKNTMMRSHGVSVLGIFNLEKDDMLYILVGQQGEDACPSTNQLIQKVCIGENNVIEEEIRVNRSVHEWAGGGGGGGGATYVFKMKDGVPVPLIIAAGGGGRAYGAKTDTFHPERLENNSSVLGLNGNSGAAGGGGGWNDNTSLLWAGKSLQEGATGGHSCPQAMKKWGWETRGGFGGGGGGCSSGGGGGGYIGGNAASNNDPEMDGEDGVSFISPLGILYTPALKVMEGHGEVNIKHYLNCSHCEVDECHMDPESHKVICFCDHGTVLAEDGVSCIVSPTPEPHLPLSLILSVVTSALVAALVLAFSGIMIVYRRKHQELQAMQMELQSPEYKLSKLRTSTIMTDYNPNYCFAGKTSSISDLKEVPRKNITLIRGLGHGAFGEVYEGQVSGMPNDPSPLQVAVKTLPEVCSEQDELDFLMEALIISKFNHQNIVRCIGVSLQSLPRFILLELMAGGDLKSFLRETRPRPSQPSSLAMLDLLHVARDIACGCQYLEENHFIHRDIAARNCLLTCPGPGRVAKIGDFGMARDIYRASYYRKGGCAMLPVKWMPPEAFMEGIFTSKTDTWSFGVLLWEIFSLGYMPYPSKSNQEVLEFVTSGGRMDPPKNCPGPVYRIMTQCWQHQPEDRPNFAIILERIEYCTQDPDVINTALPIEYGPLVEEEEKVPVRPKDPEGVPPLLVSQQAKREEERSPAAPPPLPTTSSGKAAKKPTAAEISVRVPRGPAVEGGHVNMAFSQSNPPSELHKVHGSRNKPTSLWNPTYGSWFTEKPTKKNNPIAKKEPHDRGNLGLEGSCTVPPNVATGRLPGASLLLEPSSLTANMKEVPLFRLRHFPCGNVNYGYQQQGLPLEAATAPGAGHYEDTILKSKNSMNQPGP TTPMQSO TT Successful TTPMQSO FM Kinase TTPMQSO KE hsa05223:Non-small cell lung cancer TTS64P2 ID TTS64P2 TTS64P2 TN Androgen receptor (AR) TTS64P2 UP P10275 TTS64P2 UC ANDR_HUMAN TTS64P2 BC Nuclear hormone receptor TTS64P2 SN Testosterone receptor; Nuclear receptor subfamily 3 group C member 4; NR3C4; Dihydrotestosterone receptor; DHTR TTS64P2 GN AR TTS64P2 FC Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. TTS64P2 PD 5VO4; 5V8Q; 5T8J; 5T8E; 5JJM TTS64P2 SQ MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSALECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPYGYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ TTS64P2 TT Successful TTS64P2 FM Zinc finger TTS64P2 KE hsa04114:Oocyte meiosis; hsa05200:Pathways in cancer; hsa05215:Prostate cancer TTS64P2 RC R-HSA-383280:Nuclear Receptor transcription pathway; R-HSA-5625886:Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 TT8DBY3 ID TT8DBY3 TT8DBY3 TN Angiotensin II receptor type-1 (AGTR1) TT8DBY3 UP P30556 TT8DBY3 UC AGTR1_HUMAN TT8DBY3 BC GPCR rhodopsin TT8DBY3 SN Type-1 angiotensin II receptor; Angiotensin II type-1 receptor; Angiotensin II receptor 1; Angiotensin 1 receptor; AT2R1B; AT2R1; AT1BR; AT1AR; AT1; AGTR1B; AGTR1A TT8DBY3 GN AGTR1 TT8DBY3 FC Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Receptor for angiotensin II. TT8DBY3 PD 6DO1; 4ZUD; 4YAY; 1ZV0 TT8DBY3 SQ MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPAPCFEVE TT8DBY3 TT Successful TT8DBY3 FM GPCR rhodopsin TT8DBY3 KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04614:Renin-angiotensin system; hsa04924:Renin secretion; hsa05200:Pathways in cancer TT8DBY3 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTL69WB ID TTL69WB TTL69WB TN Angiotensin-converting enzyme (ACE) TTL69WB UP P12821 TTL69WB UC ACE_HUMAN TTL69WB BC Glycosylase TTL69WB SN Kininase II; Dipeptidyl carboxypeptidase I; DCP1; DCP; CD143 antigen; CD143; ACE TTL69WB GN SLC33A1 TTL69WB FC Able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. TTL69WB EC EC 3.2.1.- TTL69WB PD 6QS1; 6H5X; 6H5W; 6F9V; 6F9U TTL69WB SQ MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSADEAGAQLFAQSYNSSAEQVLFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQAGSSRPWQEVLKDMVGLDALDAQPLLKYFQPVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQARVGQWLLLFLGIALLVATLGLSQRLFSIRHRSLHRHSHGPQFGSEVELRHS TTL69WB TT Successful TTL69WB FM Peptidase TTL69WB KE hsa04614:Renin-angiotensin system; hsa05142:Chagas disease (American trypanosomiasis); hsa05410:Hypertrophic cardiomyopathy (HCM) TTL69WB RC R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins TTB2MXP ID TTB2MXP TTB2MXP TN Angiotensinogenase renin (REN) TTB2MXP UP P00797 TTB2MXP UC RENI_HUMAN TTB2MXP BC Peptidase TTB2MXP SN Renin; Angiotensinogenase TTB2MXP GN REN TTB2MXP FC Renin is a highly specific endopeptidase, whose only knownfunction is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. TTB2MXP EC EC 3.4.23.15 TTB2MXP PD 6I3F; 5VRP; 5VPM; 5V8V; 5TMK TTB2MXP SQ MDGWRRMPRWGLLLLLWGSCTFGLPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR TTB2MXP TT Successful TTB2MXP KE hsa04614:Renin-angiotensin system TTB2MXP RC R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins TTSZLWK ID TTSZLWK TTSZLWK TN Aromatase (CYP19A1) TTSZLWK UP P11511 TTSZLWK UC CP19A_HUMAN TTSZLWK BC Paired donor oxygen oxidoreductase TTSZLWK SN P-450AROM; Estrogen synthetase; Estrogen synthase; Cytochrome P450 19A1; Cytochrome P-450AROM; CYPXIX; CYP19; CYAR; ARO1 TTSZLWK GN CYP19A1 TTSZLWK FC Catalyzes the formation of aromatic C18 estrogens from C19 androgens. TTSZLWK EC EC 1.14.14.14 TTSZLWK PD 5JL9; 5JL7; 5JL6; 5JKW; 5JKV TTSZLWK SQ MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLISHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHPDETKNMLEMIFTPRNSDRCLEH TTSZLWK TT Successful TTSZLWK FM Oxidoreductases acting on paired donors TTSZLWK KE hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways; hsa04913:Ovarian steroidogenesis TTSZLWK RC R-HSA-211976:Endogenous sterols TTN451K ID TTN451K TTN451K TN Aromatic-L-amino-acid decarboxylase (DDC) TTN451K UP P20711 TTN451K UC DDC_HUMAN TTN451K BC Carbon-carbon lyase TTN451K SN DOPA decarboxylase; AADC TTN451K GN DDC TTN451K FC Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. TTN451K EC EC 4.1.1.28 TTN451K PD 3RCH; 3RBL; 3RBF TTN451K SQ MNASEFRRRGKEMVDYMANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDVEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIMEKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMVATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVNEALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE TTN451K TT Successful TTN451K FM Carbon carbon lyase TTN451K KE hsa00340:Histidine metabolism; hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism; hsa00380:Tryptophan metabolism; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse; hsa04728:Dopaminergic synapse; hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05034:Alcoholism TTA4LDE ID TTA4LDE TTA4LDE TN Calcineurin (PPP3CA) TTA4LDE UP Q08209 TTA4LDE UC PP2BA_HUMAN TTA4LDE BC Phosphoric monoester hydrolase TTA4LDE SN Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform; Calmodulin-dependent calcineurin A subunit alpha isoform; CNA; CAM-PRP catalytic subunit; CALNA TTA4LDE GN PPP3CA TTA4LDE FC Many of the substrates contain a PxIxIT motif and/or a LxVP motif. In response to increased Ca(2+) levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation. In response to increased Ca(2+) levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion. Dephosphorylates heat shock protein HSPB1. Dephosphorylates and activates transcription factor NFATC1. In response to increased Ca(2+) levels, regulates NFAT-mediated transcription probably by dephosphorylating NFAT and promoting its nuclear translocation. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32. May dephosphorylate CRTC2 at 'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins. Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. TTA4LDE EC EC 3.1.3.16 TTA4LDE PD 5SVE; 5C1V; 4Q5U; 4F0Z; 3LL8 TTA4LDE SQ MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITSFEEAKGLDRINERMPPRRDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ TTA4LDE TT Successful TTA4LDE FM Phosphoric monoester hydrolase TTA4LDE KE hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04114:Oocyte meiosis; hsa04210:Apoptosis; hsa04310:Wnt signaling pathway; hsa04360:Axon guidance; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04720:Long-term potentiation; hsa04724:Glutamatergic synapse; hsa04728:Dopaminergic synapse; hsa04921:Oxytocin signaling pathway; hsa04922:Glucagon signaling pathway; hsa05010:Alzheimer's disease; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05031:Amphetamine addiction; hsa05152:Tuberculosis; hsa05166:HTLV-I infection TTA4LDE RC R-HSA-180024:DARPP-32 events; R-HSA-2871809:FCERI mediated Ca+2 mobilization; R-HSA-4086398:Ca2+ pathway TTU6BFZ ID TTU6BFZ TTU6BFZ TN Candida Thymidylate synthase (Candi TMP1) TTU6BFZ UP P12461 TTU6BFZ UC TYSY_CANAL TTU6BFZ BC Methyltransferase TTU6BFZ SN Tsase of Candida albicans; TS of Candida albicans; TMP1; Human recombinant thymidylate synthase; HrTS TTU6BFZ GN Candi TMP1 TTU6BFZ FC Contributes to thede novo mitochondrial thymidylate biosynthesis pathway. TTU6BFZ EC EC 2.1.1.45 TTU6BFZ SQ MTVSPNTAEQAYLDLCKRIIDEGEHRPDRTGTGTKSLFAPPQLRFDLSNDTFPLLTTKKVFSKGIIHELLWFVAGSTDAKILSEKGVKIWEGNGSREFLDKLGLTHRREGDLGPVYGFQWRHFGAEYKDCDSDYTGQGFDQLQDVIKKLKTNPYDRRIIMSAWNPPDFAKMALPPCHVFCQFYVNFPTSSPDPNNPKQAKTAKPKLSCLLYQRSCDMGLGVPFNIASYALLTKMIAHVVDMDCGEFIHTLGDAHVYLDHIDALKEQFERIPKQFPKLVIKEERKNEIKSIDDFKFEDFEIVGYEPYPPIKMKMSV TTU6BFZ TT Successful TTU6BFZ KE hsa00240:Pyrimidine metabolism; hsa00670:One carbon pool by folate; hsa01100:Metabolic pathways TTU6BFZ RC R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-500753:Pyrimidine biosynthesis; R-HSA-69205:G1/S-Specific Transcription TTMSFAW ID TTMSFAW TTMSFAW TN Cannabinoid receptor 2 (CB2) TTMSFAW UP P34972 TTMSFAW UC CNR2_HUMAN TTMSFAW BC GPCR rhodopsin TTMSFAW SN hCB2; Cannabinoid CB2 receptor; CX5; CB2B; CB2A; CB-2 TTMSFAW GN CNR2 TTMSFAW FC May function in inflammatory response, nociceptive transmission and bone homeostasis. Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. TTMSFAW PD 5ZTY; 2KI9 TTMSFAW SQ MEECWVTEIANGSKDGLDSNPMKDYMILSGPQKTAVAVLCTLLGLLSALENVAVLYLILSSHQLRRKPSYLFIGSLAGADFLASVVFACSFVNFHVFHGVDSKAVFLLKIGSVTMTFTASVGSLLLTAIDRYLCLRYPPSYKALLTRGRALVTLGIMWVLSALVSYLPLMGWTCCPRPCSELFPLIPNDYLLSWLLFIAFLFSGIIYTYGHVLWKAHQHVASLSGHQDRQVPGMARMRLDVRLAKTLGLVLAVLLICWFPVLALMAHSLATTLSDQVKKAFAFCSMLCLINSMVNPVIYALRSGEIRSSAHHCLAHWKKCVRGLGSEAKEEAPRSSVTETEADGKITPWPDSRDLDLSDC TTMSFAW TT Successful TTMSFAW FM GPCR rhodopsin TTMSFAW KE hsa04080:Neuroactive ligand-receptor interaction TTMSFAW RC R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events TTCFSPE ID TTCFSPE TTCFSPE TN Carbonic anhydrase VI (CA-VI) TTCFSPE UP P23280 TTCFSPE UC CAH6_HUMAN TTCFSPE BC Alpha-carbonic anhydrase TTCFSPE SN Secreted carbonic anhydrase; Salivary carbonic anhydrase; Carbonic anhydrase 6; Carbonate dehydratase VI TTCFSPE GN CA6 TTCFSPE FC Its role in saliva is unknown. Reversible hydration of carbon dioxide. TTCFSPE EC EC 4.2.1.1 TTCFSPE PD 3FE4 TTCFSPE SQ MRALVLLLSLFLLGGQAQHVSDWTYSEGALDEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQMHFHWGGASSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNYPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKTIHNDYRRTQPLNHRVVESNFPNQEYTLGSEFQFYLHKIEEILDYLRRALN TTCFSPE TT Successful TTCFSPE FM Carbon oxygen lyase TTCFSPE KE hsa00910:Nitrogen metabolism TTCFSPE RC R-HSA-1475029:Reversible hydration of carbon dioxide TTSYM0R ID TTSYM0R TTSYM0R TN Carbonic anhydrase XII (CA-XII) TTSYM0R UP O43570 TTSYM0R UC CAH12_HUMAN TTSYM0R BC Alpha-carbonic anhydrase TTSYM0R SN Tumor antigen HOM-RCC-3.1.3; Carbonic anhydrase 12; Carbonate dehydratase XII TTSYM0R GN CA12 TTSYM0R FC Reversible hydration of carbon dioxide. TTSYM0R EC EC 4.2.1.1 TTSYM0R PD 6G7A; 6G5L; 5MSB; 5MSA; 5LLP TTSYM0R SQ MPRRSLHAAAVLLLVILKEQPSSPAPVNGSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGLQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSHLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPREMINNFRQVQKFDERLVYTSFSQVQVCTAAGLSLGIILSLALAGILGICIVVVVSIWLFRRKSIKKGDNKGVIYKPATKMETEAHA TTSYM0R TT Successful TTSYM0R KE hsa00910:Nitrogen metabolism TTSYM0R RC R-HSA-1475029:Reversible hydration of carbon dioxide TTEYTKG ID TTEYTKG TTEYTKG TN Carbonic anhydrase XIV (CA-XIV) TTEYTKG UP Q9ULX7 TTEYTKG UC CAH14_HUMAN TTEYTKG BC Alpha-carbonic anhydrase TTEYTKG SN UNQ690/PRO1335; Carbonic anhydrase 14; Carbonate dehydratase XIV TTEYTKG GN CA14 TTEYTKG FC Reversible hydration of carbon dioxide. TTEYTKG EC EC 4.2.1.1 TTEYTKG PD 5CJF; 4LU3 TTEYTKG SQ MLFSALLLEVIWILAADGGQHWTYEGPHGQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPLDLHNNGHTVQLSLPSTLYLGGLPRKYVAAQLHLHWGQKGSPGGSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGETKNIAYEHILSHLHEVRHKDQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNYRALQPLNQRMVFASFIQAGSSYTTGEMLSLGVGILVGCLCLLLAVYFIARKIRKKRLENRKSVVFTSAQATTEA TTEYTKG TT Successful TTEYTKG KE hsa00910:Nitrogen metabolism TTEYTKG RC R-HSA-1475029:Reversible hydration of carbon dioxide TTKWFB8 ID TTKWFB8 TTKWFB8 TN Catechol-O-methyl-transferase (COMT) TTKWFB8 UP P21964 TTKWFB8 UC COMT_HUMAN TTKWFB8 BC Methyltransferase TTKWFB8 SN S-COMT; MB-COMT; Catechol-O-methyltransferase; COMT TTKWFB8 GN COMT TTKWFB8 FC Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. TTKWFB8 EC EC 2.1.1.6 TTKWFB8 PD 5LSA; 4XUE; 4XUD; 4XUC; 4PYK TTKWFB8 SQ MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP TTKWFB8 TT Successful TTKWFB8 KE hsa00140:Steroid hormone biosynthesis; hsa00350:Tyrosine metabolism; hsa01100:Metabolic pathways; hsa04728:Dopaminergic synapse TT2WR1T ID TT2WR1T TT2WR1T TN Cationic trypsinogen (PRSS1) TT2WR1T UP P07477 TT2WR1T UC TRY1_HUMAN TT2WR1T BC Peptidase TT2WR1T SN Trypsin-1; Trypsin I; TRYP1; TRY1; TRP1; Serine protease 1; Beta-trypsin TT2WR1T GN PRSS1 TT2WR1T FC Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates. TT2WR1T EC EC 3.4.21.4 TT2WR1T PD 4WXV; 4WWY; 2RA3; 1TRN; 1FXY TT2WR1T SQ MNPLLILTFVAAALAAPFDDDDKIVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS TT2WR1T TT Successful TT2WR1T KE hsa04080:Neuroactive ligand-receptor interaction; hsa04972:Pancreatic secretion; hsa04974:Protein digestion and absorption; hsa05164:Influenza A TT2WR1T RC R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-196741:Cobalamin (Cbl, vitamin B12) transport and metabolism TT2CEJG ID TT2CEJG TT2CEJG TN C-C chemokine receptor type 5 (CCR5) TT2CEJG UP P51681 TT2CEJG UC CCR5_HUMAN TT2CEJG BC GPCR rhodopsin TT2CEJG SN HIV-1 fusion coreceptor; HIV-1 fusion co-receptor; Chemokine receptor CCR5; CMKBR5; CHEMR13; CD195 antigen; CD195; CCR-5; CC-CKR-5; C-C CKR-5 TT2CEJG GN CCR5 TT2CEJG FC May play a role in the control of granulocytic lineage proliferation or differentiation. Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. TT2CEJG PD 6MET; 6MEO; 6FGP; 5YY4; 5YD5 TT2CEJG SQ MDYQVSSPIYDINYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNMLVILILINCKRLKSMTDIYLLNLAISDLFFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAVVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQKEGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQEISVGL TT2CEJG TT Successful TT2CEJG KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa05145:Toxoplasmosis; hsa05203:Viral carcinogenesis TT2CEJG RC R-HSA-173107:Binding and entry of HIV virion; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TT6L509 ID TT6L509 TT6L509 TN Coagulation factor IIa (F2) TT6L509 UP P00734 TT6L509 UC THRB_HUMAN TT6L509 BC Peptidase TT6L509 SN Prothrombin; Coagulation factor II TT6L509 GN F2 TT6L509 FC Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. TT6L509 EC EC 3.4.21.5 TT6L509 PD 8KME; 7KME; 6EO9; 6EO8; 6EO7 TT6L509 SQ MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE TT6L509 TT Successful TT6L509 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04610:Complement and coagulation cascades; hsa04810:Regulation of actin cytoskeleton TT6L509 RC R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-140875:Common Pathway of Fibrin Clot Formation; R-HSA-159740:Gamma-carboxylation of protein precursors; R-HSA-159763:Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus; R-HSA-159782:Removal of aminoterminal propeptides from gamma-carboxylated proteins; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-375276:Peptide ligand-binding receptors; R-HSA-381426:Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-416476:G alpha (q) signalling events; R-HSA-456926:Thrombin signalling through proteinase activated receptors (PARs) TTFEZ5Q ID TTFEZ5Q TTFEZ5Q TN Coagulation factor IX (F9) TTFEZ5Q UP P00740 TTFEZ5Q UC FA9_HUMAN TTFEZ5Q BC Peptidase TTFEZ5Q SN Plasma thromboplastin component; PTC protein; Factor IX; Christmas factor TTFEZ5Q GN F9 TTFEZ5Q FC Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. TTFEZ5Q EC EC 3.4.21.22 TTFEZ5Q PD 6MV4; 5VYG; 5TNT; 5TNO; 5JBC TTFEZ5Q SQ MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT TTFEZ5Q TT Successful TTFEZ5Q FM Peptidase TTFEZ5Q KE hsa04610:Complement and coagulation cascades TTFEZ5Q RC R-HSA-140834:Extrinsic Pathway of Fibrin Clot Formation; R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-159740:Gamma-carboxylation of protein precursors; R-HSA-159763:Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus; R-HSA-159782:Removal of aminoterminal propeptides from gamma-carboxylated proteins TTF0EGX ID TTF0EGX TTF0EGX TN Coagulation factor VII (F7) TTF0EGX UP P08709 TTF0EGX UC FA7_HUMAN TTF0EGX BC Peptidase TTF0EGX SN Serum prothrombin conversion accelerator; SPCA; Proconvertin; Eptacog alfa TTF0EGX GN F7 TTF0EGX FC Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium. TTF0EGX EC EC 3.4.21.21 TTF0EGX PD 5U6J; 5TQG; 5TQF; 5TQE; 5PB6 TTF0EGX SQ MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP TTF0EGX TT Successful TTF0EGX KE hsa04610:Complement and coagulation cascades TTF0EGX RC R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-140834:Extrinsic Pathway of Fibrin Clot Formation; R-HSA-159740:Gamma-carboxylation of protein precursors; R-HSA-159763:Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus; R-HSA-159782:Removal of aminoterminal propeptides from gamma-carboxylated proteins TTCIHJA ID TTCIHJA TTCIHJA TN Coagulation factor Xa (F10) TTCIHJA UP P00742 TTCIHJA UC FA10_HUMAN TTCIHJA BC Peptidase TTCIHJA SN Fxa; Factor Xa; F10; Activated coagulation factor X TTCIHJA GN F10 TTCIHJA FC Factor Xa is avitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. TTCIHJA EC EC 3.4.21.6 TTCIHJA PD 6RK9; 5VOF; 5VOE; 5K0H; 5JZU TTCIHJA SQ MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK TTCIHJA TT Successful TTCIHJA KE hsa04610:Complement and coagulation cascades TTCIHJA RC R-HSA-140834:Extrinsic Pathway of Fibrin Clot Formation; R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-140875:Common Pathway of Fibrin Clot Formation; R-HSA-159740:Gamma-carboxylation of protein precursors; R-HSA-159763:Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus; R-HSA-159782:Removal of aminoterminal propeptides from gamma-carboxylated proteins TT7LRQH ID TT7LRQH TT7LRQH TN Complement C1s component (C1S) TT7LRQH UP P09871 TT7LRQH UC C1S_HUMAN TT7LRQH BC Peptidase TT7LRQH SN Complement component 1 subcomponent s; Complement C1s subcomponent; C1-esterase; C1 esterase TT7LRQH GN C1S TT7LRQH FC C1r activates C1s so that it can, in turn, activate C2 and C4. C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. TT7LRQH EC EC 3.4.21.42 TT7LRQH PD 6F1H; 6F1C; 4LOT; 4LOS; 4LOR TT7LRQH SQ MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIELSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVFVAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCGIPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPKCVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGNREPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVKMGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKVEKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCGTYGLYTRVKNYVDWIMKTMQENSTPRED TT7LRQH TT Successful TT7LRQH FM Peptidase TT7LRQH KE hsa04610:Complement and coagulation cascades; hsa05133:Pertussis; hsa05150:Staphylococcus aureus infection; hsa05322:Systemic lupus erythematosus TT0PG8F ID TT0PG8F TT0PG8F TN Cyclin-dependent kinase 4 (CDK4) TT0PG8F UP P11802 TT0PG8F UC CDK4_HUMAN TT0PG8F BC Kinase TT0PG8F SN PSK-J3; Cell division protein kinase 4 TT0PG8F GN CDK4 TT0PG8F FC Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. TT0PG8F EC EC 2.7.11.22 TT0PG8F PD 5FWP; 5FWM; 5FWL; 5FWK; 3G33 TT0PG8F SQ MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE TT0PG8F TT Successful TT0PG8F FM Kinase TT0PG8F KE hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04530:Tight junction; hsa04660:T cell receptor signaling pathway; hsa05161:Hepatitis B; hsa05162:Measles; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05212:Pancreatic cancer; hsa05214:Glioma; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer TT0PG8F RC R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-2559585:Oncogene Induced Senescence; R-HSA-3214858:RMTs methylate histone arginines; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-69229:Ubiquitin-dependent degradation of Cyclin D1; R-HSA-69231:Cyclin D associated events in G1; R-HSA-912446:Meiotic recombination TTO0FDJ ID TTO0FDJ TTO0FDJ TN Cyclin-dependent kinase 6 (CDK6) TTO0FDJ UP Q00534 TTO0FDJ UC CDK6_HUMAN TTO0FDJ BC Kinase TTO0FDJ SN Serine/threonine-protein kinase PLSTIRE; Serine/threonine protein kinase PLSTIRE; Cell division protein kinase 6; CDKN6 TTO0FDJ GN CDK6 TTO0FDJ FC Phosphorylates pRB/RB1 and NPM1. Interacts with D-type G1 cyclins during interphase at G1 to form a pRB/RB1 kinase and controls the entrance into the cell cycle. Involved in initiation and maintenance of cell cycle exit during cell differentiation; prevents cell proliferation and regulates negatively cell differentiation, but is required for the proliferation of specific cell types (e. g. erythroid and hematopoietic cells). Essential for cell proliferation within the dentate gyrus of the hippocampus and the subventricular zone of the lateral ventricles. Required during thymocyte development. Promotes the production of newborn neurons, probably by modulating G1 length. Promotes, at least in astrocytes, changes in patterns of gene expression, changes in the actin cytoskeleton including loss of stress fibers, and enhanced motility during cell differentiation. Prevents myeloid differentiation by interfering with RUNX1 and reducing its transcription transactivation activity, but promotes proliferation of normal myeloid progenitors. Delays senescence. Promotes the proliferation of beta-cells in pancreatic islets of Langerhans. May play a role in the centrosome organization during the cell cycle phases. Serine/threonine-protein kinase involved in the control of the cell cycle and differentiation; promotes G1/S transition. TTO0FDJ EC EC 2.7.11.22 TTO0FDJ PD 5L2T; 5L2S; 5L2I; 4TTH; 4EZ5 TTO0FDJ SQ MEKDGLCRADQQYECVAEIGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLFDVCTVSRTDRETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGEEDWPRDVALPRQAFHSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPYFQDLERCKENLDSHLPPSQNTSELNTA TTO0FDJ TT Successful TTO0FDJ FM Kinase TTO0FDJ KE hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa05161:Hepatitis B; hsa05162:Measles; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05214:Glioma; hsa05218:Melanoma; hsa05220:Chronic myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer TTO0FDJ RC R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-2559585:Oncogene Induced Senescence; R-HSA-69231:Cyclin D associated events in G1 TT5ZWB6 ID TT5ZWB6 TT5ZWB6 TN Dihydrodiol dehydrogenase type I (AKR1C3) TT5ZWB6 UP P42330 TT5ZWB6 UC AK1C3_HUMAN TT5ZWB6 BC Short-chain dehydrogenases reductase TT5ZWB6 SN Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; Testosterone 17-beta-dehydrogenase 5; Prostaglandin F synthase; PGFS; KIAA0119; Indanol dehydrogenase; HSD17B5; HA1753; Dihydrodiol dehydrogenase 3; DDH1; DD3; DD-3; Chlordecone reductase homolog HAKRb; Aldo-keto reductase family 1 member C3; 3-alpha-hydroxysteroid dehydrogenase type 2; 3-alpha-HSD type II, brain; 3-alpha-HSD type 2; 17-beta-hydroxysteroid dehydrogenase type 5; 17-beta-HSD 5 TT5ZWB6 GN AKR1C3 TT5ZWB6 FC Catalyzes the conversion of aldehydes and ketones to alcohols. Catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta-PGF2 to PGD2. Functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. Can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites. Preferentially transforms androstenedione (4-dione) to testosterone. TT5ZWB6 EC EC 1.-.-.- TT5ZWB6 PD 6GXK; 6F78; 6F2U; 5JM5; 5HNU TT5ZWB6 SQ MDSKHQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFASHPNYPYSDEY TT5ZWB6 TT Successful TT5ZWB6 FM CH CH donor oxidoreductase TT5ZWB6 KE hsa00140:Steroid hormone biosynthesis; hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04913:Ovarian steroidogenesis TT5ZWB6 RC R-HSA-975634:Retinoid metabolism and transport TTDIGC1 ID TTDIGC1 TTDIGC1 TN Dipeptidyl peptidase 4 (DPP-4) TTDIGC1 UP P27487 TTDIGC1 UC DPP4_HUMAN TTDIGC1 BC Peptidase TTDIGC1 SN Tcell activation antigen CD26; TP103; T-cell activation antigen CD26; Dipeptidyl peptidase IV; Dipeptidyl peptidase 4 soluble form; DPP-IV; DPP IV; DPP 4; CD26; Adenosine deaminase complexing protein-2; Adenosine deaminase complexing protein 2; ADCP2; ADCP-2; ADABP TTDIGC1 GN DPP4 TTDIGC1 FC Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. TTDIGC1 EC EC 3.4.14.5 TTDIGC1 PD 6B1O; 6B1E; 5ZID; 5Y7K; 5Y7J TTDIGC1 SQ MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP TTDIGC1 TT Successful TTDIGC1 FM Peptidase TTDIGC1 KE hsa04974:Protein digestion and absorption TTOM3J0 ID TTOM3J0 TTOM3J0 TN Estrogen receptor beta (ESR2) TTOM3J0 UP Q92731 TTOM3J0 UC ESR2_HUMAN TTOM3J0 BC Nuclear hormone receptor TTOM3J0 SN Oestrogen receptor beta; Nuclear receptor subfamily 3 group A member 2; NR3A2; Erbeta; ESTRB; ER-beta; Beta-1 TTOM3J0 GN ESR2 TTOM3J0 FC Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA-binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual. Nuclear hormone receptor. TTOM3J0 PD 5TOA; 4ZI1; 4J26; 4J24; 3OMQ TTOM3J0 SQ MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ TTOM3J0 TT Successful TTOM3J0 FM Nuclear hormone receptor TTOM3J0 KE hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway TTOM3J0 RC R-HSA-383280:Nuclear Receptor transcription pathway TTZFDBT ID TTZFDBT TTZFDBT TN Follicle-stimulating hormone receptor (FSHR) TTZFDBT UP P23945 TTZFDBT UC FSHR_HUMAN TTZFDBT BC GPCR rhodopsin TTZFDBT SN LGR1; Follitropin receptor; FSH-R TTZFDBT GN FSHR TTZFDBT FC G protein-coupled receptor for follitropin, the follicle-stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways. TTZFDBT PD 4MQW; 4AY9; 1XWD; 1XUN TTZFDBT SQ MALLLVSLLAFLSLGSGCHHRICHCSNRVFLCQESKVTEIPSDLPRNAIELRFVLTKLRVIQKGAFSGFGDLEKIEISQNDVLEVIEADVFSNLPKLHEIRIEKANNLLYINPEAFQNLPNLQYLLISNTGIKHLPDVHKIHSLQKVLLDIQDNINIHTIERNSFVGLSFESVILWLNKNGIQEIHNCAFNGTQLDELNLSDNNNLEELPNDVFHGASGPVILDISRTRIHSLPSYGLENLKKLRARSTYNLKKLPTLEKLVALMEASLTYPSHCCAFANWRRQISELHPICNKSILRQEVDYMTQARGQRSSLAEDNESSYSRGFDMTYTEFDYDLCNEVVDVTCSPKPDAFNPCEDIMGYNILRVLIWFISILAITGNIIVLVILTTSQYKLTVPRFLMCNLAFADLCIGIYLLLIASVDIHTKSQYHNYAIDWQTGAGCDAAGFFTVFASELSVYTLTAITLERWHTITHAMQLDCKVQLRHAASVMVMGWIFAFAAALFPIFGISSYMKVSICLPMDIDSPLSQLYVMSLLVLNVLAFVVICGCYIHIYLTVRNPNIVSSSSDTRIAKRMAMLIFTDFLCMAPISFFAISASLKVPLITVSKAKILLVLFHPINSCANPFLYAIFTKNFRRDFFILLSKCGCYEMQAQIYRTETSSTVHNTHPRNGHCSSAPRVTNGSTYILVPLSHLAQN TTZFDBT TT Successful TTZFDBT FM GPCR rhodopsin TTZFDBT KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04913:Ovarian steroidogenesis TTZFDBT RC R-HSA-375281:Hormone ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events TT2B9KF ID TT2B9KF TT2B9KF TN Fyn tyrosine protein kinase (FYN) TT2B9KF UP P06241 TT2B9KF UC FYN_HUMAN TT2B9KF BC Kinase TT2B9KF SN Tyrosine-protein kinase Fyn; Src-like kinase; SLK; Proto-oncogene tyrosine-protein kinase Fyn; Proto-oncogene c-Fyn; Proto-oncogene Syn; Fyn p59-Fyn; Fyn Protooncogene Syn TT2B9KF GN FYN TT2B9KF FC Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. TT2B9KF EC EC 2.7.10.2 TT2B9KF PD 6IPZ; 6IPY; 6EDF; 4ZNX; 4U1P TT2B9KF SQ MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL TT2B9KF TT Successful TT2B9KF FM Kinase TT2B9KF KE hsa04071:Sphingolipid signaling pathway; hsa04360:Axon guidance; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04611:Platelet activation; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04725:Cholinergic synapse; hsa05020:Prion diseases; hsa05130:Pathogenic Escherichia coli infection; hsa05162:Measles; hsa05416:Viral myocarditis TT2B9KF RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1433559:Regulation of KIT signaling; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-2029481:FCGR activation; R-HSA-210990:PECAM1 interactions; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-2424491:DAP12 signaling; R-HSA-2682334:EPH-Ephrin signaling; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-373753:Nephrin interactions; R-HSA-375165:NCAM signaling for neurite out-growth; R-HSA-389356:CD28 co-stimulation; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389359:CD28 dependent Vav1 pathway; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-3928665:EPH-ephrin mediated repulsion of cells; R-HSA-399956:CRMPs in Sema3A signaling; R-HSA-418885:DCC mediated attractive signaling; R-HSA-418886:Netrin mediated repulsion signals; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5621480:Dectin-2 family; R-HSA-5621575:CD209 (DC-SIGN) signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-75892:Platelet Adhesion to exposed collagen; R-HSA-912631:Regulation of signaling by CBL; R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTVFO0U ID TTVFO0U TTVFO0U TN Gastrin/cholecystokinin type B receptor (CCKBR) TTVFO0U UP P32239 TTVFO0U UC GASR_HUMAN TTVFO0U BC GPCR rhodopsin TTVFO0U SN Cholecystokinin-2 receptor; CCKRB; CCK2-R; CCK-BR; CCK-B receptor TTVFO0U GN CCKBR TTVFO0U FC The CCK-B receptors occur throughout the central nervous system where they modulate anxiety, analgesia, arousal, and neuroleptic activity. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Receptor for gastrin and cholecystokinin. TTVFO0U PD 1L4T TTVFO0U SQ MELLKLNRSVQGTGPGPGASLCRPGAPLLNSSSVGNLSCEPPRIRGAGTRELELAIRITLYAVIFLMSVGGNMLIIVVLGLSRRLRTVTNAFLLSLAVSDLLLAVACMPFTLLPNLMGTFIFGTVICKAVSYLMGVSVSVSTLSLVAIALERYSAICRPLQARVWQTRSHAARVIVATWLLSGLLMVPYPVYTVVQPVGPRVLQCVHRWPSARVRQTWSVLLLLLLFFIPGVVMAVAYGLISRELYLGLRFDGDSDSDSQSRVRNQGGLPGAVHQNGRCRPETGAVGEDSDGCYVQLPRSRPALELTALTAPGPGSGSRPTQAKLLAKKRVVRMLLVIVVLFFLCWLPVYSANTWRAFDGPGAHRALSGAPISFIHLLSYASACVNPLVYCFMHRRFRQACLETCARCCPRPPRARPRALPDEDPPTPSIASLSRLSYTTISTLGPG TTVFO0U TT Successful TTVFO0U FM GPCR rhodopsin TTVFO0U KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04971:Gastric acid secretion TTVFO0U RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-881907:Gastrin-CREB signalling pathway via PKC and MAPK TTYRL6O ID TTYRL6O TTYRL6O TN Glucocorticoid receptor (NR3C1) TTYRL6O UP P04150 TTYRL6O UC GCR_HUMAN TTYRL6O BC Nuclear hormone receptor TTYRL6O SN Nuclear receptor subfamily 3 group C member 1; GRL; GR TTYRL6O GN NR3C1 TTYRL6O FC Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). TTYRL6O PD 6EL9; 6EL7; 6EL6; 6DXK; 6CFN TTYRL6O SQ MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK TTYRL6O TT Successful TTYRL6O FM Zinc finger TTYRL6O KE hsa04080:Neuroactive ligand-receptor interaction TTYRL6O RC R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression TTKN8W0 ID TTKN8W0 TTKN8W0 TN Glucose-6-phosphate dehydrogenase (G6PD) TTKN8W0 UP P11413 TTKN8W0 UC G6PD_HUMAN TTKN8W0 BC CH-OH donor oxidoreductase TTKN8W0 SN Glucose-6-phosphate 1-dehydrogenase TTKN8W0 GN G6PD TTKN8W0 FC The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. TTKN8W0 EC EC 1.1.1.49 TTKN8W0 PD 6.00E+08; 6.00E+07; 5UKW; 2BHL; 2BH9 TTKN8W0 SQ MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL TTKN8W0 TT Successful TTKN8W0 FM Short-chain dehydrogenases reductases TTKN8W0 KE hsa00030:Pentose phosphate pathway; hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa05230:Central carbon metabolism in cancer TTKN8W0 RC R-HSA-5628897:TP53 Regulates Metabolic Genes TT9G4N0 ID TT9G4N0 TT9G4N0 TN Glutamate carboxypeptidase II (GCPII) TT9G4N0 UP Q04609 TT9G4N0 UC FOLH1_HUMAN TT9G4N0 BC Peptidase TT9G4N0 SN Pteroylpoly-gamma-glutamate carboxypeptidase; Prostate-specific membrane antigen; PSMA; PSM; NAALADase I; NAALAD1; N-acetylated-alpha-linked acidic dipeptidase I; Membrane glutamate carboxypeptidase; MGCP; Glutamate carboxypeptidase 2; GIG27; Folylpoly-gamma-glutamate carboxypeptidase; Folate hydrolase 1; FOLH; FGCP; Cell growth-inhibiting gene 27 protein TT9G4N0 GN FOLH1 TT9G4N0 FC Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Involved in prostate tumor progression. Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. TT9G4N0 EC EC 3.4.17.21 TT9G4N0 PD 6HKZ; 6HKJ; 6H7Z; 6H7Y; 6FE5 TT9G4N0 SQ MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA TT9G4N0 TT Successful TT9G4N0 KE hsa00250:Alanine, aspartate and glutamate metabolism; hsa01100:Metabolic pathways; hsa04977:Vitamin digestion and absorption TT9G4N0 RC R-HSA-70614:Amino acid synthesis and interconversion (transamination) TTCYE56 ID TTCYE56 TTCYE56 TN Glutathione-dependent PGD synthase (HPGDS) TTCYE56 UP O60760 TTCYE56 UC HPGDS_HUMAN TTCYE56 BC Intramolecular oxidoreductases TTCYE56 SN HPGDS; Glutathione-S-transferase; GST class-alpha TTCYE56 GN HPGDS TTCYE56 FC Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a widerange of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide. TTCYE56 EC EC 5.3.99.2 TTCYE56 PD 6N4E; 5YX1; 5YWX; 5YWE; 5AIX TTCYE56 SQ MPNYKLTYFNMRGRAEIIRYIFAYLDIQYEDHRIEQADWPEIKSTLPFGKIPILEVDGLTLHQSLAIARYLTKNTDLAGNTEMEQCHVDAIVDTLDDFMSCFPWAEKKQDVKEQMFNELLTYNAPHLMQDLDTYLGGREWLIGNSVTWADFYWEICSTTLLVFKPDLLDNHPRLVTLRKKVQAIPAVANWIKRRPQTKL TTCYE56 TT Successful TTCYE56 KE hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways TTRZQE3 ID TTRZQE3 TTRZQE3 TN Glycogen synthase kinase-3 alpha (GSK-3A) TTRZQE3 UP P49840 TTRZQE3 UC GSK3A_HUMAN TTRZQE3 BC Kinase TTRZQE3 SN Serine/threonineprotein kinase GSK3A; Serine/threonine-protein kinase GSK3A; Glycogen synthase kinase3 alpha; Glycogen synthase kinase 3; GSK3 alpha; GSK-3 alpha; GSK-3 TTRZQE3 GN GSK3A TTRZQE3 FC Requires primed phosphorylation of the majority of its substrates. Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. Regulates glycogen metabolism in liver, but not in muscle. May also mediate the development of insulin resistance by regulating activation of transcription factors. In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin. Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease. May be involved in the regulation of replication in pancreatic beta-cells. Is necessary for the establishment of neuronal polarity and axon outgrowth. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, leading to activate KAT5/TIP60 acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer. Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1. TTRZQE3 EC EC 2.7.11.26 TTRZQE3 PD 2DFM TTRZQE3 SQ MSGGGPSGGGPGGSGRARTSSFAEPGGGGGGGGGGPGGSASGPGGTGGGKASVGAMGGGVGASSSGGGPGGSGGGGSGGPGAGTSFPPPGVKLGRDSGKVTTVVATLGQGPERSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNLVLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDELRCLGTQLPNNRPLPPLFNFSAGELSIQPSLNAILIPPHLRSPAGTTTLTPSSQALTETPTSSDWQSTDATPTLTNSS TTRZQE3 TT Successful TTRZQE3 FM Kinase TTRZQE3 RC R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-381038:XBP1(S) activates chaperone genes; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer TT78R5H ID TT78R5H TT78R5H TN Heat shock protein 90 alpha (HSP90A) TT78R5H UP P07900 TT78R5H UC HS90A_HUMAN TT78R5H BC Heat shock protein TT78R5H SN Renal carcinoma antigen NY-REN-38; Lipopolysaccharide-associated protein 2; LPS-associated protein 2; LAP-2; Heat shock protein HSP 90-alpha; Heat shock 86 kDa; HSPCA; HSPC1; HSP90A; HSP86; HSP 86 TT78R5H GN HSP90AA1 TT78R5H FC Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues(). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. TT78R5H PD 6GR5; 6GR4; 6GR3; 6GR1; 6GQU TT78R5H SQ MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLEGDDDTSRMEEVD TT78R5H TT Successful TT78R5H FM Heat shock protein TT78R5H KE hsa04141:Protein processing in endoplasmic reticulum; hsa04151:PI3K-Akt signaling pathway; hsa04612:Antigen processing and presentation; hsa04621:NOD-like receptor signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa05200:Pathways in cancer; hsa05215:Prostate cancer TT78R5H RC R-HSA-1236382:Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1474151:Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-203615:eNOS activation; R-HSA-2565942:Regulation of PLK1 Activity at G2/M Transition; R-HSA-3371568:Attenuation phase; R-HSA-3371571:HSF1-dependent transactivation; R-HSA-380259:Loss of Nlp from mitotic centrosomes; R-HSA-380270:Recruitment of mitotic centrosome proteins and complexes; R-HSA-380284:Loss of proteins required for interphase microtubule organization?from the centrosome; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5218920:VEGFR2 mediated vascular permeability; R-HSA-5620912:Anchoring of the basal body to the plasma membrane; R-HSA-5637810:Constitutive Signaling by EGFRvIII TTR7GJO ID TTR7GJO TTR7GJO TN Heparanase (HPSE) TTR7GJO UP Q9Y251 TTR7GJO UC HPSE_HUMAN TTR7GJO BC Glycosylase TTR7GJO SN Hpa1; Heparanase-1; Heparanase 8 kDa subunit; Heparanase 50 kDa subunit; HSE1; HPSE1; HPR1; HPA; HEP protein; Endo-glucoronidase TTR7GJO GN HPSE TTR7GJO FC Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis. Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. TTR7GJO EC EC 3.2.1.166 TTR7GJO PD 5LA7; 5LA4; 5L9Z; 5L9Y; 5E9C TTR7GJO SQ MLLRSKPALPPPLMLLLLGPLGPLSPGALPRPAQAQDVVDLDFFTQEPLHLVSPSFLSVTIDANLATDPRFLILLGSPKLRTLARGLSPAYLRFGGTKTDFLIFDPKKESTFEERSYWQSQVNQDICKYGSIPPDVEEKLRLEWPYQEQLLLREHYQKKFKNSTYSRSSVDVLYTFANCSGLDLIFGLNALLRTADLQWNSSNAQLLLDYCSSKGYNISWELGNEPNSFLKKADIFINGSQLGEDFIQLHKLLRKSTFKNAKLYGPDVGQPRRKTAKMLKSFLKAGGEVIDSVTWHHYYLNGRTATKEDFLNPDVLDIFISSVQKVFQVVESTRPGKKVWLGETSSAYGGGAPLLSDTFAAGFMWLDKLGLSARMGIEVVMRQVFFGAGNYHLVDENFDPLPDYWLSLLFKKLVGTKVLMASVQGSKRRKLRVYLHCTNTDNPRYKEGDLTLYAINLHNVTKYLRLPYPFSNKQVDKYLLRPLGPHGLLSKSVQLNGLTLKMVDDQTLPPLMEKPLRPGSSLGLPAFSYSFFVIRNAKVAACI TTR7GJO TT Successful TTR7GJO FM Glycosylase TTR7GJO KE hsa00531:Glycosaminoglycan degradation; hsa01100:Metabolic pathways; hsa05205:Proteoglycans in cancer TTR7GJO RC R-HSA-2024096:HS-GAG degradation TTTIBOJ ID TTTIBOJ TTTIBOJ TN Histamine H1 receptor (H1R) TTTIBOJ UP P35367 TTTIBOJ UC HRH1_HUMAN TTTIBOJ BC GPCR rhodopsin TTTIBOJ SN HH1R; H1R TTTIBOJ GN HRH1 TTTIBOJ FC In peripheral tissues, the H1 subclass of histamine receptors mediates the contraction of smooth muscles, increase in capillary permeability due to contraction of terminal venules, and catecholamine release from adrenal medulla, as well as mediating neurotransmission in the central nervous system. TTTIBOJ PD 3RZE TTTIBOJ SQ MSLPNSSCLLEDKMCEGNKTTMASPQLMPLVVVLSTICLVTVGLNLLVLYAVRSERKLHTVGNLYIVSLSVADLIVGAVVMPMNILYLLMSKWSLGRPLCLFWLSMDYVASTASIFSVFILCIDRYRSVQQPLRYLKYRTKTRASATILGAWFLSFLWVIPILGWNHFMQQTSVRREDKCETDFYDVTWFKVMTAIINFYLPTLLMLWFYAKIYKAVRQHCQHRELINRSLPSFSEIKLRPENPKGDAKKPGKESPWEVLKRKPKDAGGGSVLKSPSQTPKEMKSPVVFSQEDDREVDKLYCFPLDIVHMQAAAEGSSRDYVAVNRSHGQLKTDEQGLNTHGASEISEDQMLGDSQSFSRTDSDTTTETAPGKGKLRSGSNTGLDYIKFTWKRLRSHSRQYVSGLHMNRERKAAKQLGFIMAAFILCWIPYFIFFMVIAFCKNCCNEHLHMFTIWLGYINSTLNPLIYPLCNENFKKTFKRILHIRS TTTIBOJ TT Successful TTTIBOJ FM GPCR rhodopsin TTTIBOJ KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04750:Inflammatory mediator regulation of TRP channels TTTIBOJ RC R-HSA-390650:Histamine receptors; R-HSA-416476:G alpha (q) signalling events TT5FNQT ID TT5FNQT TT5FNQT TN Human immunodeficiency virus Protease (HIV PR) TT5FNQT UP P03366 (501-599) TT5FNQT UC POL_HV1B1 TT5FNQT BC Peptidase TT5FNQT SN HIV Retropepsin; HIV PR TT5FNQT GN HIV PR TT5FNQT FC Gag-Pol polyprotein: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. TT5FNQT EC EC 3.4.23.16 TT5FNQT PD 6OE3; 6HAK; 6ELI; 6DUH; 6DUG TT5FNQT SQ PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNF TT5FNQT TT Successful TT50QJ3 ID TT50QJ3 TT50QJ3 TN Influenza Neuraminidase (Influ NA) TT50QJ3 UP P03470 TT50QJ3 UC NRAM_I33A0 TT50QJ3 BC Glycosylase TT50QJ3 SN STNA; NEU1; NANase; N-acylneuraminate glycohydrolase; Influ Sialidase TT50QJ3 GN Influ NA TT50QJ3 FC Unlike other strains, A/WSN/33 neuraminidase binds and activates plasminogen into plasmin in the vicinity of HA so that activated plasmin cleaves HA rendering the virus infectious. TT50QJ3 EC EC 3.2.1.18 TT50QJ3 SQ MNPNQKIITIGSICMVVGIISLILQIGNIISIWISHSIQTGNQNHTGICNQGIITYNVVAGQDSTSVILTGNSSLCPIRGWAIHSKDNGIRIGSKGDVFVIREPFISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPYRALMSCPVGEAPSPYNSRFESVAWSASACHDGMGWLTIGISGPDNGAVAVLKYNGIITETIKSWRKKILRTQESECTCVNGSCFTIMTDGPSNGLASYKIFKIEKGKVTKSIELNAPNSHYEECSCYPDTGKVMCVCRDNWHGSNRPWVSFDQNLDYQIGYICSGVFGDNPRPKDGPGSCGPVSADGANGVKGFSYRYGNGVWIGRTKSDSSRHGFEMIWDPNGWTETDSRFSVRQDVVAMTDRSGYSGSFVQHPELTGLDCMRPCFWVELIRGRPEEETIWTSGSIISFCGVNSDTVDWSWPDGAELPFTIDK TT50QJ3 TT Successful TT50QJ3 KE stm00511:Other glycan degradation TTHRID2 ID TTHRID2 TTHRID2 TN Insulin-like growth factor I receptor (IGF1R) TTHRID2 UP P08069 TTHRID2 UC IGF1R_HUMAN TTHRID2 BC Kinase TTHRID2 SN Type 1 insulin-like growth factor receptor; Insulin-like growth factor 1 receptor; IGF-IR; IGF-I receptor; IGF-1R; IGF-1 receptor; CD221 antigen; CD221 TTHRID2 GN IGF1R TTHRID2 FC Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R. Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). TTHRID2 EC EC 2.7.10.1 TTHRID2 PD 5U8R; 5U8Q; 5HZN; 5FXS; 5FXR TTHRID2 SQ MKSGSGGGSPTSLWGLLFLSAALSLWPTSGEICGPGIDIRNDYQQLKRLENCTVIEGYLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTVDWSLILDAVSNNYIVGNKPPKECGDLCPGTMEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSTCGKRACTENNECCHPECLGSCSAPDNDTACVACRHYYYAGVCVPACPPNTYRFEGWRCVDRDFCANILSAESSDSEGFVIHDGECMQECPSGFIRNGSQSMYCIPCEGPCPKVCEEEKKTKTIDSVTSAQMLQGCTIFKGNLLINIRRGNNIASELENFMGLIEVVTGYVKIRHSHALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWDHRNLTIKAGKMYFAFNPKLCVSEIYRMEEVTGTKGRQSKGDINTRNNGERASCESDVLHFTSTTTSKNRIIITWHRYRPPDYRDLISFTVYYKEAPFKNVTEYDGQDACGSNSWNMVDVDLPPNKDVEPGILLHGLKPWTQYAVYVKAVTLTMVENDHIRGAKSEILYIRTNASVPSIPLDVLSASNSSSQLIVKWNPPSLPNGNLSYYIVRWQRQPQDGYLYRHNYCSKDKIPIRKYADGTIDIEEVTENPKTEVCGGEKGPCCACPKTEAEKQAEKEEAEYRKVFENFLHNSIFVPRPERKRRDVMQVANTTMSSRSRNTTAADTYNITDPEELETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTGYENFIHLIIALPVAVLLIVGGLVIMLYVFHRKRNNSRLGNGVLYASVNPEYFSAADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKEEMEPGFREVSFYYSEENKLPEPEELDLEPENMESVPLDPSASSSSLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNERALPLPQSSTC TTHRID2 TT Successful TTHRID2 FM Kinase TTHRID2 KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04114:Oocyte meiosis; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04730:Long-term depression; hsa04913:Ovarian steroidogenesis; hsa04914:Progesterone-mediated oocyte maturation; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05205:Proteoglycans in cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma TTHRID2 RC R-HSA-2428928:IRS-related events triggered by IGF1R; R-HSA-2428933:SHC-related events triggered by IGF1R TT4BT06 ID TT4BT06 TT4BT06 TN Integrin alpha-4 (ITGA4) TT4BT06 UP P13612 TT4BT06 UC ITA4_HUMAN TT4BT06 BC Integrin TT4BT06 SN Very late antigen 4; VLA4 subunit alpha; VLA-4 subunit alpha; VLA-4; Integrin alphaIV; Integrin alpha4; Integrin alpha-IV; CD49d; CD49 antigenlike family member D; CD49 antigen-like family member D TT4BT06 GN ITGA4 TT4BT06 FC Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. TT4BT06 PD 5FPI; 5C7Z; 4HKC; 3V4V; 3V4P TT4BT06 SQ MAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD TT4BT06 TT Successful TT4BT06 KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04514:Cell adhesion molecules (CAMs); hsa04640:Hematopoietic cell lineage; hsa04670:Leukocyte transendothelial migration; hsa04672:Intestinal immune network for IgA production; hsa04810:Regulation of actin cytoskeleton; hsa05140:Leishmaniasis; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TT4BT06 RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-216083:Integrin cell surface interactions TTT7PJU ID TTT7PJU TTT7PJU TN Janus kinase 3 (JAK-3) TTT7PJU UP P52333 TTT7PJU UC JAK3_HUMAN TTT7PJU BC Kinase TTT7PJU SN Tyrosine-protein kinase JAK3; Leukocyte janus kinase; L-JAK TTT7PJU GN JAK3 TTT7PJU FC Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. Following ligand binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A AND STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion. Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. TTT7PJU EC EC 2.7.10.2 TTT7PJU PD 6NY4; 6GLB; 6GLA; 6GL9; 6DUD TTT7PJU SQ MAPPSEETPLIPQRSCSLLSTEAGALHVLLPARGPGPPQRLSFSFGDHLAEDLCVQAAKASGILPVYHSLFALATEDLSCWFPPSHIFSVEDASTQVLLYRIRFYFPNWFGLEKCHRFGLRKDLASAILDLPVLEHLFAQHRSDLVSGRLPVGLSLKEQGECLSLAVLDLARMAREQAQRPGELLKTVSYKACLPPSLRDLIQGLSFVTRRRIRRTVRRALRRVAACQADRHSLMAKYIMDLERLDPAGAAETFHVGLPGALGGHDGLGLLRVAGDGGIAWTQGEQEVLQPFCDFPEIVDISIKQAPRVGPAGEHRLVTVTRTDNQILEAEFPGLPEALSFVALVDGYFRLTTDSQHFFCKEVAPPRLLEEVAEQCHGPITLDFAINKLKTGGSRPGSYVLRRSPQDFDSFLLTVCVQNPLGPDYKGCLIRRSPTGTFLLVGLSRPHSSLRELLATCWDGGLHVDGVAVTLTSCCIPRPKEKSNLIVVQRGHSPPTSSLVQPQSQYQLSQMTFHKIPADSLEWHENLGHGSFTKIYRGCRHEVVDGEARKTEVLLKVMDAKHKNCMESFLEAASLMSQVSYRHLVLLHGVCMAGDSTMVQEFVHLGAIDMYLRKRGHLVPASWKLQVVKQLAYALNYLEDKGLPHGNVSARKVLLAREGADGSPPFIKLSDPGVSPAVLSLEMLTDRIPWVAPECLREAQTLSLEADKWGFGATVWEVFSGVTMPISALDPAKKLQFYEDRQQLPAPKWTELALLIQQCMAYEPVQRPSFRAVIRDLNSLISSDYELLSDPTPGALAPRDGLWNGAQLYACQDPTIFEERHLKYISQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRQSLRLVMEYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPSAEFLRMMGCERDVPALCRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDMLWSGSRGCETHAFTAHPEGKHHSLSFS TTT7PJU TT Successful TTT7PJU FM Kinase TTT7PJU KE hsa04062:Chemokine signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04630:Jak-STAT signaling pathway; hsa05162:Measles; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05203:Viral carcinogenesis; hsa05340:Primary immunodeficiency TTT7PJU RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1266695:Interleukin-7 signaling; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-451927:Interleukin-2 signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-912526:Interleukin receptor SHC signaling TTXZEAJ ID TTXZEAJ TTXZEAJ TN Leukotriene A-4 hydrolase (LTA4H) TTXZEAJ UP P09960 TTXZEAJ UC LKHA4_HUMAN TTXZEAJ BC Ether bond hydrolase TTXZEAJ SN Leukotriene A4 hydrolase; Leukotriene A(4)Leukotriene A-4 hydrolase hydrolase; Leukotriene A(4) hydrolase; LTA4; LTA-H; LTA-4hydrolase; LTA-4 hydrolase TTXZEAJ GN LTA4H TTXZEAJ FC Has also aminopeptidase activity. Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. TTXZEAJ EC EC 3.3.2.6 TTXZEAJ PD 6END; 6ENC; 6ENB; 5NIE; 5NID TTXZEAJ SQ MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVGKDLKVD TTXZEAJ TT Successful TTXZEAJ KE hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways TTMF541 ID TTMF541 TTMF541 TN Liver carboxylesterase (CES1) TTMF541 UP P23141 TTMF541 UC EST1_HUMAN TTMF541 BC Carboxylic ester hydrolase TTMF541 SN Serine esterase 1; Monocyte/macrophage serine esterase; Human carboxylesterase 1; HMSE; HCE1; CES1; Brain carboxylesterase hBr1; Acyl coenzyme A:cholesterol acyltransferase TTMF541 GN CES1 TTMF541 FC Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl coa ester. TTMF541 EC EC 3.1.1.1 TTMF541 PD 5A7H; 5A7G; 5A7F; 4AB1; 3K9B TTMF541 SQ MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIPMQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKDKEVAFWTNLFAKKAVEKPPQTEHIEL TTMF541 TT Successful TTMF541 KE hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways TTMTWOS ID TTMTWOS TTMTWOS TN Matrix metalloproteinase-7 (MMP-7) TTMTWOS UP P09237 TTMTWOS UC MMP7_HUMAN TTMTWOS BC Peptidase TTMTWOS SN Uterine metalloproteinase; Pump-1 protease; PUMP1; Matrin; Matrilysin; MPSL1 TTMTWOS GN MMP7 TTMTWOS FC Activates procollagenase. Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. TTMTWOS EC EC 3.4.24.23 TTMTWOS PD 5UE5; 5UE2; 2Y6D; 2Y6C; 2MZI TTMTWOS SQ MRLTVLCAVCLLPGSLALPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNSRKK TTMTWOS TT Successful TTMTWOS FM Peptidase TTMTWOS KE hsa04310:Wnt signaling pathway TTMTWOS RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures TTD0CIQ ID TTD0CIQ TTD0CIQ TN Melanocortin receptor 4 (MC4R) TTD0CIQ UP P32245 TTD0CIQ UC MC4R_HUMAN TTD0CIQ BC GPCR rhodopsin TTD0CIQ SN MC4-R TTD0CIQ GN MC4R TTD0CIQ FC Plays a central role in energy homeostasis and somatic growth. This receptor is mediated by G proteins that stimulate adenylate cyclase (cAMP). Receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. TTD0CIQ PD 2IQW; 2IQV; 2IQU; 2IQS; 2IQR TTD0CIQ SQ MVNSTHRGMHTSLHLWNRSSYRLHSNASESLGKGYSDGGCYEQLFVSPEVFVTLGVISLLENILVIVAIAKNKNLHSPMYFFICSLAVADMLVSVSNGSETIVITLLNSTDTDAQSFTVNIDNVIDSVICSSLLASICSLLSIAVDRYFTIFYALQYHNIMTVKRVGIIISCIWAACTVSGILFIIYSDSSAVIICLITMFFTMLALMASLYVHMFLMARLHIKRIAVLPGTGAIRQGANMKGAITLTILIGVFVVCWAPFFLHLIFYISCPQNPYCVCFMSHFNLYLILIMCNSIIDPLIYALRSQELRKTFKEIICCYPLGGLCDLSSRY TTD0CIQ TT Successful TTD0CIQ KE hsa04080:Neuroactive ligand-receptor interaction TTD0CIQ RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events TT0WAIE ID TT0WAIE TT0WAIE TN Melatonin receptor type 1A (MTNR1A) TT0WAIE UP P48039 TT0WAIE UC MTR1A_HUMAN TT0WAIE BC GPCR rhodopsin TT0WAIE SN Mel1a receptor; Mel1AR; Mel-1A-R TT0WAIE GN MTNR1A TT0WAIE FC Likely to mediate the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity. High affinity receptor for melatonin. TT0WAIE PD 6ME5; 6ME4; 6ME3; 6ME2 TT0WAIE SQ MQGNGSALPNASQPVLRGDGARPSWLASALACVLIFTIVVDILGNLLVILSVYRNKKLRNAGNIFVVSLAVADLVVAIYPYPLVLMSIFNNGWNLGYLHCQVSGFLMGLSVIGSIFNITGIAINRYCYICHSLKYDKLYSSKNSLCYVLLIWLLTLAAVLPNLRAGTLQYDPRIYSCTFAQSVSSAYTIAVVVFHFLVPMIIVIFCYLRIWILVLQVRQRVKPDRKPKLKPQDFRNFVTMFVVFVLFAICWAPLNFIGLAVASDPASMVPRIPEWLFVASYYMAYFNSCLNAIIYGLLNQNFRKEYRRIIVSLCTARVFFVDSSNDVADRVKWKPSPLMTNNNVVKVDSV TT0WAIE TT Successful TT0WAIE FM GPCR rhodopsin TT0WAIE KE hsa04080:Neuroactive ligand-receptor interaction; hsa04713:Circadian entrainment TT0WAIE RC R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events TT32JK8 ID TT32JK8 TT32JK8 TN Melatonin receptor type 1B (MTNR1B) TT32JK8 UP P49286 TT32JK8 UC MTR1B_HUMAN TT32JK8 BC GPCR rhodopsin TT32JK8 SN Mel1b receptor; Mel1b melatonin receptor; Mel-1B-R TT32JK8 GN MTNR1B TT32JK8 FC Likely to mediate the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity. High affinity receptor for melatonin. TT32JK8 PD 6ME9; 6ME8; 6ME7; 6ME6 TT32JK8 SQ MSENGSFANCCEAGGWAVRPGWSGAGSARPSRTPRPPWVAPALSAVLIVTTAVDVVGNLLVILSVLRNRKLRNAGNLFLVSLALADLVVAFYPYPLILVAIFYDGWALGEEHCKASAFVMGLSVIGSVFNITAIAINRYCYICHSMAYHRIYRRWHTPLHICLIWLLTVVALLPNFFVGSLEYDPRIYSCTFIQTASTQYTAAVVVIHFLLPIAVVSFCYLRIWVLVLQARRKAKPESRLCLKPSDLRSFLTMFVVFVIFAICWAPLNCIGLAVAINPQEMAPQIPEGLFVTSYLLAYFNSCLNAIVYGLLNQNFRREYKRILLALWNPRHCIQDASKGSHAEGLQSPAPPIIGVQHQADAL TT32JK8 TT Successful TT32JK8 FM GPCR rhodopsin TT32JK8 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04713:Circadian entrainment TT32JK8 RC R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events TTGP7BY ID TTGP7BY TTGP7BY TN Monoamine oxidase type B (MAO-B) TTGP7BY UP P27338 TTGP7BY UC AOFB_HUMAN TTGP7BY BC CH-NH(2) donor oxidoreductase TTGP7BY SN MAO-B; Amine oxidase [flavin-containing] B TTGP7BY GN MAOB TTGP7BY FC Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine. TTGP7BY EC EC 1.4.3.4 TTGP7BY PD 6FWC; 6FW0; 6FVZ; 5MRL; 4CRT TTGP7BY SQ MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV TTGP7BY TT Successful TTGP7BY FM CH NH2 donor oxidoreductase TTGP7BY KE hsa00260:Glycine, serine and threonine metabolism; hsa00330:Arginine and proline metabolism; hsa00340:Histidine metabolism; hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism; hsa00380:Tryptophan metabolism; hsa00982:Drug metabolism - cytochrome P450; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse; hsa04728:Dopaminergic synapse; hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05034:Alcoholism TT3OT40 ID TT3OT40 TT3OT40 TN Multidrug resistance protein 1 (ABCB1) TT3OT40 UP P08183 TT3OT40 UC MDR1_HUMAN TT3OT40 BC ABC transporter TT3OT40 SN PGY1; P-glycoprotein 1; MDR1; CD243 antigen; CD243; ATP-binding cassette sub-family B member 1 TT3OT40 GN ABCB1 TT3OT40 FC Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. TT3OT40 EC EC 7.6.2.2 TT3OT40 PD 6QEX; 6FN4; 6FN1; 6C0V TT3OT40 SQ MDLEGDRNGGAKKKNFFKLNNKSEKDKKEKKPTVSVFSMFRYSNWLDKLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAADESKSEIDALEMSSNDSRSSLIRKRSTRRSVRGSQAQDRKLSTKEALDESIPPVSFWRIMKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGTKRQ TT3OT40 TT Successful TT3OT40 FM Acid anhydrides hydrolase TT3OT40 KE hsa02010:ABC transporters; hsa04976:Bile secretion; hsa05206:MicroRNAs in cancer TT3OT40 RC R-HSA-382556:ABC-family proteins mediated transport TTOI92F ID TTOI92F TTOI92F TN Multidrug resistance-associated protein 1 (ABCC1) TTOI92F UP P33527 TTOI92F UC MRP1_HUMAN TTOI92F BC ABC transporter TTOI92F SN MRP1; MRP; Leukotriene C(4) transporter; LTC4 transporter; ATP-binding cassette sub-family C member 1 TTOI92F GN ABCC1 TTOI92F FC Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs. Hydrolyzes ATP with low efficiency. Mediates export of organic anions and drugs from the cytoplasm. TTOI92F EC EC 7.6.2.2 TTOI92F PD 4C3Z; 2CBZ TTOI92F SQ MALRGFCSADGSDPLWDWNVTWNTSNPDFTKCFQNTVLVWVPCFYLWACFPFYFLYLSRHDRGYIQMTPLNKTKTALGFLLWIVCWADLFYSFWERSRGIFLAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMTALKEDAQVDLFRDITFYVYFSLLLIQLVLSCFSDRSPLFSETIHDPNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNKEDTSEQVVPVLVKNWKKECAKTRKQPVKVVYSSKDPAQPKESSKVDANEEVEALIVKSPQKEWNPSLFKVLYKTFGPYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAVYVTIDENNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGGTNSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNDSLRENILFGCQLEEPYYRSVIQACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGVTGVSGPGKEAKQMENGMLVTDSAGKQLQRQLSSSSSYSGDISRHHNSTAELQKAEAKKEETWKLMEADKAQTGQVKLSVYWDYMKAIGLFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSMAKDAGLV TTOI92F TT Successful TTOI92F FM ABC transporter TTOI92F KE hsa02010:ABC transporters; hsa04071:Sphingolipid signaling pathway; hsa04977:Vitamin digestion and absorption; hsa05206:MicroRNAs in cancer TTOI92F RC R-HSA-196741:Cobalamin (Cbl, vitamin B12) transport and metabolism; R-HSA-382556:ABC-family proteins mediated transport TTQ13Z5 ID TTQ13Z5 TTQ13Z5 TN Muscarinic acetylcholine receptor M3 (CHRM3) TTQ13Z5 UP P20309 TTQ13Z5 UC ACM3_HUMAN TTQ13Z5 BC GPCR rhodopsin TTQ13Z5 SN M3 receptor; CHRM3 TTQ13Z5 GN CHRM3 TTQ13Z5 FC The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. TTQ13Z5 PD 2CSA TTQ13Z5 SQ MTLHNNSTTSPLFPNISSSWIHSPSDAGLPPGTVTHFGSYNVSRAAGNFSSPDGTTDDPLGGHTVWQVVFIAFLTGILALVTIIGNILVIVSFKVNKQLKTVNNYFLLSLACADLIIGVISMNLFTTYIIMNRWALGNLACDLWLAIDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTTKRAGVMIGLAWVISFVLWAPAILFWQYFVGKRTVPPGECFIQFLSEPTITFGTAIAAFYMPVTIMTILYWRIYKETEKRTKELAGLQASGTEAETENFVHPTGSSRSCSSYELQQQSMKRSNRRKYGRCHFWFTTKSWKPSSEQMDQDHSSSDSWNNNDAAASLENSASSDEEDIGSETRAIYSIVLKLPGHSTILNSTKLPSSDNLQVPEEELGMVDLERKADKLQAQKSVDDGGSFPKSFSKLPIQLESAVDTAKTSDVNSSVGKSTATLPLSFKEATLAKRFALKTRSQITKRKRMSLVKEKKAAQTLSAILLAFIITWTPYNIMVLVNTFCDSCIPKTFWNLGYWLCYINSTVNPVCYALCNKTFRTTFKMLLLCQCDKKKRRKQQYQQRQSVIFHKRAPEQAL TTQ13Z5 TT Successful TTQ13Z5 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa04810:Regulation of actin cytoskeleton; hsa04911:Insulin secretion; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion TTQ13Z5 RC R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-399997:Acetylcholine regulates insulin secretion; R-HSA-416476:G alpha (q) signalling events TTXABCW ID TTXABCW TTXABCW TN NT-3 growth factor receptor (TrkC) TTXABCW UP Q16288 TTXABCW UC NTRK3_HUMAN TTXABCW BC Kinase TTXABCW SN TrkC tyrosine kinase; Trk-C; TRKC; Neurotrophic tyrosine kinase receptor type 3; NT3 growth factor receptor; GP145TrkC; GP145-TrkC TTXABCW GN NTRK3 TTXABCW FC Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation. Receptor tyrosine kinase involved in nervous system and probably heart development. TTXABCW EC EC 2.7.10.1 TTXABCW PD 4YMJ; 3V5Q; 1WWC TTXABCW SQ MDVSLCPAKCSFWRIFLLGSVWLDYVGSVLACPANCVCSKTEINCRRPDDGNLFPLLEGQDSGNSNGNASINITDISRNITSIHIENWRSLHTLNAVDMELYTGLQKLTIKNSGLRSIQPRAFAKNPHLRYINLSSNRLTTLSWQLFQTLSLRELQLEQNFFNCSCDIRWMQLWQEQGEAKLNSQNLYCINADGSQLPLFRMNISQCDLPEISVSHVNLTVREGDNAVITCNGSGSPLPDVDWIVTGLQSINTHQTNLNWTNVHAINLTLVNVTSEDNGFTLTCIAENVVGMSNASVALTVYYPPRVVSLEEPELRLEHCIEFVVRGNPPPTLHWLHNGQPLRESKIIHVEYYQEGEISEGCLLFNKPTHYNNGNYTLIAKNPLGTANQTINGHFLKEPFPESTDNFILFDEVSPTPPITVTHKPEEDTFGVSIAVGLAAFACVLLVVLFVMINKYGRRSKFGMKGPVAVISGEEDSASPLHHINHGITTPSSLDAGPDTVVIGMTRIPVIENPQYFRQGHNCHKPDTYVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGMSRDVYSTDYYRLFNPSGNDFCIWCEVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHALGKATPIYLDILG TTXABCW TT Successful TTXABCW FM Kinase TTXABCW RC R-HSA-170984:ARMS-mediated activation; R-HSA-187024:NGF-independant TRKA activation; R-HSA-198203:PI3K/AKT activation TT5TPI6 ID TT5TPI6 TT5TPI6 TN Opioid receptor sigma 1 (OPRS1) TT5TPI6 UP Q99720 TT5TPI6 UC SGMR1_HUMAN TT5TPI6 BC GPCR rhodopsin TT5TPI6 SN hSigmaR1; Sigma1R; Sigma1-receptor; Sigma non-opioid intracellular receptor 1; Sigma 1-type opioid receptor; SRBP; SR31747-binding protein; SR31747 binding protein 1; SR-BP; SIG-1R; Opioid receptor, sigma 1, isoform 1; OPRS1 protein; Aging-associated gene 8 protein; AAG8 TT5TPI6 GN SIGMAR1 TT5TPI6 FC Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration. Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112. Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. TT5TPI6 PD 6DK1; 6DK0; 6DJZ; 5HK2; 5HK1 TT5TPI6 SQ MQWAVGRRWAWAALLLAVAAVLTQVVWLWLGTQSFVFQREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSRGHSGRYWAEISDTIISGTFHQWREGTTKSEVFYPGETVVHGPGEATAVEWGPNTWMVEYGRGVIPSTLAFALADTVFSTQDFLTLFYTLRSYARGLRLELTTYLFGQDP TT5TPI6 TT Successful TT5TPI6 FM ERG2 family TTUMGNO ID TTUMGNO TTUMGNO TN Ornithine decarboxylase (ODC1) TTUMGNO UP P11926 TTUMGNO UC DCOR_HUMAN TTUMGNO BC Carbon-carbon lyase TTUMGNO SN ODC TTUMGNO GN ODC1 TTUMGNO FC Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. TTUMGNO EC EC 4.1.1.17 TTUMGNO PD 5BWA; 4ZGY; 2OO0; 2ON3; 1D7K TTUMGNO SQ MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQFQNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV TTUMGNO TT Successful TTUMGNO FM Carbon carbon lyase TTJ584C ID TTJ584C TTJ584C TN Peroxisome proliferator-activated receptor alpha (PPARA) TTJ584C UP Q07869 TTJ584C UC PPARA_HUMAN TTJ584C BC Nuclear hormone receptor TTJ584C SN Peroxisome proliferater-activated receptor alpha; PPARalpha; PPAR-alpha; PPAR; Nuclear receptor subfamily 1 group C member 1; NR1C1 TTJ584C GN PPARA TTJ584C FC Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2. Ligand-activated transcription factor. TTJ584C PD 5HYK; 5AZT; 4CI4; 4BCR; 3VI8 TTJ584C SQ MVDTESPLCPLSPLEAGDLESPLSEEFLQEMGNIQEISQSIGEDSSGSFGFTEYQYLGSCPGSDGSVITDTLSPASSPSSVTYPVVPGSVDESPSGALNIECRICGDKASGYHYGVHACEGCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSEKAKLKAEILTCEHDIEDSETADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPFVIHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCTSVETVTELTEFAKAIPGFANLDLNDQVTLLKYGVYEAIFAMLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKFDFAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEKMQEGIVHVLRLHLQSNHPDDIFLFPKLLQKMADLRQLVTEHAQLVQIIKKTESDAALHPLLQEIYRDMY TTJ584C TT Successful TTJ584C FM Zinc finger TTJ584C KE hsa03320:PPAR signaling pathway; hsa04024:cAMP signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04922:Glucagon signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05160:Hepatitis C TTJ584C RC R-HSA-1368082:RORA activates gene expression; R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-1989781:PPARA activates gene expression; R-HSA-2032785:YAP1- and WWTR1 (TAZ)-stimulated gene expression; R-HSA-2151201:Transcriptional activation of mitochondrial biogenesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP); R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-383280:Nuclear Receptor transcription pathway; R-HSA-400206:Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha); R-HSA-400253:Circadian Clock TTZMAO3 ID TTZMAO3 TTZMAO3 TN Peroxisome proliferator-activated receptor gamma (PPAR-gamma) TTZMAO3 UP P37231 TTZMAO3 UC PPARG_HUMAN TTZMAO3 BC Nuclear hormone receptor TTZMAO3 SN PPAR-gamma; Nuclear receptor subfamily 1 group C member 3; NR1C3 TTZMAO3 GN PPARG TTZMAO3 FC Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels (By similarity). TTZMAO3 PD 6MD4; 6MD2; 6MD1; 6MD0; 6MCZ TTZMAO3 SQ MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY TTZMAO3 TT Successful TTZMAO3 FM Nuclear hormone receptor TTZMAO3 KE hsa03320:PPAR signaling pathway; hsa04152:AMPK signaling pathway; hsa04380:Osteoclast differentiation; hsa05016:Huntington's disease; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05216:Thyroid cancer TTZMAO3 RC R-HSA-1989781:PPARA activates gene expression; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-383280:Nuclear Receptor transcription pathway TT06AWU ID TT06AWU TT06AWU TN Phosphodiesterase 3A (PDE3A) TT06AWU UP Q14432 TT06AWU UC PDE3A_HUMAN TT06AWU BC Phosphoric diester hydrolase TT06AWU SN cGMP-inhibited 3',5'-cyclic phosphodiesterase A; Phosphodiesterase 3A; Cyclic GMP-inhibited phosphodiesterase A; Cyclic GMP inhibited phosphodiesterase A; CGI-PDE A TT06AWU GN PDE3A TT06AWU FC Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. TT06AWU EC EC 3.1.4.17 TT06AWU PD 1LRC TT06AWU SQ MAVPGDAARVRDKPVHSGVSQAPTAGRDCHHRADPASPRDSGCRGCWGDLVLQPLRSSRKLSSALCAGSLSFLLALLVRLVRGEVGCDLEQCKEAAAAEEEEAAPGAEGGVFPGPRGGAPGGGARLSPWLQPSALLFSLLCAFFWMGLYLLRAGVRLPLAVALLAACCGGEALVQIGLGVGEDHLLSLPAAGVVLSCLAAATWLVLRLRLGVLMIALTSAVRTVSLISLERFKVAWRPYLAYLAGVLGILLARYVEQILPQSAEAAPREHLGSQLIAGTKEDIPVFKRRRRSSSVVSAEMSGCSSKSHRRTSLPCIPREQLMGHSEWDHKRGPRGSQSSGTSITVDIAVMGEAHGLITDLLADPSLPPNVCTSLRAVSNLLSTQLTFQAIHKPRVNPVTSLSENYTCSDSEESSEKDKLAIPKRLRRSLPPGLLRRVSSTWTTTTSATGLPTLEPAPVRRDRSTSIKLQEAPSSSPDSWNNPVMMTLTKSRSFTSSYAISAANHVKAKKQSRPGALAKISPLSSPCSSPLQGTPASSLVSKISAVQFPESADTTAKQSLGSHRALTYTQSAPDLSPQILTPPVICSSCGRPYSQGNPADEPLERSGVATRTPSRTDDTAQVTSDYETNNNSDSSDIVQNEDETECLREPLRKASACSTYAPETMMFLDKPILAPEPLVMDNLDSIMEQLNTWNFPIFDLVENIGRKCGRILSQVSYRLFEDMGLFEAFKIPIREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLSTVINDHGSTSDSDSDSGFTHGHMGYVFSKTYNVTDDKYGCLSGNIPALELMALYVAAAMHDYDHPGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLINLDHVEFKHFRFLVIEAILATDLKKHFDFVAKFNGKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKELHLQWTDGIVNEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCNSYDSAGLMPGKWVEDSDESGDTDDPEEEEEEAPAPNEEETCENNESPKKKTFKRRKIYCQITQHLLQNHKMWKKVIEEEQRLAGIENQSLDQTPQSHSSEQIQAIKEEEEEKGKPRGEEIPTQKPDQ TT06AWU TT Successful TT06AWU FM Phosphoric diester hydrolase TT06AWU KE hsa00230:Purine metabolism; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa05032:Morphine addiction TT06AWU RC R-HSA-418457:cGMP effects; R-HSA-418555:G alpha (s) signalling events TTZ97H5 ID TTZ97H5 TTZ97H5 TN Phosphodiesterase 4A (PDE4A) TTZ97H5 UP P27815 TTZ97H5 UC PDE4A_HUMAN TTZ97H5 BC Phosphoric diester hydrolase TTZ97H5 SN cAMP-specific 3',5'-cyclic phosphodiesterase 4A; Type 4A cAMP phosphodiesterase; PDE46; DPDE2 TTZ97H5 GN PDE4A TTZ97H5 FC Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. TTZ97H5 EC EC 3.1.4.53 TTZ97H5 PD 3TVX; 3I8V; 2QYK TTZ97H5 SQ MEPPTVPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERAERERQPHRPIERADAMDTSDRPGLRTTRMSWPSSFHGTGTGSGGAGGGSSRRFEAENGPTPSPGRSPLDSQASPGLVLHAGAATSQRRESFLYRSDSDYDMSPKTMSRNSSVTSEAHAEDLIVTPFAQVLASLRSVRSNFSLLTNVPVPSNKRSPLGGPTPVCKATLSEETCQQLARETLEELDWCLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISTTFLDKQNEVEIPSPTMKEREKQQAPRPRPSQPPPPPVPHLQPMSQITGLKKLMHSNSLNNSNIPRFGVKTDQEELLAQELENLNKWGLNIFCVSDYAGGRSLTCIMYMIFQERDLLKKFRIPVDTMVTYMLTLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLSKRQRQSLRKMVIDMVLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLELYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVHPDAQEILDTLEDNRDWYYSAIRQSPSPPPEEESRGPGHPPLPDKFQFELTLEEEEEEEISMAQIPCTAQEALTAQGLSGVEEALDATIAWEASPAQESLEVMAQEASLEAELEAVYLTQQAQSTGSAPVAPDEFSSREEFVVAVSHSSPSALALQSPLLPAWRTLSVSEHAPGLPGLPSTAAEVEAQREHQAAKRACSACAGTFGEDTSALPAPGGGGSGGDPT TTZ97H5 TT Successful TTZ97H5 FM Phosphoric diester hydrolase TTZ97H5 KE hsa00230:Purine metabolism; hsa04024:cAMP signaling pathway; hsa05032:Morphine addiction TTZ97H5 RC R-HSA-180024:DARPP-32 events; R-HSA-418555:G alpha (s) signalling events TT9V5JH ID TT9V5JH TT9V5JH TN Phospholipase A2 (PLA2G1B) TT9V5JH UP P04054 TT9V5JH UC PA21B_HUMAN TT9V5JH BC Carboxylic ester hydrolase TT9V5JH SN Secreted phospholipase A(2); Phosphatidylcholine 2-acylhydrolase 1B; PLA2G1B; Group IB phospholipase A2 TT9V5JH GN PLA2G1B TT9V5JH FC PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides, this releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules. TT9V5JH EC EC 3.1.1.4 TT9V5JH PD 3ELO; 1YSK TT9V5JH SQ MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPVDELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNCDRNAAICFSKAPYNKAHKNLDTKKYCQS TT9V5JH TT Successful TT9V5JH KE hsa00564:Glycerophospholipid metabolism; hsa00565:Ether lipid metabolism; hsa00590:Arachidonic acid metabolism; hsa00591:Linoleic acid metabolism; hsa00592:alpha-Linolenic acid metabolism; hsa01100:Metabolic pathways; hsa04014:Ras signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04972:Pancreatic secretion; hsa04975:Fat digestion and absorption TT9V5JH RC R-HSA-1482788:Acyl chain remodelling of PC; R-HSA-1482839:Acyl chain remodelling of PE; R-HSA-1482922:Acyl chain remodelling of PI TTEUNMR ID TTEUNMR TTEUNMR TN PI3-kinase alpha (PIK3CA) TTEUNMR UP P42336 TTEUNMR UC PK3CA_HUMAN TTEUNMR BC Kinase TTEUNMR SN p110alpha; Serine/threonine protein kinase PIK3CA; PtdIns3kinase subunit p110alpha; PtdIns3kinase subunit alpha; PtdIns-3-kinase subunit p110-alpha; PtdIns-3-kinase subunit alpha; Phosphoinositide3kinase catalytic alpha polypeptide; Phosphoinositide-3-kinase catalytic alpha polypeptide; Phosphatidylinositol 4,5bisphosphate 3kinase catalytic subunit alpha isoform; Phosphatidylinositol 4,5bisphosphate 3kinase 110 kDa catalytic subunit alpha; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform; Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha; PI3kinase subunit alpha; PI3Kalpha; PI3K-alpha; PI3-kinase subunit alpha TTEUNMR GN PIK3CA TTEUNMR FC Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. Also has serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS. Plays a role in the positive regulation of phagocytosis and pinocytosis. TTEUNMR EC EC 2.7.1.153 TTEUNMR PD 6NCT; 5XGJ; 5XGI; 5XGH; 5UL1 TTEUNMR SQ MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLITIKHELFKEARKYPLHQLLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFAIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMDCFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSREAGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAMELLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRRPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQECTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDWIFHTIKQHALN TTEUNMR TT Successful TTEUNMR FM Kinase TTEUNMR KE hsa00562:Inositol phosphate metabolism; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04070:Phosphatidylinositol signaling system; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04960:Aldosterone-regulated sodium reabsorption; hsa04973:Carbohydrate digestion and absorption; hsa05100:Bacterial invasion of epithelial cells; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTEUNMR RC R-HSA-109704:PI3K Cascade; R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1236382:Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1250342:PI3K events in ERBB4 signaling; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-180292:GAB1 signalosome; R-HSA-1963642:PI3K events in ERBB2 signaling; R-HSA-198203:PI3K/AKT activation; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-210993:Tie2 Signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-2424491:DAP12 signaling; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-373753:Nephrin interactions; R-HSA-388841:Costimulation by the CD28 family; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-416476:G alpha (q) signalling events; R-HSA-416482:G alpha (12/13) signalling events; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-5637810:Constitutive Signaling by EGFRvIII; R-HSA-5654689:PI-3K cascade:FGFR1; R-HSA-5654695:PI-3K cascade:FGFR2; R-HSA-5654710:PI-3K cascade:FGFR3; R-HSA-5654720:PI-3K cascade:FGFR4; R-HSA-912526:Interleukin receptor SHC signaling; R-HSA-912631:Regulation of signaling by CBL TTGBPJE ID TTGBPJE TTGBPJE TN PI3-kinase delta (PIK3CD) TTGBPJE UP O00329 TTGBPJE UC PK3CD_HUMAN TTGBPJE BC Kinase TTGBPJE SN PtdIns-3-kinase subunit p110-delta; PtdIns-3-kinase subunit delta; Phosphoinositide 3-kinase delta; Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, delta isoform; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform; Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta; PI3Kdelta; PI3K-delta; PI3-kinase subunit delta; PI3-kinase p110 subunit delta; P110delta TTGBPJE GN PIK3CD TTGBPJE FC Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Have a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Have important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function. Isoform 2 may be involved in stabilizing total RAS levels, resulting in increased ERK phosphorylation and increased PI3K activity. TTGBPJE EC EC 2.7.1.153 TTGBPJE PD 6G6W; 5VLR; 5UBT; 5T8F; 5M6U TTGBPJE SQ MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ TTGBPJE TT Successful TTGBPJE FM Kinase TTGBPJE KE hsa00562:Inositol phosphate metabolism; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04070:Phosphatidylinositol signaling system; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04960:Aldosterone-regulated sodium reabsorption; hsa04973:Carbohydrate digestion and absorption; hsa05100:Bacterial invasion of epithelial cells; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTGBPJE RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-912526:Interleukin receptor SHC signaling; R-HSA-912631:Regulation of signaling by CBL; R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTHBTOP ID TTHBTOP TTHBTOP TN PI3-kinase gamma (PIK3CG) TTHBTOP UP P48736 TTHBTOP UC PK3CG_HUMAN TTHBTOP BC Kinase TTHBTOP SN p120-PI3K; p110gamma; Serine/threonine protein kinase PIK3CG; PtdIns-3-kinase subunit p110-gamma; PtdIns-3-kinase subunit gamma; PtdIns-3-kinase p110; Phosphoinositol-3 kinase; Phosphoinositide-3-kinase catalytic gamma polypeptide; Phosphoinositide 3-Kinase gamma; Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, gamma isoform; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform; Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma; PI3Kgamma; PI3K-gamma; PI3K; PI3-kinase subunit gamma; PI3-kinase p110 subunit gamma TTHBTOP GN PIK3CG TTHBTOP FC Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Together with PIK3CD participates in T-lymphocyte development. Required for B-lymphocyte development and signaling. Together with PIK3CD participates in neutrophil respiratory burst. Together with PIK3CD is involved in neutrophil chemotaxis and extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to GRK2 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contributes to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis. TTHBTOP EC EC 2.7.1.153 TTHBTOP PD 6GQ7; 6FH5; 6C1S; 6AUD; 5T23 TTHBTOP SQ MELENYKQPVVLREDNCRRRRRMKPRSAAASLSSMELIPIEFVLPTSQRKCKSPETALLHVAGHGNVEQMKAQVWLRALETSVAADFYHRLGPHHFLLLYQKKGQWYEIYDKYQVVQTLDCLRYWKATHRSPGQIHLVQRHPPSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGLVTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDTPGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNGEEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRKFRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKIKDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEYVLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEGDRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQQEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYLLQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAYLRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGWTVQFNWFLHLVLGIKQGEKHSA TTHBTOP TT Successful TTHBTOP FM Kinase TTHBTOP KE hsa00562:Inositol phosphate metabolism; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04070:Phosphatidylinositol signaling system; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04960:Aldosterone-regulated sodium reabsorption; hsa04973:Carbohydrate digestion and absorption; hsa05100:Bacterial invasion of epithelial cells; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTHBTOP RC R-HSA-109704:PI3K Cascade; R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1236382:Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1250342:PI3K events in ERBB4 signaling; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-180292:GAB1 signalosome; R-HSA-1963642:PI3K events in ERBB2 signaling; R-HSA-198203:PI3K/AKT activation; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-210993:Tie2 Signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-2424491:DAP12 signaling; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-373753:Nephrin interactions; R-HSA-388841:Costimulation by the CD28 family; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-416476:G alpha (q) signalling events; R-HSA-416482:G alpha (12/13) signalling events; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-5637810:Constitutive Signaling by EGFRvIII; R-HSA-5654689:PI-3K cascade:FGFR1; R-HSA-5654695:PI-3K cascade:FGFR2; R-HSA-5654710:PI-3K cascade:FGFR3; R-HSA-5654720:PI-3K cascade:FGFR4; R-HSA-912526:Interleukin receptor SHC signaling; R-HSA-912631:Regulation of signaling by CBL TTP86E2 ID TTP86E2 TTP86E2 TN Plasminogen (PLG) TTP86E2 UP P00747 TTP86E2 UC PLMN_HUMAN TTP86E2 BC Peptidase TTP86E2 SN Plasmin TTP86E2 GN PLG TTP86E2 FC In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. TTP86E2 EC EC 3.4.21.7 TTP86E2 PD 6D40; 6D3Z; 6D3Y; 6D3X; 5UGG TTP86E2 SQ MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN TTP86E2 TT Successful TTP86E2 FM Peptidase TTP86E2 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection; hsa05164:Influenza A TTP86E2 RC R-HSA-114608:Platelet degranulation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-381426:Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-75205:Dissolution of Fibrin Clot TTI7421 ID TTI7421 TTI7421 TN Platelet-derived growth factor receptor beta (PDGFRB) TTI7421 UP P09619 TTI7421 UC PGFRB_HUMAN TTI7421 BC Kinase TTI7421 SN Platelet-derived growth factor receptor 1; PDGFR1; PDGFR-beta; PDGFR-1; PDGFR; PDGF-R-beta; CD140b antigen; CD140b; CD140 antigen-like family member B; Beta-type platelet-derived growth factor receptor; Beta-PDGFR; Beta platelet-derived growth factor receptor TTI7421 GN PDGFRB TTI7421 FC Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. TTI7421 EC EC 2.7.10.1 TTI7421 PD 3MJG; 2PLE; 2PLD; 2L6W; 2IUI TTI7421 SQ MRLPGAMPALALKGELLLLSLLLLLEPQISQGLVVTPPGPELVLNVSSTFVLTCSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFVPDPTVGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLGEVGTLQFAELHRSRTLQVVFEAYPPPTVLWFKDNRTLGDSSAGEIALSTRNVSETRYVSELTLVRVKVAEAGHYTMRAFHEDAEVQLSFQLQINVPVRVLELSESHPDSGEQTVRCRGRGMPQPNIIWSACRDLKRCPRELPPTLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRCTLRNAVGQDTQEVIVVPHSLPFKVVVISAILALVVLTIISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPMQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQHHSDKRRPPSAELYSNALPVGLPLPSHVSLTGESDGGYMDMSKDESVDYVPMLDMKGDVKYADIESSNYMAPYDNYVPSAPERTCRATLINESPVLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGFHGLRSPLDTSSVLYTAVQPNEGDNDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQDEPEPEPQLELQVEPEPELEQLPDSGCPAPRAEAEDSFL TTI7421 TT Successful TTI7421 FM Kinase TTI7421 KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04540:Gap junction; hsa04810:Regulation of actin cytoskeleton; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTI7421 RC R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5673001:RAF/MAP kinase cascade TTVDSZ0 ID TTVDSZ0 TTVDSZ0 TN Poly [ADP-ribose] polymerase 1 (PARP1) TTVDSZ0 UP P09874 TTVDSZ0 UC PARP1_HUMAN TTVDSZ0 BC Glycosyltransferases TTVDSZ0 SN Protein poly-ADP-ribosyltransferase PARP1; Poly[ADP-ribose] synthetase-1; Poly[ADP-ribose] synthase 1; Poly(ADP-ribose)polymerase-1; PPOL; PARP-1; NAD(+)Poly [ADP-ribose] polymerase-1 ADP-ribosyltransferase-1; NAD(+) ADP-ribosyltransferase-1; NAD(+) ADP-ribosyltransferase 1; DNA ADP-ribosyltransferase PARP1; ARTD1; ADPRT 1; ADPRT; ADP-ribosyltransferase diphtheria toxin-like 1 TTVDSZ0 GN PARP1 TTVDSZ0 FC Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of glutamate and aspartate residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR. Also mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity. Probably also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1. Catalyzes the poly-ADP-ribosylation of histones in a HPF1-dependent manner. Involved in the base excision repair (BER) pathway by catalyzing the poly-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation. In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Acts as a regulator of transcription: positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming. Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. TTVDSZ0 EC EC 2.4.2.30 TTVDSZ0 PD 6GHK; 6BHV; 5XSU; 5XST; 5XSR TTVDSZ0 SQ MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW TTVDSZ0 TT Successful TTVDSZ0 FM Hexosyltransferase TTVDSZ0 KE hsa03410:Base excision repair; hsa04064:NF-kappa B signaling pathway TTVDSZ0 RC R-HSA-5696400:Dual Incision in GG-NER TT8NGED ID TT8NGED TT8NGED TN Prostaglandin G/H synthase 1 (COX-1) TT8NGED UP P23219 TT8NGED UC PGH1_HUMAN TT8NGED BC Paired donor oxygen oxidoreductase TT8NGED SN Prostaglandin-endoperoxide synthase 1; Prostaglandin H2 synthase 1; PHS 1; PGHS-1; PGH synthase 1; Cyclooxygenase-1; COX1; COX-1 TT8NGED GN PTGS1 TT8NGED FC Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells. TT8NGED EC EC 1.14.99.1 TT8NGED SQ MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWEFVNATFIREMLMRLVLTVRSNLIPSPPTYNSAHDYISWESFSNVSYYTRILPSVPKDCPTPMGTKGKKQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKVGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFNIVKTATLKKLVCLNTKTCPYVSFRVPDASQDDGPAVERPSTEL TT8NGED TT Successful TT8NGED KE hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04611:Platelet activation; hsa04726:Serotonergic synapse TTBZ7OD ID TTBZ7OD TTBZ7OD TN Protein kinase C epsilon (PRKCE) TTBZ7OD UP Q02156 TTBZ7OD UC KPCE_HUMAN TTBZ7OD BC Kinase TTBZ7OD SN Protein kinase C epsilon type; PKCE; PKC epsilon; NPKC-epsilon TTBZ7OD GN PRKCE TTBZ7OD FC Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. In HeLa cells, contributes to hepatocyte growth factor (HGF)-induced cell migration, and in human corneal epithelial cells, plays a critical role in wound healing after activation by HGF. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2. 2). In prostate cancer cells, interacts with and phosphorylates STAT3, which increases DNA-binding and transcriptional activity of STAT3 and seems to be essential for prostate cancer cell invasion. Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. TTBZ7OD EC EC 2.7.11.13 TTBZ7OD PD 5LIH; 2WH0 TTBZ7OD SQ MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP TTBZ7OD TT Successful TTBZ7OD FM Kinase TTBZ7OD KE hsa04022:cGMP-PKG signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04530:Tight junction; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04930:Type II diabetes mellitus; hsa05206:MicroRNAs in cancer TTBZ7OD RC R-HSA-114508:Effects of PIP2 hydrolysis; R-HSA-1489509:DAG and IP3 signaling; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-418597:G alpha (z) signalling events TTRFOXJ ID TTRFOXJ TTRFOXJ TN Protein kinase C gamma (PRKCG) TTRFOXJ UP P05129 TTRFOXJ UC KPCG_HUMAN TTRFOXJ BC Kinase TTRFOXJ SN PRKCG; PKCG; PKC-gamma TTRFOXJ GN PRKCG TTRFOXJ FC Calcium-activated, phospholipid-and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance ofmorphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation anddegradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resultingin phase resetting of the cerebral cortex clock. TTRFOXJ EC EC 2.7.11.13 TTRFOXJ PD 2UZP; 2.00E+73 TTRFOXJ SQ MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM TTRFOXJ TT Successful TTRFOXJ KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04070:Phosphatidylinositol signaling system; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04310:Wnt signaling pathway; hsa04370:VEGF signaling pathway; hsa04510:Focal adhesion; hsa04530:Tight junction; hsa04540:Gap junction; hsa04650:Natural killer cell mediated cytotoxicity; hsa04666:Fc gamma R-mediated phagocytosis; hsa04670:Leukocyte transendothelial migration; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04727:GABAergic synapse; hsa04728:Dopaminergic synapse; hsa04730:Long-term depression; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04911:Insulin secretion; hsa04916:Melanogenesis; hsa04918:Thyroid hormone synthesis; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04960:Aldosterone-regulated sodium reabsorption; hsa04961:Endocrine and other factor-regulated calcium reabsorption; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa05031:Amphetamine addiction; hsa05032:Morphine addiction; hsa05110:Vibrio cholerae infection; hsa05143:African trypanosomiasis; hsa05146:Amoebiasis; hsa05161:Hepatitis B; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05214:Glioma; hsa05223:Non-small cell lung cancer; hsa05231:Choline metabolism in cancer TTRFOXJ RC R-HSA-111933:Calmodulin induced events; R-HSA-114516:Disinhibition of SNARE formation; R-HSA-416993:Trafficking of GluR2-containing AMPA receptors; R-HSA-418597:G alpha (z) signalling events; R-HSA-5099900:WNT5A-dependent internalization of FZD4; R-HSA-76005:Response to elevated platelet cytosolic Ca2+ TTNDSF4 ID TTNDSF4 TTNDSF4 TN Proto-oncogene c-Met (MET) TTNDSF4 UP P08581 TTNDSF4 UC MET_HUMAN TTNDSF4 BC Kinase TTNDSF4 SN Tyrosine-protein kinase Met; Scatter factor receptor; SF receptor; Met proto-oncogene tyrosine kinase; Hepatocyte growth factor receptor; HGF/SF receptor; HGF-SF receptor; HGF receptor; C-met; C-Met receptor tyrosine kinase TTNDSF4 GN MET TTNDSF4 FC Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells. May regulate cortical bone osteogenesis. Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. TTNDSF4 EC EC 2.7.10.1 TTNDSF4 PD 6I04; 6GCU; 5YA5; 5UAF; 5UAD TTNDSF4 SQ MKAPAVLAPGILVLLFTLVQRSNGECKEALAKSEMNVNMKYQLPNFTAETPIQNVILHEHHIFLGATNYIYVLNEEDLQKVAEYKTGPVLEHPDCFPCQDCSSKANLSGGVWKDNINMALVVDTYYDDQLISCGSVNRGTCQRHVFPHNHTADIQSEVHCIFSPQIEEPSQCPDCVVSALGAKVLSSVKDRFINFFVGNTINSSYFPDHPLHSISVRRLKETKDGFMFLTDQSYIDVLPEFRDSYPIKYVHAFESNNFIYFLTVQRETLDAQTFHTRIIRFCSINSGLHSYMEMPLECILTEKRKKRSTKKEVFNILQAAYVSKPGAQLARQIGASLNDDILFGVFAQSKPDSAEPMDRSAMCAFPIKYVNDFFNKIVNKNNVRCLQHFYGPNHEHCFNRTLLRNSSGCEARRDEYRTEFTTALQRVDLFMGQFSEVLLTSISTFIKGDLTIANLGTSEGRFMQVVVSRSGPSTPHVNFLLDSHPVSPEVIVEHTLNQNGYTLVITGKKITKIPLNGLGCRHFQSCSQCLSAPPFVQCGWCHDKCVRSEECLSGTWTQQICLPAIYKVFPNSAPLEGGTRLTICGWDFGFRRNNKFDLKKTRVLLGNESCTLTLSESTMNTLKCTVGPAMNKHFNMSIIISNGHGTTQYSTFSYVDPVITSISPKYGPMAGGTLLTLTGNYLNSGNSRHISIGGKTCTLKSVSNSILECYTPAQTISTEFAVKLKIDLANRETSIFSYREDPIVYEIHPTKSFISGGSTITGVGKNLNSVSVPRMVINVHEAGRNFTVACQHRSNSEIICCTTPSLQQLNLQLPLKTKAFFMLDGILSKYFDLIYVHNPVFKPFEKPVMISMGNENVLEIKGNDIDPEAVKGEVLKVGNKSCENIHLHSEAVLCTVPNDLLKLNSELNIEWKQAISSTVLGKVIVQPDQNFTGLIAGVVSISTALLLLLGFFLWLKKRKQIKDLGSELVRYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGSCRQVQYPLTDMSPILTSGDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHYVHVNATYVNVKCVAPYPSLLSSEDNADDEVDTRPASFWETS TTNDSF4 TT Successful TTNDSF4 FM Kinase TTNDSF4 KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04360:Axon guidance; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa05100:Bacterial invasion of epithelial cells; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05144:Malaria; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma; hsa05218:Melanoma; hsa05230:Central carbon metabolism in cancer TTNDSF4 RC R-HSA-416550:Sema4D mediated inhibition of cell attachment and migration TTSZ6Y3 ID TTSZ6Y3 TTSZ6Y3 TN Proto-oncogene c-Ros (ROS1) TTSZ6Y3 UP P08922 TTSZ6Y3 UC ROS1_HUMAN TTSZ6Y3 BC Kinase TTSZ6Y3 SN c-Ros receptor tyrosine kinase; Receptor tyrosine kinase c-ros oncogene 1; ROS; Proto-oncogene tyrosine-protein kinase ROS; Proto-oncogene c-Ros-1; MCF3 TTSZ6Y3 GN ROS1 TTSZ6Y3 FC Orphan receptor tyrosine kinase (RTK) that plays a role in epithelial cell differentiation and regionalization of the proximal epididymal epithelium. May activate several downstream signaling pathways related to cell differentiation, proliferation, growth and survival including the PI3 kinase-mTOR signaling pathway. Mediates the phosphorylation of PTPN11, an activator of this pathway. May also phosphorylate and activate the transcription factor STAT3 to control anchorage-independent cell growth. Mediates the phosphorylation and the activation of VAV3, a guanine nucleotide exchange factor regulating cell morphology. May activate other downstream signaling proteins including AKT1, MAPK1, MAPK3, IRS1 and PLCG2. TTSZ6Y3 EC EC 2.7.10.1 TTSZ6Y3 PD 4UXL; 3ZBF TTSZ6Y3 SQ MKNIYCLIPKLVNFATLGCLWISVVQCTVLNSCLKSCVTNLGQQLDLGTPHNLSEPCIQGCHFWNSVDQKNCALKCRESCEVGCSSAEGAYEEEVLENADLPTAPFASSIGSHNMTLRWKSANFSGVKYIIQWKYAQLLGSWTYTKTVSRPSYVVKPLHPFTEYIFRVVWIFTAQLQLYSPPSPSYRTHPHGVPETAPLIRNIESSSPDTVEVSWDPPQFPGGPILGYNLRLISKNQKLDAGTQRTSFQFYSTLPNTIYRFSIAAVNEVGEGPEAESSITTSSSAVQQEEQWLFLSRKTSLRKRSLKHLVDEAHCLRLDAIYHNITGISVDVHQQIVYFSEGTLIWAKKAANMSDVSDLRIFYRGSGLISSISIDWLYQRMYFIMDELVCVCDLENCSNIEEITPPSISAPQKIVADSYNGYVFYLLRDGIYRADLPVPSGRCAEAVRIVESCTLKDFAIKPQAKRIIYFNDTAQVFMSTFLDGSASHLILPRIPFADVKSFACENNDFLVTDGKVIFQQDALSFNEFIVGCDLSHIEEFGFGNLVIFGSSSQLHPLPGRPQELSVLFGSHQALVQWKPPALAIGANVILISDIIELFELGPSAWQNWTYEVKVSTQDPPEVTHIFLNISGTMLNVPELQSAMKYKVSVRASSPKRPGPWSEPSVGTTLVPASEPPFIMAVKEDGLWSKPLNSFGPGEFLSSDIGNVSDMDWYNNSLYYSDTKGDVFVWLLNGTDISENYHLPSIAGAGALAFEWLGHFLYWAGKTYVIQRQSVLTGHTDIVTHVKLLVNDMVVDSVGGYLYWTTLYSVESTRLNGESSLVLQTQPWFSGKKVIALTLDLSDGLLYWLVQDSQCIHLYTAVLRGQSTGDTTITEFAAWSTSEISQNALMYYSGRLFWINGFRIITTQEIGQKTSVSVLEPARFNQFTIIQTSLKPLPGNFSFTPKVIPDSVQESSFRIEGNASSFQILWNGPPAVDWGVVFYSVEFSAHSKFLASEQHSLPVFTVEGLEPYALFNLSVTPYTYWGKGPKTSLSLRAPETVPSAPENPRIFILPSGKCCNKNEVVVEFRWNKPKHENGVLTKFEIFYNISNQSITNKTCEDWIAVNVTPSVMSFQLEGMSPRCFIAFQVRAFTSKGPGPYADVVKSTTSEINPFPHLITLLGNKIVFLDMDQNQVVWTFSAERVISAVCYTADNEMGYYAEGDSLFLLHLHNRSSSELFQDSLVFDITVITIDWISRHLYFALKESQNGMQVFDVDLEHKVKYPREVKIHNRNSTIISFSVYPLLSRLYWTEVSNFGYQMFYYSIISHTLHRILQPTATNQQNKRNQCSCNVTEFELSGAMAIDTSNLEKPLIYFAKAQEIWAMDLEGCQCWRVITVPAMLAGKTLVSLTVDGDLIYWIITAKDSTQIYQAKKGNGAIVSQVKALRSRHILAYSSVMQPFPDKAFLSLASDTVEPTILNATNTSLTIRLPLAKTNLTWYGITSPTPTYLVYYAEVNDRKNSSDLKYRILEFQDSIALIEDLQPFSTYMIQIAVKNYYSDPLEHLPPGKEIWGKTKNGVPEAVQLINTTVRSDTSLIISWRESHKPNGPKESVRYQLAISHLALIPETPLRQSEFPNGRLTLLVTRLSGGNIYVLKVLACHSEEMWCTESHPVTVEMFNTPEKPYSLVPENTSLQFNWKAPLNVNLIRFWVELQKWKYNEFYHVKTSCSQGPAYVCNITNLQPYTSYNVRVVVVYKTGENSTSLPESFKTKAGVPNKPGIPKLLEGSKNSIQWEKAEDNGCRITYYILEIRKSTSNNLQNQNLRWKMTFNGSCSSVCTWKSKNLKGIFQFRVVAANNLGFGEYSGISENIILVGDDFWIPETSFILTIIVGIFLVVTIPLTFVWHRRLKNQKSAKEGVTVLINEDKELAELRGLAAGVGLANACYAIHTLPTQEEIENLPAFPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFRNFFLNSIYKSRDEANNSGVINESFEGEDGDVICLNSDDIMPVALMETKNREGLNYMVLATECGQGEEKSEGPLGSQESESCGLRKEEKEPHADKDFCQEKQVAYCPSGKPEGLNYACLTHSGYGDGSD TTSZ6Y3 TT Successful TTSZ6Y3 FM Kinase TTELIN2 ID TTELIN2 TTELIN2 TN PTPN1 messenger RNA (PTPN1 mRNA) TTELIN2 UP P18031 TTELIN2 UC PTN1_HUMAN TTELIN2 BC mRNA target TTELIN2 SN Tyrosine-protein phosphatase non-receptor type 1 (mRNA); PTP-1B (mRNA) TTELIN2 GN PTPN1 TTELIN2 FC Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET. Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. TTELIN2 EC EC 3.1.3.48 TTELIN2 PD 6CWV; 6CWU; 6BAI; 6B95; 6B90 TTELIN2 SQ MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHNGKCREFFPNHQWVKEETQEDKDCPIKEEKGSPLNAAPYGIESMSQDTEVRSRVVGGSLRGAQAASPAKGEPSLPEKDEDHALSYWKPFLVNMCVATVLTAGAYLCYRFLFNSNT TTELIN2 TT Successful TTELIN2 FM mRNA target TTELIN2 KE hsa04520:Adherens junction; hsa04910:Insulin signaling pathway TTELIN2 RC R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-877312:Regulation of IFNG signaling; R-HSA-912694:Regulation of IFNA signaling; R-HSA-982772:Growth hormone receptor signaling TTBWDI0 ID TTBWDI0 TTBWDI0 TN Ribonucleoside-diphosphate reductase M2 (RRM2) TTBWDI0 UP P31350 TTBWDI0 UC RIR2_HUMAN TTBWDI0 BC CH/CH(2) oxidoreductase TTBWDI0 SN Ribonucleotide reductase small subunit; Ribonucleotide reductase small chain; Ribonucleoside-diphosphate reductase subunit M2; RR2 TTBWDI0 GN RRM2 TTBWDI0 FC Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling. Provides the precursors necessary for DNA synthesis. TTBWDI0 EC EC 1.17.4.1 TTBWDI0 PD 3VPO; 3VPN; 3VPM; 3OLJ; 2UW2 TTBWDI0 SQ MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKTKAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSSPTENSFTLDADF TTBWDI0 TT Successful TTBWDI0 FM CH CH2 group oxidoreductase TTBWDI0 KE hsa00230:Purine metabolism; hsa00240:Pyrimidine metabolism; hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways; hsa04115:p53 signaling pathway TTBWDI0 RC R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-69205:G1/S-Specific Transcription TTBFROQ ID TTBFROQ TTBFROQ TN S-adenosylmethionine decarboxylase proenzyme (AMD1) TTBFROQ UP P17707 TTBFROQ UC DCAM_HUMAN TTBFROQ BC Carbon-carbon lyase TTBFROQ SN SamDC; S-adenosylmethioninedecarboxylase; AdoMetDC; AMD TTBFROQ GN AMD1 TTBFROQ FC Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. Essential for biosynthesis of the polyamines spermidine and spermine. TTBFROQ EC EC 4.1.1.50 TTBFROQ PD 3H0W; 3H0V; 3EPB; 3EPA; 3EP9 TTBFROQ SQ MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS TTBFROQ TT Successful TTBFROQ FM Carbon carbon lyase TTBFROQ KE hsa00270:Cysteine and methionine metabolism; hsa00330:Arginine and proline metabolism; hsa01100:Metabolic pathways TT8J1S3 ID TT8J1S3 TT8J1S3 TN Smoothened homolog (SMO) TT8J1S3 UP Q99835 TT8J1S3 UC SMO_HUMAN TT8J1S3 BC GPCR frizzled TT8J1S3 SN Smo-D473H; SMOH; Protein Gx TT8J1S3 GN SMO TT8J1S3 FC Binding of sonic hedgehog (SHH) to its receptor patched is thought to prevent normal inhibition by patched of smoothened (SMO). Required for the accumulation of KIF7, GLI2 and GLI3 in the cilia. Interacts with DLG5 at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation. G protein-coupled receptor that probably associates with the patched protein (PTCH) to transduce the hedgehog's proteins signal. TT8J1S3 PD 5V57; 5V56; 5L7I; 5L7D; 4QIN TT8J1S3 SQ MAAARPARGPELPLLGLLLLLLLGDPGRGAASSGNATGPGPRSAGGSARRSAAVTGPPPPLSHCGRAAPCEPLRYNVCLGSVLPYGATSTLLAGDSDSQEEAHGKLVLWSGLRNAPRCWAVIQPLLCAVYMPKCENDRVELPSRTLCQATRGPCAIVERERGWPDFLRCTPDRFPEGCTNEVQNIKFNSSGQCEVPLVRTDNPKSWYEDVEGCGIQCQNPLFTEAEHQDMHSYIAAFGAVTGLCTLFTLATFVADWRNSNRYPAVILFYVNACFFVGSIGWLAQFMDGARREIVCRADGTMRLGEPTSNETLSCVIIFVIVYYALMAGVVWFVVLTYAWHTSFKALGTTYQPLSGKTSYFHLLTWSLPFVLTVAILAVAQVDGDSVSGICFVGYKNYRYRAGFVLAPIGLVLIVGGYFLIRGVMTLFSIKSNHPGLLSEKAASKINETMLRLGIFGFLAFGFVLITFSCHFYDFFNQAEWERSFRDYVLCQANVTIGLPTKQPIPDCEIKNRPSLLVEKINLFAMFGTGIAMSTWVWTKATLLIWRRTWCRLTGQSDDEPKRIKKSKMIAKAFSKRHELLQNPGQELSFSMHTVSHDGPVAGLAFDLNEPSADVSSAWAQHVTKMVARRGAILPQDISVTPVATPVPPEEQANLWLVEAEISPELQKRLGRKKKRRKRKKEVCPLAPPPELHPPAPAPSTIPRLPQLPRQKCLVAAGAWGAGDSCRQGAWTLVSNPFCPEPSPPQDPFLPSAPAPVAWAHGRRQGLGPIHSRTNLMDTELMDADSDF TT8J1S3 TT Successful TT8J1S3 FM GPCR rhodopsin TT8J1S3 KE hsa04340:Hedgehog signaling pathway; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05217:Basal cell carcinoma TT8J1S3 RC R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-5610787:Hedgehog 'off' state; R-HSA-5635838:Activation of SMO TT9JZCK ID TT9JZCK TT9JZCK TN Sphingosine-1-phosphate receptor 1 (S1PR1) TT9JZCK UP P21453 TT9JZCK UC S1PR1_HUMAN TT9JZCK BC GPCR rhodopsin TT9JZCK SN Sphingosine 1-phosphate receptor Edg-1; S1P1; S1P receptor Edg-1; S1P receptor 1; Endothelial differentiation G-protein coupled receptor 1; CHEDG1; CD363 TT9JZCK GN S1PR1 TT9JZCK FC Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis. Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury. G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. TT9JZCK PD 3V2Y; 3V2W TT9JZCK SQ MGPTSVPLVKAHRSSVSDYVNYDIIVRHYNYTGKLNISADKENSIKLTSVVFILICCFIILENIFVLLTIWKTKKFHRPMYYFIGNLALSDLLAGVAYTANLLLSGATTYKLTPAQWFLREGSMFVALSASVFSLLAIAIERYITMLKMKLHNGSNNFRLFLLISACWVISLILGGLPIMGWNCISALSSCSTVLPLYHKHYILFCTTVFTLLLLSIVILYCRIYSLVRTRSRRLTFRKNISKASRSSEKSLALLKTVIIVLSVFIACWAPLFILLLLDVGCKVKTCDILFRAEYFLVLAVLNSGTNPIIYTLTNKEMRRAFIRIMSCCKCPSGDSAGKFKRPIIAGMEFSRSKSDNSSHPQKDEGDNPETIMSSGNVNSSS TT9JZCK TT Successful TT9JZCK FM GPCR rhodopsin TT9JZCK KE hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TT9JZCK RC R-HSA-418594:G alpha (i) signalling events; R-HSA-419408:Lysosphingolipid and LPA receptors TTIQUX7 ID TTIQUX7 TTIQUX7 TN Steroid 11-beta-hydroxylase (CYP11B1) TTIQUX7 UP P15538 TTIQUX7 UC C11B1_HUMAN TTIQUX7 BC Paired donor oxygen oxidoreductase TTIQUX7 SN S11BH; P450C11; P-450c11; CYPXIB1; CYP11B1 TTIQUX7 GN CYP11B1 TTIQUX7 FC Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB. TTIQUX7 EC EC 1.14.15.4 TTIQUX7 PD 6M7X TTIQUX7 SQ MALRAKAEVCMAVPWLSLQRAQALGTRAARVPRTVLPFEAMPRRPGNRWLRLLQIWREQGYEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELSPDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVASSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRPERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQEDIKMVYSFILRPSMFPLLTFRAIN TTIQUX7 TT Successful TTIQUX7 KE hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways TTIQUX7 RC R-HSA-194002:Glucocorticoid biosynthesis; R-HSA-211976:Endogenous sterols TTRA5BZ ID TTRA5BZ TTRA5BZ TN Steroid 17-alpha-monooxygenase (S17AH) TTRA5BZ UP P05093 TTRA5BZ UC CP17A_HUMAN TTRA5BZ BC Paired donor oxygen oxidoreductase TTRA5BZ SN Steroid 17-alpha-hydroxylase/17,20 lyase; P450c17; P450-C17; P450 17; CYPXVII; CYP17A1; CYP 17; 17 alpha-Hydroxylase/C17-20-lyase TTRA5BZ GN CYP17A1 TTRA5BZ FC Conversion of pregnenolone and progesterone to their 17- alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty. TTRA5BZ EC EC 1.14.14.19 TTRA5BZ PD 6CIZ; 6CIR; 6CHI; 5UYS; 5IRV TTRA5BZ SQ MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVISLICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIPKVVFLIDSFKVKIKVRQAWREAQAEGST TTRA5BZ TT Successful TTRA5BZ KE hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways; hsa04913:Ovarian steroidogenesis; hsa04917:Prolactin signaling pathway TTRA5BZ RC R-HSA-193048:Androgen biosynthesis; R-HSA-194002:Glucocorticoid biosynthesis; R-HSA-211976:Endogenous sterols TTHM0R1 ID TTHM0R1 TTHM0R1 TN Steryl-sulfatase (STS) TTHM0R1 UP P08842 TTHM0R1 UC STS_HUMAN TTHM0R1 BC Sulfuric ester hydrolase TTHM0R1 SN Steryl-sulfate sulfohydrolase; Steroid sulfatase; STS; Estrone sulfatase; Arylsulfatase C; ASC TTHM0R1 GN STS TTHM0R1 FC Conversion of sulfated steroid precursors to estrogens during pregnancy. TTHM0R1 EC EC 3.1.6.2 TTHM0R1 PD 1P49 TTHM0R1 SQ MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTTGFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPLNCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRIIDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPVGSNGCFATHVCFCFGSYVTHHDPPLLFDISKDPRERNPLTPASEPRFYEILKVMQEAADRHTQTLPEVPDQFSWNNFLWKPWLQLCCPSTGLSCQCDREKQDKRLSR TTHM0R1 TT Successful TTHM0R1 KE hsa00140:Steroid hormone biosynthesis TTHM0R1 RC R-HSA-1660662:Glycosphingolipid metabolism TTP3QRF ID TTP3QRF TTP3QRF TN Thymidine kinase 1 (TK1) TTP3QRF UP P04183 TTP3QRF UC KITH_HUMAN TTP3QRF BC Kinase TTP3QRF SN Thymidine kinase, cytosolic TTP3QRF GN TK1 TTP3QRF FC cytosol, identical protein binding, thymidine kinase activity, zinc ion binding, DNA metabolic process, nucleobase-containing compound metabolic process, protein homotetramerization, pyrimidine nucleoside salvage, thymidine metabolic process TTP3QRF EC EC 2.7.1.21 TTP3QRF PD 2WVJ; 2ORV; 1XBT; 1W4R TTP3QRF SQ MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTRYSSSFCTHDRNTMEALPACLLRDVAQEALGVAVIGIDEGQFFPDIVEFCEAMANAGKTVIVAALDGTFQRKPFGAILNLVPLAESVVKLTAVCMECFREAAYTKRLGTEKEVEVIGGADKYHSVCRLCYFKKASGQPAGPDNKENCPVPGKPGEAVAARKLFAPQQILQCSPAN TTP3QRF TT Successful TTP3QRF FM Kinase TTO0IB8 ID TTO0IB8 TTO0IB8 TN Thymidine phosphorylase (TYMP) TTO0IB8 UP P19971 TTO0IB8 UC TYPH_HUMAN TTO0IB8 BC Pentosyltransferase TTO0IB8 SN TdRPase; TYMP; TP; Platelet-derived endothelial cell growth factor; PDECGF; PD-ECGF; Gliostatin TTO0IB8 GN TYMP TTO0IB8 FC Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. TTO0IB8 EC EC 2.4.2.4 TTO0IB8 PD 2WK6; 2WK5; 2J0F; 1UOU TTO0IB8 SQ MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARALCSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPPQQ TTO0IB8 TT Successful TTO0IB8 KE hsa00240:Pyrimidine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways; hsa05219:Bladder cancer TTM1TDX ID TTM1TDX TTM1TDX TN Tryptase alpha/beta-1 (Tryptase) TTM1TDX UP Q15661 TTM1TDX UC TRYB1_HUMAN TTM1TDX BC Peptidase TTM1TDX SN Tryptase-1; Tryptase alpha-1; Tryptase I; TPSB1; TPS2; TPS1 TTM1TDX GN TPSAB1 TTM1TDX FC May play a role in innate immunity. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates. Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. TTM1TDX EC EC 3.4.21.59 TTM1TDX PD 5WI6; 5F03; 4MQA; 4MPX; 4MPW TTM1TDX SQ MLNLLLLALPVLASRAYAAPAPGQALQRVGIVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPKKP TTM1TDX TT Successful TTM1TDX FM Peptidase S1 family TTM1TDX RC R-HSA-1592389:Activation of Matrix Metalloproteinases TTOU65C ID TTOU65C TTOU65C TN Tyrosine-protein kinase SYK (SYK) TTOU65C UP P43405 TTOU65C UC KSYK_HUMAN TTOU65C BC Kinase TTOU65C SN p72-Syk; Spleen tyrosine kinase TTOU65C GN SYK TTOU65C FC Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development. Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. It also phosphorylates and activates PLCG1 and the PKC signaling pathway. It also phosphorylates BTK and regulates its activity in B-cell antigen receptor (BCR)-coupled signaling. In addition to its function downstream of BCR plays also a role in T-cell receptor signaling. Plays also a crucial role in the innate immune response to fungal, bacterial and viral pathogens. It is for instance activated by the membrane lectin CLEC7A. Upon stimulation by fungal proteins, CLEC7A together with SYK activates immune cells inducing the production of ROS. Also activates the inflammasome and NF-kappa-B-mediated transcription of chemokines and cytokines in presence of pathogens. Regulates neutrophil degranulation and phagocytosis through activation of the MAPK signaling cascade. Required for the stimulation of neutrophil phagocytosis by IL15. Also mediates the activation of dendritic cells by cell necrosis stimuli. Also involved in mast cells activation. Involved in interleukin-3/IL3-mediated signaling pathway in basophils. Also functions downstream of receptors mediating cell adhesion. Relays for instance, integrin-mediated neutrophils and macrophages activation and P-selectin receptor/SELPG-mediated recruitment of leukocytes to inflammatory loci. Plays also a role in non-immune processes. It is for instance involved in vascular development where it may regulate blood and lymphatic vascular separation. It is also required for osteoclast development and function. Functions in the activation of platelets by collagen, mediating PLCG2 phosphorylation and activation. May be coupled to the collagen receptor by the ITAM domain-containing FCER1G. Also activated by the membrane lectin CLEC1B that is required for activation of platelets by PDPN/podoplanin. Involved in platelet adhesion being activated by ITGB3 engaged by fibrinogen. Together with CEACAM20, enhances production of the cytokine CXCL8/IL-8 via the NFKB pathway and may thus have a role in the intestinal immune response. Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). TTOU65C EC EC 2.7.10.2 TTOU65C PD 6HM7; 6HM6; 5Y5U; 5Y5T; 5TT7 TTOU65C SQ MASSGMADSANHLPFFFGNITREEAEDYLVQGGMSDGLYLLRQSRNYLGGFALSVAHGRKAHHYTIERELNGTYAIAGGRTHASPADLCHYHSQESDGLVCLLKKPFNRPQGVQPKTGPFEDLKENLIREYVKQTWNLQGQALEQAIISQKPQLEKLIATTAHEKMPWFHGKISREESEQIVLIGSKTNGKFLIRARDNNGSYALCLLHEGKVLHYRIDKDKTGKLSIPEGKKFDTLWQLVEHYSYKADGLLRVLTVPCQKIGTQGNVNFGGRPQLPGSHPATWSAGGIISRIKSYSFPKPGHRKSSPAQGNRQESTVSFNPYEPELAPWAADKGPQREALPMDTEVYESPYADPEEIRPKEVYLDRKLLTLEDKELGSGNFGTVKKGYYQMKKVVKTVAVKILKNEANDPALKDELLAEANVMQQLDNPYIVRMIGICEAESWMLVMEMAELGPLNKYLQQNRHVKDKNIIELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGKWPVKWYAPECINYYKFSSKSDVWSFGVLMWEAFSYGQKPYRGMKGSEVTAMLEKGERMGCPAGCPREMYDLMNLCWTYDVENRPGFAAVELRLRNYYYDVVN TTOU65C TT Successful TTOU65C FM Kinase TTOU65C KE hsa04064:NF-kappa B signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04380:Osteoclast differentiation; hsa04611:Platelet activation; hsa04650:Natural killer cell mediated cytotoxicity; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa05152:Tuberculosis; hsa05169:Epstein-Barr virus infection; hsa05203:Viral carcinogenesis TTOU65C RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-2029481:FCGR activation; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-2424491:DAP12 signaling; R-HSA-2454202:Fc epsilon receptor (FCERI) signaling; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-2871809:FCERI mediated Ca+2 mobilization; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-451927:Interleukin-2 signaling; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-5621480:Dectin-2 family; R-HSA-912631:Regulation of signaling by CBL; R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTGY7WI ID TTGY7WI TTGY7WI TN Urokinase-type plasminogen activator (PLAU) TTGY7WI UP P00749 TTGY7WI UC UROK_HUMAN TTGY7WI BC Peptidase TTGY7WI SN UPA; U-plasminogen activator TTGY7WI GN PLAU TTGY7WI FC Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. TTGY7WI EC EC 3.4.21.73 TTGY7WI PD 6NMB; 5ZC5; 5ZAJ; 5ZAH; 5ZAG TTGY7WI SQ MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRRRPWCYVQVGLKPLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHTKEENGLAL TTGY7WI TT Successful TTGY7WI FM Peptidase TTGY7WI KE hsa04064:NF-kappa B signaling pathway; hsa04610:Complement and coagulation cascades; hsa05202:Transcriptional misregulation in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer TTGY7WI RC R-HSA-75205:Dissolution of Fibrin Clot TT1VAUK ID TT1VAUK TT1VAUK TN VEGFR1 messenger RNA (VEGFR1 mRNA) TT1VAUK UP P17948 TT1VAUK UC VGFR1_HUMAN TT1VAUK BC mRNA target TT1VAUK SN Vascular permeability factor receptor (mRNA); VEGFR1 (mRNA); VEGFR-1 (mRNA); VEGF-1 receptor (mRNA); Tyrosine-protein kinase receptor FLT (mRNA); Tyrosine-protein kinase FRT (mRNA); Fms-like tyrosine kinase 1 (mRNA); FRT (mRNA); FLT (mRNA) TT1VAUK GN FLT1 TT1VAUK FC May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Likewise, isoforms lacking a transmembrane domain, such as isoform 2, isoform 3 and isoform 4, may function as decoy receptors for VEGFA. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Isoform 1 phosphorylates PLCG. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1. Isoform 7 has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion. Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. TT1VAUK EC EC 2.7.10.1 TT1VAUK PD 5T89; 5EX3; 5ABD; 4CL7; 4CKV TT1VAUK SQ MVSYWDTGVLLCALLSCLLLTGSSSGSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNTSVHIYDKAFITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTATLIVNVKPQIYEKAVSSFPDPALYPLGSRQILTCTAYGIPQPTIKWFWHPCNHNHSEARCDFCSNNEESFILDADSNMGNRIESITQRMAIIEGKNKMASTLVVADSRISGIYICIASNKVGTVGRNISFYITDVPNGFHVNLEKMPTEGEDLKLSCTVNKFLYRDVTWILLRTVNNRTMHYSISKQKMAITKEHSITLNLTIMNVSLQDSGTYACRARNVYTGEEILQKKEITIRDQEAPYLLRNLSDHTVAISSSTTLDCHANGVPEPQITWFKNNHKIQQEPGIILGPGSSTLFIERVTEEDEGVYHCKATNQKGSVESSAYLTVQGTSDKSNLELITLTCTCVAATLFWLLLTLFIRKMKRSSSEIKTDYLSIIMDPDEVPLDEQCERLPYDASKWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRTVAVKMLKEGATASEYKALMTELKILTHIGHHLNVVNLLGACTKQGGPLMVIVEYCKYGNLSNYLKSKRDLFFLNKDAALHMEPKKEKMEPGLEQGKKPRLDSVTSSESFASSGFQEDKSLSDVEEEEDSDGFYKEPITMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDTRLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGGSPYPGVQMDEDFCSRLREGMRMRAPEYSTPEIYQIMLDCWHRDPKERPRFAELVEKLGDLLQANVQQDGKDYIPINAILTGNSGFTYSTPAFSEDFFKESISAPKFNSGSSDDVRYVNAFKFMSLERIKTFEELLPNATSMFDDYQGDSSTLLASPMLKRFTWTDSKPKASLKIDLRVTSKSKESGLSDVSRPSFCHSSCGHVSEGKRRFTYDHAELERKIACCSPPPDYNSVVLYSTPPI TT1VAUK TT Successful TT1VAUK FM mRNA target TT1VAUK KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa05202:Transcriptional misregulation in cancer; hsa05323:Rheumatoid arthritis TT1VAUK RC R-HSA-194306:Neurophilin interactions with VEGF and VEGFR; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization TTK59TV ID TTK59TV TTK59TV TN Vitamin D3 receptor (VDR) TTK59TV UP P11473 TTK59TV UC VDR_HUMAN TTK59TV BC Nuclear hormone receptor TTK59TV SN Vitamin D(3) receptor; Nuclear vitamin D receptor; Nuclear receptor subfamily 1 group I member 1; NR1I1; 1,25-dihydroxyvitamin D3 receptor TTK59TV GN VDR TTK59TV FC Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3-responsive target genes. Plays a central role in calcium homeostasis. Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells. TTK59TV PD 5YT2; 5YSY; 5V39; 5GT4; 4ITF TTK59TV SQ MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAALIEAIQDRLSNTLQTYIRCRHPPPGSHLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPECSMKLTPLVLEVFGNEIS TTK59TV TT Successful TTK59TV FM Nuclear hormone receptor TTK59TV KE hsa04961:Endocrine and other factor-regulated calcium reabsorption; hsa04978:Mineral absorption; hsa05152:Tuberculosis TTK59TV RC R-HSA-383280:Nuclear Receptor transcription pathway TT4FDG6 ID TT4FDG6 TT4FDG6 TN Voltage-gated calcium channel alpha Cav2.2 (CACNA1B) TT4FDG6 UP Q00975 TT4FDG6 UC CAC1B_HUMAN TT4FDG6 BC Voltage-gated ion channel TT4FDG6 SN Voltage-gated calcium channel alpha subunit Cav2.2; Voltage-dependent N-type calcium channel alpha-1B subunit; N-type Ca2+ channel; Calcium channel, L type, alpha-1 polypeptide isoform 5; CACNA1B; Brain calcium channel III; BIII TT4FDG6 GN CACNA1B TT4FDG6 FC Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin- IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons. TT4FDG6 PD 2LCM TT4FDG6 SQ MVRFGDELGGRYGGPGGGERARGGGAGGAGGPGPGGLQPGQRVLYKQSIAQRARTMALYNPIPVKQNCFTVNRSLFVFSEDNVVRKYAKRITEWPPFEYMILATIIANCIVLALEQHLPDGDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFVFHKGSYLRNGWNVMDFVVVLTGILATAGTDFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYMGKFHKACFPNSTDAEPVGDFPCGKEAPARLCEGDTECREYWPGPNFGITNFDNILFAILTVFQCITMEGWTDILYNTNDAAGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYLEWIFKAEEVMLAEEDRNAEEKSPLDVLKRAATKKSRNDLIHAEEGEDRFADLCAVGSPFARASLKSGKTESSSYFRRKEKMFRFFIRRMVKAQSFYWVVLCVVALNTLCVAMVHYNQPRRLTTTLYFAEFVFLGLFLTEMSLKMYGLGPRSYFRSSFNCFDFGVIVGSVFEVVWAAIKPGSSFGISVLRALRLLRIFKVTKYWSSLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFQDETPTTNFDTFPAAILTVFQILTGEDWNAVMYHGIESQGGVSKGMFSSFYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEEEMEEAANQKLALQKAKEVAEVSPMSAANISIAARQQNSAKARSVWEQRASQLRLQNLRASCEALYSEMDPEERLRFATTRHLRPDMKTHLDRPLVVELGRDGARGPVGGKARPEAAEAPEGVDPPRRHHRHRDKDKTPAAGDQDRAEAPKAESGEPGAREERPRPHRSHSKEAAGPPEARSERGRGPGPEGGRRHHRRGSPEEAAEREPRRHRAHRHQDPSKECAGAKGERRARHRGGPRAGPREAESGEEPARRHRARHKAQPAHEAVEKETTEKEATEKEAEIVEADKEKELRNHQPREPHCDLETSGTVTVGPMHTLPSTCLQKVEEQPEDADNQRNVTRMGSQPPDPNTIVHIPVMLTGPLGEATVVPSGNVDLESQAEGKKEVEADDVMRSGPRPIVPYSSMFCLSPTNLLRRFCHYIVTMRYFEVVILVVIALSSIALAAEDPVRTDSPRNNALKYLDYIFTGVFTFEMVIKMIDLGLLLHPGAYFRDLWNILDFIVVSGALVAFAFSGSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVLNILIVYMLFMFIFAVIAVQLFKGKFFYCTDESKELERDCRGQYLDYEKEEVEAQPRQWKKYDFHYDNVLWALLTLFTVSTGEGWPMVLKHSVDATYEEQGPSPGYRMELSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKVMSECSLEKNERACIDFAISAKPLTRYMPQNRQSFQYKTWTFVVSPPFEYFIMAMIALNTVVLMMKFYDAPYEYELMLKCLNIVFTSMFSMECVLKIIAFGVLNYFRDAWNVFDFVTVLGSITDILVTEIAETNNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALDDDTSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLSNQACDEQANATECGSDFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFIRVWAEYDPAACGRISYNDMFEMLKHMSPPLGLGKKCPARVAYKRLVRMNMPISNEDMTVHFTSTLMALIRTALEIKLAPAGTKQHQCDAELRKEISVVWANLPQKTLDLLVPPHKPDEMTVGKVYAALMIFDFYKQNKTTRDQMQQAPGGLSQMGPVSLFHPLKATLEQTQPAVLRGARVFLRQKSSTSLSNGGAIQNQESGIKESVSWGTQRTQDAPHEARPPLERGHSTEIPVGRSGALAVDVQMQSITRRGPDGEPQPGLESQGRAASMPRLAAETQPVTDASPMKRSISTLAQRPRGTHLCSTTPDRPPPSQASSHHHHHRCHRRRDRKQRSLEKGPSLSADMDGAPSSAVGPGLPPGEGPTGCRRERERRQERGRSQERRQPSSSSSEKQRFYSCDRFGGREPPKPKPSLSSHPTSPTAGQEPGPHPQGSGSVNGSPLLSTSGASTPGRGGRRQLPQTPLTPRPSITYKTANSSPIHFAGAQTSLPAFSPGRLSRGLSEHNALLQRDPLSQPLAPGSRIGSDPYLGQRLDSEASVHALPEDTLTFEEAVATNSGRSSRTSYVSSLTSQSHPLRRVPNGYHCTLGLSSGGRARHSYHHPDQDHWC TT4FDG6 TT Successful TT4FDG6 KE hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04721:Synaptic vesicle cycle; hsa04723:Retrograde endocannabinoid signaling; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04727:GABAergic synapse; hsa04728:Dopaminergic synapse; hsa04742:Taste transduction; hsa04930:Type II diabetes mellitus; hsa05032:Morphine addiction; hsa05033:Nicotine addiction TT4FDG6 RC R-HSA-112308:Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels TTG21IS ID TTG21IS TTG21IS TN HUMAN basigin (BSG) TTG21IS UP P35613 TTG21IS UC BASI_HUMAN TTG21IS BC Basigin protein TTG21IS SN UNQ6505/PRO21383; Tumor cell-derived collagenase stimulatory factor; TCSF; OK blood group antigen; Leukocyte activation antigen M6; Extracellular matrix metalloproteinase inducer; EMMPRIN; 5F7 TTG21IS GN BSG TTG21IS FC Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes. Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3, SLC16A8, SLC16A11 and SLC16A12 to the plasma membrane. TTG21IS PD 5XF0; 5X0T; 4U0Q; 3QR2; 3QQN TTG21IS SQ MAAALFVLLGFALLGTHGASGAAGFVQAPLSQQRWVGGSVELHCEAVGSPVPEIQWWFEGQGPNDTCSQLWDGARLDRVHIHATYHQHAASTISIDTLVEEDTGTYECRASNDPDRNHLTRAPRVKWVRAQAVVLVLEPGTVFTTVEDLGSKILLTCSLNDSATEVTGHRWLKGGVVLKEDALPGQKTEFKVDSDDQWGEYSCVFLPEPMGTANIQLHGPPRVKAVKSSEHINEGETAMLVCKSESVPPVTDWAWYKITDSEDKALMNGSESRFFVSSSQGRSELHIENLNMEADPGQYRCNGTSSKGSDQAIITLRVRSHLAALWPFLGIVAEVLVLVTIIFIYEKRRKPEDVLDDDDAGSAPLKSSGQHQNDKGKNVRQRNSS TT1CN09 ID TT1CN09 TT1CN09 TN HUMAN toll-like receptor 3 (TLR3) TT1CN09 UP O15455 TT1CN09 UC TLR3_HUMAN TT1CN09 BC Toll-like receptor TT1CN09 SN CD283 TT1CN09 GN TLR3 TT1CN09 FC Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response. TT1CN09 PD 5GS0; 3ULV; 3ULU; 2MKA; 2MK9 TT1CN09 SQ MRQTLPCIYFWGGLLPFGMLCASSTTKCTVSHEVADCSHLKLTQVPDDLPTNITVLNLTHNQLRRLPAANFTRYSQLTSLDVGFNTISKLEPELCQKLPMLKVLNLQHNELSQLSDKTFAFCTNLTELHLMSNSIQKIKNNPFVKQKNLITLDLSHNGLSSTKLGTQVQLENLQELLLSNNKIQALKSEELDIFANSSLKKLELSSNQIKEFSPGCFHAIGRLFGLFLNNVQLGPSLTEKLCLELANTSIRNLSLSNSQLSTTSNTTFLGLKWTNLTMLDLSYNNLNVVGNDSFAWLPQLEYFFLEYNNIQHLFSHSLHGLFNVRYLNLKRSFTKQSISLASLPKIDDFSFQWLKCLEHLNMEDNDIPGIKSNMFTGLINLKYLSLSNSFTSLRTLTNETFVSLAHSPLHILNLTKNKISKIESDAFSWLGHLEVLDLGLNEIGQELTGQEWRGLENIFEIYLSYNKYLQLTRNSFALVPSLQRLMLRRVALKNVDSSPSPFQPLRNLTILDLSNNNIANINDDMLEGLEKLEILDLQHNNLARLWKHANPGGPIYFLKGLSHLHILNLESNGFDEIPVEVFKDLFELKIIDLGLNNLNTLPASVFNNQVSLKSLNLQKNLITSVEKKVFGPAFRNLTELDMRFNPFDCTCESIAWFVNWINETHTNIPELSSHYLCNTPPHYHGFPVRLFDTSSCKDSAPFELFFMINTSILLIFIFIVLLIHFEGWRISFYWNVSVHRVLGFKEIDRQTEQFEYAAYIIHAYKDKDWVWEHFSSMEKEDQSLKFCLEERDFEAGVFELEAIVNSIKRSRKIIFVITHHLLKDPLCKRFKVHHAVQQAIEQNLDSIILVFLEEIPDYKLNHALCLRRGMFKSHCILNWPVQKERIGAFRHKLQVALGSKNSVH TT1CN09 FM Toll-like receptor family TTSQIFT ID TTSQIFT TTSQIFT TN 5-HT 1A receptor (HTR1A) TTSQIFT UP P08908 TTSQIFT UC 5HT1A_HUMAN TTSQIFT BC GPCR rhodopsin TTSQIFT SN Serotonin receptor 1A; G-21; ADRBRL1; ADRB2RL1; 5-hydroxytryptamine receptor 1A; 5-HT1A receptor; 5-HT1A; 5-HT-1A TTSQIFT GN HTR1A TTSQIFT FC Functions as a receptor for various drugs and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling inhibits adenylate cyclase activity and activates a phosphatidylinositol-calcium second messenger system that regulates the release of Ca(2+) ions from intracellular stores. Plays a role in the regulation of 5-hydroxytryptamine release and in the regulation of dopamine and 5-hydroxytryptamine metabolism. Plays a role in the regulation of dopamine and 5-hydroxytryptamine levels in the brain, and thereby affects neural activity, mood and behavior. Plays a role in the response to anxiogenic stimuli. G-protein coupled receptor for 5-hydroxytryptamine (serotonin). TTSQIFT SQ MDVLSPGQGNNTTSPPAPFETGGNTTGISDVTVSYQVITSLLLGTLIFCAVLGNACVVAAIALERSLQNVANYLIGSLAVTDLMVSVLVLPMAALYQVLNKWTLGQVTCDLFIALDVLCCTSSILHLCAIALDRYWAITDPIDYVNKRTPRRAAALISLTWLIGFLISIPPMLGWRTPEDRSDPDACTISKDHGYTIYSTFGAFYIPLLLMLVLYGRIFRAARFRIRKTVKKVEKTGADTRHGASPAPQPKKSVNGESGSRNWRLGVESKAGGALCANGAVRQGDDGAALEVIEVHRVGNSKEHLPLPSEAGPTPCAPASFERKNERNAEAKRKMALARERKTVKTLGIIMGTFILCWLPFFIVALVLPFCESSCHMPTLLGAIINWLGYSNSLLNPVIYAYFNKDFQNAFKKIIKCKFCRQ TTSQIFT TT Successful TTSQIFT FM GPCR rhodopsin TTSQIFT KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse TTSQIFT RC R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events TTK8CXU ID TTK8CXU TTK8CXU TN 5-HT 1B receptor (HTR1B) TTK8CXU UP P28222 TTK8CXU UC 5HT1B_HUMAN TTK8CXU BC GPCR rhodopsin TTK8CXU SN Serotonin receptor 1B; Serotonin 1D beta receptor; S12; HTR1DB; 5-hydroxytryptamine receptor 1B; 5-HT1B receptor; 5-HT1B; 5-HT-1D-beta; 5-HT-1B TTK8CXU GN HTR1B TTK8CXU FC Functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances, such as lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries. G-protein coupled receptor for 5-hydroxytryptamine (serotonin). TTK8CXU PD 6G79; 5V54; 4IAR; 4IAQ; 2G1X TTK8CXU SQ MEEPGAQCAPPPPAGSETWVPQANLSSAPSQNCSAKDYIYQDSISLPWKVLLVMLLALITLATTLSNAFVIATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYTVTGRWTLGQVVCDFWLSSDITCCTASILHLCVIALDRYWAITDAVEYSAKRTPKRAAVMIALVWVFSISISLPPFFWRQAKAEEEVSECVVNTDHILYTVYSTVGAFYFPTLLLIALYGRIYVEARSRILKQTPNRTGKRLTRAQLITDSPGSTSSVTSINSRVPDVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGAFIVCWLPFFIISLVMPICKDACWFHLAIFDFFTWLGYLNSLINPIIYTMSNEDFKQAFHKLIRFKCTS TTK8CXU TT Successful TTK8CXU FM GPCR rhodopsin TTK8CXU KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse TTK8CXU RC R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events TTJQOD7 ID TTJQOD7 TTJQOD7 TN 5-HT 2A receptor (HTR2A) TTJQOD7 UP P28223 TTJQOD7 UC 5HT2A_HUMAN TTJQOD7 BC GPCR rhodopsin TTJQOD7 SN Serotonin receptor 2A; HTR2; 5-hydroxytryptamine receptor 2A; 5-HT-2A; 5-HT-2 TTJQOD7 GN HTR2A TTJQOD7 FC G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions from intracellular stores. Affects neural activity, perception, cognition and mood. Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction. TTJQOD7 PD 6A94; 6A93 TTJQOD7 SQ MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV TTJQOD7 TT Successful TTJQOD7 FM GPCR rhodopsin TTJQOD7 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04726:Serotonergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels TTJQOD7 RC R-HSA-390666:Serotonin receptors; R-HSA-416476:G alpha (q) signalling events TT0K1SC ID TT0K1SC TT0K1SC TN 5-HT 2B receptor (HTR2B) TT0K1SC UP P41595 TT0K1SC UC 5HT2B_HUMAN TT0K1SC BC GPCR rhodopsin TT0K1SC SN Serotonin receptor 2B; 5-hydroxytryptamine receptor 2B; 5-HT2B; 5-HT-2B; 5-HT 2B TT0K1SC GN HTR2B TT0K1SC FC Functions as a receptor for various ergot alkaloid derivatives and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down-stream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores. Plays a role in the regulation of dopamine and 5-hydroxytryptamine release, 5-hydroxytryptamine uptake and in the regulation of extracellular dopamine and 5-hydroxytryptamine levels, and thereby affects neural activity. May play a role in the perception of pain. Plays a role in the regulation of behavior, including impulsive behavior. Required for normal proliferation of embryonic cardiac myocytes and normal heart development. Protects cardiomyocytes against apoptosis. Plays a role in the adaptation of pulmonary arteries to chronic hypoxia. Plays a role in vasoconstriction. Required for normal osteoblast function and proliferation, and for maintaining normal bone density. Required for normal proliferation of the interstitial cells of Cajal in the intestine. G-protein coupled receptor for 5-hydroxytryptamine (serotonin). TT0K1SC PD 6DS0; 6DRZ; 6DRY; 6DRX; 5TVN TT0K1SC SQ MALSYRVSELQSTIPEHILQSTFVHVISSNWSGLQTESIPEEMKQIVEEQGNKLHWAALLILMVIIPTIGGNTLVILAVSLEKKLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEAMWPLPLVLCPAWLFLDVLFSTASIMHLCAISVDRYIAIKKPIQANQYNSRATAFIKITVVWLISIGIAIPVPIKGIETDVDNPNNITCVLTKERFGDFMLFGSLAAFFTPLAIMIVTYFLTIHALQKKAYLVKNKPPQRLTWLTVSTVFQRDETPCSSPEKVAMLDGSRKDKALPNSGDETLMRRTSTIGKKSVQTISNEQRASKVLGIVFFLFLLMWCPFFITNITLVLCDSCNQTTLQMLLEIFVWIGYVSSGVNPLVYTLFNKTFRDAFGRYITCNYRATKSVKTLRKRSSKIYFRNPMAENSKFFKKHGIRNGINPAMYQSPMRLRSSTIQSSSIILLDTLLLTENEGDKTEEQVSYV TT0K1SC TT Successful TT0K1SC FM GPCR rhodopsin TT0K1SC KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04726:Serotonergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels TT0K1SC RC R-HSA-390666:Serotonin receptors; R-HSA-416476:G alpha (q) signalling events TTWJBZ5 ID TTWJBZ5 TTWJBZ5 TN 5-HT 2C receptor (HTR2C) TTWJBZ5 UP P28335 TTWJBZ5 UC 5HT2C_HUMAN TTWJBZ5 BC GPCR rhodopsin TTWJBZ5 SN Serotonin receptor 2C; HTR1C; 5HT-1C; 5-hydroxytryptamine receptor 2C; 5-hydroxytryptamine receptor 1C; 5-HTR2C; 5-HT2C receptor; 5-HT2C; 5-HT1C; 5-HT-2C; 5-HT-1C TTWJBZ5 GN HTR2C TTWJBZ5 FC Functions as a receptor for various drugs and psychoactive substances, including ergot alkaloid derivatives, 1-2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down-stream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores. Regulates neuronal activity via the activation of short transient receptor potential calcium channels in the brain, and thereby modulates the activation of pro-opiomelacortin neurons and the release of CRH that then regulates the release of corticosterone. Plays a role in the regulation of appetite and eating behavior, responses to anxiogenic stimuli and stress. Plays a role in insulin sensitivity and glucose homeostasis. G-protein coupled receptor for 5-hydroxytryptamine (serotonin). TTWJBZ5 PD 6BQH; 6BQG TTWJBZ5 SQ MVNLRNAVHSFLVHLIGLLVWQCDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV TTWJBZ5 TT Successful TTWJBZ5 FM GPCR rhodopsin TTWJBZ5 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04726:Serotonergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels TTWJBZ5 RC R-HSA-390666:Serotonin receptors; R-HSA-416476:G alpha (q) signalling events TT07C3Y ID TT07C3Y TT07C3Y TN 5-HT 4 receptor (HTR4) TT07C3Y UP Q13639 TT07C3Y UC 5HT4R_HUMAN TT07C3Y BC GPCR rhodopsin TT07C3Y SN Serotonin receptor 4; 5-hydroxytryptamine receptor 4; 5-HT4 receptor; 5-HT4; 5-HT-4 TT07C3Y GN HTR4 TT07C3Y FC The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. TT07C3Y PD 5EM9 TT07C3Y SQ MDKLDANVSSEEGFGSVEKVVLLTFLSTVILMAILGNLLVMVAVCWDRQLRKIKTNYFIVSLAFADLLVSVLVMPFGAIELVQDIWIYGEVFCLVRTSLDVLLTTASIFHLCCISLDRYYAICCQPLVYRNKMTPLRIALMLGGCWVIPTFISFLPIMQGWNNIGIIDLIEKRKFNQNSNSTYCVFMVNKPYAITCSVVAFYIPFLLMVLAYYRIYVTAKEHAHQIQMLQRAGASSESRPQSADQHSTHRMRTETKAAKTLCIIMGCFCLCWAPFFVTNIVDPFIDYTVPGQVWTAFLWLGYINSGLNPFLYAFLNKSFRRAFLIILCCDDERYRRPSILGQTVPCSTTTINGSTHVLRDAVECGGQWESQCHPPATSPLVAAQPSDT TT07C3Y TT Successful TT07C3Y KE hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse TT07C3Y RC R-HSA-390666:Serotonin receptors; R-HSA-418555:G alpha (s) signalling events TTY84UG ID TTY84UG TTY84UG TN Acetyl-CoA carboxylase 2 (ACACB) TTY84UG UP O00763 TTY84UG UC ACACB_HUMAN TTY84UG BC Carbon-carbon ligase TTY84UG SN Acetyl-Coenzyme A carboxylase beta; Acetyl CoA carboxylase beta; ACCbeta; ACC2; ACC-beta; ACACB TTY84UG GN ACACB TTY84UG FC Catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in inhibition of fatty acid and glucose oxidation and enhancement of fat storage. May play a role in regulation of mitochondrial fatty acid oxidation through malonyl- CoA-dependent inhibition of carnitine palmitoyltransferase 1. TTY84UG EC EC 6.4.1.2 TTY84UG PD 5KKN; 4HQ6; 3TDC; 3JRX; 3JRW TTY84UG SQ MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQRNGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGTGTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSVAGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGKRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGALNVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVARLELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIKLKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRVEHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSDELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCVVEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTRNFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVPILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQLELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGSRLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSFGNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPKDILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIGSFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFKYLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSLAYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQLGGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSRAPYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAVKDFNREKLPLMIFANWRGFSGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLKAREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVKQEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIRENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST TTY84UG TT Successful TTY84UG KE hsa00061:Fatty acid biosynthesis; hsa00620:Pyruvate metabolism; hsa00640:Propanoate metabolism; hsa01100:Metabolic pathways; hsa01212:Fatty acid metabolism; hsa04152:AMPK signaling pathway; hsa04910:Insulin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04922:Glucagon signaling pathway TTY84UG RC R-HSA-163765:ChREBP activates metabolic gene expression; R-HSA-200425:Import of palmitoyl-CoA into the mitochondrial matrix; R-HSA-2426168:Activation of gene expression by SREBF (SREBP) TTM2AOE ID TTM2AOE TTM2AOE TN Adenosine A2a receptor (ADORA2A) TTM2AOE UP P29274 TTM2AOE UC AA2AR_HUMAN TTM2AOE BC GPCR rhodopsin TTM2AOE SN Adenosine receptor A2a; ADORA2; A2a Adenosine receptor; A(2A) adenosine receptor TTM2AOE GN ADORA2A TTM2AOE FC The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Receptor for adenosine. TTM2AOE PD 6MH8; 6GDG; 6AQF; 5WF6; 5WF5 TTM2AOE SQ MPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADIAVGVLAIPFAITISTGFCAACHGCLFIACFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGTRAKGIIAICWVLSFAIGLTPMLGWNNCGQPKEGKNHSQGCGEGQVACLFEDVVPMNYMVYFNFFACVLVPLLLMLGVYLRIFLAARRQLKQMESQPLPGERARSTLQKEVHAAKSLAIIVGLFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHTNSVVNPFIYAYRIREFRQTFRKIIRSHVLRQQEPFKAAGTSARVLAAHGSDGEQVSLRLNGHPPGVWANGSAPHPERRPNGYALGLVSGGSAQESQGNTGLPDVELLSHELKGVCPEPPGLDDPLAQDGAGVS TTM2AOE TT Successful TTM2AOE FM GPCR rhodopsin TTM2AOE KE hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction; hsa05012:Parkinson's disease; hsa05034:Alcoholism TTM2AOE RC R-HSA-187024:NGF-independant TRKA activation; R-HSA-417973:Adenosine P1 receptors; R-HSA-418555:G alpha (s) signalling events; R-HSA-5683826:Surfactant metabolism TTLP57V ID TTLP57V TTLP57V TN Adenosine deaminase (ADA) TTLP57V UP P00813 TTLP57V UC ADA_HUMAN TTLP57V BC Carbon-nitrogen hydrolase TTLP57V SN Adenosine aminohydrolase; ADA1 TTLP57V GN ADA TTLP57V FC Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion. Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion. Enhances CD4+ T-cell differentiation and proliferation. Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change. Stimulates plasminogen activation. Plays a role in male fertility. Plays a protective role in early postimplantation embryonic development. Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. TTLP57V EC EC 3.5.4.4 TTLP57V PD 3IAR; 1M7M TTLP57V SQ MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDFLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAIDLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGYHTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFKSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAGQNL TTLP57V TT Successful TTLP57V FM Carbon-nitrogen hydrolase TTLP57V KE hsa00230:Purine metabolism; hsa01100:Metabolic pathways; hsa05340:Primary immunodeficiency TTLP57V RC R-HSA-74217:Purine salvage TT2CJVK ID TT2CJVK TT2CJVK TN Adrenergic receptor beta-2 (ADRB2) TT2CJVK UP P07550 TT2CJVK UC ADRB2_HUMAN TT2CJVK BC GPCR rhodopsin TT2CJVK SN Beta-2 adrenoreceptor; Beta-2 adrenoceptor; Beta-2 adrenergic receptor; B2AR; ADRB2R TT2CJVK GN ADRB2 TT2CJVK FC The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. TT2CJVK PD 6MXT; 5X7D; 5JQH; 5D6L; 5D5B TT2CJVK SQ MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL TT2CJVK TT Successful TT2CJVK FM GPCR rhodopsin TT2CJVK KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04144:Endocytosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04970:Salivary secretion TT2CJVK RC R-HSA-390696:Adrenoceptors; R-HSA-418555:G alpha (s) signalling events TT3MOS2 ID TT3MOS2 TT3MOS2 TN Aldehyde oxidase (AOX1) TT3MOS2 UP Q06278 TT3MOS2 UC AOXA_HUMAN TT3MOS2 BC Aldehyde/oxo donor oxidoreductase TT3MOS2 SN AOX1 TT3MOS2 GN AOX1 TT3MOS2 FC Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and N- methylphthalazinium, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir topenciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. TT3MOS2 EC EC 1.2.3.1 TT3MOS2 PD 6Q6Q; 5EPG; 4UHX; 4UHW TT3MOS2 SQ MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPGMVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCCLDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRKWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKLIGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPVHYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYCDDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAEKFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKYIQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGEDMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEIDQTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGSRAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETVPNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVGYFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAIDIGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSNTLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNVPI TT3MOS2 TT Successful TT3MOS2 KE hsa00280:Valine, leucine and isoleucine degradation; hsa00350:Tyrosine metabolism; hsa00380:Tryptophan metabolism; hsa00750:Vitamin B6 metabolism; hsa00760:Nicotinate and nicotinamide metabolism; hsa00830:Retinol metabolism; hsa00982:Drug metabolism - cytochrome P450; hsa01100:Metabolic pathways TTMR5UV ID TTMR5UV TTMR5UV TN Alkaline phosphatase tissue-nonspecific (ALPL) TTMR5UV UP P05186 TTMR5UV UC PPBT_HUMAN TTMR5UV BC Phosphoric monoester hydrolase TTMR5UV SN TNSALP; Liver/bone/kidney isozyme; Alkaline phosphatase, tissue-nonspecific isozyme; Alkaline phosphatase liver/bone/kidney isozyme; AP-TNAP TTMR5UV GN ALPL TTMR5UV FC This isozyme plays a key role in skeletal mineralization by regulating levels of diphosphate (PPi). TTMR5UV EC EC 3.1.3.1 TTMR5UV SQ MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF TTMR5UV TT Successful TTMR5UV FM Phosphoric monoester hydrolases TTMR5UV KE hsa00790:Folate biosynthesis; hsa01100:Metabolic pathways TTIS03D ID TTIS03D TTIS03D TN Alpha-galactosidase A (GLA) TTIS03D UP P06280 TTIS03D UC AGAL_HUMAN TTIS03D BC Glycosylase TTIS03D SN Melibiase; INN=Agalsidase; Alpha-D-galactoside galactohydrolase; Alpha-D-galactosidase A TTIS03D GN GLA TTIS03D FC A homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. Predominantly hydrolyzes ceramide trihexoside, and can catalyze the hydrolysis of melibiose into galactose and glucose. TTIS03D EC EC 3.2.1.22 TTIS03D PD 4NXS; 3TV8; 3S5Z; 3S5Y; 3LXC TTIS03D SQ MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL TTIS03D TT Successful TTIS03D KE hsa00052:Galactose metabolism; hsa00561:Glycerolipid metabolism; hsa00600:Sphingolipid metabolism; hsa00603:Glycosphingolipid biosynthesis - globo series; hsa04142:Lysosome TTIS03D RC R-HSA-1660662:Glycosphingolipid metabolism TTDM6HZ ID TTDM6HZ TTDM6HZ TN Alpha-N-acetylglucosaminidase (NAGLU) TTDM6HZ UP P54802 TTDM6HZ UC ANAG_HUMAN TTDM6HZ BC Glycosylase TTDM6HZ SN UFHSD1; NAGLU; NAG; N-acetyl-alpha-glucosaminidase; Alpha-N-acetylglucosaminidase82 kDa form; Alpha-N-acetylglucosaminidase77 kDa form TTDM6HZ GN NAGLU TTDM6HZ FC Involved in the degradation of heparan sulfate. TTDM6HZ EC EC 3.2.1.50 TTDM6HZ PD 4XWH TTDM6HZ SQ MEAVAVAAAVGVLLLAGAGGAAGDEAREAAAVRALVARLLGPGPAADFSVSVERALAAKPGLDTYSLGGGGAARVRVRGSTGVAAAAGLHRYLRDFCGCHVAWSGSQLRLPRPLPAVPGELTEATPNRYRYYQNVCTQSYSFVWWDWARWEREIDWMALNGINLALAWSGQEAIWQRVYLALGLTQAEINEFFTGPAFLAWGRMGNLHTWDGPLPPSWHIKQLYLQHRVLDQMRSFGMTPVLPAFAGHVPEAVTRVFPQVNVTKMGSWGHFNCSYSCSFLLAPEDPIFPIIGSLFLRELIKEFGTDHIYGADTFNEMQPPSSEPSYLAAATTAVYEAMTAVDTEAVWLLQGWLFQHQPQFWGPAQIRAVLGAVPRGRLLVLDLFAESQPVYTRTASFQGQPFIWCMLHNFGGNHGLFGALEAVNGGPEAARLFPNSTMVGTGMAPEGISQNEVVYSLMAELGWRKDPVPDLAAWVTSFAARRYGVSHPDAGAAWRLLLRSVYNCSGEACRGHNRSPLVRRPSLQMNTSIWYNRSDVFEAWRLLLTSAPSLATSPAFRYDLLDLTRQAVQELVSLYYEEARSAYLSKELASLLRAGGVLAYELLPALDEVLASDSRFLLGSWLEQARAAAVSEAEADFYEQNSRYQLTLWGPEGNILDYANKQLAGLVANYYTPRWRLFLEALVDSVAQGIPFQQHQFDKNVFQLEQAFVLSKQRYPSQPRGDTVDLAKKIFLKYYPRWVAGSW TTDM6HZ TT Successful TTDM6HZ KE hsa00531:Glycosaminoglycan degradation; hsa01100:Metabolic pathways; hsa04142:Lysosome TTDM6HZ RC R-HSA-2024096:HS-GAG degradation TTE4KHA ID TTE4KHA TTE4KHA TN Amyloid beta A4 protein (APP) TTE4KHA UP P05067 TTE4KHA UC A4_HUMAN TTE4KHA BC Amyloid beta-protein peptide TTE4KHA SN Protease nexin-II; PreA4; PN-II; Cerebral vascular amyloid peptide; CVAP; Amyloid-beta precursor protein; Amyloid-beta A4 protein; Alzheimer disease amyloid protein; APPI; APP; AD1; ABPP; A4 TTE4KHA GN APP TTE4KHA FC Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. TTE4KHA PD 6IYC; 6GFI; 6CO3; 5W3P; 5VZY TTE4KHA SQ MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN TTE4KHA TT Successful TTE4KHA FM Peptidase TTE4KHA KE hsa04330:Notch signaling pathway; hsa05010:Alzheimer's disease TTE4KHA RC R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-193692:Regulated proteolysis of p75NTR; R-HSA-205043:NRIF signals cell death from the nucleus; R-HSA-2122948:Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TTQVOEI ID TTQVOEI TTQVOEI TN Angiotensin II receptor type-2 (AGTR2) TTQVOEI UP P50052 TTQVOEI UC AGTR2_HUMAN TTQVOEI BC GPCR rhodopsin TTQVOEI SN Type-2 angiotensin II receptor; Angiotensin II type-2 receptor; Angiotensin II receptor 2; AT2 TTQVOEI GN AGTR2 TTQVOEI FC Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation. Receptor for angiotensin II. TTQVOEI PD 5UNH; 5UNG; 5UNF TTQVOEI SQ MKGNSTLATTSKNITSGLHFGLVNISGNNESTLNCSQKPSDKHLDAIPILYYIIFVIGFLVNIVVVTLFCCQKGPKKVSSIYIFNLAVADLLLLATLPLWATYYSYRYDWLFGPVMCKVFGSFLTLNMFASIFFITCMSVDRYQSVIYPFLSQRRNPWQASYIVPLVWCMACLSSLPTFYFRDVRTIEYLGVNACIMAFPPEKYAQWSAGIALMKNILGFIIPLIFIATCYFGIRKHLLKTNSYGKNRITRDQVLKMAAAVVLAFIICWLPFHVLTFLDALAWMGVINSCEVIAVIDLALPFAILLGFTNSCVNPFLYCFVGNRFQQKLRSVFRVPITWLQGKRESMSCRKSSSLREMETFVS TTQVOEI TT Successful TTQVOEI FM GPCR rhodopsin TTQVOEI KE hsa04080:Neuroactive ligand-receptor interaction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04614:Renin-angiotensin system TTQVOEI RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTJGNVC ID TTJGNVC TTJGNVC TN Apoptosis regulator Bcl-2 (BCL-2) TTJGNVC UP P10415 TTJGNVC UC BCL2_HUMAN TTJGNVC BC B-cell lymphoma Bcl-2 TTJGNVC SN Bcl-2 TTJGNVC GN BCL2 TTJGNVC FC Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release. Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. TTJGNVC PD 6GL8; 5VAY; 5VAX; 5VAU; 5JSN TTJGNVC SQ MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK TTJGNVC TT Successful TTJGNVC FM BCL2 family TTJGNVC KE hsa04064:NF-kappa B signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04141:Protein processing in endoplasmic reticulum; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04510:Focal adhesion; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05215:Prostate cancer; hsa05222:Small cell lung cancer TTJGNVC RC R-HSA-111447:Activation of BAD and translocation to mitochondria; R-HSA-111453:BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members; R-HSA-844455:The NLRP1 inflammasome TTJW1GN ID TTJW1GN TTJW1GN TN ATP-binding cassette transporter A1 (ABCA1) TTJW1GN UP O95477 TTJW1GN UC ABCA1_HUMAN TTJW1GN BC ABC transporter TTJW1GN SN Cholesterol mobilizing transporter ABCA1; Cholesterol efflux regulatory protein; CERP; ATP-binding cassette transporter (ABCA1) transmembrane protein; ATP-binding cassette sub-family A member 1; ATP-binding cassette 1; ABC1; ABC-1 TTJW1GN GN ABCA1 TTJW1GN FC Involved in the efflux of intracellular cholesterol and phospholipids and their transfer to apoliproteins to form nascent high density lipoproteins/HDLs. cAMP-dependent and sulfonylurea-sensitive anion transporter. TTJW1GN EC EC 7.6.2.1 TTJW1GN PD 5XJY TTJW1GN SQ MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILHKVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPILRTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGSVYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTGITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAPVPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDAIKQMKKHLKLAKDSSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFGLAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV TTJW1GN TT Successful TTJW1GN FM ABC transporter TTJW1GN KE hsa02010:ABC transporters; hsa04975:Fat digestion and absorption TTJW1GN RC R-HSA-194223:HDL-mediated lipid transport; R-HSA-1989781:PPARA activates gene expression TTP835K ID TTP835K TTP835K TN ATP-binding cassette transporter C8 (ABCC8) TTP835K UP Q09428 TTP835K UC ABCC8_HUMAN TTP835K BC ABC transporter TTP835K SN Sulfonylurea receptor 1; SUR1-type K(ATP) channel; SUR1; Kir6.2/SUR1; ATPbinding cassette subfamily C member 8; ABCC8 TTP835K GN ABCC8 TTP835K FC Putative subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive K(+) channels and insulin release. TTP835K PD 6C3P; 6C3O TTP835K SQ MPLAFCGSENHSAAYRVDQGVLNNGCFVDALNVVPHVFLLFITFPILFIGWGSQSSKVHIHHSTWLHFPGHNLRWILTFMLLFVLVCEIAEGILSDGVTESHHLHLYMPAGMAFMAAVTSVVYYHNIETSNFPKLLIALLVYWTLAFITKTIKFVKFLDHAIGFSQLRFCLTGLLVILYGMLLLVEVNVIRVRRYIFFKTPREVKPPEDLQDLGVRFLQPFVNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQVRKDIQGTQGARAIWQALSHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLGKENDVFQPKTQFLGVYFVSSQEFLANAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSAEIREEQCAPHEPTPQGPASKYQAVPLRVVNRKRPAREDCRGLTGPLQSLVPSADGDADNCCVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVTERKATEPPQGLSRAMSSRDGLLQDEEEEEEEAAESEEDDNLSSMLHQRAEIPWRACAKYLSSAGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAESYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK TTP835K TT Successful TTP835K KE hsa02010:ABC transporters; hsa04911:Insulin secretion; hsa04930:Type II diabetes mellitus TTP835K RC R-HSA-382556:ABC-family proteins mediated transport; R-HSA-422356:Regulation of insulin secretion TTIMJ02 ID TTIMJ02 TTIMJ02 TN ATP-binding cassette transporter G2 (ABCG2) TTIMJ02 UP Q9UNQ0 TTIMJ02 UC ABCG2_HUMAN TTIMJ02 BC ABC transporter TTIMJ02 SN Urate exporter; Placenta-specific ATP-binding cassette transporter; Mitoxantrone resistance-associated protein; MXR; CDw338; CD338; Breast cancer resistance protein; BCRP1; BCRP; ABCP TTIMJ02 GN ABCG2 TTIMJ02 FC Plays a role in porphyrin homeostasis as it is able to mediates the export of protoporhyrin IX (PPIX) both from mitochondria to cytosol and from cytosol to extracellular space, and cellular export of hemin, and heme. Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain. Appears to play a major role in the multidrug resistance phenotype of several cancer cell lines. Implicated in the efflux of numerous drugs and xenobiotics: mitoxantrone, the photosensitizer pheophorbide, camptothecin, methotrexate, azidothymidine (AZT), and the anthracyclines daunorubicin and doxorubicin. High-capacity urate exporter functioning in both renal and extrarenal urate excretion. TTIMJ02 PD 6HZM; 6HIJ; 6HCO; 6HBU; 6FFC TTIMJ02 SQ MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS TTIMJ02 TT Successful TTIMJ02 FM ABC transporter TT4ILYC ID TT4ILYC TT4ILYC TN Bacterial Dihydropteroate synthetase (Bact folP) TT4ILYC UP P0AC13 TT4ILYC UC DHPS_ECOLI TT4ILYC BC Alkyl aryl transferase TT4ILYC SN folP; H2Pte synthase; Dihydropteroate synthase; Dihydropteroate pyrophosphorylase; DHPS TT4ILYC GN Bact folP TT4ILYC FC Dhps catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide. TT4ILYC EC EC 2.5.1.15 TT4ILYC PD 1AJZ; 1AJ2; 1AJ0 TT4ILYC SQ MKLFAQGTSLDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKVGAHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAEVNRYFIEQIARCEQAGIAKEKLLLDPGFGFGKNLSHNYSLLARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSLACAVIAAMQGAHIIRVHDVKETVEAMRVVEATLSAKENKRYE TT4ILYC TT Successful TTVTX4N ID TTVTX4N TTVTX4N TN Bacterial Fatty acid synthetase I (Bact inhA) TTVTX4N UP P9WGR1 TTVTX4N UC INHA_MYCTU TTVTX4N BC CH-CH donor oxidoreductase TTVTX4N SN Enoyl-[acyl-carrier-protein] reductase [NADH]; Bacterial InhA TTVTX4N GN Bact inhA TTVTX4N FC Involved in the resistance against the antituberculosis drugs isoniazid and ethionamide. TTVTX4N PD 6GHN; 6GH4; 6GH1; 6GGM; 6EP8 TTVTX4N SQ MTGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTGDIIYADGGAHTQLL TTVTX4N TT Successful TTM6QSK ID TTM6QSK TTM6QSK TN B-cell receptor CD22 (CD22) TTM6QSK UP P20273 TTM6QSK UC CD22_HUMAN TTM6QSK BC Immunoglobulin TTM6QSK SN T-cell surface antigen Leu-14; Siglec-2; Sialic acid-binding Ig-like lectin 2; SIGLEC2; Leu-14; BL-CAM; B-lymphocyte cell adhesion molecule TTM6QSK GN CD22 TTM6QSK FC May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Mediates B-cell B-cell interactions. TTM6QSK PD 5VL3; 5VKM; 5VKJ TTM6QSK SQ MHLLGPWLLLLVLEYLAFSDSSKWVFEHPETLYAWEGACVWIPCTYRALDGDLESFILFHNPEYNKNTSKFDGTRLYESTKDGKVPSEQKRVQFLGDKNKNCTLSIHPVHLNDSGQLGLRMESKTEKWMERIHLNVSERPFPPHIQLPPEIQESQEVTLTCLLNFSCYGYPIQLQWLLEGVPMRQAAVTSTSLTIKSVFTRSELKFSPQWSHHGKIVTCQLQDADGKFLSNDTVQLNVKHTPKLEIKVTPSDAIVREGDSVTMTCEVSSSNPEYTTVSWLKDGTSLKKQNTFTLNLREVTKDQSGKYCCQVSNDVGPGRSEEVFLQVQYAPEPSTVQILHSPAVEGSQVEFLCMSLANPLPTNYTWYHNGKEMQGRTEEKVHIPKILPWHAGTYSCVAENILGTGQRGPGAELDVQYPPKKVTTVIQNPMPIREGDTVTLSCNYNSSNPSVTRYEWKPHGAWEEPSLGVLKIQNVGWDNTTIACAACNSWCSWASPVALNVQYAPRDVRVRKIKPLSEIHSGNSVSLQCDFSSSHPKEVQFFWEKNGRLLGKESQLNFDSISPEDAGSYSCWVNNSIGQTASKAWTLEVLYAPRRLRVSMSPGDQVMEGKSATLTCESDANPPVSHYTWFDWNNQSLPYHSQKLRLEPVKVQHSGAYWCQGTNSVGKGRSPLSTLTVYYSPETIGRRVAVGLGSCLAILILAICGLKLQRRWKRTQSQQGLQENSSGQSFFVRNKKVRRAPLSEGPHSLGCYNPMMEDGISYTTLRFPEMNIPRTGDAESSEMQRPPPDCDDTVTYSALHKRQVGDYENVIPDFPEDEGIHYSELIQFGVGERPQAQENVDYVILKH TTM6QSK TT Successful TTM6QSK FM Immunoglobulin TTM6QSK KE hsa04514:Cell adhesion molecules (CAMs); hsa04640:Hematopoietic cell lineage; hsa04662:B cell receptor signaling pathway TTM6QSK RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTWMIDN ID TTWMIDN TTWMIDN TN B-cell-activating factor (TNFSF13B) TTWMIDN UP Q9Y275 TTWMIDN UC TN13B_HUMAN TTWMIDN BC Cytokine: tumor necrosis factor TTWMIDN SN ZTNF4; UNQ401/PRO738; Tumor necrosis factor ligand superfamily member 13B; TNFSF20; TNF-and APOL-related leukocyte expressed ligand 1; TNF- and APOL-related leukocyte expressed ligand 1; TALL1; TALL-1; Dendritic cell-derived TNF-like molecule; CD257; BLyS; BAFF; B lymphocyte stimulator; B cell-activating factor TTWMIDN GN TNFSF13B TTWMIDN FC TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response. Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TTWMIDN PD 6FXN; 5Y9J; 4ZCH; 4V46; 3V56 TTWMIDN SQ MDDSTEREQSRLTSCLKKREEMKLKECVSILPRKESPSVRSSKDGKLLAATLLLALLSCCLTVVSFYQVAALQGDLASLRAELQGHHAEKLPAGAGAPKAGLEEAPAVTAGLKIFEPPAPGEGNSSQNSRNKRAVQGPEETVTQDCLQLIADSETPTIQKGSYTFVPWLLSFKRGSALEEKENKILVKETGYFFIYGQVLYTDKTYAMGHLIQRKKVHVFGDELSLVTLFRCIQNMPETLPNNSCYSAGIAKLEEGDELQLAIPRENAQISLDGDVTFFGALKLL TTWMIDN TT Successful TTWMIDN FM Cytokine: tumor necrosis factor TTWMIDN KE hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05323:Rheumatoid arthritis TTWMIDN RC R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5669034:TNFs bind their physiological receptors; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway TTKN7QR ID TTKN7QR TTKN7QR TN BDNF/NT-3 growth factors receptor (TrkB) TTKN7QR UP Q16620 TTKN7QR UC NTRK2_HUMAN TTKN7QR BC Kinase TTKN7QR SN Tropomyosin-related kinase B; TrkB tyrosine kinase; Trk-B; TRKB; Neurotrophic tyrosine kinase receptor type 2; GP145-TrkB TTKN7QR GN NTRK2 TTKN7QR FC Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia. Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. TTKN7QR EC EC 2.7.10.1 TTKN7QR PD 5MO9; 4AT5; 4AT4; 4AT3; 4ASZ TTKN7QR SQ MSSWIRWHGPAMARLWGFCWLVVGFWRAAFACPTSCKCSASRIWCSDPSPGIVAFPRLEPNSVDPENITEIFIANQKRLEIINEDDVEAYVGLRNLTIVDSGLKFVAHKAFLKNSNLQHINFTRNKLTSLSRKHFRHLDLSELILVGNPFTCSCDIMWIKTLQEAKSSPDTQDLYCLNESSKNIPLANLQIPNCGLPSANLAAPNLTVEEGKSITLSCSVAGDPVPNMYWDVGNLVSKHMNETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEKQISAHFMGWPGIDDGANPNYPDVIYEDYGTAANDIGDTTNRSNEIPSTDVTDKTGREHLSVYAVVVIASVVGFCLLVMLFLLKLARHSKFGMKGPASVISNDDDSASPLHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG TTKN7QR TT Successful TTKN7QR FM Kinase TTKN7QR KE hsa04010:MAPK signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa05034:Alcoholism TTKN7QR RC R-HSA-187024:NGF-independant TRKA activation TTW640A ID TTW640A TTW640A TN B-lymphocyte surface antigen B4 (CD19) TTW640A UP P15391 TTW640A UC CD19_HUMAN TTW640A BC Immunoglobulin TTW640A SN T-cell surface antigen Leu-12; Leu-12; Differentiation antigen CD19; B-lymphocyte antigen CD19 TTW640A GN CD19 TTW640A FC Decreases the threshold for activation of downstream signaling pathways and for triggering B-cell responses to antigens. Activates signaling pathways that lead to the activation of phosphatidylinositol 3-kinase and the mobilization of intracellular Ca(2+) stores. Is not required for early steps during B cell differentiation in the blood marrow. Required for normal differentiation of B-1 cells. Required for normal B cell differentiation and proliferation in response to antigen challenges. Required for normal levels of serum immunoglobulins, and for production of high-affinity antibodies in response to antigen challenge. Functions as coreceptor for the B-cell antigen receptor complex (BCR) on B-lymphocytes. TTW640A PD 6AL5 TTW640A SQ MPPPRLLFFLLFLTPMEVRPEEPLVVKVEEGDNAVLQCLKGTSDGPTQQLTWSRESPLKPFLKLSLGLPGLGIHMRPLAIWLFIFNVSQQMGGFYLCQPGPPSEKAWQPGWTVNVEGSGELFRWNVSDLGGLGCGLKNRSSEGPSSPSGKLMSPKLYVWAKDRPEIWEGEPPCLPPRDSLNQSLSQDLTMAPGSTLWLSCGVPPDSVSRGPLSWTHVHPKGPKSLLSLELKDDRPARDMWVMETGLLLPRATAQDAGKYYCHRGNLTMSFHLEITARPVLWHWLLRTGGWKVSAVTLAYLIFCLCSLVGILHLQRALVLRRKRKRMTDPTRRFFKVTPPPGSGPQNQYGNVLSLPTPTSGLGRAQRWAAGLGGTAPSYGNPSSDVQADGALGSRSPPGVGPEEEEGEGYEEPDSEEDSEFYENDSNLGQDQLSQDGSGYENPEDEPLGPEDEDSFSNAESYENEDEELTQPVARTMDFLSPHGSAWDPSREATSLGSQSYEDMRGILYAAPQLRSIRGQPGPNHEEDADSYENMDNPDGPDPAWGGGGRMGTWSTR TTW640A TT Successful TTW640A FM Immunoglobulin TTW640A KE hsa04151:PI3K-Akt signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04662:B cell receptor signaling pathway; hsa05169:Epstein-Barr virus infection; hsa05340:Primary immunodeficiency TTW640A RC R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTLWS2O ID TTLWS2O TTLWS2O TN Calcitonin receptor (CALCR) TTLWS2O UP P30988 TTLWS2O UC CALCR_HUMAN TTLWS2O BC GPCR secretin TTLWS2O SN CT-R TTLWS2O GN CALCR TTLWS2O FC The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The calcitonin receptor is thought to couple to the heterotrimeric guanosine triphosphate-binding protein that is sensitive to cholera toxin. This is a receptor for calcitonin. TTLWS2O PD 6NIY; 5UZ7; 5II0 TTLWS2O SQ MRFTFTSRCLALFLLLNHPTPILPAFSNQTYPTIEPKPFLYVVGRKKMMDAQYKCYDRMQQLPAYQGEGPYCNRTWDGWLCWDDTPAGVLSYQFCPDYFPDFDPSEKVTKYCDEKGVWFKHPENNRTWSNYTMCNAFTPEKLKNAYVLYYLAIVGHSLSIFTLVISLGIFVFFRSLGCQRVTLHKNMFLTYILNSMIIIIHLVEVVPNGELVRRDPVSCKILHFFHQYMMACNYFWMLCEGIYLHTLIVVAVFTEKQRLRWYYLLGWGFPLVPTTIHAITRAVYFNDNCWLSVETHLLYIIHGPVMAALVVNFFFLLNIVRVLVTKMRETHEAESHMYLKAVKATMILVPLLGIQFVVFPWRPSNKMLGKIYDYVMHSLIHFQGFFVATIYCFCNNEVQTTVKRQWAQFKIQWNQRWGRRPSNRSARAAAAAAEAGDIPIYICHQEPRNEPANNQGEESAEIIPLNIIEQESSA TTLWS2O TT Successful TTLWS2O FM GPCR secretin TTLWS2O KE hsa04080:Neuroactive ligand-receptor interaction; hsa04380:Osteoclast differentiation TTLWS2O RC R-HSA-418555:G alpha (s) signalling events; R-HSA-419812:Calcitonin-like ligand receptors TT6OEDT ID TT6OEDT TT6OEDT TN Cannabinoid receptor 1 (CB1) TT6OEDT UP P21554 TT6OEDT UC CNR1_HUMAN TT6OEDT BC GPCR rhodopsin TT6OEDT SN Cannabinoid CB1 receptor; CNR; CB-R; CANN6 TT6OEDT GN CNR1 TT6OEDT FC Mediates many cannabinoid-induced effects, acting, among others, on food intake, memory loss, gastrointestinal motility, catalepsy, ambulatory activity, anxiety, chronic pain. Signaling typically involves reduction in cyclic AMP. In the hypothalamus, may have a dual effect on mitochondrial respiration depending upon the agonist dose and possibly upon the cell type. Increases respiration at low doses, while decreases respiration at high doses. At high doses, CNR1 signal transduction involves G-protein alpha-i protein activation and subsequent inhibition of mitochondrial soluble adenylate cyclase, decrease in cyclic AMP concentration, inhibition of protein kinase A (PKA)-dependent phosphorylation of specific subunits of the mitochondrial electron transport system, including NDUFS2. In the hypothalamus, inhibits leptin-induced reactive oxygen species (ROS) formation and mediates cannabinoid-induced increase in SREBF1 and FASN gene expression. In response to cannabinoids, drives the release of orexigenic beta-endorphin, but not that of melanocyte-stimulating hormone alpha/alpha-MSH, from hypothalamic POMC neurons, hence promoting food intake. In the hippocampus, regulates cellular respiration and energy production in response to cannabinoids. Involved in cannabinoid-dependent depolarization-induced suppression of inhibition (DSI), a process in which depolarization of CA1 postsynaptic pyramidal neurons mobilizes eCBs, which retrogradely activate presynaptic CB1 receptors, transiently decreasing GABAergic inhibitory neurotransmission. Also reduces excitatory synaptic transmission. In superior cervical ganglions and cerebral vascular smooth muscle cells, inhibits voltage-gated Ca(2+) channels in a constitutive, as well as agonist-dependent manner. In cerebral vascular smooth muscle cells, cannabinoid-induced inhibition of voltage-gated Ca(2+) channels leads to vasodilation and decreased vascular tone. Induces leptin production in adipocytes and reduces LRP2-mediated leptin clearance in the kidney, hence participating in hyperleptinemia. In adipose tissue, CNR1 signaling leads to increased expression of SREBF1, ACACA and FASN genes. In the liver, activation by endocannabinoids leads to increased de novo lipogenesis and reduced fatty acid catabolism, associated with increased expression of SREBF1/SREBP-1, GCK, ACACA, ACACB and FASN genes. May also affect de novo cholesterol synthesis and HDL-cholesteryl ether uptake. Peripherally modulates energy metabolism. In high carbohydrate diet-induced obesity, may decrease the expression of mitochondrial dihydrolipoyl dehydrogenase/DLD in striated muscles, as well as that of selected glucose/ pyruvate metabolic enzymes, hence affecting energy expenditure through mitochondrial metabolism. In response to cannabinoid anandamide, elicits a proinflammatory response in macrophages, which involves NLRP3 inflammasome activation and IL1B and IL18 secretion. In macrophages infiltrating pancreatic islets, this process may participate in the progression of type-2 diabetes and associated loss of pancreatic beta-cells. G-protein coupled receptor for endogenous cannabinoids (eCBs), including N-arachidonoylethanolamide (also called anandamide or AEA) and 2-arachidonoylglycerol (2-AG), as well as phytocannabinoids, such as delta(9)-tetrahydrocannabinol (THC). TT6OEDT PD 6N4B; 5XRA; 5XR8; 5U09; 5TGZ TT6OEDT SQ MKSILDGLADTTFRTITTDLLYVGSNDIQYEDIKGDMASKLGYFPQKFPLTSFRGSPFQEKMTAGDNPQLVPADQVNITEFYNKSLSSFKENEENIQCGENFMDIECFMVLNPSQQLAIAVLSLTLGTFTVLENLLVLCVILHSRSLRCRPSYHFIGSLAVADLLGSVIFVYSFIDFHVFHRKDSRNVFLFKLGGVTASFTASVGSLFLTAIDRYISIHRPLAYKRIVTRPKAVVAFCLMWTIAIVIAVLPLLGWNCEKLQSVCSDIFPHIDETYLMFWIGVTSVLLLFIVYAYMYILWKAHSHAVRMIQRGTQKSIIIHTSEDGKVQVTRPDQARMDIRLAKTLVLILVVLIICWGPLLAIMVYDVFGKMNKLIKTVFAFCSMLCLLNSTVNPIIYALRSKDLRHAFRSMFPSCEGTAQPLDNSMGDSDCLHKHANNAASVHRAAESCIKSTVKIAKVTMSVSTDTSAEAL TT6OEDT TT Successful TT6OEDT FM GPCR rhodopsin TT6OEDT KE hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling TT6OEDT RC R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events TTSYVO6 ID TTSYVO6 TTSYVO6 TN Cholesterol desmolase (CYP11A1) TTSYVO6 UP P05108 TTSYVO6 UC CP11A_HUMAN TTSYVO6 BC Paired donor oxygen oxidoreductase TTSYVO6 SN P450(scc); Cytochrome P450(scc); Cytochrome P450 11A1; Cholesterol side-chain cleavage enzyme, mitochondrial; CYPXIA1; CYP11A TTSYVO6 GN CYP11A1 TTSYVO6 FC Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone, the precursor of most steroid hormones. TTSYVO6 EC EC 1.14.15.6 TTSYVO6 PD 3NA1; 3NA0; 3N9Z; 3N9Y TTSYVO6 SQ MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWLNLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPERFLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVSVLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQMFHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRGILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAARHQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIYALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINMLENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ TTSYVO6 TT Successful TTSYVO6 FM Paired donor oxidoreductase TTSYVO6 KE hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways; hsa04913:Ovarian steroidogenesis TTSYVO6 RC R-HSA-211976:Endogenous sterols TTEB0GD ID TTEB0GD TTEB0GD TN Cholinesterase (BCHE) TTEB0GD UP P06276 TTEB0GD UC CHLE_HUMAN TTEB0GD BC Type-B carboxylesterase/lipase TTEB0GD SN Pseudocholinesterase; Choline esterase II; CHE1; Butyrylcholine esterase; Acylcholine acylhydrolase TTEB0GD GN BCHE TTEB0GD FC Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. TTEB0GD EC EC 3.1.1.8 TTEB0GD PD 6QAE; 6QAD; 6QAC; 6QAB; 6QAA TTEB0GD SQ MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCVGL TTEB0GD TT Successful TT7EFHR ID TT7EFHR TT7EFHR TN Corticotropin-releasing factor receptor 1 (CRHR1) TT7EFHR UP P34998 TT7EFHR UC CRFR1_HUMAN TT7EFHR BC GPCR secretin TT7EFHR SN Corticotropin-releasing hormone type 1 receptor; Corticotropin-releasing hormone receptor 1; CRHR1; CRH-R 1; CRF1; CRF-R1; CRF-R; CRF-1 receptor; CRF receptor TT7EFHR GN CRHR1 TT7EFHR FC G-protein coupled receptor for CRH (corticotropin- releasing factor) and UCN (urocortin). Has high affinity for CRH and UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels. Inhibits the activity of the calcium channel CACNA1H. Required for normal embryonic development of the adrenal gland and for normal hormonal responses to stress. Plays a role in the response to anxiogenic stimuli. TT7EFHR PD 4Z9G; 4K5Y; 3EHU; 3EHT; 3EHS TT7EFHR SQ MGGHPQLRLVKALLLLGLNPVSASLQDQHCESLSLASNISGLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVRYNTTNNGYRECLANGSWAARVNYSECQEILNEEKKSKVHYHVAVIINYLGHCISLVALLVAFVLFLRLRPGCTHWGDQADGALEVGAPWSGAPFQVRRSIRCLRNIIHWNLISAFILRNATWFVVQLTMSPEVHQSNVGWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTYSTDRLRKWMFICIGWGVPFPIIVAWAIGKLYYDNEKCWFGKRPGVYTDYIYQGPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDEVSRVVFIYFNSFLESFQGFFVSVFYCFLNSEVRSAIRKRWHRWQDKHSIRARVARAMSIPTSPTRVSFHSIKQSTAV TT7EFHR TT Successful TT7EFHR KE hsa04080:Neuroactive ligand-receptor interaction; hsa04730:Long-term depression TT7EFHR RC R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-418555:G alpha (s) signalling events TTMWT8Z ID TTMWT8Z TTMWT8Z TN C-X-C chemokine receptor type 1 (CXCR1) TTMWT8Z UP P25024 TTMWT8Z UC CXCR1_HUMAN TTMWT8Z BC GPCR rhodopsin TTMWT8Z SN Interleukin-8 receptor A; IL8RA; IL-8R A; IL-8 receptor type 1; High affinity interleukin-8 receptor A; CXCR-1; CXC-R1; CMKAR1; CDw128a; CD181 TTMWT8Z GN CXCR1 TTMWT8Z FC Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activate a phosphatidylinositol-calcium second messenger system. This receptor binds to IL-8 with a high affinity and to MGSA (GRO) with a low affinity. Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor. TTMWT8Z PD 2LNL; 1ILQ; 1ILP TTMWT8Z SQ MSNITDPQMWDFDDLNFTGMPPADEDYSPCMLETETLNKYVVIIAYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMNLSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNIGRALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL TTMWT8Z TT Successful TTMWT8Z KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa05120:Epithelial cell signaling in Helicobacter pylori infection TTMWT8Z RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TT30C9G ID TT30C9G TT30C9G TN C-X-C chemokine receptor type 2 (CXCR2) TT30C9G UP P25025 TT30C9G UC CXCR2_HUMAN TT30C9G BC GPCR rhodopsin TT30C9G SN Interleukin-8 receptor B; IL8RB; IL-8R B; IL-8 receptor type 2; High affinity interleukin-8 receptor B; GRO/MGSA receptor; CXCR-2; CXC-R2; CDw128b; CD182 TT30C9G GN CXCR2 TT30C9G FC Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Binds to IL-8 with high affinity. Also binds with high affinity to CXCL3, GRO/MGSA and NAP-2. Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor. TT30C9G PD 5TYT; 4Q3H TT30C9G SQ MEDFNMESDSFEDFWKGEDLSNYSYSSTLPPFLLDAAPCEPESLEINKYFVVIIYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRYLVKFICLSIWGLSLLLALPVLLFRRTVYSSNVSPACYEDMGNNTANWRMLLRILPQSFGFIVPLLIMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQETCERRNHIDRALDATEILGILHSCLNPLIYAFIGQKFRHGLLKILAIHGLISKDSLPKDSRPSFVGSSSGHTSTTL TT30C9G TT Successful TT30C9G FM GPCR rhodopsin TT30C9G KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa05120:Epithelial cell signaling in Helicobacter pylori infection TT30C9G RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTBID49 ID TTBID49 TTBID49 TN C-X-C chemokine receptor type 4 (CXCR4) TTBID49 UP P61073 TTBID49 UC CXCR4_HUMAN TTBID49 BC GPCR rhodopsin TTBID49 SN Stromal cell-derived factor 1 receptor; SDF-1 receptor; NPYRL; Lipopolysaccharide-associated protein 3; Leukocyte-derived seven transmembrane domain receptor; LPS-associated protein 3; LESTR; LCR1; LAP-3; HM89; Fusin; FB22; Chemokine receptor CXCR4; CXCR-4; CXC-R4; CD184 antigen; CD184 TTBID49 GN CXCR4 TTBID49 FC Involved in the AKT signaling cascade. Plays a role in regulation of cell migration, e. g. during wound healing. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival. Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation. TTBID49 PD 4RWS; 3OE9; 3OE8; 3OE6; 3OE0 TTBID49 SQ MEGISIYTSDNYTEEMGSGDYDSMKEPCFREENANFNKIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWIPALLLTIPDFIFANVSEADDRYICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSVSRGSSLKILSKGKRGGHSSVSTESESSSFHSS TTBID49 TT Successful TTBID49 FM GPCR rhodopsin TTBID49 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa04360:Axon guidance; hsa04670:Leukocyte transendothelial migration; hsa04672:Intestinal immune network for IgA production; hsa05200:Pathways in cancer TTBID49 RC R-HSA-173107:Binding and entry of HIV virion; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTPURFN ID TTPURFN TTPURFN TN Cyclic ADP-ribose hydrolase 1 (CD38) TTPURFN UP P28907 TTPURFN UC CD38_HUMAN TTPURFN BC Glycosylase TTPURFN SN cADPr hydrolase 1; T10; Cyclic ADPribose hydrolase 1; ADPribosyl cyclase 1; ADPRC 1; ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1; ADP-ribosyl cyclase 1; 2'-phospho-cyclic-ADP-ribose transferase; 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase; 2'-phospho-ADP-ribosyl cyclase TTPURFN GN CD38 TTPURFN FC Has cADPr hydrolase activity. Also moonlights as a receptor in cells of the immune system. Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. TTPURFN EC EC 3.2.2.6 TTPURFN PD 6EDR; 5F21; 5F1O; 5F1K; 4XJT TTPURFN SQ MANCEFSPVSGDKPCCRLSRRAQLCLGVSILVLILVVVLAVVVPRWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI TTPURFN TT Successful TTPURFN FM Glycosylase TTPURFN KE hsa00760:Nicotinate and nicotinamide metabolism; hsa01100:Metabolic pathways; hsa04020:Calcium signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04921:Oxytocin signaling pathway; hsa04970:Salivary secretion; hsa04972:Pancreatic secretion; hsa05169:Epstein-Barr virus infection TTI2S1D ID TTI2S1D TTI2S1D TN Cytotoxic T-lymphocyte protein 4 (CTLA-4) TTI2S1D UP P16410 TTI2S1D UC CTLA4_HUMAN TTI2S1D BC Immunoglobulin TTI2S1D SN Cytotoxic T-lymphocyte-associated antigen 4; CTLA-4; CD152 TTI2S1D GN CTLA4 TTI2S1D FC Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28. TTI2S1D PD 5XJ3; 5TRU; 5GGV; 3OSK; 3BX7 TTI2S1D SQ MACLGFQRHKAQLNLATRTWPCTLLFFLLFIPVFCKAMHVAQPAVVLASSRGIASFVCEYASPGKATEVRVTVLRQADSQVTEVCAATYMMGNELTFLDDSICTGTSSGNQVNLTIQGLRAMDTGLYICKVELMYPPPYYLGIGNGTQIYVIDPEPCPDSDFLLWILAAVSSGLFFYSFLLTAVSLSKMLKKRSPLTTGVYVKMPPTEPECEKQFQPYFIPIN TTI2S1D TT Successful TTI2S1D FM Immunoglobulin TTI2S1D KE hsa04514:Cell adhesion molecules (CAMs); hsa04660:T cell receptor signaling pathway; hsa05320:Autoimmune thyroid disease; hsa05323:Rheumatoid arthritis TTI2S1D RC R-HSA-389513:CTLA4 inhibitory signaling TTVG215 ID TTVG215 TTVG215 TN Debrisoquine 4-hydroxylase (CYP2D6) TTVG215 UP P10635 TTVG215 UC CP2D6_HUMAN TTVG215 BC Paired donor oxygen oxidoreductase TTVG215 SN P450-DB1; Cytochrome P450-DB1; Cytochrome P450 2D6; CYPIID6; CYP2DL1 TTVG215 GN CYP2D6 TTVG215 FC It is involved in the metabolism of drugs such as antiarrhythmics, adrenoceptor antagonists, and tricyclic antidepressants. Responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. TTVG215 EC EC 1.14.14.- TTVG215 PD 6CSD; 6CSB; 5TFU; 5TFT; 4XRZ TTVG215 SQ MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGVFAFLVSPSPYELCAVPR TTVG215 TT Successful TTVG215 FM Oxidoreductases acting on paired donors TTVG215 KE hsa00980:Metabolism of xenobiotics by cytochrome P450; hsa00982:Drug metabolism - cytochrome P450; hsa04726:Serotonergic synapse TTVG215 RC R-HSA-211981:Xenobiotics TTYUENF ID TTYUENF TTYUENF TN Dehydropeptidase I (DPEP1) TTYUENF UP P16444 TTYUENF UC DPEP1_HUMAN TTYUENF BC Peptidase TTYUENF SN hRDP; Renal dipeptidase; RDP; Microsomal dipeptidase; MDP; Dipeptidase 1; Dehydropeptidase-I TTYUENF GN DPEP1 TTYUENF FC Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity. Hydrolyzes a wide range of dipeptides. TTYUENF EC EC 3.4.13.19 TTYUENF PD 1ITU; 1ITQ TTYUENF SQ MWSGWWLWPLVAVCTADFFRDEAERIMRDSPVIDGHNDLPWQLLDMFNNRLQDERANLTTLAGTHTNIPKLRAGFVGGQFWSVYTPCDTQNKDAVRRTLEQMDVVHRMCRMYPETFLYVTSSAGIRQAFREGKVASLIGVEGGHSIDSSLGVLRALYQLGMRYLTLTHSCNTPWADNWLVDTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVSVATMKATLQLSRAPVIFSHSSAYSVCASRRNVPDDVLRLVKQTDSLVMVNFYNNYISCTNKANLSQVADHLDHIKEVAGARAVGFGGDFDGVPRVPEGLEDVSKYPDLIAELLRRNWTEAEVKGALADNLLRVFEAVEQASNLTQAPEEEPIPLDQLGGSCRTHYGYSSGASSLHRHWGLLLASLAPLVLCLSLL TTYUENF TT Successful TTYUENF FM Peptidase TTYUENF RC R-HSA-5423646:Aflatoxin activation and detoxification TTYZVDJ ID TTYZVDJ TTYZVDJ TN Dihydrofolate reductase (DHFR) TTYZVDJ UP P00374 TTYZVDJ UC DYR_HUMAN TTYZVDJ BC CH-NH donor oxidoreductase TTYZVDJ SN DYR; DHFRP1 TTYZVDJ GN DHFR TTYZVDJ FC Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2. Key enzyme in folate metabolism. TTYZVDJ EC EC 1.5.1.3 TTYZVDJ PD 6DE4; 6DAV; 6A7E; 6A7C; 5HVE TTYZVDJ SQ MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND TTYZVDJ TT Successful TTYZVDJ FM Oxidoreductases acting on CH-NH group of donors TTYZVDJ KE hsa00670:One carbon pool by folate; hsa00790:Folate biosynthesis; hsa01100:Metabolic pathways TTYZVDJ RC R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-1474151:Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation; R-HSA-196757:Metabolism of folate and pterines; R-HSA-69205:G1/S-Specific Transcription TTGTQHC ID TTGTQHC TTGTQHC TN DNA topoisomerase I (TOP1) TTGTQHC UP P11387 TTGTQHC UC TOP1_HUMAN TTGTQHC BC Topoisomerase TTGTQHC SN DNA topoisomerase I TTGTQHC GN TOP1 TTGTQHC FC Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component ARNTL/BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the ARNTL/BMAL1 promoter. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. TTGTQHC EC EC 5.6.2.2 TTGTQHC PD 1TL8; 1T8I; 1SEU; 1SC7; 1RRJ TTGTQHC SQ MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF TTGTQHC TT Successful TTGTQHC FM DNA topoisomerase TT4NVEM ID TT4NVEM TT4NVEM TN DNA topoisomerase II beta (TOP2B) TT4NVEM UP Q02880 TT4NVEM UC TOP2B_HUMAN TT4NVEM BC ATP-hydrolyzing DNA topoisomerase TT4NVEM SN Topo IIbeta; TOP2beta; TOP2B TT4NVEM GN TOP2B TT4NVEM FC Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. TT4NVEM EC EC 5.6.2.3 TT4NVEM PD 5ZRF; 5ZQF; 5ZEN; 5ZAD; 5GWJ TT4NVEM SQ MAKSGGCGAGAGVGGGNGALTWVTLFDQNNAAKKEESETANKNDSSKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQFMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLSKFKMEKLDKDIVALMTRRAYDLAGSCRGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSTLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEDETQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDAKGREVNDLKRKSPSDLWKEDLAAFVEELDKVESQEREDVLAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIIPEITAMKADASKKLLKKKKGDLDTAAVKVEFDEEFSGAPVEGAGEEALTPSVPINKGPKPKREKKEPGTRVRKTPTSSGKPSAKKVKKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDADDDDDDNNDLEELKVKASPITNDGEDEFVPSDGLDKDEYTFSPGKSKATPEKSLHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDSASVFSPSFGLKQTDKVPSKTVAAKKGKPSSDTVPKPKRAPKQKKVVEAVNSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKTSKTTSKKPKKTSFDQDSDVDIFPSDFPTEPPSLPRTGRARKEVKYFAESDEEEDDVDFAMFN TT4NVEM TT Successful TTZFYLI ID TTZFYLI TTZFYLI TN Dopamine D1 receptor (D1R) TTZFYLI UP P21728 TTZFYLI UC DRD1_HUMAN TTZFYLI BC GPCR rhodopsin TTZFYLI SN D(1A) dopamine receptor TTZFYLI GN DRD1 TTZFYLI FC Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase. TTZFYLI PD 1OZ5 TTZFYLI SQ MRTLNTSAMDGTGLVVERDFSVRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTSPSDGNATSLAETIDNCDSSLSRTYAISSSVISFYIPVAIMIVTYTRIYRIAQKQIRRIAALERAAVHAKNCQTTTGNGKPVECSQPESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFILNCILPFCGSGETQPFCIDSNTFDVFVWFGWANSSLNPIIYAFNADFRKAFSTLLGCYRLCPATNNAIETVSINNNGAAMFSSHHEPRGSISKECNLVYLIPHAVGSSEDLKKEEAAGIARPLEKLSPALSVILDYDTDVSLEKIQPITQNGQHPT TTZFYLI TT Successful TTZFYLI FM GPCR rhodopsin TTZFYLI KE hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04728:Dopaminergic synapse; hsa05012:Parkinson's disease; hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05032:Morphine addiction; hsa05034:Alcoholism TTZFYLI RC R-HSA-390651:Dopamine receptors; R-HSA-418555:G alpha (s) signalling events TTEX248 ID TTEX248 TTEX248 TN Dopamine D2 receptor (D2R) TTEX248 UP P14416 TTEX248 UC DRD2_HUMAN TTEX248 BC GPCR rhodopsin TTEX248 SN Dopamine receptor 2; D(2) dopamine receptor TTEX248 GN DRD2 TTEX248 FC Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. TTEX248 PD 6CM4; 5AER; 1I15 TTEX248 SQ MDPLNLSWYDDDLERQNWSRPFNGSDGKADRPHYNYYATLLTLLIAVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISIVWVLSFTISCPLLFGLNNADQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRRRRKRVNTKRSSRAFRAHLRAPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARRAQELEMEMLSSTSPPERTRYSPIPPSHHQLTLPDPSHHGLHSTPDSPAKPEKNGHAKDHPKIAKIFEIQTMPNGKTRTSLKTMSRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFLKILHC TTEX248 TT Successful TTEX248 FM GPCR rhodopsin TTEX248 KE hsa04015:Rap1 signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04728:Dopaminergic synapse; hsa05012:Parkinson's disease; hsa05030:Cocaine addiction; hsa05034:Alcoholism TTEX248 RC R-HSA-390651:Dopamine receptors; R-HSA-418594:G alpha (i) signalling events TT4C8EA ID TT4C8EA TT4C8EA TN Dopamine D3 receptor (D3R) TT4C8EA UP P35462 TT4C8EA UC DRD3_HUMAN TT4C8EA BC GPCR rhodopsin TT4C8EA SN D(3) dopamine receptor TT4C8EA GN DRD3 TT4C8EA FC Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation. TT4C8EA PD 3PBL TT4C8EA SQ MASLSQLSSHLNYTCGAENSTGASQARPHAYYALSYCALILAIVFGNGLVCMAVLKERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPTVCSISNPDFVIYSSVVSFYLPFGVTVLVYARIYVVLKQRRRKRILTRQNSQCNSVRPGFPQQTLSPDPAHLELKRYYSICQDTALGGPGFQERGGELKREEKTRNSLSPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGVPLREKKATQMVAIVLGAFIVCWLPFFLTHVLNTHCQTCHVSPELYSATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC TT4C8EA TT Successful TT4C8EA FM GPCR rhodopsin TT4C8EA KE hsa04080:Neuroactive ligand-receptor interaction; hsa04728:Dopaminergic synapse TT4C8EA RC R-HSA-390651:Dopamine receptors; R-HSA-418594:G alpha (i) signalling events TTE0A2F ID TTE0A2F TTE0A2F TN Dopamine D4 receptor (D4R) TTE0A2F UP P21917 TTE0A2F UC DRD4_HUMAN TTE0A2F BC GPCR rhodopsin TTE0A2F SN DRD4; D(2C)D(4) dopamine receptor dopamine receptor TTE0A2F GN DRD4 TTE0A2F FC Dopamine receptor responsible for neuronal signaling in the mesolimbic system of the brain, an area of the brain that regulates emotion and complex behavior. Its activity is mediated by G proteins which inhibit adenylyl cyclase. Modulates the circadian rhythm of contrast sensitivity by regulating the rhythmic expression of NPAS2 in the retinal ganglion cells. TTE0A2F PD 5WIV; 5WIU TTE0A2F SQ MGNRSTADADGLLAGRGPAAGASAGASAGLAGQGAAALVGGVLLIGAVLAGNSLVCVSVATERALQTPTNSFIVSLAAADLLLALLVLPLFVYSEVQGGAWLLSPRLCDALMAMDVMLCTASIFNLCAISVDRFVAVAVPLRYNRQGGSRRQLLLIGATWLLSAAVAAPVLCGLNDVRGRDPAVCRLEDRDYVVYSSVCSFFLPCPLMLLLYWATFRGLQRWEVARRAKLHGRAPRRPSGPGPPSPTPPAPRLPQDPCGPDCAPPAPGLPRGPCGPDCAPAAPSLPQDPCGPDCAPPAPGLPPDPCGSNCAPPDAVRAAALPPQTPPQTRRRRRAKITGRERKAMRVLPVVVGAFLLCWTPFFVVHITQALCPACSVPPRLVSAVTWLGYVNSALNPVIYTVFNAEFRNVFRKALRACC TTE0A2F TT Successful TTE0A2F KE hsa04080:Neuroactive ligand-receptor interaction; hsa04728:Dopaminergic synapse TTE0A2F RC R-HSA-390651:Dopamine receptors; R-HSA-418594:G alpha (i) signalling events TTAUX24 ID TTAUX24 TTAUX24 TN Erythropoietin Receptor (EPOR) TTAUX24 UP P19235 TTAUX24 UC EPOR_HUMAN TTAUX24 BC Cytokine receptor TTAUX24 SN Full-length form; EPO-R TTAUX24 GN EPOR TTAUX24 FC Mediates erythropoietin-induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade. In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase. Receptor for erythropoietin. TTAUX24 PD 6E2Q; 4Y5Y; 4Y5X; 4Y5V; 2MV6 TTAUX24 SQ MDHLGASLWPQVGSLCLLLAGAAWAPPPNLPDPKFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGNYSFSYQLEDEPWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLDAPVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGNGAGSVQRVEILEGRTECVLSNLRGRTRYTFAVRARMAEPSFGGFWSAWSEPVSLLTPSDLDPLILTLSLILVVILVLLTVLALLSHRRALKQKIWPGIPSPESEFEGLFTTHKGNFQLWLYQNDGCLWWSPCTPFTEDPPASLEVLSERCWGTMQAVEPGTDDEGPLLEPVGSEHAQDTYLVLDKWLLPRNPPSEDLPGPGGSVDIVAMDEGSEASSCSSALASKPSPEGASAASFEYTILDPSSQLLRPWTLCPELPPTPPHLKYLYLVVSDSGISTDYSSGDSQGAQGGLSDGPYSNPYENSLIPAAEPLPPSYVACS TTAUX24 TT Successful TTAUX24 FM Type I cytokine receptor TTAUX24 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage TTPNQAC ID TTPNQAC TTPNQAC TN Estrogen-related receptor-alpha (ESRRA) TTPNQAC UP P11474 TTPNQAC UC ERR1_HUMAN TTPNQAC BC Nuclear hormone receptor TTPNQAC SN Nuclear receptor subfamily 3 group B member 1; NR3B1; Estrogen-relatedreceptor, alpha; Estrogen-relatedreceptor alpha; Estrogen-related receptor alpha; Estrogen receptor-like 1; ESRL1; ERRalpha; ERR1; ERR-alpha TTPNQAC GN ESRRA TTPNQAC FC Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism. Induces the expression of PERM1 in the skeletal muscle. Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. TTPNQAC PD 3K6P; 3D24; 2PJL; 1XB7 TTPNQAC SQ MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVALAPGPAPTRCLPGHKEEEDGEGAGPGEQGGGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAAPVNALVSHLLVVEPEKLYAMPDPAGPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD TTPNQAC TT Successful TTPNQAC FM Nuclear hormone receptor TTPNQAC RC R-HSA-1989781:PPARA activates gene expression; R-HSA-2151201:Transcriptional activation of mitochondrial biogenesis; R-HSA-383280:Nuclear Receptor transcription pathway TTBUYHA ID TTBUYHA TTBUYHA TN Extracellular calcium-sensing receptor (CASR) TTBUYHA UP P41180 TTBUYHA UC CASR_HUMAN TTBUYHA BC GPCR glutamate TTBUYHA SN hCasR; Parathyroid cell calciumreceptor; Parathyroid cell calcium-sensing receptor 1; Parathyroid calcium receptor; Parathyroid Cell calcium-sensing receptor; PCaR1; GPRC2A; CaSR TTBUYHA GN CASR TTBUYHA FC Senses fluctuations in the circulating calcium concentration and modulates the production of parathyroid hormone (PTH) in parathyroid glands. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. The G-protein-coupled receptor activity is activated by a co-agonist mechanism: aromatic amino acids, such as Trp or Phe, act concertedly with divalent cations, such as calcium or magnesium, to achieve full receptor activation. G-protein-coupled receptor that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis. TTBUYHA PD 5K5T; 5K5S; 5FBK; 5FBH TTBUYHA SQ MAFYSCCWVLLALTWHTSAYGPDQRAQKKGDIILGGLFPIHFGVAAKDQDLKSRPESVECIRYNFRGFRWLQAMIFAIEEINSSPALLPNLTLGYRIFDTCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSEHIPSTIAVVGATGSGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQFKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKFREEAEERDICIDFSELISQYSDEEEIQHVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGKIWLASEAWASSSLIAMPQYFHVVGGTIGFALKAGQIPGFREFLKKVHPRKSVHNGFAKEFWEETFNCHLQEGAKGPLPVDTFLRGHEESGDRFSNSSTAFRPLCTGDENISSVETPYIDYTHLRISYNVYLAVYSIAHALQDIYTCLPGRGLFTNGSCADIKKVEAWQVLKHLRHLNFTNNMGEQVTFDECGDLVGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINEEKILWSGFSREVPFSNCSRDCLAGTRKGIIEGEPTCCFECVECPDGEYSDETDASACNKCPDDFWSNENHTSCIAKEIEFLSWTEPFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLLCCFSSSLFFIGEPQDWTCRLRQPAFGISFVLCISCILVKTNRVLLVFEAKIPTSFHRKWWGLNLQFLLVFLCTFMQIVICVIWLYTAPPSSYRNQELEDEIIFITCHEGSLMALGFLIGYTCLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWISFIPAYASTYGKFVSAVEVIAILAASFGLLACIFFNKIYIILFKPSRNTIEEVRCSTAAHAFKVAARATLRRSNVSRKRSSSLGGSTGSTPSSSISSKSNSEDPFPQPERQKQQQPLALTQQEQQQQPLTLPQQQRSQQQPRCKQKVIFGSGTVTFSLSFDEPQKNAMAHRNSTHQNSLEAQKSSDTLTRHEPLLPLQCGETDLDLTVQETGLQGPVGGDQRPEVEDPEELSPALVVSSSQSFVISGGGSTVTENVVNS TTBUYHA TT Successful TTBUYHA FM GPCR glutamate TTBUYHA RC R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors) TTS4UGC ID TTS4UGC TTS4UGC TN Farnesoid X-activated receptor (FXR) TTS4UGC UP Q96RI1 TTS4UGC UC NR1H4_HUMAN TTS4UGC BC Nuclear hormone receptor TTS4UGC SN Retinoid X receptor-interacting protein 14; RXR-interacting protein 14; RIP14; Nuclear receptor subfamily 1 group H member 4; HRR1; Farnesol receptor HRR-1; FXR; Bile acid receptor; BAR TTS4UGC GN NR1H4 TTS4UGC FC Ligand-activated transcription factor. Receptor for bile acids (BAs) such as chenodeoxycholic acid (CDCA), lithocholic acid, deoxycholic acid (DCA) and allocholic acid (ACA). Plays a essential role in BA homeostasis through the regulation of genes involved in BA synthesis, conjugation and enterohepatic circulation. Also regulates lipid and glucose homeostasis and is involved innate immune response. The FXR-RXR heterodimer binds predominantly to farnesoid X receptor response elements (FXREs) containing two inverted repeats of the consensus sequence 5'-AGGTCA-3' in which the monomers are spaced by 1 nucleotide (IR-1) but also to tandem repeat DR1 sites with lower affinity, and can be activated by either FXR or RXR-specific ligands. It is proposed that monomeric nuclear receptors such as NR5A2/LRH-1 bound to coregulatory nuclear responsive element (NRE) halfsites located in close proximity to FXREs modulate transcriptional activity (By similarity). In the liver activates transcription of the corepressor NR0B2 thereby indirectly inhibiting CYP7A1 and CYP8B1 (involved in BA synthesis) implicating at least in part histone demethylase KDM1A resulting in epigenomic repression, and SLC10A1/NTCP (involved in hepatic uptake of conjugated BAs). Activates transcription of the repressor MAFG (involved in regulation of BA synthesis) (By similarity). Activates transcription of SLC27A5/BACS and BAAT (involved in BA conjugation), ABCB11/BSEP (involved in bile salt export) by directly recruiting histone methyltransferase CARM1, and ABCC2/MRP2 (involved in secretion of conjugated BAs) and ABCB4 (involved in secretion of phosphatidylcholine in the small intestine). Activates transcription of SLC27A5/BACS and BAAT (involved in BA conjugation), ABCB11/BSEP (involved in bile salt export) by directly recruiting histone methyltransferase CARM1, and ABCC2/MRP2 (involved in secretion of conjugated BAs) and ABCB4 (involved in secretion of phosphatidylcholine in the small intestine). In the intestine activates FGF19 expression and secretion leading to hepatic CYP7A1 repression. The function also involves the coordinated induction of hepatic KLB/beta-klotho expression (By similarity). Regulates transcription of liver UGT2B4 and SULT2A1 involved in BA detoxification; binding to the UGT2B4 promoter seems to imply a monomeric transactivation independent of RXRA. Modulates lipid homeostasis by activating liver NR0B2/SHP-mediated repression of SREBF1 (involved in de novo lipogenesis), expression of PLTP (involved in HDL formation), SCARB1 (involved in HDL hepatic uptake), APOE, APOC1, APOC4, PPARA (involved in beta-oxidation of fatty acids), VLDLR and SDC1 (involved in the hepatic uptake of LDL and IDL remnants), and inhibiting expression of MTTP (involved in VLDL assembly. Increases expression of APOC2 (promoting lipoprotein lipase activity implicated in triglyceride clearance). Transrepresses APOA1 involving a monomeric competition with NR2A1 for binding to a DR1 element. Also reduces triglyceride clearance by inhibiting expression of ANGPTL3 and APOC3 (both involved in inhibition of lipoprotein lipase). Involved in glucose homeostasis by modulating hepatic gluconeogenesis through activation of NR0B2/SHP-mediated repression of respective genes. Modulates glycogen synthesis (inducing phosphorylation of glycogen synthase kinase-3) (By similarity). Modulates glucose-stimulated insulin secretion and is involved in insulin resistance. Involved in intestinal innate immunity. Plays a role in protecting the distal small intestine against bacterial overgrowth and preservation of the epithelial barrier (By similarity). Down-regulates inflammatory cytokine expression in several types of immune cells including macrophages and mononuclear cells. Mediates trans-repression of TLR4-induced cytokine expression; the function seems to require its sumoylation and prevents N-CoR nuclear receptor corepressor clearance from target genes such as IL1B and NOS2. Involved in the TLR9-mediated protective mechanism in intestinal inflammation. Plays an anti-inflammatory role in liver inflammation; proposed to inhibit proinflammatory (but not antiapoptotic) NF-kappa-B signaling) (By similarity). TTS4UGC PD 6A60; 6A5Z; 6A5Y; 6A5X; 6A5W TTS4UGC SQ MVMQFQGLENPIQISPHCSCTPSGFFMEMMSMKPAKGVLTEQVAGPLGQNLEVEPYSQYSNVQFPQVQPQISSSSYYSNLGFYPQQPEEWYSPGIYELRRMPAETLYQGETEVAEMPVTKKPRMGASAGRIKGDELCVVCGDRASGYHYNALTCEGCKGFFRRSITKNAVYKCKNGGNCVMDMYMRRKCQECRLRKCKEMGMLAECMYTGLLTEIQCKSKRLRKNVKQHADQTVNEDSEGRDLRQVTSTTKSCREKTELTPDQQTLLHFIMDSYNKQRMPQEITNKILKEEFSAEENFLILTEMATNHVQVLVEFTKKLPGFQTLDHEDQIALLKGSAVEAMFLRSAEIFNKKLPSGHSDLLEERIRNSGISDEYITPMFSFYKSIGELKMTQEEYALLTAIVILSPDRQYIKDREAVEKLQEPLLDVLQKLCKIHQPENPQHFACLLGRLTELRTFNHHHAEMLMSWRVNDHKFTPLLCEIWDVQ TTS4UGC TT Successful TTS4UGC FM Nuclear hormone receptor family TTS4UGC KE hsa04976:Bile secretion TTS4UGC RC R-HSA-159418:Recycling of bile acids and salts; R-HSA-1989781:PPARA activates gene expression; R-HSA-211976:Endogenous sterols TT7AOUD ID TT7AOUD TT7AOUD TN Fatty acid synthase (FASN) TT7AOUD UP P49327 TT7AOUD UC FAS_HUMAN TT7AOUD BC Acyltransferase TT7AOUD SN Yeast fatty acid synthase; Fatty-acyl-CoA synthase; Fatty acyl-CoA synthetase enzyme; FAS TT7AOUD GN FASN TT7AOUD FC Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities as an acyl carrier protein. TT7AOUD EC EC 2.3.1.85 TT7AOUD PD 6NNA; 5C37; 4Z49; 4W9N; 4W82 TT7AOUD SQ MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARRVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEAQWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSLAWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLARALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQWDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRLLWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVVSRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVAALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESLFSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRPVWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPGAQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEEPEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG TT7AOUD TT Successful TT7AOUD FM Acyltransferase TT7AOUD KE hsa00061:Fatty acid biosynthesis; hsa01100:Metabolic pathways; hsa01212:Fatty acid metabolism; hsa04152:AMPK signaling pathway; hsa04910:Insulin signaling pathway TT7AOUD RC R-HSA-163765:ChREBP activates metabolic gene expression; R-HSA-2426168:Activation of gene expression by SREBF (SREBP); R-HSA-75105:Fatty Acyl-CoA Biosynthesis TTB6UM0 ID TTB6UM0 TTB6UM0 TN Fatty aldehyde dehydrogenase (ALDH3A2) TTB6UM0 UP P51648 TTB6UM0 UC AL3A2_HUMAN TTB6UM0 BC Aldehyde/oxo donor oxidoreductase TTB6UM0 SN Microsomal aldehyde dehydrogenase; Aldehyde dehydrogenase family 3 member A2; Aldehyde dehydrogenase 10; ALDH10 TTB6UM0 GN ALDH3A2 TTB6UM0 FC Catalyzes the oxidation of medium and long chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid. TTB6UM0 EC EC 1.2.1.3 TTB6UM0 PD 4QGK TTB6UM0 SQ MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKEKLGLLLLTFLGIVAAVLVKAEYY TTB6UM0 TT Successful TTMW94E ID TTMW94E TTMW94E TN FK506-binding protein 1A (FKBP1A) TTMW94E UP P62942 TTMW94E UC FKB1A_HUMAN TTMW94E BC Cis-trans-isomerase TTMW94E SN Rotamase; Peptidyl-prolyl cis-trans isomerase FKBP1A; PPIase FKBP1A; Immunophillin FKBP; Immunophilin FKBP12; FKBP12; FKBP1; FKBP-1A; FKBP-12; FK-binding protein 12; Calstabin-1; 12 kDa FKBP; 12 kDa FK506-binding protein TTMW94E GN FKBP1A TTMW94E FC Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. TTMW94E EC EC 5.2.1.8 TTMW94E PD 5I7Q; 5I7P; 4ODR; 4ODQ; 4ODP TTMW94E SQ MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE TTMW94E TT Successful TTMW94E FM Cis trans isomerase TTT2LD9 ID TTT2LD9 TTT2LD9 TN GABA transaminase (ABAT) TTT2LD9 UP P80404 TTT2LD9 UC GABT_HUMAN TTT2LD9 BC Transaminase TTT2LD9 SN L-AIBAT; Gamma-amino-N-butyrate transaminase; GABA-T; GABA-AT; GABA aminotransferase; ABAT; (S)-3-amino-2-methylpropionate transaminase TTT2LD9 GN ABAT TTT2LD9 FC Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate andbeta-alanine. TTT2LD9 EC EC 2.6.1.19 TTT2LD9 SQ MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMKQLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQNASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYRSKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLLDLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVFRDHHAHLFLNIFSDILADFK TTT2LD9 TT Successful TTT2LD9 KE hsa00250:Alanine, aspartate and glutamate metabolism; hsa00280:Valine, leucine and isoleucine degradation; hsa00410:beta-Alanine metabolism; hsa00640:Propanoate metabolism; hsa00650:Butanoate metabolism; hsa01100:Metabolic pathways; hsa04727:GABAergic synapse TT1MPAY ID TT1MPAY TT1MPAY TN GABA(A) receptor alpha-1 (GABRA1) TT1MPAY UP P14867 TT1MPAY UC GBRA1_HUMAN TT1MPAY BC Ligand-gated ion channel TT1MPAY SN Gamma-aminobutyric acid receptor subunit alpha-1; GABA(A) receptor subunit alpha-1 TT1MPAY GN GABRA1 TT1MPAY FC Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel. The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer (By similarity). The alpha1/beta2/gamma2 receptor and the alpha1/beta3/gamma2 receptor exhibit synaptogenic activity. GABRA1-mediated plasticity in the orbitofrontal cortex regulates context-dependent action selection (By similarity). Functions also as histamine receptor and mediates cellular responses to histamine (By similarity). TT1MPAY PD 6I53; 6D6U; 6D6T; 6D1S; 6CDU TT1MPAY SQ MRKSPGLSDCLWAWILLLSTLTGRSYGQPSLQDELKDNTTVFTRILDRLLDGYDNRLRPGLGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHACPLKFGSYAYTRAEVVYEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGYAWDGKSVVPEKPKKVKDPLIKKNNTYAPTATSYTPNLARGDPGLATIAKSATIEPKEVKPETKPPEPKKTFNSVSKIDRLSRIAFPLLFGIFNLVYWATYLNREPQLKAPTPHQ TT1MPAY TT Successful TT1MPAY KE hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction TT1MPAY RC R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation TT37EDJ ID TT37EDJ TT37EDJ TN GABA(A) receptor alpha-3 (GABRA3) TT37EDJ UP P34903 TT37EDJ UC GBRA3_HUMAN TT37EDJ BC Neurotransmitter receptor TT37EDJ SN Gamma-aminobutyric acid receptor subunit alpha-3; GABA-A receptor alpha 3; GABA(A)Gamma-aminobutyric-acid receptor alpha-3 subunit precursor receptor; GABA(A) receptor subunit alpha-3 TT37EDJ GN GABRA3 TT37EDJ FC GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. TT37EDJ SQ MIITQTSHCYMTSLGILFLINILPGTTGQGESRRQEPGDFVKQDIGGLSPKHAPDIPDDSTDNITIFTRILDRLLDGYDNRLRPGLGDAVTEVKTDIYVTSFGPVSDTDMEYTIDVFFRQTWHDERLKFDGPMKILPLNNLLASKIWTPDTFFHNGKKSVAHNMTTPNKLLRLVDNGTLLYTMRLTIHAECPMHLEDFPMDVHACPLKFGSYAYTTAEVVYSWTLGKNKSVEVAQDGSRLNQYDLLGHVVGTEIIRSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRSWAWEGKKVPEALEMKKKTPAAPAKKTSTTFNIVGTTYPINLAKDTEFSTISKGAAPSASSTPTIIASPKATYVQDSPTETKTYNSVSKVDKISRIIFPVLFAIFNLVYWATYVNRESAIKGMIRKQ TT37EDJ TT Successful TT37EDJ FM Ligand-gated ion channel TT37EDJ KE hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction TT37EDJ RC R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation TTNZPQ1 ID TTNZPQ1 TTNZPQ1 TN GABA(A) receptor alpha-5 (GABRA5) TTNZPQ1 UP P31644 TTNZPQ1 UC GBRA5_HUMAN TTNZPQ1 BC Ligand-gated ion channel TTNZPQ1 SN GABRA5; GABAA alpha 5; GABA-A alpha-5 TTNZPQ1 GN GABRA5 TTNZPQ1 FC GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. TTNZPQ1 PD 6A96; 5OJM; 5O8F TTNZPQ1 SQ MDNGMFSGFIMIKNLLLFCISMNLSSHFGFSQMPTSSVKDETNDNITIFTRILDGLLDGYDNRLRPGLGERITQVRTDIYVTSFGPVSDTEMEYTIDVFFRQSWKDERLRFKGPMQRLPLNNLLASKIWTPDTFFHNGKKSIAHNMTTPNKLLRLEDDGTLLYTMRLTISAECPMQLEDFPMDAHACPLKFGSYAYPNSEVVYVWTNGSTKSVVVAEDGSRLNQYHLMGQTVGTENISTSTGEYTIMTAHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGWAWDGKKALEAAKIKKKREVILNKSTNAFTTGKMSHPPNIPKEQTPAGTSNTTSVSVKPSEEKTSESKKTYNSISKIDKMSRIVFPVLFGTFNLVYWATYLNREPVIKGAASPK TTNZPQ1 TT Successful TTNZPQ1 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction TTNZPQ1 RC R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation TTZA1NY ID TTZA1NY TTZA1NY TN GABA(A) receptor beta-2 (GABRB2) TTZA1NY UP P47870 TTZA1NY UC GBRB2_HUMAN TTZA1NY BC Neurotransmitter receptor TTZA1NY SN GABRB2; GABA(A) receptor subunit beta-2 TTZA1NY GN GABRB2 TTZA1NY FC Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand- gated chloride channel. TTZA1NY PD 6D6U; 6D6T TTZA1NY SQ MWRVRKRGYFGIWSFPLIIAAVCAQSVNDPSNMSLVKETVDRLLKGYDIRLRPDFGGPPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGDDNAVTGVTKIELPQFSIVDYKLITKKVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFMALLEYALVNYIFFGRGPQRQKKAAEKAASANNEKMRLDVNKIFYKDIKQNGTQYRSLWDPTGNLSPTRRTTNYDFSLYTMDPHENILLSTLEIKNEMATSEAVMGLGDPRSTMLAYDASSIQYRKAGLPRHSFGRNALERHVAQKKSRLRRRASQLKITIPDLTDVNAIDRWSRIFFPVVFSFFNIVYWLYYVN TTZA1NY TT Successful TTZA1NY KE hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04726:Serotonergic synapse; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction TTZA1NY RC R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation TT06RH5 ID TT06RH5 TT06RH5 TN GABA(A) receptor gamma-2 (GABRG2) TT06RH5 UP P18507 TT06RH5 UC GBRG2_HUMAN TT06RH5 BC Neurotransmitter receptor TT06RH5 SN Gamma-aminobutyric acid receptor subunit gamma-2; GABA(A) receptor subunit gamma-2 TT06RH5 GN GABRG2 TT06RH5 FC Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel. The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer. The alpha1/beta2/gamma2 receptor and the alpha1/beta3/gamma2 receptor exhibit synaptogenic activity. The alpha2/beta2/gamma2 receptor exhibits synatogenic activity whereas the alpha2/beta3/gamma2 receptor shows very little or no synaptogenic activity. Functions also as histamine receptor and mediates cellular responses to histamine. Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. TT06RH5 PD 6I53; 6HUP; 6HUO; 6HUK; 6HUJ TT06RH5 SQ MSSPNIWSTGSSVYSTPVFSQKMTVWILLLLSLYPGFTSQKSDDDYEDYASNKTWVLTPKVPEGDVTVILNNLLEGYDNKLRPDIGVKPTLIHTDMYVNSIGPVNAINMEYTIDIFFAQTWYDRRLKFNSTIKVLRLNSNMVGKIWIPDTFFRNSKKADAHWITTPNRMLRIWNDGRVLYTLRLTIDAECQLQLHNFPMDEHSCPLEFSSYGYPREEIVYQWKRSSVEVGDTRSWRLYQFSFVGLRNTTEVVKTTSGDYVVMSVYFDLSRRMGYFTIQTYIPCTLIVVLSWVSFWINKDAVPARTSLGITTVLTMTTLSTIARKSLPKVSYVTAMDLFVSVCFIFVFSALVEYGTLHYFVSNRKPSKDKDKKKKNPAPTIDIRPRSATIQMNNATHLQERDEEYGYECLDGKDCASFFCCFEDCRTGAWRHGRIHIRIAKMDSYARIFFPTAFCLFNLVYWVSYLYL TT06RH5 TT Successful TT06RH5 FM Ligand gated ion channel TT06RH5 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction TT06RH5 RC R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation TTF1QVM ID TTF1QVM TTF1QVM TN Gastric H(+)/K(+) ATPase alpha (ATP4A) TTF1QVM UP P20648 TTF1QVM UC ATP4A_HUMAN TTF1QVM BC Acid anhydrides hydrolase TTF1QVM SN Gastric H+/K+ ATPase alpha subunit; Gastric H(+)/K(+)-ATPase; ATP4A TTF1QVM GN ATP4A TTF1QVM FC Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for acid production in the stomach. TTF1QVM EC EC 7.2.2.19 TTF1QVM SQ MGKAENYELYSVELGPGPGGDMAAKMSKKKKAGGGGGKRKEKLENMKKEMEINDHQLSVAELEQKYQTSATKGLSASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLAIALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILAAQGCKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTVQGLVVNTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFIVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQLYLNEKDYPPGYAFDVEAMNFPSSGLCFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPRNPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEGWFPLLCVGLRAQWEDHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEVCQIADVLIRKTRRLSAFQQGFFRNKILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPLPYGILIFVYDEIRKLGVRCCPGSWWDQELYY TTF1QVM TT Successful TTF1QVM KE hsa00190:Oxidative phosphorylation; hsa04966:Collecting duct acid secretion; hsa04971:Gastric acid secretion TTF1QVM RC R-HSA-936837:Ion transport by P-type ATPases TT9O6WS ID TT9O6WS TT9O6WS TN Glucagon receptor (GCGR) TT9O6WS UP P47871 TT9O6WS UC GLR_HUMAN TT9O6WS BC GPCR secretin TT9O6WS SN GLR; GL-R TT9O6WS GN GCGR TT9O6WS FC Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system. G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. TT9O6WS PD 5XEZ; 5EE7; 4LF3; 4L6R; 4ERS TT9O6WS SQ MPPCQPQRPLLLLLLLLACQPQVPSAQVMDFLFEKWKLYGDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPANTTANISCPWYLPWHHKVQHRFVFKRCGPDGQWVRGPRGQPWRDASQCQMDGEEIEVQKEVAKMYSSFQVMYTVGYSLSLGALLLALAILGGLSKLHCTRNAIHANLFASFVLKASSVLVIDGLLRTRYSQKIGDDLSVSTWLSDGAVAGCRVAAVFMQYGIVANYCWLLVEGLYLHNLLGLATLPERSFFSLYLGIGWGAPMLFVVPWAVVKCLFENVQCWTSNDNMGFWWILRFPVFLAILINFFIFVRIVQLLVAKLRARQMHHTDYKFRLAKSTLTLIPLLGVHEVVFAFVTDEHAQGTLRSAKLFFDLFLSSFQGLLVAVLYCFLNKEVQSELRRRWHRWRLGKVLWEERNTSNHRASSSPGHGPPSKELQFGRGGGSQDSSAETPLAGGLPRLAESPF TT9O6WS TT Successful TT9O6WS FM GPCR secretin TT9O6WS KE hsa04080:Neuroactive ligand-receptor interaction; hsa04922:Glucagon signaling pathway TT9O6WS RC R-HSA-163359:Glucagon signaling in metabolic regulation; R-HSA-416476:G alpha (q) signalling events; R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors TTVIMDE ID TTVIMDE TTVIMDE TN Glucagon-like peptide 1 receptor (GLP1R) TTVIMDE UP P43220 TTVIMDE UC GLP1R_HUMAN TTVIMDE BC GPCR secretin TTVIMDE SN GLP-1R; GLP-1-R; GLP-1 receptor TTVIMDE GN GLP1R TTVIMDE FC Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels. Plays a role in regulating insulin secretion in response to GLP-1. G-protein coupled receptor for glucagon-like peptide 1 (GLP-1). TTVIMDE PD 6GB1; 6B3J; 5VEX; 5VEW; 5OTX TTVIMDE SQ MAGAPGPLRLALLLLGMVGRAGPRPQGATVSLWETVQKWREYRRQCQRSLTEDPPPATDLFCNRTFDEYACWPDGEPGSFVNVSCPWYLPWASSVPQGHVYRFCTAEGLWLQKDNSSLPWRDLSECEESKRGERSSPEEQLLFLYIIYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLSCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVLSEQWIFRLYVSIGWGVPLLFVVPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVNFLIFVRVICIVVSKLKANLMCKTDIKCRLAKSTLTLIPLLGTHEVIFAFVMDEHARGTLRFIKLFTELSFTSFQGLMVAILYCFVNNEVQLEFRKSWERWRLEHLHIQRDSSMKPLKCPTSSLSSGATAGSSMYTATCQASCS TTVIMDE TT Successful TTVIMDE FM GPCR secretin TTVIMDE KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04911:Insulin secretion TTVIMDE RC R-HSA-381676:Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors TT1B5PU ID TT1B5PU TT1B5PU TN Glucosylceramidase (GBA) TT1B5PU UP P04062 TT1B5PU UC GLCM_HUMAN TT1B5PU BC Glycosylase TT1B5PU SN SGTase; Lysosomal acid glucosylceramidase; Lysosomal acid GCase; Imiglucerase; GLUC; GC; D-glucosyl-N-acylsphingosine glucohydrolase; Cholesteryl-beta-glucosidase; Cholesterol glucosyltransferase; Beta-glucocerebrosidase; Beta-GC; Alglucerase; Acid beta-glucosidase TT1B5PU GN GBA TT1B5PU FC Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramide/GlcCer into free ceramide and glucose. Thereby, plays a central role in the degradation of complex lipids and the turnover of cellular membranes. Through the production of ceramides, participates to the PKC-activated salvage pathway of ceramide formation. Also plays a role in cholesterol metabolism. May either catalyze the glucosylation of cholesterol, through a transglucosylation reaction that transfers glucose from glucosylceramide to cholesterol. The short chain saturated C8:0-GlcCer and the mono-unsaturated C18:0-GlcCer being the most effective glucose donors for that transglucosylation reaction. Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl-beta-D-glucoside to ceramide. Finally, may also hydrolyze cholesteryl-beta-D-glucoside to produce D-glucose and cholesterol. TT1B5PU EC EC 3.2.1.45 TT1B5PU PD 6Q6N; 6Q6L; 6Q6K; 5LVX; 3RIL TT1B5PU SQ MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ TT1B5PU TT Successful TT1B5PU KE hsa00511:Other glycan degradation; hsa00600:Sphingolipid metabolism; hsa01100:Metabolic pathways; hsa04142:Lysosome TT1B5PU RC R-HSA-1660662:Glycosphingolipid metabolism TT0MYE2 ID TT0MYE2 TT0MYE2 TN Glutamate receptor ionotropic kainate 1 (GRIK1) TT0MYE2 UP P39086 TT0MYE2 UC GRIK1_HUMAN TT0MYE2 BC Glutamate-gated ion channel TT0MYE2 SN Glutamate receptor 5; GluR5 kainate receptor; GluR5; GluR-5; GRIK1; Excitatory amino acid receptor 3; EAA3 TT0MYE2 GN GRIK1 TT0MYE2 FC Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading tothe opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus. TT0MYE2 PD 4MF3; 3FVO; 3FVN; 3FVK; 3FVG TT0MYE2 SQ MEHGTLLAQPGLWTRDTSWALLYFLCYILPQTAPQVLRIGGIFETVENEPVNVEELAFKFAVTSINRNRTLMPNTTLTYDIQRINLFDSFEASRRACDQLALGVAALFGPSHSSSVSAVQSICNALEVPHIQTRWKHPSVDNKDLFYINLYPDYAAISRAILDLVLYYNWKTVTVVYEDSTGLIRLQELIKAPSRYNIKIKIRQLPSGNKDAKPLLKEMKKGKEFYVIFDCSHETAAEILKQILFMGMMTEYYHYFFTTLDLFALDLELYRYSGVNMTGFRLLNIDNPHVSSIIEKWSMERLQAPPRPETGLLDGMMTTEAALMYDAVYMVAIASHRASQLTVSSLQCHRHKPWRLGPRFMNLIKEARWDGLTGHITFNKTNGLRKDFDLDIISLKEEGTEKAAGEVSKHLYKVWKKIGIWNSNSGLNMTDSNKDKSSNITDSLANRTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKELSNILGFIYDVKLVPDGKYGAQNDKGEWNGMVKELIDHRADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYVLLACLGVSCVLFVIARFTPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSSRQQTALVRNSDEGIQRVLTTDYALLMESTSIEYVTQRNCNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEDNKEASALGVENIGGIFIVLAAGLVLSVFVAIGEFIYKSRKNNDIEQAFCFFYGLQCKQTHPTNSTSGTTLSTDLECGKLIREERGIRKQSSVHTV TT0MYE2 TT Successful TT0MYE2 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse TTLD29N ID TTLD29N TTLD29N TN Glutamate receptor ionotropic NMDA 1 (NMDAR1) TTLD29N UP Q05586 TTLD29N UC NMDZ1_HUMAN TTLD29N BC Glutamate-gated ion channel TTLD29N SN NmethylDaspartate receptor subunit NR1; NMDR1; NMD-R1; N-methyl-D-aspartate receptor subunit NR1; Glutamate receptor ionotropic, NMDA 1; Glutamate [NMDA] receptor subunit zeta1; Glutamate [NMDA] receptor subunit zeta-1; GluN1 TTLD29N GN GRIN1 TTLD29N FC Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition. Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. TTLD29N PD 6IRH; 6IRG; 6IRF; 6IRA; 5TPA TTLD29N SQ MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES TTLD29N TT Successful TTLD29N KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04724:Glutamatergic synapse; hsa05010:Alzheimer's disease; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05016:Huntington's disease; hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05033:Nicotine addiction; hsa05034:Alcoholism TTLD29N RC R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-438066:Unblocking of NMDA receptor, glutamate binding and activation; R-HSA-442729:CREB phosphorylation through the activation of CaMKII; R-HSA-442982:Ras activation uopn Ca2+ infux through NMDA receptor; R-HSA-5673001:RAF/MAP kinase cascade TTKJEMQ ID TTKJEMQ TTKJEMQ TN Glutamate receptor ionotropic NMDA 2A (NMDAR2A) TTKJEMQ UP Q12879 TTKJEMQ UC NMDE1_HUMAN TTKJEMQ BC Glutamate-gated ion channel TTKJEMQ SN NR2A; NMDA receptor NR2A; N-methyl D-aspartate receptor subtype 2A; HNR2A; Glutamate receptor ionotropic, NMDA 2A; Glutamate [NMDA] receptor subunit epsilon-1; GluN2A TTKJEMQ GN GRIN2A TTKJEMQ FC Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition; channels containing GRIN1 and GRIN2A have higher sensitivity to glutamate and faster kinetics than channels formed by GRIN1 and GRIN2B. Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning. Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. TTKJEMQ PD 6IRH; 6IRG; 6IRF; 6IRA; 5TPA TTKJEMQ SQ MGRVGYWTLLVLPALLVWRGPAPSAAAEKGPPALNIAVMLGHSHDVTERELRTLWGPEQAAGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVAQMLDFISSHTFVPILGIHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTTIFPGYREFISFVKTTVDNSFVGWDMQNVITLDTSFEDAKTQVQLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWIVPSLVSGNTELIPKEFPSGLISVSYDDWDYSLEARVRDGIGILTTAASSMLEKFSYIPEAKASCYGQMERPEVPMHTLHPFMVNVTWDGKDLSFTEEGYQVHPRLVVIVLNKDREWEKVGKWENHTLSLRHAVWPRYKSFSDCEPDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNGTVSPSAFLEPFSASVWVMMFVMLLIVSAIAVFVFEYFSPVGYNRNLAKGKAPHGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHNEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFIWEHLFYWKLRFCFTGVCSDRPGLLFSISRGIYSCIHGVHIEEKKKSPDFNLTGSQSNMLKLLRSAKNISSMSNMNSSRMDSPKRAADFIQRGSLIMDMVSDKGNLMYSDNRSFQGKESIFGDNMNELQTFVANRQKDNLNNYVFQGQHPLTLNESNPNTVEVAVSTESKANSRPRQLWKKSVDSIRQDSLSQNPVSQRDEATAENRTHSLKSPRYLPEEMAHSDISETSNRATCHREPDNSKNHKTKDNFKRSVASKYPKDCSEVERTYLKTKSSSPRDKIYTIDGEKEPGFHLDPPQFVENVTLPENVDFPDPYQDPSENFRKGDSTLPMNRNPLHNEEGLSNNDQYKLYSKHFTLKDKGSPHSETSERYRQNSTHCRSCLSNMPTYSGHFTMRSPFKCDACLRMGNLYDIDEDQMLQETGNPATGEQVYQQDWAQNNALQLQKNKLRISRQHSYDNIVDKPRELDLSRPSRSISLKDRERLLEGNFYGSLFSVPSSKLSGKKSSLFPQGLEDSKRSKSLLPDHTSDNPFLHSHRDDQRLVIGRCPSDPYKHSLPSQAVNDSYLRSSLRSTASYCSRDSRGHNDVYISEHVMPYAANKNNMYSTPRVLNSCSNRRVYKKMPSIESDV TTKJEMQ TT Successful TTKJEMQ FM Glutamate gated ion channel TTKJEMQ KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04724:Glutamatergic synapse; hsa04728:Dopaminergic synapse; hsa05010:Alzheimer's disease; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05033:Nicotine addiction; hsa05034:Alcoholism; hsa05322:Systemic lupus erythematosus TTKJEMQ RC R-HSA-438066:Unblocking of NMDA receptor, glutamate binding and activation; R-HSA-442729:CREB phosphorylation through the activation of CaMKII; R-HSA-442982:Ras activation uopn Ca2+ infux through NMDA receptor; R-HSA-5673001:RAF/MAP kinase cascade TTN9D8E ID TTN9D8E TTN9D8E TN Glutamate receptor ionotropic NMDA 2B (NMDAR2B) TTN9D8E UP Q13224 TTN9D8E UC NMDE2_HUMAN TTN9D8E BC Glutamate-gated ion channel TTN9D8E SN NR3; NR2B; NMDA receptor subunit 2B; NMDA receptor NR2B; NMDA NR2B receptor; N-methylD-aspartate receptor subtype 2B; N-methyl-D-aspartate receptor subunit 3; N-methyl D-aspartate receptor subtype 2B; HNR3; Glutamate receptor ionotropic, NMDA 2B; Glutamate receptor NR2B subunit; Glutamate [NMDA] receptor subunit epsilon-2; GluN2B TTN9D8E GN GRIN2B TTN9D8E FC Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death. Contributes to neural pattern formation in the developing brain. Plays a role in long-term depression (LTD) of hippocampus membrane currents and in synaptic plasticity. Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. TTN9D8E PD 5EWM; 5EWL; 5EWJ; 2IPV; 1S2S TTN9D8E SQ MKPRAECCSPKFWLVLAVLAVSGSRARSQKSPPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVFADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVPAEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVESVDPLSGTCMRNTVPCQKRIVTENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEHLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFSDYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSASSIDGLYDCDNPPFTTQSRSISKKPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKRRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTKENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHIKHGTGDKHGVVSGVPAPWEKNLTNVEWEDRSGGNFCRSCPSKLHNYSTTVTGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAAPVAVTSNASTTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPRSVSLKDKGRFMDGSPYAHMFEMSAGESTFANNKSSVPTAGHHHHNNPGGGYMLSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKARPDFRALVTNKPVVSALHGAVPARFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV TTN9D8E TT Successful TTN9D8E FM Glutamate gated ion channel TTN9D8E KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04724:Glutamatergic synapse; hsa04728:Dopaminergic synapse; hsa05010:Alzheimer's disease; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05016:Huntington's disease; hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05033:Nicotine addiction; hsa05034:Alcoholism; hsa05322:Systemic lupus erythematosus TTN9D8E RC R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-438066:Unblocking of NMDA receptor, glutamate binding and activation; R-HSA-442729:CREB phosphorylation through the activation of CaMKII; R-HSA-442982:Ras activation uopn Ca2+ infux through NMDA receptor; R-HSA-5673001:RAF/MAP kinase cascade TTC70AJ ID TTC70AJ TTC70AJ TN Granulocyte colony-stimulating factor receptor (G-CSF-R) TTC70AJ UP Q99062 TTC70AJ UC CSF3R_HUMAN TTC70AJ BC Cytokine receptor TTC70AJ SN c-fms; GCSFR; GCSF receptor; G-CSF receptor; Fms proto-oncogene; CD114 TTC70AJ GN CSF3R TTC70AJ FC Plays a crucial role in the proliferation, differientation and survival of cells along the neutrophilic lineage. In addition it may function in some adhesion or recognition events at the cell surface. Receptor for granulocyte colony-stimulating factor (CSF3), essential for granulocytic maturation. TTC70AJ PD 2D9Q; 1AZ7 TTC70AJ SQ MARLGNCSLTWAALIILLLPGSLEECGHISVSAPIVHLGDPITASCIIKQNCSHLDPEPQILWRLGAELQPGGRQQRLSDGTQESIITLPHLNHTQAFLSCCLNWGNSLQILDQVELRAGYPPAIPHNLSCLMNLTTSSLICQWEPGPETHLPTSFTLKSFKSRGNCQTQGDSILDCVPKDGQSHCCIPRKHLLLYQNMGIWVQAENALGTSMSPQLCLDPMDVVKLEPPMLRTMDPSPEAAPPQAGCLQLCWEPWQPGLHINQKCELRHKPQRGEASWALVGPLPLEALQYELCGLLPATAYTLQIRCIRWPLPGHWSDWSPSLELRTTERAPTVRLDTWWRQRQLDPRTVQLFWKPVPLEEDSGRIQGYVVSWRPSGQAGAILPLCNTTELSCTFHLPSEAQEVALVAYNSAGTSRPTPVVFSESRGPALTRLHAMARDPHSLWVGWEPPNPWPQGYVIEWGLGPPSASNSNKTWRMEQNGRATGFLLKENIRPFQLYEIIVTPLYQDTMGPSQHVYAYSQEMAPSHAPELHLKHIGKTWAQLEWVPEPPELGKSPLTHYTIFWTNAQNQSFSAILNASSRGFVLHGLEPASLYHIHLMAASQAGATNSTVLTLMTLTPEGSELHIILGLFGLLLLLTCLCGTAWLCCSPNRKNPLWPSVPDPAHSSLGSWVPTIMEEDAFQLPGLGTPPITKLTVLEEDEKKPVPWESHNSSETCGLPTLVQTYVLQGDPRAVSTQPQSQSGTSDQVLYGQLLGSPTSPGPGHYLRCDSTQPLLAGLTPSPKSYENLWFQASPLGTLVTPAPSQEDDCVFGPLLNFPLLQGIRVHGMEALGSF TTC70AJ TT Successful TTC70AJ FM Cytokine receptor TTC70AJ KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05200:Pathways in cancer TTWXB3E ID TTWXB3E TTWXB3E TN Hepatitis C virus NS3 helicase (HCV NS3) TTWXB3E UP P26664 (1027-1657) TTWXB3E UC POLG_HCV1 TTWXB3E BC Peptidase TTWXB3E SN HCV Hepacivirin; HCV NS3P; HCV p70 TTWXB3E GN HCV NS3 TTWXB3E FC Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). TTWXB3E EC EC 3.4.21.98 TTWXB3E PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TTWXB3E SQ APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVVT TTWXB3E TT Successful TTMVBWH ID TTMVBWH TTMVBWH TN Hepatitis C virus RNA-directed RNA polymerase (HCV NS5B) TTMVBWH UP P26664 (2421-3011) TTMVBWH UC POLG_HCV1 TTMVBWH BC Peptidase TTMVBWH SN HCV NS5B; HCV p68 TTMVBWH GN HCV NS5B TTMVBWH FC Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). TTMVBWH EC EC 2.7.7.48 TTMVBWH PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TTMVBWH SQ SMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRQKKVTFDRLQVLDSHYQDVLKEVKAAASKVKANLLSVEEACSLTPPHSAKSKFGYGAKDVRCHARKAVTHINSVWKDLLEDNVTPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVTKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGFSYDTRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCRASGVLTTSCGNTLTCYIKARAACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALDCEIYGACYSIEPLDLPPIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRARSVRARLLARGGRAAICGKYLFNWAVRTKLKLTPIAAAGQLDLSGWFTAGYSGGDIYHSVSHARPRWIWFCLLLLAAGVGIYLLPNR TTMVBWH TT Successful TT2B6EV ID TT2B6EV TT2B6EV TN Histamine N-methyltransferase (HNMT) TT2B6EV UP P50135 TT2B6EV UC HNMT_HUMAN TT2B6EV BC Methyltransferase TT2B6EV SN Histamine-N-methyltransferase; HNMT; HMT TT2B6EV GN HNMT TT2B6EV FC Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine. TT2B6EV EC EC 2.1.1.8 TT2B6EV PD 2AOX; 2AOW; 2AOV; 2AOU; 2AOT TT2B6EV SQ MASSMRSLFSDHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIGRIGDTKSEIKILSIGGGAGEIDLQILSKVQAQYPGVCINNEVVEPSAEQIAKYKELVAKTSNLENVKFAWHKETSSEYQSRMLEKKELQKWDFIHMIQMLYYVKDIPATLKFFHSLLGTNAKMLIIVVSGSSGWDKLWKKYGSRFPQDDLCQYITSDDLTQMLDNLGLKYECYDLLSTMDISDCFIDGNENGDLLWDFLTETCNFNATAPPDLRAELGKDLQEPEFSAKKEGKVLFNNTLSFIVIEA TT2B6EV TT Successful TT2B6EV KE hsa00340:Histidine metabolism TT5FH9Y ID TT5FH9Y TT5FH9Y TN Human immunodeficiency virus Integrase (HIV IN) TT5FH9Y UP P03366 (1160-1447) TT5FH9Y UC POL_HV1B1 TT5FH9Y BC Integrase TT5FH9Y SN HIV IN TT5FH9Y GN HIV IN TT5FH9Y FC Gag-Pol polyprotein: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. TT5FH9Y EC EC 2.7.7.- TT5FH9Y PD 6OE3; 6HAK; 6ELI; 6DUH; 6DUG TT5FH9Y SQ FLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTSATVKAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED TT5FH9Y TT Successful TT8DSFC ID TT8DSFC TT8DSFC TN Hydroxyphenylpyruvate dioxygenase (HPD) TT8DSFC UP P32754 TT8DSFC UC HPPD_HUMAN TT8DSFC BC Single donor oxidoreductase TT8DSFC SN HPPDase; HPD; F Alloantigen; 4HPPD TT8DSFC GN HPD TT8DSFC FC Key enzyme in the degradation of tyrosine. TT8DSFC EC EC 1.13.11.27 TT8DSFC PD 5EC3; 3ISQ TT8DSFC SQ MTTYSDKGAKPERGRFLHFHSVTFWVGNAKQAASFYCSKMGFEPLAYRGLETGSREVVSHVIKQGKIVFVLSSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCDYIVQKARERGAKIMREPWVEQDKFGKVKFAVLQTYGDTTHTLVEKMNYIGQFLPGYEAPAFMDPLLPKLPKCSLEMIDHIVGNQPDQEMVSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPINEPAPGKKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRHLRERGLEFLSVPSTYYKQLREKLKTAKIKVKENIDALEELKILVDYDEKGYLLQIFTKPVQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQNLRGNLTNMETNGVVPGM TT8DSFC TT Successful TT8DSFC KE mmu00130:Ubiquinone and other terpenoid-quinone biosynthesis; mmu00350:Tyrosine metabolism; mmu00360:Phenylalanine metabolism; mmu01100:Metabolic pathways TTA1L39 ID TTA1L39 TTA1L39 TN ICAM1 messenger RNA (ICAM1 mRNA) TTA1L39 UP P05362 TTA1L39 UC ICAM1_HUMAN TTA1L39 BC mRNA target TTA1L39 SN Major group rhinovirus receptor (mRNA); Intercellular adhesion molecule 1 (mRNA); ICAM-1 (mRNA); CD54 (mRNA) TTA1L39 GN ICAM1 TTA1L39 FC During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). TTA1L39 PD 6EIT; 5MZA; 3TCX; 2OZ4; 1Z7Z TTA1L39 SQ MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTRKVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP TTA1L39 TT Successful TTA1L39 FM mRNA target TTA1L39 KE hsa04064:NF-kappa B signaling pathway; hsa04514:Cell adhesion molecules (CAMs); hsa04650:Natural killer cell mediated cytotoxicity; hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05150:Staphylococcus aureus infection; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05323:Rheumatoid arthritis; hsa05416:Viral myocarditis TTA1L39 RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-216083:Integrin cell surface interactions; R-HSA-877300:Interferon gamma signaling TTZJYKH ID TTZJYKH TTZJYKH TN Indoleamine 2,3-dioxygenase 1 (IDO1) TTZJYKH UP P14902 TTZJYKH UC I23O1_HUMAN TTZJYKH BC Oxygenase TTZJYKH SN Indoleamine-pyrrole 2,3-dioxygenase; INDO; IDO-1; IDO TTZJYKH GN IDO1 TTZJYKH FC Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses. Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T-cells. Acts as a suppressor of anti-tumor immunity. Limits the growth of intracellular pathogens by depriving tryptophan. Protects the fetus from maternal immune rejection. Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. TTZJYKH EC EC 1.13.11.52 TTZJYKH PD 6MQ6; 6F0A; 6DPR; 6DPQ; 6CXV TTZJYKH SQ MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG TTZJYKH TT Successful TTZJYKH FM Oxidoreductases acting on single donors TTZJYKH KE hsa00380:Tryptophan metabolism; hsa01100:Metabolic pathways; hsa05143:African trypanosomiasis TTZJYKH RC R-HSA-71240:Tryptophan catabolism TTXT3PU ID TTXT3PU TTXT3PU TN Influenza M2 protein (Influ M) TTXT3PU UP P06821 TTXT3PU UC M2_I34A1 TTXT3PU BC Influenza viruses matrix protein TTXT3PU SN Matrix protein M2; M2 proton channel; M TTXT3PU GN Influ M TTXT3PU FC Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. TTXT3PU PD 5DLM TTXT3PU SQ MSLLTEVETPIRNEWGCRCNGSSDPLAIAANIIGILHLILWILDRLFFKCIYRRFKYGLKGGPSTEGVPKSMREEYRKEQQSAVDADDGHFVSIELE TTXT3PU TT Successful TTTB4UP ID TTTB4UP TTTB4UP TN Inosine-5'-monophosphate dehydrogenase 2 (IMPDH2) TTTB4UP UP P12268 TTTB4UP UC IMDH2_HUMAN TTTB4UP BC CH-OH donor oxidoreductase TTTB4UP SN IMPDH-II; IMPDH 2; IMPD2; IMPD 2; IMP dehydrogenase 2 TTTB4UP GN IMPDH2 TTTB4UP FC Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors. Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. TTTB4UP EC EC 1.1.1.205 TTTB4UP PD 6I0O; 6I0M; 1NFB; 1NF7; 1B3O TTTB4UP SQ MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF TTTB4UP TT Successful TTTB4UP FM Short-chain dehydrogenases reductases TTTB4UP KE hsa00230:Purine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways TTTB4UP RC R-HSA-73817:Purine ribonucleoside monophosphate biosynthesis TT2EDHU ID TT2EDHU TT2EDHU TN Insulin-degrading enzyme (IDE) TT2EDHU UP P14735 TT2EDHU UC IDE_HUMAN TT2EDHU BC Peptidase TT2EDHU SN Insulysin; Insulinase; Insulin protease; Abeta-degrading protease TT2EDHU GN IDE TT2EDHU FC Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin. Contributes to the regulation of peptide hormone signaling cascades and regulation of blood glucose homeostasis via its role in the degradation of insulin, glucagon and IAPP. Plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia. Involved in antigen processing. Produces both the N terminus and the C terminus of MAGEA3-derived antigenic peptide (EVDPIGHLY) that is presented to cytotoxic T lymphocytes by MHC class I. Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. TT2EDHU EC EC 3.4.24.56 TT2EDHU PD 6MQ3; 6EDS; 6BYZ; 6BFC; 6BF9 TT2EDHU SQ MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL TT2EDHU TT Successful TT2EDHU KE hsa05010:Alzheimer's disease TT48WR6 ID TT48WR6 TT48WR6 TN Integrin alpha-L (ITGAL) TT48WR6 UP P20701 TT48WR6 UC ITAL_HUMAN TT48WR6 BC Integrin TT48WR6 SN Lymphocyte Function-associated Antigen-1; Leukocyte function-associated molecule 1 alpha chain; Leukocyte function associated molecule 1, alpha chain; Leukocyte adhesion glycoprotein LFA-1 alpha chain; LFA-1A; LFA-1; CD11a; CD11 antigen-like family member A TT48WR6 GN ITGAL TT48WR6 FC Integrin ITGAL/ITGB2 is a receptor for F11R. Integin ITGAL/ITGB2 is a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL. Involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes. Contributes to natural killer cell cytotoxicity. Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils. Required for generation of common lymphoid progenitor cells in bone marrow, indicating a role in lymphopoiesis. Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages. Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. TT48WR6 PD 6CKB; 6BXJ; 6BXF; 6BXB; 5E6U TT48WR6 SQ MKDSCITVMAMALLSGFFFFAPASSYNLDVRGARSFSPPRAGRHFGYRVLQVGNGVIVGAPGEGNSTGSLYQCQSGTGHCLPVTLRGSNYTSKYLGMTLATDPTDGSILACDPGLSRTCDQNTYLSGLCYLFRQNLQGPMLQGRPGFQECIKGNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSNTSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGNIDAAKDIIRYIIGIGKHFQTKESQETLHKFASKPASEFVKILDTFEKLKDLFTELQKKIYVIEGTSKQDLTSFNMELSSSGISADLSRGHAVVGAVGAKDWAGGFLDLKADLQDDTFIGNEPLTPEVRAGYLGYTVTWLPSRQKTSLLASGAPRYQHMGRVLLFQEPQGGGHWSQVQTIHGTQIGSYFGGELCGVDVDQDGETELLLIGAPLFYGEQRGGRVFIYQRRQLGFEEVSELQGDPGYPLGRFGEAITALTDINGDGLVDVAVGAPLEEQGAVYIFNGRHGGLSPQPSQRIEGTQVLSGIQWFGRSIHGVKDLEGDGLADVAVGAESQMIVLSSRPVVDMVTLMSFSPAEIPVHEVECSYSTSNKMKEGVNITICFQIKSLIPQFQGRLVANLTYTLQLDGHRTRRRGLFPGGRHELRRNIAVTTSMSCTDFSFHFPVCVQDLISPINVSLNFSLWEEEGTPRDQRAQGKDIPPILRPSLHSETWEIPFEKNCGEDKKCEANLRVSFSPARSRALRLTAFASLSVELSLSNLEEDAYWVQLDLHFPPGLSFRKVEMLKPHSQIPVSCEELPEESRLLSRALSCNVSSPIFKAGHSVALQMMFNTLVNSSWGDSVELHANVTCNNEDSDLLEDNSATTIIPILYPINILIQDQEDSTLYVSFTPKGPKIHQVKHMYQVRIQPSIHDHNIPTLEAVVGVPQPPSEGPITHQWSVQMEPPVPCHYEDLERLPDAAEPCLPGALFRCPVVFRQEILVQVIGTLELVGEIEASSMFSLCSSLSISFNSSKHFHLYGSNASLAQVVMKVDVVYEKQMLYLYVLSGIGGLLLLLLIFIVLYKVGFFKRNLKEKMEAGRGVPNGIPAEDSEQLASGQEAGDPGCLKPLHEKDSESGGGKD TT48WR6 TT Successful TT48WR6 FM Integrin TT48WR6 KE hsa04015:Rap1 signaling pathway; hsa04514:Cell adhesion molecules (CAMs); hsa04650:Natural killer cell mediated cytotoxicity; hsa04670:Leukocyte transendothelial migration; hsa04810:Regulation of actin cytoskeleton; hsa05144:Malaria; hsa05150:Staphylococcus aureus infection; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05323:Rheumatoid arthritis; hsa05416:Viral myocarditis TT48WR6 RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-216083:Integrin cell surface interactions TTLT9XQ ID TTLT9XQ TTLT9XQ TN Integrin beta-7 (ITGB7) TTLT9XQ UP P26010 TTLT9XQ UC ITB7_HUMAN TTLT9XQ BC Integrin TTLT9XQ SN Gut homing receptor beta subunit TTLT9XQ GN ITGB7 TTLT9XQ FC Integrin alpha-4/beta-7 interacts with the cell surface adhesion molecules MADCAM1 which is normally expressed by the vascular endothelium of the gastrointestinal tract. Interacts also with VCAM1 and fibronectin, an extracellular matrix component. It recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin. Interactions involves the tripeptide L-D-T in MADCAM1, and L-D-V in fibronectin. Binds to HIV-1 gp120, thereby allowing the virus to enter GALT, which is thought to be the major trigger of AIDS disease. Interaction would involve a tripeptide L-D-I in HIV-1 gp120. Integrin alpha-E/beta-7 (HML-1) is a receptor for E-cadherin. Integrin alpha-4/beta-7 (Peyer patches-specific homing receptor LPAM-1) is an adhesion molecule that mediates lymphocyte migration and homing to gut-associated lymphoid tissue (GALT). TTLT9XQ PD 3V4V; 3V4P; 2BRQ TTLT9XQ SQ MVALPMVLVLLLVLSRGESELDAKIPSTGDATEWRNPHLSMLGSCQPAPSCQKCILSHPSCAWCKQLNFTASGEAEARRCARREELLARGCPLEELEEPRGQQEVLQDQPLSQGARGEGATQLAPQRVRVTLRPGEPQQLQVRFLRAEGYPVDLYYLMDLSYSMKDDLERVRQLGHALLVRLQEVTHSVRIGFGSFVDKTVLPFVSTVPSKLRHPCPTRLERCQSPFSFHHVLSLTGDAQAFEREVGRQSVSGNLDSPEGGFDAILQAALCQEQIGWRNVSRLLVFTSDDTFHTAGDGKLGGIFMPSDGHCHLDSNGLYSRSTEFDYPSVGQVAQALSAANIQPIFAVTSAALPVYQELSKLIPKSAVGELSEDSSNVVQLIMDAYNSLSSTVTLEHSSLPPGVHISYESQCEGPEKREGKAEDRGQCNHVRINQTVTFWVSLQATHCLPEPHLLRLRALGFSEELIVELHTLCDCNCSDTQPQAPHCSDGQGHLQCGVCSCAPGRLGRLCECSVAELSSPDLESGCRAPNGTGPLCSGKGHCQCGRCSCSGQSSGHLCECDDASCERHEGILCGGFGRCQCGVCHCHANRTGRACECSGDMDSCISPEGGLCSGHGRCKCNRCQCLDGYYGALCDQCPGCKTPCERHRDCAECGAFRTGPLATNCSTACAHTNVTLALAPILDDGWCKERTLDNQLFFFLVEDDARGTVVLRVRPQEKGADHTQAIVLGCVGGIVAVGLGLVLAYRLSVEIYDRREYSRFEKEQQQLNWKQDSNPLYKSAITTTINPRFQEADSPTL TTLT9XQ TT Successful TTLT9XQ KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04514:Cell adhesion molecules (CAMs); hsa04672:Intestinal immune network for IgA production; hsa04810:Regulation of actin cytoskeleton; hsa05202:Transcriptional misregulation in cancer; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTLT9XQ RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-216083:Integrin cell surface interactions TT93WF5 ID TT93WF5 TT93WF5 TN Interferon-gamma (IFNG) TT93WF5 UP P01579 TT93WF5 UC IFNG_HUMAN TT93WF5 BC Cytokine: interferon TT93WF5 SN Interferon gamma; Immune interferon; IFN-gamma TT93WF5 GN IFNG TT93WF5 FC Produced by lymphocytes activated by specific antigens or mitogens. IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions. It is a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. TT93WF5 PD 6E3L; 6E3K; 3BES; 1HIG; 1FYH TT93WF5 SQ MKYTSYILAFQLCIVLGSLGCYCQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ TT93WF5 TT Successful TT93WF5 FM Interferon TT93WF5 KE hsa03050:Proteasome; hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04140:Regulation of autophagy; hsa04350:TGF-beta signaling pathway; hsa04380:Osteoclast differentiation; hsa04612:Antigen processing and presentation; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04940:Type I diabetes mellitus; hsa05132:Salmonella infection; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05321:Inflammatory bowel disease (IBD); hsa05322:Systemic lupus erythematosus; hsa05323:Rheumatoid arthritis; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease TT93WF5 RC R-HSA-877300:Interferon gamma signaling; R-HSA-877312:Regulation of IFNG signaling TTWOTEA ID TTWOTEA TTWOTEA TN Interleukin 1 receptor type 1 (IL1R1) TTWOTEA UP P14778 TTWOTEA UC IL1R1_HUMAN TTWOTEA BC Cytokine receptor TTWOTEA SN p80; Interleukin-1 receptor type I; Interleukin-1 receptor type 1; Interleukin-1 receptor alpha; IL1RT1; IL1RA; IL1R; IL-1RT1; IL-1RT-1; IL-1R-alpha; IL-1R-1; CD121a; CD121 antigen-like family member A TTWOTEA GN IL1R1 TTWOTEA FC Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the coreceptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. Involved in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells. TTWOTEA PD 4GAF; 4DEP; 1ITB; 1IRA; 1G0Y TTWOTEA SQ MKVLLRLICFIALLISSLEADKCKEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKISAKFVENEPNLCYNAQAIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPTRPVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRFYKHPFTCFAKNTHGIDAAYIQLIYPVTNFQKHMIGICVTLTVIIVCSVFIYKIFKIDIVLWYRDSCYDFLPIKASDGKTYDAYILYPKTVGEGSTSDCDIFVFKVLPEVLEKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSWLGGSSEEQIAMYNALVQDGIKVVLLELEKIQDYEKMPESIKFIKQKHGAIRWSGDFTQGPQSAKTRFWKNVRYHMPVQRRSPSSKHQLLSPATKEKLQREAHVPLG TTWOTEA TT Successful TTWOTEA FM Immunoglobulin TTWOTEA KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04210:Apoptosis; hsa04380:Osteoclast differentiation; hsa04640:Hematopoietic cell lineage; hsa04750:Inflammatory mediator regulation of TRP channels; hsa05146:Amoebiasis; hsa05166:HTLV-I infection TTWOTEA RC R-HSA-446652:Interleukin-1 signaling TT10Y9E ID TT10Y9E TT10Y9E TN Interleukin 2 receptor alpha (IL2RA) TT10Y9E UP P01589 TT10Y9E UC IL2RA_HUMAN TT10Y9E BC Cytokine receptor TT10Y9E SN TAC antigen; Interleukin-2 receptor subunit alpha; IL2-RA; IL-2R subunit alpha; IL-2-RA; IL-2 receptor subunit alpha; IL-2 receptor alpha subunit; CD25 antigen; CD25 TT10Y9E GN IL2RA TT10Y9E FC The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells. Receptor for interleukin-2. TT10Y9E PD 3NFP; 3IU3; 2ERJ; 2B5I; 1Z92 TT10Y9E SQ MDSYLLMWGLLTFIMVPGCQAELCDDDPPEIPHATFKAMAYKEGTMLNCECKRGFRRIKSGSLYMLCTGNSSHSSWDNQCQCTSSATRNTTKQVTPQPEEQKERKTTEMQSPMQPVDQASLPGHCREPPPWENEATERIYHFVVGQMVYYQCVQGYRALHRGPAESVCKMTHGKTRWTQPQLICTGEMETSQFPGEEKPQASPEGRPESETSCLVTTTDFQIQTEMAATMETSIFTTEYQVAVAGCVFLLISVLLLSGLTWQRRQRKSRRTI TT10Y9E TT Successful TT10Y9E FM Cytokine receptor TT10Y9E KE hsa04060:Cytokine-cytokine receptor interaction; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05162:Measles; hsa05166:HTLV-I infection TT10Y9E RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-451927:Interleukin-2 signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-912526:Interleukin receptor SHC signaling TTDWHC3 ID TTDWHC3 TTDWHC3 TN Interleukin 4 receptor alpha (IL4R) TTDWHC3 UP P24394 TTDWHC3 UC IL4RA_HUMAN TTDWHC3 BC Cytokine receptor TTDWHC3 SN Interleukin-4 receptor subunit alpha; IL4RA; IL-4RA; IL-4R-alpha; IL-4R subunit alpha; IL-4 receptor subunit alpha; CD124 antigen; CD124; 582J2.1 TTDWHC3 GN IL4R TTDWHC3 FC Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2. Receptor for both interleukin 4 and interleukin 13. TTDWHC3 PD 5E4E; 3BPO; 3BPN; 3BPL; 1ITE TTDWHC3 SQ MGWLCSGLLFPVSCLVLLQVASSGNMKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWAGQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNYLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLRIAASTLKSGISYRARVRAWAQCYNTTWSEWSPSTKWHNSYREPFEQHLLLGVSVSCIVILAVCLLCYVSITKIKKEWWDQIPNPARSRLVAIIIQDAQGSQWEKRSRGQEPAKCPHWKNCLTKLLPCFLEHNMKRDEDPHKAAKEMPFQGSGKSAWCPVEISKTVLWPESISVVRCVELFEAPVECEEEEEVEEEKGSFCASPESSRDDFQEGREGIVARLTESLFLDLLGEENGGFCQQDMGESCLLPPSGSTSAHMPWDEFPSAGPKEAPPWGKEQPLHLEPSPPASPTQSPDNLTCTETPLVIAGNPAYRSFSNSLSQSPCPRELGPDPLLARHLEEVEPEMPCVPQLSEPTTVPQPEPETWEQILRRNVLQHGAAAAPVSAPTSGYQEFVHAVEQGGTQASAVVGLGPPGEAGYKAFSSLLASSAVSPEKCGFGASSGEEGYKPFQDLIPGCPGDPAPVPVPLFTFGLDREPPRSPQSSHLPSSSPEHLGLEPGEKVEDMPKPPLPQEQATDPLVDSLGSGIVYSALTCHLCGHLKQCHGQEDGGQTPVMASPCCGCCCGDRSSPPTTPLRAPDPSPGGVPLEASLCPASLAPSGISEKSKSSSSFHPAPGNAQSSSQTPKIVNFVSVGPTYMRVS TTDWHC3 TT Successful TTDWHC3 FM Cytokine receptor TTDWHC3 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05321:Inflammatory bowel disease (IBD) TTRYK0X ID TTRYK0X TTRYK0X TN Interleukin-1 beta (IL1B) TTRYK0X UP P01584 TTRYK0X UC IL1B_HUMAN TTRYK0X BC Cytokine: interleukin TTRYK0X SN IL1F2; IL-1beta; IL-1 beta; Catabolin TTRYK0X GN IL1B TTRYK0X FC Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. Potent proinflammatory cytokine. TTRYK0X PD 9ILB; 7I1B; 6I1B; 5MVZ; 5I1B TTRYK0X SQ MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS TTRYK0X TT Successful TTRYK0X FM Interleukin TTRYK0X KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04210:Apoptosis; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04640:Hematopoietic cell lineage; hsa04668:TNF signaling pathway; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04940:Type I diabetes mellitus; hsa05010:Alzheimer's disease; hsa05020:Prion diseases; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis; hsa05332:Graft-versus-host disease TTRYK0X RC R-HSA-446652:Interleukin-1 signaling; R-HSA-448706:Interleukin-1 processing; R-HSA-5660668:CLEC7A/inflammasome pathway TTRTK6Y ID TTRTK6Y TTRTK6Y TN Interleukin-12 alpha (IL12A) TTRTK6Y UP P29459 TTRTK6Y UC IL12A_HUMAN TTRTK6Y BC Cytokine: interleukin TTRTK6Y SN NKSF1; NKSF; NK cell stimulatory factor chain 1; NK cell stimulatory factor; Interleukin-12 subunit alpha; IL-12A; IL-12 subunit p35; IL-12; Cytotoxic lymphocyte maturation factor 35 kDa subunit; CLMF p35 TTRTK6Y GN IL12A TTRTK6Y FC Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC. TTRTK6Y PD 3HMX; 1F45 TTRTK6Y SQ MCPARSLLLVATLVLLDHLSLARNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS TTRTK6Y TT Successful TTRTK6Y FM Interleukin TTRTK6Y KE hsa04060:Cytokine-cytokine receptor interaction; hsa04620:Toll-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04940:Type I diabetes mellitus; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05321:Inflammatory bowel disease (IBD); hsa05330:Allograft rejection TTG0MT6 ID TTG0MT6 TTG0MT6 TN Interleukin-17 (IL17) TTG0MT6 UP Q16552 TTG0MT6 UC IL17_HUMAN TTG0MT6 BC Cytokine: interleukin TTG0MT6 SN Interleukin-17A; IL-17A; IL-17; Cytotoxic T-lymphocyte-associated antigen 8; Cytotoxic T lymphocyte-associated antigen 8; CTLA8; CTLA-8 TTG0MT6 GN IL17A TTG0MT6 FC The heterodimer formed by IL17A and IL17F is a ligand for the heterodimeric complex formed by IL17RA and IL17RC. Involved in inducing stromal cells to produce proinflammatory and hematopoietic cytokines. Ligand for IL17RA and IL17RC. TTG0MT6 PD 5VB9; 5NAN; 5N92; 5N7W; 5HI5 TTG0MT6 SQ MTPGKTSLVSLLLLLSLEAIVKAGITIPRNPGCPNSEDKNFPRTVMVNLNIHNRNTNTNPKRSSDYYNRSTSPWNLHRNEDPERYPSVIWEAKCRHLGCINADGNVDYHMNSVPIQQEILVLRREPPHCPNSFRLEKILVSVGCTCVTPIVHHVA TTG0MT6 TT Successful TTG0MT6 FM Interleukin TTG0MT6 KE hsa04060:Cytokine-cytokine receptor interaction; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis TTPREZD ID TTPREZD TTPREZD TN Interleukin-5 (IL5) TTPREZD UP P05113 TTPREZD UC IL5_HUMAN TTPREZD BC Cytokine: interleukin TTPREZD SN TRF protein; T-cell replacing factor; IL-5; Eosinophil differentiation factor; B-cell differentiation factor I; B cell differentiation factor I TTPREZD GN IL5 TTPREZD FC Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells. TTPREZD PD 3VA2; 3QT2; 1HUL TTPREZD SQ MRMLLHLSLLALGAAYVYAIPTEIPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQGIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWIIES TTPREZD TT Successful TTPREZD FM Growth factor TTPREZD KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05310:Asthma; hsa05320:Autoimmune thyroid disease; hsa05321:Inflammatory bowel disease (IBD); hsa05330:Allograft rejection TTPREZD RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-912526:Interleukin receptor SHC signaling TTT1V78 ID TTT1V78 TTT1V78 TN Interleukin-6 (IL6) TTT1V78 UP P05231 TTT1V78 UC IL6_HUMAN TTT1V78 BC Cytokine: interleukin TTT1V78 SN Interferon beta-2; IL-6; IFNB2; IFN-beta-2; Hybridoma growth factor; CTL differentiation factor; CDF; BSF-2; B-cell stimulatory factor 2 TTT1V78 GN IL6 TTT1V78 FC It is a potent inducer of the acute phase response. Plays an essential role in the final differentiation of B-cells into Ig-secreting cells Involved in lymphocyte and monocyte differentiation. Acts on B-cells, T-cells, hepatocytes, hematopoietic progenitor cells and cells of the CNS. Required for the generation of T(H)17 cells. Also acts as a myokine. It is discharged into the bloodstream after muscle contraction and acts to increase the breakdown of fats and to improve insulin resistance. It induces myeloma and plasmacytoma growth and induces nerve cells differentiation. Cytokine with a wide variety of biological functions. TTT1V78 PD 5FUC; 4ZS7; 4O9H; 4NI9; 4NI7 TTT1V78 SQ MNSFSTSAFGPVAFSLGLLLVLPAAFPAPVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM TTT1V78 TT Successful TTT1V78 FM Interleukin TTT1V78 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04668:TNF signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05020:Prion diseases; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis; hsa05332:Graft-versus-host disease; hsa05410:Hypertrophic cardiomyopathy (HCM) TTT1V78 RC R-HSA-1059683:Interleukin-6 signaling; R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-112411:MAPK1 (ERK2) activation; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP) TTCTE1G ID TTCTE1G TTCTE1G TN Interleukin-8 (IL8) TTCTE1G UP P10145 TTCTE1G UC IL8_HUMAN TTCTE1G BC Cytokine: interleukin TTCTE1G SN T-cell chemotactic factor; Protein 3-10C; Neutrophil-activating protein 1; NAP-1; Monocyte-derived neutrophil-activating peptide; Monocyte-derived neutrophil chemotactic factor; MONAP; MDNCF; IL8; IL-8; Granulocyte chemotactic protein 1; GCP-1; Emoctakin; Chemokine (C-X-C motif) ligand 8; C-X-C motif chemokine 8 TTCTE1G GN CXCL8 TTCTE1G FC IL-8 is a chemotactic factor that attracts neutrophils, basophils, and T-cells, but not monocytes. It is also involved in neutrophil activation. It is released from several cell types in response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold higher activity on neutrophil activation, IL-8(5-77) has increased activity on neutrophil activation and IL-8(7-77) has a higher affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77), respectively. TTCTE1G PD 5WDZ; 5D14; 4XDX; 3IL8; 2IL8 TTCTE1G SQ MTSKLAVALLAAFLISAALCEGAVLPRSAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS TTCTE1G TT Successful TTCTE1G FM Intercrine-alpha family TTCTE1G KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05142:Chagas disease (American trypanosomiasis); hsa05144:Malaria; hsa05146:Amoebiasis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05219:Bladder cancer; hsa05323:Rheumatoid arthritis TTCTE1G RC R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-375276:Peptide ligand-binding receptors; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-380994:ATF4 activates genes; R-HSA-418594:G alpha (i) signalling events TTXWASR ID TTXWASR TTXWASR TN Intestinal maltase-glucoamylase (MGAM) TTXWASR UP O43451 TTXWASR UC MGA_HUMAN TTXWASR BC Glycosylase TTXWASR SN MGAM TTXWASR GN MGAM TTXWASR FC May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing. TTXWASR PD 3TOP; 3TON; 3L4Z; 3L4Y; 3L4X TTXWASR SQ MARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTPDPGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDNGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWSIKIRDEEKIDCYPDENGASAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADISLKSSVYANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNKNRYEVPVPLNIPSMPSSTPEGQLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFSDMFIRISTRLPSKYLYGFGETEHRSYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPLPALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEIASLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAISGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYVAFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDASLNHPPYMPHLESRDRGLSSKTLCMESQQILPDGSLVQHYNVHNLYGWSQTRPTYEAVQEVTGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFFQDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDVAFVNISRTVLQTRYTLLPYLYTLMHKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRARWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRQKFMGFKIALDDEGTAGGWLFWDDGQSIDTYGKGLYYLASFSASQNTMQSHIIFNNYITGTNPLKLGYIEIWGVGSVPVTSVSISVSGMVITPSFNNDPTTQVLSIDVTDRNISLHNFTSLTWISTL TTXWASR TT Successful TTXWASR KE hsa00052:Galactose metabolism; hsa00500:Starch and sucrose metabolism; hsa01100:Metabolic pathways; hsa04973:Carbohydrate digestion and absorption TT6DM01 ID TT6DM01 TT6DM01 TN Janus kinase 1 (JAK-1) TT6DM01 UP P23458 TT6DM01 UC JAK1_HUMAN TT6DM01 BC Kinase TT6DM01 SN Tyrosine-protein kinase JAK1; JAK1B; JAK1A TT6DM01 GN JAK1 TT6DM01 FC Kinase partner for the interleukin (IL)-2 receptor as well as interleukin (IL)-10 receptor. Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. TT6DM01 EC EC 2.7.10.2 TT6DM01 PD 6N7D; 6N7C; 6N7B; 6N7A; 6N79 TT6DM01 SQ MQYLNIKEDCNAMAFCAKMRSSKKTEVNLEAPEPGVEVIFYLSDREPLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKKIPDATPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLENKHKKDEEKNKIREEWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKGRYSLHGSDRSFPSLGDLMSHLKKQILRTDNISFMLKRCCQPKPREISNLLVATKKAQEWQPVYPMSQLSFDRILKKDLVQGEHLGRGTRTHIYSGTLMDYKDDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDPGIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK TT6DM01 TT Successful TT6DM01 FM Kinase TT6DM01 KE hsa04151:PI3K-Akt signaling pathway; hsa04380:Osteoclast differentiation; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04630:Jak-STAT signaling pathway; hsa05140:Leishmaniasis; hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05212:Pancreatic cancer TT6DM01 RC R-HSA-1059683:Interleukin-6 signaling; R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-112411:MAPK1 (ERK2) activation; R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1169408:ISG15 antiviral mechanism; R-HSA-1266695:Interleukin-7 signaling; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-451927:Interleukin-2 signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-877300:Interferon gamma signaling; R-HSA-877312:Regulation of IFNG signaling; R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912526:Interleukin receptor SHC signaling; R-HSA-912694:Regulation of IFNA signaling TTUE541 ID TTUE541 TTUE541 TN Leukocyte surface antigen Leu-16 (CD20) TTUE541 UP P11836 TTUE541 UC CD20_HUMAN TTUE541 BC CD20 calcium channel TTUE541 SN Membrane-spanning 4-domains subfamily A member 1; Leu-16; Bp35; B-lymphocyte surface antigen B1; B-lymphocyte antigen CD20 TTUE541 GN MS4A1 TTUE541 FC Functions as a store-operated calcium (SOC) channel component promoting calcium influx after activation by the B-cell receptor/BCR. B-lymphocyte-specific membrane protein that plays a role in the regulation of cellular calcium influx necessary for the development, differentiation, and activation of B-lymphocytes. TTUE541 PD 3PP4; 3BKY; 2OSL; 1S8B TTUE541 SQ MTTPRNSVNGTFPAEPMKGPIAMQSGPKPLFRRMSSLVGPTQSFFMRESKTLGAVQIMNGLFHIALGGLLMIPAGIYAPICVTVWYPLWGGIMYIISGSLLAATEKNSRKCLVKGKMIMNSLSLFAAISGMILSIMDILNIKISHFLKMESLNFIRAHTPYINIYNCEPANPSEKNSPSTQYCYSIQSLFLGILSVMLIFAFFQELVIAGIVENEWKRTCSRPKSNIVLLSAEEKKEQTIEIKEEVVGLTETSSQPKNEEDIEIIPIQEEEEEETETNFPEPPQDQESSPIENDSSP TTUE541 TT Successful TTUE541 FM CD20 calcium channel TTUE541 KE hsa04640:Hematopoietic cell lineage TTOF3WZ ID TTOF3WZ TTOF3WZ TN Lipoprotein lipase (LPL) TTOF3WZ UP P06858 TTOF3WZ UC LIPL_HUMAN TTOF3WZ BC Carboxylic ester hydrolase TTOF3WZ SN LIPD TTOF3WZ GN LPL TTOF3WZ FC Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans. Key enzyme in triglyceride metabolism. TTOF3WZ EC EC 3.1.1.34 TTOF3WZ PD 6OB0; 6OAZ; 6OAU; 6E7K TTOF3WZ SQ MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG TTOF3WZ TT Successful TTOF3WZ FM Carboxylic ester hydrolase TTOF3WZ KE hsa00561:Glycerolipid metabolism; hsa03320:PPAR signaling pathway; hsa05010:Alzheimer's disease TTOF3WZ RC R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-975634:Retinoid metabolism and transport TTEDJN4 ID TTEDJN4 TTEDJN4 TN Low-affinity nerve growth factor receptor (NGFR) TTEDJN4 UP P08138 TTEDJN4 UC TNR16_HUMAN TTEDJN4 BC Cytokine receptor TTEDJN4 SN p75 ICD; Tumor necrosis factor receptor superfamily member 16; TNFRSF16; P75neurotrophin receptor (p75(NTR)); P75NTR; P75ICD; NGFreceptor; NGF-P75 receptor; NGF receptor; Lowaffinity neurotrophin receptor p75NTR; Low affinity neurotrophin receptor p75NTR; Gp80-LNGFR; CD271; 75kD-neurotrophin receptor TTEDJN4 GN NGFR TTEDJN4 FC Low affinity receptor which can bind to NGF, BDNF, NT-3, and NT-4. Can mediate cell survival as well as cell death of neural cells. Necessary for the circadian oscillation of the clock genes ARNTL/BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver. Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake. TTEDJN4 PD 5ZGG; 3EWV; 2N97; 2N83; 2N80 TTEDJN4 SQ MGAGATGRAMDGPRLLLLLLLGVSLGGAKEACPTGLYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDSVTFSDVVSATEPCKPCTECVGLQSMSAPCVEADDAVCRCAYGYYQDETTGRCEACRVCEAGSGLVFSCQDKQNTVCEECPDGTYSDEANHVDPCLPCTVCEDTERQLRECTRWADAECEEIPGRWITRSTPPEGSDSTAPSTQEPEAPPEQDLIASTVAGVVTTVMGSSQPVVTRGTTDNLIPVYCSILAAVVVGLVAYIAFKRWNSCKQNKQGANSRPVNQTPPPEGEKLHSDSGISVDSQSLHDQQPHTQTASGQALKGDGGLYSSLPPAKREEVEKLLNGSAGDTWRHLAGELGYQPEHIDSFTHEACPVRALLASWATQDSATLDALLAALRRIQRADLVESLCSESTATSPV TTEDJN4 TT Successful TTEDJN4 FM Cytokine receptor TTEDJN4 KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa05202:Transcriptional misregulation in cancer TTEDJN4 RC R-HSA-193634:Axonal growth inhibition (RHOA activation); R-HSA-193648:NRAGE signals death through JNK; R-HSA-193670:p75NTR negatively regulates cell cycle via SC1; R-HSA-193692:Regulated proteolysis of p75NTR; R-HSA-205025:NADE modulates death signalling; R-HSA-205043:NRIF signals cell death from the nucleus; R-HSA-209543:p75NTR recruits signalling complexes; R-HSA-209560:NF-kB is activated and signals survival; R-HSA-209563:Axonal growth stimulation TTYT93M ID TTYT93M TTYT93M TN MAP kinase p38 (MAPK12) TTYT93M UP P53778 TTYT93M UC MK12_HUMAN TTYT93M BC Kinase TTYT93M SN Stress-activated protein kinase 3; SAPK3; Mitogen-activated proteinkinase p38 gamma; Mitogen-activated proteinkinase 12; MAPK12; Extracellular signal-regulated kinase 6; ERK6; ERK5; ERK-6 TTYT93M GN MAPK12 TTYT93M FC Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down-regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma- radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12-signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. TTYT93M EC EC 2.7.11.24 TTYT93M PD 4QUM; 1CM8 TTYT93M SQ MSSPPPARSGFYRQEVTKTAWEVRAVYRDLQPVGSGAYGAVCSAVDGRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLMKHEKLGEDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMKVTGTPPAEFVQRLQSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLVLDAEQRVTAGEALAHPYFESLHDTEDEPQVQKYDDSFDDVDRTLDEWKRVTYKEVLSFKPPRQLGARVSKETPL TTYT93M TT Successful TTYT93M KE hsa04010:MAPK signaling pathway; hsa04015:Rap1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04114:Oocyte meiosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04723:Retrograde endocannabinoid signaling; hsa04728:Dopaminergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04917:Prolactin signaling pathway; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05164:Influenza A; hsa05169:Epstein-Barr virus infection; hsa05205:Proteoglycans in cancer TTYT93M RC R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-171007:p38MAPK events; R-HSA-2151209:Activation of PPARGC1A (PGC-1alpha) by phosphorylation; R-HSA-375170:CDO in myogenesis; R-HSA-376172:DSCAM interactions; R-HSA-4420097:VEGFA-VEGFR2 Pathway TT7HC21 ID TT7HC21 TT7HC21 TN Membrane copper amine oxidase (AOC3) TT7HC21 UP Q16853 TT7HC21 UC AOC3_HUMAN TT7HC21 BC CH-NH(2) donor oxidoreductase TT7HC21 SN Vascular adhesion protein-1; Vascular adhesion protein 1; VAP1; VAP-1; Semicarbazide-sensitive amine oxidase; SSAO; Membrane primary amine oxidase; HPAO; Copper amine oxidase TT7HC21 GN AOC3 TT7HC21 FC Has semicarbazide-sensitive (SSAO) monoamine oxidase activity. May play a role in adipogenesis. Cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. TT7HC21 EC EC 1.4.3.21 TT7HC21 PD 4BTY; 4BTX; 4BTW; 3ALA; 2Y74 TT7HC21 SQ MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLVYEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQAPKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFHPSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVWAEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSADSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN TT7HC21 TT Successful TT7HC21 KE hsa00260:Glycine, serine and threonine metabolism; hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism; hsa00410:beta-Alanine metabolism; hsa01100:Metabolic pathways TTCQ21Y ID TTCQ21Y TTCQ21Y TN Methylmalonyl-CoA mutase (MMUT) TTCQ21Y UP P22033 TTCQ21Y UC MUTA_HUMAN TTCQ21Y BC Intramolecular transferases TTCQ21Y SN Methylmalonyl-CoA isomerase; MUT; MCM TTCQ21Y GN MUT TTCQ21Y FC Involved in the degradation of several amino acids, odd- chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species. TTCQ21Y EC EC 5.4.99.2 TTCQ21Y PD 3BIC; 2XIQ; 2XIJ TTCQ21Y SQ MLRAKNQLFLLSPHYLRQVKESSGSRLIQQRLLHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQSV TTCQ21Y TT Successful TTCQ21Y KE hsa00280:Valine, leucine and isoleucine degradation; hsa00630:Glyoxylate and dicarboxylate metabolism; hsa00640:Propanoate metabolism; hsa01100:Metabolic pathways; hsa01200:Carbon metabolism TTCQ21Y RC R-HSA-196741:Cobalamin (Cbl, vitamin B12) transport and metabolism TT26PHO ID TT26PHO TT26PHO TN Mineralocorticoid receptor (MR) TT26PHO UP P08235 TT26PHO UC MCR_HUMAN TT26PHO BC Nuclear hormone receptor TT26PHO SN Nuclear receptor subfamily 3 group C member 2; Mineralocorticoid receptor; MLR; MCR; Inner ear mineralocorticoid receptor; Delta TT26PHO GN NR3C2 TT26PHO FC Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels. Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. TT26PHO PD 6GGG; 6GG8; 6GEV; 5MWY; 5MWP TT26PHO SQ METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNSTQGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYEQQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAVVKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPNVENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSPANINNSRCSVSSPSNTNNRSTLSSPAASTVGSICSPVNNAFSYTASGTSAGSSTLRDVVPSPDTQEKGAQEVPFPKTEEVESAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNSKINSDSSFSVPIKQESTKHSCSGTSFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGFDGNCEGSGFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSARDQSFQHLSSFPPVNTLVESWKSHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPSKICLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRLQKCLQAGMNLGARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEEGTTYIAPAKEPSVNTALVPQLSTISRALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKCPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAMLVEIISDQLPKVESGNAKPLYFHRK TT26PHO TT Successful TT26PHO FM Zinc finger TT26PHO KE hsa04960:Aldosterone-regulated sodium reabsorption TTZ9SOR ID TTZ9SOR TTZ9SOR TN Muscarinic acetylcholine receptor M1 (CHRM1) TTZ9SOR UP P11229 TTZ9SOR UC ACM1_HUMAN TTZ9SOR BC GPCR rhodopsin TTZ9SOR SN M1 receptor TTZ9SOR GN CHRM1 TTZ9SOR FC Primary transducing effect is Pi turnover. The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. TTZ9SOR PD 6OIJ; 5CXV TTZ9SOR SQ MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPRSSPNTVKRPTKKGRDRAGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGSVHRTPSRQC TTZ9SOR TT Successful TTZ9SOR FM GPCR rhodopsin TTZ9SOR KE hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04725:Cholinergic synapse; hsa04810:Regulation of actin cytoskeleton TTZ9SOR RC R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-416476:G alpha (q) signalling events TTYEG6Q ID TTYEG6Q TTYEG6Q TN Muscarinic acetylcholine receptor M2 (CHRM2) TTYEG6Q UP P08172 TTYEG6Q UC ACM2_HUMAN TTYEG6Q BC GPCR rhodopsin TTYEG6Q SN M2 receptor; CHRM2 TTYEG6Q GN CHRM2 TTYEG6Q FC The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol. TTYEG6Q PD 6OIK; 5ZKC; 5ZKB; 5ZK8; 5ZK3 TTYEG6Q SQ MNNSTNSSNNSLALTSPYKTFEVVFIVLVAGSLSLVTIIGNILVMVSIKVNRHLQTVNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGPVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQFIVGVRTVEDGECYIQFFSNAAVTFGTAIAAFYLPVIIMTVLYWHISRASKSRIKKDKKEPVANQDPVSPSLVQGRIVKPNNNNMPSSDDGLEHNKIQNGKAPRDPVTENCVQGEEKESSNDSTSVSAVASNMRDDEITQDENTVSTSLGHSKDENSKQTCIRIGTKTPKSDSCTPTNTTVEVVGSSGQNGDEKQNIVARKIVKMTKQPAKKKPPPSREKKVTRTILAILLAFIITWAPYNVMVLINTFCAPCIPNTVWTIGYWLCYINSTINPACYALCNATFKKTFKHLLMCHYKNIGATR TTYEG6Q TT Successful TTYEG6Q KE hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04725:Cholinergic synapse; hsa04810:Regulation of actin cytoskeleton TTYEG6Q RC R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-418594:G alpha (i) signalling events TTQ3JTF ID TTQ3JTF TTQ3JTF TN Muscarinic acetylcholine receptor M4 (CHRM4) TTQ3JTF UP P08173 TTQ3JTF UC ACM4_HUMAN TTQ3JTF BC GPCR rhodopsin TTQ3JTF SN M4 receptor; CHRM4 TTQ3JTF GN CHRM4 TTQ3JTF FC The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is inhibition of adenylate cyclase. TTQ3JTF PD 6D9H; 5DSG TTQ3JTF SQ MANFTPVNGSSGNQSVRLVTSSSHNRYETVEMVFIATVTGSLSLVTVVGNILVMLSIKVNRQLQTVNNYFLFSLACADLIIGAFSMNLYTVYIIKGYWPLGAVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPARRTTKMAGLMIAAAWVLSFVLWAPAILFWQFVVGKRTVPDNQCFIQFLSNPAVTFGTAIAAFYLPVVIMTVLYIHISLASRSRVHKHRPEGPKEKKAKTLAFLKSPLMKQSVKKPPPGEAAREELRNGKLEEAPPPALPPPPRPVADKDTSNESSSGSATQNTKERPATELSTTEATTPAMPAPPLQPRALNPASRWSKIQIVTKQTGNECVTAIEIVPATPAGMRPAANVARKFASIARNQVRKKRQMAARERKVTRTIFAILLAFILTWTPYNVMVLVNTFCQSCIPDTVWSIGYWLCYVNSTINPACYALCNATFKKTFRHLLLCQYRNIGTAR TTQ3JTF TT Successful TTQ3JTF KE hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa04810:Regulation of actin cytoskeleton TTQ3JTF RC R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-418594:G alpha (i) signalling events TTCS3P1 ID TTCS3P1 TTCS3P1 TN Mycobacterium D-alanine-D-alanine ligase A (MycB ddl) TTCS3P1 UP P9WP31 TTCS3P1 UC DDL_MYCTU TTCS3P1 BC Carbon-nitrogen ligase TTCS3P1 SN ddlA; D-alanylalanine synthetase A; D-Ala-D-Ala ligase A TTCS3P1 GN MycB ddl TTCS3P1 FC Cell wall formation. TTCS3P1 EC EC 6.3.2.4 TTCS3P1 PD 3LWB TTCS3P1 SQ MSANDRRDRRVRVAVVFGGRSNEHAISCVSAGSILRNLDSRRFDVIAVGITPAGSWVLTDANPDALTITNRELPQVKSGSGTELALPADPRRGGQLVSLPPGAGEVLESVDVVFPVLHGPYGEDGTIQGLLELAGVPYVGAGVLASAVGMDKEFTKKLLAADGLPVGAYAVLRPPRSTLHRQECERLGLPVFVKPARGGSSIGVSRVSSWDQLPAAVARARRHDPKVIVEAAISGRELECGVLEMPDGTLEASTLGEIRVAGVRGREDSFYDFATKYLDDAAELDVPAKVDDQVAEAIRQLAIRAFAAIDCRGLARVDFFLTDDGPVINEINTMPGFTTISMYPRMWAASGVDYPTLLATMIETTLARGVGLH TTCS3P1 TT Successful TTCS3P1 KE mtu00473:D-Alanine metabolism; mtu00550:Peptidoglycan biosynthesis; mtu01100:Metabolic pathways; mtu01502:Vancomycin resistance TTTJF7V ID TTTJF7V TTTJF7V TN NADH dehydrogenase (MT-ND3) TTTJF7V UP P03897 TTTJF7V UC NU3M_HUMAN TTTJF7V BC NADH/NADPH oxidoreductase TTTJF7V SN ND; NADH-ubiquinone oxidoreductase; NADH; MTND; MT-ND3; MT-ND TTTJF7V GN MT-ND3 TTTJF7V FC Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in thetransfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. TTTJF7V EC EC 7.1.1.2 TTTJF7V PD 5XTD; 5XTC TTTJF7V SQ MNFALILMINTLLALLLMIITFWLPQLNGYMEKSTPYECGFDPMSPARVPFSMKFFLVAITFLLFDLEIALLLPLPWALQTTNLPLMVMSSLLLIIILALSLAYEWLQKGLDWTE TTTJF7V TT Successful TTTJF7V KE hsa00190:Oxidative phosphorylation; hsa01100:Metabolic pathways; hsa05012:Parkinson's disease TT4H1MQ ID TT4H1MQ TT4H1MQ TN Neuronal acetylcholine receptor alpha-4 (CHRNA4) TT4H1MQ UP P43681 TT4H1MQ UC ACHA4_HUMAN TT4H1MQ BC Neurotransmitter receptor TT4H1MQ SN Nicotinic acetylcholine receptor alpha4; CHRNA4; Alpha-4 nAChR TT4H1MQ GN CHRNA4 TT4H1MQ FC After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasmamembrane permeable to sodium ions. TT4H1MQ PD 6CNK; 6CNJ; 5KXI; 2LLY; 2GVT TT4H1MQ SQ MELGGPGAPRLLPPLLLLLGTGLLRASSHVETRAHAEERLLKKLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPADYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFHDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVNMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPTWVRRVFLDIVPRLLLMKRPSVVKDNCRRLIESMHKMASAPRFWPEPEGEPPATSGTQSLHPPSPSFCVPLDVPAEPGPSCKSPSDQLPPQQPLEAEKASPHPSPGPCRPPHGTQAPGLAKARSLSVQHMSSPGEAVEGGVRCRSRSIQYCVPRDDAAPEADGQAAGALASRNTHSAELPPPDQPSPCKCTCKKEPSSVSPSATVKTRSTKAPPPHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAGMI TT4H1MQ TT Successful TT4H1MQ KE hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa05033:Nicotine addiction TT4H1MQ RC R-HSA-629587:Highly sodium permeable acetylcholine nicotinic receptors; R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors; R-HSA-629597:Highly calcium permeable nicotinic acetylcholine receptors TT27RFC ID TT27RFC TT27RFC TN Opioid receptor delta (OPRD1) TT27RFC UP P41143 TT27RFC UC OPRD_HUMAN TT27RFC BC GPCR rhodopsin TT27RFC SN OPRD; Delta-type opioid receptor; Delta opioid receptor; DOR-1; D-OR-1 TT27RFC GN OPRD1 TT27RFC FC Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine. G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. TT27RFC PD 4RWD; 4RWA; 4N6H; 2IQM; 1OZC TT27RFC SQ MEPAPSAGAELQPPLFANASDAYPSACPSAGANASGPPGARSASSLALAIAITALYSAVCAVGLLGNVLVMFGIVRYTKMKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTRPRDGAVVCMLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDIDRRDPLVVAALHLCIALGYANSSLNPVLYAFLDENFKRCFRQLCRKPCGRPDPSSFSRAREATARERVTACTPSDGPGGGAAA TT27RFC TT Successful TT27RFC FM GPCR rhodopsin TT27RFC KE hsa04022:cGMP-PKG signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TT27RFC RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTQW87Y ID TTQW87Y TTQW87Y TN Opioid receptor kappa (OPRK1) TTQW87Y UP P41145 TTQW87Y UC OPRK_HUMAN TTQW87Y BC GPCR rhodopsin TTQW87Y SN OPRK; Kappa-type opioid receptor; Kappa opioid receptor; KOR-1; KOR; K-OR-1 TTQW87Y GN OPRK1 TTQW87Y FC Functions as receptor for various synthetic opioids and for the psychoactive diterpene salvinorin A. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain. Plays a role in mediating reduced physical activity upon treatment with synthetic opioids. Plays a role in the regulation of salivation in response to synthetic opioids. May play a role in arousal and regulation of autonomic and neuroendocrine functions. G-protein coupled opioid receptor that functions as receptor for endogenous alpha-neoendorphins and dynorphins, but has low affinity for beta-endorphins. TTQW87Y PD 6B73; 4DJH; 2IQN; 2A0D TTQW87Y SQ MDSPIQIFRGEPGPTCAPSACLPPNSSAWFPGWAEPDSNGSAGSEDAQLEPAHISPAIPVIITAVYSVVFVVGLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSTVYLMNSWPFGDVLCKIVISIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPLKAKIINICIWLLSSSVGISAIVLGGTKVREDVDVIECSLQFPDDDYSWWDLFMKICVFIFAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNLRRITRLVLVVVAVFVVCWTPIHIFILVEALGSTSHSTAALSSYYFCIALGYTNSSLNPILYAFLDENFKRCFRDFCFPLKMRMERQSTSRVRNTVQDPAYLRDIDGMNKPV TTQW87Y TT Successful TTQW87Y KE hsa04080:Neuroactive ligand-receptor interaction TTQW87Y RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTKWM86 ID TTKWM86 TTKWM86 TN Opioid receptor mu (MOP) TTKWM86 UP P35372 TTKWM86 UC OPRM_HUMAN TTKWM86 BC GPCR rhodopsin TTKWM86 SN hMOP; Mu-type opioid receptor; Mu opioid receptor; Mu opiate receptor; MOR1A; MOR1; MOR-1; M-OR-1 TTKWM86 GN OPRM1 TTKWM86 FC Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone. Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors. The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extent to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15. They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B. Also couples to adenylate cyclase stimulatory G alpha proteins. The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4. Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization. Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction. The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins. The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation. Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling. Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling. Endogenous ligands induce rapid desensitization, endocytosis and recycling whereas morphine induces only low desensitization and endocytosis. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties. Involved in neurogenesis. Isoform 12 couples to GNAS and is proposed to be involved in excitatory effects. Isoform 16 and isoform 17 do not bind agonists but may act through oligomerization with binding-competent OPRM1 isoforms and reduce their ligand binding activity. Receptor for endogenous opioids such as beta-endorphin and endomorphin. TTKWM86 SQ MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRTDLGGRDSLCPPTGSPSMITAITIMALYSIVCVVGLFGNFLVMYVIVRYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP TTKWM86 TT Successful TTKWM86 FM GPCR rhodopsin TTKWM86 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04915:Estrogen signaling pathway; hsa05032:Morphine addiction TTKWM86 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TT9E8HR ID TT9E8HR TT9E8HR TN Osteoclast differentiation factor (ODF) TT9E8HR UP O14788 TT9E8HR UC TNF11_HUMAN TT9E8HR BC Cytokine: tumor necrosis factor TT9E8HR SN Tumor necrosis factor ligand superfamily member 11; TRANCE; TNF-related activation-induced cytokine; Receptor activatorof nuclear factor kappa B ligand; Receptor activator of nuclear factor kappa-B ligand; RANKL; Osteoprotegerin ligand; OPGL; CD254 TT9E8HR GN TNFSF11 TT9E8HR FC Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy. Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts. During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation. Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. TT9E8HR PD 5BNQ; 3URF TT9E8HR SQ MRRASRDYTKYLRGSEEMGGGPGAPHEGPLHAPPPPAPHQPPAASRSMFVALLGLGLGQVVCSVALFFYFRAQMDPNRISEDGTHCIYRILRLHENADFQDTTLESQDTKLIPDSCRRIKQAFQGAVQKELQHIVGSQHIRAEKAMVDGSWLDLAKRSKLEAQPFAHLTINATDIPSGSHKVSLSSWYHDRGWAKISNMTFSNGKLIVNQDGFYYLYANICFRHHETSGDLATEYLQLMVYVTKTSIKIPSSHTLMKGGSTKYWSGNSEFHFYSINVGGFFKLRSGEEISIEVSNPSLLDPDQDATYFGAFKVRDID TT9E8HR TT Successful TT9E8HR FM Tumor necrosis factor TT9E8HR KE hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04380:Osteoclast differentiation; hsa04917:Prolactin signaling pathway; hsa05323:Rheumatoid arthritis TT9E8HR RC R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5669034:TNFs bind their physiological receptors; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway TTXMY0J ID TTXMY0J TTXMY0J TN Pancreatic triacylglycerol lipase (PNLIP) TTXMY0J UP P16233 TTXMY0J UC LIPP_HUMAN TTXMY0J BC Carboxylic ester hydrolase TTXMY0J SN Pancreatic lipase; PTL; PL TTXMY0J GN PNLIP TTXMY0J FC Catalyses the following chemical reaction: triacylglycerol + H2O diacylglycerol + a carboxylate. Acts only on an ester-water interface. TTXMY0J EC EC 3.1.1.3 TTXMY0J PD 1N8S; 1LPB; 1LPA; 1GPL TTXMY0J SQ MLPLWTLSLLLGAVAGKEVCYERLGCFSDDSPWSGITERPLHILPWSPKDVNTRFLLYTNENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGHLDFFPNGGVEMPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGFPCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDASNFARWRYKVSVTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLPRVGASKIIVETNVGKQFNFCSPETVREEVLLTLTPC TTXMY0J TT Successful TTXMY0J KE hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways; hsa04972:Pancreatic secretion; hsa04975:Fat digestion and absorption; hsa04977:Vitamin digestion and absorption TTXMY0J RC R-HSA-975634:Retinoid metabolism and transport TTSKMI8 ID TTSKMI8 TTSKMI8 TN Phosphodiesterase 4D (PDE4D) TTSKMI8 UP Q08499 TTSKMI8 UC PDE4D_HUMAN TTSKMI8 BC Phosphoric diester hydrolase TTSKMI8 SN cAMP-specific 3',5'-cyclic phosphodiesterase 4D; PDE43; DPDE3 TTSKMI8 GN PDE4D TTSKMI8 FC Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. TTSKMI8 EC EC 3.1.4.53 TTSKMI8 PD 6NJJ; 6NJI; 6NJH; 6FW3; 6FTW TTSKMI8 SQ MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPPPPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRAMDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQANFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNFAALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRPMSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAPDDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPLDEQVEEEAVGEEEESQPEACVIDDRSPDT TTSKMI8 TT Successful TTSKMI8 FM Phosphoric diester hydrolases TTSKMI8 KE hsa00230:Purine metabolism; hsa04024:cAMP signaling pathway; hsa05032:Morphine addiction TTSKMI8 RC R-HSA-180024:DARPP-32 events; R-HSA-418555:G alpha (s) signalling events TTZ3IFB ID TTZ3IFB TTZ3IFB TN Phosphogluconate dehydrogenase (PGD) TTZ3IFB UP P52209 TTZ3IFB UC 6PGD_HUMAN TTZ3IFB BC CH-OH donor oxidoreductase TTZ3IFB SN PGDH; 6PGDH; 6-phosphogluconate dehydrogenase, decarboxylating; 6-phosphogluconate dehydrogenase TTZ3IFB GN PGD TTZ3IFB FC Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. TTZ3IFB EC EC 1.1.1.44 TTZ3IFB PD 5UQ9; 4GWK; 4GWG; 2JKV TTZ3IFB SQ MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVVGAQSLKEMVSKLKKPRRIILLVKAGQAVDDFIEKLVPLLDTGDIIIDGGNSEYRDTTRRCRDLKAKGILFVGSGVSGGEEGARYGPSLMPGGNKEAWPHIKTIFQGIAAKVGTGEPCCDWVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFYDGYRHEMLPASLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGTVSSSSYNA TTZ3IFB TT Successful TTZ3IFB FM Short-chain dehydrogenases reductases TTZ3IFB KE hsa00030:Pentose phosphate pathway; hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism TTMF8H9 ID TTMF8H9 TTMF8H9 TN Plasma kallikrein (KLKB1) TTMF8H9 UP P03952 TTMF8H9 UC KLKB1_HUMAN TTMF8H9 BC Peptidase TTMF8H9 SN Plasma prekallikrein; Plasma kallikrein light chain; Plasma kallikrein heavy chain; PKK; Kininogenin; KLK3; Fletcher factor TTMF8H9 GN KLKB1 TTMF8H9 FC It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin. The enzyme cleaves Lys-Arg and Arg-Ser bonds. TTMF8H9 EC EC 3.4.21.34 TTMF8H9 PD 6O1S; 6O1G; 6I44; 5TJX; 5F8Z TTMF8H9 SQ MILFKQATYFISLFATVSCGCLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDMEKRFGCFLKDSVTGTLPKVHRTGAVSGHSLKQCGHQISACHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTNNIRCQFFSYATQTFHKAEYRNNCLLKYSPGGTPTAIKVLSNVESGFSLKPCALSEIGCHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKIESQRNVCLLKTSESGTPSSSTPQENTISGYSLLTCKRTLPEPCHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSLLPEDCKEEKCKCFLRLSMDGSPTRIAYGTQGSSGYSLRLCNTGDNSVCTTKTSTRIVGGTNSSWGEWPWQVSLQVKLTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDVWRIYSGILNLSDITKDTPFSQIKEIIIHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGEIQNILQKVNIPLVTNEECQKRYQDYKITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWILEKTQSSDGKAQMQSPA TTMF8H9 TT Successful TTMF8H9 KE hsa04610:Complement and coagulation cascades TTMF8H9 RC R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-1592389:Activation of Matrix Metalloproteinases TTQL5VC ID TTQL5VC TTQL5VC TN Platelet-activating factor receptor (PTAFR) TTQL5VC UP P25105 TTQL5VC UC PTAFR_HUMAN TTQL5VC BC GPCR rhodopsin TTQL5VC SN PTAFR; PAF-R TTQL5VC GN PTAFR TTQL5VC FC Receptor for platelet activating factor, a chemotactic phospholipid mediator that possesses potent inflammatory, smooth- muscle contractile and hypotensive activity. Seems to mediate its action via a G protein that activates a phosphatidylinositol- calcium second messenger system. TTQL5VC PD 2B0X TTQL5VC SQ MEPHDSSHMDSEFRYTLFPIVYSIIFVLGVIANGYVLWVFARLYPCKKFNEIKIFMVNLTMADMLFLITLPLWIVYYQNQGNWILPKFLCNVAGCLFFINTYCSVAFLGVITYNRFQAVTRPIKTAQANTRKRGISLSLVIWVAIVGAASYFLILDSTNTVPDSAGSGNVTRCFEHYEKGSVPVLIIHIFIVFSFFLVFLIILFCNLVIIRTLLMQPVQQQRNAEVKRRALWMVCTVLAVFIICFVPHHVVQLPWTLAELGFQDSKFHQAINDAHQVTLCLLSTNCVLDPVIYCFLTKKFRKHLTEKFYSMRSSRKCSRATTDTVTEVVVPFNQIPGNSLKN TTQL5VC TT Successful TTQL5VC KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa05150:Staphylococcus aureus infection TTQL5VC RC R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-416476:G alpha (q) signalling events; R-HSA-877300:Interferon gamma signaling TTUV8G9 ID TTUV8G9 TTUV8G9 TN Progesterone receptor (PGR) TTUV8G9 UP P06401 TTUV8G9 UC PRGR_HUMAN TTUV8G9 BC Nuclear hormone receptor TTUV8G9 SN PR; Nuclear receptor subfamily 3 group C member 3; NR3C3 TTUV8G9 GN PGR TTUV8G9 FC Depending on the isoform, progesterone receptor functions as transcriptional activator or repressor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. TTUV8G9 PD 5CC0; 4OAR; 4APU; 4A2J; 3ZRB TTUV8G9 SQ MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGVPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK TTUV8G9 TT Successful TTUV8G9 FM Zinc finger TTUV8G9 KE hsa04114:Oocyte meiosis; hsa04914:Progesterone-mediated oocyte maturation TTUV8G9 RC R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-383280:Nuclear Receptor transcription pathway TTBRG7E ID TTBRG7E TTBRG7E TN Proprotein convertase subtilisin/kexin type 9 (PCSK9) TTBRG7E UP Q8NBP7 TTBRG7E UC PCSK9_HUMAN TTBRG7E BC Peptidase TTBRG7E SN Subtilisin/kexin-like protease PC9; Proprotein convertase 9; PC9; Neural apoptosis-regulated convertase 1; NARC1; NARC-1 TTBRG7E GN PCSK9 TTBRG7E FC Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways. TTBRG7E EC EC 3.4.21.- TTBRG7E PD 6MV5; 6F5G; 6E4Z; 6E4Y; 5VLP TTBRG7E SQ MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEGAVTAVAICCRSRHLAQASQELQ TTBRG7E TT Successful TTOFYT1 ID TTOFYT1 TTOFYT1 TN Prostacyclin receptor (PTGIR) TTOFYT1 UP P43119 TTOFYT1 UC PI2R_HUMAN TTOFYT1 BC GPCR rhodopsin TTOFYT1 SN Prostanoid IP receptor; Prostaglandin I2 receptor; PRIPR; PGI2 receptor; PGI receptor; IP prostanoid receptor TTOFYT1 GN PTGIR TTOFYT1 FC The activity of this receptor is mediated by G(s) proteins which activate adenylate cyclase. Receptor for prostacyclin (prostaglandin I2 or PGI2). TTOFYT1 SQ MADSCRNLTYVRGSVGPATSTLMFVAGVVGNGLALGILSARRPARPSAFAVLVTGLAATDLLGTSFLSPAVFVAYARNSSLLGLARGGPALCDAFAFAMTFFGLASMLILFAMAVERCLALSHPYLYAQLDGPRCARLALPAIYAFCVLFCALPLLGLGQHQQYCPGSWCFLRMRWAQPGGAAFSLAYAGLVALLVAAIFLCNGSVTLSLCRMYRQQKRHQGSLGPRPRTGEDEVDHLILLALMTVVMAVCSLPLTIRCFTQAVAPDSSSEMGDLLAFRFYAFNPILDPWVFILFRKAVFQRLKLWVCCLCLGPAHGDSQTPLSQLASGRRDPRAPSAPVGKEGSCVPLSAWGEGQVEPLPPTQQSSGSAVGTSSKAEASVACSLC TTOFYT1 TT Successful TTOFYT1 FM GPCR rhodopsin TTOFYT1 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction; hsa04611:Platelet activation TTOFYT1 RC R-HSA-391908:Prostanoid ligand receptors; R-HSA-418555:G alpha (s) signalling events TTFJ8Q1 ID TTFJ8Q1 TTFJ8Q1 TN Protein kinase C alpha (PRKCA) TTFJ8Q1 UP P17252 TTFJ8Q1 UC KPCA_HUMAN TTFJ8Q1 BC Kinase TTFJ8Q1 SN Protein kinase C alpha type; PRKACA; PKCalpha; PKCA; PKC-alpha; PKC-A TTFJ8Q1 GN PRKCA TTFJ8Q1 FC Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42. Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. TTFJ8Q1 EC EC 2.7.11.13 TTFJ8Q1 PD 4RA4; 4DNL; 3IW4; 2ELI TTFJ8Q1 SQ MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV TTFJ8Q1 TT Successful TTFJ8Q1 FM Kinase TTFJ8Q1 KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04070:Phosphatidylinositol signaling system; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04310:Wnt signaling pathway; hsa04370:VEGF signaling pathway; hsa04510:Focal adhesion; hsa04530:Tight junction; hsa04540:Gap junction; hsa04650:Natural killer cell mediated cytotoxicity; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04670:Leukocyte transendothelial migration; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04727:GABAergic synapse; hsa04728:Dopaminergic synapse; hsa04730:Long-term depression; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04911:Insulin secretion; hsa04912:GnRH signaling pathway; hsa04916:Melanogenesis; hsa04918:Thyroid hormone synthesis; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04960:Aldosterone-regulated sodium reabsorption; hsa04961:Endocrine and other factor-regulated calcium reabsorption; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa05031:Amphetamine addiction; hsa05032:Morphine addiction; hsa05110:Vibrio cholerae infection; hsa05130:Pathogenic Escherichia coli infection; hsa05143:African trypanosomiasis; hsa05146:Amoebiasis; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05214:Glioma; hsa05223:Non-small cell lung cancer; hsa05231:Choline metabolism in cancer TTFJ8Q1 RC R-HSA-111933:Calmodulin induced events; R-HSA-114516:Disinhibition of SNARE formation; R-HSA-1433559:Regulation of KIT signaling; R-HSA-2179392:EGFR Transactivation by Gastrin; R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade; R-HSA-3000170:Syndecan interactions; R-HSA-399997:Acetylcholine regulates insulin secretion; R-HSA-4086398:Ca2+ pathway; R-HSA-416993:Trafficking of GluR2-containing AMPA receptors; R-HSA-418597:G alpha (z) signalling events; R-HSA-4419969:Depolymerisation of the Nuclear Lamina; R-HSA-450520:HuR (ELAVL1) binds and stabilizes mRNA; R-HSA-5099900:WNT5A-dependent internalization of FZD4; R-HSA-5218921:VEGFR2 mediated cell proliferation; R-HSA-76005:Response to elevated platelet cytosolic Ca2+ TTL935N ID TTL935N TTL935N TN Proteinase activated receptor 1 (F2R) TTL935N UP P25116 TTL935N UC PAR1_HUMAN TTL935N BC GPCR rhodopsin TTL935N SN Thrombin receptor; Proteinase-activated receptor 1; Protease-activated receptor-1; Protease activated receptor 1; PAR1; PAR-1; Coagulation factor II receptor; CF2R TTL935N GN F2R TTL935N FC May play a role in platelets activation and in vascular development. High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. TTL935N PD 3VW7; 3LU9; 3HKJ; 3HKI; 3BEF TTL935N SQ MGPRRLLLVAACFSLCGPLLSARTRARRPESKATNATLDPRSFLLRNPNDKYEPFWEDEEKNESGLTEYRLVSINKSSPLQKQLPAFISEDASGYLTSSWLTLFVPSVYTGVFVVSLPLNIMAIVVFILKMKVKKPAVVYMLHLATADVLFVSVLPFKISYYFSGSDWQFGSELCRFVTAAFYCNMYASILLMTVISIDRFLAVVYPMQSLSWRTLGRASFTCLAIWALAIAGVVPLLLKEQTIQVPGLNITTCHDVLNETLLEGYYAYYFSAFSAVFFFVPLIISTVCYVSIIRCLSSSAVANRSKKSRALFLSAAVFCIFIICFGPTNVLLIAHYSFLSHTSTTEAAYFAYLLCVCVSSISCCIDPLIYYYASSECQRYVYSILCCKESSDPSSYNSSGQLMASKMDTCSSNLNNSIYKKLLT TTL935N TT Successful TTL935N FM GPCR rhodopsin TTL935N KE hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04610:Complement and coagulation cascades; hsa04611:Platelet activation; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer TTL935N RC R-HSA-140875:Common Pathway of Fibrin Clot Formation; R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-456926:Thrombin signalling through proteinase activated receptors (PARs) TTCWXFA ID TTCWXFA TTCWXFA TN Protein-tyrosine phosphatase sigma (R-PTP-sigma) TTCWXFA UP Q13332 TTCWXFA UC PTPRS_HUMAN TTCWXFA BC Phosphoric monoester hydrolase TTCWXFA SN Receptor-type tyrosine-protein phosphatase sigma; Receptor-type tyrosine-protein phosphatase S; R-PTP-S TTCWXFA GN PTPRS TTCWXFA FC Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulation of neurite outgrowth. Contributes to the inhibition of neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also after nerve transection. Plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. Required for normal brain development, especially for normal development of the pituitary gland and the olfactory bulb. Functions as tyrosine phosphatase. Mediates dephosphorylation of NTRK1, NTRK2 and NTRK3. Plays a role in down-regulation of signaling cascades that lead to the activation of Akt and MAP kinases. Down-regulates TLR9-mediated activation of NF-kappa-B, as well as production of TNF, interferon alpha and interferon beta. Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycan. TTCWXFA EC EC 3.1.3.48 TTCWXFA PD 4PBX; 4BPC; 2YD9; 2YD3; 2YD2 TTCWXFA SQ MAPTWGPGMVSVVGPMGLLVVLLVGGCAAEEPPRFIKEPKDQIGVSGGVASFVCQATGDPKPRVTWNKKGKKVNSQRFETIEFDESAGAVLRIQPLRTPRDENVYECVAQNSVGEITVHAKLTVLREDQLPSGFPNIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDPSASNGRIKQLRSETFESTPIRGALQIESSEETDQGKYECVATNSAGVRYSSPANLYVRELREVRRVAPRFSILPMSHEIMPGGNVNITCVAVGSPMPYVKWMQGAEDLTPEDDMPVGRNVLELTDVKDSANYTCVAMSSLGVIEAVAQITVKSLPKAPGTPMVTENTATSITITWDSGNPDPVSYYVIEYKSKSQDGPYQIKEDITTTRYSIGGLSPNSEYEIWVSAVNSIGQGPPSESVVTRTGEQAPASAPRNVQARMLSATTMIVQWEEPVEPNGLIRGYRVYYTMEPEHPVGNWQKHNVDDSLLTTVGSLLEDETYTVRVLAFTSVGDGPLSDPIQVKTQQGVPGQPMNLRAEARSETSITLSWSPPRQESIIKYELLFREGDHGREVGRTFDPTTSYVVEDLKPNTEYAFRLAARSPQGLGAFTPVVRQRTLQSKPSAPPQDVKCVSVRSTAILVSWRPPPPETHNGALVGYSVRYRPLGSEDPEPKEVNGIPPTTTQILLEALEKWTQYRITTVAHTEVGPGPESSPVVVRTDEDVPSAPPRKVEAEALNATAIRVLWRSPAPGRQHGQIRGYQVHYVRMEGAEARGPPRIKDVMLADAQWETDDTAEYEMVITNLQPETAYSITVAAYTMKGDGARSKPKVVVTKGAVLGRPTLSVQQTPEGSLLARWEPPAGTAEDQVLGYRLQFGREDSTPLATLEFPPSEDRYTASGVHKGATYVFRLAARSRGGLGEEAAEVLSIPEDTPRGHPQILEAAGNASAGTVLLRWLPPVPAERNGAIVKYTVAVREAGALGPARETELPAAAEPGAENALTLQGLKPDTAYDLQVRAHTRRGPGPFSPPVRYRTFLRDQVSPKNFKVKMIMKTSVLLSWEFPDNYNSPTPYKIQYNGLTLDVDGRTTKKLITHLKPHTFYNFVLTNRGSSLGGLQQTVTAWTAFNLLNGKPSVAPKPDADGFIMVYLPDGQSPVPVQSYFIVMVPLRKSRGGQFLTPLGSPEDMDLEELIQDISRLQRRSLRHSRQLEVPRPYIAARFSVLPPTFHPGDQKQYGGFDNRGLEPGHRYVLFVLAVLQKSEPTFAASPFSDPFQLDNPDPQPIVDGEEGLIWVIGPVLAVVFIICIVIAILLYKNKPDSKRKDSEPRTKCLLNNADLAPHHPKDPVEMRRINFQTPDSGLRSPLREPGFHFESMLSHPPIPIADMAEHTERLKANDSLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYVDGYRCQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTRLEEKSRIKCDQYWPNRGTETYGFIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKPEKTVDVYGHVTLMRSQRNYMVQTEDQYSFIHEALLEAVGCGNTEVPARSLYAYIQKLAQVEPGEHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGSFDHYAT TTCWXFA TT Successful TTCWXFA FM Phosphoric monoester hydrolase TTCWXFA RC R-HSA-3000178:ECM proteoglycans TTJLP0R ID TTJLP0R TTJLP0R TN Quinone reductase 2 (NQO2) TTJLP0R UP P16083 TTJLP0R UC NQO2_HUMAN TTJLP0R BC Diphenol donor oxidoreductase TTJLP0R SN Quinone oxidoreductase 2; Qui reductase 2; QR2; NRH:quinone oxidoreductase 2; NRH:qui oxidoreductase 2; NQO2; NAD(P)H qui oxidoreductase 2 TTJLP0R GN NQO2 TTJLP0R FC The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. TTJLP0R EC EC 1.10.5.1 TTJLP0R PD 5LBZ; 5LBY; 5LBW; 5LBU; 5LBT TTJLP0R SQ MAGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLEPRATDKDITGTLSNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ TTJLP0R TT Successful TT1Q3IE ID TT1Q3IE TT1Q3IE TN Retinoic acid receptor gamma (RARG) TT1Q3IE UP P13631 TT1Q3IE UC RARG_HUMAN TT1Q3IE BC Nuclear hormone receptor TT1Q3IE SN RAR-gamma; Nuclear receptor subfamily 1 group B member 3; NR1B3 TT1Q3IE GN RARG TT1Q3IE FC Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). TT1Q3IE PD 6FX0; 5M24; 4LBD; 3LBD; 2LBD TT1Q3IE SQ MATNKERLFAAGALGPGSGYPGAGFPFAFPGALRGSPPFEMLSPSFRGLGQPDLPKEMASLSVETQSTSSEEMVPSSPSPPPPPRVYKPCFVCNDKSSGYHYGVSSCEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKEAVRNDRNKKKKEVKEEGSPDSYELSPQLEELITKVSKAHQETFPSLCQLGKYTTNSSADHRVQLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLSIADQITLLKAACLDILMLRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFAGQLLPLEMDDTETGLLSAICLICGDRMDLEEPEKVDKLQEPLLEALRLYARRRRPSQPYMFPRMLMKITDLRGISTKGAERAITLKMEIPGPMPPLIREMLENPEMFEDDSSQPGPHPNASSEDEVPGGQGKGGLKSPA TT1Q3IE TT Successful TT1Q3IE FM Nuclear hormone receptor TT1Q3IE RC R-HSA-383280:Nuclear Receptor transcription pathway TTH029C ID TTH029C TTH029C TN Retinoic acid receptor RXR-gamma (RXRG) TTH029C UP P48443 TTH029C UC RXRG_HUMAN TTH029C BC Nuclear hormone receptor TTH029C SN Retinoid X receptor gamma; Nuclear receptor subfamily 2 group B member 3; NR2B3 TTH029C GN RXRG TTH029C FC Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. Receptor for retinoic acid. TTH029C PD 2GL8 TTH029C SQ MYGNYSHFMKFPAGYGGSPGHTGSTSMSPSAALSTGKPMDSHPSYTDTPVSAPRTLSAVGTPLNALGSPYRVITSAMGPPSGALAAPPGINLVAPPSSQLNVVNSVSSSEDIKPLPGLPGIGNMNYPSTSPGSLVKHICAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLIYTCRDNKDCLIDKRQRNRCQYCRYQKCLVMGMKREAVQEERQRSRERAESEAECATSGHEDMPVERILEAELAVEPKTESYGDMNMENSTNDPVTNICHAADKQLFTLVEWAKRIPHFSDLTLEDQVILLRAGWNELLIASFSHRSVSVQDGILLATGLHVHRSSAHSAGVGSIFDRVLTELVSKMKDMQMDKSELGCLRAIVLFNPDAKGLSNPSEVETLREKVYATLEAYTKQKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLETPLQIT TTH029C TT Successful TTH029C FM Nuclear hormone receptor family TTH029C KE hsa03320:PPAR signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05216:Thyroid cancer; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer TTH029C RC R-HSA-383280:Nuclear Receptor transcription pathway TT3ROYC ID TT3ROYC TT3ROYC TN Serotonin transporter (SERT) TT3ROYC UP P31645 TT3ROYC UC SC6A4_HUMAN TT3ROYC BC Neurotransmitter:sodium symporter TT3ROYC SN Solute carrier family 6 member 4; HTT; 5HTT; 5HT transporter TT3ROYC GN SLC6A4 TT3ROYC FC Plays a key role in mediating regulation of the availability of serotonin to other receptors of serotonergic systems. Terminates the action of serotonin and recycles it in a sodium-dependent manner. Serotonin transporter whose primary function in the central nervous system involves the regulation of serotonergic signaling via transport of serotonin molecules from the synaptic cleft back into the pre-synaptic terminal for re-utilization. TT3ROYC PD 6DZZ; 6DZY; 6DZW; 6DZV; 6AWQ TT3ROYC SQ METTPLNSQKQLSACEDGEDCQENGVLQKVVPTPGDKVESGQISNGYSAVPSPGAGDDTRHSIPATTTTLVAELHQGERETWGKKVDFLLSVIGYAVDLGNVWRFPYICYQNGGGAFLLPYTIMAIFGGIPLFYMELALGQYHRNGCISIWRKICPIFKGIGYAICIIAFYIASYYNTIMAWALYYLISSFTDQLPWTSCKNSWNTGNCTNYFSEDNITWTLHSTSPAEEFYTRHVLQIHRSKGLQDLGGISWQLALCIMLIFTVIYFSIWKGVKTSGKVVWVTATFPYIILSVLLVRGATLPGAWRGVLFYLKPNWQKLLETGVWIDAAAQIFFSLGPGFGVLLAFASYNKFNNNCYQDALVTSVVNCMTSFVSGFVIFTVLGYMAEMRNEDVSEVAKDAGPSLLFITYAEAIANMPASTFFAIIFFLMLITLGLDSTFAGLEGVITAVLDEFPHVWAKRRERFVLAVVITCFFGSLVTLTFGGAYVVKLLEEYATGPAVLTVALIEAVAVSWFYGITQFCRDVKEMLGFSPGWFWRICWVAISPLFLLFIICSFLMSPPQLRLFQYNYPYWSIILGYCIGTSSFICIPTYIAYRLIITPGTFKERIIKSITPETPTEIPCGDIRLNAV TT3ROYC TT Successful TT3ROYC FM Neurotransmitter sodium symporter TT3ROYC KE hsa04726:Serotonergic synapse TTH8FZW ID TTH8FZW TTH8FZW TN Signal transducer and activator of transcription 3 (STAT3) TTH8FZW UP P40763 TTH8FZW UC STAT3_HUMAN TTH8FZW BC Transcription factor TTH8FZW SN Acute-phase response factor; APRF TTH8FZW GN STAT3 TTH8FZW FC Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity. Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1. Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (By similarity). May play an apoptotic role by transctivating BIRC5 expression under LEP activation. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (By similarity). TTH8FZW PD 5U5S; 5AX3 TTH8FZW SQ MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMELTSECATSPM TTH8FZW TT Successful TTH8FZW FM Transcription factor TTH8FZW KE hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04630:Jak-STAT signaling pathway; hsa04917:Prolactin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa05145:Toxoplasmosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05221:Acute myeloid leukemia; hsa05321:Inflammatory bowel disease (IBD) TTH8FZW RC R-HSA-1059683:Interleukin-6 signaling; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-2892247:POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation; R-HSA-452723:Transcriptional regulation of pluripotent stem cells; R-HSA-982772:Growth hormone receptor signaling TTWK8D0 ID TTWK8D0 TTWK8D0 TN Sodium pump subunit alpha-1 (ATP1A1) TTWK8D0 UP P05023 TTWK8D0 UC AT1A1_HUMAN TTWK8D0 BC Acid anhydrides hydrolase TTWK8D0 SN Sodium/potassium-transporting ATPase alpha1; Sodium pump 1; Na+/K+ ATPase 1; ATP1A1 TTWK8D0 GN ATP1A1 TTWK8D0 FC This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of atp coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions. TTWK8D0 EC EC 7.2.2.13 TTWK8D0 SQ MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY TTWK8D0 TT Successful TTWK8D0 KE hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04911:Insulin secretion; hsa04918:Thyroid hormone synthesis; hsa04919:Thyroid hormone signaling pathway; hsa04960:Aldosterone-regulated sodium reabsorption; hsa04961:Endocrine and other factor-regulated calcium reabsorption; hsa04964:Proximal tubule bicarbonate reclamation; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04973:Carbohydrate digestion and absorption; hsa04974:Protein digestion and absorption; hsa04976:Bile secretion; hsa04978:Mineral absorption TTWK8D0 RC R-HSA-936837:Ion transport by P-type ATPases TTS31JH ID TTS31JH TTS31JH TN Staphylococcus Plastid RNA polymerase beta (Stap-coc rpoB) TTS31JH UP P47768 TTS31JH UC RPOB_STAA8 TTS31JH BC Kinase TTS31JH SN Transcriptase beta chain; RpoB; RNAP beta subunit; RNA polymerase beta subunit; DNA-directed RNA polymerase beta chain TTS31JH GN Stap-coc rpoB TTS31JH FC DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. TTS31JH EC EC 2.7.7.6 TTS31JH SQ MAGQVVQYGRHRKRRNYARISEVLELPNLIEIQTKSYEWFLREGLIEMFRDISPIEDFTGNLSLEFVDYRLGEPKYDLEESKNRDATYAAPLRVKVRLIIKETGEVKEQEVFMGDFPLMTDTGTFVINGAERVIVSQLVRSPSVYFNEKIDKNGRENYDATIIPNRGAWLEYETDAKDVVYVRIDRTRKLPLTVLLRALGFSSDQEIVDLLGDNEYLRNTLEKDGTENTEQALLEIYERLRPGEPPTVENAKSLLYSRFFDPKRYDLASVGRYKTNKKLHLKHRLFNQKLAEPIVNTETGEIVVEEGTVLDRRKIDEIMDVLESNANSEVFELHGSVIDEPVEIQSIKVYVPNDDEGRTTTVIGNAFPDSEVKCITPADIIASMSYFFNLLSGIGYTDDIDHLGNRRLRSVGELLQNQFRIGLSRMERVVRERMSIQDTESITPQQLINIRPVIASIKEFFGSSQLSQFMDQANPLAELTHKRRLSALGPGGLTRERAQMEVRDVHYSHYGRMCPIETPEGPNIGLINSLSSYARVNEFGFIETPYRKVDLDTHAITDQIDYLTADEEDSYVVAQANSKLDENGRFMDDEVVCRFRGNNTVMAKEKMDYMDVSPKQVVSAATACIPFLENDDSNRALMGANMQRQAVPLMNPEAPFVGTGMEHVAARDSGAAITAKHRGRVEHVESNEILVRRLVEENGVEHEGELDRYPLAKFKRSNSGTCYNQRPIVAVGDVVEYNEILADGPSMELGEMALGRNVVVGFMTWDGYNYEDAVIMSERLVKDDVYTSIHIEEYESEARDTKLGPEEITRDIPNVSESALKNLDDRGIVYIGAEVKDGDILVGKVTPKGVTELTAEERLLHAIFGEKAREVRDTSLRVPHGAGGIVLDVKVFNREEGDDTLSPGVNQLVRVYIVQKRKIHVGDKMCGRHGNKGVISKIVPEEDMPYLPDGRPIDIMLNPLGVPSRMNIGQVLELHLGMAAKNLGIHVASPVFDGANDDDVWSTIEEAGMARDGKTVLYDGRTGEPFDNRISVGVMYMLKLAHMVDDKLHARSTGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEILTYKSDDTVGRVKTYEAIVKGENISRPSVPESFRVLMKELQSLGLDVKVMDEQDNEIEMTDVDDDDVVERKVDLQQNDAPETQKEVTD TTS31JH TT Successful TTS31JH KE sao00230:Purine metabolism; sao00240:Pyrimidine metabolism; sao01100:Metabolic pathways; sao03020:RNA polymerase TTIXTO3 ID TTIXTO3 TTIXTO3 TN Staphylococcus Topoisomerase IV (Stap-coc parC) TTIXTO3 UP Q6G9K4 TTIXTO3 UC PARC_STAAS TTIXTO3 BC Topoisomerase GyrA ParC TTIXTO3 SN Topoisomerase IV subunit A; DNA topoisomerase 4 subunit A TTIXTO3 GN Stap-coc parC TTIXTO3 FC Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule. TTIXTO3 EC EC 5.6.2.3 TTIXTO3 PD 2INR TTIXTO3 SQ MSEIIQDLSLEDVLGDRFGRYSKYIIQERALPDVRDGLKPVQRRILYAMYSSGNTHDKNFRKSAKTVGDVIGQYHPHGDSSVYEAMVRLSQDWKLRHVLIEMHGNNGSIDNDPPAAMRYTEAKLSLLAEELLRDINKETVSFIPNYDDTTLEPMVLPSRFPNLLVNGSTGISAGYATDIPPHNLAEVIQATLKYIDNPDITVNQLMKYIKGPDFPTGGIIQGIDGIKKAYESGKGRIIVRSKVEEETLRNGRKQLIITEIPYEVNKSSLVKRIDELRADKKVDGIVEVRDETDRTGLRIAIELKKDVNSESIKNYLYKNSDLQISYNFNMVAISDGRPKLMGIRQIIDSYLNHQIEVVANRTKFELDNAEKRMHIVEGLIKALSILDKVIELIRSSKNKRDAKENLIEVYEFTEEQAEAIVMLQLYRLTNTDIVALEGEHKELEALIKQLRHILDNHDALLNVIKEELNEIKKKFKSERLSLIEAEIEEIKIDKEVMVPSEEVILSMTRHGYIKRTSIRSFNASGVEDIGLKDGDSLLKHQEVNTQDTVLVFTNKGRYLFIPVHKLADIRWKELGQHVSQIVPIEEDEVVINVFNEKDFNTDAFYVFATQNGMIKKSTVPLFKTTRFNKPLIATKVKENDDLISVMRFEKDQLITVITNKGMSLTYNTSELSDTGLRAAGVKSINLKAEDFVVVTEGVSENDTILMATQRGSLKRISFKILQVAKRAQRGITLLKELKKNPHRIVAAHVVTGEHSQYTLYSKSNEEHGLINDIHKSEQYTNGSFIVDTDDFGEVIDMYIS TTIXTO3 TT Successful TTZPO1L ID TTZPO1L TTZPO1L TN Substance-P receptor (TACR1) TTZPO1L UP P25103 TTZPO1L UC NK1R_HUMAN TTZPO1L BC GPCR rhodopsin TTZPO1L SN Tachykinin receptor 1; Tachykinin neurokinin 1 receptor; Tachykinin 1 receptor; TACR1; Substance P receptor; SPR; Neurokinin 1 receptor; NK-1R; NK-1 receptor TTZPO1L GN TACR1 TTZPO1L FC This is a receptor for the tachykinin neuropeptide substance P. It is probably associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance P > substance K > neuromedin-K. TTZPO1L PD 6HLP; 6HLO; 6HLL; 6.00E+59; 2KSB TTZPO1L SQ MDNVLPVDSDLSPNISTNTSEPNQFVQPAWQIVLWAAAYTVIVVTSVVGNVVVMWIILAHKRMRTVTNYFLVNLAFAEASMAAFNTVVNFTYAVHNEWYYGLFYCKFHNFFPIAAVFASIYSMTAVAFDRYMAIIHPLQPRLSATATKVVICVIWVLALLLAFPQGYYSTTETMPSRVVCMIEWPEHPNKIYEKVYHICVTVLIYFLPLLVIGYAYTVVGITLWASEIPGDSSDRYHEQVSAKRKVVKMMIVVVCTFAICWLPFHIFFLLPYINPDLYLKKFIQQVYLAIMWLAMSSTMYNPIIYCCLNDRFRLGFKHAFRCCPFISAGDYEGLEMKSTRYLQTQGSVYKVSRLETTISTVVGAHEEEPEDGPKATPSSLDLTSNCSSRSDSKTMTESFSFSSNVLS TTZPO1L TT Successful TTZPO1L KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa05162:Measles TTZPO1L RC R-HSA-416476:G alpha (q) signalling events TTJUWVB ID TTJUWVB TTJUWVB TN Succinate-semialdehyde dehydrogenase (ALDH5A1) TTJUWVB UP P51649 TTJUWVB UC SSDH_HUMAN TTJUWVB BC Aldehyde/oxo donor oxidoreductase TTJUWVB SN Succinic dehydrogenase; Succinate-semialdehyde dehydrogenase, mitochondrial; SSADH; NAD(+)-dependent succinic semialdehyde dehydrogenase; Aldehyde dehydrogenase family 5 member A1 TTJUWVB GN ALDH5A1 TTJUWVB FC Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). TTJUWVB EC EC 1.2.1.24 TTJUWVB PD 2W8R; 2W8Q; 2W8P; 2W8O; 2W8N TTJUWVB SQ MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL TTJUWVB TT Successful TTJUWVB FM Oxidoreductases acting on aldehyde or oxo group of donors TTJUWVB KE hsa00250:Alanine, aspartate and glutamate metabolism; hsa00650:Butanoate metabolism; hsa01100:Metabolic pathways TTT3P91 ID TTT3P91 TTT3P91 TN Synaptic vesicle glycoprotein 2A (SV2A) TTT3P91 UP Q7L0J3 TTT3P91 UC SV2A_HUMAN TTT3P91 BC Major facilitator superfamily TTT3P91 SN SV2A TTT3P91 GN SV2A TTT3P91 FC Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles. TTT3P91 PD 4V11 TTT3P91 SQ MEEGFRDRAAFIRGAKDIAKEVKKHAAKKVVKGLDRVQDEYSRRSYSRFEEEDDDDDFPAPSDGYYRGEGTQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLAGVRGGLSDGEGPPGGRGEAQRRKEREELAQQYEAILRECGHGRFQWTLYFVLGLALMADGVEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGVYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRFFLENGKHDEAWMVLKQVHDTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRWGVRALSLGGQVWGNFLSCFGPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDYASRTKVFPGERVEHVTFNFTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVTSSNTFFRNCTFINTVFYNTDLFEYKFVNSRLINSTFLHNKEGCPLDVTGTGEGAYMVYFVSFLGTLAVLPGNIVSALLMDKIGRLRMLAGSSVMSCVSCFFLSFGNSESAMIALLCLFGGVSIASWNALDVLTVELYPSDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFASAALALGSSLALKLPETRGQVLQ TTT3P91 TT Successful TTT3P91 KE hsa04512:ECM-receptor interaction TTN2JFW ID TTN2JFW TTN2JFW TN T-cell surface glycoprotein CD4 (CD4) TTN2JFW UP P01730 TTN2JFW UC CD4_HUMAN TTN2JFW BC Immunoglobulin TTN2JFW SN T-cell surface antigen T4/Leu-3 TTN2JFW GN CD4 TTN2JFW FC In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages. Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. TTN2JFW PD 6MET; 6MEO; 6EDU; 6CM3; 5VN3 TTN2JFW SQ MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI TTN2JFW TT Successful TTN2JFW FM Immunoglobulin TTN2JFW KE hsa04514:Cell adhesion molecules (CAMs); hsa04612:Antigen processing and presentation; hsa04640:Hematopoietic cell lineage; hsa04660:T cell receptor signaling pathway; hsa05340:Primary immunodeficiency TTN2JFW RC R-HSA-173107:Binding and entry of HIV virion; R-HSA-202427:Phosphorylation of CD3 and TCR zeta chains; R-HSA-202430:Translocation of ZAP-70 to Immunological synapse; R-HSA-202433:Generation of second messenger molecules; R-HSA-389948:PD-1 signaling TTQY2EJ ID TTQY2EJ TTQY2EJ TN TERT messenger RNA (TERT mRNA) TTQY2EJ UP O14746 TTQY2EJ UC TERT_HUMAN TTQY2EJ BC mRNA target TTQY2EJ SN Telomerase-associated protein 2 (mRNA); Telomerase catalytic subunit (mRNA); TRT (mRNA); TP2 (mRNA); TCS1 (mRNA); HEST2 (mRNA); EST2 (mRNA) TTQY2EJ GN TERT TTQY2EJ FC Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis. Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. TTQY2EJ EC EC 2.7.7.49 TTQY2EJ PD 5UGW; 5MER; 5MEQ; 5MEP; 5MEO TTQY2EJ SQ MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQVWKNPTFFLRVISDTASLCYSILKAKNAGMSLGAKGAAGPLPSEAVQWLCHQAFLLKLTRHRVTYVPLLGSLRTAQTQLSRKLPGTTLTALEAAANPALPSDFKTILD TTQY2EJ TT Successful TTQY2EJ FM mRNA target TTQY2EJ KE hsa05166:HTLV-I infection TTQY2EJ RC R-HSA-201722:Formation of the beta-catenin:TCF transactivating complex TT2O84V ID TT2O84V TT2O84V TN Thromboxane A2 receptor (TBXA2R) TT2O84V UP P21731 TT2O84V UC TA2R_HUMAN TT2O84V BC GPCR rhodopsin TT2O84V SN TXA2-R; TXA2 receptor; Prostanoid TP receptor TT2O84V GN TBXA2R TT2O84V FC The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. In the kidney, the binding of TXA2 to glomerular TP receptors causes intense vasoconstriction. Activates phospholipase C. Isoform 1 activates adenylyl cyclase. Isoform 2 inhibits adenylyl cyclase. Receptor for thromboxane A2 (TXA2), a potent stimulator of platelet aggregation. TT2O84V PD 1LBN TT2O84V SQ MWPNGSSLGPCFRPTNITLEERRLIASPWFAASFCVVGLASNLLALSVLAGARQGGSHTRSSFLTFLCGLVLTDFLGLLVTGTIVVSQHAALFEWHAVDPGCRLCRFMGVVMIFFGLSPLLLGAAMASERYLGITRPFSRPAVASQRRAWATVGLVWAAALALGLLPLLGVGRYTVQYPGSWCFLTLGAESGDVAFGLLFSMLGGLSVGLSFLLNTVSVATLCHVYHGQEAAQQRPRDSEVEMMAQLLGIMVVASVCWLPLLVFIAQTVLRNPPAMSPAGQLSRTTEKELLIYLRVATWNQILDPWVYILFRRAVLRRLQPRLSTRPRSLSLQPQLTQRSGLQ TT2O84V TT Successful TT2O84V FM GPCR rhodopsin TT2O84V KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04611:Platelet activation TT2O84V RC R-HSA-391908:Prostanoid ligand receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-416482:G alpha (12/13) signalling events; R-HSA-428930:Thromboxane signalling through TP receptor TT52XDZ ID TT52XDZ TT52XDZ TN Thyroid peroxidase (TPO) TT52XDZ UP P07202 TT52XDZ UC PERT_HUMAN TT52XDZ BC Peroxidases TT52XDZ SN Thyroperoxidase; TPO TT52XDZ GN TPO TT52XDZ FC Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). TT52XDZ EC EC 1.11.1.8 TT52XDZ SQ MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQRNLKKRGILSPAQLLSFSKLPEPTSGVIARAAEIMETSIQAMKRKVNLKTQQSQHPTDALSEDLLSIIANMSGCLPYMLPPKCPNTCLANKYRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQSTSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITGMNLEAWRETFPQDDKCGFPESVENGDFVHCEESGRRVLVYSCRHGYELQGREQLTCTQEGWDFQPPLCKDVNECADGAHPPCHASARCRNTKGGFQCLCADPYELGDDGRTCVDSGRLPRVTWISMSLAALLIGGFAGLTSTVICRWTRTGTKSTLPISETGGGTPELRCGKHQAVGTSPQRAAAQDSEQESAGMEGRDTHRLPRAL TT52XDZ TT Successful TT52XDZ KE hsa00350:Tyrosine metabolism; hsa01100:Metabolic pathways; hsa04918:Thyroid hormone synthesis; hsa05320:Autoimmune thyroid disease TT52XDZ RC R-HSA-209968:Thyroxine biosynthesis TT4J8MF ID TT4J8MF TT4J8MF TN Thyrotropin-releasing hormone receptor (TRHR) TT4J8MF UP P34981 TT4J8MF UC TRFR_HUMAN TT4J8MF BC GPCR rhodopsin TT4J8MF SN Thyroliberin receptor; TRH-R TT4J8MF GN TRHR TT4J8MF FC Receptor for thyrotropin-releasing hormone. This receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. TT4J8MF SQ MENETVSELNQTQLQPRAVVALEYQVVTILLVLIICGLGIVGNIMVVLVVMRTKHMRTPTNCYLVSLAVADLMVLVAAGLPNITDSIYGSWVYGYVGCLCITYLQYLGINASSCSITAFTIERYIAICHPIKAQFLCTFSRAKKIIIFVWAFTSLYCMLWFFLLDLNISTYKDAIVISCGYKISRNYYSPIYLMDFGVFYVVPMILATVLYGFIARILFLNPIPSDPKENSKTWKNDSTHQNTNLNVNTSNRCFNSTVSSRKQVTKMLAVVVILFALLWMPYRTLVVVNSFLSSPFQENWFLLFCRICIYLNSAINPVIYNLMSQKFRAAFRKLCNCKQKPTEKPANYSVALNYSVIKESDHFSTELDDITVTDTYLSATKVSFDDTCLASEVSFSQS TT4J8MF TT Successful TT4J8MF KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TT4J8MF RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTXAGYU ID TTXAGYU TTXAGYU TN Tissue-type plasminogen activator (PLAT) TTXAGYU UP P00750 TTXAGYU UC TPA_HUMAN TTXAGYU BC Peptidase TTXAGYU SN TPA; T-plasminogen activator; T-PA; Reteplase; Alteplase TTXAGYU GN PLAT TTXAGYU FC By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration. Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. TTXAGYU EC EC 3.4.21.68 TTXAGYU PD 5ZLZ; 5BRR; 1TPN; 1TPM; 1TPK TTXAGYU SQ MDAMKRGLCCVLLLCGAVFVSPSQEIHARFRRGARSYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP TTXAGYU TT Successful TTXAGYU FM Peptidase TTXAGYU KE hsa04610:Complement and coagulation cascades; hsa05202:Transcriptional misregulation in cancer TTXAGYU RC R-HSA-75205:Dissolution of Fibrin Clot TTHGXBU ID TTHGXBU TTHGXBU TN T-lymphocyte activation antigen CD86 (FUN1) TTHGXBU UP P42081 TTHGXBU UC CD86_HUMAN TTHGXBU BC Immunoglobulin TTHGXBU SN FUN-1; CTLA-4 counter-receptor B7.2; CD86; CD28LG2; BU63; B70; Activation B7-2 antigen TTHGXBU GN CD86 TTHGXBU FC Receptor involved in the costimulatory signal essential for t-lymphocyte proliferation and interleukin-2 production, by binding cd28 or ctla-4. May play a critical role in the early events of t-cell activation and costimulationof naive t-cells, such as deciding between immunity and anergy that is made by t-cells within 24 hours after activation. Isoform 2 interferes with the formation of cd86 clusters, and thus acts as a negative regulator of t-cell activation. TTHGXBU PD 5YXK; 1NCN; 1I85 TTHGXBU SQ MDPQCTMGLSNILFVMAFLLSGAAPLKIQAYFNETADLPCQFANSQNQSLSELVVFWQDQENLVLNEVYLGKEKFDSVHSKYMGRTSFDSDSWTLRLHNLQIKDKGLYQCIIHHKKPTGMIRIHQMNSELSVLANFSQPEIVPISNITENVYINLTCSSIHGYPEPKKMSVLLRTKNSTIEYDGVMQKSQDNVTELYDVSISLSVSFPDVTSNMTIFCILETDKTRLLSSPFSIELEDPQPPPDHIPWITAVLPTVIICVMVFCLILWKWKKKKRPRNSYKCGTNTMEREESEQTKKREKIHIPERSDEAQRVFKSSKTSSCDKSDTCF TTHGXBU TT Successful TTHGXBU KE hsa04514:Cell adhesion molecules (CAMs); hsa04620:Toll-like receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa04940:Type I diabetes mellitus; hsa05202:Transcriptional misregulation in cancer; hsa05320:Autoimmune thyroid disease; hsa05322:Systemic lupus erythematosus; hsa05323:Rheumatoid arthritis; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease; hsa05416:Viral myocarditis TTHGXBU RC R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-389356:CD28 co-stimulation; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389359:CD28 dependent Vav1 pathway; R-HSA-389513:CTLA4 inhibitory signaling TTPTXIN ID TTPTXIN TTPTXIN TN Translocator protein (TSPO) TTPTXIN UP P30536 TTPTXIN UC TSPO_HUMAN TTPTXIN BC Cholesterol/porphyrin uptake translocator TTPTXIN SN Peripheral-type benzodiazepine receptor; Peripheral benzodiazepine receptor; PKBS; PBR; Mitochondrial benzodiazepine receptor; MBR; BZRP TTPTXIN GN TSPO TTPTXIN FC Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism, but its precise physiological role is controversial. It is apparently not required for steroid hormone biosynthesis. Was initially identified as peripheral-type benzodiazepine receptor; can also bind isoquinoline carboxamides. Can bind protoporphyrin IX and may play a role in the transport of porphyrins and heme. TTPTXIN SQ MAPPWVPAMGFTLAPSLGCFVGSRFVHGEGLRWYAGLQKPSWHPPHWVLGPVWGTLYSAMGYGSYLVWKELGGFTEKAVVPLGLYTGQLALNWAWPPIFFGARQMGWALVDLLLVSGAAAATTVAWYQVSPLAARLLYPYLAWLAFTTTLNYCVWRDNHGWRGGRRLPE TTPTXIN TT Successful TTPTXIN FM Translocator protein TTPTXIN KE hsa04080:Neuroactive ligand-receptor interaction; hsa05166:HTLV-I infection TTF8CQI ID TTF8CQI TTF8CQI TN Tumor necrosis factor (TNF) TTF8CQI UP P01375 TTF8CQI UC TNFA_HUMAN TTF8CQI BC Cytokine: tumor necrosis factor TTF8CQI SN Tumour necrosis factor alpha; Tumour necrosis factor; Tumor necrosis factor ligand superfamily member 2; TNFalpha; TNFSF2; TNFA; TNF-alpha; TNF-a; TNF alpha; Cachectin TTF8CQI GN TNF TTF8CQI FC It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Upregulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective. Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line. Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance. Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. TTF8CQI PD 5YOY; 5WUX; 5UUI; 5TSW; 5MU8 TTF8CQI SQ MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL TTF8CQI TT Successful TTF8CQI FM Tumor necrosis factor TTF8CQI KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04210:Apoptosis; hsa04350:TGF-beta signaling pathway; hsa04380:Osteoclast differentiation; hsa04612:Antigen processing and presentation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04668:TNF signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04940:Type I diabetes mellitus; hsa05010:Alzheimer's disease; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05133:Pertussis; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05205:Proteoglycans in cancer; hsa05310:Asthma; hsa05321:Inflammatory bowel disease (IBD); hsa05322:Systemic lupus erythematosus; hsa05323:Rheumatoid arthritis; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05414:Dilated cardiomyopathy TTF8CQI RC R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-5357786:TNFR1-induced proapoptotic signaling; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5626978:TNFR1-mediated ceramide production; R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-75893:TNF signaling TTULVH8 ID TTULVH8 TTULVH8 TN Tyrosinase (TYR) TTULVH8 UP P14679 TTULVH8 UC TYRO_HUMAN TTULVH8 BC Paired donor oxygen oxidoreductase TTULVH8 SN Tumor rejection antigen AB; SK29-AB; Monophenol monooxygenase; LB24-AB TTULVH8 GN TYR TTULVH8 FC Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine. In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone. This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. TTULVH8 EC EC 1.14.18.1 TTULVH8 SQ MLLAVLYCLLWSFQTSAGHFPRACVSSKNLMEKECCPPWSGDRSPCGQLSGRGSCQNILLSNAPLGPQFPFTGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFWGPNCTERRLLVRRNIFDLSAPEKDKFFAYLTLAKHTISSDYVIPIGTYGQMKNGSTPMFNDINIYDLFVWMHYYVSMDALLGGSEIWRDIDFAHEAPAFLPWHRLFLLRWEQEIQKLTGDENFTIPYWDWRDAEKCDICTDEYMGGQHPTNPNLLSPASFFSSWQIVCSRLEEYNSHQSLCNGTPEGPLRRNPGNHDKSRTPRLPSSADVEFCLSLTQYESGSMDKAANFSFRNTLEGFASPLTGIADASQSSMHNALHIYMNGTMSQVQGSANDPIFLLHHAFVDSIFEQWLRRHRPLQEVYPEANAPIGHNRESYMVPFIPLYRNGDFFISSKDLGYDYSYLQDSDPDSFQDYIKSYLEQASRIWSWLLGAAMVGAVLTALLAGLVSLLCRHKRKQLPEEKQPLLMEKEDYHSLYQSHL TTULVH8 TT Successful TTULVH8 FM Paired donor oxidoreductase TTULVH8 KE hsa00350:Tyrosine metabolism; hsa00740:Riboflavin metabolism; hsa01100:Metabolic pathways; hsa04916:Melanogenesis TTUHP71 ID TTUHP71 TTUHP71 TN Tyrosine 3-monooxygenase (TH) TTUHP71 UP P07101 TTUHP71 UC TY3H_HUMAN TTUHP71 BC Paired donor oxygen oxidoreductase TTUHP71 SN Tyrosine 3-hydroxylase; TH TTUHP71 GN TH TTUHP71 FC Plays an important role in the physiology of adrenergic neurones. TTUHP71 EC EC 1.14.16.2 TTUHP71 PD 4J6S; 2XSN TTUHP71 SQ MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG TTUHP71 TT Successful TTUHP71 KE hsa00350:Tyrosine metabolism; hsa01100:Metabolic pathways; hsa04728:Dopaminergic synapse; hsa04917:Prolactin signaling pathway; hsa05012:Parkinson's disease; hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05034:Alcoholism TTZPY6J ID TTZPY6J TTZPY6J TN Tyrosine-protein kinase UFO (AXL) TTZPY6J UP P30530 TTZPY6J UC UFO_HUMAN TTZPY6J BC Kinase TTZPY6J SN UFO; Tyrosine-protein kinase receptor UFO; AXL oncogene TTZPY6J GN AXL TTZPY6J FC Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, ALX binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response. TTZPY6J EC EC 2.7.10.1 TTZPY6J PD 5VXZ; 5U6B; 4RA0; 2C5D TTZPY6J SQ MAWRCPRMGRVPLAWCLALCGWACMAPRGTQAEESPFVGNPGNITGARGLTGTLRCQLQVQGEPPEVHWLRDGQILELADSTQTQVPLGEDEQDDWIVVSQLRITSLQLSDTGQYQCLVFLGHQTFVSQPGYVGLEGLPYFLEEPEDRTVAANTPFNLSCQAQGPPEPVDLLWLQDAVPLATAPGHGPQRSLHVPGLNKTSSFSCEAHNAKGVTTSRTATITVLPQQPRNLHLVSRQPTELEVAWTPGLSGIYPLTHCTLQAVLSDDGMGIQAGEPDPPEEPLTSQASVPPHQLRLGSLHPHTPYHIRVACTSSQGPSSWTHWLPVETPEGVPLGPPENISATRNGSQAFVHWQEPRAPLQGTLLGYRLAYQGQDTPEVLMDIGLRQEVTLELQGDGSVSNLTVCVAAYTAAGDGPWSLPVPLEAWRPGQAQPVHQLVKEPSTPAFSWPWWYVLLGAVVAAACVLILALFLVHRRKKETRYGEVFEPTVERGELVVRYRVRKSYSRRTTEATLNSLGISEELKEKLRDVMVDRHKVALGKTLGEGEFGAVMEGQLNQDDSILKVAVKTMKIAICTRSELEDFLSEAVCMKEFDHPNVMRLIGVCFQGSERESFPAPVVILPFMKHGDLHSFLLYSRLGDQPVYLPTQMLVKFMADIASGMEYLSTKRFIHRDLAARNCMLNENMSVCVADFGLSKKIYNGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQPADCLDGLYALMSRCWELNPQDRPSFTELREDLENTLKALPPAQEPDEILYVNMDEGGGYPEPPGAAGGADPPTQPDPKDSCSCLTAAEVHPAGRYVLCPSTTPSPAQPADRGSPAAPGQEDGA TTZPY6J TT Successful TTZPY6J FM Kinase TTZPY6J RC R-HSA-4420097:VEGFA-VEGFR2 Pathway TT4TFGN ID TT4TFGN TT4TFGN TN Vasopressin V1a receptor (V1AR) TT4TFGN UP P37288 TT4TFGN UC V1AR_HUMAN TT4TFGN BC GPCR rhodopsin TT4TFGN SN Vascular/hepatic-type arginine vasopressin receptor; V1aR; V1a vasopressin receptor; Antidiuretic hormone receptor 1a; AVPR1; AVPR V1a TT4TFGN GN AVPR1A TT4TFGN FC The activity of this receptor is mediated by G proteins which activate a phosphatidyl-inositol-calcium second messenger system. Has been involved in social behaviors, including affiliation and attachment. Receptor for arginine vasopressin. TT4TFGN PD 1YTV TT4TFGN SQ MRLSAGPDAGPSGNSSPWWPLATGAGNTSREAEALGEGNGPPRDVRNEELAKLEIAVLAVTFAVAVLGNSSVLLALHRTPRKTSRMHLFIRHLSLADLAVAFFQVLPQMCWDITYRFRGPDWLCRVVKHLQVFGMFASAYMLVVMTADRYIAVCHPLKTLQQPARRSRLMIAAAWVLSFVLSTPQYFVFSMIEVNNVTKARDCWATFIQPWGSRAYVTWMTGGIFVAPVVILGTCYGFICYNIWCNVRGKTASRQSKGAEQAGVAFQKGFLLAPCVSSVKSISRAKIRTVKMTFVIVTAYIVCWAPFFIIQMWSVWDPMSVWTESENPTITITALLGSLNSCCNPWIYMFFSGHLLQDCVQSFPCCQNMKEKFNKEDTDSMSRRQTFYSNNRSPTNSTGMWKDSPKSSKSIKFIPVST TT4TFGN TT Successful TT4TFGN FM GPCR rhodopsin TT4TFGN KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction TT4TFGN RC R-HSA-388479:Vasopressin-like receptors; R-HSA-416476:G alpha (q) signalling events TTEUC8H ID TTEUC8H TTEUC8H TN Vitamin K epoxide reductase complex 1 (VKORC1) TTEUC8H UP Q9BQB6 TTEUC8H UC VKOR1_HUMAN TTEUC8H BC Short-chain dehydrogenases reductase TTEUC8H SN Vitamin K1 2,3-epoxide reductase subunit 1; VKORC1; VKOR; UNQ308/PRO351; MSTP576; MSTP134 TTEUC8H GN VKORC1 TTEUC8H FC Involved invitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development. TTEUC8H EC EC 1.17.4.4 TTEUC8H SQ MGSTWGSPGWVRLALCLTGLVLSLYALHVKAARARDRDYRALCDVGTAISCSRVFSSRWGRGFGLVEHVLGQDSILNQSNSIFGCIFYTLQLLLGCLRTRWASVLMLLSSLVSLAGSVYLAWILFFVLYDFCIVCITTYAINVSLMWLSFRKVQEPQGKAKRH TTEUC8H TT Successful TTEUC8H KE hsa00130:Ubiquinone and other terpenoid-quinone biosynthesis TTZUXYS ID TTZUXYS TTZUXYS TN Vitamin K-dependent protein C (PROC) TTZUXYS UP P04070 TTZUXYS UC PROC_HUMAN TTZUXYS BC Peptidase TTZUXYS SN Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; PROC; Blood coagulation factor XIV; Autoprothrombin IIA; Anticoagulant protein C; Activation peptide TTZUXYS GN PROC TTZUXYS FC Protein C is avitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. TTZUXYS EC EC 3.4.21.69 TTZUXYS PD 4DT7; 3JTC; 3F6U; 2PCT; 1PCU TTZUXYS SQ MWQLTSLLLFVATWGISGTPAPLDSVFSSSERAHQVLRIRKRANSFLEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHVDGDQCLVLPLEHPCASLCCGHGTCIDGIGSFSCDCRSGWEGRFCQREVSFLNCSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQCHPAVKFPCGRPWKRMEKKRSHLKRDTEDQEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRDKEAPQKSWAP TTZUXYS TT Successful TTZUXYS KE hsa04610:Complement and coagulation cascades TTZUXYS RC R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-140875:Common Pathway of Fibrin Clot Formation; R-HSA-159740:Gamma-carboxylation of protein precursors; R-HSA-159763:Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus; R-HSA-159782:Removal of aminoterminal propeptides from gamma-carboxylated proteins; R-HSA-202733:Cell surface interactions at the vascular wall TTQ6VDM ID TTQ6VDM TTQ6VDM TN Voltage-gated potassium channel Kv11.1 (KCNH2) TTQ6VDM UP Q12809 TTQ6VDM UC KCNH2_HUMAN TTQ6VDM BC Voltage-gated ion channel TTQ6VDM SN hERG1; hERG-1; Voltage-gated potassium channel subunit Kv11.1; Potassium voltage-gated channel subfamily H member 2; HERG K+ channel; HERG; H-ERG; Ether-a-go-go-related protein 1; Ether-a-go-go-related gene potassium channel 1; Ether-a-go-go related protein 1; Ether-a-go-go related gene potassium channel 1; Eag related protein 1; Eag homolog; ERG-1; ERG TTQ6VDM GN KCNH2 TTQ6VDM FC Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr). Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. TTQ6VDM PD 5VA3; 5VA2; 5VA1; 4HQA; 4HP9 TTQ6VDM SQ MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEKDMVGSPAHDTNHRGPPTSWLAPGRAKTFRLKLPALLALTARESSVRSGGAGGAGAPGAVVVDVDLTPAAPSSESLALDEVTAMDNHVAGLGPAEERRALVGPGSPPRSAPGQLPSPRAHSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGVLPPPPRHASTGAMHPLRSGLLNSTSDSDLVRYRTISKIPQITLNFVDLKGDPFLASPTSDREIIAPKIKERTHNVTEKVTQVLSLGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLKETEEGPPATECGYACQPLAVVDLIVDIMFIVDILINFRTTYVNANEEVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSRIGWLHNLGDQIGKPYNSSGLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLEVLDMYPEFSDHFWSSLEITFNLRDTNMIPGSPGSTELEGGFSRQRKRKLSFRRRTDKDTEQPGEVSALGPGRAGAGPSSRGRPGGPWGESPSSGPSSPESSEDEGPGRSSSPLRLVPFSSPRPPGEPPGGEPLMEDCEKSSDTCNPLSGAFSGVSNIFSFWGDSRGRQYQELPRCPAPTPSLLNIPLSSPGRRPRGDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSAVTTPGPGPTSTSPLLPVSPLPTLTLDSLSQVSQFMACEELPPGAPELPQEGPTRRLSLPGQLGALTSQPLHRHGSDPGS TTQ6VDM TT Successful TTQ6VDM FM Voltage gated ion channel TTQ6VDM RC R-HSA-1296072:Voltage gated Potassium channels TT846HF ID TT846HF TT846HF TN Voltage-gated potassium channel Kv7.1 (KCNQ1) TT846HF UP P51787 TT846HF UC KCNQ1_HUMAN TT846HF BC Voltage-gated ion channel TT846HF SN Voltage-gated potassium channel subunit Kv7.1; Potassium voltage-gated channel subfamily KQT member 1; Kv7.1; KVLQT1; KQT-like 1; KCNQ1 channel; KCNA9; KCNA8; IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1; IKs producing slow voltage-gated potassium channel alpha subunit KvLQT1 TT846HF GN KCNQ1 TT846HF FC Associates with KCNE beta subunits that modulates current kinetics. Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current. Promotes also a delayed voltage activated potassium current showing outward rectification characteristic. During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current. When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions. This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents. During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion. Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion. When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current. When associated with KCNE4, inhibits voltage-gated potassium channel activity. When associated with KCNE5, this complex only conducts current upon strong and continued depolarization. Also forms a heterotetramer with KCNQ5; has a voltage-gated potassium channel activity. Binds with phosphatidylinositol 4,5-bisphosphate. Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon. TT846HF PD 4V0C; 4UMO; 3HFE; 3HFC; 3BJ4 TT846HF SQ MAAASSPPRAERKRWGWGRLPGARRGSAGLAKKCPFSLELAEGGPAGGALYAPIAPGAPGPAPPASPAAPAAPPVASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGWKCFVYHFAVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKKKKFKLDKDNGVTPGEKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFMRTNSFAEDLDLEGETLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVTQLDQRLALITDMLHQLLSLHGGSTPGSGGPPREGGAHITQPCGSGGSVDPELFLPSNTLPTYEQLTVPRRGPDEGS TT846HF TT Successful TT846HF FM Voltage gated ion channel TT846HF KE hsa04261:Adrenergic signaling in cardiomyocytes; hsa04725:Cholinergic synapse; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04974:Protein digestion and absorption; hsa05110:Vibrio cholerae infection TT846HF RC R-HSA-1296072:Voltage gated Potassium channels TTZOVE0 ID TTZOVE0 TTZOVE0 TN Voltage-gated sodium channel alpha Nav1.5 (SCN5A) TTZOVE0 UP Q14524 TTZOVE0 UC SCN5A_HUMAN TTZOVE0 BC Voltage-gated ion channel TTZOVE0 SN Voltage-gated sodium channel subunit alpha Nav1.5; Sodium channel protein type V subunit alpha; Sodium channel protein type 5 subunit alpha; Sodium channel protein cardiac muscle subunit alpha; HH1 TTZOVE0 GN SCN5A TTZOVE0 FC Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant Na(+) channel isoform. This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels. This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. TTZOVE0 PD 6MUD; 5DBR; 4OVN; 4JQ0; 4DJC TTZOVE0 SQ MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLKNGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRKRMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSEADFADDENSTAGESESHHTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGVVSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQRALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTDLTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQLALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVPPTRKETRFEEGEQPGQGTPGDPEPVCVPIAVAESDTDDQEEDEENSLGTEEESSKQQESQPVSGGPEAPPDSRTWSQVSATASSEAEASASQADWRQQWKAEPQAPGCGETPEDSCSEGSTADMTNTAELLEQIPDLGQDVKDPEDCFTEGCVRRCPCCAVDTTQAPGKVWWRLRKTCYHIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSQCESLNLTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKINILAKINLLFVAIFTGECIVKLAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPTLPNSNGSRGDCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYSVLSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSAMVIQRAFRRHLLQRSLKHASFLFRQQAGSGLSEEDAPEREGLIAYVMSENFSRPLGPPSSSSISSTSFPPSYDSVTRATSDNLQVRGSDYSHSEDLADFPPSPDRDRESIV TTZOVE0 TT Successful TTZOVE0 FM Voltage gated ion channel TTZOVE0 KE hsa04261:Adrenergic signaling in cardiomyocytes TTZOVE0 RC R-HSA-445095:Interaction between L1 and Ankyrins TT7RJY8 ID TT7RJY8 TT7RJY8 TN Xanthine dehydrogenase/oxidase (XDH) TT7RJY8 UP P47989 TT7RJY8 UC XDH_HUMAN TT7RJY8 BC CH/CH(2) oxidoreductase TT7RJY8 SN Xanthine oxidase; Xanthine dehydrogenase; XDHA TT7RJY8 GN XDH TT7RJY8 FC Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro). Key enzyme in purine degradation. TT7RJY8 PD 2E1Q; 2CKJ TT7RJY8 SQ MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDRLQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCCMNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQASTLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFGAACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISDLNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSAFKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKEELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLDPTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRYENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDKVTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDLKKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKMLGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGRHPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGRLCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKLEGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGALLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAASVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLGYSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAVGEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVTGVPENCKPWSVRV TT7RJY8 TT Successful TT7RJY8 FM Oxidoreductases acting on CH or CH(2) groups TT7RJY8 KE hsa00230:Purine metabolism; hsa00232:Caffeine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways; hsa04146:Peroxisome TT7RJY8 RC R-HSA-74259:Purine catabolism TTS586L ID TTS586L TTS586L TN HUMAN cathepsin L (CTSL) TTS586L UP P07711 TTS586L UC CATL1_HUMAN TTS586L BC Peptidase TTS586L SN Major excreted protein; MEP; Cathepsin L1; CTSL1 TTS586L GN CTSL TTS586L FC Important for the overall degradation of proteins in lysosomes. TTS586L EC EC 3.4.22.15 TTS586L PD 6F06; 6EZX; 6EZP; 5MQY; 5MAJ TTS586L SQ MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV TTS586L FM Peptidase TTUD6MS ID TTUD6MS TTUD6MS TN HUMAN dibasic-processing enzyme (Furin) TTUD6MS UP P09958 TTUD6MS UC FURIN_HUMAN TTUD6MS BC Peptidase TTUD6MS SN Paired basic amino acid residuecleaving enzyme; Paired basic amino acid residue-cleaving enzyme; PCSK3; PACE; FUR; Dibasicprocessing enzyme TTUD6MS GN FURIN TTUD6MS FC Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. TTUD6MS EC EC 3.4.21.75 TTUD6MS PD 6HZD; 6HZC; 6HZB; 6HZA; 6HLE TTUD6MS SQ MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL TTUD6MS FM Peptidase TTY732E ID TTY732E TTY732E TN MERS-CoV helicase (Hel) TTY732E UP K9N7C7 (5311-5908) TTY732E UC R1AB_CVEMC (5311-5908) TTY732E BC Coronaviruses polyprotein 1ab family TTY732E SN MERS-CoV Helicase; MERS-CoV Hel TTY732E GN MERS-CoV rep; MERS-CoV 1a-1b TTY732E FC Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. TTY732E EC EC 3.6.4.12 TTY732E SQ AVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVCNAPGCGVSDVTKLYLGGMSYFCVDHRPVCSFPLCANGLVFGLYKNMCTGSPSIVEFNRLATCDWTESGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERQLLLVWEAGKSKPPLNRNYVFTGYHITKNSKVQLGEYIFERIDYSDAVSYKSSTTYKLTVGDIFVLTSHSVATLTAPTIVNQERYVKITGLYPTITVPEEFASHVANFQKSGYSKYVTVQGPPGTGKSHFAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDRFKVNETNSQYLFSTINALPETSADILVVDEVSMCTNYDLSIINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSMCYRCPKEIVSTVSALVYNNKLLAKKELSGQCFKILYKGNVTHDASSAINRPQLTFVKNFITANPAWSKAVFISPYNSQNAVARSMLGLTTQTVDSSQGSEYQYVIFCQTADTAHANNINRFNVAITRAQKGILCVMTSQALFESLEFTELSFTNYKLQ TTYJOLE ID TTYJOLE TTYJOLE TN MERS-CoV papain-like proteinase (PL-PRO) TTYJOLE UP K9N7C7 (854-2740) TTYJOLE UC R1AB_CVEMC (854-2740) TTYJOLE BC Coronaviruses polyprotein 1ab family TTYJOLE SN MERS-CoV PLpro; MERS-CoV Non-structural protein 3; MERS-CoV nsp3 TTYJOLE GN MERS-CoV rep; MERS-CoV 1a-1b TTYJOLE FC Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. TTYJOLE EC EC 3.4.19.12 TTYJOLE SQ APVKKVAFGGDQVHEVAAVRSVTVEYNIHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFSLHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIAQVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVITECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNILHVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSLTFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPLGYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLLHWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMTLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTYSPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKGKPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVSFVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFATRTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVDLSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRANSFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQTSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGKRTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKIVGG TTOA6YT ID TTOA6YT TTOA6YT TN MERS-CoV RNA-directed RNA polymerase (RdRp) TTOA6YT UP K9N7C7 (4378-5310) TTOA6YT UC R1AB_CVEMC (4378-5310) TTOA6YT BC Coronaviruses polyprotein 1ab family TTOA6YT SN MERS-CoV RNA-directed RNA polymerase; MERS-CoV Pol; MERS-CoV RdRp TTOA6YT GN MERS-CoV rep; MERS-CoV 1a-1b TTOA6YT FC Responsible for replication and transcription of the viral RNA genome. TTOA6YT EC EC 2.7.7.48 TTOA6YT SQ SKDSNFLKRVRGSIVNARIEPCSSGLSTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVELDDQGHHLDSYFVVKRHTMENYELEKHCYDLLRDCDAVAPHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNSEVLKAILVKYGCCDVTYFENKLWFDFVENPSVIGVYHKLGERVRQAILNTVKFCDHMVKAGLVGVLTLDNQDLNGKWYDFGDFVITQPGSGVAIVDSYYSYLMPVLSMTDCLAAETHRDCDFNKPLIEWPLTEYDFTDYKVQLFEKYFKYWDQTYHANCVNCTDDRCVLHCANFNVLFAMTMPKTCFGPIVRKIFVDGVPFVVSCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASSNAFLDLRTSCFSVAALTTGLTFQTVRPGNFNQDFYDFVVSKGFFKEGSSVTLKHFFFAQDGNAAITDYNYYSYNLPTMCDIKQMLFCMEVVNKYFEIYDGGCLNASEVVVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAMTKRNVIPTMTQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGATCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYIAGIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHEDIEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDNSAKFWEEAFYRDLYSSPTTLQ TTPZG3C ID TTPZG3C TTPZG3C TN SARS-CoV 3C-like protease (3CLpro) TTPZG3C UP P0C6X7 (3241-3546) TTPZG3C UC R1AB_CVHSA (3241-3546) TTPZG3C BC Coronaviruses polyprotein 1ab family TTPZG3C SN SARS-CoV 3C-like protease; SARS-CoV 3CLp; SARS-CoV 3CL-PRO; SARS-CoV 3CLpro TTPZG3C GN SARS-CoV rep; SARS-CoV 1a-1b TTPZG3C FC Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH. TTPZG3C EC EC 3.4.22.- TTPZG3C SQ SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTILEDEFTPFDVVRQCSGVTFQ TTL3H2W ID TTL3H2W TTL3H2W TN SARS-CoV envelope small membrane protein (E) TTL3H2W UP P59637 TTL3H2W UC VEMP_CVHSA TTL3H2W BC Betacoronaviruses E protein family. TTL3H2W SN SARS-CoV E protein; SARS-CoV sM protein TTL3H2W GN SARS-CoV E; SARS-CoV 4; SARS-CoV sM TTL3H2W FC Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis (By similarity). Activates the host NLRP3 inflammasome, leading to IL-1beta overproduction. TTL3H2W PD 2MM4; 5X29 TTL3H2W SQ MYSFVSEETGTLIVNSVLLFLAFVVFLLVTLAILTALRLCAYCCNIVNVSLVKPTVYVYSRVKNLNSSEGVPDLLV TTQKWR5 ID TTQKWR5 TTQKWR5 TN SARS-CoV helicase (Hel) TTQKWR5 UP P0C6X7 (5302-5902) TTQKWR5 UC R1AB_CVHSA (5302-5902) TTQKWR5 BC Coronaviruses polyprotein 1ab family TTQKWR5 SN SARS-CoV Helicase; SARS-CoV Hel TTQKWR5 GN SARS-CoV rep; SARS-CoV 1a-1b TTQKWR5 FC Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. TTQKWR5 EC EC 3.6.4.12 TTQKWR5 SQ AMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNVNRFNVAITRAKIGILCIMSDRDLYDKLQFTSLE TTRGHB2 ID TTRGHB2 TTRGHB2 TN SARS-CoV papain-like proteinase (PL-PRO) TTRGHB2 UP P0C6X7 (819-2740) TTRGHB2 UC R1AB_CVHSA (819-2740) TTRGHB2 BC Coronaviruses polyprotein 1ab family TTRGHB2 SN SARS-CoV papain-like proteinase; SARS-CoV PL2-PRO; SARS-CoV PL-PRO; SARS-CoV SARS coronavirus main proteinase; Non-structural protein 3 TTRGHB2 GN SARS-CoV rep; SARS-CoV 1a-1b TTRGHB2 FC Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6 together are sufficient to form DMV. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. TTRGHB2 EC EC 3.4.19.12 TTRGHB2 SQ PIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAVVKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGLPLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAANIHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQKPVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRARAGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGVSIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQMTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENTSITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFTKSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYCNGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVECTTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCATTRQVVNVITTKISLKGG TTKXI53 ID TTKXI53 TTKXI53 TN SARS-CoV RNA-directed RNA polymerase (RdRp) TTKXI53 UP P0C6X7 (4370-5301) TTKXI53 UC R1AB_CVHSA (4370-5301) TTKXI53 BC Coronaviruses polyprotein 1ab family TTKXI53 SN SARS-CoV RNA-directed RNA polymerase; SARS-CoV Pol; SARS-CoV RdRp; SARS-CoV nsp12 polymerase TTKXI53 GN SARS-CoV rep; SARS-CoV 1a-1b TTKXI53 FC Responsible for replication and transcription of the viral RNA genome. TTKXI53 EC EC 2.7.7.48 TTKXI53 SQ SADASTFLNRVCGVSAARLTPCGTGTSTDVVYRAFDIYNEKVAGFAKFLKTNCCRFQEKDEEGNLLDSYFVVKRHTMSNYQHEETIYNLVKDCPAVAVHDFFKFRVDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQSLLKTVQFCDAMRDAGIVGVLTLDNQDLNGNWYDFGDFVQVAPGCGVPIVDSYYSLLMPILTLTRALAAESHMDADLAKPLIKWDLLKYDFTEERLCLFDRYFKYWDQTYHPNCINCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVETPHLMGWDYPKCDRAMPNMLRIMASLVLARKHNTCCNLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDHEFVDEFYAYLRKHFSMMILSDDAVVCYNSNYAAQGLVASIKNFKAVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQ TTTL19V ID TTTL19V TTTL19V TN SARS-CoV spike glycoprotein (S) TTTL19V UP P59594 TTTL19V UC SPIKE_CVHSA TTTL19V BC Betacoronaviruses spike protein family TTTL19V SN S glycoprotein; Spike glycoprotein; E2; Peplomer protein TTTL19V GN SARS-CoV S; SARS-CoV 2 TTTL19V FC Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 and CLEC4M/DC-SIGNR receptors and internalization of the virus into the endosomes of the host cell induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes. TTTL19V PD 1WNC; 1WYY; 1ZV7 TTTL19V SQ MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT TT85VHW ID TT85VHW TT85VHW TN MERS-CoV spike glycoprotein (S) TT85VHW UP A0A140AYZ5 TT85VHW UC A0A140AYZ5_9BETC TT85VHW BC Betacoronaviruses spike protein family TT85VHW SN MERS-CoV S glycoprotein; MERS-CoV E2; MERS-CoV Peplomer protein TT85VHW GN MERS-CoV S TT85VHW FC Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. TT85VHW SQ MIHSVFLLMFLLTPTESYVDVGPDSVKSACIEVDIQQTFFDKTWPRPIDVSKADGIIYPQGRTYSNITITYQGLFPYQGDHGDMYVYSAGHATGTTPQKLFVANYSQDVKQFANGFVVRIGAAANSTGTVIISPSTSATIRKIYPAFMLGSSVGNFSDGKMGRFFNHTLVLLPDGCGTLLRAFYCILEPRSGNHCPAGNSYTSFATYHTPATDCSDGNYNRNASLNSFKEYFNLRNCTFMYTYNITEDEILEWFGITQTAQGVHLFSSRYVDLYGGNMFQFATLPVYDTIKYYSIIPHSIRSIQSDRKAWAAFYVYKLQPLTFLLDFSVDGYIRRAIDCGFNDLSQLHCSYESFDVESGVYSVSSFEAKPSGSVVEQAEGVECDFSPLLSGTPPQVYNFKRLVFTNCNYNLTKLLSLFSVNDFTCSQISPAAIASNCYSSLILDYFSYPLSMKSDLSVSSAGPISQFNYKQSFSNPTCLILATVPHNLTTITKPLKYSYINKCSRLLSDDRTEVPQLVNANQYSPCVSTVPSTVWEDGDYYRKQLSPLEGGGWLVASGSTVAMTEQLQMGFGITVQYGTDTNSVCPKLEFANDTKIASQLGNCVEYSLYGVSGRGVFQNCTAVGVRQQRFVYDAYQNLVGYYSDDGNYYCLRACVSVPVSVIYDKETKTHATLFGSVACEHISSTMSQYSRSTRSMLKRRDSTYGPLQTPVGCVLGLVNSSLFVEDCKLPLGQSLCALPDTPSTLTPRSVRSVPGEMRLASIAFNHPIQVDQLNSSYFKLSIPTNFSFGVTQEYIQTTIQKVTVDCKQYVCNGFQKCEQLLREYGQFCSKINQALHGANLRQDDSVRNLFASVKSSQSSPIIPGFGGDFNLTLLEPVSISTGSRSARSAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFRKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPQVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH TTJ4EIV ID TTJ4EIV TTJ4EIV TN MERS-CoV spike glycoprotein S2 subunit (S S2) TTJ4EIV UP A0A140AYZ5 (748-1353) TTJ4EIV UC A0A140AYZ5_9BETC (748-1353) TTJ4EIV BC Betacoronaviruses spike protein family TTJ4EIV SN MERS-CoV S glycoprotein S2 subunit; MERS-CoV E2 S2 subunit; MERS-CoV Peplomer protein S2 subunit TTJ4EIV GN MERS-CoV S TTJ4EIV FC Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. TTJ4EIV SQ TPSTLTPRSVRSVPGEMRLASIAFNHPIQVDQLNSSYFKLSIPTNFSFGVTQEYIQTTIQKVTVDCKQYVCNGFQKCEQLLREYGQFCSKINQALHGANLRQDDSVRNLFASVKSSQSSPIIPGFGGDFNLTLLEPVSISTGSRSARSAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFRKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPQVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH TT6MSOK ID TT6MSOK TT6MSOK TN 5-HT 1D receptor (HTR1D) TT6MSOK UP P28221 TT6MSOK UC 5HT1D_HUMAN TT6MSOK BC GPCR rhodopsin TT6MSOK SN Serotonin receptor 1D; Serotonin 1D alpha receptor; HTRL; HTR1DA; 5HT1D; 5-hydroxytryptamine receptor 1D; 5-HT1D receptor; 5-HT1D; 5-HT-1D-alpha; 5-HT-1D TT6MSOK GN HTR1D TT6MSOK FC Functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction. G-protein coupled receptor for 5-hydroxytryptamine (serotonin). TT6MSOK SQ MSPLNQSAEGLPQEASNRSLNATETSEAWDPRTLQALKISLAVVLSVITLATVLSNAFVLTTILLTRKLHTPANYLIGSLATTDLLVSILVMPISIAYTITHTWNFGQILCDIWLSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAATMIAIVWAISICISIPPLFWRQAKAQEEMSDCLVNTSQISYTIYSTCGAFYIPSVLLIILYGRIYRAARNRILNPPSLYGKRFTTAHLITGSAGSSLCSLNSSLHEGHSHSAGSPLFFNHVKIKLADSALERKRISAARERKATKILGIILGAFIICWLPFFVVSLVLPICRDSCWIHPALFDFFTWLGYLNSLINPIIYTVFNEEFRQAFQKIVPFRKAS TT6MSOK TT Successful TT6MSOK KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse TT6MSOK RC R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events TTPC4TU ID TTPC4TU TTPC4TU TN 5-HT 3A receptor (HTR3A) TTPC4TU UP P46098 TTPC4TU UC 5HT3A_HUMAN TTPC4TU BC GPCR rhodopsin TTPC4TU SN Serotonin-gated ion channel receptor; Serotonin receptor 3A; HTR3; 5HT3R; 5-hydroxytryptamine receptor 3A; 5-HT3RA; 5-HT3A; 5-HT3-A; 5-HT 3A TTPC4TU GN HTR3A TTPC4TU FC This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses in neurons. It is a cation-specific, but otherwise relatively nonselective, ion channel. TTPC4TU SQ MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA TTPC4TU TT Successful TTPC4TU KE hsa04726:Serotonergic synapse TTPC4TU RC R-HSA-975298:Ligand-gated ion channel transport TTFZDNP ID TTFZDNP TTFZDNP TN Activation B7-1 antigen (CD80) TTFZDNP UP P33681 TTFZDNP UC CD80_HUMAN TTFZDNP SN T-lymphocyte activation antigen CD80; LAB7; CTLA-4 counter-receptor B7.1; CD28LG1; CD28LG; BB1; B7 TTFZDNP GN CD80 TTFZDNP FC T-cell proliferation and cytokine production is induced by the binding of CD28, binding to CTLA-4 has opposite effects and inhibits T-cell activation. Involved in the costimulatory signal essential for T-lymphocyte activation. TTFZDNP PD 1I8L; 1DR9 TTFZDNP SQ MGHTRRQGTSPSKCPYLNFFQLLVLAGLSHFCSGVIHVTKEVKEVATLSCGHNVSVEELAQTRIYWQKEKKMVLTMMSGDMNIWPEYKNRTIFDITNNLSIVILALRPSDEGTYECVVLKYEKDAFKREHLAEVTLSVKADFPTPSISDFEIPTSNIRRIICSTSGGFPEPHLSWLENGEELNAINTTVSQDPETELYAVSSKLDFNMTTNHSFMCLIKYGHLRVNQTFNWNTTKQEHFPDNLLPSWAITLISVNGIFVICCLTYCFAPRCRERRRNERLRRESVRPV TTFZDNP TT Successful TTFZDNP KE hsa04514:Cell adhesion molecules (CAMs); hsa04620:Toll-like receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa04940:Type I diabetes mellitus; hsa05320:Autoimmune thyroid disease; hsa05322:Systemic lupus erythematosus; hsa05323:Rheumatoid arthritis; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease; hsa05416:Viral myocarditis TTFZDNP RC R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-389356:CD28 co-stimulation; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389359:CD28 dependent Vav1 pathway; R-HSA-389513:CTLA4 inhibitory signaling TTNE7KG ID TTNE7KG TTNE7KG TN Adenosine A2b receptor (ADORA2B) TTNE7KG UP P29275 TTNE7KG UC AA2BR_HUMAN TTNE7KG BC GPCR rhodopsin TTNE7KG SN Adenosine receptor A2b; A2b Adenosine receptor TTNE7KG GN ADORA2B TTNE7KG FC The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Receptor for adenosine. TTNE7KG SQ MLLETQDALYVALELVIAALSVAGNVLVCAAVGTANTLQTPTNYFLVSLAAADVAVGLFAIPFAITISLGFCTDFYGCLFLACFVLVLTQSSIFSLLAVAVDRYLAICVPLRYKSLVTGTRARGVIAVLWVLAFGIGLTPFLGWNSKDSATNNCTEPWDGTTNESCCLVKCLFENVVPMSYMVYFNFFGCVLPPLLIMLVIYIKIFLVACRQLQRTELMDHSRTTLQREIHAAKSLAMIVGIFALCWLPVHAVNCVTLFQPAQGKNKPKWAMNMAILLSHANSVVNPIVYAYRNRDFRYTFHKIISRYLLCQADVKSGNGQAGVQPALGVGL TTNE7KG TT Successful TTNE7KG FM GPCR rhodopsin TTNE7KG KE hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction; hsa05034:Alcoholism TTNE7KG RC R-HSA-417973:Adenosine P1 receptors; R-HSA-418555:G alpha (s) signalling events; R-HSA-5683826:Surfactant metabolism TTV1ZSQ ID TTV1ZSQ TTV1ZSQ TN Adenylate cyclase type 1 (ADCY1) TTV1ZSQ UP Q08828 TTV1ZSQ UC ADCY1_HUMAN TTV1ZSQ BC Phosphorus-oxygen lyase TTV1ZSQ SN Ca(2+)/calmodulin-activated adenylyl cyclase; Adenylyl cyclase 1; Adenylate cyclase type I; ATP pyrophosphate-lyase 1 TTV1ZSQ GN ADCY1 TTV1ZSQ FC Mediates responses to increased cellular Ca(2+)/calmodulin levels. May be involved in regulatory processes in the central nervous system. May play a role in memory and learning. Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina. Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. TTV1ZSQ EC EC 4.6.1.1 TTV1ZSQ SQ MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAATLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQQVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVRSLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQRKAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSHRRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALRTASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQKYHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRVQCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALPTLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAVSGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNLLPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEIIADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFDVLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQVTEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRAGLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA TTV1ZSQ TT Successful TTV1ZSQ FM Phosphorus-oxygen lyases TTV1ZSQ KE hsa00230:Purine metabolism; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04114:Oocyte meiosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04540:Gap junction; hsa04611:Platelet activation; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04727:GABAergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04911:Insulin secretion; hsa04912:GnRH signaling pathway; hsa04913:Ovarian steroidogenesis; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04918:Thyroid hormone synthesis; hsa04921:Oxytocin signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04976:Bile secretion; hsa05032:Morphine addiction; hsa05142:Chagas disease (American trypanosomiasis); hsa05146:Amoebiasis; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05414:Dilated cardiomyopathy TTV1ZSQ RC R-HSA-163359:Glucagon signaling in metabolic regulation; R-HSA-163615:PKA activation; R-HSA-164378:PKA activation in glucagon signalling; R-HSA-418555:G alpha (s) signalling events; R-HSA-418594:G alpha (i) signalling events; R-HSA-418597:G alpha (z) signalling events; R-HSA-432040:Vasopressin regulates renal water homeostasis via Aquaporins; R-HSA-5610787:Hedgehog 'off' state TTNGILX ID TTNGILX TTNGILX TN Adrenergic receptor alpha-1A (ADRA1A) TTNGILX UP P35348 TTNGILX UC ADA1A_HUMAN TTNGILX BC GPCR rhodopsin TTNGILX SN Alpha-adrenergic receptor 1c; Alpha-1C adrenergic receptor; Alpha-1A adrenoreceptor; Alpha-1A adrenoceptor; Alpha-1A adrenergic receptor; Alpha adrenergic receptor 1c; Alpha 1A-adrenoreceptor; Alpha 1A-adrenoceptor; ADRA1C TTNGILX GN ADRA1A TTNGILX FC Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes. This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. TTNGILX SQ MVFLSGNASDSSNCTQPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV TTNGILX TT Successful TTNGILX FM GPCR rhodopsin TTNGILX KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04152:AMPK signaling pathway; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04970:Salivary secretion TTNGILX RC R-HSA-390696:Adrenoceptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-416482:G alpha (12/13) signalling events TTWG9A4 ID TTWG9A4 TTWG9A4 TN Adrenergic receptor alpha-2A (ADRA2A) TTWG9A4 UP P08913 TTWG9A4 UC ADA2A_HUMAN TTWG9A4 BC GPCR rhodopsin TTWG9A4 SN Alpha-2AAR; Alpha-2A adrenoreceptor; Alpha-2A adrenoceptor; Alpha-2A adrenergic receptor; Alpha-2 adrenergic receptor subtype C10; ADRAR; ADRA2R TTWG9A4 GN ADRA2A TTWG9A4 FC The rank order of potency for agonists of this receptor is oxymetazoline > clonidine > epinephrine > norepinephrine > phenylephrine > dopamine > p-synephrine > p-tyramine > serotonin = p-octopamine. For antagonists, the rank order is yohimbine > phentolamine = mianserine > chlorpromazine = spiperone = prazosin > propanolol > alprenolol = pindolol. Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. TTWG9A4 PD 1HOF; 1HOD; 1HO9; 1HLL TTWG9A4 SQ MFRQEQPLAEGSFAPMGSLQPDAGNASWNGTEAPGGGARATPYSLQVTLTLVCLAGLLMLLTVFGNVLVIIAVFTSRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKAWCEIYLALDVLFCTSSIVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIITVWVISAVISFPPLISIEKKGGGGGPQPAEPRCEINDQKWYVISSCIGSFFAPCLIMILVYVRIYQIAKRRTRVPPSRRGPDAVAAPPGGTERRPNGLGPERSAGPGGAEAEPLPTQLNGAPGEPAPAGPRDTDALDLEESSSSDHAERPPGPRRPERGPRGKGKARASQVKPGDSLPRRGPGATGIGTPAAGPGEERVGAAKASRWRGRQNREKRFTFVLAVVIGVFVVCWFPFFFTYTLTAVGCSVPRTLFKFFFWFGYCNSSLNPVIYTIFNHDFRRAFKKILCRGDRKRIV TTWG9A4 TT Successful TTWG9A4 KE hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTWG9A4 RC R-HSA-390696:Adrenoceptors; R-HSA-392023:Adrenaline signalling through Alpha-2 adrenergic receptor; R-HSA-400042:Adrenaline,noradrenaline inhibits insulin secretion; R-HSA-418594:G alpha (i) signalling events; R-HSA-418597:G alpha (z) signalling events; R-HSA-5683826:Surfactant metabolism TTWM4TY ID TTWM4TY TTWM4TY TN Adrenergic receptor alpha-2B (ADRA2B) TTWM4TY UP P18089 TTWM4TY UC ADA2B_HUMAN TTWM4TY BC GPCR rhodopsin TTWM4TY SN Subtype C2; Alpha-2BAR; Alpha-2B adrenoreceptor; Alpha-2B adrenoceptor; Alpha-2B adrenergic receptor; Alpha-2 adrenergic receptor subtype C2; ADRA2RL1; ADRA2L1 TTWM4TY GN ADRA2B TTWM4TY FC The rank order of potency for agonists of this receptor is clonidine > norepinephrine > epinephrine = oxymetazoline > dopamine > p-tyramine = phenylephrine > serotonin > p-synephrine / p-octopamine. For antagonists, the rank order is yohimbine > chlorpromazine > phentolamine > mianserine > spiperone > prazosin > alprenolol > propanolol > pindolol. Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. TTWM4TY PD 2CVA TTWM4TY SQ MDHQDPYSVQATAAIAAAITFLILFTIFGNALVILAVLTSRSLRAPQNLFLVSLAAADILVATLIIPFSLANELLGYWYFRRTWCEVYLALDVLFCTSSIVHLCAISLDRYWAVSRALEYNSKRTPRRIKCIILTVWLIAAVISLPPLIYKGDQGPQPRGRPQCKLNQEAWYILASSIGSFFAPCLIMILVYLRIYLIAKRSNRRGPRAKGGPGQGESKQPRPDHGGALASAKLPALASVASAREVNGHSKSTGEKEEGETPEDTGTRALPPSWAALPNSGQGQKEGVCGASPEDEAEEEEEEEEEEEECEPQAVPVSPASACSPPLQQPQGSRVLATLRGQVLLGRGVGAIGGQWWRRRAQLTREKRFTFVLAVVIGVFVLCWFPFFFSYSLGAICPKHCKVPHGLFQFFFWIGYCNSSLNPVIYTIFNQDFRRAFRRILCRPWTQTAW TTWM4TY TT Successful TTWM4TY KE hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTWM4TY RC R-HSA-390696:Adrenoceptors; R-HSA-392023:Adrenaline signalling through Alpha-2 adrenergic receptor; R-HSA-418594:G alpha (i) signalling events; R-HSA-418597:G alpha (z) signalling events TT2NUT5 ID TT2NUT5 TT2NUT5 TN Adrenergic receptor alpha-2C (ADRA2C) TT2NUT5 UP P18825 TT2NUT5 UC ADA2C_HUMAN TT2NUT5 BC GPCR rhodopsin TT2NUT5 SN Subtype C4; Alpha-2CAR; Alpha-2C adrenoreceptor; Alpha-2C adrenoceptor; Alpha-2C adrenergic receptor; Alpha-2 adrenergic receptor subtype C4; ADRA2RL2; ADRA2L2 TT2NUT5 GN ADRA2C TT2NUT5 FC Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. TT2NUT5 SQ MASPALAAALAVAAAAGPNASGAGERGSGGVANASGASWGPPRGQYSAGAVAGLAAVVGFLIVFTVVGNVLVVIAVLTSRALRAPQNLFLVSLASADILVATLVMPFSLANELMAYWYFGQVWCGVYLALDVLFCTSSIVHLCAISLDRYWSVTQAVEYNLKRTPRRVKATIVAVWLISAVISFPPLVSLYRQPDGAAYPQCGLNDETWYILSSCIGSFFAPCLIMGLVYARIYRVAKLRTRTLSEKRAPVGPDGASPTTENGLGAAAGAGENGHCAPPPADVEPDESSAAAERRRRRGALRRGGRRRAGAEGGAGGADGQGAGPGAAESGALTASRSPGPGGRLSRASSRSVEFFLSRRRRARSSVCRRKVAQAREKRFTFVLAVVMGVFVLCWFPFFFSYSLYGICREACQVPGPLFKFFFWIGYCNSSLNPVIYTVFNQDFRRSFKHILFRRRRRGFRQ TT2NUT5 TT Successful TT2NUT5 KE hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TT2NUT5 RC R-HSA-390696:Adrenoceptors; R-HSA-392023:Adrenaline signalling through Alpha-2 adrenergic receptor; R-HSA-400042:Adrenaline,noradrenaline inhibits insulin secretion; R-HSA-418594:G alpha (i) signalling events; R-HSA-418597:G alpha (z) signalling events; R-HSA-5683826:Surfactant metabolism TTR6W5O ID TTR6W5O TTR6W5O TN Adrenergic receptor beta-1 (ADRB1) TTR6W5O UP P08588 TTR6W5O UC ADRB1_HUMAN TTR6W5O BC GPCR rhodopsin TTR6W5O SN Beta-1 adrenoreceptor; Beta-1 adrenoceptor; Beta-1 adrenergic receptor; B1AR; ADRB1R TTR6W5O GN ADRB1 TTR6W5O FC Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling. TTR6W5O PD 2LSQ TTR6W5O SQ MGAGVLVLGASEPGNLSSAAPLPDGAATAARLLVPASPPASLLPPASESPEPLSQQWTAGMGLLMALIVLLIVAGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTRARARGLVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLGGPARPPSPSPSPVPAPAPPPGPPRPAAAAATAPLANGRAGKRRPSRLVALREQKALKTLGIIMGVFTLCWLPFFLANVVKAFHRELVPDRLFVFFNWLGYANSAFNPIIYCRSPDFRKAFQRLLCCARRAARRRHATHGDRPRASGCLARPGPPPSPGAASDDDDDDVVGATPPARLLEPWAGCNGGAAADSDSSLDEPCRPGFASESKV TTR6W5O TT Successful TTR6W5O FM GPCR rhodopsin TTR6W5O KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04144:Endocytosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04540:Gap junction; hsa04970:Salivary secretion; hsa05414:Dilated cardiomyopathy TTR6W5O RC R-HSA-390696:Adrenoceptors; R-HSA-418555:G alpha (s) signalling events TTA7UJC ID TTA7UJC TTA7UJC TN Alpha-1-antitrypsin (SERPINA1) TTA7UJC UP P01009 TTA7UJC UC A1AT_HUMAN TTA7UJC BC Serpin protein TTA7UJC SN SERPINA1; PRO0684/PRO2209; Alpha1-proteinase; Alpha-1-antiproteinase; Alpha-1 protease inhibitor TTA7UJC GN SERPINA1 TTA7UJC FC Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. TTA7UJC PD 9API; 8API; 7API; 5NBV; 5NBU TTA7UJC SQ MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK TTA7UJC TT Successful TTA7UJC KE hsa04610:Complement and coagulation cascades TTA7UJC RC R-HSA-114608:Platelet degranulation; R-HSA-204005:COPII (Coat Protein 2) Mediated Vesicle Transport; R-HSA-5694530:Cargo concentration in the ER TTZFTY4 ID TTZFTY4 TTZFTY4 TN Amidophosphoribosyltransferase (PPAT) TTZFTY4 UP Q06203 TTZFTY4 UC PUR1_HUMAN TTZFTY4 BC Short-chain dehydrogenases reductase TTZFTY4 SN Glutamine phosphoribosylpyrophosphate amidotransferase; GPAT; ATase TTZFTY4 GN PPAT TTZFTY4 FC Catalyzes the conversion of 5-phosphoribosyl-1-pyrophosphate (PRPP) into 5-phosphoribosyl-1-amine (PRA), using the amine group from a glutamine side-chain. TTZFTY4 EC EC 2.4.2.14 TTZFTY4 SQ MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPTFKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFLSIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKEKKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW TTZFTY4 TT Successful TTZFTY4 KE hsa00230:Purine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways TTZFTY4 RC R-HSA-73817:Purine ribonucleoside monophosphate biosynthesis TT4QPUL ID TT4QPUL TT4QPUL TN Antithrombin-III (ATIII) TT4QPUL UP P01008 TT4QPUL UC ANT3_HUMAN TT4QPUL BC Serpin protein TT4QPUL SN SERPINC1; ATIII; AT3 TT4QPUL GN SERPINC1 TT4QPUL FC Most important serine protease inhibitorin plasma that regulates the blood coagulation cascade. At-iii inhibits thrombin as well as factors ixa, xa and xia. Its inhibitory activity is greatly enhanced in the presence of heparin. TT4QPUL PD 4EB1; 3KCG; 3EVJ; 2ZNH; 2HIJ TT4QPUL SQ MYSNVIGTVTSGKRKVYLLSLLLIGFWDCVTCHGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANPCVK TT4QPUL TT Successful TT4QPUL KE hsa04610:Complement and coagulation cascades TT4QPUL RC R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-140875:Common Pathway of Fibrin Clot Formation TTN1IE2 ID TTN1IE2 TTN1IE2 TN APOB messenger RNA (APOB mRNA) TTN1IE2 UP P04114 TTN1IE2 UC APOB_HUMAN TTN1IE2 BC mRNA target TTN1IE2 SN Apolipoprotein B48 (mRNA); Apolipoprotein B-100 (mRNA); Apo B48 (mRNA); Apo B100 (mRNA); Apo B-100 (mRNA) TTN1IE2 GN APOB TTN1IE2 FC Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor. Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). TTN1IE2 SQ MDPPRPALLALLALPALLLLLLAGARAEEEMLENVSLVCPKDATRFKHLRKYTYNYEAESSSGVPGTADSRSATRINCKVELEVPQLCSFILKTSQCTLKEVYGFNPEGKALLKKTKNSEEFAAAMSRYELKLAIPEGKQVFLYPEKDEPTYILNIKRGIISALLVPPETEEAKQVLFLDTVYGNCSTHFTVKTRKGNVATEISTERDLGQCDRFKPIRTGISPLALIKGMTRPLSTLISSSQSCQYTLDAKRKHVAEAICKEQHLFLPFSYKNKYGMVAQVTQTLKLEDTPKINSRFFGEGTKKMGLAFESTKSTSPPKQAEAVLKTLQELKKLTISEQNIQRANLFNKLVTELRGLSDEAVTSLLPQLIEVSSPITLQALVQCGQPQCSTHILQWLKRVHANPLLIDVVTYLVALIPEPSAQQLREIFNMARDQRSRATLYALSHAVNNYHKTNPTGTQELLDIANYLMEQIQDDCTGDEDYTYLILRVIGNMGQTMEQLTPELKSSILKCVQSTKPSLMIQKAAIQALRKMEPKDKDQEVLLQTFLDDASPGDKRLAAYLMLMRSPSQADINKIVQILPWEQNEQVKNFVASHIANILNSEELDIQDLKKLVKEALKESQLPTVMDFRKFSRNYQLYKSVSLPSLDPASAKIEGNLIFDPNNYLPKESMLKTTLTAFGFASADLIEIGLEGKGFEPTLEALFGKQGFFPDSVNKALYWVNGQVPDGVSKVLVDHFGYTKDDKHEQDMVNGIMLSVEKLIKDLKSKEVPEARAYLRILGEELGFASLHDLQLLGKLLLMGARTLQGIPQMIGEVIRKGSKNDFFLHYIFMENAFELPTGAGLQLQISSSGVIAPGAKAGVKLEVANMQAELVAKPSVSVEFVTNMGIIIPDFARSGVQMNTNFFHESGLEAHVALKAGKLKFIIPSPKRPVKLLSGGNTLHLVSTTKTEVIPPLIENRQSWSVCKQVFPGLNYCTSGAYSNASSTDSASYYPLTGDTRLELELRPTGEIEQYSVSATYELQREDRALVDTLKFVTQAEGAKQTEATMTFKYNRQSMTLSSEVQIPDFDVDLGTILRVNDESTEGKTSYRLTLDIQNKKITEVALMGHLSCDTKEERKIKGVISIPRLQAEARSEILAHWSPAKLLLQMDSSATAYGSTVSKRVAWHYDEEKIEFEWNTGTNVDTKKMTSNFPVDLSDYPKSLHMYANRLLDHRVPQTDMTFRHVGSKLIVAMSSWLQKASGSLPYTQTLQDHLNSLKEFNLQNMGLPDFHIPENLFLKSDGRVKYTLNKNSLKIEIPLPFGGKSSRDLKMLETVRTPALHFKSVGFHLPSREFQVPTFTIPKLYQLQVPLLGVLDLSTNVYSNLYNWSASYSGGNTSTDHFSLRARYHMKADSVVDLLSYNVQGSGETTYDHKNTFTLSYDGSLRHKFLDSNIKFSHVEKLGNNPVSKGLLIFDASSSWGPQMSASVHLDSKKKQHLFVKEVKIDGQFRVSSFYAKGTYGLSCQRDPNTGRLNGESNLRFNSSYLQGTNQITGRYEDGTLSLTSTSDLQSGIIKNTASLKYENYELTLKSDTNGKYKNFATSNKMDMTFSKQNALLRSEYQADYESLRFFSLLSGSLNSHGLELNADILGTDKINSGAHKATLRIGQDGISTSATTNLKCSLLVLENELNAELGLSGASMKLTTNGRFREHNAKFSLDGKAALTELSLGSAYQAMILGVDSKNIFNFKVSQEGLKLSNDMMGSYAEMKFDHTNSLNIAGLSLDFSSKLDNIYSSDKFYKQTVNLQLQPYSLVTTLNSDLKYNALDLTNNGKLRLEPLKLHVAGNLKGAYQNNEIKHIYAISSAALSASYKADTVAKVQGVEFSHRLNTDIAGLASAIDMSTNYNSDSLHFSNVFRSVMAPFTMTIDAHTNGNGKLALWGEHTGQLYSKFLLKAEPLAFTFSHDYKGSTSHHLVSRKSISAALEHKVSALLTPAEQTGTWKLKTQFNNNEYSQDLDAYNTKDKIGVELTGRTLADLTLLDSPIKVPLLLSEPINIIDALEMRDAVEKPQEFTIVAFVKYDKNQDVHSINLPFFETLQEYFERNRQTIIVVLENVQRNLKHINIDQFVRKYRAALGKLPQQANDYLNSFNWERQVSHAKEKLTALTKKYRITENDIQIALDDAKINFNEKLSQLQTYMIQFDQYIKDSYDLHDLKIAIANIIDEIIEKLKSLDEHYHIRVNLVKTIHDLHLFIENIDFNKSGSSTASWIQNVDTKYQIRIQIQEKLQQLKRHIQNIDIQHLAGKLKQHIEAIDVRVLLDQLGTTISFERINDILEHVKHFVINLIGDFEVAEKINAFRAKVHELIERYEVDQQIQVLMDKLVELAHQYKLKETIQKLSNVLQQVKIKDYFEKLVGFIDDAVKKLNELSFKTFIEDVNKFLDMLIKKLKSFDYHQFVDETNDKIREVTQRLNGEIQALELPQKAEALKLFLEETKATVAVYLESLQDTKITLIINWLQEALSSASLAHMKAKFRETLEDTRDRMYQMDIQQELQRYLSLVGQVYSTLVTYISDWWTLAAKNLTDFAEQYSIQDWAKRMKALVEQGFTVPEIKTILGTMPAFEVSLQALQKATFQTPDFIVPLTDLRIPSVQINFKDLKNIKIPSRFSTPEFTILNTFHIPSFTIDFVEMKVKIIRTIDQMLNSELQWPVPDIYLRDLKVEDIPLARITLPDFRLPEIAIPEFIIPTLNLNDFQVPDLHIPEFQLPHISHTIEVPTFGKLYSILKIQSPLFTLDANADIGNGTTSANEAGIAASITAKGESKLEVLNFDFQANAQLSNPKINPLALKESVKFSSKYLRTEHGSEMLFFGNAIEGKSNTVASLHTEKNTLELSNGVIVKINNQLTLDSNTKYFHKLNIPKLDFSSQADLRNEIKTLLKAGHIAWTSSGKGSWKWACPRFSDEGTHESQISFTIEGPLTSFGLSNKINSKHLRVNQNLVYESGSLNFSKLEIQSQVDSQHVGHSVLTAKGMALFGEGKAEFTGRHDAHLNGKVIGTLKNSLFFSAQPFEITASTNNEGNLKVRFPLRLTGKIDFLNNYALFLSPSAQQASWQVSARFNQYKYNQNFSAGNNENIMEAHVGINGEANLDFLNIPLTIPEMRLPYTIITTPPLKDFSLWEKTGLKEFLKTTKQSFDLSVKAQYKKNKHRHSITNPLAVLCEFISQSIKSFDRHFEKNRNNALDFVTKSYNETKIKFDKYKAEKSHDELPRTFQIPGYTVPVVNVEVSPFTIEMSAFGYVFPKAVSMPSFSILGSDVRVPSYTLILPSLELPVLHVPRNLKLSLPDFKELCTISHIFIPAMGNITYDFSFKSSVITLNTNAELFNQSDIVAHLLSSSSSVIDALQYKLEGTTRLTRKRGLKLATALSLSNKFVEGSHNSTVSLTTKNMEVSVATTTKAQIPILRMNFKQELNGNTKSKPTVSSSMEFKYDFNSSMLYSTAKGAVDHKLSLESLTSYFSIESSTKGDVKGSVLSREYSGTIASEANTYLNSKSTRSSVKLQGTSKIDDIWNLEVKENFAGEATLQRIYSLWEHSTKNHLQLEGLFFTNGEHTSKATLELSPWQMSALVQVHASQPSSFHDFPDLGQEVALNANTKNQKIRWKNEVRIHSGSFQSQVELSNDQEKAHLDIAGSLEGHLRFLKNIILPVYDKSLWDFLKLDVTTSIGRRQHLRVSTAFVYTKNPNGYSFSIPVKVLADKFIIPGLKLNDLNSVLVMPTFHVPFTDLQVPSCKLDFREIQIYKKLRTSSFALNLPTLPEVKFPEVDVLTKYSQPEDSLIPFFEITVPESQLTVSQFTLPKSVSDGIAALDLNAVANKIADFELPTIIVPEQTIEIPSIKFSVPAGIVIPSFQALTARFEVDSPVYNATWSASLKNKADYVETVLDSTCSSTVQFLEYELNVLGTHKIEDGTLASKTKGTFAHRDFSAEYEEDGKYEGLQEWEGKAHLNIKSPAFTDLHLRYQKDKKGISTSAASPAVGTVGMDMDEDDDFSKWNFYYSPQSSPDKKLTIFKTELRVRESDEETQIKVNWEEEAASGLLTSLKDNVPKATGVLYDYVNKYHWEHTGLTLREVSSKLRRNLQNNAEWVYQGAIRQIDDIDVRFQKAASGTTGTYQEWKDKAQNLYQELLTQEGQASFQGLKDNVFDGLVRVTQEFHMKVKHLIDSLIDFLNFPRFQFPGKPGIYTREELCTMFIREVGTVLSQVYSKVHNGSEILFSYFQDLVITLPFELRKHKLIDVISMYRELLKDLSKEAQEVFKAIQSLKTTEVLRNLQDLLQFIFQLIEDNIKQLKEMKFTYLINYIQDEINTIFSDYIPYVFKLLKENLCLNLHKFNEFIQNELQEASQELQQIHQYIMALREEYFDPSIVGWTVKYYELEEKIVSLIKNLLVALKDFHSEYIVSASNFTSQLSSQVEQFLHRNIQEYLSILTDPDGKGKEKIAELSATAQEIIKSQAIATKKIISDYHQQFRYKLQDFSDQLSDYYEKFIAESKRLIDLSIQNYHTFLIYITELLKKLQSTTVMNPYMKLAPGELTIIL TTN1IE2 TT Successful TTN1IE2 FM mRNA target TTN1IE2 KE hsa04975:Fat digestion and absorption; hsa04977:Vitamin digestion and absorption TTN1IE2 RC R-HSA-171052:LDL-mediated lipid transport; R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-3000471:Scavenging by Class B Receptors; R-HSA-3000480:Scavenging by Class A Receptors; R-HSA-3000497:Scavenging by Class H Receptors; R-HSA-432142:Platelet sensitization by LDL; R-HSA-975634:Retinoid metabolism and transport TT4WT91 ID TT4WT91 TT4WT91 TN Asparaginase (ASRGL1) TT4WT91 UP Q7L266 TT4WT91 UC ASGL1_HUMAN TT4WT91 BC Peptidase TT4WT91 SN Lasparagine amidohydrolase; Isoaspartyl peptidase/Lasparaginase beta chain; Isoaspartyl peptidase/Lasparaginase; Isoaspartyl dipeptidase; Betaaspartylpeptidase; Asparaginaselike protein 1; ASRGL1 TT4WT91 GN ASRGL1 TT4WT91 FC Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L- Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. TT4WT91 EC EC 3.4.19.5 TT4WT91 PD 4ZM9; 4PVS; 4PVR; 4PVQ; 4PVP TT4WT91 SQ MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP TT4WT91 TT Successful TTGY8IW ID TTGY8IW TTGY8IW TN B2 bradykinin receptor (BDKRB2) TTGY8IW UP P30411 TTGY8IW UC BKRB2_HUMAN TTGY8IW BC GPCR rhodopsin TTGY8IW SN Bradykinin B2 receptor; BKR2; BK-2 receptor; BK B(2) receptor; B2R TTGY8IW GN BDKRB2 TTGY8IW FC It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. Receptor for bradykinin. TTGY8IW SQ MFSPWKISMFLSVREDSVPTTASFSADMLNVTLQGPTLNGTFAQSKCPQVEWLGWLNTIQPPFLWVLFVLATLENIFVLSVFCLHKSSCTVAEIYLGNLAAADLILACGLPFWAITISNNFDWLFGETLCRVVNAIISMNLYSSICFLMLVSIDRYLALVKTMSMGRMRGVRWAKLYSLVIWGCTLLLSSPMLVFRTMKEYSDEGHNVTACVISYPSLIWEVFTNMLLNVVGFLLPLSVITFCTMQIMQVLRNNEMQKFKEIQTERRATVLVLVVLLLFIICWLPFQISTFLDTLHRLGILSSCQDERIIDVITQIASFMAYSNSCLNPLVYVIVGKRFRKKSWEVYQGVCQKGGCRSEPIQMENSMGTLRTSISVERQIHKLQDWAGSRQ TTGY8IW TT Successful TTGY8IW KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04610:Complement and coagulation cascades; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04810:Regulation of actin cytoskeleton; hsa04961:Endocrine and other factor-regulated calcium reabsorption; hsa05142:Chagas disease (American trypanosomiasis); hsa05200:Pathways in cancer TTGY8IW RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events TTLP6GN ID TTLP6GN TTLP6GN TN Bacterial DD-carboxypeptidase (Bact vanYB) TTLP6GN UP Q47746 TTLP6GN UC VANY_ENTFA TTLP6GN BC Peptidase TTLP6GN SN vanYB; DD-peptidase; DD-carboxypeptidase; D-alanyl-D-alanine carboxypeptidase-transpeptidase TTLP6GN GN Bact vanYB TTLP6GN FC Vancomycin-inducible, penicillin-resistant, DD- carboxypeptidase that hydrolyzes depsipeptide- and D-alanyl-D- alanine-containing peptidoglycan precursors. Insensitive to beta- lactams. TTLP6GN EC EC 3.4.16.4 TTLP6GN PD 6A6A; 5ZHW; 5ZHF; 5HNM TTLP6GN SQ MEKSNYHSNVNHHKRHMKQSGEKRAFLWAFIISFTVCTLFLGWRLVSVLEATQLPPIPATHTGSGTGVAENPEENTLATAKEQGDEQEWSLILVNRQNPIPAQYDVELEQLSNGERIDIRISPYLQDLFDAARADGVYPIVASGYRTTEKQQEIMDEKVAEYKAKGYTSAQAKAEAETWVAVPGTSEHQLGLAVDINADGIHSTGNEVYRWLDENSYRFGFIRRYPPDKTEITGVSNEPWHYRYVGIEAATKIYHQGLCLEEYLNTEK TTLP6GN TT Successful TT6KYJ5 ID TT6KYJ5 TT6KYJ5 TN Bacterial Isoleucyl-tRNA synthetase (Bact ileS) TT6KYJ5 UP P00956 TT6KYJ5 UC SYI_ECOLI TT6KYJ5 BC Carbon-oxygen ligase TT6KYJ5 SN ileS; Isoleucine--tRNA ligase of Escherichia coli; IRS of Escherichia coli TT6KYJ5 GN Bact ileS TT6KYJ5 FC Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). TT6KYJ5 EC EC 6.1.1.5 TT6KYJ5 SQ MSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIVKSKGLSGYDSPYVPGWDCHGLPIELKVEQEYGKPGEKFTAAEFRAKCREYAATQVDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGKIIGNGHLHKGAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFQAVDQDALKAKFAVSNVNGPISLVIWTTTPWTLPANRAISIAPDFDYALVQIDGQAVILAKDLVESVMQRIGVTDYTILGTVKGAELELLRFTHPFMGFDVPAILGDHVTLDAGTGAVHTAPGHGPDDYVIGQKYGLETANPVGPDGTYLPGTYPTLDGVNVFKANDIVVALLQEKGALLHVEKMQHSYPCCWRHKTPIIFRATPQWFVSMDQKGLRAQSLKEIKGVQWIPDWGQARIESMVANRPDWCISRQRTWGVPMSLFVHKDTEELHPRTLELMEEVAKRVEVDGIQAWWDLDAKEILGDEADQYVKVPDTLDVWFDSGSTHSSVVDVRPEFAGHAADMYLEGSDQHRGWFMSSLMISTAMKGKAPYRQVLTHGFTVDGQGRKMSKSIGNTVSPQDVMNKLGADILRLWVASTDYTGEMAVSDEILKRAADSYRRIRNTARFLLANLNGFDPAKDMVKPEEMVVLDRWAVGCAKAAQEDILKAYEAYDFHEVVQRLMRFCSVEMGSFYLDIIKDRQYTAKADSVARRSCQTALYHIAEALVRWMAPILSFTADEVWGYLPGEREKYVFTGEWYEGLFGLADSEAMNDAFWDELLKVRGEVNKVIEQARADKKVGGSLEAAVTLYAEPELSAKLTALGDELRFVLLTSGATVADYNDAPADAQQSEVLKGLKVALSKAEGEKCPRCWHYTQDVGKVAEHAEICGRCVSNVAGDGEKRKFA TT6KYJ5 TT Successful TTICX3S ID TTICX3S TTICX3S TN Bacterial UDP-N-acetylglucosamine carboxyvinyltransferase (Bact murA) TTICX3S UP P0A749 TTICX3S UC MURA_ECOLI TTICX3S BC Alkyl aryl transferase TTICX3S SN UDP-N-acetylglucosamine enolpyruvyl transferase; UDP-GlcNAcenolpyruvyl transferase; MurA protein; MurA; Enoylpyruvate transferase; EPT TTICX3S GN Bact murA TTICX3S FC Cell wall formation. Adds enolpyruvyl to UDP-n- acetylglucosamine. Target for the antibiotic phosphomycin. TTICX3S PD 3SWD; 3KR6; 3KQJ; 3ISS; 2Z2C TTICX3S SQ MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNGSVHIDARDVNVFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEGTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIERVKGE TTICX3S TT Successful TTJBPN3 ID TTJBPN3 TTJBPN3 TN Biliverdin reductase A (BLVRA) TTJBPN3 UP P53004 TTJBPN3 UC BIEA_HUMAN TTJBPN3 BC CH-CH donor oxidoreductase TTJBPN3 SN Biliverdin-IX alpha-reductase; BVR A; BVR; BLVRA; BLVR TTJBPN3 GN BLVRA TTJBPN3 FC Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor. TTJBPN3 EC EC 1.3.1.24 TTJBPN3 PD 2H63 TTJBPN3 SQ MNAEPERKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQQISLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERKEDQYMKMTVCLETEKKSPLSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVGVNKNIFLKDQNIFVQKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCSRK TTJBPN3 TT Successful TTJBPN3 KE hsa00860:Porphyrin and chlorophyll metabolism TTRLZHP ID TTRLZHP TTRLZHP TN cAMP-dependent chloride channel (CFTR) TTRLZHP UP P13569 TTRLZHP UC CFTR_HUMAN TTRLZHP BC ABC transporter TTRLZHP SN cAMPdependent chloride channel; Cystic fibrosis transmembrane conductance regulator; Channel conductancecontrolling ATPase; ATPbinding cassette subfamily C member 7; ATP-binding cassette sub-family C member 7; ABCC7 TTRLZHP GN CFTR TTRLZHP FC Mediates the transport of chloride ions across the cell membrane. Channel activity is coupled to ATP hydrolysis. The ion channel is also permeable to HCO(3-); selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Plays an important role in airway fluid homeostasis. Contributes to the regulation of the pH and the ion content of the airway surface fluid layer and thereby plays an important role in defense against pathogens. Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex. Inhibits the activity of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G. Inhibits the activity of the ENaC channel containing subunits SCNN1D, SCNN1B and SCNN1G, but not of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7. Can inhibit the chloride channel activity of ANO1. Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation. Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis. TTRLZHP EC EC 5.6.1.6 TTRLZHP PD 6MSM; 6HEP; 5UAK; 5TGK; 5TFJ TTRLZHP SQ MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL TTRLZHP TT Successful TTRLZHP FM Acid anhydrides hydrolase TTRLZHP KE hsa02010:ABC transporters; hsa04024:cAMP signaling pathway; hsa04152:AMPK signaling pathway; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04976:Bile secretion; hsa05110:Vibrio cholerae infection TTRLZHP RC R-HSA-382556:ABC-family proteins mediated transport TT42M75 ID TT42M75 TT42M75 TN Carbamoyl-phosphate synthetase I (CPS1) TT42M75 UP P31327 TT42M75 UC CPSM_HUMAN TT42M75 BC Carbon-nitrogen ligase TT42M75 SN Carbamoyl-phosphate synthase [ammonia], mitochondrial; CPSase I; CPS1 TT42M75 GN CPS1 TT42M75 FC Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell. TT42M75 EC EC 6.3.4.16 TT42M75 PD 5OJO; 5DOU; 5DOT; 4UUB; 4UUA TT42M75 SQ MTRILTAFKVVRTLKTGFGFTNVTAHQKWKFSRPGIRLLSVKAQTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTALDELGLSKYLESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDFVDPNKQNLIAEVSTKDVKVYGKGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILESDRKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDNTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGKATTITSVLPKPALVASRVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQADTVYFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIEGFTPRLPMNKEWPSNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAGVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEKHLPTLDHPIIPADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKAA TT42M75 TT Successful TT42M75 KE hsa00250:Alanine, aspartate and glutamate metabolism; hsa00330:Arginine and proline metabolism; hsa00910:Nitrogen metabolism; hsa01100:Metabolic pathways; hsa01200:Carbon metabolism; hsa01230:Biosynthesis of amino acids TTDL0NY ID TTDL0NY TTDL0NY TN Carnitine O-palmitoyltransferase I (CPT1B) TTDL0NY UP Q92523 TTDL0NY UC CPT1B_HUMAN TTDL0NY BC Acyltransferase TTDL0NY SN KIAA1670; Carnitine palmitoyltransferase I-like protein; Carnitine palmitoyltransferase I; Carnitine palmitoyltransferase 1B; Carnitine palmitoyl-transferase I; Carnitine o-palmitoyltransferase-1; Carnitine O-palmitoyltransferase I, muscle isoform; Carnitine O-palmitoyltransferase 1, muscle isoform; CPTI-M; CPTI-L; CPT1-M; CPT-1; CPT I; CPT TTDL0NY GN CPT1B TTDL0NY FC mitochondrial outer membrane, mitochondrion, carnitine O-palmitoyltransferase activity, carnitine metabolic process, carnitine shuttle, fatty acid beta-oxidation, long-chain fatty acid transport. TTDL0NY EC EC 2.3.1.21 TTDL0NY SQ MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPTSWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTGIFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPRVSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEEYIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALGIVPMCSYQMERMFNTTRIPGKDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDLEMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVALDEESYSYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPIIGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIESSYQVAKALADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREGRTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCLYLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGYGVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS TTDL0NY TT Successful TTDL0NY FM Acyltransferase TTDL0NY KE hsa00071:Fatty acid degradation; hsa01212:Fatty acid metabolism; hsa03320:PPAR signaling pathway; hsa04152:AMPK signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04922:Glucagon signaling pathway TTDL0NY RC R-HSA-1368082:RORA activates gene expression; R-HSA-1989781:PPARA activates gene expression; R-HSA-200425:Import of palmitoyl-CoA into the mitochondrial matrix TT7HQD0 ID TT7HQD0 TT7HQD0 TN C-C chemokine receptor type 4 (CCR4) TT7HQD0 UP P51679 TT7HQD0 UC CCR4_HUMAN TT7HQD0 BC GPCR rhodopsin TT7HQD0 SN K5-5; CMKBR4; CD194; CCR-4; CC-CKR-4; CC chemokine receptor 4; C-CCKR-4; C-C CKR-4 TT7HQD0 GN CCR4 TT7HQD0 FC The activity of this receptor is mediated by G(i) proteins which activate a phosphatidylinositol-calcium second messenger system. Can function as a chemoattractant homing receptor on circulating memory lymphocytes and as a coreceptor for some primary HIV-2 isolates. In the CNS, could mediate hippocampal-neuron survival. High affinity receptor for the C-C type chemokines CCL17/TARC, CCL22/MDC and CKLF isoform 1/CKLF1. TT7HQD0 SQ MNPTDIADTTLDESIYSNYYLYESIPKPCTKEGIKAFGELFLPPLYSLVFVFGLLGNSVVVLVLFKYKRLRSMTDVYLLNLAISDLLFVFSLPFWGYYAADQWVFGLGLCKMISWMYLVGFYSGIFFVMLMSIDRYLAIVHAVFSLRARTLTYGVITSLATWSVAVFASLPGFLFSTCYTERNHTYCKTKYSLNSTTWKVLSSLEINILGLVIPLGIMLFCYSMIIRTLQHCKNEKKNKAVKMIFAVVVLFLGFWTPYNIVLFLETLVELEVLQDCTFERYLDYAIQATETLAFVHCCLNPIIYFFLGEKFRKYILQLFKTCRGLFVLCQYCGLLQIYSADTPSSSYTQSTMDHDLHDAL TT7HQD0 TT Successful TT7HQD0 FM GPCR rhodopsin TT7HQD0 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa05203:Viral carcinogenesis TT7HQD0 RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTPHEX3 ID TTPHEX3 TTPHEX3 TN Ceramide glucosyltransferase (UGCG) TTPHEX3 UP Q16739 TTPHEX3 UC CEGT_HUMAN TTPHEX3 BC Hexosyltransferase TTPHEX3 SN UGCG; UDP-glucose:N-acylsphingosine D-glucosyltransferase; UDP-glucose ceramideglucosyltransferase; Glucosylceramide synthase; GLCT-1 TTPHEX3 GN UGCG TTPHEX3 FC Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide. May also serve as a "flippase". TTPHEX3 EC EC 2.4.1.80 TTPHEX3 SQ MALLDLALEGMAVFGFVLFLVLWLMHFMAIIYTRLHLNKKATDKQPYSKLPGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMPGYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEKVGLVHGLPYVADRQGFAATLEQVYFGTSHPRYYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRGWRFAMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVASLIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMTIYIFLSALWDPTISWRTGRYRLRCGGTAEEILDV TTPHEX3 TT Successful TTPHEX3 KE hsa00600:Sphingolipid metabolism; hsa01100:Metabolic pathways TTPHEX3 RC R-HSA-1660662:Glycosphingolipid metabolism TT1O264 ID TT1O264 TT1O264 TN Coagulation factor Va (F5) TT1O264 UP P12259 TT1O264 UC FA5_HUMAN TT1O264 SN Factor Va; F5 TT1O264 GN F5 TT1O264 FC Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin. TT1O264 PD 3S9C; 3P70; 3P6Z; 1Y61; 1FV4 TT1O264 SQ MFPGCPRLWVLVVLGTSWVGWGSQGTEAAQLRQFYVAAQGISWSYRPEPTNSSLNLSVTSFKKIVYREYEPYFKKEKPQSTISGLLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFNSGLIGPLLICKKGTLTEGGTQKTFDKQIVLLFAVFDESKSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDIKNCPKKTRNLKKITREQRRHMKRWEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIGKHYKKVMYTQYEDESFTKHTVNPNMKEDGILGPIIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDEVNSSFTSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYSDVDIMRDIASGLIGLLLICKSRSLDRRGIQRAADIEQQAVFAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFTGHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRDVKCIPDDDEDSYEIFEPPESTVMATRKMHDRLEPEDEESDADYDYQNRLAAALGIRSFRNSSLNQEEEEFNLTALALENGTEFVSSNTDIIVGSNYSSPSNISKFTVNNLAEPQKAPSHQQATTAGSPLRHLIGKNSVLNSSTAEHSSPYSEDPIEDPLQPDVTGIRLLSLGAGEFKSQEHAKHKGPKVERDQAAKHRFSWMKLLAHKVGRHLSQDTGSPSGMRPWEDLPSQDTGSPSRMRPWKDPPSDLLLLKQSNSSKILVGRWHLASEKGSYEIIQDTDEDTAVNNWLISPQNASRAWGESTPLANKPGKQSGHPKFPRVRHKSLQVRQDGGKSRLKKSQFLIKTRKKKKEKHTHHAPLSPRTFHPLRSEAYNTFSERRLKHSLVLHKSNETSLPTDLNQTLPSMDFGWIASLPDHNQNSSNDTGQASCPPGLYQTVPPEEHYQTFPIQDPDQMHSTSDPSHRSSSPELSEMLEYDRSHKSFPTDISQMSPSSEHEVWQTVISPDLSQVTLSPELSQTNLSPDLSHTTLSPELIQRNLSPALGQMPISPDLSHTTLSPDLSHTTLSLDLSQTNLSPELSQTNLSPALGQMPLSPDLSHTTLSLDFSQTNLSPELSHMTLSPELSQTNLSPALGQMPISPDLSHTTLSLDFSQTNLSPELSQTNLSPALGQMPLSPDPSHTTLSLDLSQTNLSPELSQTNLSPDLSEMPLFADLSQIPLTPDLDQMTLSPDLGETDLSPNFGQMSLSPDLSQVTLSPDISDTTLLPDLSQISPPPDLDQIFYPSESSQSLLLQEFNESFPYPDLGQMPSPSSPTLNDTFLSKEFNPLVIVGLSKDGTDYIEIIPKEEVQSSEDDYAEIDYVPYDDPYKTDVRTNINSSRDPDNIAAWYLRSNNGNRRNYYIAAEEISWDYSEFVQRETDIEDSDDIPEDTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILGPIIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSAVNPEKDIHSGLIGPLLICQKGILHKDSNMPMDMREFVLLFMTFDEKKSWYYEKKSRSSWRLTSSEMKKSHEFHAINGMIYSLPGLKMYEQEWVRLHLLNIGGSQDIHVVHFHGQTLLENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLIMDRDCRMPMGLSTGIISDSQIKASEFLGYWEPRLARLNNGGSYNAWSVEKLAAEFASKPWIQVDMQKEVIITGIQTQGAKHYLKSCYTTEFYVAYSSNQINWQIFKGNSTRNVMYFNGNSDASTIKENQFDPPIVARYIRISPTRAYNRPTLRLELQGCEVNGCSTPLGMENGKIENKQITASSFKKSWWGDYWEPFRARLNAQGRVNAWQAKANNNKQWLEIDLLKIKKITAIITQGCKSLSSEMYVKSYTIHYSEQGVEWKPYRLKSSMVDKIFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWNQSIALRLELFGCDIY TT1O264 TT Successful TT1O264 KE hsa04610:Complement and coagulation cascades TT1O264 RC R-HSA-114608:Platelet degranulation; R-HSA-140875:Common Pathway of Fibrin Clot Formation; R-HSA-204005:COPII (Coat Protein 2) Mediated Vesicle Transport; R-HSA-5694530:Cargo concentration in the ER TT1290U ID TT1290U TT1290U TN Coagulation factor VIII (F8) TT1290U UP P00451 TT1290U UC FA8_HUMAN TT1290U SN Procoagulant component; F8C; Antihemophilic factor; AHF TT1290U GN F8 TT1290U FC Factor VIII, along with calcium and phospholipid, acts as a cofactor for F9/factor IXa when it converts F10/factor X to the activated form, factor Xa. TT1290U PD 5K8D; 4XZU; 4PT6; 4KI5; 4BDV TT1290U SQ MQIELSTCFFLCLLRFCFSATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHVDLVKDLNSGLIGALLVCREGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRFDDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNMERDLASGLIGPLLICYKESVDQRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDFLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYEDSYEDISAYLLSKNNAIEPRSFSQNSRHPSTRQKQFNATTIPENDIEKTDPWFAHRTPMPKIQNVSSSDLLMLLRQSPTPHGLSLSDLQEAKYETFSDDPSPGAIDSNNSLSEMTHFRPQLHHSGDMVFTPESGLQLRLNEKLGTTAATELKKLDFKVSSTSNNLISTIPSDNLAAGTDNTSSLGPPSMPVHYDSQLDTTLFGKKSSPLTESGGPLSLSEENNDSKLLESGLMNSQESSWGKNVSSTESGRLFKGKRAHGPALLTKDNALFKVSISLLKTNKTSNNSATNRKTHIDGPSLLIENSPSVWQNILESDTEFKKVTPLIHDRMLMDKNATALRLNHMSNKTTSSKNMEMVQQKKEGPIPPDAQNPDMSFFKMLFLPESARWIQRTHGKNSLNSGQGPSPKQLVSLGPEKSVEGQNFLSEKNKVVVGKGEFTKDVGLKEMVFPSSRNLFLTNLDNLHENNTHNQEKKIQEEIEKKETLIQENVVLPQIHTVTGTKNFMKNLFLLSTRQNVEGSYDGAYAPVLQDFRSLNDSTNRTKKHTAHFSKKGEEENLEGLGNQTKQIVEKYACTTRISPNTSQQNFVTQRSKRALKQFRLPLEETELEKRIIVDDTSTQWSKNMKHLTPSTLTQIDYNEKEKGAITQSPLSDCLTRSHSIPQANRSPLPIAKVSSFPSIRPIYLTRVLFQDNSSHLPAASYRKKDSGVQESSHFLQGAKKNNLSLAILTLEMTGDQREVGSLGTSATNSVTYKKVENTVLPKPDLPKTSGKVELLPKVHIYQKDLFPTETSNGSPGHLDLVEGSLLQGTEGAIKWNEANRPGKVPFLRVATESSAKTPSKLLDPLAWDNHYGTQIPKEEWKSQEKSPEKTAFKKKDTILSLNACESNHAIAAINEGQNKPEIEVTWAKQGRTERLCSQNPPVLKRHQREITRTTLQSDQEEIDYDDTISVEMKKEDFDIYDEDENQSPRSFQKKTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLY TT1290U TT Successful TT1290U FM Multicopper oxidase TT1290U KE hsa04610:Complement and coagulation cascades TT1290U RC R-HSA-114608:Platelet degranulation; R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-140875:Common Pathway of Fibrin Clot Formation; R-HSA-204005:COPII (Coat Protein 2) Mediated Vesicle Transport; R-HSA-5694530:Cargo concentration in the ER TTJL8VG ID TTJL8VG TTJL8VG TN Corticosteroid-binding globulin (SERPINA6) TTJL8VG UP P08185 TTJL8VG UC CBG_HUMAN TTJL8VG BC Serpin protein TTJL8VG SN Transcortin; SERPINA6; CBG TTJL8VG GN SERPINA6 TTJL8VG FC Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species. TTJL8VG PD 4C49; 4C41; 4BB2; 2VDY; 2VDX TTJL8VG SQ MPLLLYTCLLWLPTSGLWTVQAMDPNAAYVNMSNHHRGLASANVDFAFSLYKHLVALSPKKNIFISPVSISMALAMLSLGTCGHTRAQLLQGLGFNLTERSETEIHQGFQHLHQLFAKSDTSLEMTMGNALFLDGSLELLESFSADIKHYYESEVLAMNFQDWATASRQINSYVKNKTQGKIVDLFSGLDSPAILVLVNYIFFKGTWTQPFDLASTREENFYVDETTVVKVPMMLQSSTISYLHDSELPCQLVQMNYVGNGTVFFILPDKGKMNTVIAALSRDTINRWSAGLTSSQVDLYIPKVTISGVYDLGDVLEEMGIADLFTNQANFSRITQDAQLKSSKVVHKAVLQLNEEGVDTAGSTGVTLNLTSKPIILRFNQPFIIMIFDHFTWSSLFLARVMNPV TTJL8VG TT Successful TTAQ6ZW ID TTAQ6ZW TTAQ6ZW TN Cytochrome P450 2A6 (CYP2A6) TTAQ6ZW UP P11509 TTAQ6ZW UC CP2A6_HUMAN TTAQ6ZW BC Paired donor oxygen oxidoreductase TTAQ6ZW SN Cytochrome P450(I); Cytochrome P450 IIA3; Coumarin 7-hydroxylase; CYPIIA6; CYP2A6; CYP2A3 TTAQ6ZW GN CYP2A6 TTAQ6ZW FC Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Possesses low phenacetin O-deethylation activity. TTAQ6ZW EC EC 1.14.13.- TTAQ6ZW PD 4RUI; 4EJJ; 3T3R; 3T3Q; 3EBS TTAQ6ZW SQ MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMKISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSNGERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSNVISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQLLQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFIGGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQRFGDVIPMSLARRVKKDTKFRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEKGQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGFATIPRNYTMSFLPR TTAQ6ZW TT Successful TTR7UJ3 ID TTR7UJ3 TTR7UJ3 TN Cytoplasmic thioredoxin reductase (TXNRD1) TTR7UJ3 UP Q16881 TTR7UJ3 UC TRXR1_HUMAN TTR7UJ3 BC Sulfur donor oxidoreductase TTR7UJ3 SN Thioredoxin reductase TR1; Thioredoxin reductase 1, cytoplasmic; KM-102-derived reductase-like factor; KDRF; Gene associated with retinoic and interferon-induced mortality 12 protein; Gene associated with retinoic and IFN-induced mortality 12 protein; GRIM12; GRIM-12 TTR7UJ3 GN TXNRD1 TTR7UJ3 FC Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid. TTR7UJ3 EC EC 1.8.1.9 TTR7UJ3 PD 3QFB; 3QFA; 2ZZC; 2ZZB; 2ZZ0 TTR7UJ3 SQ MGCAEGKAVAAAAPTELQTKGKNGDGRRRSAKDHHPGKTLPENPAGFTSTATADSRALLQAYIDGHSVVIFSRSTCTRCTEVKKLFKSLCVPYFVLELDQTEDGRALEGTLSELAAETDLPVVFVKQRKIGGHGPTLKAYQEGRLQKLLKMNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSGASILQAGCUG TTR7UJ3 TT Successful TTJHKYD ID TTJHKYD TTJHKYD TN Delta-aminolevulinic acid dehydratase (ALAD) TTJHKYD UP P13716 TTJHKYD UC HEM2_HUMAN TTJHKYD BC Alpha-carbonic anhydrase TTJHKYD SN Porphobilinogen synthase; Delta-aminolevulinate dehydratase; ALADH; ALAD TTJHKYD GN ALAD TTJHKYD FC Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. TTJHKYD EC EC 4.2.1.24 TTJHKYD PD 5HNR; 5HMS; 1PV8; 1.00E+51 TTJHKYD SQ MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE TTJHKYD TT Successful TTJHKYD KE hsa00860:Porphyrin and chlorophyll metabolism; hsa01100:Metabolic pathways TTF8P9I ID TTF8P9I TTF8P9I TN Diacylglycerol acyltransferase 1 (DGAT1) TTF8P9I UP O75907 TTF8P9I UC DGAT1_HUMAN TTF8P9I BC Acyltransferase TTF8P9I SN Retinol O-fatty-acyltransferase; Diglyceride acyltransferase; Diacylglycerol O-acyltransferase 1; DGAT; Acyl-CoA retinol O-fatty-acyltransferase; ARAT; AGRP1; ACAT-related gene product 1 TTF8P9I GN DGAT1 TTF8P9I FC Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders. TTF8P9I EC EC 2.3.1.20 TTF8P9I SQ MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVGSGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPAAVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHTVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWMVPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREFYRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVSVPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLNYEAPAAEA TTF8P9I TT Successful TTF8P9I FM Acyltransferase TTF8P9I KE hsa00561:Glycerolipid metabolism; hsa00830:Retinol metabolism; hsa01100:Metabolic pathways; hsa04975:Fat digestion and absorption TTF8P9I RC R-HSA-1482883:Acyl chain remodeling of DAG and TAG; R-HSA-75109:Triglyceride Biosynthesis TTLVP78 ID TTLVP78 TTLVP78 TN Dihydroorotate dehydrogenase (DHODH) TTLVP78 UP Q02127 TTLVP78 UC PYRD_HUMAN TTLVP78 BC CH-CH donor oxidoreductase TTLVP78 SN Dihydroorotate oxidase; Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOdehase; DHODH TTLVP78 GN DHODH TTLVP78 FC Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. TTLVP78 EC EC 1.3.5.2 TTLVP78 PD 6FMD; 6ET4; 6CJG; 6CJF; 5ZFB TTLVP78 SQ MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR TTLVP78 TT Successful TTLVP78 KE hsa00240:Pyrimidine metabolism; hsa01100:Metabolic pathways TTLVP78 RC R-HSA-500753:Pyrimidine biosynthesis TTS2PH3 ID TTS2PH3 TTS2PH3 TN Dopamine D5 receptor (D5R) TTS2PH3 UP P21918 TTS2PH3 UC DRD5_HUMAN TTS2PH3 BC GPCR rhodopsin TTS2PH3 SN Dopamine receptor 5; DRD5; D1beta dopamine receptor; D(5)D(1B) dopamine receptor dopamine receptor; D(5) dopamine receptor TTS2PH3 GN DRD5 TTS2PH3 FC Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase. TTS2PH3 SQ MLPPGSNGTAYPGQFALYQQLAQGNAVGGSAGAPPLGPSQVVTACLLTLLIIWTLLGNVLVCAAIVRSRHLRANMTNVFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFGAFCDVWVAFDIMCSTASILNLCVISVDRYWAISRPFRYKRKMTQRMALVMVGLAWTLSILISFIPVQLNWHRDQAASWGGLDLPNNLANWTPWEEDFWEPDVNAENCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIAQVQIRRISSLERAAEHAQSCRSSAACAPDTSLRASIKKETKVLKTLSVIMGVFVCCWLPFFILNCMVPFCSGHPEGPPAGFPCVSETTFDVFVWFGWANSSLNPVIYAFNADFQKVFAQLLGCSHFCSRTPVETVNISNELISYNQDIVFHKEIAAAYIHMMPNAVTPGNREVDNDEEEGPFDRMFQIYQTSPDGDPVAESVWELDCEGEISLDKITPFTPNGFH TTS2PH3 TT Successful TTS2PH3 KE hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04728:Dopaminergic synapse TTS2PH3 RC R-HSA-390651:Dopamine receptors; R-HSA-418555:G alpha (s) signalling events TTVBI8W ID TTVBI8W TTVBI8W TN Dopamine transporter (DAT) TTVBI8W UP Q01959 TTVBI8W UC SC6A3_HUMAN TTVBI8W BC Neurotransmitter:sodium symporter TTVBI8W SN Solute carrier family 6 member 3; Sodium-dependent dopamine transporter; DAT1; DAT; DA transporter TTVBI8W GN SLC6A3 TTVBI8W FC Amine transporter. Terminates the action of dopamine by its high affinity sodium-dependent reuptake into presynaptic terminals. TTVBI8W SQ MSKSKCSVGLMSSVVAPAKEPNAVGPKEVELILVKEQNGVQLTSSTLTNPRQSPVEAQDRETWGKKIDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLLFMVIAGMPLFYMELALGQFNREGAAGVWKICPILKGVGFTVILISLYVGFFYNVIIAWALHYLFSSFTTELPWIHCNNSWNSPNCSDAHPGDSSGDSSGLNDTFGTTPAAEYFERGVLHLHQSHGIDDLGPPRWQLTACLVLVIVLLYFSLWKGVKTSGKVVWITATMPYVVLTALLLRGVTLPGAIDGIRAYLSVDFYRLCEASVWIDAATQVCFSLGVGFGVLIAFSSYNKFTNNCYRDAIVTTSINSLTSFSSGFVVFSFLGYMAQKHSVPIGDVAKDGPGLIFIIYPEAIATLPLSSAWAVVFFIMLLTLGIDSAMGGMESVITGLIDEFQLLHRHRELFTLFIVLATFLLSLFCVTNGGIYVFTLLDHFAAGTSILFGVLIEAIGVAWFYGVGQFSDDIQQMTGQRPSLYWRLCWKLVSPCFLLFVVVVSIVTFRPPHYGAYIFPDWANALGWVIATSSMAMVPIYAAYKFCSLPGSFREKLAYAIAPEKDRELVDRGEVRQFTLRHWLKV TTVBI8W TT Successful TTVBI8W FM Neurotransmitter sodium symporter TTVBI8W KE hsa04728:Dopaminergic synapse; hsa05012:Parkinson's disease; hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05034:Alcoholism TTVBI8W RC R-HSA-442660:Na+/Cl- dependent neurotransmitter transporters TT05DLS ID TT05DLS TT05DLS TN E3 ubiquitin-protein ligase COP1 (RFWD2) TT05DLS UP Q8NHY2 TT05DLS UC COP1_HUMAN TT05DLS BC Acyltransferase TT05DLS SN hCOP1; RNF200; RING-type E3 ubiquitin transferase RFWD2; RING finger protein 200; RING finger and WD repeat domain protein 2; E3 ubiquitinprotein ligase RFWD2; Constitutive photomorphogenesis protein 1 homolog; COP1 TT05DLS GN RFWD2 TT05DLS FC E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif. E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. TT05DLS EC EC 2.3.2.27 TT05DLS PD 5IGQ; 5HQG TT05DLS SQ MSGSRQAGSGSAGTSPGSSAASSVTSASSSLSSSPSPPSVAVSAAALVSGGVAQAAGSGGLGGPVRPVLVAPAVSGSGGGAVSTGLSRHSCAARPSAGVGGSSSSLGSGSRKRPLLAPLCNGLINSYEDKSNDFVCPICFDMIEEAYMTKCGHSFCYKCIHQSLEDNNRCPKCNYVVDNIDHLYPNFLVNELILKQKQRFEEKRFKLDHSVSSTNGHRWQIFQDWLGTDQDNLDLANVNLMLELLVQKKKQLEAESHAAQLQILMEFLKVARRNKREQLEQIQKELSVLEEDIKRVEEMSGLYSPVSEDSTVPQFEAPSPSHSSIIDSTEYSQPPGFSGSSQTKKQPWYNSTLASRRKRLTAHFEDLEQCYFSTRMSRISDDSRTASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNGSSIVSSIEFDRDCDYFAIAGVTKKIKVYEYDTVIQDAVDIHYPENEMTCNSKISCISWSSYHKNLLASSDYEGTVILWDGFTGQRSKVYQEHEKRCWSVDFNLMDPKLLASGSDDAKVKLWSTNLDNSVASIEAKANVCCVKFSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVFKGHRKAVSYAKFVSGEEIVSASTDSQLKLWNVGKPYCLRSFKGHINEKNFVGLASNGDYIACGSENNSLYLYYKGLSKTLLTFKFDTVKSVLDKDRKEDDTNEFVSAVCWRALPDGESNVLIAANSQGTIKVLELV TT05DLS TT Successful TT05DLS FM Carbon-nitrogen ligase TT05DLS KE hsa04115:p53 signaling pathway; hsa04120:Ubiquitin mediated proteolysis TTKRD0G ID TTKRD0G TTKRD0G TN Endothelin A receptor (EDNRA) TTKRD0G UP P25101 TTKRD0G UC EDNRA_HUMAN TTKRD0G BC GPCR rhodopsin TTKRD0G SN HET-AR; Endothelin-1 receptor; Endothelin receptor type A; Endothelin receptor A; ETRA; ETA-R; ETA receptor; ETA; ET-A TTKRD0G GN EDNRA TTKRD0G FC Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3. Receptor for endothelin-1. TTKRD0G SQ METLCLRASFWLALVGCVISDNPERYSTNLSNHVDDFTTFRGTELSFLVTTHQPTNLVLPSNGSMHNYCPQQTKITSAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFDHNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLVTAIEIVSIWILSFILAIPEAIGFVMVPFEYRGEQHKTCMLNATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWFPLHLSRILKKTVYNEMDKNRCELLSFLLLMDYIGINLATMNSCINPIALYFVSKKFKNCFQSCLCCCCYQSKSLMTSVPMNGTSIQWKNHDQNNHNTDRSSHKDSMN TTKRD0G TT Successful TTKRD0G FM GPCR rhodopsin TTKRD0G KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction; hsa04924:Renin secretion; hsa05200:Pathways in cancer TTKRD0G RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TT3ZTGU ID TT3ZTGU TT3ZTGU TN Endothelin B receptor (EDNRB) TT3ZTGU UP P24530 TT3ZTGU UC EDNRB_HUMAN TT3ZTGU BC GPCR rhodopsin TT3ZTGU SN Endothelin receptor type B; Endothelin receptor Non-selective type; Endothelin receptor B; ETRB; ET-BR; ET-B TT3ZTGU GN EDNRB TT3ZTGU FC Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Non-specific receptor for endothelin 1, 2, and 3. TT3ZTGU PD 6IGL; 6IGK; 5XPR; 5X93; 5GLI TT3ZTGU SQ MQPPPSLCGRALVALVLACGLSRIWGEERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYNQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS TT3ZTGU TT Successful TT3ZTGU KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04916:Melanogenesis; hsa05200:Pathways in cancer TT3ZTGU RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TT1QFLA ID TT1QFLA TT1QFLA TN Eukaryotic elongation factor 2 kinase (eEF-2K) TT1QFLA UP O00418 TT1QFLA UC EF2K_HUMAN TT1QFLA BC Kinase TT1QFLA SN eEF-2K; eEF-2 kinase; Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase TT1QFLA GN EEF2K TT1QFLA FC Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. TT1QFLA EC EC 2.7.11.20 TT1QFLA PD 5KS5; 5J8H TT1QFLA SQ MADEDLIFRLEGVDGGQSPRAGHDGDSDGDSDDEEGYFICPITDDPSSNQNVNSKVNKYYSNLTKSERYSSSGSPANSFHFKEAWKHAIQKAKHMPDPWAEFHLEDIATERATRHRYNAVTGEWLDDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRDVYFEDVRLQMEAKLWGEEYNRHKPPKQVDIMQMCIIELKDRPGKPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTETGTDFGDGNLGVRGMALFFYSHACNRICESMGLAPFDLSPRERDAVNQNTKLLQSAKTILRGTEEKCGSPQVRTLSGSRPPLLRPLSENSGDENMSDVTFDSLPSSPSSATPHSQKLDHLHWPVFSDLDNMASRDHDHLDNHRESENSGDSGYPSEKRGELDDPEPREHGHSYSNRKYESDEDSLGSSGRVCVEKWNLLNSSRLHLPRASAVALEVQRLNALDLEKKIGKSILGKVHLAMVRYHEGGRFCEKGEEWDQESAVFHLEHAANLGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRQSMILVARAFDSGQNLSPDRCQDWLEALHWYNTALEMTDCDEGGEYDGMQDEPRYMMLAREAEMLFTGGYGLEKDPQRSGDLYTQAAEAAMEAMKGRLANQYYQKAEEAWAQMEE TT1QFLA TT Successful TT1QFLA KE hsa04152:AMPK signaling pathway; hsa04921:Oxytocin signaling pathway TTQ6VF4 ID TTQ6VF4 TTQ6VF4 TN Ferrochelatase (FECH) TTQ6VF4 UP P22830 TTQ6VF4 UC HEMH_HUMAN TTQ6VF4 BC Ferrochelatase TTQ6VF4 SN Protoheme ferro-lyase; Heme synthetase; FECH TTQ6VF4 GN FECH TTQ6VF4 FC Catalyzes the ferrous insertion into protoporphyrin IX. TTQ6VF4 EC EC 4.99.1.1 TTQ6VF4 PD 4MK4; 4KMM; 4KLR; 4KLC; 4KLA TTQ6VF4 SQ MRSLGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQVQPQKRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADHILKELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTSQQL TTQ6VF4 TT Successful TTQ6VF4 KE hsa00860:Porphyrin and chlorophyll metabolism; hsa01100:Metabolic pathways TTGKIED ID TTGKIED TTGKIED TN Fibroblast growth factor-2 (FGF2) TTGKIED UP P09038 TTGKIED UC FGF2_HUMAN TTGKIED BC Growth factor TTGKIED SN bFGF; Heparin-binding growth factor 2; HBGF-2; Fibroblast growth factor 2; FGFB; FGF-2; Basic fibroblast growth factor TTGKIED GN FGF2 TTGKIED FC Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4. Also acts as an integrin ligand which is required for FGF2 signaling. Binds to integrin ITGAV:ITGB3. Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Can induce angiogenesis. TTGKIED PD 5X1O; 4OEG; 4OEF; 4OEE; 4FGF TTGKIED SQ MVGVGGGDVEDVTPRPGGCQISGRGARGCNGIPGAAAWEAALPRRRPRRHPSVNPRSRAAGSPRTRGRRTEERPSGSRLGDRGRGRALPGGRLGGRGRGRAPERVGGRGRGRGTAAPRAAPAARGSRPGPAGTMAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS TTGKIED TT Successful TTGKIED FM Growth factor TTGKIED KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05218:Melanoma TTGKIED RC R-HSA-109704:PI3K Cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-190322:FGFR4 ligand binding and activation; R-HSA-190372:FGFR3c ligand binding and activation; R-HSA-190375:FGFR2c ligand binding and activation; R-HSA-190377:FGFR2b ligand binding and activation; R-HSA-2033514:FGFR3 mutant receptor activation; R-HSA-2033519:Activated point mutants of FGFR2; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-2892247:POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation; R-HSA-3000170:Syndecan interactions; R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-5654219:Phospholipase C-mediated cascade: FGFR1; R-HSA-5654221:Phospholipase C-mediated cascade; R-HSA-5654227:Phospholipase C-mediated cascade; R-HSA-5654228:Phospholipase C-mediated cascade; R-HSA-5654688:SHC-mediated cascade:FGFR1; R-HSA-5654689:PI-3K cascade:FGFR1; R-HSA-5654693:FRS-mediated FGFR1 signaling; R-HSA-5654695:PI-3K cascade:FGFR2; R-HSA-5654699:SHC-mediated cascade:FGFR2; R-HSA-5654700:FRS-mediated FGFR2 signaling; R-HSA-5654704:SHC-mediated cascade:FGFR3; R-HSA-5654706:FRS-mediated FGFR3 signaling; R-HSA-5654710:PI-3K cascade:FGFR3; R-HSA-5654712:FRS-mediated FGFR4 signaling; R-HSA-5654719:SHC-mediated cascade:FGFR4; R-HSA-5654720:PI-3K cascade:FGFR4; R-HSA-5654726:Negative regulation of FGFR1 signaling; R-HSA-5654727:Negative regulation of FGFR2 signaling; R-HSA-5654732:Negative regulation of FGFR3 signaling; R-HSA-5654733:Negative regulation of FGFR4 signaling; R-HSA-5673001:RAF/MAP kinase cascade TTCEKVZ ID TTCEKVZ TTCEKVZ TN Fibroblast growth factor-4 (FGF4) TTCEKVZ UP P08620 TTCEKVZ UC FGF4_HUMAN TTCEKVZ BC Heparin-binding growth factors family TTCEKVZ SN Transforming protein KS3; Heparinbinding growth factor 4; Heparin secretorytransforming protein 1; HST1; HST; HBGF4; Fibroblast growth factor 4; FGF4 TTCEKVZ GN FGF4 TTCEKVZ FC Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal limb and cardiac valve development during embryogenesis. TTCEKVZ PD 1IJT TTCEKVZ SQ MSGPGTAAVALLPAVLLALLAPWAGRGGAAAPTAPNGTLEAELERRWESLVALSLARLPVAAQPKEAAVQSGAGDYLLGIKRLRRLYCNVGIGFHLQALPDGRIGGAHADTRDSLLELSPVERGVVSIFGVASRFFVAMSSKGKLYGSPFFTDECTFKEILLPNNYNAYESYKYPGMFIALSKNGKTKKGNRVSPTMKVTHFLPRL TTCEKVZ TT Successful TTCEKVZ KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer; hsa05218:Melanoma TTCEKVZ RC R-HSA-109704:PI3K Cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-190322:FGFR4 ligand binding and activation; R-HSA-190372:FGFR3c ligand binding and activation; R-HSA-190375:FGFR2c ligand binding and activation; R-HSA-2033514:FGFR3 mutant receptor activation; R-HSA-2033519:Activated point mutants of FGFR2; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5654219:Phospholipase C-mediated cascade: FGFR1; R-HSA-5654221:Phospholipase C-mediated cascade; R-HSA-5654227:Phospholipase C-mediated cascade; R-HSA-5654228:Phospholipase C-mediated cascade; R-HSA-5654688:SHC-mediated cascade:FGFR1; R-HSA-5654689:PI-3K cascade:FGFR1; R-HSA-5654693:FRS-mediated FGFR1 signaling; R-HSA-5654695:PI-3K cascade:FGFR2; R-HSA-5654699:SHC-mediated cascade:FGFR2; R-HSA-5654700:FRS-mediated FGFR2 signaling; R-HSA-5654704:SHC-mediated cascade:FGFR3; R-HSA-5654706:FRS-mediated FGFR3 signaling; R-HSA-5654710:PI-3K cascade:FGFR3; R-HSA-5654712:FRS-mediated FGFR4 signaling; R-HSA-5654719:SHC-mediated cascade:FGFR4; R-HSA-5654720:PI-3K cascade:FGFR4; R-HSA-5654726:Negative regulation of FGFR1 signaling; R-HSA-5654727:Negative regulation of FGFR2 signaling; R-HSA-5654732:Negative regulation of FGFR3 signaling; R-HSA-5654733:Negative regulation of FGFR4 signaling; R-HSA-5673001:RAF/MAP kinase cascade TTVC37M ID TTVC37M TTVC37M TN Folate receptor alpha (FOLR1) TTVC37M UP P15328 TTVC37M UC FOLR1_HUMAN TTVC37M BC Folate receptor TTVC37M SN Ovarian tumorassociated antigen MOv18; KB cells FBP; Folate receptor, adult; Folate receptor 1; FRalpha; FOLR1; Adult folatebinding protein TTVC37M GN FOLR1 TTVC37M FC Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pHafter receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release. Required for normal embryonic development and normal cell proliferation. TTVC37M PD 5IZQ; 4LRH; 4KMX; 4KM7; 4KM6 TTVC37M SQ MAQRMTTQLLLLLVWVAVVGEAQTRIAWARTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLYECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTVLCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMSGAGPWAAWPFLLSLALMLLWLLS TTVC37M TT Successful TTVC37M KE hsa04144:Endocytosis TTVC37M RC R-HSA-204005:COPII (Coat Protein 2) Mediated Vesicle Transport; R-HSA-5694530:Cargo concentration in the ER TTPRKM0 ID TTPRKM0 TTPRKM0 TN GABA transporter GAT-1 (SLC6A1) TTPRKM0 UP P30531 TTPRKM0 UC SC6A1_HUMAN TTPRKM0 BC Neurotransmitter:sodium symporter TTPRKM0 SN Solute carrier family 6 member 1; Sodium- and chloride-dependent GABA transporter 1; GAT1; GAT-1; GABT1; GABATR; GABA transporter 1 TTPRKM0 GN SLC6A1 TTPRKM0 FC Terminates the action of GABA by its high affinity sodium-dependent reuptake into presynaptic terminals. TTPRKM0 SQ MATNGSKVADGQISTEVSEAPVANDKPKTLVVKVQKKAADLPDRDTWKGRFDFLMSCVGYAIGLGNVWRFPYLCGKNGGGAFLIPYFLTLIFAGVPLFLLECSLGQYTSIGGLGVWKLAPMFKGVGLAAAVLSFWLNIYYIVIISWAIYYLYNSFTTTLPWKQCDNPWNTDRCFSNYSMVNTTNMTSAVVEFWERNMHQMTDGLDKPGQIRWPLAITLAIAWILVYFCIWKGVGWTGKVVYFSATYPYIMLIILFFRGVTLPGAKEGILFYITPNFRKLSDSEVWLDAATQIFFSYGLGLGSLIALGSYNSFHNNVYRDSIIVCCINSCTSMFAGFVIFSIVGFMAHVTKRSIADVAASGPGLAFLAYPEAVTQLPISPLWAILFFSMLLMLGIDSQFCTVEGFITALVDEYPRLLRNRRELFIAAVCIISYLIGLSNITQGGIYVFKLFDYYSASGMSLLFLVFFECVSISWFYGVNRFYDNIQEMVGSRPCIWWKLCWSFFTPIIVAGVFIFSAVQMTPLTMGNYVFPKWGQGVGWLMALSSMVLIPGYMAYMFLTLKGSLKQRIQVMVQPSEDIVRPENGPEQPQAGSSTSKEAYI TTPRKM0 TT Successful TTPRKM0 FM Neurotransmitter sodium symporter TTPRKM0 KE hsa04727:GABAergic synapse TTPRKM0 RC R-HSA-442660:Na+/Cl- dependent neurotransmitter transporters TTDCVZW ID TTDCVZW TTDCVZW TN Gamma-aminobutyric acid B receptor (GABBR) TTDCVZW UP Q9UBS5; O75899 TTDCVZW UC GABR1_HUMAN; GABR2_HUMAN TTDCVZW BC GPCR glutamate TTDCVZW SN Gamma-aminobutyric acid type B receptor; GPRC3; GABABR; GABA-BR; GABA-B-R; GABA-B receptor TTDCVZW GN GABBR1; GABBR2 TTDCVZW FC Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception. Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. TTDCVZW SQ MLLLLLLAPLFLRPPGAGGAQTPNATSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKIYDPSINCTVDEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRNQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDVLTLAIWQIVDPLHRTIETFAKEEPKEDIDVSILPQLEHCSSRKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQLRSRRHPPTPPEPSGGLPRGPPEPPDRLSCDGSRVHLLYK TTDCVZW TT Successful TTDCVZW FM GPCR glutamate TTDCVZW KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04727:GABAergic synapse; hsa04915:Estrogen signaling pathway; hsa05032:Morphine addiction TTDCVZW RC R-HSA-1296041:Activation of G protein gated Potassium channels; R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors); R-HSA-997272:Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits TTIKWV4 ID TTIKWV4 TTIKWV4 TN Geranyltranstransferase (FDPS) TTIKWV4 UP P14324 TTIKWV4 UC FPPS_HUMAN TTIKWV4 BC Alkyl aryl transferase TTIKWV4 SN KIAA1293; Geranylgeranyl pyrophosphate synthase; Geranylgeranyl diphosphate synthase; GGPS1; GGPPSase; GGPP synthase; Farnesyltranstransferase; Farnesyl pyrophosphate synthase; Farnesyl diphosphate synthase; FPS protein; FPP synthase; Dimethylallyltranstransferase; (2E,6E)-farnesyl diphosphate synthase TTIKWV4 GN FDPS TTIKWV4 FC FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. TTIKWV4 EC EC 2.5.1.10 TTIKWV4 PD 5YGI; 5KSX; 5JV2; 5JV1; 5JV0 TTIKWV4 SQ MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAWHSARCWCQAWTEEPRALCSSLRMNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK TTIKWV4 TT Successful TTIKWV4 KE hsa00900:Terpenoid backbone biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics TTIKWV4 RC R-HSA-191273:Cholesterol biosynthesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP) TTVPQTF ID TTVPQTF TTVPQTF TN Glutamate receptor AMPA 1 (GRIA1) TTVPQTF UP P42261 TTVPQTF UC GRIA1_HUMAN TTVPQTF BC Glutamate-gated ion channel TTVPQTF SN Glutamate receptor ionotropic, AMPA 1; Glutamate receptor 1; GluR-K1; GluR-A; GluR-1; GluA1; GLUR1; GLUH1; AMPA-selective glutamate receptor 1 TTVPQTF GN GRIA1 TTVPQTF FC L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. Ionotropic glutamate receptor. TTVPQTF SQ MQHIFAFFCTGFLGAVVGANFPNNIQIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVDTSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPAKIMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAATDAQAGGDNSSVQNRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSRSESKRMKGFCLIPQQSINEAIRTSTLPRNSGAGASSGGSGENGRVVSHDFPKSMQSIPCMSHSSGMPLGATGL TTVPQTF TT Successful TTVPQTF FM Glutamate gated ion channel TTVPQTF KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04728:Dopaminergic synapse; hsa04730:Long-term depression; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05031:Amphetamine addiction; hsa05033:Nicotine addiction TTVPQTF RC R-HSA-204005:COPII (Coat Protein 2) Mediated Vesicle Transport; R-HSA-399719:Trafficking of AMPA receptors; R-HSA-416993:Trafficking of GluR2-containing AMPA receptors; R-HSA-438066:Unblocking of NMDA receptor, glutamate binding and activation; R-HSA-5694530:Cargo concentration in the ER TT9HLZ0 ID TT9HLZ0 TT9HLZ0 TN Glutamate receptor AMPA 2 (GRIA2) TT9HLZ0 UP P42262 TT9HLZ0 UC GRIA2_HUMAN TT9HLZ0 BC Glutamate-gated ion channel TT9HLZ0 SN Glutamate receptor ionotropic, AMPA 2; Glutamate receptor 2; GluRK2; GluRB; GluR2; GluR-K2; GluR-B; GluR-2; GluA2; AMPAselective glutamate receptor 2; AMPA-selective glutamate receptor 2 TT9HLZ0 GN GRIA2 TT9HLZ0 FC L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting. Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. TT9HLZ0 PD 5ZG3; 5ZG2; 5ZG1; 5ZG0; 5YBG TT9HLZ0 SQ MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDEMYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI TT9HLZ0 TT Successful TT9HLZ0 FM Glutamate-gated ion channel family TTZ8EM9 ID TTZ8EM9 TTZ8EM9 TN Glycine receptor (GlyR) TTZ8EM9 UP P23415; P23416; O75311; Q5JXX5; P48167 TTZ8EM9 UC GLRA1_HUMAN; GLRA2_HUMAN; GLRA3_HUMAN; GLRA4_HUMAN; GLRB_HUMAN TTZ8EM9 BC Neurotransmitter receptor TTZ8EM9 SN Glycine receptor TTZ8EM9 GN GLRA1; GLRA2; GLRA3; GLRA4; GLRB TTZ8EM9 FC The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing). TTZ8EM9 SQ MYSFNTLRLYLWETIVFFSLAASKEAEAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDSIWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLFQEDEAGEGRFNFSAYGMGPACLQAKDGISVKGANNSNTTNPPPAPSKSPEEMRKLFIQRAKKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNQ TTZ8EM9 TT Successful TTZ8EM9 KE hsa04080:Neuroactive ligand-receptor interaction TTZ8EM9 RC R-HSA-975298:Ligand-gated ion channel transport TT6MP2Z ID TT6MP2Z TT6MP2Z TN GMCSFR-alpha (CSF2RA) TT6MP2Z UP P15509 TT6MP2Z UC CSF2R_HUMAN TT6MP2Z BC Type I cytokine receptor family TT6MP2Z SN GMR; GM-CSFR; GM-CSF-R-alpha; CSF2RA; CDw116; CD116 antigen TT6MP2Z GN CSF2RA TT6MP2Z FC Low affinity receptor for granulocyte-macrophage colony- stimulating factor. Transduces a signal that results in the proliferation, differentiation, and functional activation of hematopoietic cells. TT6MP2Z PD 4RS1; 4NKQ TT6MP2Z SQ MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHEGVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHLDNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSNVTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLLINVSGDLENRYNFPSSEPRAKHSVKIRAADVRILNWSSWSEAIEFGSDDGNLGSVYIYVLLIVGTLVCGIVLGFLFKRFLRIQRLFPPVPQIKDKLNDNHEVEDEIIWEEFTPEEGKGYREEVLTVKEIT TT6MP2Z TT Successful TT6MP2Z KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05200:Pathways in cancer TT6MP2Z RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-5683826:Surfactant metabolism; R-HSA-912526:Interleukin receptor SHC signaling TT8R70G ID TT8R70G TT8R70G TN Gonadotropin-releasing hormone receptor (GNRHR) TT8R70G UP P30968 TT8R70G UC GNRHR_HUMAN TT8R70G BC GPCR rhodopsin TT8R70G SN Hypothalamic gonadotropin-releasing hormone receptor; Gonadotrophin releasing hormone receptor; GnRH-R; GnRH receptor; GRHR TT8R70G GN GNRHR TT8R70G FC Receptor for gonadotropin releasing hormone (GnRH) that mediates the action of GnRH to stimulate the secretion of the gonadotropic hormones luteinizing hormone (LH) and follicle-stimulating hormone (FSH). This receptor mediates its action by association with G-proteins that activate a phosphatidylinositol-calcium second messenger system. Isoform 2 may act as an inhibitor of GnRH-R signaling. TT8R70G SQ MANSASPEQNQNHCSAINNSIPLMQGNLPTLTLSGKIRVTVTFFLFLLSATFNASFLLKLQKWTQKKEKGKKLSRMKLLLKHLTLANLLETLIVMPLDGMWNITVQWYAGELLCKVLSYLKLFSMYAPAFMMVVISLDRSLAITRPLALKSNSKVGQSMVGLAWILSSVFAGPQLYIFRMIHLADSSGQTKVFSQCVTHCSFSQWWHQAFYNFFTFSCLFIIPLFIMLICNAKIIFTLTRVLHQDPHELQLNQSKNNIPRARLKTLKMTVAFATSFTVCWTPYYVLGIWYWFDPEMLNRLSDPVNHFFFLFAFLNPCFDPLIYGYFSL TT8R70G TT Successful TT8R70G FM GPCR rhodopsin TT8R70G KE hsa04080:Neuroactive ligand-receptor interaction; hsa04912:GnRH signaling pathway TT8R70G RC R-HSA-375281:Hormone ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TT5TQ2W ID TT5TQ2W TT5TQ2W TN Granulocyte colony-stimulating factor (CSF3) TT5TQ2W UP P09919 TT5TQ2W UC CSF3_HUMAN TT5TQ2W BC Cytokine: interleukin TT5TQ2W SN Pluripoietin; Lenograstim; G-CSF; CSF3 TT5TQ2W GN CSF3 TT5TQ2W FC Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes. TT5TQ2W PD 5ZO6; 5GW9; 2D9Q; 1RHG; 1PGR TT5TQ2W SQ MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLVSECATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP TT5TQ2W TT Successful TT5TQ2W KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05144:Malaria TTNYZG2 ID TTNYZG2 TTNYZG2 TN Granulocyte-macrophage colony-stimulating factor (CSF2) TTNYZG2 UP P04141 TTNYZG2 UC CSF2_HUMAN TTNYZG2 BC Growth factor TTNYZG2 SN Sargramostim; Molgramostin; GM-CSF; Colony-stimulating factor; CSF2; CSF TTNYZG2 GN CSF2 TTNYZG2 FC Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. TTNYZG2 PD 6BFS; 6BFQ; 5D72; 5D71; 5D70 TTNYZG2 SQ MWLQSLLLLGTVACSISAPARSPSPSTQPWEHVNAIQEARRLLNLSRDTAAEMNETVEVISEMFDLQEPTCLQTRLELYKQGLRGSLTKLKGPLTMMASHYKQHCPPTPETSCATQIITFESFKENLKDFLLVIPFDCWEPVQE TTNYZG2 TT Successful TTNYZG2 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04668:TNF signaling pathway; hsa05132:Salmonella infection; hsa05146:Amoebiasis; hsa05166:HTLV-I infection; hsa05202:Transcriptional misregulation in cancer; hsa05323:Rheumatoid arthritis TTNYZG2 RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-912526:Interleukin receptor SHC signaling TTKMAZ6 ID TTKMAZ6 TTKMAZ6 TN Growth hormone receptor (GHR) TTKMAZ6 UP P10912 TTKMAZ6 UC GHR_HUMAN TTKMAZ6 BC Cytokine receptor TTKMAZ6 SN Somatotropin receptor; Serum bindingprotein; GH receptor TTKMAZ6 GN GHR TTKMAZ6 FC On ligand binding, couples to the JAK2/STAT5 pathway. Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. TTKMAZ6 PD 5OHD; 5OEK; 3HHR; 2AEW; 1KF9 TTKMAZ6 SQ MDLWQLLLTLALAGSSDAFSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKTEESDTDRLLSSDHEKSHSNLGVKDGDSGRTSCCEPDILETDFNANDIHEGTSEVAQPQRLKGEADLLCLDQKNQNNSPYHDACPATQQPSVIQAEKNKPQPLPTEGAESTHQAAHIQLSNPSSLSNIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHPEMVSLCQENFLMDNAYFCEADAKKCIPVAPHIKVESHIQPSLNQEDIYITTESLTTAAGRPGTGEHVPGSEMPVPDYTSIHIVQSPQGLILNATALPLPDKEFLSSCGYVSTDQLNKIMP TTKMAZ6 TT Successful TTKMAZ6 FM Transmembrane protein TTKMAZ6 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway TTKMAZ6 RC R-HSA-1170546:Prolactin receptor signaling; R-HSA-982772:Growth hormone receptor signaling TTWDC17 ID TTWDC17 TTWDC17 TN Growth hormone secretagogue receptor 1 (GHSR) TTWDC17 UP Q92847 TTWDC17 UC GHSR_HUMAN TTWDC17 BC GPCR rhodopsin TTWDC17 SN Growth hormone secretagogue receptor; Ghrelin receptor; GHSR; GHS-R; GHRP; GH-releasing peptide receptor TTWDC17 GN GHSR TTWDC17 FC Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Binds also other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-0677, adenosine). TTWDC17 SQ MWNATPSEEPGFNLTLADLDWDASPGNDSLGDELLQLFPAPLLAGVTATCVALFVVGIAGNLLTMLVVSRFRELRTTTNLYLSSMAFSDLLIFLCMPLDLVRLWQYRPWNFGDLLCKLFQFVSESCTYATVLTITALSVERYFAICFPLRAKVVVTKGRVKLVIFVIWAVAFCSAGPIFVLVGVEHENGTDPWDTNECRPTEFAVRSGLLTVMVWVSSIFFFLPVFCLTVLYSLIGRKLWRRRRGDAVVGASLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSFEPGSLEIAQISQYCNLVSFVLFYLSAAINPILYNIMSKKYRVAVFRLLGFEPFSQRKLSTLKDESSRAWTESSINT TTWDC17 TT Successful TTWDC17 KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTWDC17 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTLDPRG ID TTLDPRG TTLDPRG TN Guanylyl cyclase C (GUCY2C) TTLDPRG UP P25092 TTLDPRG UC GUC2C_HUMAN TTLDPRG BC Phosphorus-oxygen lyase TTLDPRG SN hSTAR; STA receptor; Intestinal guanylate cyclase; Heat-stable enterotoxin receptor; GUC2C; GC-C TTLDPRG GN GUCY2C TTLDPRG FC Receptor for the E.coli heat-stable enterotoxin (E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GC-C). Also activated by the endogenous peptides guanylin and uroguanylin. TTLDPRG EC EC 4.6.1.2 TTLDPRG SQ MKTLLLDLALWSLLFQPGWLSFSSQVSQNCHNGSYEISVLMMGNSAFAEPLKNLEDAVNEGLEIVRGRLQNAGLNVTVNATFMYSDGLIHNSGDCRSSTCEGLDLLRKISNAQRMGCVLIGPSCTYSTFQMYLDTELSYPMISAGSFGLSCDYKETLTRLMSPARKLMYFLVNFWKTNDLPFKTYSWSTSYVYKNGTETEDCFWYLNALEASVSYFSHELGFKVVLRQDKEFQDILMDHNRKSNVIIMCGGPEFLYKLKGDRAVAEDIVIILVDLFNDQYFEDNVTAPDYMKNVLVLTLSPGNSLLNSSFSRNLSPTKRDFALAYLNGILLFGHMLKIFLENGENITTPKFAHAFRNLTFEGYDGPVTLDDWGDVDSTMVLLYTSVDTKKYKVLLTYDTHVNKTYPVDMSPTFTWKNSKLPNDITGRGPQILMIAVFTLTGAVVLLLLVALLMLRKYRKDYELRQKKWSHIPPENIFPLETNETNHVSLKIDDDKRRDTIQRLRQCKYDKKRVILKDLKHNDGNFTEKQKIELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLREVLNDTISYPDGTFMDWEFKISVLYDIAKGMSYLHSSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPKKDLWTAPEHLRQANISQKGDVYSYGIIAQEIILRKETFYTLSCRDRNEKIFRVENSNGMKPFRPDLFLETAEEKELEVYLLVKNCWEEDPEKRPDFKKIETTLAKIFGLFHDQKNESYMDTLIRRLQLYSRNLEHLVEERTQLYKAERDRADRLNFMLLPRLVVKSLKEKGFVEPELYEEVTIYFSDIVGFTTICKYSTPMEVVDMLNDIYKSFDHIVDHHDVYKVETIGDAYMVASGLPKRNGNRHAIDIAKMALEILSFMGTFELEHLPGLPIWIRIGVHSGPCAAGVVGIKMPRYCLFGDTVNTASRMESTGLPLRIHVSGSTIAILKRTECQFLYEVRGETYLKGRGNETTYWLTGMKDQKFNLPTPPTVENQQRLQAEFSDMIANSLQKRQAAGIRSQKPRRVASYKKGTLEYLQLNTTDKESTYF TTLDPRG TT Successful TTQO71U ID TTQO71U TTQO71U TN Hemoglobin (HB) TTQO71U UP P69905 TTQO71U UC HBA_HUMAN TTQO71U BC Pore-forming globin TTQO71U SN Hemoglobin subunit alpha; Hemoglobin alpha chain; HBA1; Alpha-globin TTQO71U GN HBA2 TTQO71U FC Involved in oxygen transport from the lung to the various peripheral tissues. TTQO71U PD 6NBD; 6NBC; 6HBW; 6HAL; 6DI4 TTQO71U SQ MVLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR TTQO71U TT Successful TTQO71U KE hsa05143:African trypanosomiasis; hsa05144:Malaria TTQO71U RC R-HSA-1237044:Erythrocytes take up carbon dioxide and release oxygen; R-HSA-1247673:Erythrocytes take up oxygen and release carbon dioxide; R-HSA-2168880:Scavenging of heme from plasma TTQHJ1K ID TTQHJ1K TTQHJ1K TN Histamine H2 receptor (H2R) TTQHJ1K UP P25021 TTQHJ1K UC HRH2_HUMAN TTQHJ1K BC GPCR rhodopsin TTQHJ1K SN Histamine receptor 2; HH2R; Gastric receptor I TTQHJ1K GN HRH2 TTQHJ1K FC Appears to regulate gastrointestinal motility and intestinal secretion. Possible role in regulating cell growth and differentiation. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase and, through a separate G protein-dependent mechanism, the phosphoinositide/protein kinase (PKC) signaling pathway. The H2 subclass of histamine receptors mediates gastric acid secretion. TTQHJ1K SQ MAPNGTASSFCLDSTACKITITVVLAVLILITVAGNVVVCLAVGLNRRLRNLTNCFIVSLAITDLLLGLLVLPFSAIYQLSCKWSFGKVFCNIYTSLDVMLCTASILNLFMISLDRYCAVMDPLRYPVLVTPVRVAISLVLIWVISITLSFLSIHLGWNSRNETSKGNHTTSKCKVQVNEVYGLVDGLVTFYLPLLIMCITYYRIFKVARDQAKRINHISSWKAATIREHKATVTLAAVMGAFIICWFPYFTAFVYRGLRGDDAINEVLEAIVLWLGYANSALNPILYAALNRDFRTGYQQLFCCRLANRNSHKTSLRSNASQLSRTQSREPRQQEEKPLKLQVWSGTEVTAPQGATDR TTQHJ1K TT Successful TTQHJ1K KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04971:Gastric acid secretion TTQHJ1K RC R-HSA-390650:Histamine receptors; R-HSA-418555:G alpha (s) signalling events TTLUQ8E ID TTLUQ8E TTLUQ8E TN Hormone sensitive lipase (LIPE) TTLUQ8E UP Q05469 TTLUQ8E UC LIPS_HUMAN TTLUQ8E BC Carboxylic ester hydrolase TTLUQ8E SN Hormone-sensitive lipase; HSL TTLUQ8E GN LIPE TTLUQ8E FC In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production. TTLUQ8E EC EC 3.1.1.79 TTLUQ8E SQ MEPGSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPLTQQETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLGKESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQETPEQSDKQTTPVQGAKSKQGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVGSSSDTDSPATMGGMVAQGVKLGFKGKSGYKVMSGYSGTSPHEKTSARNHRHYQDTASRLIHNMDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAHLFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWKAFWNITEMEVLSSLANMASATVRVSRLLSLPPEAFEMPLTADPTLTVTISPPLAHTGPGPVLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPRPQQAPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERICLAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLQPAASPSRLLSLMDPLLPLSVLSKCVSAYAGAKTEDHSNSDQKALGMMGLVRRDTALLLRDFRLGASSWLNSFLELSGRKSQKMSEPIAEPMRRSVSEAALAQPQGPLGTDSLKNLTLRDLSLRGNSETSSDTPEMSLSAETLSPSTPSDVNFLLPPEDAGEEAEAKNELSPMDRGLGVRAAFPEGFHPRRSSQGATQMPLYSSPIVKNPFMSPLLAPDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVEDLPHGFLTLAALCRETRQAAELCVERIRLVLTPPAGAGPSGETGAAGVDGGCGGRH TTLUQ8E TT Successful TTLUQ8E FM Carboxylic ester hydrolase TTLUQ8E KE hsa04024:cAMP signaling pathway; hsa04152:AMPK signaling pathway; hsa04910:Insulin signaling pathway TTLUQ8E RC R-HSA-163560:Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis TT84ETX ID TT84ETX TT84ETX TN Human immunodeficiency virus Reverse transcriptase (HIV RT) TT84ETX UP P03366 (600-1159) TT84ETX UC POL_HV1B1 TT84ETX SN HIV p66 RT; HIV Exoribonuclease H TT84ETX GN HIV RT TT84ETX FC Gag-Pol polyprotein: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. TT84ETX EC EC 2.7.7.49 TT84ETX PD 6OE3; 6HAK; 6ELI; 6DUH; 6DUG TT84ETX SQ PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKIL TT84ETX TT Successful TTNY2AP ID TTNY2AP TTNY2AP TN Iduronate 2-sulfatase (IDS) TTNY2AP UP P22304 TTNY2AP UC IDS_HUMAN TTNY2AP BC Sulfuric ester hydrolase TTNY2AP SN Idursulfase; Iduronate 2sulfatase 14 kDa chain; IDS; AlphaLiduronate sulfate sulfatase TTNY2AP GN IDS TTNY2AP FC Required for the lysosomal degradation ofheparan sulfate and dermatan sulfate. TTNY2AP EC EC 3.1.6.13 TTNY2AP PD 6IOZ; 5FQL TTNY2AP SQ MPPPRTGRGLLWLGLVLSSVCVALGSETQANSTTDALNVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKVFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPEVPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEAGEKLFPYLDPFDSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPVPSFHVELCREGKNLLKHFRFRDLEEDPYLPGNPRELIAYSQYPRPSDIPQWNSDKPSLKDIKIMGYSIRTIDYRYTVWVGFNPDEFLANFSDIHAGELYFVDSDPLQDHNMYNDSQGGDLFQLLMP TTNY2AP TT Successful TTNY2AP KE hsa00531:Glycosaminoglycan degradation; hsa01100:Metabolic pathways; hsa04142:Lysosome TTNY2AP RC R-HSA-2024096:HS-GAG degradation; R-HSA-2024101:CS/DS degradation TTXT21W ID TTXT21W TTXT21W TN Immunoglobulin gamma Fc receptor IIA (FCGR2A) TTXT21W UP P12318 TTXT21W UC FCG2A_HUMAN TTXT21W BC Immunoglobulin TTXT21W SN Low affinity immunoglobulin gamma Fc region receptor II-a; IgG Fc receptor II-a; FcRII-a; Fc-gamma-RIIa; Fc-gamma RII-a; FCGR2A1; FCG2A; CDw32 A; CD32 A TTXT21W GN FCGR2A TTXT21W FC Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens. Promotes phagocytosis of opsonized antigens. TTXT21W PD 3RY6; 3RY5; 3RY4; 3D5O; 1H9V TTXT21W SQ MTMETQMSQNVCPRNLWLLQPLTVLLLLASADSQAAAPPKAVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQVPSMGSSSPMGIIVAVVIATAVAAIVAAVVALIYCRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQLEETNNDYETADGGYMTLNPRAPTDDDKNIYLTLPPNDHVNSNN TTXT21W TT Successful TTXT21W FM Transmembrane protein TTXT21W KE hsa04145:Phagosome; hsa04380:Osteoclast differentiation; hsa04611:Platelet activation; hsa04666:Fc gamma R-mediated phagocytosis; hsa05140:Leishmaniasis; hsa05150:Staphylococcus aureus infection; hsa05152:Tuberculosis; hsa05322:Systemic lupus erythematosus TTXT21W RC R-HSA-2029481:FCGR activation; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-2029485:Role of phospholipids in phagocytosis TTF4CAM ID TTF4CAM TTF4CAM TN Influenza Hemagglutinin (Influ HA) TTF4CAM UP P03452 TTF4CAM UC HEMA_I34A1 TTF4CAM BC Influenza viruses hemagglutinin TTF4CAM SN Hemagglutinin TTF4CAM GN Influ HA TTF4CAM FC Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. TTF4CAM PD 1RVZ; 1RVX; 1RU7 TTF4CAM SQ MKANLLVLLCALAAADADTICIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDSHNGKLCRLKGIAPLQLGKCNIAGWLLGNPECDPLLPVRSWSYIVETPNSENGICYPGDFIDYEELREQLSSVSSFERFEIFPKESSWPNHNTNGVTAACSHEGKSSFYRNLLWLTEKEGSYPKLKNSYVNKKGKEVLVLWGIHHPPNSKEQQNLYQNENAYVSVVTSNYNRRFTPEIAERPKVRDQAGRMNYYWTLLKPGDTIIFEANGNLIAPMYAFALSRGFGSGIITSNASMHECNTKCQTPLGAINSSLPYQNIHPVTIGECPKYVRSAKLRMVTGLRNIPSIQSRGLFGAIAGFIEGGWTGMIDGWYGYHHQNEQGSGYAADQKSTQNAINGITNKVNTVIEKMNIQFTAVGKEFNKLEKRMENLNKKVDDGFLDIWTYNAELLVLLENERTLDFHDSNVKNLYEKVKSQLKNNAKEIGNGCFEFYHKCDNECMESVRNGTYDYPKYSEESKLNREKVDGVKLESMGIYQILAIYSTVASSLVLLVSLGAISFWMCSNGSLQCRICI TTF4CAM TT Successful TTL7C8Q ID TTL7C8Q TTL7C8Q TN Inosine-5'-monophosphate dehydrogenase 1 (IMPDH1) TTL7C8Q UP P20839 TTL7C8Q UC IMDH1_HUMAN TTL7C8Q BC CH-OH donor oxidoreductase TTL7C8Q SN Superoxide-inducible protein 12; SOI12; Probable inosine-5'-monophosphate dehydrogenase IMD1; NAD-dependent inosine monophosphate dehydrogenase; Inosine dehydrogenase; IMPDH-I; IMPDH 1; IMPDH; IMPD1; IMPD 1; IMPD; IMP dehydrogenase 1; IMP dehydrogenase TTL7C8Q GN IMPDH1 TTL7C8Q FC Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors. Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. TTL7C8Q EC EC 1.1.1.205 TTL7C8Q PD 1JCN TTL7C8Q SQ MADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY TTL7C8Q TT Successful TTL7C8Q FM IMPDH/GMPR family TTCT6F7 ID TTCT6F7 TTCT6F7 TN Intercellular adhesion molecule ICAM-1 (ICAM1) TTCT6F7 UP P05362 TTCT6F7 UC ICAM1_HUMAN TTCT6F7 BC Immunoglobulin TTCT6F7 SN Major group rhinovirus receptor; Intercellular adhesion molecule 1; ICAM-1; CD54 TTCT6F7 GN ICAM1 TTCT6F7 FC During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). TTCT6F7 PD 6EIT; 5MZA; 3TCX; 2OZ4; 1Z7Z TTCT6F7 SQ MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTRKVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP TTCT6F7 TT Successful TTCT6F7 FM Immunoglobulin TTCT6F7 KE hsa04064:NF-kappa B signaling pathway; hsa04514:Cell adhesion molecules (CAMs); hsa04650:Natural killer cell mediated cytotoxicity; hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05150:Staphylococcus aureus infection; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05323:Rheumatoid arthritis; hsa05416:Viral myocarditis TTCT6F7 RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-216083:Integrin cell surface interactions; R-HSA-877300:Interferon gamma signaling TTMQB37 ID TTMQB37 TTMQB37 TN Interferon alpha/beta receptor 2 (IFNAR2) TTMQB37 UP P48551 TTMQB37 UC INAR2_HUMAN TTMQB37 BC Cytokine receptor TTMQB37 SN Type I interferon receptor 2; Type I interferon receptor; Interferon alpha/beta receptor; Interferon alpha binding protein; IFNARB; IFNABR; IFN-alpha/beta receptor 2; IFN-alpha-REC; IFN-alpha binding protein; IFN-R-2; IFN-R TTMQB37 GN IFNAR2 TTMQB37 FC Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1. Isoform 3 is a potent inhibitor of type I IFN receptor activity. Associates with IFNAR1 to form the type I interferon receptor. TTMQB37 PD 3SE4; 3SE3; 3S9D; 3S8W; 2LAG TTMQB37 SQ MLLSQNAFIFRSLNLVLMVYISLVFGISYDSPDYTDESCTFKISLRNFRSILSWELKNHSIVPTHYTLLYTIMSKPEDLKVVKNCANTTRSFCDLTDEWRSTHEAYVTVLEGFSGNTTLFSCSHNFWLAIDMSFEPPEFEIVGFTNHINVMVKFPSIVEEELQFDLSLVIEEQSEGIVKKHKPEIKGNMSGNFTYIIDKLIPNTNYCVSVYLEHSDEQAVIKSPLKCTLLPPGQESESAESAKIGGIITVFLIALVLTSTIVTLKWIGYICLRNSLPKVLNFHNFLAWPFPNLPPLEAMDMVEVIYINRKKKVWDYNYDDESDSDTEAAPRTSGGGYTMHGLTVRPLGQASATSTESQLIDPESEEEPDLPEVDVELPTMPKDSPQQLELLSGPCERRKSPLQDPFPEEDYSSTEGSGGRITFNVDLNSVFLRVLDDEDSDDLEAPLMLSSHLEEMVDPEDPDNVQSNHLLASGEGTQPTFPSPSSEGLWSEDAPSDQSDTSESDVDLGDGYIMR TTMQB37 TT Successful TTMQB37 FM Cytokine receptor TTMQB37 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection TTMQB37 RC R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912694:Regulation of IFNA signaling TT13TL0 ID TT13TL0 TT13TL0 TN Interferon gamma receptor (IFNGR2) TT13TL0 UP P38484 TT13TL0 UC INGR2_HUMAN TT13TL0 BC Cytokine receptor TT13TL0 SN Interferon gamma transducer 1; Interferon gamma receptor beta-chain; Interferon gamma receptor accessory factor 1; Interferon gamma receptor 2; IFNGT1; IFNGR; IFN-gamma-R2; IFN-gamma-R-beta; IFN-gamma-R; IFN-gamma receptor 2; CDw119; CD119; AF-1 TT13TL0 GN IFNGR2 TT13TL0 FC Ligand binding stimulates activation of the JAK/STAT signaling pathway. Required for signal transduction in contrast to other receptor subunit responsible for ligand binding. Associates with IFNGR1 to form a receptor for the cytokine interferon gamma (IFNG) (, ,). TT13TL0 PD 6E3L; 6E3K; 5EH1 TT13TL0 SQ MRPTLLWSLLLLLGVFAAAAAAPPDPLSQLPAPQHPKIRLYNAEQVLSWEPVALSNSTRPVVYQVQFKYTDSKWFTADIMSIGVNCTQITATECDFTAASPSAGFPMDFNVTLRLRAELGALHSAWVTMPWFQHYRNVTVGPPENIEVTPGEGSLIIRFSSPFDIADTSTAFFCYYVHYWEKGGIQQVKGPFRSNSISLDNLKPSRVYCLQVQAQLLWNKSNIFRVGHLSNISCYETMADASTELQQVILISVGTFSLLSVLAGACFFLVLKYRGLIKYWFHTPPSIPLQIEEYLKDPTQPILEALDKDSSPKDDVWDSVSIISFPEKEQEDVLQTL TT13TL0 TT Successful TT13TL0 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04380:Osteoclast differentiation; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa05132:Salmonella infection; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05321:Inflammatory bowel disease (IBD) TT13TL0 RC R-HSA-877300:Interferon gamma signaling; R-HSA-877312:Regulation of IFNG signaling TTSIUJ9 ID TTSIUJ9 TTSIUJ9 TN Interferon-alpha 2 (IFNA2) TTSIUJ9 UP P01563 TTSIUJ9 UC IFNA2_HUMAN TTSIUJ9 BC Cytokine: interferon TTSIUJ9 SN LeIF A; Interferon alphaA; Interferon alpha2; Interferon alpha-A; Interferon alpha-2; IFNalpha2; IFNA2C; IFNA2B; IFNA2A; IFN-alpha-2 TTSIUJ9 GN IFNA2 TTSIUJ9 FC Produced by macrophages, IFN-alpha have antiviral activities. TTSIUJ9 PD 4Z5R; 4YPG; 3SE3; 3S9D; 2LMS TTSIUJ9 SQ MALTFALLVALLVLSCKSSCSVGCDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE TTSIUJ9 TT Successful TTSIUJ9 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04140:Regulation of autophagy; hsa04151:PI3K-Akt signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05320:Autoimmune thyroid disease TTSIUJ9 RC R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912694:Regulation of IFNA signaling; R-HSA-933541:TRAF6 mediated IRF7 activation; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TT4TZ8J ID TT4TZ8J TT4TZ8J TN Interferon-beta (IFNB1) TT4TZ8J UP P01574 TT4TZ8J UC IFNB_HUMAN TT4TZ8J BC Cytokine: interferon TT4TZ8J SN Interferon beta; IFNbeta; IFNB; IFN-beta; IFB; Fibroblast interferon TT4TZ8J GN IFNB1 TT4TZ8J FC Has antiviral, antibacterial and anticancer activities. TT4TZ8J PD 1AU1 TT4TZ8J SQ MTNKCLLQIALLLCFSTTALSMSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN TT4TZ8J TT Successful TT4TZ8J FM Interferon TT4TZ8J KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa05142:Chagas disease (American trypanosomiasis); hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection TT4TZ8J RC R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912694:Regulation of IFNA signaling; R-HSA-918233:TRAF3-dependent IRF activation pathway; R-HSA-933541:TRAF6 mediated IRF7 activation; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTENHJ0 ID TTENHJ0 TTENHJ0 TN Interleukin 3 receptor alpha (IL3RA) TTENHJ0 UP P26951 TTENHJ0 UC IL3RA_HUMAN TTENHJ0 BC Cytokine receptor TTENHJ0 SN Interleukin-3 receptor subunit alpha; IL3R; IL-3RA; IL-3R-alpha; IL-3R subunit alpha; IL-3 receptor subunit alpha; CD123 antigen; CD123 TTENHJ0 GN IL3RA TTENHJ0 FC This is a receptor for interleukin-3. TTENHJ0 PD 5UWC; 5UV8; 4JZJ TTENHJ0 SQ MVLLWLTLLLIALPCLLQTKEDPNPPITNLRMKAKAQQLTWDLNRNVTDIECVKDADYSMPAVNNSYCQFGAISLCEVTNYTVRVANPPFSTWILFPENSGKPWAGAENLTCWIHDVDFLSCSWAVGPGAPADVQYDLYLNVANRRQQYECLHYKTDAQGTRIGCRFDDISRLSSGSQSSHILVRGRSAAFGIPCTDKFVVFSQIEILTPPNMTAKCNKTHSFMHWKMRSHFNRKFRYELQIQKRMQPVITEQVRDRTSFQLLNPGTYTVQIRARERVYEFLSAWSTPQRFECDQEEGANTRAWRTSLLIALGTLLALVCVFVICRRYLVMQRLFPRIPHMKDPIGDSFQNDKLVVWEAGKAGLEECLVTEVQVVQKT TTENHJ0 TT Successful TTENHJ0 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage TTENHJ0 RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-912526:Interleukin receptor SHC signaling TT0E5SK ID TT0E5SK TT0E5SK TN Interleukin 6 receptor (IL6R) TT0E5SK UP P08887; P40189 TT0E5SK UC IL6RA_HUMAN; IL6RB_HUMAN TT0E5SK BC Cytokine receptor TT0E5SK SN Membrane glycoprotein; Interleukin-6 receptor; IL-6R; IL-6 receptor TT0E5SK GN IL6R; IL6ST TT0E5SK FC Low concentration of a soluble form of IL6 receptor acts as an agonist of IL6 activity. TT0E5SK SQ MLAVGCALLAALLAAPGAALAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGSHPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQLSCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPPANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWMVKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESRSPPAENEVSTPMQALTTNKDDDNILFRDSANATSLPVQDSSSVPLPTFLVAGGSLAFGTLLCIAIVLRFKKTWKLRALKEGKTSMHPPYSLGQLVPERPRPTPVLVPLISPPVSPSSLGSDNTSSHNRPDARDPRSPYDISNTDYFFPR TT0E5SK TT Successful TT0E5SK KE hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04932:Non-alcoholic fatty liver disease (NAFLD) TT0E5SK RC R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-112411:MAPK1 (ERK2) activation TTGW72V ID TTGW72V TTGW72V TN Interleukin-12 beta (IL12B) TTGW72V UP P29460 TTGW72V UC IL12B_HUMAN TTGW72V BC Cytokine: interleukin TTGW72V SN NKSF2; NK cell stimulatory factor chain 2; Interleukin12 subunit beta; Interleukin-12 subunit beta; IL12 subunit p40; IL-12B; IL-12 subunit p40; Cytotoxic lymphocyte maturation factor 40 kDa subunit; CLMF p40 TTGW72V GN IL12B TTGW72V FC Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC. TTGW72V PD 5NJD; 5MZV; 5MXA; 5MJ4; 5MJ3 TTGW72V SQ MCHQQLVISWFSLVFLASPLVAIWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS TTGW72V TT Successful TTGW72V FM Cytokine: interleukin TTGW72V KE hsa04060:Cytokine-cytokine receptor interaction; hsa04620:Toll-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04940:Type I diabetes mellitus; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05321:Inflammatory bowel disease (IBD); hsa05330:Allograft rejection TTF89GD ID TTF89GD TTF89GD TN Interleukin-2 (IL2) TTF89GD UP P60568 TTF89GD UC IL2_HUMAN TTF89GD BC Cytokine: interleukin TTF89GD SN TCGF; T-cell growth factor; IL-2; Aldesleukin TTF89GD GN IL2 TTF89GD FC Produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells. TTF89GD PD 5UTZ; 5M5E; 5LQB; 4NEM; 4NEJ TTF89GD SQ MYRMQLLSCIALSLALVTNSAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT TTF89GD TT Successful TTF89GD FM Interleukin TTF89GD KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa04940:Type I diabetes mellitus; hsa05142:Chagas disease (American trypanosomiasis); hsa05162:Measles; hsa05166:HTLV-I infection; hsa05320:Autoimmune thyroid disease; hsa05321:Inflammatory bowel disease (IBD); hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease TTF89GD RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-451927:Interleukin-2 signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-912526:Interleukin receptor SHC signaling TTC1GLB ID TTC1GLB TTC1GLB TN Interleukin-23 (IL23) TTC1GLB UP Q9NPF7 TTC1GLB UC IL23A_HUMAN TTC1GLB BC Cytokine: interleukin TTC1GLB SN UNQ2498/PRO5798; SGRF; P40 subunit of interleukin-23; Interleukin-23 subunit p19; Interleukin-23 subunit alpha; Interleukin 23 subunit alpha; IL-23p19; IL-23-A; IL-23 subunit alpha; IL-23 TTC1GLB GN IL23A TTC1GLB FC IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis. Associates with IL12B to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. TTC1GLB PD 5NJD; 5MZV; 5MXA; 5MJ4; 5MJ3 TTC1GLB SQ MLGSRAVMLLLLLPWTAQGRAVPGGSSPAWTQCQQLSQKLCTLAWSAHPLVGHMDLREEGDEETTNDVPHIQCGDGCDPQGLRDNSQFCLQRIHQGLIFYEKLLGSDIFTGEPSLLPDSPVGQLHASLLGLSQLLQPEGHHWETQQIPSLSPSQPWQRLLLRFKILRSLQAFVAVAARVFAHGAATLSP TTC1GLB TT Successful TTC1GLB FM Interleukin TTC1GLB KE hsa04060:Cytokine-cytokine receptor interaction; hsa04620:Toll-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04940:Type I diabetes mellitus; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05321:Inflammatory bowel disease (IBD); hsa05330:Allograft rejection TT0HD6V ID TT0HD6V TT0HD6V TN Leptin receptor (LEPR) TT0HD6V UP P48357 TT0HD6V UC LEPR_HUMAN TT0HD6V BC Cytokine receptor TT0HD6V SN OBR; OB-R; OB receptor; LEP-R; HuB219; DB; CD295 TT0HD6V GN LEPR TT0HD6V FC On ligand binding, mediates LEP central and peripheral effects through the activation of different signaling pathways such as JAK2/STAT3 and MAPK cascade/FOS. In the hypothalamus, LEP acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic and affects innate and adaptive immunity. Control of energy homeostasis and melanocortin production (stimulation of POMC and full repression of AgRP transcription) is mediated by STAT3 signaling, whereas distinct signals regulate NPY and the control of fertility, growth and glucose homeostasis. Involved in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus. Has a specific effect on T lymphocyte responses, differentially regulating the proliferation of naive and memory T -ells. Leptin increases Th1 and suppresses Th2 cytokine production. Receptor for hormone LEP/leptin. TT0HD6V PD 6E2P; 3V6O TT0HD6V SQ MICQKFCVVLLHWEFIYVITAFNLSYPITPWRFKLSCMPPNSTYDYFLLPAGLSKNTSNSNGHYETAVEPKFNSSGTHFSNLSKTTFHCCFRSEQDRNCSLCADNIEGKTFVSTVNSLVFQQIDANWNIQCWLKGDLKLFICYVESLFKNLFRNYNYKVHLLYVLPEVLEDSPLVPQKGSFQMVHCNCSVHECCECLVPVPTAKLNDTLLMCLKITSGGVIFQSPLMSVQPINMVKPDPPLGLHMEITDDGNLKISWSSPPLVPFPLQYQVKYSENSTTVIREADKIVSATSLLVDSILPGSSYEVQVRGKRLDGPGIWSDWSTPRVFTTQDVIYFPPKILTSVGSNVSFHCIYKKENKIVPSKEIVWWMNLAEKIPQSQYDVVSDHVSKVTFFNLNETKPRGKFTYDAVYCCNEHECHHRYAELYVIDVNINISCETDGYLTKMTCRWSTSTIQSLAESTLQLRYHRSSLYCSDIPSIHPISEPKDCYLQSDGFYECIFQPIFLLSGYTMWIRINHSLGSLDSPPTCVLPDSVVKPLPPSSVKAEITINIGLLKISWEKPVFPENNLQFQIRYGLSGKEVQWKMYEVYDAKSKSVSLPVPDLCAVYAVQVRCKRLDGLGYWSNWSNPAYTVVMDIKVPMRGPEFWRIINGDTMKKEKNVTLLWKPLMKNDSLCSVQRYVINHHTSCNGTWSEDVGNHTKFTFLWTEQAHTVTVLAINSIGASVANFNLTFSWPMSKVNIVQSLSAYPLNSSCVIVSWILSPSDYKLMYFIIEWKNLNEDGEIKWLRISSSVKKYYIHDHFIPIEKYQFSLYPIFMEGVGKPKIINSFTQDDIEKHQSDAGLYVIVPVIISSSILLLGTLLISHQRMKKLFWEDVPNPKNCSWAQGLNFQKPETFEHLFIKHTASVTCGPLLLEPETISEDISVDTSWKNKDEMMPTTVVSLLSTTDLEKGSVCISDQFNSVNFSEAEGTEVTYEDESQRQPFVKYATLISNSKPSETGEEQGLINSSVTKCFSSKNSPLKDSFSNSSWEIEAQAFFILSDQHPNIISPHLTFSEGLDELLKLEGNFPEENNDKKSIYYLGVTSIKKRESGVLLTDKSRVSCPFPAPCLFTDIRVLQDSCSHFVENNINLGTSSKKTFASYMPQFQTCSTQTHKIMENKMCDLTV TT0HD6V TT Successful TT0HD6V FM Cytokine receptor TT0HD6V KE hsa04060:Cytokine-cytokine receptor interaction; hsa04080:Neuroactive ligand-receptor interaction; hsa04152:AMPK signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD) TTGKOY9 ID TTGKOY9 TTGKOY9 TN Leukotriene CysLT1 receptor (CYSLTR1) TTGKOY9 UP Q9Y271 TTGKOY9 UC CLTR1_HUMAN TTGKOY9 BC GPCR rhodopsin TTGKOY9 SN Leukotriene D4-receptor; LTD4 receptor; HMTMF81; HG55; G-protein coupled receptor HG55; Cysteinyl leukotriene receptor 1; Cysteinyl leukotriene D4 receptor; CysLTR1; CYSLT1 TTGKOY9 GN CYSLTR1 TTGKOY9 FC Stimulation by LTD4 results in the contraction and proliferation of smooth muscle, edema, eosinophil migration and damage to the mucus layer in the lung. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTD4 >> LTE4 = LTC4 >> LTB4. Receptor for cysteinyl leukotrienes mediating bronchoconstriction of individuals with and without asthma. TTGKOY9 SQ MDETGNLTVSSATCHDTIDDFRNQVYSTLYSMISVVGFFGNGFVLYVLIKTYHKKSAFQVYMINLAVADLLCVCTLPLRVVYYVHKGIWLFGDFLCRLSTYALYVNLYCSIFFMTAMSFFRCIAIVFPVQNINLVTQKKARFVCVGIWIFVILTSSPFLMAKPQKDEKNNTKCFEPPQDNQTKNHVLVLHYVSLFVGFIIPFVIIIVCYTMIILTLLKKSMKKNLSSHKKAIGMIMVVTAAFLVSFMPYHIQRTIHLHFLHNETKPCDSVLRMQKSVVITLSLAASNCCFDPLLYFFSGGNFRKRLSTFRKHSLSSVTYVPRKKASLPEKGEEICKV TTGKOY9 TT Successful TTGKOY9 FM GPCR rhodopsin TTGKOY9 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTGKOY9 RC R-HSA-391906:Leukotriene receptors; R-HSA-416476:G alpha (q) signalling events TTH0DUS ID TTH0DUS TTH0DUS TN Low-density lipoprotein receptor (LDL-R) TTH0DUS UP P01130 TTH0DUS UC LDLR_HUMAN TTH0DUS BC Low density lipoprotein receptor TTH0DUS SN LDL receptor TTH0DUS GN LDLR TTH0DUS FC In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. TTH0DUS PD 5OYL; 5OY9; 4NE9; 3SO6; 3P5C TTH0DUS SQ MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA TTH0DUS TT Successful TTH0DUS KE hsa04144:Endocytosis; hsa04913:Ovarian steroidogenesis; hsa04976:Bile secretion; hsa05145:Toxoplasmosis; hsa05160:Hepatitis C TTH0DUS RC R-HSA-171052:LDL-mediated lipid transport; R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-975634:Retinoid metabolism and transport TT2O4W9 ID TT2O4W9 TT2O4W9 TN Luteinizing hormone receptor (LHCGR) TT2O4W9 UP P22888 TT2O4W9 UC LSHR_HUMAN TT2O4W9 BC GPCR rhodopsin TT2O4W9 SN Luteinizing hormone-releasing hormone receptor; LSH-R; LHRH receptor; LHCGR; LH/CG-R TT2O4W9 GN LHCGR TT2O4W9 FC Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. TT2O4W9 PD 1XUL; 1LUT TT2O4W9 SQ MKQRFSALQLLKLLLLLQPPLPRALREALCPEPCNCVPDGALRCPGPTAGLTRLSLAYLPVKVIPSQAFRGLNEVIKIEISQIDSLERIEANAFDNLLNLSEILIQNTKNLRYIEPGAFINLPRLKYLSICNTGIRKFPDVTKVFSSESNFILEICDNLHITTIPGNAFQGMNNESVTLKLYGNGFEEVQSHAFNGTTLTSLELKENVHLEKMHNGAFRGATGPKTLDISSTKLQALPSYGLESIQRLIATSSYSLKKLPSRETFVNLLEATLTYPSHCCAFRNLPTKEQNFSHSISENFSKQCESTVRKVNNKTLYSSMLAESELSGWDYEYGFCLPKTPRCAPEPDAFNPCEDIMGYDFLRVLIWLINILAIMGNMTVLFVLLTSRYKLTVPRFLMCNLSFADFCMGLYLLLIASVDSQTKGQYYNHAIDWQTGSGCSTAGFFTVFASELSVYTLTVITLERWHTITYAIHLDQKLRLRHAILIMLGGWLFSSLIAMLPLVGVSNYMKVSICFPMDVETTLSQVYILTILILNVVAFFIICACYIKIYFAVRNPELMATNKDTKIAKKMAILIFTDFTCMAPISFFAISAAFKVPLITVTNSKVLLVLFYPINSCANPFLYAIFTKTFQRDFFLLLSKFGCCKRRAELYRRKDFSAYTSNCKNGFTGSNKPSQSTLKLSTLHCQGTALLDKTRYTEC TT2O4W9 TT Successful TT2O4W9 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04913:Ovarian steroidogenesis; hsa04917:Prolactin signaling pathway TT2O4W9 RC R-HSA-375281:Hormone ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events TTJVYO3 ID TTJVYO3 TTJVYO3 TN Myeloid cell surface antigen CD33 (CD33) TTJVYO3 UP P20138 TTJVYO3 UC CD33_HUMAN TTJVYO3 BC Immunoglobulin TTJVYO3 SN Siglec-3; Sialic acid-binding Ig-like lectin 3; SIGLEC3; Gp67 TTJVYO3 GN CD33 TTJVYO3 FC Preferentially recognizes and binds alpha-2,3- and more avidly alpha-2,6-linked sialic acid-bearing glycans. Upon engagement of ligands such as C1q or syalylated glycoproteins, two immunoreceptor tyrosine-based inhibitory motifs (ITIMs) located in CD33 cytoplasmic tail are phosphorylated by Src-like kinases such as LCK. These phosphorylations provide docking sites for the recruitment and activation of protein-tyrosine phosphatases PTPN6/SHP-1 and PTPN11/SHP-2. In turn, these phosphatases regulate downstream pathways through dephosphorylation of signaling molecules. One of the repressive effect of CD33 on monocyte activation requires phosphoinositide 3-kinase/PI3K. Sialic-acid-binding immunoglobulin-like lectin (Siglec) that plays a role in mediating cell-cell interactions and in maintaining immune cells in a resting state. TTJVYO3 PD 6D4A; 6D49; 6D48; 5J0B; 5J06 TTJVYO3 SQ MPLLLLLPLLWAGALAMDPNFWLQVQESVTVQEGLCVLVPCTFFHPIPYYDKNSPVHGYWFREGAIISRDSPVATNKLDQEVQEETQGRFRLLGDPSRNNCSLSIVDARRRDNGSYFFRMERGSTKYSYKSPQLSVHVTDLTHRPKILIPGTLEPGHSKNLTCSVSWACEQGTPPIFSWLSAAPTSLGPRTTHSSVLIITPRPQDHGTNLTCQVKFAGAGVTTERTIQLNVTYVPQNPTTGIFPGDGSGKQETRAGVVHGAIGGAGVTALLALCLCLIFFIVKTHRRKAARTAVGRNDTHPTTGSASPKHQKKSKLHGPTETSSCSGAAPTVEMDEELHYASLNFHGMNPSKDTSTEYSEVRTQ TTJVYO3 TT Successful TTJVYO3 KE hsa04640:Hematopoietic cell lineage TTJVYO3 RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell TTT9YPO ID TTT9YPO TTT9YPO TN N-acetylgalactosamine 6 sulfatase (GALNS) TTT9YPO UP P34059 TTT9YPO UC GALNS_HUMAN TTT9YPO BC Sulfuric ester hydrolase TTT9YPO SN N-acetylgalactosamine-6-sulfate sulfatase; N-acetylgalactosamine-6-sulfatase; Galactose-6-sulfate sulfatase; GalNAc6S sulfatase; GalN6S; Chondroitinsulfatase; Chondroitinase TTT9YPO GN GALNS TTT9YPO FC Catalyzes the chemical reaction of cleaving off the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of the macromolecule chondroitin sulfate and, similarly, of the D-galactose 6-sulfate units of the macromolecule keratan sulfate. TTT9YPO EC EC 3.1.6.4 TTT9YPO PD 4FDJ; 4FDI TTT9YPO SQ MAAVVAATRWWQLLLVLSAAGMGASGAPQPPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQEIVGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKARPNIPVYRDWEMVGRYYEEFPINLKTGEANLTQIYLQEALDFIKRQARHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISAPEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNLLPTLLQGRLMDRPIFYYRGDTLMAATLGQHKAHFWTWTNSWENFRQGIDFCPGQNVSGVTTHNLEDHTKLPLIFHLGRDPGERFPLSFASAEYQEALSRITSVVQQHQEALVPAQPQLNVCNWAVMNWAPPGCEKLGKCLTPPESIPKKCLWSH TTT9YPO TT Successful TTT9YPO KE hsa00531:Glycosaminoglycan degradation; hsa01100:Metabolic pathways; hsa04142:Lysosome TTF4E0J ID TTF4E0J TTF4E0J TN Neuronal acetylcholine receptor alpha-2 (CHRNA2) TTF4E0J UP Q15822 TTF4E0J UC ACHA2_HUMAN TTF4E0J BC Neurotransmitter receptor TTF4E0J SN CHRNA2 TTF4E0J GN CHRNA2 TTF4E0J FC After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. TTF4E0J PD 5FJV TTF4E0J SQ MGPSCPVFLSFTKLSLWWLLLTPAGGEEAKRPPPRAPGDPLSSPSPTALPQGGSHTETEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSDCGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHTMPHWVRGALLGCVPRWLLMNRPPPPVELCHPLRLKLSPSYHWLESNVDAEEREVVVEEEDRWACAGHVAPSVGTLCSHGHLHSGASGPKAEALLQEGELLLSPHMQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVIDRIFLWLFIIVCFLGTIGLFLPPFLAGMI TTF4E0J TT Successful TTF4E0J KE hsa04080:Neuroactive ligand-receptor interaction TTF4E0J RC R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors; R-HSA-629597:Highly calcium permeable nicotinic acetylcholine receptors TTLA931 ID TTLA931 TTLA931 TN Neuronal acetylcholine receptor alpha-7 (CHRNA7) TTLA931 UP P36544 TTLA931 UC ACHA7_HUMAN TTLA931 BC Neurotransmitter receptor TTLA931 SN Nicotinic acetylcholine receptor subunit alpha 7; Nicotinic acetylcholine receptor alpha7; CHRNA7; Alpha7 nicotinic receptor; Alpha7 nAChR; Alpha-7 nAChR; Alpha(7) nicotinic receptor TTLA931 GN CHRNA7 TTLA931 FC After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin. TTLA931 PD 5AFN; 5AFM; 5AFL; 5AFK; 5AFJ TTLA931 SQ MRCSPGGVWLALAASLLHVSLQGEFQRKLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWTDHYLQWNVSEYPGVKTVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNSSGHCQYLPPGIFKSSCYIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPGKRSERFYECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPDGGKMPKWTRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLASVEMSAVAPPPASNGNLLYIGFRGLDGVHCVPTPDSGVVCGRMACSPTHDEHLLHGGQPPEGDPDLAKILEEVRYIANRFRCQDESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDFA TTLA931 TT Successful TTLA931 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa05033:Nicotine addiction; hsa05204:Chemical carcinogenesis TTLA931 RC R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors TTIPJCB ID TTIPJCB TTIPJCB TN Neuropilin-1 (NRP1) TTIPJCB UP O14786 TTIPJCB UC NRP1_HUMAN TTIPJCB BC Neuropilin and tolloid-like TTIPJCB SN Vascular endothelial cell growth factor 165 receptor; VEGF165R; Platelet-derived endothelial cell growth factor receptor; NRP; Membrane-bound; CD304 TTIPJCB GN NRP1 TTIPJCB FC It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 isoform of PGF, The VEGF165 isoform of VEGFA and VEGFB. Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulate VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development. The membrane-bound isoform 1 is a receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. TTIPJCB PD 6FMF; 6FMC; 5L73; 5JHK; 5JGQ TTIPJCB SQ MERGLPLLCAVLALVLAPAGAFRNDKCGDTIKIESPGYLTSPGYPHSYHPSEKCEWLIQAPDPYQRIMINFNPHFDLEDRDCKYDYVEVFDGENENGHFRGKFCGKIAPPPVVSSGPFLFIKFVSDYETHGAGFSIRYEIFKRGPECSQNYTTPSGVIKSPGFPEKYPNSLECTYIVFVPKMSEIILEFESFDLEPDSNPPGGMFCRYDRLEIWDGFPDVGPHIGRYCGQKTPGRIRSSSGILSMVFYTDSAIAKEGFSANYSVLQSSVSEDFKCMEALGMESGEIHSDQITASSQYSTNWSAERSRLNYPENGWTPGEDSYREWIQVDLGLLRFVTAVGTQGAISKETKKKYYVKTYKIDVSSNGEDWITIKEGNKPVLFQGNTNPTDVVVAVFPKPLITRFVRIKPATWETGISMRFEVYGCKITDYPCSGMLGMVSGLISDSQITSSNQGDRNWMPENIRLVTSRSGWALPPAPHSYINEWLQIDLGEEKIVRGIIIQGGKHRENKVFMRKFKIGYSNNGSDWKMIMDDSKRKAKSFEGNNNYDTPELRTFPALSTRFIRIYPERATHGGLGLRMELLGCEVEAPTAGPTTPNGNLVDECDDDQANCHSGTGDDFQLTGGTTVLATEKPTVIDSTIQSEFPTYGFNCEFGWGSHKTFCHWEHDNHVQLKWSVLTSKTGPIQDHTGDGNFIYSQADENQKGKVARLVSPVVYSQNSAHCMTFWYHMSGSHVGTLRVKLRYQKPEEYDQLVWMAIGHQGDHWKEGRVLLHKSLKLYQVIFEGEIGKGNLGGIAVDDISINNHISQEDCAKPADLDKKNPEIKIDETGSTPGYEGEGEGDKNISRKPGNVLKTLDPILITIIAMSALGVLLGAVCGVVLYCACWHNGMSERNLSALENYNFELVDGVKLKKDKLNTQSTYSEA TTIPJCB TT Successful TTIPJCB FM Neuropilin family TTIPJCB KE hsa04360:Axon guidance; hsa05166:HTLV-I infection TTIPJCB RC R-HSA-194306:Neurophilin interactions with VEGF and VEGFR; R-HSA-399956:CRMPs in Sema3A signaling; R-HSA-447041:CHL1 interactions TTPD1CN ID TTPD1CN TTPD1CN TN Niemann-Pick C1-like protein 1 (NPC1L1) TTPD1CN UP Q9UHC9 TTPD1CN UC NPCL1_HUMAN TTPD1CN SN Niemann-Pick C1 Like 1; NPC1L1 TTPD1CN GN NPC1L1 TTPD1CN FC Plays a major role in cholesterol homeostasis. Is critical for the uptake of cholesterol across the plasma membrane of the intestinal enterocyte. Is the direct molecular target of ezetimibe, a drug that inhibits cholesterol absorption. Lack of activity leads to multiple lipid transport defects. The protein may have a function in the transport of multiple lipids and their homeostasis, and may play a critical role in regulating lipid metabolism. Acts as a negative regulator of NPC2 and down- regulates its expression and secretion by inhibiting its maturation and accelerating its degradation. TTPD1CN PD 3QNT TTPD1CN SQ MAEAGLRGWLLWALLLRLAQSEPYTTIHQPGYCAFYDECGKNPELSGSLMTLSNVSCLSNTPARKITGDHLILLQKICPRLYTGPNTQACCSAKQLVSLEASLSITKALLTRCPACSDNFVNLHCHNTCSPNQSLFINVTRVAQLGAGQLPAVVAYEAFYQHSFAEQSYDSCSRVRVPAAATLAVGTMCGVYGSALCNAQRWLNFQGDTGNGLAPLDITFHLLEPGQAVGSGIQPLNEGVARCNESQGDDVATCSCQDCAASCPAIARPQALDSTFYLGQMPGSLVLIIILCSVFAVVTILLVGFRVAPARDKSKMVDPKKGTSLSDKLSFSTHTLLGQFFQGWGTWVASWPLTILVLSVIPVVALAAGLVFTELTTDPVELWSAPNSQARSEKAFHDQHFGPFFRTNQVILTAPNRSSYRYDSLLLGPKNFSGILDLDLLLELLELQERLRHLQVWSPEAQRNISLQDICYAPLNPDNTSLYDCCINSLLQYFQNNRTLLLLTANQTLMGQTSQVDWKDHFLYCANAPLTFKDGTALALSCMADYGAPVFPFLAIGGYKGKDYSEAEALIMTFSLNNYPAGDPRLAQAKLWEEAFLEEMRAFQRRMAGMFQVTFMAERSLEDEINRTTAEDLPIFATSYIVIFLYISLALGSYSSWSRVMVDSKATLGLGGVAVVLGAVMAAMGFFSYLGIRSSLVILQVVPFLVLSVGADNIFIFVLEYQRLPRRPGEPREVHIGRALGRVAPSMLLCSLSEAICFFLGALTPMPAVRTFALTSGLAVILDFLLQMSAFVALLSLDSKRQEASRLDVCCCVKPQELPPPGQGEGLLLGFFQKAYAPFLLHWITRGVVLLLFLALFGVSLYSMCHISVGLDQELALPKDSYLLDYFLFLNRYFEVGAPVYFVTTLGYNFSSEAGMNAICSSAGCNNFSFTQKIQYATEFPEQSYLAIPASSWVDDFIDWLTPSSCCRLYISGPNKDKFCPSTVNSLNCLKNCMSITMGSVRPSVEQFHKYLPWFLNDRPNIKCPKGGLAAYSTSVNLTSDGQVLDTVAILSPRLEYSGTISAHCNLYLLDSTSRFMAYHKPLKNSQDYTEALRAARELAANITADLRKVPGTDPAFEVFPYTITNVFYEQYLTILPEGLFMLSLCLVPTFAVSCLLLGLDLRSGLLNLLSIVMILVDTVGFMALWGISYNAVSLINLVSAVGMSVEFVSHITRSFAISTKPTWLERAKEATISMGSAVFAGVAMTNLPGILVLGLAKAQLIQIFFFRLNLLITLLGLLHGLVFLPVILSYVGPDVNPALALEQKRAEEAVAAVMVASCPNHPSRVSTADNIYVNHSFEGSIKGAGAISNFLPNNGRQF TTPD1CN TT Successful TTPD1CN KE hsa04975:Fat digestion and absorption TTAWNKZ ID TTAWNKZ TTAWNKZ TN Norepinephrine transporter (NET) TTAWNKZ UP P23975 TTAWNKZ UC SC6A2_HUMAN TTAWNKZ BC Neurotransmitter:sodium symporter TTAWNKZ SN Solute carrier family 6 member 2; Sodium-dependent noradrenaline transporter; SLC6A2; NET1; NET; NAT1 TTAWNKZ GN SLC6A2 TTAWNKZ FC Amine transporter. Terminates the action of noradrenaline by its high affinity sodium-dependent reuptake into presynaptic terminals. TTAWNKZ SQ MLLARMNPQVQPENNGADTGPEQPLRARKTAELLVVKERNGVQCLLAPRDGDAQPRETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQYNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFSSFTLNLPWTDCGHTWNSPNCTDPKLLNGSVLGNHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLMVVVIVLYFSLWKGVKTSGKVVWITATLPYFVLFVLLVHGVTLPGASNGINAYLHIDFYRLKEATVWIDAATQIFFSLGAGFGVLIAFASYNKFDNNCYRDALLTSSINCITSFVSGFAIFSILGYMAHEHKVNIEDVATEGAGLVFILYPEAISTLSGSTFWAVVFFVMLLALGLDSSMGGMEAVITGLADDFQVLKRHRKLFTFGVTFSTFLLALFCITKGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSNDIQQMMGFRPGLYWRLCWKFVSPAFLLFVVVVSIINFKPLTYDDYIFPPWANWVGWGIALSSMVLVPIYVIYKFLSTQGSLWERLAYGITPENEHHLVAQRDIRQFQLQHWLAI TTAWNKZ TT Successful TTAWNKZ RC R-HSA-442660:Na+/Cl- dependent neurotransmitter transporters TTSXVID ID TTSXVID TTSXVID TN Nuclear factor NF-kappa-B (NFKB) TTSXVID UP P19838; Q00653; Q04206; Q01201; Q04864 TTSXVID UC NFKB1_HUMAN; NFKB2_HUMAN; TF65_HUMAN; RELB_HUMAN; REL_HUMAN TTSXVID SN Nuclear factor of kappa light polypeptide gene enhancer in B-cells; DNA-binding factor KBF TTSXVID GN NFKB1; NFKB2; RELA; RELB; REL TTSXVID FC NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. TTSXVID SQ MAEDDPYLGRPEQMFHLDPSLTHTIFNPEVFQPQMALPTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGGTGSTGPGYSFPHYGFPTYGGITFHPGTTKSNAGMKHGTMDTESKKDPEGCDKSDDKNTVNLFGKVIETTEQDQEPSEATVGNGEVTLTYATGTKEESAGVQDNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWENAGEDEGVVPGTTPLDMATSWQVFDILNGKPYEPEFTSDDLLAQGDMKQLAEDVKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQAASSPVKTTSQAHSLPLSPASTRQQIDELRDSDSVCDSGVETSFRKLSFTESLTSGASLLTLNKMPHDYGQEGPLEGKI TTSXVID TT Successful TTSXVID KE hsa04010:MAPK signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04380:Osteoclast differentiation; hsa05134:Legionellosis; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis TTSXVID RC R-HSA-1810476:RIP-mediated NFkB activation via ZBP1; R-HSA-3134963:DEx/H-box helicases activate type I IFN and inflammatory cytokines production; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-448706:Interleukin-1 processing; R-HSA-5603027:IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR); R-HSA-5603029:IkBA variant leads to EDA-ID; R-HSA-5607761:Dectin-1 mediated noncanonical NF-kB signaling; R-HSA-5676590:NIK-->noncanonical NF-kB signaling; R-HSA-933542:TRAF6 mediated NF-kB activation TT9N02I ID TT9N02I TT9N02I TN Orexin receptor type 2 (HCRTR2) TT9N02I UP O43614 TT9N02I UC OX2R_HUMAN TT9N02I BC GPCR rhodopsin TT9N02I SN Ox2r; Ox2-R; Ox-2-R; Orexin-2 receptor; Hypocretin receptor type 2; HFGANP TT9N02I GN HCRTR2 TT9N02I FC Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding. Nonselective, high-affinity receptor for both orexin-A and orexin-B neuropeptides. TT9N02I PD 5WS3; 5WQC; 4S0V TT9N02I SQ MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW TT9N02I TT Successful TT9N02I FM GPCR rhodopsin TT9N02I KE hsa04080:Neuroactive ligand-receptor interaction TT9N02I RC R-HSA-416476:G alpha (q) signalling events TTV2A1R ID TTV2A1R TTV2A1R TN Oxalosuccinate decarboxylase (IDH1) TTV2A1R UP O75874 TTV2A1R UC IDHC_HUMAN TTV2A1R BC Short-chain dehydrogenases reductase TTV2A1R SN PICD; NADP(+)-specific ICDH; Isocitrate dehydrogenase [NADP] cytoplasmic; IDP; IDH; Cytosolic NADP-isocitrate dehydrogenase TTV2A1R GN IDH1 TTV2A1R FC Catalyses the NADPH-dependent reduction of alpha-ketoglutarate to R(-)-2-hydroxyglutarate (2HG). TTV2A1R EC EC 1.1.1.42 TTV2A1R PD 6BL2; 6BL1; 6BL0; 6BKZ; 6BKY TTV2A1R SQ MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL TTV2A1R TT Successful TTV2A1R KE hsa00020:Citrate cycle (TCA cycle); hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa01210:2-Oxocarboxylic acid metabolism; hsa01230:Biosynthesis of amino acids; hsa04146:Peroxisome; hsa05230:Central carbon metabolism in cancer TTZ1DT0 ID TTZ1DT0 TTZ1DT0 TN P2Y purinoceptor 12 (P2RY12) TTZ1DT0 UP Q9H244 TTZ1DT0 UC P2Y12_HUMAN TTZ1DT0 BC GPCR rhodopsin TTZ1DT0 SN SP1999; P2Y12 platelet ADP receptor; P2Y12; P2Y(cyc); P2Y(ADP)P2Y purinoceptor 12; P2Y(ADP); P2Y(AC); P2T(AC); P2RY12; Nucleotide P2Y(12) receptor; Adenosine P2Y12 receptor; ADPG-R; ADP-glucose receptor TTZ1DT0 GN P2RY12 TTZ1DT0 FC Receptor for ADP and ATP coupled to G-proteins that inhibit the adenylyl cyclase second messenger system. Not activated by UDP and UTP. Required for normal platelet aggregation and blood coagulation. TTZ1DT0 PD 4PY0; 4PXZ; 4NTJ; 1Y9C; 1VZ1 TTZ1DT0 SQ MQAVDNLTSAPGNTSLCTRDYKITQVLFPLLYTVLFFVGLITNGLAMRIFFQIRSKSNFIIFLKNTVISDLLMILTFPFKILSDAKLGTGPLRTFVCQVTSVIFYFTMYISISFLGLITIDRYQKTTRPFKTSNPKNLLGAKILSVVIWAFMFLLSLPNMILTNRQPRDKNVKKCSFLKSEFGLVWHEIVNYICQVIFWINFLIVIVCYTLITKELYRSYVRTRGVGKVPRKKVNVKVFIIIAVFFICFVPFHFARIPYTLSQTRDVFDCTAENTLFYVKESTLWLTSLNACLDPFIYFFLCKSFRNSLISMLKCPNSATSLSQDNRKKEQDGGDPNEETPM TTZ1DT0 TT Successful TTZ1DT0 KE hsa04611:Platelet activation TTZ1DT0 RC R-HSA-417957:P2Y receptors; R-HSA-418594:G alpha (i) signalling events TT3NKIB ID TT3NKIB TT3NKIB TN Pancreatic elastase 1 (CELA1) TT3NKIB UP Q9UNI1 TT3NKIB UC CELA1_HUMAN TT3NKIB BC Peptidase TT3NKIB SN Elastase; CELA1 TT3NKIB GN CELA1 TT3NKIB FC Acts upon elastin. TT3NKIB EC EC 3.4.21.36 TT3NKIB SQ MLVLYGHSTQDLPETNARVVGGTEAGRNSWPSQISLQYRSGGSRYHTCGGTLIRQNWVMTAAHCVDYQKTFRVVAGDHNLSQNDGTEQYVSVQKIVVHPYWNSDNVAAGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGQLAQTLQQAYLPSVDYAICSSSSYWGSTVKNTMVCAGGDGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFVSSRGCNVSRKPTVFTQVSAYISWINNVIASN TT3NKIB TT Successful TTFPD47 ID TTFPD47 TTFPD47 TN Parathyroid hormone 1 receptor (PTH1R) TTFPD47 UP Q03431 TTFPD47 UC PTH1R_HUMAN TTFPD47 BC GPCR secretin TTFPD47 SN Parathyroid hormone-related peptide (PTHRP); PTH1R; PTH/PTHrP type I receptor; PTH/PTHr receptor TTFPD47 GN PTH1R TTFPD47 FC This is a receptor for parathyroid hormone and for parathyroid hormone-related peptide. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase and also a phosphatidylinositol-calcium second messenger system. TTFPD47 PD 6NBI; 6NBH; 6NBF; 5EMB; 4Z8J TTFPD47 SQ MGTARIAPGLALLLCCPVLSSAYALVDADDVMTKEEQIFLLHRAQAQCEKRLKEVLQRPASIMESDKGWTSASTSGKPRKDKASGKLYPESEEDKEAPTGSRYRGRPCLPEWDHILCWPLGAPGEVVAVPCPDYIYDFNHKGHAYRRCDRNGSWELVPGHNRTWANYSECVKFLTNETREREVFDRLGMIYTVGYSVSLASLTVAVLILAYFRRLHCTRNYIHMHLFLSFMLRAVSIFVKDAVLYSGATLDEAERLTEEELRAIAQAPPPPATAAAGYAGCRVAVTFFLYFLATNYYWILVEGLYLHSLIFMAFFSEKKYLWGFTVFGWGLPAVFVAVWVSVRATLANTGCWDLSSGNKKWIIQVPILASIVLNFILFINIVRVLATKLRETNAGRCDTRQQYRKLLKSTLVLMPLFGVHYIVFMATPYTEVSGTLWQVQMHYEMLFNSFQGFFVAIIYCFCNGEVQAEIKKSWSRWTLALDFKRKARSGSSSYSYGPMVSHTSVTNVGPRVGLGLPLSPRLLPTATTNGHPQLPGHAKPGTPALETLETTPPAMAAPKDDGFLNGSCSGLDEEASGPERPPALLQEEWETVM TTFPD47 TT Successful TTFPD47 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04961:Endocrine and other factor-regulated calcium reabsorption TTFPD47 RC R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-418555:G alpha (s) signalling events TTGSVH2 ID TTGSVH2 TTGSVH2 TN Phenylalanine hydroxylase (PAH) TTGSVH2 UP P00439 TTGSVH2 UC PH4H_HUMAN TTGSVH2 BC Paired donor oxygen oxidoreductase TTGSVH2 SN Phenylalanine4hydroxylase; Phenylalanine-4-hydroxylase; Phe4monooxygenase; Phe-4-monooxygenase TTGSVH2 GN PAH TTGSVH2 FC Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine. TTGSVH2 EC EC 1.14.16.1 TTGSVH2 PD 6PAH; 6N1K; 5PAH; 5FII; 4PAH TTGSVH2 SQ MSTAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSINSEIGILCSALQKIK TTGSVH2 TT Successful TTGSVH2 FM Oxidoreductases acting on paired donors TTGSVH2 KE hsa00360:Phenylalanine metabolism; hsa00400:Phenylalanine, tyrosine and tryptophan biosynthesis; hsa01100:Metabolic pathways; hsa01230:Biosynthesis of amino acids TT48I1Y ID TT48I1Y TT48I1Y TN Placenta growth factor (PlGF) TT48I1Y UP P49763 TT48I1Y UC PLGF_HUMAN TT48I1Y BC Growth factor TT48I1Y SN SHGC-10760; PlGF-2; PLGF; PGFL; D12S1900 TT48I1Y GN PGF TT48I1Y FC It binds to the receptor FLT1/VEGFR-1. Isoform PlGF-2 binds NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent manner. Also promotes cell tumor growth. Growth factor active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. TT48I1Y PD 1RV6; 1FZV TT48I1Y SQ MPVMRLFPCFLQLLAGLALPAVPPQQWALSAGNGSSEVEVVPFQEVWGRSYCRALERLVDVVSEYPSEVEHMFSPSCVSLLRCTGCCGDENLHCVPVETANVTMQLLKIRSGDRPSYVELTFSQHVRCECRHSPGRQSPDMPGDFRADAPSFLPPRRSLPMLFRMEWGCALTGSQSAVWPSSPVPEEIPRMHPGRNGKKQQRKPLREKMKPERCGDAVPRR TT48I1Y TT Successful TT48I1Y FM Growth factor TT48I1Y KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa05200:Pathways in cancer TT48I1Y RC R-HSA-194313:VEGF ligand-receptor interactions; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization TTLH4J3 ID TTLH4J3 TTLH4J3 TN Plasmodium DOXP reductoisomerase (Malaria DXR) TTLH4J3 UP O96693 TTLH4J3 UC DXR_PLAFX TTLH4J3 BC Short-chain dehydrogenases reductase TTLH4J3 SN IspC; DXR; DXP reductoisomerase; DOXP reductoisomerase; 2-C-Methyl-d-erythritol 4-phosphate synthase; 1-deoxyxylulose-5-phosphate reductoisomerase TTLH4J3 GN Malaria DXR TTLH4J3 FC Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). TTLH4J3 EC EC 1.1.1.267 TTLH4J3 PD 4KP7; 4GAE; 3WQS; 3WQR; 3WQQ TTLH4J3 SQ MKKYIYIYFFFITITINDLVINNTSKCVSIERRKNNAYINYGIGYNGPDNKITKSRRCKRIKLCKKDLIDIGAIKKPINVAIFGSTGSIGTNALNIIRECNKIENVFNVKALYVNKSVNELYEQAREFLPEYLCIHDKSVYEELKELVKNIKDYKPIILCGDEGMKEICSSNSIDKIVIGIDSFQGLYSTMYAIMNNKIVALANKESIVSAGFFLKKLLNIHKNAKIIPVDSEHSAIFQCLDNNKVLKTKCLQDNFSKINNINKIFLCSSGGPFQNLTMDELKNVTSENALKHPKWKMGKKITIDSATMMNKGLEVIETHFLFDVDYNDIEVIVHKECIIHSCVEFIDKSVISQMYYPDMQIPILYSLTWPDRIKTNLKPLDLAQVSTLTFHKPSLEHFPCIKLAYQAGIKGNFYPTVLNASNEIANNLFLNNKIKYFDISSIISQVLESFNSQKVSENSEDLMKQILQIHSWAKDKATDIYNKHNSS TTLH4J3 TT Successful TT8ZLTI ID TT8ZLTI TT8ZLTI TN Programmed cell death 1 ligand 1 (PD-L1) TT8ZLTI UP Q9NZQ7 TT8ZLTI UC PD1L1_HUMAN TT8ZLTI BC Immunoglobulin TT8ZLTI SN hPD-L1; Programmed death ligand 1; PDL1; PDCD1LG1; PDCD1L1; PDCD1 ligand 1; B7H1; B7-H1; B7 homolog 1 TT8ZLTI GN CD274 TT8ZLTI FC As a ligand for the inhibitory receptor PDCD1/PD-1, modulates the activation threshold of T-cells and limits T-cell effector response. Through a yet unknown activating receptor, may costimulate T-cell subsets that predominantly produce interleukin-10 (IL10). Plays a critical role in induction and maintenance of immune tolerance to self. TT8ZLTI PD 6R3K; 6NP9; 6NOS; 6NOJ; 6NNV TT8ZLTI SQ MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET TT8ZLTI TT Successful TT8ZLTI FM Immunoglobulin TT8ZLTI KE hsa04514:Cell adhesion molecules (CAMs) TT8ZLTI RC R-HSA-389948:PD-1 signaling TTNBFWK ID TTNBFWK TTNBFWK TN Programmed cell death protein 1 (PD-1) TTNBFWK UP Q15116 TTNBFWK UC PDCD1_HUMAN TTNBFWK BC Immunoglobulin TTNBFWK SN hPD1; hPD-1; Protein PD1; Protein PD-1; PD1; CD279 TTNBFWK GN PDCD1 TTNBFWK FC Delivers inhibitory signals upon binding to ligands CD274/PDCD1L1 and CD273/PDCD1LG2. Following T-cell receptor (TCR) engagement, PDCD1 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation. Suppresses T-cell activation through the recruitment of PTPN11/SHP-2: following ligand-binding, PDCD1 is phosphorylated within the ITSM motif, leading to the recruitment of the protein tyrosine phosphatase PTPN11/SHP-2 that mediates dephosphorylation of key TCR proximal signaling molecules, such as ZAP70, PRKCQ/PKCtheta and CD247/CD3zeta. Inhibitory receptor on antigen activated T-cells that plays a critical role in induction and maintenance of immune tolerance to self. TTNBFWK PD 5WT9; 5JXE; 5IUS; 5GGS; 5GGR TTNBFWK SQ MQIPQAPWPVVWAVLQLGWRPGWFLDSPDRPWNPPTFSPALLVVTEGDNATFTCSFSNTSESFVLNWYRMSPSNQTDKLAAFPEDRSQPGQDCRFRVTQLPNGRDFHMSVVRARRNDSGTYLCGAISLAPKAQIKESLRAELRVTERRAEVPTAHPSPSPRPAGQFQTLVVGVVGGLLGSLVLLVWVLAVICSRAARGTIGARRTGQPLKEDPSAVPVFSVDYGELDFQWREKTPEPPVPCVPEQTEYATIVFPSGMGTSSPARRGSADGPRSAQPLRPEDGHCSWPL TTNBFWK TT Successful TTNBFWK FM Immunoglobulin TTNBFWK KE hsa04514:Cell adhesion molecules (CAMs); hsa04660:T cell receptor signaling pathway TTNBFWK RC R-HSA-389948:PD-1 signaling TT1ZAVI ID TT1ZAVI TT1ZAVI TN Prostaglandin E2 receptor EP2 (PTGER2) TT1ZAVI UP P43116 TT1ZAVI UC PE2R2_HUMAN TT1ZAVI BC GPCR rhodopsin TT1ZAVI SN Prostanoid EP2 receptor; Prostaglandin E2 receptor EP2 subtype; PGE2 receptor EP2 subtype; PGE receptor, EP2 subtype; PGE receptor EP2 subtype; EP2 receptor TT1ZAVI GN PTGER2 TT1ZAVI FC The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. The subsequent raise in intracellular cAMP is responsible for the relaxing effect of this receptor on smooth muscle. Receptor for prostaglandin E2 (PGE2). TT1ZAVI SQ MGNASNDSQSEDCETRQWLPPGESPAISSVMFSAGVLGNLIALALLARRWRGDVGCSAGRRSSLSLFHVLVTELVFTDLLGTCLISPVVLASYARNQTLVALAPESRACTYFAFAMTFFSLATMLMLFAMALERYLSIGHPYFYQRRVSRSGGLAVLPVIYAVSLLFCSLPLLDYGQYVQYCPGTWCFIRHGRTAYLQLYATLLLLLIVSVLACNFSVILNLIRMHRRSRRSRCGPSLGSGRGGPGARRRGERVSMAEETDHLILLAIMTITFAVCSLPFTIFAYMNETSSRKEKWDLQALRFLSINSIIDPWVFAILRPPVLRLMRSVLCCRISLRTQDATQTSCSTQSDASKQADL TT1ZAVI TT Successful TT1ZAVI FM GPCR rhodopsin TT1ZAVI KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04924:Renin secretion; hsa05200:Pathways in cancer TT1ZAVI RC R-HSA-391908:Prostanoid ligand receptors; R-HSA-418555:G alpha (s) signalling events TTT2ZAR ID TTT2ZAR TTT2ZAR TN Prostaglandin F2-alpha receptor (PTGFR) TTT2ZAR UP P43088 TTT2ZAR UC PF2R_HUMAN TTT2ZAR BC GPCR rhodopsin TTT2ZAR SN Prostanoid FP receptor; PGF2-alpha receptor; PGF2 alpha receptor; PGF receptor; FP prostanoid receptor; FP prostaglandin receptor TTT2ZAR GN PTGFR TTT2ZAR FC The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. Initiates luteolysis in the corpus luteum. Isoforms 2 to 7 do not bind PGF2-alpha but are proposed to modulate signaling by participating in variant receptor complexes; heterodimers between isoform 1 and isoform 5 are proposed to be a receptor for prostamides including the synthetic analog bimatoprost. Receptor for prostaglandin F2-alpha (PGF2-alpha). TTT2ZAR SQ MSMNNSKQLVSPAAALLSNTTCQTENRLSVFFSVIFMTVGILSNSLAIAILMKAYQRFRQKSKASFLLLASGLVITDFFGHLINGAIAVFVYASDKEWIRFDQSNVLCSIFGICMVFSGLCPLLLGSVMAIERCIGVTKPIFHSTKITSKHVKMMLSGVCLFAVFIALLPILGHRDYKIQASRTWCFYNTEDIKDWEDRFYLLLFSFLGLLALGVSLLCNAITGITLLRVKFKSQQHRQGRSHHLEMVIQLLAIMCVSCICWSPFLVTMANIGINGNHSLETCETTLFALRMATWNQILDPWVYILLRKAVLKNLYKLASQCCGVHVISLHIWELSSIKNSLKVAAISESPVAEKSAST TTT2ZAR TT Successful TTT2ZAR FM GPCR rhodopsin TTT2ZAR KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTT2ZAR RC R-HSA-391908:Prostanoid ligand receptors; R-HSA-416476:G alpha (q) signalling events TTVKILB ID TTVKILB TTVKILB TN Prostaglandin G/H synthase 2 (COX-2) TTVKILB UP P35354 TTVKILB UC PGH2_HUMAN TTVKILB BC Paired donor oxygen oxidoreductase TTVKILB SN Prostaglandin-endoperoxide synthase 2; Prostaglandin H2 synthase 2; PHS II; PGHS-2; PGH synthase 2; Cyclooxygenase-2; COX2; COX-2 TTVKILB GN PTGS2 TTVKILB FC Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. In cancer cells, PTGS2 is a key step in the production of prostaglandin E2 (PGE2), which plays important roles in modulating motility, proliferation and resistance to apoptosis. During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs), especially 15-R-lipoxin A4, that regulates phagocytic microglia (By similarity). TTVKILB EC EC 1.14.99.1 TTVKILB PD 5KIR; 5IKV; 5IKT; 5IKR; 5IKQ TTVKILB SQ MLARALLLCAVLALSHTANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFLTRIKLFLKPTPNTVHYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNADYGYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKYQIIDGEMYPPTVKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQNRIAAEFNTLYHWHPLLPDTFQIHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAGRVAGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEVGFQIINTASIQSLICNNVKGCPFTSFSVPDPELIKTVTINASSSRSGLDDINPTVLLKERSTEL TTVKILB TT Successful TTVKILB FM Cytochrome c oxidase subunit 2 family TTVKILB KE hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04064:NF-kappa B signaling pathway; hsa04370:VEGF signaling pathway; hsa04668:TNF signaling pathway; hsa04723:Retrograde endocannabinoid signaling; hsa04726:Serotonergic synapse; hsa04913:Ovarian steroidogenesis; hsa04921:Oxytocin signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa05140:Leishmaniasis; hsa05200:Pathways in cancer; hsa05204:Chemical carcinogenesis; hsa05206:MicroRNAs in cancer; hsa05222:Small cell lung cancer TTISP28 ID TTISP28 TTISP28 TN Retinoic acid receptor beta (RARB) TTISP28 UP P10826 TTISP28 UC RARB_HUMAN TTISP28 BC Nuclear hormone receptor TTISP28 SN RAR-epsilon; RAR-beta; Nuclear receptor subfamily 1 group B member 2; NR1B2; HBV-activated protein; HAP TTISP28 GN RARB TTISP28 FC Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function. Receptor for retinoic acid. TTISP28 PD 5UAN; 4JYI; 4JYH; 4JYG; 4DM8 TTISP28 SQ MTTSGHACPVPAVNGHMTHYPATPYPLLFPPVIGGLSLPPLHGLHGHPPPSGCSTPSPATIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKETSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPTKVDKLQEPLLEALKIYIRKRRPSKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPSSSGNTAEHSPSISPSSVENSGVSQSPLVQ TTISP28 TT Successful TTISP28 FM Nuclear hormone receptor TTISP28 KE hsa05200:Pathways in cancer; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer TTISP28 RC R-HSA-383280:Nuclear Receptor transcription pathway TT6PEUO ID TT6PEUO TT6PEUO TN Retinoic acid receptor RXR-alpha (RXRA) TT6PEUO UP P19793 TT6PEUO UC RXRA_HUMAN TT6PEUO BC Nuclear hormone receptor TT6PEUO SN Retinoid X receptor alpha; RXRalpha; Nuclear receptor subfamily 2 group B member 1; NR2B1 TT6PEUO GN RXRA TT6PEUO FC Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes. Receptor for retinoic acid. TT6PEUO PD 6HN6; 6FBR; 6FBQ; 6A60; 6A5Z TT6PEUO SQ MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPINGMGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVPAHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT TT6PEUO TT Successful TT6PEUO FM Zinc-finger TT6PEUO KE hsa03320:PPAR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04976:Bile secretion; hsa05160:Hepatitis C; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05216:Thyroid cancer; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer TT6PEUO RC R-HSA-1368082:RORA activates gene expression; R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-159418:Recycling of bile acids and salts; R-HSA-1989781:PPARA activates gene expression; R-HSA-200425:Import of palmitoyl-CoA into the mitochondrial matrix; R-HSA-2032785:YAP1- and WWTR1 (TAZ)-stimulated gene expression; R-HSA-204174:Regulation of pyruvate dehydrogenase (PDH) complex; R-HSA-211976:Endogenous sterols; R-HSA-2151201:Transcriptional activation of mitochondrial biogenesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP); R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-383280:Nuclear Receptor transcription pathway; R-HSA-400206:Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha); R-HSA-400253:Circadian Clock TTL2ADK ID TTL2ADK TTL2ADK TN Rotamase A (PPIA) TTL2ADK UP P62937 TTL2ADK UC PPIA_HUMAN TTL2ADK BC Cis-trans-isomerases TTL2ADK SN PPIA; Cyclophilin A; CyPA TTL2ADK GN PPIA TTL2ADK FC Ppiases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. TTL2ADK EC EC 5.2.1.8 TTL2ADK PD 6GJY; 6GJR; 6GJP; 6GJN; 6GJM TTL2ADK SQ MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE TTL2ADK TT Successful TTL2ADK RC R-HSA-114608:Platelet degranulation; R-HSA-162585:Uncoating of the HIV Virion; R-HSA-162588:Budding and maturation of HIV virion; R-HSA-162592:Integration of provirus; R-HSA-162594:Early Phase of HIV Life Cycle; R-HSA-164516:Minus-strand DNA synthesis; R-HSA-164525:Plus-strand DNA synthesis; R-HSA-173107:Binding and entry of HIV virion; R-HSA-175474:Assembly Of The HIV Virion; R-HSA-180689:APOBEC3G mediated resistance to HIV-1 infection; R-HSA-210991:Basigin interactions TT6ZFQ4 ID TT6ZFQ4 TT6ZFQ4 TN Rotamase B (PPIB) TT6ZFQ4 UP P23284 TT6ZFQ4 UC PPIB_HUMAN TT6ZFQ4 BC Cis-trans-isomerase TT6ZFQ4 SN SCYLP; S-cyclophilin; Peptidyl-prolyl cis-trans isomerase B; PPIase B; Cyclophilin B; CYPB; CYP-S1 TT6ZFQ4 GN PPIB TT6ZFQ4 FC PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. TT6ZFQ4 EC EC 5.2.1.8 TT6ZFQ4 PD 3ICI; 3ICH; 1CYN TT6ZFQ4 SQ MLRLSERNMKVLLAAALIAGSVFFLLLPGPSAADEKKKGPKVTVKVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVIIADCGKIEVEKPFAIAKE TT6ZFQ4 TT Successful TT6ZFQ4 FM Cis-trans-isomerases TT6ZFQ4 RC R-HSA-1650814:Collagen biosynthesis and modifying enzymes TTFLH0E ID TTFLH0E TTFLH0E TN Serine/threonine PP1-alpha (PPP1CA) TTFLH0E UP P62136 TTFLH0E UC PP1A_HUMAN TTFLH0E BC Phosphoric monoester hydrolase TTFLH0E SN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit; Protein phosphatase 1alpha; PPP1A; PP-1A TTFLH0E GN PPP1CA TTFLH0E FC Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective. Dephosphorylates CENPA. Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy. Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. TTFLH0E EC EC 3.1.3.16 TTFLH0E PD 6GHM; 6G0J; 6G0I; 6DNO; 6DCX TTFLH0E SQ MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK TTFLH0E TT Successful TTFLH0E FM Phosphoric monoester hydrolases TTFNGC9 ID TTFNGC9 TTFNGC9 TN Serum albumin (ALB) TTFNGC9 UP P02768 TTFNGC9 UC ALBU_HUMAN TTFNGC9 SN Serum albumin TTFNGC9 GN ALB TTFNGC9 FC Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. TTFNGC9 PD 6JE7; 6EZQ; 6A7P; 5Z0B; 5YOQ TTFNGC9 SQ MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL TTFNGC9 TT Successful TTFNGC9 FM Serum albumin TTFNGC9 RC R-HSA-114608:Platelet degranulation; R-HSA-159418:Recycling of bile acids and salts; R-HSA-194223:HDL-mediated lipid transport; R-HSA-2168880:Scavenging of heme from plasma TTIND6G ID TTIND6G TTIND6G TN Somatostatin receptor type 1 (SSTR1) TTIND6G UP P30872 TTIND6G UC SSR1_HUMAN TTIND6G BC GPCR rhodopsin TTIND6G SN Sst(1); Somatostatin receptor 1; SSTR1; SS1R; SRIF-2 TTIND6G GN SSTR1 TTIND6G FC Receptor for somatostatin with higher affinity for somatostatin-14 than -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphataseand Na(+)/H(+) exchanger via pertussis toxin insensitive G proteins. TTIND6G SQ MFPNGTASSPSSSPSPSPGSCGEGGGSRGPGAGAADGMEEPGRNASQNGTLSEGQGSAILISFIYSVVCLVGLCGNSMVIYVILRYAKMKTATNIYILNLAIADELLMLSVPFLVTSTLLRHWPFGALLCRLVLSVDAVNMFTSIYCLTVLSVDRYVAVVHPIKAARYRRPTVAKVVNLGVWVLSLLVILPIVVFSRTAANSDGTVACNMLMPEPAQRWLVGFVLYTFLMGFLLPVGAICLCYVLIIAKMRMVALKAGWQQRKRSERKITLMVMMVVMVFVICWMPFYVVQLVNVFAEQDDATVSQLSVILGYANSCANPILYGFLSDNFKRSFQRILCLSWMDNAAEEPVDYYATALKSRAYSVEDFQPENLESGGVFRNGTCTSRITTL TTIND6G TT Successful TTIND6G KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTIND6G RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTZ6T9E ID TTZ6T9E TTZ6T9E TN Somatostatin receptor type 2 (SSTR2) TTZ6T9E UP P30874 TTZ6T9E UC SSR2_HUMAN TTZ6T9E BC GPCR rhodopsin TTZ6T9E SN Sst(2); Somatostatin receptor 2; SS2R; SS2-R; SS-2-R; SRIF-1 TTZ6T9E GN SSTR2 TTZ6T9E FC Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate in neuron development and maturation during brain development. Mediates negative regulation of insulin receptor signaling through PTPN6. Inactivates SSTR3 receptor function following heterodimerization. TTZ6T9E SQ MDMADEPLNGSHTWLSIPFDLNGSVVSTNTSNQTEPYYDLTSNAVLTFIYFVVCIIGLCGNTLVIYVILRYAKMKTITNIYILNLAIADELFMLGLPFLAMQVALVHWPFGKAICRVVMTVDGINQFTSIFCLTVMSIDRYLAVVHPIKSAKWRRPRTAKMITMAVWGVSLLVILPIMIYAGLRSNQWGRSSCTINWPGESGAWYTGFIIYTFILGFLVPLTIICLCYLFIIIKVKSSGIRVGSSKRKKSEKKVTRMVSIVVAVFIFCWLPFYIFNVSSVSMAISPTPALKGMFDFVVVLTYANSCANPILYAFLSDNFKKSFQNVLCLVKVSGTDDGERSDSKQDKSRLNETTETQRTLLNGDLQTSI TTZ6T9E TT Successful TTZ6T9E FM GPCR rhodopsin TTZ6T9E KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04971:Gastric acid secretion TTZ6T9E RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTJX3UE ID TTJX3UE TTJX3UE TN Somatostatin receptor type 3 (SSTR3) TTJX3UE UP P32745 TTJX3UE UC SSR3_HUMAN TTJX3UE BC GPCR rhodopsin TTJX3UE SN SSTR3; SSR-28; SS3R TTJX3UE GN SSTR3 TTJX3UE FC Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. TTJX3UE SQ MDMLHPSSVSTTSEPENASSAWPPDATLGNVSAGPSPAGLAVSGVLIPLVYLVVCVVGLLGNSLVIYVVLRHTASPSVTNVYILNLALADELFMLGLPFLAAQNALSYWPFGSLMCRLVMAVDGINQFTSIFCLTVMSVDRYLAVVHPTRSARWRTAPVARTVSAAVWVASAVVVLPVVVFSGVPRGMSTCHMQWPEPAAAWRAGFIIYTAALGFFGPLLVICLCYLLIVVKVRSAGRRVWAPSCQRRRRSERRVTRMVVAVVALFVLCWMPFYVLNIVNVVCPLPEEPAFFGLYFLVVALPYANSCANPILYGFLSYRFKQGFRRVLLRPSRRVRSQEPTVGPPEKTEEEDEEEEDGEESREGGKGKEMNGRVSQITQPGTSGQERPPSRVASKEQQLLPQEASTGEKSSTMRISYL TTJX3UE TT Successful TTJX3UE KE hsa04080:Neuroactive ligand-receptor interaction TTJX3UE RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TT2BC4G ID TT2BC4G TT2BC4G TN Somatostatin receptor type 5 (SSTR5) TT2BC4G UP P35346 TT2BC4G UC SSR5_HUMAN TT2BC4G BC GPCR rhodopsin TT2BC4G SN Somatostatin receptor 5; SSTR5; SS5R TT2BC4G GN SSTR5 TT2BC4G FC Receptor for somatostatin 28 and to a lesser extent for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Increases cell growth inhibition activity of SSTR2 following heterodimerization. TT2BC4G SQ MEPLFPASTPSWNASSPGAASGGGDNRTLVGPAPSAGARAVLVPVLYLLVCAAGLGGNTLVIYVVLRFAKMKTVTNIYILNLAVADVLYMLGLPFLATQNAASFWPFGPVLCRLVMTLDGVNQFTSVFCLTVMSVDRYLAVVHPLSSARWRRPRVAKLASAAAWVLSLCMSLPLLVFADVQEGGTCNASWPEPVGLWGAVFIIYTAVLGFFAPLLVICLCYLLIVVKVRAAGVRVGCVRRRSERKVTRMVLVVVLVFAGCWLPFFTVNIVNLAVALPQEPASAGLYFFVVILSYANSCANPVLYGFLSDNFRQSFQKVLCLRKGSGAKDADATEPRPDRIRQQQEATPPAHRAAANGLMQTSKL TT2BC4G TT Successful TT2BC4G KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TT2BC4G RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTHI19T ID TTHI19T TTHI19T TN Staphylococcus Beta-lactamase (Stap-coc blaZ) TTHI19T UP P00807 TTHI19T UC BLAC_STAAU TTHI19T BC Carbon-nitrogen hydrolase TTHI19T SN blaZ; Cephalosporinase TTHI19T GN Stap-coc blaZ TTHI19T FC This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. TTHI19T EC EC 3.5.2.6 TTHI19T PD 3BLM; 1PIO; 1OME; 1KGG; 1KGF TTHI19T SQ MKKLIFLIVIALVLSACNSNSSHAKELNDLEKKYNAHIGVYALDTKSGKEVKFNSDKRFAYASTSKAINSAILLEQVPYNKLNKKVHINKDDIVAYSPILEKYVGKDITLKALIEASMTYSDNTANNKIIKEIGGIKKVKQRLKELGDKVTNPVRYEIELNYYSPKSKKDTSTPAAFGKTLNKLIANGKLSKENKKFLLDLMLNNKSGDTLIKDGVPKDYKVADKSGQAITYASRNDVAFVYPKGQSEPIVLVIFTNKDNKSDKPNDKLISETAKSVMKEF TTHI19T TT Successful TTT02K8 ID TTT02K8 TTT02K8 TN Steroid 5-alpha-reductase 2 (SRD5A2) TTT02K8 UP P31213 TTT02K8 UC S5A2_HUMAN TTT02K8 BC CH-CH donor oxidoreductase TTT02K8 SN Type 2 steroid 5alpha-reductase (5alpha-R); SRD5A2; SR type 2; 5-alpha reductase 2; 5 alpha-SR2 TTT02K8 GN SRD5A2 TTT02K8 FC Converts testosterone (T) into 5-alpha- dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology. TTT02K8 EC EC 1.3.1.22 TTT02K8 SQ MQVQCQQSPVLAGSATLVALGALALYVAKPSGYGKHTESLKPAATRLPARAAWFLQELPSFAVPAGILARQPLSLFGPPGTVLLGLFCVHYFHRTFVYSLLNRGRPYPAILILRGTAFCTGNGVLQGYYLIYCAEYPDGWYTDIRFSLGVFLFILGMGINIHSDYILRQLRKPGEISYRIPQGGLFTYVSGANFLGEIIEWIGYALATWSLPALAFAFFSLCFLGLRAFHHHRFYLKMFEDYPKSRKALIPFIF TTT02K8 TT Successful TTT02K8 KE hsa00140:Steroid hormone biosynthesis; hsa05215:Prostate cancer TTT02K8 RC R-HSA-193048:Androgen biosynthesis TTF45NW ID TTF45NW TTF45NW TN Strychnine-binding glycine receptor (GLRA1) TTF45NW UP P23415 TTF45NW UC GLRA1_HUMAN TTF45NW BC Neurotransmitter receptor TTF45NW SN Strychnine-insensitive glycine receptor; Strychnine binding subunit; Glycine receptor 48 kDa subunit; GLRA1 TTF45NW GN GLRA1 TTF45NW FC The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing). TTF45NW PD 4X5T; 2M6I; 2M6B; 1VRY; 1MOT TTF45NW SQ MYSFNTLRLYLWETIVFFSLAASKEAEAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDSIWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLFQEDEAGEGRFNFSAYGMGPACLQAKDGISVKGANNSNTTNPPPAPSKSPEEMRKLFIQRAKKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNQ TTF45NW TT Successful TTF45NW KE hsa04080:Neuroactive ligand-receptor interaction TTF45NW RC R-HSA-975298:Ligand-gated ion channel transport TTNZRI3 ID TTNZRI3 TTNZRI3 TN Synaptic vesicle amine transporter (SLC18A2) TTNZRI3 UP Q05940 TTNZRI3 UC VMAT2_HUMAN TTNZRI3 BC Major facilitator superfamily TTNZRI3 SN Vesicular amine transporter; Vesicular Monoamine Transporter; VMAT; VAT; Solute carrier family 18 member 2; SLC18A2; Monoamine transporter TTNZRI3 GN SLC18A2 TTNZRI3 FC Involved in the ATP-dependent vesicular transport of biogenic amine neurotransmitters. Pumps cytosolic monoamines including dopamine, norepinephrine, serotonin, and histamine into synaptic vesicles. Requisite for vesicular amine storage prior to secretion via exocytosis. TTNZRI3 SQ MALSELALVRWLQESRRSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNATEIQTARPVHTASISDSFQSIFSYYDNSTMVTGNATRDLTLHQTATQHMVTNASAVPSDCPSEDKDLLNENVQVGLLFASKATVQLITNPFIGLLTNRIGYPIPIFAGFCIMFVSTIMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGNVMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPIWMMETMCSRKWQLGVAFLPASISYLIGTNIFGILAHKMGRWLCALLGMIIVGVSILCIPFAKNIYGLIAPNFGVGFAIGMVDSSMMPIMGYLVDLRHVSVYGSVYAIADVAFCMGYAIGPSAGGAIAKAIGFPWLMTIIGIIDILFAPLCFFLRSPPAKEEKMAILMDHNCPIKTKMYTQNNIQSYPIGEDEESESD TTNZRI3 TT Successful TTNZRI3 KE hsa04721:Synaptic vesicle cycle; hsa04726:Serotonergic synapse; hsa04728:Dopaminergic synapse; hsa05012:Parkinson's disease; hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05034:Alcoholism TTNZRI3 RC R-HSA-181430:Norepinephrine Neurotransmitter Release Cycle; R-HSA-442660:Na+/Cl- dependent neurotransmitter transporters TTBGTFN ID TTBGTFN TTBGTFN TN T-cell surface glycoprotein CD1a (CD1A) TTBGTFN UP P06126 TTBGTFN UC CD1A_HUMAN TTBGTFN BC Immunoglobulin TTBGTFN SN hTa1 thymocyteantigen; hTa1 thymocyte antigen; T-cell surfaceantigen T6/Leu-6; T-cell surface antigen T6/Leu-6; CD1a TTBGTFN GN CD1A TTBGTFN FC Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. TTBGTFN PD 5J1A; 4X6F; 4X6E; 4X6D; 4X6C TTBGTFN SQ MLFLLLPLLAVLPGDGNADGLKEPLSFHVTWIASFYNHSWKQNLVSGWLSDLQTHTWDSNSSTIVFLCPWSRGNFSNEEWKELETLFRIRTIRSFEGIRRYAHELQFEYPFEIQVTGGCELHSGKVSGSFLQLAYQGSDFVSFQNNSWLPYPVAGNMAKHFCKVLNQNQHENDITHNLLSDTCPRFILGLLDAGKAHLQRQVKPEAWLSHGPSPGPGHLQLVCHVSGFYPKPVWVMWMRGEQEQQGTQRGDILPSADGTWYLRATLEVAAGEAADLSCRVKHSSLEGQDIVLYWEHHSSVGFIILAVIVPLLLLIGLALWFRKRCFC TTBGTFN TT Successful TTBGTFN KE hsa04640:Hematopoietic cell lineage TTZAT79 ID TTZAT79 TTZAT79 TN T-cell surface glycoprotein CD3 epsilon (CD3E) TTZAT79 UP P07766 TTZAT79 UC CD3E_HUMAN TTZAT79 SN T3E; T-cell surface glycoprotein CD3 epsilon chain; T-cell surface antigen T3/Leu-4 epsilon chain; CD3e TTZAT79 GN CD3E TTZAT79 FC When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition of this role of signal transduction in T-cell activation, CD3E plays an essential role in correct T-cell development. Initiates the TCR-CD3 complex assembly by forming the two heterodimers CD3D/CD3E and CD3G/CD3E. Participates also in internalization and cell surface down-regulation of TCR-CD3 complexes via endocytosis sequences present in CD3E cytosolic region. Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. TTZAT79 PD 2ROL; 1XIW; 1SY6; 1A81 TTZAT79 SQ MQSGTHWRVLGLCLLSVGVWGQDGNEEMGGITQTPYKVSISGTTVILTCPQYPGSEILWQHNDKNIGGDEDDKNIGSDEDHLSLKEFSELEQSGYYVCYPRGSKPEDANFYLYLRARVCENCMEMDVMSVATIVIVDICITGGLLLLVYYWSKNRKAKAKPVTRGAGAGGRQRGQNKERPPPVPNPDYEPIRKGQRDLYSGLNQRRI TTZAT79 TT Successful TTZAT79 KE hsa04640:Hematopoietic cell lineage; hsa04660:T cell receptor signaling pathway; hsa05142:Chagas disease (American trypanosomiasis); hsa05162:Measles; hsa05166:HTLV-I infection; hsa05340:Primary immunodeficiency TTZAT79 RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202427:Phosphorylation of CD3 and TCR zeta chains; R-HSA-202430:Translocation of ZAP-70 to Immunological synapse; R-HSA-202433:Generation of second messenger molecules; R-HSA-389948:PD-1 signaling TTIHYA4 ID TTIHYA4 TTIHYA4 TN Thrombopoietin receptor (MPL) TTIHYA4 UP P40238 TTIHYA4 UC TPOR_HUMAN TTIHYA4 BC Cytokine receptor TTIHYA4 SN TPOR; TPO-R; Proto-oncogene c-Mpl; Myeloproliferative leukemia protein; CD110 antigen; CD110; C-mpl TTIHYA4 GN MPL TTIHYA4 FC May represent a regulatory molecule specific for TPO-R-dependent immune responses. Receptor for thrombopoietin that acts as a primary regulator of megakaryopoiesis and platelet production. TTIHYA4 SQ MPSWALFMVTSCLLLAPQNLAQVSSQDVSLLASDSEPLKCFSRTFEDLTCFWDEEEAAPSGTYQLLYAYPREKPRACPLSSQSMPHFGTRYVCQFPDQEEVRLFFPLHLWVKNVFLNQTRTQRVLFVDSVGLPAPPSIIKAMGGSQPGELQISWEEPAPEISDFLRYELRYGPRDPKNSTGPTVIQLIATETCCPALQRPHSASALDQSPCAQPTMPWQDGPKQTSPSREASALTAEGGSCLISGLQPGNSYWLQLRSEPDGISLGGSWGSWSLPVTVDLPGDAVALGLQCFTLDLKNVTCQWQQQDHASSQGFFYHSRARCCPRDRYPIWENCEEEEKTNPGLQTPQFSRCHFKSRNDSIIHILVEVTTAPGTVHSYLGSPFWIHQAVRLPTPNLHWREISSGHLELEWQHPSSWAAQETCYQLRYTGEGHQDWKVLEPPLGARGGTLELRPRSRYRLQLRARLNGPTYQGPWSSWSDPTRVETATETAWISLVTALHLVLGLSAVLGLLLLRWQFPAHYRRLRHALWPSLPDLHRVLGQYLRDTAALSPPKATVSDTCEEVEPSLLEILPKSSERTPLPLCSSQAQMDYRRLQPSCLGTMPLSVCPPMAESGSCCTTHIANHSYLPLSYWQQP TTIHYA4 TT Successful TTIHYA4 FM Cytokine receptor TTIHYA4 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway TTTSEPU ID TTTSEPU TTTSEPU TN Thyroid hormone receptor alpha (THRA) TTTSEPU UP P10827 TTTSEPU UC THA_HUMAN TTTSEPU BC Nuclear hormone receptor TTTSEPU SN V-erbA-related protein 7; THRA2; THRA1; Nuclear receptor subfamily 1 group A member 1; NR1A1; ERBA1; EAR7; EAR-7; C-erbA-alpha; C-erbA-1 TTTSEPU GN THRA TTTSEPU FC High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. Isoform Alpha-1: Nuclear hormone receptor that can act as a repressor or activator of transcription. TTTSEPU PD 4LNX; 4LNW; 3JZB; 3ILZ; 3HZF TTTSEPU SQ MEQKPSKVECGSDPEENSARSPDGKRKRKNGQCSLKTSMSGYIPSYLDKDEQCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPTYSCKYDSCCVIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEQNRERRRKEEMIRSLQQRPEPTPEEWDLIHIATEAHRSTNAQGSHWKQRRKFLPDDIGQSPIVSMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESDTLTLSGEMAVKREQLKNGGLGVVSDAIFELGKSLSAFNLDDTEVALLQAVLLMSTDRSGLLCVDKIEKSQEAYLLAFEHYVNHRKHNIPHFWPKLLMKEREVQSSILYKGAAAEGRPGGSLGVHPEGQQLLGMHVVQGPQVRQLEQQLGEAGSLQGPVLQHQSPKSPQQRLLELLHRSGILHARAVCGEDDSSEADSPSSSEEEPEVCEDLAGNAASP TTTSEPU TT Successful TTTSEPU FM Nuclear hormone receptor family TTTSEPU KE hsa04080:Neuroactive ligand-receptor interaction; hsa04919:Thyroid hormone signaling pathway TTTSEPU RC R-HSA-383280:Nuclear Receptor transcription pathway TTGER3L ID TTGER3L TTGER3L TN Thyroid hormone receptor beta (THRB) TTGER3L UP P10828 TTGER3L UC THB_HUMAN TTGER3L BC Nuclear hormone receptor TTGER3L SN c-erbA-beta; c-erbA-2; THR1; Nuclear receptor subfamily 1 group A member 2; NR1A2; ERBA2 TTGER3L GN THRB TTGER3L FC High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. Nuclear hormone receptor that can act as a repressor or activator of transcription. TTGER3L PD 4ZO1; 3JZC; 3IMY; 3GWS; 3D57 TTGER3L SQ MTPNSMTENGLTAWDKPKHCPDREHDWKLVGMSEACLHRKSHSERRSTLKNEQSSPHLIQTTWTSSIFHLDHDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYEGKCVIDKVTRNQCQECRFKKCIYVGMATDLVLDDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSLSSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKYQDSFLLAFEHYINYRKHHVTHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED TTGER3L TT Successful TTGER3L FM Nuclear hormone receptor family TTGER3L KE hsa04080:Neuroactive ligand-receptor interaction; hsa04919:Thyroid hormone signaling pathway TTGER3L RC R-HSA-383280:Nuclear Receptor transcription pathway TT6NYJA ID TT6NYJA TT6NYJA TN Thyrotropin receptor (TSHR) TT6NYJA UP P16473 TT6NYJA UC TSHR_HUMAN TT6NYJA BC GPCR rhodopsin TT6NYJA SN Thyroid stimulating hormone receptor; TSHR; TSH-R; TSH receptor TT6NYJA GN TSHR TT6NYJA FC Receptor for thyrothropin. Plays a central role in controlling thyroid cell metabolism. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Also acts as a receptor for thyrostimulin (gpa2+gpb5). TT6NYJA PD 3G04; 2XWT; 1XUM TT6NYJA SQ MRPADLLQLVLLLDLPRDLGGMGCSSPPCECHQEEDFRVTCKDIQRIPSLPPSTQTLKLIETHLRTIPSHAFSNLPNISRIYVSIDVTLQQLESHSFYNLSKVTHIEIRNTRNLTYIDPDALKELPLLKFLGIFNTGLKMFPDLTKVYSTDIFFILEITDNPYMTSIPVNAFQGLCNETLTLKLYNNGFTSVQGYAFNGTKLDAVYLNKNKYLTVIDKDAFGGVYSGPSLLDVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSMQSLRQRKSVNALNSPLHQEYEENLGDSIVGYKEKSKFQDTHNNAHYYVFFEEQEDEIIGFGQELKNPQEETLQAFDSHYDYTICGDSEDMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSLLALLGNVFVLLILLTSHYKLNVPRFLMCNLAFADFCMGMYLLLIASVDLYTHSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHACAIMVGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIVFVLTLNIVAFVIVCCCYVKIYITVRNPQYNPGDKDTKIAKRMAVLIFTDFICMAPISFYALSAILNKPLITVSNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGICKRQAQAYRGQRVPPKNSTDIQVQKVTHDMRQGLHNMEDVYELIENSHLTPKKQGQISEEYMQTVL TT6NYJA TT Successful TT6NYJA KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04918:Thyroid hormone synthesis; hsa05320:Autoimmune thyroid disease TT6NYJA RC R-HSA-375281:Hormone ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events TTRJ1K4 ID TTRJ1K4 TTRJ1K4 TN Toll-like receptor 7 (TLR7) TTRJ1K4 UP Q9NYK1 TTRJ1K4 UC TLR7_HUMAN TTRJ1K4 BC Toll-like receptor TTRJ1K4 SN Toll-like receptor 7 TTRJ1K4 GN TLR7 TTRJ1K4 FC Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR7 is a nucleotide-sensing TLR which is activated by single-stranded RNA. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). TTRJ1K4 SQ MVFPMWTLKRQILILFNIILISKLLGARWFPKTLPCDVTLDVPKNHVIVDCTDKHLTEIPGGIPTNTTNLTLTINHIPDISPASFHRLDHLVEIDFRCNCVPIPLGSKNNMCIKRLQIKPRSFSGLTYLKSLYLDGNQLLEIPQGLPPSLQLLSLEANNIFSIRKENLTELANIEILYLGQNCYYRNPCYVSYSIEKDAFLNLTKLKVLSLKDNNVTAVPTVLPSTLTELYLYNNMIAKIQEDDFNNLNQLQILDLSGNCPRCYNAPFPCAPCKNNSPLQIPVNAFDALTELKVLRLHSNSLQHVPPRWFKNINKLQELDLSQNFLAKEIGDAKFLHFLPSLIQLDLSFNFELQVYRASMNLSQAFSSLKSLKILRIRGYVFKELKSFNLSPLHNLQNLEVLDLGTNFIKIANLSMFKQFKRLKVIDLSVNKISPSGDSSEVGFCSNARTSVESYEPQVLEQLHYFRYDKYARSCRFKNKEASFMSVNESCYKYGQTLDLSKNSIFFVKSSDFQHLSFLKCLNLSGNLISQTLNGSEFQPLAELRYLDFSNNRLDLLHSTAFEELHKLEVLDISSNSHYFQSEGITHMLNFTKNLKVLQKLMMNDNDISSSTSRTMESESLRTLEFRGNHLDVLWREGDNRYLQLFKNLLKLEELDISKNSLSFLPSGVFDGMPPNLKNLSLAKNGLKSFSWKKLQCLKNLETLDLSHNQLTTVPERLSNCSRSLKNLILKNNQIRSLTKYFLQDAFQLRYLDLSSNKIQMIQKTSFPENVLNNLKMLLLHHNRFLCTCDAVWFVWWVNHTEVTIPYLATDVTCVGPGAHKGQSVISLDLYTCELDLTNLILFSLSISVSLFLMVMMTASHLYFWDVWYIYHFCKAKIKGYQRLISPDCCYDAFIVYDTKDPAVTEWVLAELVAKLEDPREKHFNLCLEERDWLPGQPVLENLSQSIQLSKKTVFVMTDKYAKTENFKIAFYLSHQRLMDEKVDVIILIFLEKPFQKSKFLQLRKRLCGSSVLEWPTNPQAHPYFWQCLKNALATDNHVAYSQVFKETV TTRJ1K4 TT Successful TTRJ1K4 FM Toll like receptor TTRJ1K4 KE hsa04620:Toll-like receptor signaling pathway; hsa05162:Measles; hsa05164:Influenza A TTRJ1K4 RC R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-975110:TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling; R-HSA-975138:TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation; R-HSA-975155:MyD88 dependent cascade initiated on endosome TTELV3W ID TTELV3W TTELV3W TN Transformation-sensitive protein p120 (TRPA1) TTELV3W UP O75762 TTELV3W UC TRPA1_HUMAN TTELV3W BC Transient receptor potential catioin channel TTELV3W SN TRPA1; Ankyrin-like with transmembrane domains protein 1; ANKTM1 TTELV3W GN TRPA1 TTELV3W FC Receptor-activated non-selective cation channel involved in detection of pain and possibly also in cold perception and inner ear function. Has a central role in the pain response to endogenous inflammatory mediators and to a diverse array of volatile irritants, such as mustard oil, garlic and acrolein, an irritant from tears gas and vehicule exhaust fumes. Acts also as a ionotropic cannabinoid receptor by being activated by delta(9)- tetrahydrocannabinol (THC), the psychoactive component of marijuana. Not involved in menthol sensation. May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds. Probably operated by a phosphatidylinositol second messenger system. TTELV3W PD 3J9P TTELV3W SQ MKRSLRKMWRPGEKKEPQGVVYEDVPDDTEDFKESLKVVFEGSAYGLQNFNKQKKLKRCDDMDTFFLHYAAAEGQIELMEKITRDSSLEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEHGYSRQLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSYSGSVDIVNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGHAKAVALLLSHNADIVLNKQQASFLHLALHNKRKEVVLTIIRSKRWDECLKIFSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHSTEDKSCRDYYIEYNFKYLQCPLEFTKKTPTQDVIYEPLTALNAMVQNNRIELLNHPVCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIKPGMAFNSTGIINETSDHSEILDTTNSYLIKTCMILVFLSSIFGYCKEAGQIFQQKRNYFMDISNVLEWIIYTTGIIFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQRFENCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNLQDPFSSPLLSIIQTFSMMLGDINYRESFLEPYLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLAVGDIAEVQKHASLKRIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYPNKPRSGGMLFHIFCFLFCTGEIRQEIPNADKSLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISETEDDDSHCSFQDRFKKEQMEQRNSRWNTVLRAVKAKTHHLEP TTELV3W TT Successful TTELV3W KE hsa04750:Inflammatory mediator regulation of TRP channels TTELV3W RC R-HSA-3295583:TRP channels TTR9XHZ ID TTR9XHZ TTR9XHZ TN Transforming growth factor beta 1 (TGFB1) TTR9XHZ UP P01137 TTR9XHZ UC TGFB1_HUMAN TTR9XHZ BC Growth factor TTR9XHZ SN Transforming growth factor beta-1 proprotein; Transforming growth factor beta-1; TGFB; TGF-beta1; TGF-beta 1 TTR9XHZ GN TGFB1 TTR9XHZ FC Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. TTR9XHZ PD 5VQP; 5FFO; 4KV5; 3KFD; 1KLD TTR9XHZ SQ MPPSGLRLLLLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS TTR9XHZ TT Successful TTR9XHZ FM Growth factor TTR9XHZ KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04144:Endocytosis; hsa04350:TGF-beta signaling pathway; hsa04380:Osteoclast differentiation; hsa04390:Hippo signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05220:Chronic myeloid leukemia; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05414:Dilated cardiomyopathy TTR9XHZ RC R-HSA-114608:Platelet degranulation; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-2173789:TGF-beta receptor signaling activates SMADs; R-HSA-2173791:TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition); R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-3304356:SMAD2/3 Phosphorylation Motif Mutants in Cancer; R-HSA-3315487:SMAD2/3 MH2 Domain Mutants in Cancer; R-HSA-3645790:TGFBR2 Kinase Domain Mutants in Cancer; R-HSA-3656532:TGFBR1 KD Mutants in Cancer; R-HSA-3656535:TGFBR1 LBD Mutants in Cancer; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation TTMI6F5 ID TTMI6F5 TTMI6F5 TN Transient receptor potential cation channel V1 (TRPV1) TTMI6F5 UP Q8NER1 TTMI6F5 UC TRPV1_HUMAN TTMI6F5 BC Transient receptor potential catioin channel TTMI6F5 SN Vanilloid receptor 1; VR1; TrpV1; Transient receptor potential cation channel subfamily V member 1; Osm-9-like TRP channel 1; OTRPC1; Capsaicin receptor TTMI6F5 GN TRPV1 TTMI6F5 FC Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis. TTMI6F5 SQ MKKWSSTDLGAAADPLQKDTCPDPLDGDPNSRPPPAKPQLSTAKSRTRLFGKGDSEEAFPVDCPHEEGELDSCPTITVSPVITIQRPGDGPTGARLLSQDSVAASTEKTLRLYDRRSIFEAVAQNNCQDLESLLLFLQKSKKHLTDNEFKDPETGKTCLLKAMLNLHDGQNTTIPLLLEIARQTDSLKELVNASYTDSYYKGQTALHIAIERRNMALVTLLVENGADVQAAAHGDFFKKTKGRPGFYFGELPLSLAACTNQLGIVKFLLQNSWQTADISARDSVGNTVLHALVEVADNTADNTKFVTSMYNEILMLGAKLHPTLKLEELTNKKGMTPLALAAGTGKIGVLAYILQREIQEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFLVYCLYMIIFTMAAYYRPVDGLPPFKMEKTGDYFRVTGEILSVLGGVYFFFRGIQYFLQRRPSMKTLFVDSYSEMLFFLQSLFMLATVVLYFSHLKEYVASMVFSLALGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYIVFLFGFSTAVVTLIEDGKNDSLPSESTSHRWRGPACRPPDSSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGYTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSSRVSGRHWKNFALVPLLREASARDRQSAQPEEVYLRQFSGSLKPEDAEVFKSPAASGEK TTMI6F5 TT Successful TTMI6F5 FM Transient receptor family TTMI6F5 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04750:Inflammatory mediator regulation of TRP channels TTMI6F5 RC R-HSA-3295583:TRP channels TTEAID7 ID TTEAID7 TTEAID7 TN Trypanosoma Cruzipain (Trypano CYSP) TTEAID7 UP P25779 TTEAID7 UC CYSP_TRYCR TTEAID7 BC Peptidase TTEAID7 SN Cruzaine; Major cysteine proteinase TTEAID7 GN Trypano CYSP TTEAID7 FC The cysteine protease may play an important role in the development and differentiation of the parasites at several stages of their life cycle. TTEAID7 EC EC 3.4.22.51 TTEAID7 PD 4XUI; 4W5C; 4W5B; 4QH6; 4PI3 TTEAID7 SQ MSGWARALLLAAVLVVMACLVPAATASLHAEETLTSQFAEFKQKHGRVYESAAEEAFRLSVFRENLFLARLHAAANPHATFGVTPFSDLTREEFRSRYHNGAAHFAAAQERARVPVKVEVVGAPAAVDWRARGAVTAVKDQGQCGSCWAFSAIGNVECQWFLAGHPLTNLSEQMLVSCDKTDSGCSGGLMNNAFEWIVQENNGAVYTEDSYPYASGEGISPPCTTSGHTVGATITGHVELPQDEAQIAAWLAVNGPVAVAVDASSWMTYTGGVMTSCVSEQLDHGVLLVGYNDSAAVPYWIIKNSWTTQWGEEGYIRIAKGSNQCLVKEEASSAVVGGPGPTPEPTTTTTTSAPGPSPSYFVQMSCTDAACIVGCENVTLPTGQCLLTTSGVSAIVTCGAETLTEEVFLTSTHCSGPSVRSSVPLNKCNRLLRGSVEFFCGSSSSGRLADVDRQRRHQPYHSRHRRL TTEAID7 TT Successful TTRTKPV ID TTRTKPV TTRTKPV TN Trypanosoma Trypanothione reductase (Trypano TPR) TTRTKPV UP P39051 TTRTKPV UC TYTR_TRYBB TTRTKPV BC Sulfur donor oxidoreductase TTRTKPV SN TRYR; TPR; Parasite-specific trypanothione reductase; N(1),N(8)-bis(glutathionyl)spermidine reductase TTRTKPV GN Trypano TPR TTRTKPV FC Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase. TTRTKPV EC EC 1.8.1.12 TTRTKPV PD 2WBA TTRTKPV SQ MSKIFDLVVIGAGSGGLEAGWNAATLYKKRVAVIDVQTHHGPPHYAALGGTCVNVGCVPKKLMVTGAQYMDHLRESAGFGWEFDGSSVKANWKKLIAAKNEAVLDINKSYEGMFNDTEGLDFFLGWGSLESKNVVVVRETADPKSAVKERLQADHILLATGSWPQMPAIPGVEHCISSNEAFYLPEPPRRVLTVGGGFISVEFAGIFNAYKPPGGKVTLCYRNNLILRGFDETIREEVTKQLTANGIEIMTNENPAKVSLNTDGSKHVTFESGKTLDVDVVMMAIGRIPRTNDLQLGNVGVKLTPKGGVQVDEFSRTNVPNIYAIGDITDRLMLTPVAINEGAALVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLIEEVAAKEFEKVAVYMSSFTPLMHNISGSKYKKFVAKIVTNHSDGTVLGVHLLGDGAPEIIQAVGVCLRLNAKISDFYNTIGVHPTSAEELCSMRTPSYYYLKGEKMETLPESSL TTRTKPV TT Successful TTOHSBA ID TTOHSBA TTOHSBA TN Vascular endothelial growth factor A (VEGFA) TTOHSBA UP P15692 TTOHSBA UC VEGFA_HUMAN TTOHSBA BC Growth factor TTOHSBA SN Vascular permeability factor; VPF; VEGF-A; VEGF TTOHSBA GN VEGFA TTOHSBA FC Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development. Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. TTOHSBA PD 6D3O; 6BFT; 5T89; 5O4E; 5HHD TTOHSBA SQ MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPHPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR TTOHSBA TT Successful TTOHSBA FM Growth factor TTOHSBA KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04370:VEGF signaling pathway; hsa04510:Focal adhesion; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05219:Bladder cancer; hsa05323:Rheumatoid arthritis TTOHSBA RC R-HSA-114608:Platelet degranulation; R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-194313:VEGF ligand-receptor interactions; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization TTPJQHE ID TTPJQHE TTPJQHE TN Vascular endothelial growth factor B (VEGFB) TTPJQHE UP P49765 TTPJQHE UC VEGFB_HUMAN TTPJQHE BC Growth factor TTPJQHE SN VRF; VEGF-related factor; VEGF-B TTPJQHE GN VEGFB TTPJQHE FC VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis. Growth factor for endothelial cells. TTPJQHE PD 2XAC; 2VWE; 2C7W TTPJQHE SQ MSPLLRRLLLAALLQLAPAQAPVSQPDAPGHQRKVVSWIDVYTRATCQPREVVVPLTVELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIRYPSSQLGEMSLEEHSQCECRPKKKDSAVKPDRAATPHHRPQPRSVPGWDSAPGAPSPADITHPTPAPGPSAHAAPSTTSALTPGPAAAAADAAASSVAKGGA TTPJQHE TT Successful TTPJQHE FM Growth factor TTPJQHE KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa05200:Pathways in cancer TTPJQHE RC R-HSA-114608:Platelet degranulation; R-HSA-194313:VEGF ligand-receptor interactions; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization TTL9MHW ID TTL9MHW TTL9MHW TN Vasopressin V1b receptor (V1BR) TTL9MHW UP P47901 TTL9MHW UC V1BR_HUMAN TTL9MHW BC GPCR rhodopsin TTL9MHW SN Vasopressin V3 receptor; Vasopressin V(1b) Receptor; VPR3; V1bR; Antidiuretic hormone receptor 1b; AVPR3; AVPR V3; AVPR V1b TTL9MHW GN AVPR1B TTL9MHW FC The activity of this receptor is mediated by G proteins which activate a phosphatidyl-inositol-calcium second messenger system. Receptor for arginine vasopressin. TTL9MHW SQ MDSGPLWDANPTPRGTLSAPNATTPWLGRDEELAKVEIGVLATVLVLATGGNLAVLLTLGQLGRKRSRMHLFVLHLALTDLAVALFQVLPQLLWDITYRFQGPDLLCRAVKYLQVLSMFASTYMLLAMTLDRYLAVCHPLRSLQQPGQSTYLLIAAPWLLAAIFSLPQVFIFSLREVIQGSGVLDCWADFGFPWGPRAYLTWTTLAIFVLPVTMLTACYSLICHEICKNLKVKTQAWRVGGGGWRTWDRPSPSTLAATTRGLPSRVSSINTISRAKIRTVKMTFVIVLAYIACWAPFFSVQMWSVWDKNAPDEDSTNVAFTISMLLGNLNSCCNPWIYMGFNSHLLPRPLRHLACCGGPQPRMRRRLSDGSLSSRHTTLLTRSSCPATLSLSLSLTLSGRPRPEESPRDLELADGEGTAETIIF TTL9MHW TT Successful TTL9MHW KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction TTL9MHW RC R-HSA-388479:Vasopressin-like receptors; R-HSA-416476:G alpha (q) signalling events TTK8R02 ID TTK8R02 TTK8R02 TN Vasopressin V2 receptor (V2R) TTK8R02 UP P30518 TTK8R02 UC V2R_HUMAN TTK8R02 BC GPCR rhodopsin TTK8R02 SN Renal-type arginine vasopressin receptor; DIR3; DIR; Antidiuretic hormone receptor; AVPR V2; ADHR TTK8R02 GN AVPR2 TTK8R02 FC The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Involved in renal water reabsorption. Receptor for arginine vasopressin. TTK8R02 PD 4JQI TTK8R02 SQ MLMASTTSAVPGHPSLPSLPSNSSQERPLDTRDPLLARAELALLSIVFVAVALSNGLVLAALARRGRRGHWAPIHVFIGHLCLADLAVALFQVLPQLAWKATDRFRGPDALCRAVKYLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGSGAHWNRPVLVAWAFSLLLSLPQLFIFAQRNVEGGSGVTDCWACFAEPWGRRTYVTWIALMVFVAPTLGIAACQVLIFREIHASLVPGPSERPGGRRRGRRTGSPGEGAHVSAAVAKTVRMTLVIVVVYVLCWAPFFLVQLWAAWDPEAPLEGAPFVLLMLLASLNSCTNPWIYASFSSSVSSELRSLLCCARGRTPPSLGPQDESCTTASSSLAKDTSS TTK8R02 TT Successful TTK8R02 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04962:Vasopressin-regulated water reabsorption TTK8R02 RC R-HSA-388479:Vasopressin-like receptors; R-HSA-418555:G alpha (s) signalling events; R-HSA-432040:Vasopressin regulates renal water homeostasis via Aquaporins TTZIFHC ID TTZIFHC TTZIFHC TN Voltage-gated calcium channel alpha Cav1.2 (CACNA1C) TTZIFHC UP Q13936 TTZIFHC UC CAC1C_HUMAN TTZIFHC BC Voltage-gated ion channel TTZIFHC SN Voltage-gated calcium channel subunit alpha Cav1.2; Voltage-dependent L-type calcium channel subunit alpha-1C; Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle; CCHL1A1; CACNL1A1; CACN2; CACH2 TTZIFHC GN CACNA1C TTZIFHC FC Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm. Plays an important role in excitation-contraction coupling in the heart. Required for normal heart development and normal regulation of heart rhythm. Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. TTZIFHC PD 6DAF; 6DAE; 6DAD; 6C0A; 5V2Q TTZIFHC SQ MVNENTRMYIPEENHQGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWQAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGSTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGIADVPAEDDPSPCALETGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWVNDAVGRDWPWIYFVTLIIIGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGMDEEKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPNWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRFDCFVVCGGILETILVETKIMSPLGISVLRCVRLLRIFKITRYWNSLSNLVASLLNSVRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMQTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQELVEKPAVGESKEEKIELKSITADGESPPATKINMDDLQPNENEDKSPYPNPETTGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSSNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILFYFDIVFTTIFTIEIALKILGNADYVFTSIFTLEIILKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAECKGNYITYKDGEVDHPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKGYFSDPWNVFDFLIVIGSIIDVILSETNHYFCDAWNTFDALIVVGSIVDIAITEVNPAEHTQCSPSMNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESEPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTVMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFRRAGGLFGNHVSYYQSDGRSAFPQTFTTQRPLHINKAGSSQGDTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRLPRPAGYPSTVSTVEGHGPPLSPAIRVQEVAWKLSSNRERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPSRCHSRESQAAMAGQEETSQDETYEVKMNHDTEACSEPSLLSTEMLSYQDDENRQLTLPEEDKRDIRQSPKRGFLRSASLGRRASFHLECLKRQKDRGGDISQKTVLPLHLVHHQALAVAGLSPLLQRSHSPASFPRPFATPPATPGSRGWPPQPVPTLRLEGVESSEKLNSSFPSIHCGSWAETTPGGGGSSAARRVRPVSLMVPSQAGAPGRQFHGSASSLVEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIEEMESAADNILSGGAPQSPNGALLPFVNCRDAGQDRAGGEEDAGCVRARGRPSEEELQDSRVYVSSL TTZIFHC TT Successful TTZIFHC FM Voltage-gated ion channel TTZIFHC KE hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04727:GABAergic synapse; hsa04728:Dopaminergic synapse; hsa04911:Insulin secretion; hsa04912:GnRH signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04930:Type II diabetes mellitus; hsa05010:Alzheimer's disease; hsa05031:Amphetamine addiction; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTZIFHC RC R-HSA-400042:Adrenaline,noradrenaline inhibits insulin secretion; R-HSA-419037:NCAM1 interactions; R-HSA-422356:Regulation of insulin secretion TT729IR ID TT729IR TT729IR TN Voltage-gated calcium channel alpha Cav3.1 (CACNA1G) TT729IR UP O43497 TT729IR UC CAC1G_HUMAN TT729IR BC Voltage-gated ion channel TT729IR SN Voltage-gated calcium channel alpha subunit Cav3.1; Voltage-dependent T-type calcium channel; NBR13; Cav3.1c; CACNA1G TT729IR GN CACNA1G TT729IR FC Voltage-sensitive calcium channels (vscc) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release and gene expression. TT729IR SQ MDEEEDGAGAEESGQPRSFMRLNDLSGAGGRPGPGSAEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERISMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLERYYQTENEDESPFICSQPRENGMRSCRSVPTLRGDGGGGPPCGLDYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAAGVRVGLLSSPAPLGGQETQPSSSCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRAPRASPEIQDRDANGSRRLMLPPPSTPALSGAPPGGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPETLKEKALVEVAASSGPPTLTSLNIPPGPYSSMHKLLETQSTGACQSSCKISSPCLKADSGACGPDSCPYCARAGAGEVELADREMPDSDSEAVYEFTQDAQHSDLRDPHSRRQRSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEEISKREDASGQLSCIQLPVDSQGGDANKSESEPDFFSPSLDGDGDRKKCLALVSLGEHPELRKSLLPPLIIHTAATPMSLPKSTSTGLGEALGPASRRTSSSGSAEPGAAHEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEERASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRGSASEHQDCNGKSASGRLARALRPDDPPLDGDDADDEGNLSKGERVRAWIRARLPACCLERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLRRLEKKRRNLMLDDVIASGSSASAASEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGPDSPDSPKPGALHPAAHARSASHFSLEHPTDRQLFDTISLLIQGSLEWELKLMDELAGPGGQPSAFPSAPSLGGSDPQIPLAEMEALSLTSEIVSEPSCSLALTDDSLPDDMHTLLLSALESNMQPHPTELPGPDLLTVRKSGVSRTHSLPNDSYMCRHGSTAEGPLGHRGWGLPKAQSGSVLSVHSQPADTSYILQLPKDAPHLLQPHSAPTWGTIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLAEVSGPSPPLARAYSFWGQSSTQAQQHSRSHSKISKHMTPPAPCPGPEPNWGKGPPETRSSLELDTELSWISGDLLPPGGQEEPPSPRDLKKCYSVEAQSCQRRPTSWLDEQRRHSIAVSCLDSGSQPHLGTDPSNLGGQPLGGPGSRPKKKLSPPSITIDPPESQGPRTPPSPGICLRRRAPSSDSKDPLASGPPDSMAASPSPKKDVLSLSGLSSDPADLDP TT729IR TT Successful TT729IR KE hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04713:Circadian entrainment; hsa04930:Type II diabetes mellitus TT729IR RC R-HSA-419037:NCAM1 interactions TTZPWGN ID TTZPWGN TTZPWGN TN Voltage-gated calcium channel alpha Cav3.2 (CACNA1H) TTZPWGN UP O95180 TTZPWGN UC CAC1H_HUMAN TTZPWGN BC Voltage-gated ion channel TTZPWGN SN Voltage-gated calcium channel subunit alpha Cav3.2; Voltage-dependent T-type calcium channel subunit alpha-1H; Low-voltage-activated calcium channel alpha1 3.2 subunit TTZPWGN GN CACNA1H TTZPWGN FC Voltage-sensitive calcium channel that gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group. A particularity of this type of channel is an opening at quite negative potentials, and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle (Probable). They may also be involved in the modulation of firing patterns of neurons. In the adrenal zona glomerulosa, participates in the signaling pathway leading to aldosterone production in response to either AGT/angiotensin II, or hyperkalemia. TTZPWGN SQ MTEGARAADEVRVPLGAPPPGPAALVGASPESPGAPGREAERGSELGVSPSESPAAERGAELGADEEQRVPYPALAATVFFCLGQTTRPRSWCLRLVCNPWFEHVSMLVIMLNCVTLGMFRPCEDVECGSERCNILEAFDAFIFAFFAVEMVIKMVALGLFGQKCYLGDTWNRLDFFIVVAGMMEYSLDGHNVSLSAIRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLDSAFVRNNNLTFLRPYYQTEEGEENPFICSSRRDNGMQKCSHIPGRRELRMPCTLGWEAYTQPQAEGVGAARNACINWNQYYNVCRSGDSNPHNGAINFDNIGYAWIAIFQVITLEGWVDIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRARHLSNDSTLASFSEPGSCYEELLKYVGHIFRKVKRRSLRLYARWQSRWRKKVDPSAVQGQGPGHRQRRAGRHTASVHHLVYHHHHHHHHHYHFSHGSPRRPGPEPGACDTRLVRAGAPPSPPSPGRGPPDAESVHSIYHADCHIEGPQERARVAHAAATAAASLRLATGLGTMNYPTILPSGVGSGKGSTSPGPKGKWAGGPPGTGGHGPLSLNSPDPYEKIPHVVGEHGLGQAPGHLSGLSVPCPLPSPPAGTLTCELKSCPYCTRALEDPEGELSGSESGDSDGRGVYEFTQDVRHGDRWDPTRPPRATDTPGPGPGSPQRRAQQRAAPGEPGWMGRLWVTFSGKLRRIVDSKYFSRGIMMAILVNTLSMGVEYHEQPEELTNALEISNIVFTSMFALEMLLKLLACGPLGYIRNPYNIFDGIIVVISVWEIVGQADGGLSVLRTFRLLRVLKLVRFLPALRRQLVVLVKTMDNVATFCTLLMLFIFIFSILGMHLFGCKFSLKTDTGDTVPDRKNFDSLLWAIVTVFQILTQEDWNVVLYNGMASTSSWAALYFVALMTFGNYVLFNLLVAILVEGFQAEGDANRSDTDEDKTSVHFEEDFHKLRELQTTELKMCSLAVTPNGHLEGRGSLSPPLIMCTAATPMPTPKSSPFLDAAPSLPDSRRGSSSSGDPPLGDQKPPASLRSSPCAPWGPSGAWSSRRSSWSSLGRAPSLKRRGQCGERESLLSGEGKGSTDDEAEDGRAAPGPRATPLRRAESLDPRPLRPAALPPTKCRDRDGQVVALPSDFFLRIDSHREDAAELDDDSEDSCCLRLHKVLEPYKPQWCRSREAWALYLFSPQNRFRVSCQKVITHKMFDHVVLVFIFLNCVTIALERPDIDPGSTERVFLSVSNYIFTAIFVAEMMVKVVALGLLSGEHAYLQSSWNLLDGLLVLVSLVDIVVAMASAGGAKILGVLRVLRLLRTLRPLRVISRAPGLKLVVETLISSLRPIGNIVLICCAFFIIFGILGVQLFKGKFYYCEGPDTRNISTKAQCRAAHYRWVRRKYNFDNLGQALMSLFVLSSKDGWVNIMYDGLDAVGVDQQPVQNHNPWMLLYFISFLLIVSFFVLNMFVGVVVENFHKCRQHQEAEEARRREEKRLRRLERRRRSTFPSPEAQRRPYYADYSPTRRSIHSLCTSHYLDLFITFIICVNVITMSMEHYNQPKSLDEALKYCNYVFTIVFVFEAALKLVAFGFRRFFKDRWNQLDLAIVLLSLMGITLEEIEMSAALPINPTIIRIMRVLRIARVLKLLKMATGMRALLDTVVQALPQVGNLGLLFMLLFFIYAALGVELFGRLECSEDNPCEGLSRHATFSNFGMAFLTLFRVSTGDNWNGIMKDTLRECSREDKHCLSYLPALSPVYFVTFVLVAQFVLVNVVVAVLMKHLEESNKEAREDAELDAEIELEMAQGPGSARRVDADRPPLPQESPGARDAPNLVARKVSVSRMLSLPNDSYMFRPVVPASAPHPRPLQEVEMETYGAGTPLGSVASVHSPPAESCASLQIPLAVSSPARSGEPLHALSPRGTARSPSLSRLLCRQEAVHTDSLEGKIDSPRDTLDPAEPGEKTPVRPVTQGGSLQSPPRSPRPASVRTRKHTFGQRCVSSRPAAPGGEEAEASDPADEEVSHITSSACPWQPTAEPHGPEASPVAGGERDLRRLYSVDAQGFLDKPGRADEQWRPSAELGSGEPGEAKAWGPEAEPALGARRKKKMSPPCISVEPPAEDEGSARPSAAEGGSTTLRRRTPSCEATPHRDSLEPTEGSGAGGDPAAKGERWGQASCRAEHLTVPSFAFEPLDLGVPSGDPFLDGSHSVTPESRASSSGAIVPLEPPESEPPMPVGDPPEKRRGLYLTVPQCPLEKPGSPSATPAPGGGADDPV TTZPWGN TT Successful TTZPWGN KE hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04713:Circadian entrainment TTZPWGN RC R-HSA-419037:NCAM1 interactions TTFK1JQ ID TTFK1JQ TTFK1JQ TN Voltage-gated calcium channel alpha-2/delta-1 (CACNA2D1) TTFK1JQ UP P54289 TTFK1JQ UC CA2D1_HUMAN TTFK1JQ BC Voltage-gated ion channel TTFK1JQ SN Voltage-gated calcium channel subunit alpha-2/delta-1; Voltage-dependent calcium channel subunit delta-1; Voltage-dependent calcium channel subunit alpha-2-1; MHS3; CCHL2A; CACNL2A; CACNA2D1 TTFK1JQ GN CACNA2D1 TTFK1JQ FC The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Plays an important role in excitation-contraction coupling. TTFK1JQ SQ MAAGCLLALTLTLFQSLLIGPSSEEPFPSAVTIKSWVDKMQEDLVTLAKTASGVNQLVDIYEKYQDLYTVEPNNARQLVEIAARDIEKLLSNRSKALVRLALEAEKVQAAHQWREDFASNEVVYYNAKDDLDPEKNDSEPGSQRIKPVFIEDANFGRQISYQHAAVHIPTDIYEGSTIVLNELNWTSALDEVFKKNREEDPSLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHLVQANVRNKKVLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDGGEERAQEIFNKYNKDKKVRVFTFSVGQHNYDRGPIQWMACENKGYYYEIPSIGAIRINTQEYLDVLGRPMVLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNITGQFENKTNLKNQLILGVMGVDVSLEDIKRLTPRFTLCPNGYYFAIDPNGYVLLHPNLQPKPIGVGIPTINLRKRRPNIQNPKSQEPVTLDFLDAELENDIKVEIRNKMIDGESGEKTFRTLVKSQDERYIDKGNRTYTWTPVNGTDYSLALVLPTYSFYYIKAKLEETITQARYSETLKPDNFEESGYTFIAPRDYCNDLKISDNNTEFLLNFNEFIDRKTPNNPSCNADLINRVLLDAGFTNELVQNYWSKQKNIKGVKARFVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYESGIMVSKAVEIYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVILDDGGFLLMANHDDYTNQIGRFFGEIDPSLMRHLVNISVYAFNKSYDYQSVCEPGAAPKQGAGHRSAYVPSVADILQIGWWATAAAWSILQQFLLSLTFPRLLEAVEMEDDDFTASLSKQSCITEQTQYFFDNDSKSFSGVLDCGNCSRIFHGEKLMNTNLIFIMVESKGTCPCDTRLLIQAEQTSDGPNPCDMVKQPRYRKGPDVCFDNNVLEDYTDCGGVSGLNPSLWYIIGIQFLLLWLVSGSTHRLL TTFK1JQ TT Successful TTFK1JQ KE hsa04010:MAPK signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04921:Oxytocin signaling pathway; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTW0CMT ID TTW0CMT TTW0CMT TN Voltage-gated potassium channel Kv1.5 (KCNA5) TTW0CMT UP P22460 TTW0CMT UC KCNA5_HUMAN TTW0CMT BC Voltage-gated ion channel TTW0CMT SN Voltage-gatedpotassium channel subunit Kv1.5; Voltage-gated potassium channel subunit Kv1.5; Voltage-gated potassium channel HK2; Potassium voltage-gated channel subfamily A member 5; Potassium channel Kv1.5; HPCN1; HK2; 02-Sensitive Potassium Channel Kv1.5 TTW0CMT GN KCNA5 TTW0CMT FC Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. Homotetrameric channels display rapid activation and slow inactivation. May play a role in regulating the secretion of insulin in normal pancreatic islets. Isoform 2 exhibits a voltage-dependent recovery from inactivation and an excessive cumulative inactivation. Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. TTW0CMT SQ MEIALVPLENGGAMTVRGGDEARAGCGQATGGELQCPPTAGLSDGPKEPAPKGRGAQRDADSGVRPLPPLPDPGVRPLPPLPEELPRPRRPPPEDEEEEGDPGLGTVEDQALGTASLHHQRVHINISGLRFETQLGTLAQFPNTLLGDPAKRLRYFDPLRNEYFFDRNRPSFDGILYYYQSGGRLRRPVNVSLDVFADEIRFYQLGDEAMERFREDEGFIKEEEKPLPRNEFQRQVWLIFEYPESSGSARAIAIVSVLVILISIITFCLETLPEFRDERELLRHPPAPHQPPAPAPGANGSGVMAPPSGPTVAPLLPRTLADPFFIVETTCVIWFTFELLVRFFACPSKAGFSRNIMNIIDVVAIFPYFITLGTELAEQQPGGGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADNQGTHFSSIPDAFWWAVVTMTTVGYGDMRPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDHEEPAVLKEEQGTQSQGPGLDRGVQRKVSGSRGSFCKAGGTLENADSARRGSCPLEKCNVKAKSNVDLRRSLYALCLDTSRETDL TTW0CMT TT Successful TTW0CMT FM Voltage gated ion channel TTW0CMT RC R-HSA-1296072:Voltage gated Potassium channels TT90XZ8 ID TT90XZ8 TT90XZ8 TN Voltage-gated sodium channel alpha Nav1.8 (SCN10A) TT90XZ8 UP Q9Y5Y9 TT90XZ8 UC SCNAA_HUMAN TT90XZ8 BC Voltage-gated ion channel TT90XZ8 SN hPN3; Voltage-gated sodium channel subunit alpha Nav1.8; Sodium channel protein type X subunit alpha; Sodium channel protein type 10 subunit alpha; Peripheral nerve sodium channel 3; PN3 TT90XZ8 GN SCN10A TT90XZ8 FC Tetrodotoxin-resistant channel that mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. Plays a role in neuropathic pain mechanisms. TT90XZ8 SQ MEFPIGSLETNNFRRFTPESLVEIEKQIAAKQGTKKAREKHREQKDQEEKPRPQLDLKACNQLPKFYGELPAELIGEPLEDLDPFYSTHRTFMVLNKGRTISRFSATRALWLFSPFNLIRRTAIKVSVHSWFSLFITVTILVNCVCMTRTDLPEKIEYVFTVIYTFEALIKILARGFCLNEFTYLRDPWNWLDFSVITLAYVGTAIDLRGISGLRTFRVLRALKTVSVIPGLKVIVGALIHSVKKLADVTILTIFCLSVFALVGLQLFKGNLKNKCVKNDMAVNETTNYSSHRKPDIYINKRGTSDPLLCGNGSDSGHCPDGYICLKTSDNPDFNYTSFDSFAWAFLSLFRLMTQDSWERLYQQTLRTSGKIYMIFFVLVIFLGSFYLVNLILAVVTMAYEEQNQATTDEIEAKEKKFQEALEMLRKEQEVLAALGIDTTSLHSHNGSPLTSKNASERRHRIKPRVSEGSTEDNKSPRSDPYNQRRMSFLGLASGKRRASHGSVFHFRSPGRDISLPEGVTDDGVFPGDHESHRGSLLLGGGAGQQGPLPRSPLPQPSNPDSRHGEDEHQPPPTSELAPGAVDVSAFDAGQKKTFLSAEYLDEPFRAQRAMSVVSIITSVLEELEESEQKCPPCLTSLSQKYLIWDCCPMWVKLKTILFGLVTDPFAELTITLCIVVNTIFMAMEHHGMSPTFEAMLQIGNIVFTIFFTAEMVFKIIAFDPYYYFQKKWNIFDCIIVTVSLLELGVAKKGSLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTIILAIIVFVFALVGKQLLGENYRNNRKNISAPHEDWPRWHMHDFFHSFLIVFRILCGEWIENMWACMEVGQKSICLILFLTVMVLGNLVVLNLFIALLLNSFSADNLTAPEDDGEVNNLQVALARIQVFGHRTKQALCSFFSRSCPFPQPKAEPELVVKLPLSSSKAENHIAANTARGSSGGLQAPRGPRDEHSDFIANPTVWVSVPIAEGESDLDDLEDDGGEDAQSFQQEVIPKGQQEQLQQVERCGDHLTPRSPGTGTSSEDLAPSLGETWKDESVPQVPAEGVDDTSSSEGSTVDCLDPEEILRKIPELADDLEEPDDCFTEGCIRHCPCCKLDTTKSPWDVGWQVRKTCYRIVEHSWFESFIIFMILLSSGSLAFEDYYLDQKPTVKALLEYTDRVFTFIFVFEMLLKWVAYGFKKYFTNAWCWLDFLIVNISLISLTAKILEYSEVAPIKALRTLRALRPLRALSRFEGMRVVVDALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFWRCINYTDGEFSLVPLSIVNNKSDCKIQNSTGSFFWVNVKVNFDNVAMGYLALLQVATFKGWMDIMYAAVDSREVNMQPKWEDNVYMYLYFVIFIIFGGFFTLNLFVGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKFQGFVFDIVTRQAFDITIMVLICLNMITMMVETDDQSEEKTKILGKINQFFVAVFTGECVMKMFALRQYYFTNGWNVFDFIVVVLSIASLIFSAILKSLQSYFSPTLFRVIRLARIGRILRLIRAAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMSSFPHVRWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGTRGDCGSPAVGIIFFTTYIIISFLIMVNMYIAVILENFNVATEESTEPLSEDDFDMFYETWEKFDPEATQFITFSALSDFADTLSGPLRIPKPNRNILIQMDLPLVPGDKIHCLDILFAFTKNVLGESGELDSLKANMEEKFMATNLSKSSYEPIATTLRWKQEDISATVIQKAYRSYVLHRSMALSNTPCVPRAEEEAASLPDEGFVAFTANENCVLPDKSETASATSFPPSYESVTRGLSDRVNMRTSSSIQNEDEATSMELIAPGP TT90XZ8 TT Successful TT90XZ8 RC R-HSA-445095:Interaction between L1 and Ankyrins TTS41ER ID TTS41ER TTS41ER TN HUMAN cyclophilin A (CYPA) TTS41ER UP P62937 TTS41ER UC PPIA_HUMAN TTS41ER BC Cis-trans-isomerases TTS41ER SN PPIA; Cyclophilin A; CyPA TTS41ER GN PPIA TTS41ER FC Ppiases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. TTS41ER EC EC 5.2.1.8 TTS41ER PD 6GJY; 6GJR; 6GJP; 6GJN; 6GJM TTS41ER SQ MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE TT95SAZ ID TT95SAZ TT95SAZ TN HUMAN cyclophilin D (CYP3) TT95SAZ UP P30405 TT95SAZ UC PPIF_HUMAN TT95SAZ BC Cis-trans-isomerase TT95SAZ SN Peptidylprolyl cistrans isomerase F, mitochondrial; Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIase F; Mitochondrial cyclophilin; Cyclophilin F; CyPM; CyP-M; CyP-D; CYP3 TT95SAZ GN PPIF TT95SAZ FC Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis. PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. TT95SAZ EC EC 5.2.1.8 TT95SAZ PD 5NWO; 5CCS; 5CCR; 5CCQ; 5CCN TT95SAZ SQ MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCGQLS TT95SAZ FM Cis-trans-isomerases TTAW3TO ID TTAW3TO TTAW3TO TN HUMAN ERK activator kinase 1 (MEK1) TTAW3TO UP Q02750 TTAW3TO UC MP2K1_HUMAN TTAW3TO BC Kinase TTAW3TO SN PRKMK1; Mitogen-activated protein kinase kinase 1; MKK1; MEK 1; MAPKK 1; MAPK/ERKkinase 1; MAPK/ERK kinase 1; MAP kinase kinase 1; Dual specificity mitogen-activated protein kinase kinase 1 TTAW3TO GN MAP2K1 TTAW3TO FC Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator-activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis. Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. TTAW3TO EC EC 2.7.12.2 TTAW3TO PD 5YT3; 5HZE; 5EYM; 5BX0; 4U81 TTAW3TO SQ MPKKKPTPIQLNPAPDGSAVNGTSSAETNLEALQKKLEELELDEQQRKRLEAFLTQKQKVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSRPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGV TTAW3TO FM Kinase TTWX403 ID TTWX403 TTWX403 TN HUMAN ERK activator kinase 2 (MEK2) TTWX403 UP P36507 TTWX403 UC MP2K2_HUMAN TTWX403 BC Kinase TTWX403 SN PRKMK2; MKK2; MEK 2; MAPKK 2; MAPK/ERK kinase 2; MAP kinase kinase 2; Dual specificity mitogenactivated protein kinase kinase 2; Dual specificity mitogen-activated protein kinase kinase 2 TTWX403 GN MAP2K2 TTWX403 FC Activates the ERK1 and ERK2 MAP kinases. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. TTWX403 EC EC 2.7.12.2 TTWX403 PD 4H3Q; 1S9I TTWX403 SQ MLARRKPVLPALTINPTIAEGPSPTSEGASEANLVDLQKKLEELELDEQQKKRLEAFLTQKAKVGELKDDDFERISELGAGNGGVVTKVQHRPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMAPERLQGTHYSVQSDIWSMGLSLVELAVGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISPRPRPPGRPVSGHGMDSRPAMAIFELLDYIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERADLKMLTNHTFIKRSEVEEVDFAGWLCKTLRLNQPGTPTRTAV TTWX403 FM Kinase TTTU6X1 ID TTTU6X1 TTTU6X1 TN HUMAN inosine-5'-monophosphate dehydrogenase 2 (IMPDH2) TTTU6X1 UP P12268 TTTU6X1 UC IMDH2_HUMAN TTTU6X1 BC CH-OH donor oxidoreductase TTTU6X1 SN IMPDH-II; IMPDH 2; IMPD2; IMPD 2; IMP dehydrogenase 2 TTTU6X1 GN IMPDH2 TTTU6X1 FC Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors. Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. TTTU6X1 EC EC 1.1.1.205 TTTU6X1 PD 6I0O; 6I0M; 1NFB; 1NF7; 1B3O TTTU6X1 SQ MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF TTNISW6 ID TTNISW6 TTNISW6 TN HUMAN bromodomain-containing protein 2 (BRD2) TTNISW6 UP P25440 TTNISW6 UC BRD2_HUMAN TTNISW6 BC Bromodomain TTNISW6 SN Really interesting new gene 3 protein; RING3; O27.1.1; KIAA9001 TTNISW6 GN BRD2 TTNISW6 FC Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly. May play a role in spermatogenesis or folliculogenesis. TTNISW6 PD 6MOA; 6MO9; 6MO8; 6MO7; 6FFG TTNISW6 SQ MLQNVTPHNKLPGEGNAGLLGLGPEAAAPGKRIRKPSLLYEGFESPTMASVPALQLTPANPPPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPMDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMPQEEQELVVTIPKNSHKKGAKLAALQGSVTSAHQVPAVSSVSHTALYTPPPEIPTTVLNIPHPSVISSPLLKSLHSAGPPLLAVTAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGSPASPPGSLEPKAARLPPMRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKELLSKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRLMFSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTAMPPGLAKSSSESSSEESSSESSSEEEEEEDEEDEEEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQGPISKPKRKREKKEKKKKRKAEKHRGRAGADEDDKGPRAPRPPQPKKSKKASGSGGGSAALGPSGFGPSGGSGTKLPKKATKTAPPALPTGYDSEEEEESRPMSYDEKRQLSLDINKLPGEKLGRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIKKPVGKTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKANEKTESSSAQQVAVSRLSASSSSSDSSSSSSSSSSSDTSDSDSG TTDT8RP ID TTDT8RP TTDT8RP TN HUMAN casein kinase II (CSK2) TTDT8RP UP P68400; P19784; Q8NEV1; P67870 TTDT8RP UC CSK21_HUMAN; CSK22_HUMAN; CSK23_HUMAN; CSK2B_HUMAN TTDT8RP BC Kinase TTDT8RP SN Protein kinase CK2; Casein kinase II; CK2; CK II TTDT8RP FC Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry. Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue. Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. TTDT8RP EC EC 2.7.11.1 TTDT8RP PD 6Q4Q; 6Q38; 6HME; 6HBN; 6GMD TTDT8RP SQ MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAAAGAQQ TTKV8W5 ID TTKV8W5 TTKV8W5 TN HUMAN mannose receptor (MRC1) TTKV8W5 UP P22897 TTKV8W5 UC MRC1_HUMAN TTKV8W5 BC Fibronectin protein TTKV8W5 SN Macrophage mannose receptor 1like protein 1; Macrophage mannose receptor 1-like protein 1; Macrophage mannose receptor 1; MRC1L1; MMR; Human mannose receptor; Ctype lectin domain family 13 member Dlike; Ctype lectin domain family 13 member D; CLEC13DL; CLEC13D; CD206; C-type lectin domain family 13 member D-like; C-type lectin domain family 13 member D TTKV8W5 GN MRC1 TTKV8W5 FC Binds both sulfated and non-sulfated polysaccharide chains. Mediates the endocytosis of glycoproteins by macrophages. TTKV8W5 PD 5XTW; 5XTS; 1EGI; 1EGG TTKV8W5 SQ MRLPLLLVFASVIPGAVLLLDTRQFLIYNEDHKRCVDAVSPSAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQKWECKNDTLLGIKGEDLFFNYGNRQEKNIMLYKGSGLWSRWKIYGTTDNLCSRGYEAMYTLLGNANGATCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDTDKLFGYCPLKFEGSESLWNKDPLTSVSYQINSKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSGLWIGLNSLSFNSGWQWSDRSPFRYLNWLPGSPSAEPGKSCVSLNPGKNAKWENLECVQKLGYICKKGNTTLNSFVIPSESDVPTHCPSQWWPYAGHCYKIHRDEKKIQRDALTTCRKEGGDLTSIHTIEELDFIISQLGYEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLRGEPSHENNRQEDCVVMKGKDGYWADRGCEWPLGYICKMKSRSQGPEIVEVEKGCRKGWKKHHFYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRPEKYFWTGLSDIQTKGTFQWTIEEEVRFTHWNSDMPGRKPGCVAMRTGIAGGLWDVLKCDEKAKFVCKHWAEGVTHPPKPTTTPEPKCPEDWGASSRTSLCFKLYAKGKHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHKLFWLGLTYGSPSEGFTWSDGSPVSYENWAYGEPNNYQNVEYCGELKGDPTMSWNDINCEHLNNWICQIQKGQTPKPEPTPAPQDNPPVTEDGWVIYKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDAQSAYFIGLLISLDKKFAWMDGSKVDYVSWATGEPNFANEDENCVTMYSNSGFWNDINCGYPNAFICQRHNSSINATTVMPTMPSVPSGCKEGWNFYSNKCFKIFGFMEEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSAWTGLNDVNSEHTFLWTDGRGVHYTNWGKGYPGGRRSSLSYEDADCVVIIGGASNEAGKWMDDTCDSKRGYICQTRSDPSLTNPPATIQTDGFVKYGKSSYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQMETSNERVWIALNSNLTDNQYTWTDKWRVRYTNWAADEPKLKSACVYLDLDGYWKTAHCNESFYFLCKRSDEIPATEPPQLPGRCPESDHTAWIPFHGHCYYIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLKSKTNFWIGLFRNVEGTWLWINNSPVSFVNWNTGDPSGERNDCVALHASSGFWSNIHCSSYKGYICKRPKIIDAKPTHELLTTKADTRKMDPSKPSSNVAGVVIIVILLILTGAGLAAYFFYKKRRVHLPQEGAFENTLYFNSQSSPGTSDMKDLVGNIEQNEHSVI TTTPE1L ID TTTPE1L TTTPE1L TN HUMAN opioid receptor sigma 1 (OPRS1) TTTPE1L UP Q99720 TTTPE1L UC SGMR1_HUMAN TTTPE1L BC GPCR rhodopsin TTTPE1L SN hSigmaR1; Sigma1R; Sigma1-receptor; Sigma non-opioid intracellular receptor 1; Sigma 1-type opioid receptor; SRBP; SR31747-binding protein; SR31747 binding protein 1; SR-BP; SIG-1R; Opioid receptor, sigma 1, isoform 1; OPRS1 protein; Aging-associated gene 8 protein; AAG8 TTTPE1L GN SIGMAR1 TTTPE1L FC Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration. Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112. Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. TTTPE1L PD 6DK1; 6DK0; 6DJZ; 5HK2; 5HK1 TTTPE1L SQ MQWAVGRRWAWAALLLAVAAVLTQVVWLWLGTQSFVFQREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSRGHSGRYWAEISDTIISGTFHQWREGTTKSEVFYPGETVVHGPGEATAVEWGPNTWMVEYGRGVIPSTLAFALADTVFSTQDFLTLFYTLRSYARGLRLELTTYLFGQDP TTWNK8B ID TTWNK8B TTWNK8B TN HUMAN sodium pump subunit alpha-1 (ATP1A1) TTWNK8B UP P05023 TTWNK8B UC AT1A1_HUMAN TTWNK8B BC Acid anhydrides hydrolase TTWNK8B SN Sodium/potassium-transporting ATPase alpha1; Sodium pump 1; Na+/K+ ATPase 1; ATP1A1 TTWNK8B GN ATP1A1 TTWNK8B FC This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of atp coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions. TTWNK8B EC EC 7.2.2.13 TTWNK8B SQ MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY TTIGYVZ ID TTIGYVZ TTIGYVZ TN HUMAN eukaryotic initiation factor-4A (eIF4A) TTIGYVZ UP P60842; Q14240; P38919 TTIGYVZ UC IF4A1_HUMAN; IF4A2_HUMAN; IF4A3_HUMAN TTIGYVZ BC eIF4A subfamily TTIGYVZ SN eIF-4A; ATP-dependent RNA helicase Eif4a TTIGYVZ GN EIF4A1; EIF4A2; EIF4A3 TTIGYVZ FC ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon TTIGYVZ SQ MSASQDSRSRDNGPDGMEPEGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWKLDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI TTE63HY ID TTE63HY TTE63HY TN HUMAN fusion protein Bcr-Abl (Bcr-Abl) TTE63HY UP P11274-P00519 TTE63HY UC BCR_HUMAN/ABL1_HUMAN TTE63HY BC Kinase TTE63HY SN BCR-ABL fusion protein; BCR-ABL TTE63HY GN BCR-ABL1 TTE63HY FC Activates downstream signaling pathways such as STAT5, PI3K/Akt, and Erk1/2 to lead to increased cell transformation, survival, and proliferation. TTE63HY SQ MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEVMLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR TTIS0R2 ID TTIS0R2 TTIS0R2 TN HUMAN sigma intracellular receptor 2 (TMEM97) TTIS0R2 UP Q5BJF2 TTIS0R2 UC SGMR2_HUMAN TTIS0R2 BC TMEM97/sigma-2 receptor TTIS0R2 SN Transmembrane protein 97; Sigma2 receptor; Sigma-2 receptor; Meningioma-associated protein 30; MAC30 TTIS0R2 GN TMEM97 TTIS0R2 FC Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cancer cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. Under investigation for its potential diagnostic and therapeutic uses. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins. TTIS0R2 SQ MGAPATRRCVEWLLGLYFLSHIPITLFMDLQAVLPRELYPVEFRNLLKWYAKEFKDPLLQEPPAWFKSFLFCELVFQLPFFPIATYAFLKGSCKWIRTPAIIYSVHTMTTLIPILSTFLFEDFSKASGFKGQRPETLHERLTLVSVYAPYLLIPFILLIFMLRSPYYKYEEKRKKK TT854FJ ID TT854FJ TT854FJ TN MERS-CoV spike glycoprotein S2' HR1 region (S S2'HR1) TT854FJ UP A0A140AYZ5 (888-1353) TT854FJ UC A0A140AYZ5_9BETC (888-1353) TT854FJ BC Betacoronaviruses spike protein family. TT854FJ SN MERS-CoV S glycoprotein S2' heptad repeat 1 region; MERS-CoV Spike glycoprotein S2' heptad repeat 1 region; MERS-CoV E2 S2' heptad repeat 1 region; MERS-CoV Peplomer protein S2' heptad repeat 1 region TT854FJ GN MERS-CoV S TT854FJ FC Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. TT854FJ SQ SAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFRKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPQVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH TTXMITO ID TTXMITO TTXMITO TN SARS-CoV spike glycoprotein S2' HR1 region (S S2'HR1) TTXMITO UP P59594 (798-1255) TTXMITO UC SPIKE_CVHSA (798-1255) TTXMITO BC Betacoronaviruses spike protein family. TTXMITO SN SARS-CoV S glycoprotein S2' heptad repeat 1 region; SARS-CoV Spike glycoprotein S2' heptad repeat 1 region; SARS-CoV E2 S2' heptad repeat 1 region; SARS-CoV Peplomer protein S2' heptad repeat 1 region TTXMITO GN MERS-CoV S; MERS-CoV 2 TTXMITO FC Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. TTXMITO SQ SFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSC TTJB8UY ID TTJB8UY TTJB8UY TN HUMAN beta adrenergic receptor (BAR) TTJB8UY UP P08588; P07550; P13945 TTJB8UY UC ADRB1_HUMAN; ADRB2_HUMAN; ADRB3_HUMAN TTJB8UY BC G-protein coupled receptor 1 family TTJB8UY SN Beta adrenoreceptor TTJB8UY GN ADRB1; ADRB2; ADRB3 TTJB8UY FC Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling. Involved in the regulation of sleep/wake behaviors. TTJB8UY SQ MGAGVLVLGASEPGNLSSAAPLPDGAATAARLLVPASPPASLLPPASESPEPLSQQWTAGMGLLMALIVLLIVAGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTRARARGLVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLGGPARPPSPSPSPVPAPAPPPGPPRPAAAAATAPLANGRAGKRRPSRLVALREQKALKTLGIIMGVFTLCWLPFFLANVVKAFHRELVPDRLFVFFNWLGYANSAFNPIIYCRSPDFRKAFQRLLCCARRAARRRHATHGDRPRASGCLARPGPPPSPGAASDDDDDDVVGATPPARLLEPWAGCNGGAAADSDSSLDEPCRPGFASESKV TT0MI3F ID TT0MI3F TT0MI3F TN 5-HT 1F receptor (HTR1F) TT0MI3F UP P30939 TT0MI3F UC 5HT1F_HUMAN TT0MI3F BC GPCR rhodopsin TT0MI3F SN Serotonin receptor 1F; HTR1EL; 5-hydroxytryptamine receptor 1F; 5-HT1F receptor; 5-HT1F; 5-HT-1F TT0MI3F GN HTR1F TT0MI3F FC Functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. G-protein coupled receptor for 5-hydroxytryptamine (serotonin). TT0MI3F SQ MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC TT0MI3F TT Successful TT0MI3F KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse TT0MI3F RC R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events TTRUFDT ID TTRUFDT TTRUFDT TN 5-HT 5A receptor (HTR5A) TTRUFDT UP P47898 TTRUFDT UC 5HT5A_HUMAN TTRUFDT BC GPCR rhodopsin TTRUFDT SN Serotonin receptor 5A; 5-hydroxytryptamine receptor 5A; 5-HT5A; 5-HT-5A; 5-HT-5; 5-HT 5A TTRUFDT GN HTR5A TTRUFDT FC The activity of this receptor is mediated by G proteins. This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. TTRUFDT SQ MDLPVNLTSFSLSTPSPLETNHSLGKDDLRPSSPLLSVFGVLILTLLGFLVAATFAWNLLVLATILRVRTFHRVPHNLVASMAVSDVLVAALVMPLSLVHELSGRRWQLGRRLCQLWIACDVLCCTASIWNVTAIALDRYWSITRHMEYTLRTRKCVSNVMIALTWALSAVISLAPLLFGWGETYSEGSEECQVSREPSYAVFSTVGAFYLPLCVVLFVYWKIYKAAKFRVGSRKTNSVSPISEAVEVKDSAKQPQMVFTVRHATVTFQPEGDTWREQKEQRAALMVGILIGVFVLCWIPFFLTELISPLCSCDIPAIWKSIFLWLGYSNSFFNPLIYTAFNKNYNSAFKNFFSRQH TTRUFDT TT Successful TTRUFDT KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse TTRUFDT RC R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events TTBRKXS ID TTBRKXS TTBRKXS TN Adrenergic receptor alpha-1B (ADRA1B) TTBRKXS UP P35368 TTBRKXS UC ADA1B_HUMAN TTBRKXS BC GPCR rhodopsin TTBRKXS SN Alpha-1B adrenoreceptor; Alpha-1B adrenoceptor; Alpha-1B adrenergic receptor; Alpha 1B-adrenoreceptor; Alpha 1B-adrenoceptor TTBRKXS GN ADRA1B TTBRKXS FC Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes. This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. TTBRKXS SQ MNPDLDTGHNTSAPAHWGELKNANFTGPNQTSSNSTLPQLDITRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAMADLLLSFTVLPFSAALEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFVRILGCQCRGRGRRRRRRRRRLGGCAYTYRPWTRGGSLERSQSRKDSLDDSGSCLSGSQRTLPSASPSPGYLGRGAPPPVELCAFPEWKAPGALLSLPAPEPPGRRGRHDSGPLFTFKLLTEPESPGTDGGASNGGCEAAADVANGQPGFKSNMPLAPGQF TTBRKXS TT Successful TTBRKXS KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04970:Salivary secretion TTBRKXS RC R-HSA-390696:Adrenoceptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-416482:G alpha (12/13) signalling events TT34BHT ID TT34BHT TT34BHT TN Adrenergic receptor alpha-1D (ADRA1D) TT34BHT UP P25100 TT34BHT UC ADA1D_HUMAN TT34BHT BC GPCR rhodopsin TT34BHT SN Alpha-adrenergic receptor 1a; Alpha-1D adrenoreceptor; Alpha-1D adrenoceptor; Alpha-1D adrenergic receptor; Alpha adrenergic receptor 1a; Alpha 1D-adrenoreceptor; Alpha 1D-adrenoceptor; ADRA1A TT34BHT GN ADRA1D TT34BHT FC This alpha-adrenergic receptor mediates its effect through the influx of extracellular calcium. TT34BHT SQ MTFRDLLSVSFEGPRPDSSAGGSSAGGGGGSAGGAAPSEGPAVGGVPGGAGGGGGVVGAGSGEDNRSSAGEPGSAGAGGDVNGTAAVGGLVVSAQGVGVGVFLAAFILMAVAGNLLVILSVACNRHLQTVTNYFIVNLAVADLLLSATVLPFSATMEVLGFWAFGRAFCDVWAAVDVLCCTASILSLCTISVDRYVGVRHSLKYPAIMTERKAAAILALLWVVALVVSVGPLLGWKEPVPPDERFCGITEEAGYAVFSSVCSFYLPMAVIVVMYCRVYVVARSTTRSLEAGVKRERGKASEVVLRIHCRGAATGADGAHGMRSAKGHTFRSSLSVRLLKFSREKKAAKTLAIVVGVFVLCWFPFFFVLPLGSLFPQLKPSEGVFKVIFWLGYFNSCVNPLIYPCSSREFKRAFLRLLRCQCRRRRRRRPLWRVYGHHWRASTSGLRQDCAPSSGDAPPGAPLALTALPDPDPEPPGTPEMQAPVASRRKPPSAFREWRLLGPFRRPTTQLRAKVSSLSHKIRAGGAQRAEAACAQRSEVEAVSLGVPHEVAEGATCQAYELADYSNLRETDI TT34BHT TT Successful TT34BHT FM GPCR rhodopsin TT34BHT KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04970:Salivary secretion TT34BHT RC R-HSA-390696:Adrenoceptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-416482:G alpha (12/13) signalling events TTQM7TE ID TTQM7TE TTQM7TE TN Amiloride-sensitive sodium channel (ENaC) TTQM7TE UP P37088; P51168; P51170; P51172 TTQM7TE UC SCNNA_HUMAN; SCNNB_HUMAN; SCNNG_HUMAN; SCNND_HUMAN TTQM7TE BC Epithelial sodium channel TTQM7TE SN SCNE; Nonvoltage-gated sodium channel 1; NaCH; Epithelial Na(+) channel; ENaC TTQM7TE GN SCNN1A; SCNN1B; SCNN1G; SCNN1D TTQM7TE FC Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption ofsodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception. TTQM7TE SQ MEGNKLEEQDSSPPQSTPGLMKGNKREEQGLGPEPAAPQQPTAEEEALIEFHRSYRELFEFFCNNTTIHGAIRLVCSQHNRMKTAFWAVLWLCTFGMMYWQFGLLFGEYFSYPVSLNINLNSDKLVFPAVTICTLNPYRYPEIKEELEELDRITEQTLFDLYKYSSFTTLVAGSRSRRDLRGTLPHPLQRLRVPPPPHGARRARSVASSLRDNNPQVDWKDWKIGFQLCNQNKSDCFYQTYSSGVDAVREWYRFHYINILSRLPETLPSLEEDTLGNFIFACRFNQVSCNQANYSHFHHPMYGNCYTFNDKNNSNLWMSSMPGINNGLSLMLRAEQNDFIPLLSTVTGARVMVHGQDEPAFMDDGGFNLRPGVETSISMRKETLDRLGGDYGDCTKNGSDVPVENLYPSKYTQQVCIHSCFQESMIKECGCAYIFYPRPQNVEYCDYRKHSSWGYCYYKLQVDFSSDHLGCFTKCRKPCSVTSYQLSAGYSRWPSVTSQEWVFQMLSRQNNYTVNNKRNGVAKVNIFFKELNYKTNSESPSVTMVTLLSNLGSQWSLWFGSSVLSVVEMAELVFDLLVIMFLMLLRRFRSRYWSPGRGGRGAQEVASTLASSPPSHFCPHPMSLSLSQPGPAPSPALTAPPPAYATLGPRPSPGGSAGASSSTCPLGGP TTQM7TE TT Successful TTQM7TE KE hsa04742:Taste transduction; hsa04960:Aldosterone-regulated sodium reabsorption TTQM7TE RC R-HSA-2672351:Stimuli-sensing channels TTEF5MJ ID TTEF5MJ TTEF5MJ TN ATP-binding cassette transporter C9 (ABCC9) TTEF5MJ UP O60706 TTEF5MJ UC ABCC9_HUMAN TTEF5MJ BC ABC transporter TTEF5MJ SN Sulfonylurea receptor 2; SUR2; ATP-binding cassette sub-family C member 9 TTEF5MJ GN ABCC9 TTEF5MJ FC Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with KCNJ11. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation. TTEF5MJ SQ MSLSFCGNNISSYNINDGVLQNSCFVDALNLVPHVFLLFITFPILFIGWGSQSSKVQIHHNTWLHFPGHNLRWILTFALLFVHVCEIAEGIVSDSRRESRHLHLFMPAVMGFVATTTSIVYYHNIETSNFPKLLLALFLYWVMAFITKTIKLVKYCQSGLDISNLRFCITGMMVILNGLLMAVEINVIRVRRYVFFMNPQKVKPPEDLQDLGVRFLQPFVNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEIGDDSWRTGESSLPFESCKKHTGVQPKTINRKQPGRYHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMPWKTCWRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVMTNK TTEF5MJ TT Successful TTHWB7G ID TTHWB7G TTHWB7G TN Bacterial Penicillin binding protein 2 (Bact mrdA) TTHWB7G UP P0AD65 TTHWB7G UC MRDA_ECOLI TTHWB7G SN PBP-2 TTHWB7G GN Bact mrdA TTHWB7G FC Cell wall formation; PBP-2 is responsible for the determination of the rod shape of the cell. It synthesizes cross- linked peptidoglycan from lipid intermediates. TTHWB7G EC EC 3.4.16.4 TTHWB7G PD 6G9S TTHWB7G SQ MKLQNSFRDYTAESALFVRRALVAFLGILLLTGVLIANLYNLQIVRFTDYQTRSNENRIKLVPIAPSRGIIYDRNGIPLALNRTIYQIEMMPEKVDNVQQTLDALRSVVDLTDDDIAAFRKERARSHRFTSIPVKTNLTEVQVARFAVNQYRFPGVEVKGYKRRYYPYGSALTHVIGYVSKINDKDVERLNNDGKLANYAATHDIGKLGIERYYEDVLHGQTGYEEVEVNNRGRVIRQLKEVPPQAGHDIYLTLDLKLQQYIETLLAGSRAAVVVTDPRTGGVLALVSTPSYDPNLFVDGISSKDYSALLNDPNTPLVNRATQGVYPPASTVKPYVAVSALSAGVITRNTTLFDPGWWQLPGSEKRYRDWKKWGHGRLNVTRSLEESADTFFYQVAYDMGIDRLSEWMGKFGYGHYTGIDLAEERSGNMPTREWKQKRFKKPWYQGDTIPVGIGQGYWTATPIQMSKALMILINDGIVKVPHLLMSTAEDGKQVPWVQPHEPPVGDIHSGYWELAKDGMYGVANRPNGTAHKYFASAPYKIAAKSGTAQVFGLKANETYNAHKIAERLRDHKLMTAFAPYNNPQVAVAMILENGGAGPAVGTLMRQILDHIMLGDNNTDLPAENPAVAAAEDH TTHWB7G TT Successful TT85JMW ID TT85JMW TT85JMW TN Bacterial Penicillin binding protein 3 (Bact mrcA) TT85JMW UP P0AD68 TT85JMW UC FTSI_ECOLI TT85JMW BC Hexosyltransferase TT85JMW SN mrcA; Peptidoglycan synthetase ftsI; Peptidoglycan glycosyltransferase 3; Penicillin-binding protein 3; PSPB20; PBP-3; PBP 3 TT85JMW GN Bact mrcA TT85JMW FC Cell wall formation. Essential for the formation of a septum of the murein sacculus. Synthesis of cross-linked peptidoglycan from the lipid intermediates. TT85JMW EC EC 3.4.16.4 TT85JMW SQ MKAAAKTQKPKRQEEHANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVKEGDMRSLRVQQVSTSRGMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVGDRWKALANALNIPLDQLSARINANPKGRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNLSGTPKEAMRNRTITDVFEPGSTVKPMVVMTALQRGVVRENSVLNTIPYRINGHEIKDVARYSELTLTGVLQKSSNVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQRWSDIERATFSFGYGLMVTPLQLARVYATIGSYGIYRPLSITKVDPPVPGERVFPESIVRTVVHMMESVALPGGGGVKAAIKGYRIAIKTGTAKKVGPDGRYINKYIAYTAGVAPASQPRFALVVVINDPQAGKYYGGAVSAPVFGAIMGGVLRTMNIEPDALTTGDKNEFVINQGEGTGGRS TT85JMW TT Successful TT3YGCD ID TT3YGCD TT3YGCD TN Bacterial Protective antigen (Bact pagA) TT3YGCD UP P13423 TT3YGCD UC PAG_BACAN TT3YGCD BC Bacillus anthracis protective antigen TT3YGCD SN pagA; PA of Bacillus anthracis; Bacterial toxins translocating protein; Bacterial anthracis protective antigen; Bact PA83; Bact PA-83 TT3YGCD GN Bact pagA TT3YGCD FC One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death wheninjected, PA associated with EF produces edema. PA induces immunity to infection with anthrax. TT3YGCD PD 5FR3; 4NAM; 4H2A; 4EE2; 3TEZ TT3YGCD SQ MKKRKVLIPLMALSTILVSSTGNLEVIQAEVKQENRLLNESESSSQGLLGYYFSDLNFQAPMVVTSSTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQEVINKASNSNKIRLEKGRLYQIKIQYQRENPTEKGLDFKLYWTDSQNKKEVISSDNLQLPELKQKSSNSRKKRSTSAGPTVPDRDNDGIPDSLEVEGYTVDVKNKRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPLVAAYPIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEVHGNAEVHASFFDIGGSVSAGFSNSNSSTVAIDHSLSLAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPIALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNWSEVLPQIQETTARIIFNGKDLNLVERRIAAVNPSDPLETTKPDMTLKEALKIAFGFNEPNGNLQYQGKDITEFDFNFDQQTSQNIKNQLAELNATNIYTVLDKIKLNAKMNILIRDKRFHYDRNNIAVGADESVVKEAHREVINSSTEGLLLNIDKDIRKILSGYIVEIEDTEGLKEVINDRYDMLNISSLRQDGKTFIDFKKYNDKLPLYISNPNYKVNVYAVTKENTIINPSENGDTSTNGIKKILIFSKKGYEIG TT3YGCD TT Successful TT3YGCD RC R-HSA-5210891:Uptake and function of anthrax toxins TTAS2UO ID TTAS2UO TTAS2UO TN Bacterial Urease (Bact ureC) TTAS2UO UP P18314 TTAS2UO UC URE1_KLEAE TTAS2UO BC Carbon-nitrogen hydrolase TTAS2UO SN Urease subunit alpha; Urea amidohydrolase subunit alpha TTAS2UO GN Bact ureC TTAS2UO FC Catalyzes the hydrolysis of urea, leading to the production of carbon dioxide and ammonia. Allows many soil bacteria to use urea as a nitrogen source. An important virulence factor that improves survival of pathogenic bacteria under acidic conditions within the host and can also cause direct damage to the host tissue due to ammonia, CO2 or alkali production. TTAS2UO PD 4EPE; 4EPD; 4EPB; 4EP8; 2KAU TTAS2UO SQ MSNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVIRDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGNPDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQPDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTLNTIDEHLDMLMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDLGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVKRYIAKYTINPALTHGIAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGGMIAIAPMGDINASIPTPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGVAERLNLRSAIAVVKGCRTVQKADMVHNSLQPNITVDAQTYEVRVDGELITSEPADVLPMAQRYFLF TTAS2UO TT Successful TTRPKQG ID TTRPKQG TTRPKQG TN Beta-catenin (CTNNB1) TTRPKQG UP P35222 TTRPKQG UC CTNB1_HUMAN TTRPKQG BC Beta-catenin TTRPKQG SN Wnt/beta-catenin signaling pathway; PRO2286; OK/SW-cl.35; Catenin beta-1; CTNNB TTRPKQG GN CTNNB1 TTRPKQG FC In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle. Key downstream component of the canonical Wnt signaling pathway. TTRPKQG PD 6M94; 6M93; 6M92; 6M91; 6M90 TTRPKQG SQ MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL TTRPKQG TT Successful TTRPKQG KE hsa04015:Rap1 signaling pathway; hsa04310:Wnt signaling pathway; hsa04390:Hippo signaling pathway; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04530:Tight junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04670:Leukocyte transendothelial migration; hsa04916:Melanogenesis; hsa04919:Thyroid hormone signaling pathway; hsa05100:Bacterial invasion of epithelial cells; hsa05130:Pathogenic Escherichia coli infection; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05213:Endometrial cancer; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05217:Basal cell carcinoma; hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC) TTRPKQG RC R-HSA-201681:TCF dependent signaling in response to WNT; R-HSA-201722:Formation of the beta-catenin:TCF transactivating complex; R-HSA-3134973:LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production; R-HSA-375170:CDO in myogenesis; R-HSA-3769402:Deactivation of the beta-catenin transactivating complex; R-HSA-4086398:Ca2+ pathway; R-HSA-4411364:Binding of TCF/LEF:CTNNB1 to target gene promoters; R-HSA-4641262:Disassembly of the destruction complex and recruitment of AXIN to the membrane; R-HSA-5358747:S33 mutants of beta-catenin aren't phosphorylated; R-HSA-5358749:S37 mutants of beta-catenin aren't phosphorylated; R-HSA-5358751:S45 mutants of beta-catenin aren't phosphorylated; R-HSA-5358752:T41 mutants of beta-catenin aren't phosphorylated; R-HSA-5626467:RHO GTPases activate IQGAPs TTHS7CM ID TTHS7CM TTHS7CM TN Beta-glucuronidase (GUSB) TTHS7CM UP P08236 TTHS7CM UC BGLR_HUMAN TTHS7CM SN Beta-G1 TTHS7CM GN GUSB TTHS7CM FC Plays an important role in the degradation of dermatan and keratan sulfates. TTHS7CM EC EC 3.2.1.31 TTHS7CM PD 3HN3; 1BHG TTHS7CM SQ MARGSAVAWAALGPLLWGCALGLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFEEQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVVLRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTTLPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPTTYIDDITVTTSVEQDSGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYLYSLEVQLTAQTSLGPVSDFYTLPVGIRTVAVTKSQFLINGKPFYFHGVNKHEDADIRGKGFDWPLLVKDFNLLRWLGANAFRTSHYPYAEEVMQMCDRYGIVVIDECPGVGLALPQFFNNVSLHHHMQVMEEVVRRDKNHPAVVMWSVANEPASHLESAGYYLKMVIAHTKSLDPSRPVTFVSNSNYAADKGAPYVDVICLNSYYSWYHDYGHLELIQLQLATQFENWYKKYQKPIIQSEYGAETIAGFHQDPPLMFTEEYQKSLLEQYHLGLDQKRRKYVVGELIWNFADFMTEQSPTRVLGNKKGIFTRQRQPKSAAFLLRERYWKIANETRYPHSVAKSQCLENSLFT TTHS7CM TT Successful TTV3NH6 ID TTV3NH6 TTV3NH6 TN Calmodulin (CALM) TTV3NH6 UP P0DP23; P0DP24; P0DP25 TTV3NH6 UC CALM1_HUMAN; CALM2_HUMAN; CALM3_HUMAN TTV3NH6 BC Calmodulin-dependent secretion TTV3NH6 SN CaM; CALM2 TTV3NH6 GN CALM TTV3NH6 FC Calmodulin mediates the control of a largenumber of enzymes by ca(2+). Among the enzymes to be stimulated by the calmodulin-ca(2+) complex are a number of protein kinases and phosphatases. TTV3NH6 SQ MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK TTV3NH6 TT Successful TTV3NH6 KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04070:Phosphatidylinositol signaling system; hsa04114:Oocyte meiosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04728:Dopaminergic synapse; hsa04740:Olfactory transduction; hsa04744:Phototransduction; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04921:Oxytocin signaling pathway; hsa04922:Glucagon signaling pathway; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa05010:Alzheimer's disease; hsa05031:Amphetamine addiction; hsa05034:Alcoholism; hsa05133:Pertussis; hsa05152:Tuberculosis; hsa05214:Glioma TTV3NH6 RC R-HSA-111933:Calmodulin induced events; R-HSA-114608:Platelet degranulation; R-HSA-1445148:Translocation of GLUT4 to the plasma membrane; R-HSA-1474151:Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation; R-HSA-180024:DARPP-32 events; R-HSA-203615:eNOS activation; R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade; R-HSA-2871809:FCERI mediated Ca+2 mobilization; R-HSA-4086398:Ca2+ pathway; R-HSA-442729:CREB phosphorylation through the activation of CaMKII; R-HSA-442982:Ras activation uopn Ca2+ infux through NMDA receptor; R-HSA-445355:Smooth Muscle Contraction; R-HSA-5218920:VEGFR2 mediated vascular permeability; R-HSA-5218921:VEGFR2 mediated cell proliferation; R-HSA-5626467:RHO GTPases activate IQGAPs; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTFPKRB ID TTFPKRB TTFPKRB TN cAMP-dependent chloride channel F508 deletion (CFTR del F508) TTFPKRB UP P13569 (del F508) TTFPKRB UC CFTR_HUMAN TTFPKRB BC ABC transporter TTFPKRB SN cAMP-dependent chloride channel (del F508); Cystic fibrosis transmembrane conductance regulator (del F508); Channel conductance-controlling ATPase; CFTR; ATP-binding cassette sub-family C member 7 (del F508); ABCC7 (del F508) TTFPKRB GN CFTR TTFPKRB FC Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis. Mediates the transport of chloride ions across the cell membrane. Channel activity is coupled to ATP hydrolysis. The ion channel is also permeable to HCO(3-); selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Plays an important role in airway fluid homeostasis. Contributes to the regulation of the pH and the ion content of the airway surface fluid layer and thereby plays an important role in defense against pathogens. Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex. Inhibits the activity of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G. Inhibits the activity of the ENaC channel containing subunits SCNN1D, SCNN1B and SCNN1G, but not of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7. Can inhibit the chloride channel activity of ANO1. Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation. TTFPKRB EC EC 5.6.1.6 TTFPKRB PD 6MSM; 6HEP; 5UAK; 5TGK; 5TFJ TTFPKRB SQ MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL TTFPKRB TT Successful TTTSOUD ID TTTSOUD TTTSOUD TN Candida Cytochrome P450 51 (Candi ERG11) TTTSOUD UP P10613 TTTSOUD UC CP51_CANAL TTTSOUD BC Paired donor oxygen oxidoreductase TTTSOUD SN Sterol 14alpha-demethylase; Sterol 14-alpha demethylase; P450LI; P450L1; P450-14DM; Lanosterol 14 alpha-demethylase; LDM; Erg11p; ERG11; Cytochrome P450-dependent lanosterol 14-demethylase; Cytochrome P-450 lanosterol 14-alpha-demethylase; Cyt P450 14DM; CYPLI; CYPL1 TTTSOUD GN Candi ERG11 TTTSOUD FC Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. TTTSOUD PD 5V5Z; 5TZ1; 5FSA TTTSOUD SQ MAIVETVIDGINYFLSLSVTQQISILLGVPFVYNLVWQYLYSLRKDRAPLVFYWIPWFGSAASYGQQPYEFFESCRQKYGDVFSFMLLGKIMTVYLGPKGHEFVFNAKLSDVSAEDAYKHLTTPVFGKGVIYDCPNSRLMEQKKFAKFALTTDSFKRYVPKIREEILNYFVTDESFKLKEKTHGVANVMKTQPEITIFTASRSLFGDEMRRIFDRSFAQLYSDLDKGFTPINFVFPNLPLPHYWRRDAAQKKISATYMKEIKSRRERGDIDPNRDLIDSLLIHSTYKDGVKMTDQEIANLLIGILMGGQHTSASTSAWFLLHLGEKPHLQDVIYQEVVELLKEKGGDLNDLTYEDLQKLPSVNNTIKETLRMHMPLHSIFRKVTNPLRIPETNYIVPKGHYVLVSPGYAHTSERYFDNPEDFDPTRWDTAAAKANSVSFNSSDEVDYGFGKVSKGVSSPYLPFGGGRHRCIGEQFAYVQLGTILTTFVYNLRWTIDGYKVPDPDYSSMVVLPTEPAEIIWEKRETCMF TTTSOUD TT Successful TT915ZD ID TT915ZD TT915ZD TN Candida Mannose-6-phosphate isomerase (Candi PMI1) TT915ZD UP P34948 TT915ZD UC MPI_CANAL TT915ZD BC Intramolecular oxidoreductases TT915ZD SN Phosphomannose isomerase; Phosphohexomutase; PMI1; PMI TT915ZD GN Candi PMI1 TT915ZD FC Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. TT915ZD PD 5NW7; 1PMI TT915ZD SQ MSSEKLFRIQCGYQNYDWGKIGSSSAVAQFVHNSDPSITIDETKPYAELWMGTHPSVPSKAIDLNNQTLRDLVTAKPQEYLGESIITKFGSSKELPFLFKVLSIEKVLSIQAHPDKKLGAQLHAADPKNYPDDNHKPEMAIAVTDFEGFCGFKPLDQLAKTLATVPELNEIIGQELVDEFISGIKLPAEVGSQDDVNNRKLLQKVFGKLMNTDDDVIKQQTAKLLERTDREPQVFKDIDSRLPELIQRLNKQFPNDIGLFCGCLLLNHVGLNKGEAMFLQAKDPHAYISGDIIECMAASDNVVRAGFTPKFKDVKNLVEMLTYSYESVEKQKMPLQEFPRSKGDAVKSVLYDPPIAEFSVLQTIFDKSKGGKQVIEGLNGPSIVIATNGKGTIQITGDDSTKQKIDTGYVFFVAPGSSIELTADSANQDQDFTTYRAFVEA TT915ZD TT Successful TTULOB6 ID TTULOB6 TTULOB6 TN Cathelicidin antimicrobial peptide (CAMP) TTULOB6 UP P49913 TTULOB6 UC CAMP_HUMAN TTULOB6 BC Cathelicidin family TTULOB6 SN upregulating cAMP; hCAP18; CAP18; CAMP; Antibacterial protein LL37; 18 kDa cationic antimicrobial protein TTULOB6 GN CAMP TTULOB6 FC Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity. TTULOB6 SQ MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES TTULOB6 TT Successful TTULOB6 KE hsa04970:Salivary secretion; hsa05152:Tuberculosis TTULOB6 RC R-HSA-1222556:ROS production in response to bacteria TTJIH8Q ID TTJIH8Q TTJIH8Q TN CCR5 messenger RNA (CCR5 mRNA) TTJIH8Q UP P51681 TTJIH8Q UC CCR5_HUMAN TTJIH8Q BC mRNA target TTJIH8Q SN HIV-1 fusion coreceptor (mRNA); HIV-1 fusion co-receptor (mRNA); Chemokine receptor CCR5 (mRNA); CMKBR5 (mRNA); CHEMR13 (mRNA); CD195 antigen (mRNA); CD195 (mRNA); CCR-5 (mRNA); CC-CKR-5 (mRNA); C-C chemokine receptor type 5 (mRNA); C-C CKR-5 (mRNA) TTJIH8Q GN CCR5 TTJIH8Q FC May play a role in the control of granulocytic lineage proliferation or differentiation. Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. TTJIH8Q PD 6MET; 6MEO; 6FGP; 5YY4; 5YD5 TTJIH8Q SQ MDYQVSSPIYDINYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNMLVILILINCKRLKSMTDIYLLNLAISDLFFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAVVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQKEGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQEISVGL TTJIH8Q TT Successful TTJIH8Q FM mRNA target TTJIH8Q KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa05145:Toxoplasmosis; hsa05203:Viral carcinogenesis TTJIH8Q RC R-HSA-173107:Binding and entry of HIV virion; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TT30NW6 ID TT30NW6 TT30NW6 TN Chloride channel protein 2 (CLC-2) TT30NW6 UP P51788 TT30NW6 UC CLCN2_HUMAN TT30NW6 BC Chloride channel TT30NW6 SN ClC-2 chloride channel; ClC-2 Cl- channel; ClC-2; CLCN2 TT30NW6 GN CLCN2 TT30NW6 FC Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. TT30NW6 SQ MAAAAAEEGMEPRALQYEQTLMYGRYTQDLGAFAKEEAARIRLGGPEPWKGPPSSRAAPELLEYGRSRCARCRVCSVRCHKFLVSRVGEDWIFLVLLGLLMALVSWVMDYAIAACLQAQQWMSRGLNTSILLQYLAWVTYPVVLITFSAGFTQILAPQAVGSGIPEMKTILRGVVLKEYLTLKTFIAKVIGLTCALGSGMPLGKEGPFVHIASMCAALLSKFLSLFGGIYENESRNTEMLAAACAVGVGCCFAAPIGGVLFSIEVTSTFFAVRNYWRGFFAATFSAFIFRVLAVWNRDEETITALFKTRFRLDFPFDLQELPAFAVIGIASGFGGALFVYLNRKIVQVMRKQKTINRFLMRKRLLFPALVTLLISTLTFPPGFGQFMAGQLSQKETLVTLFDNRTWVRQGLVEELEPPSTSQAWNPPRANVFLTLVIFILMKFWMSALATTIPVPCGAFMPVFVIGAAFGRLVGESMAAWFPDGIHTDSSTYRIVPGGYAVVGAAALAGAVTHTVSTAVIVFELTGQIAHILPVMIAVILANAVAQSLQPSLYDSIIRIKKLPYLPELGWGRHQQYRVRVEDIMVRDVPHVALSCTFRDLRLALHRTKGRMLALVESPESMILLGSIERSQVVALLGAQLSPARRRQHMQERRATQTSPLSDQEGPPTPEASVCFQVNTEDSAFPAARGETHKPLKPALKRGPSVTRNLGESPTGSAESAGIALRSLFCGSPPPEAASEKLESCEKRKLKRVRISLASDADLEGEMSPEEILEWEEQQLDEPVNFSDCKIDPAPFQLVERTSLHKTHTIFSLLGVDHAYVTSIGRLIGIVTLKELRKAIEGSVTAQGVKVRPPLASFRDSATSSSDTETTEVHALWGPHSRHGLPREGSPSDSDDKCQ TT30NW6 TT Successful TT30NW6 KE hsa04978:Mineral absorption TT30NW6 RC R-HSA-2672351:Stimuli-sensing channels TTRHEQ4 ID TTRHEQ4 TTRHEQ4 TN Diacylglycerol O-acyltransferase 2 (DGAT2) TTRHEQ4 UP Q96PD7 TTRHEQ4 UC DGAT2_HUMAN TTRHEQ4 BC Acyltransferase TTRHEQ4 SN UNQ738/PRO1433; HMFN1045; Diglyceride acyltransferase 2 TTRHEQ4 GN DGAT2 TTRHEQ4 FC Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides. Functions also as an acyl-CoA retinol acyltransferase (ARAT). Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. TTRHEQ4 EC EC 2.3.1.20 TTRHEQ4 SQ MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHTMYMEALVKLFDKHKTKFGLPETEVLEVN TTRHEQ4 TT Successful TTRHEQ4 FM Acyltransferase TTRHEQ4 KE hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways; hsa04975:Fat digestion and absorption TTRHEQ4 RC R-HSA-1482883:Acyl chain remodeling of DAG and TAG; R-HSA-75109:Triglyceride Biosynthesis TTZPS91 ID TTZPS91 TTZPS91 TN Dihydrothymine dehydrogenase (DPYD) TTZPS91 UP Q12882 TTZPS91 UC DPYD_HUMAN TTZPS91 BC CH/CH donor oxidoreductase TTZPS91 SN Dihydrouracil dehydrogenase; Dihydropyrimidine dehydrogenase [NADP(+)]; Dihydropyrimidine dehydrogenase; DPD; DHPDHase TTZPS91 GN DPYD TTZPS91 FC Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil. Involved in pyrimidine base degradation. TTZPS91 EC EC 1.3.1.2 TTZPS91 SQ MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCFNCEKLENNFDDIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQFATEVFKAMSIPQIRNPSLPPPEKMSEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNEMTLSTLKEKGYKAAFIGIGLPEPNKDAIFQGLTQDQGFYTSKDFLPLVAKGSKAGMCACHSPLPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWNEDEDQMVHLKADVVISAFGSVLSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQYGASVSAKPELPLFYTPIDLVDISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQSPATVSHQKGKPVPRIAELMDKKLPSFGPYLEQRKKIIAENKIRLKEQNVAFSPLKRNCFIPKRPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKMVSRTTPYEPKRGVPLSVNPVC TTZPS91 TT Successful TTZPS91 FM Dihydropyrimidine dehydrogenase TTZPS91 KE hsa00240:Pyrimidine metabolism; hsa00410:beta-Alanine metabolism; hsa00770:Pantothenate and CoA biosynthesis; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways TT0IHXV ID TT0IHXV TT0IHXV TN DNA topoisomerase II (TOP2) TT0IHXV UP P11388; Q02880 TT0IHXV UC TOP2A_HUMAN; TOP2B_HUMAN TT0IHXV BC ATP-hydrolyzing DNA topoisomerase TT0IHXV SN TOP2; DNA topoisomerase 2 TT0IHXV GN TOP2A; TOP2B TT0IHXV FC Cut both strands of the DNA helix simultaneously in order to manage DNA tangles and supercoils. TT0IHXV SQ MEVSPLQPVNENMQVNKIKKNEDAKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVKGFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKNKGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQVQLNKKCSAVKHNRIKGIPKLDDANDAGGRNSTECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEMAFYSLPEFEEWKSSTPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQIDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQTTTYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSSLARLLFPPKDDHTLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREIVNNIRRLMDGEEPLPMLPSYKNFKGTIEELAPNQYVISGEVAILNSTTIEISELPVRTWTQTYKEQVLEPMLNGTEKTPPLITDYREYHTDTTVKFVVKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESAKLNNQARFILEKIDGKIIIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPDEEENEESDNEKETEKSDSVTDSGPTFNYLLDMPLWYLTKEKKDELCRLRNEKEQELDTLKRKSPSDLWKEDLATFIEELEAVEAKEKQDEQVGLPGKGGKAKGKKTQMAEVLPSPRGQRVIPRITIEMKAEAEKKNKKKIKNENTEGSPQEDGVELEGLKQRLEKKQKREPGTKTKKQTTLAFKPIKKGKKRNPWSDSESDRSSDESNFDVPPRETEPRRAATKTKFTMDLDSDEDFSDFDEKTDDEDFVPSDASPPKTKTSPKLSNKELKPQKSVVSDLEADDVKGSVPLSSSPPATHFPDETEITNPVPKKNVTVKKTAAKSQSSTSTTGAKKRAAPKGTKRDPALNSGVSQKPDPAKTKNRRKRKPSTSDDSDSNFEKIVSKAVTSKKSKGESDDFHMDFDSAVAPRAKSVRAKKPIKYLEESDEDDLF TT0IHXV TT Successful TTED8JB ID TTED8JB TTED8JB TN Epidermal growth factor (EGF) TTED8JB UP P01133 TTED8JB UC EGF_HUMAN TTED8JB BC Growth factor TTED8JB SN Proepidermal growth factor; Pro-epidermal growth factor TTED8JB GN EGF TTED8JB FC Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. Can induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. TTED8JB PD 3NJP; 2KV4; 1P9J; 1NQL; 1JL9 TTED8JB SQ MLLTLIILLPVVSKFSFVSLSAPQHWSCPEGTLAGNGNSTCVGPAPFLIFSHGNSIFRIDTEGTNYEQLVVDAGVSVIMDFHYNEKRIYWVDLERQLLQRVFLNGSRQERVCNIEKNVSGMAINWINEEVIWSNQQEGIITVTDMKGNNSHILLSALKYPANVAVDPVERFIFWSSEVAGSLYRADLDGVGVKALLETSEKITAVSLDVLDKRLFWIQYNREGSNSLICSCDYDGGSVHISKHPTQHNLFAMSLFGDRIFYSTWKMKTIWIANKHTGKDMVRINLHSSFVPLGELKVVHPLAQPKAEDDTWEPEQKLCKLRKGNCSSTVCGQDLQSHLCMCAEGYALSRDRKYCEDVNECAFWNHGCTLGCKNTPGSYYCTCPVGFVLLPDGKRCHQLVSCPRNVSECSHDCVLTSEGPLCFCPEGSVLERDGKTCSGCSSPDNGGCSQLCVPLSPVSWECDCFPGYDLQLDEKSCAASGPQPFLLFANSQDIRHMHFDGTDYGTLLSQQMGMVYALDHDPVENKIYFAHTALKWIERANMDGSQRERLIEEGVDVPEGLAVDWIGRRFYWTDRGKSLIGRSDLNGKRSKIITKENISQPRGIAVHPMAKRLFWTDTGINPRIESSSLQGLGRLVIASSDLIWPSGITIDFLTDKLYWCDAKQSVIEMANLDGSKRRRLTQNDVGHPFAVAVFEDYVWFSDWAMPSVMRVNKRTGKDRVRLQGSMLKPSSLVVVHPLAKPGADPCLYQNGGCEHICKKRLGTAWCSCREGFMKASDGKTCLALDGHQLLAGGEVDLKNQVTPLDILSKTRVSEDNITESQHMLVAEIMVSDQDDCAPVGCSMYARCISEGEDATCQCLKGFAGDGKLCSDIDECEMGVPVCPPASSKCINTEGGYVCRCSEGYQGDGIHCLDIDECQLGEHSCGENASCTNTEGGYTCMCAGRLSEPGLICPDSTPPPHLREDDHHYSVRNSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELRHAGHGQQQKVIVVAVCVVVLVMLLLLSLWGAHYYRTQKLLSKNPKNPYEESSRDVRSRRPADTEDGMSSCPQPWFVVIKEHQDLKNGGQPVAGEDGQAADGSMQPTSWRQEPQLCGMGTEQGCWIPVSSDKGSCPQVMERSFHMPSYGTQTLEGGVEKPHSLLSANPLWQQRALDPPHQMELTQ TTED8JB TT Successful TTED8JB KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04540:Gap junction; hsa04810:Regulation of actin cytoskeleton; hsa05160:Hepatitis C; hsa05200:Pathways in cancer; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05223:Non-small cell lung cancer; hsa05231:Choline metabolism in cancer TTED8JB RC R-HSA-114608:Platelet degranulation; R-HSA-1236382:Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1250196:SHC1 events in ERBB2 signaling; R-HSA-1251932:PLCG1 events in ERBB2 signaling; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-179812:GRB2 events in EGFR signaling; R-HSA-180292:GAB1 signalosome; R-HSA-180336:SHC1 events in EGFR signaling; R-HSA-182971:EGFR downregulation; R-HSA-1963640:GRB2 events in ERBB2 signaling; R-HSA-1963642:PI3K events in ERBB2 signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5637810:Constitutive Signaling by EGFRvIII; R-HSA-5673001:RAF/MAP kinase cascade TTIV96N ID TTIV96N TTIV96N TN Fatty acid-binding protein 1 (FABP1) TTIV96N UP P07148 TTIV96N UC FABPL_HUMAN TTIV96N SN L-FABP; FABP1; 14-kDa fatty-acid binding protein; 14 kDa selenium-binding protein TTIV96N GN FABP1 TTIV96N FC Binds free fatty acids andtheir coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. TTIV96N PD 6DRG; 6DO7; 6DO6; 3VG7; 3VG6 TTIV96N SQ MSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTVVQLEGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI TTIV96N TT Successful TTIV96N KE hsa03320:PPAR signaling pathway; hsa04975:Fat digestion and absorption TTIV96N RC R-HSA-163560:Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis; R-HSA-1989781:PPARA activates gene expression; R-HSA-400206:Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha) TTMS54D ID TTMS54D TTMS54D TN Fragile histidine triad protein (FHIT) TTMS54D UP P49789 TTMS54D UC FHIT_HUMAN TTMS54D BC Acid anhydride hydrolase TTMS54D SN Fragile histidinetriad protein; Fragile histidinetriad (FHIT) gene; Dinucleosidetriphosphatase; Diadenosine 5',5'''-P1,P3-triphosphate hydrolase; Bis(5'-adenosyl)-triphosphatase; AP3AASE; AP3A hydrolase TTMS54D GN FHIT TTMS54D FC Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor. Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. TTMS54D EC EC 3.6.1.29 TTMS54D PD 6FIT; 5FIT; 4FIT; 3FIT; 2FIT TTMS54D SQ MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKHDKEDFPASWRSEEEMAAEAAALRVYFQ TTMS54D TT Successful TTMS54D FM Acid anhydrides hydrolase TT0SFXH ID TT0SFXH TT0SFXH TN Fungal 1,3-beta-glucan synthase (Fung GSC2) TT0SFXH UP P40989 TT0SFXH UC FKS2_YEAST TT0SFXH BC Hexosyltransferase TT0SFXH SN GSC2 TT0SFXH GN Fung GSC2 TT0SFXH FC Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Involved in cell wall synthesis, maintenance and cell wall remodeling. TT0SFXH EC EC 2.4.1.34 TT0SFXH SQ MSYNDPNLNGQYYSNGDGTGDGNYPTYQVTQDQSAYDEYGQPIYTQNQLDDGYYDPNEQYVDGTQFPQGQDPSQDQGPYNNDASYYNQPPNMMNPSSQDGENFSDFSSYGPPSGTYPNDQYTPSQMSYPDQDGSSGASTPYGNGVVNGNGQYYDPNAIEMALPNDPYPAWTADPQSPLPIEQIEDIFIDLTNKFGFQRDSMRNMFDHFMTLLDSRSSRMSPEQALLSLHADYIGGDTANYKKWYFAAQLDMDDEIGFRNMKLGKLSRKARKAKKKNKKAMQEASPEDTEETLNQIEGDNSLEAADFRWKSKMNQLSPFEMVRQIALFLLCWGEANQVRFTPECLCFIYKCASDYLDSAQCQQRPDPLPEGDFLNRVITPLYRFIRSQVYEIVDGRYVKSEKDHNKVIGYDDVNQLFWYPEGIAKIVMEDGTRLIDLPAEERYLKLGEIPWDDVFFKTYKETRSWLHLVTNFNRIWIMHISVYWMYCAYNAPTFYTHNYQQLVDNQPLAAYKWATAALGGTVASLIQVAATLCEWSFVPRKWAGAQHLSRRFWFLCVIMGINLGPVIFVFAYDKDTVYSTAAHVVGAVMFFVAVATLVFFSVMPLGGLFTSYMKKSTRSYVASQTFTASFAPLHGLDRWMSYLVWVTVFAAKYAESYFFLILSLRDPIRILSTTSMRCTGEYWWGNKICKVQPKIVLGLMIATDFILFFLDTYLWYIVVNTVFSVGKSFYLGISILTPWRNIFTRLPKRIYSKILATTDMEIKYKPKVLISQIWNAIIISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRDSEAERRISFFAQSLSTPIPEPLPVDNMPTFTVLTPHYAERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWDCFVKDTKILAEETAAYENNEDEPEKEDALKSQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNADGLERELEKMARRKFKFLVSMQRLAKFKPHELENAEFLLRAYPDLQIAYLDEEPPLNEGEEPRIYSALIDGHCEILENGRRRPKFRVQLSGNPILGDGKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELGIEQIHPYTPGLKYEDQSTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLAQIGGKLHYGHPDFINATFMTTRGGVSKAQKGLHLNEDIYAGMNAVLRGGRIKHCEYYQCGKGRDLGFGTILNFTTKIGAGMGEQMLSREYYYLGTQLPIDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLHALAHESILCVYDRDKPITDVLYPIGCYNFHPAIDWVRRYTLSIFIVFWIAFVPIVVQELIERGLWKATQRFFRHILSLSPMFEVFAGQIYSSALLSDIAVGGARYISTGRGFATSRIPFSILYSRFAGSAIYMGSRSMLMLLFGTVAHWQAPLLWFWASLSALIFAPFIFNPHQFAWEDFFLDYRDYIRWLSRGNNKYHRNSWIGYVRMSRSRVTGFKRKLVGDESEKSAGDASRAHRTNLIMAEIIPCAIYAAGCFIAFTFINAQTGVKTTDEDRVNSTLRIIICTLAPIVIDIGVLFFCMGLSCCSGPLLGMCCKKTGSVMAGIAHGIAVVVHIVFFIVMWVLEGFSFVRMLIGVVTCIQCQRLIFHCMTVLLLTREFKNDHANTAFWTGKWYSTGLGYMAWTQPTRELTAKVIELSEFAADFVLGHVILIFQLPVICIPKIDKFHSIMLFWLKPSRQIRPPIYSLKQARLRKRMVRRYCSLYFLVLIIFAGCIVGPAVASAHVPKDLGSGLTGTFHNLVQPRNVSNNDTGSQMSTYKSHYYTHTPSLKTWSTIK TT0SFXH TT Successful TT0SFXH KE sce00500:Starch and sucrose metabolism; sce04011:MAPK signaling pathway - yeast TTBMV1G ID TTBMV1G TTBMV1G TN GABA(A) receptor alpha-2 (GABRA2) TTBMV1G UP P47869 TTBMV1G UC GBRA2_HUMAN TTBMV1G BC Neurotransmitter receptor TTBMV1G SN GABRA2; GABA-A receptor alpha 2; GABA(A)Gamma-aminobutyric-acid receptor alpha-2 subunit precursor receptor TTBMV1G GN GABRA2 TTBMV1G FC GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. TTBMV1G SQ MKTKLNIYNMQFLLFVFLVWDPARLVLANIQEDEAKNNITIFTRILDRLLDGYDNRLRPGLGDSITEVFTNIYVTSFGPVSDTDMEYTIDVFFRQKWKDERLKFKGPMNILRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRIQDDGTLLYTMRLTVQAECPMHLEDFPMDAHSCPLKFGSYAYTTSEVTYIWTYNASDSVQVAPDGSRLNQYDLLGQSIGKETIKSSTGEYTVMTAHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGWAWDGKSVVNDKKKEKASVMIQNNAYAVAVANYAPNLSKDPVLSTISKSATTPEPNKKPENKPAEAKKTFNSVSKIDRMSRIVFPVLFGTFNLVYWATYLNREPVLGVSP TTBMV1G TT Successful TTBMV1G KE hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction TTBMV1G RC R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation TTGXH6N ID TTGXH6N TTGXH6N TN GABA(A) receptor delta (GABRD) TTGXH6N UP O14764 TTGXH6N UC GBRD_HUMAN TTGXH6N BC Ligand-gated ion channel TTGXH6N SN Gammaaminobutyric acid receptor subunit delta; GABRD; GABA(A) receptor subunit delta TTGXH6N GN GABRD TTGXH6N FC GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. TTGXH6N SQ MDAPARLLAPLLLLCAQQLRGTRAMNDIGDYVGSNLEISWLPNLDGLIAGYARNFRPGIGGPPVNVALALEVASIDHISEANMEYTMTVFLHQSWRDSRLSYNHTNETLGLDSRFVDKLWLPDTFIVNAKSAWFHDVTVENKLIRLQPDGVILYSIRITSTVACDMDLAKYPMDEQECMLDLESYGYSSEDIVYYWSESQEHIHGLDKLQLAQFTITSYRFTTELMNFKSAGQFPRLSLHFHLRRNRGVYIIQSYMPSVLLVAMSWVSFWISQAAVPARVSLGITTVLTMTTLMVSARSSLPRASAIKALDVYFWICYVFVFAALVEYAFAHFNADYRKKQKAKVKVSRPRAEMDVRNAIVLFSLSAAGVTQELAISRRQRRVPGNLMGSYRSVGVETGETKKEGAARSGGQGGIRARLRPIDADTIDIYARAVFPAAFAAVNVIYWAAYAM TTGXH6N TT Successful TTGXH6N KE hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction TT1YWO5 ID TT1YWO5 TT1YWO5 TN Glucagon-like peptide 2 receptor (GLP2R) TT1YWO5 UP O95838 TT1YWO5 UC GLP2R_HUMAN TT1YWO5 BC GPCR secretin TT1YWO5 SN GLP2R; GLP2 receptor TT1YWO5 GN GLP2R TT1YWO5 FC This is a receptor for glucagon-like peptide 2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. TT1YWO5 SQ MKLGSSRAGPGRGSAGLLPGVHELPMGIPAPWGTSPLSFHRKCSLWAPGRPFLTLVLLVSIKQVTGSLLEETTRKWAQYKQACLRDLLKEPSGIFCNGTFDQYVCWPHSSPGNVSVPCPSYLPWWSEESSGRAYRHCLAQGTWQTIENATDIWQDDSECSENHSFKQNVDRYALLSTLQLMYTVGYSFSLISLFLALTLLLFLRKLHCTRNYIHMNLFASFILRTLAVLVKDVVFYNSYSKRPDNENGWMSYLSEMSTSCRSVQVLLHYFVGANYLWLLVEGLYLHTLLEPTVLPERRLWPRYLLLGWAFPVLFVVPWGFARAHLENTGCWTTNGNKKIWWIIRGPMMLCVTVNFFIFLKILKLLISKLKAHQMCFRDYKYRLAKSTLVLIPLLGVHEILFSFITDDQVEGFAKLIRLFIQLTLSSFHGFLVALQYGFANGEVKAELRKYWVRFLLARHSGCRACVLGKDFRFLGKCPKKLSEGDGAEKLRKLQPSLNSGRLLHLAMRGLGELGAQPQQDHARWPRGSSLSECSEGDVTMANTMEEILEESEI TT1YWO5 TT Successful TT1YWO5 KE hsa04080:Neuroactive ligand-receptor interaction TT1YWO5 RC R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors TT7QNVC ID TT7QNVC TT7QNVC TN Glucose-dependent insulinotropic receptor (GPR119) TT7QNVC UP Q8TDV5 TT7QNVC UC GP119_HUMAN TT7QNVC BC GPCR rhodopsin TT7QNVC SN GPR119; G-protein coupled receptor 119 TT7QNVC GN GPR119 TT7QNVC FC Receptor for the endogenous fatty-acid ethanolamide oleoylethanolamide (OEA) and lysophosphatidylcholine (LPC). Functions as a glucose-dependent insulinotropic receptor. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Seems to act through a G(s) mediated pathway. TT7QNVC SQ MESSFSFGVILAVLASLIIATNTLVAVAVLLLIHKNDGVSLCFTLNLAVADTLIGVAISGLLTDQLSSPSRPTQKTLCSLRMAFVTSSAAASVLTVMLITFDRYLAIKQPFRYLKIMSGFVAGACIAGLWLVSYLIGFLPLGIPMFQQTAYKGQCSFFAVFHPHFVLTLSCVGFFPAMLLFVFFYCDMLKIASMHSQQIRKMEHAGAMAGGYRSPRTPSDFKALRTVSVLIGSFALSWTPFLITGIVQVACQECHLYLVLERYLWLLGVGNSLLNPLIYAYWQKEVRLQLYHMALGVKKVLTSFLLFLSARNCGPERPRESSCHIVTISSSEFDG TT7QNVC TT Successful TT7QNVC KE hsa04024:cAMP signaling pathway; hsa04911:Insulin secretion TT38RM1 ID TT38RM1 TT38RM1 TN Glycoprotein IIb/IIIa receptor (GPIIb/IIIa) TT38RM1 UP P08514; P05106 TT38RM1 UC ITA2B_HUMAN; ITB3_HUMAN TT38RM1 SN Platelet membrane glycoprotein IIb; Platelet membrane glycoprotein IIIa; GP TT38RM1 GN ITGA2B; ITGB3 TT38RM1 FC Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha- IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface. TT38RM1 SQ MARALCPLQALWLLEWVLLLLGPCAAPPAWALNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAPRTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVGSQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTEEAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDFSWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPVADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVAVGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRLRGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADRKLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAIAPLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLRSRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAYGANQVAVYRAQPVVKASVQLLVQDSLNPAVKSCVLPQTKTPVSCFNIQMCVGATGHNIPQKLSLNAELQLDRQKPRQGRRVLLLGSQQAGTTLNLDLGGKHSPICHTTMAFLRDEADFRDKLSPIVLSLNVSLPPTEAGMAPAVVLHGDTHVQEQTRIVLDCGEDDVCVPQLQLTASVTGSPLLVGADNVLELQMDAANEGEGAYEAELAVHLPQGAHYMRALSNVEGFERLICNQKKENETRVVLCELGNPMKKNAQIGIAMLVSVGNLEEAGESVSFQLQIRSKNSQNPNSKIVLLDVPVRAEAQVELRGNSFPASLVVAAEEGEREQNSLDSWGPKVEHTYELHNNGPGTVNGLHLSIHLPGQSQPSDLLYILDIQPQGGLQCFPQPPVNPLKVDWGLPIPSPSPIHPAHHKRDRRQIFLPEPEQPSRLQDPVLVSCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPLDQFVLQSHAWFNVSSLPYAVPPLSLPRGEAQVWTQLLRALEERAIPIWWVLVGVLGGLLLLTILVLAMWKVGFFKRNRPPLEEDDEEGE TT38RM1 TT Successful TT38RM1 RC R-HSA-114608:Platelet degranulation; R-HSA-1566948:Elastic fibre formation; R-HSA-210990:PECAM1 interactions; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-354194:GRB2:SOS provides linkage to MAPK signaling for Integrins; R-HSA-372708:p130Cas linkage to MAPK signaling for integrins; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5674135:MAP2K and MAPK activation TTG4R8V ID TTG4R8V TTG4R8V TN Growth hormone-releasing hormone receptor (GHRHR) TTG4R8V UP Q02643 TTG4R8V UC GHRHR_HUMAN TTG4R8V BC GPCR secretin TTG4R8V SN GRFR; GRF receptor; GHRHR; GHRH receptor TTG4R8V GN GHRHR TTG4R8V FC Receptor for GRF,coupled to G proteins which activate adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone gene transcription and growth hormone secretion. TTG4R8V PD 2XDG TTG4R8V SQ MDRRMWGAHVFCVLSPLPTVLGHMHPECDFITQLREDESACLQAAEEMPNTTLGCPATWDGLLCWPTAGSGEWVTLPCPDFFSHFSSESGAVKRDCTITGWSEPFPPYPVACPVPLELLAEEESYFSTVKIIYTVGHSISIVALFVAITILVALRRLHCPRNYVHTQLFTTFILKAGAVFLKDAALFHSDDTDHCSFSTVLCKVSVAASHFATMTNFSWLLAEAVYLNCLLASTSPSSRRAFWWLVLAGWGLPVLFTGTWVSCKLAFEDIACWDLDDTSPYWWIIKGPIVLSVGVNFGLFLNIIRILVRKLEPAQGSLHTQSQYWRLSKSTLFLIPLFGIHYIIFNFLPDNAGLGIRLPLELGLGSFQGFIVAILYCFLNQEVRTEISRKWHGHDPELLPAWRTRAKWTTPSRSAAKVLTSMC TTG4R8V TT Successful TTG4R8V KE hsa04080:Neuroactive ligand-receptor interaction TTG4R8V RC R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors TTS5K1M ID TTS5K1M TTS5K1M TN Hepatitis B virus Reverse transcriptase (HBV RT) TTS5K1M UP P03159 (359-602) TTS5K1M UC DPOL_HBVA3 TTS5K1M BC DNA-directed DNA polymerase TTS5K1M SN P; HBV reverse transcriptase TTS5K1M GN HBV RT TTS5K1M FC Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse- transcribed inside the nucleocapsid. Initiation of reverse- transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'- end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, theRC- DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery. TTS5K1M EC EC 2.7.7.49 TTS5K1M SQ EHHIRIPRTPARVTGGVFLVDKNPHNTAESRLVVDFSQFSRGISRVSWPKFAVPNLQSLTNLLSSNLSWLSLDVSAAFYHIPLHPAAMPHLLIGSSGLSRYVARLSSNSRINNNQYGTMQNLHDSCSRQLYVSLMLLYKTYGWKLHLYSHPIVLGFRKIPMGVGLSPFLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGAKSVQHRESLYTAVTNFLLSLGIHLNPNKTKRWGYSLNFMGYII TTS5K1M TT Successful TTXVOJ5 ID TTXVOJ5 TTXVOJ5 TN Human immunodeficiency virus Envelope messenger RNA (HIV env mRNA) TTXVOJ5 UP P04578 TTXVOJ5 UC ENV_HV1H2 TTXVOJ5 BC mRNA target TTXVOJ5 SN HIV-1 HXB2 envelope glycoprotein gp160 (mRNA); HIV-1 HXB2 env polyprotein (mRNA) TTXVOJ5 GN HIV env mRNA TTXVOJ5 FC Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. TTXVOJ5 PD 6DLN; 6DE7; 6BXQ; 6BXP; 6B9K TTXVOJ5 SQ MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL TTXVOJ5 TT Successful TTXVOJ5 FM mRNA target TT7KTSR ID TT7KTSR TT7KTSR TN Immunoglobulin gamma Fc receptor III (FCGR3) TT7KTSR UP P08637; O75015 TT7KTSR UC FCG3A_HUMAN; FCG3B_HUMAN TT7KTSR BC Immunoglobulin TT7KTSR SN Low affinity immunoglobulin gamma Fc region receptor III; IgG Fc receptor III; IGFR3; FcRIIIb; FcRIIIa; FcRIII; FcR-10; Fc-gamma RIII; FCGR3; FCG3; CD16 TT7KTSR GN FCGR3A; FCGR3B TT7KTSR FC Receptor for the Fc region of IgG. Binds complexed or aggregated IgG and also monomeric IgG. Mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis. TT7KTSR SQ MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQWFHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKNVSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDWKDHKFKWRKDPQDK TT7KTSR TT Successful TT7KTSR KE hsa04145:Phagosome; hsa04380:Osteoclast differentiation; hsa04650:Natural killer cell mediated cytotoxicity; hsa04666:Fc gamma R-mediated phagocytosis; hsa05140:Leishmaniasis; hsa05150:Staphylococcus aureus infection; hsa05152:Tuberculosis; hsa05322:Systemic lupus erythematosus TTZOPHG ID TTZOPHG TTZOPHG TN Insulin (INS) TTZOPHG UP P01308 TTZOPHG UC INS_HUMAN TTZOPHG SN Insulin TTZOPHG GN INS TTZOPHG FC Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. TTZOPHG PD 6HN5; 6CK2; 6CEB; 6CE9; 6CE7 TTZOPHG SQ MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN TTZOPHG TT Successful TTZOPHG FM Insulin family TTZOPHG KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04114:Oocyte meiosis; hsa04140:Regulation of autophagy; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04911:Insulin secretion; hsa04913:Ovarian steroidogenesis; hsa04914:Progesterone-mediated oocyte maturation; hsa04917:Prolactin signaling pathway; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04940:Type I diabetes mellitus; hsa04950:Maturity onset diabetes of the young; hsa04960:Aldosterone-regulated sodium reabsorption; hsa05215:Prostate cancer TTZOPHG RC R-HSA-210745:Regulation of gene expression in beta cells; R-HSA-264876:Insulin processing; R-HSA-422356:Regulation of insulin secretion; R-HSA-74713:IRS activation; R-HSA-74749:Signal attenuation; R-HSA-74751:Insulin receptor signalling cascade; R-HSA-77387:Insulin receptor recycling TTZPLJS ID TTZPLJS TTZPLJS TN Interleukin 11 receptor alpha (IL11RA) TTZPLJS UP Q14626 TTZPLJS UC I11RA_HUMAN TTZPLJS BC Cytokine receptor TTZPLJS SN Interleukin-11 receptor subunit alpha; IL-11RA; IL-11R-alpha; IL-11R subunit alpha; IL-11 receptor subunit alpha TTZPLJS GN IL11RA TTZPLJS FC The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells. Essential for the normal development of craniofacial bones and teeth. Restricts suture fusion and tooth number. Receptor for interleukin-11. TTZPLJS SQ MSSSCSGLSRVLVAVATALVSASSPCPQAWGPPGVQYGQPGRSVKLCCPGVTAGDPVSWFRDGEPKLLQGPDSGLGHELVLAQADSTDEGTYICQTLDGALGGTVTLQLGYPPARPVVSCQAADYENFSCTWSPSQISGLPTRYLTSYRKKTVLGADSQRRSPSTGPWPCPQDPLGAARCVVHGAEFWSQYRINVTEVNPLGASTRLLDVSLQSILRPDPPQGLRVESVPGYPRRLRASWTYPASWPCQPHFLLKFRLQYRPAQHPAWSTVEPAGLEEVITDAVAGLPHAVRVSARDFLDAGTWSTWSPEAWGTPSTGTIPKEIPAWGQLHTQPEVEPQVDSPAPPRPSLQPHPRLLDHRDSVEQVAVLASLGILSFLGLVAGALALGLWLRLRRGGKDGSPKPGFLASVIPVDRRPGAPNL TTZPLJS TT Successful TTZPLJS KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage TTQTX98 ID TTQTX98 TTQTX98 TN Interleukin-37 (IL37) TTQTX98 UP Q9NZH6 TTQTX98 UC IL37_HUMAN TTQTX98 BC Cytokine: interleukin TTQTX98 SN Interleukin-1-related protein; Interleukin-1 zeta; Interleukin-1 homolog 4; Interleukin-1 family member 7; IL1RP1; IL1H4; IL1F7; IL-37; IL-1X; IL-1RP1; IL-1H4; IL-1H; IL-1F7; IL-1 zeta; FIL1Z; FIL1 zeta TTQTX98 GN IL37 TTQTX98 FC Suppressor of innate inflammatory and immune responses involved in curbing excessive inflammation. This function requires SMAD3. Suppresses, or reduces, proinflammatory cytokine production, including IL1A and IL6, as well as CCL12, CSF1, CSF2, CXCL13, IL1B, IL23A and IL1RN, but spares anti-inflammatory cytokines. Inhibits dendritic cell activation. TTQTX98 PD 6NCU; 5HN1 TTQTX98 SQ MSFVGENSGVKMGSEDWEKDEPQCCLEDPAGSPLEPGPSLPTMNFVHTSPKVKNLNPKKFSIHDQDHKVLVLDSGNLIAVPDKNYIRPEIFFALASSLSSASAEKGSPILLGVSKGEFCLYCDKDKGQSHPSLQLKKEKLMKLAAQKESARRPFIFYRAQVGSWNMLESAAHPGWFICTSCNCNEPVGVTDKFENRKHIEFSFQPVCKAEMSPSEVSD TTQTX98 TT Successful TTQTX98 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04061:Viral protein interaction with cytokine and cytokine receptor TTG140O ID TTG140O TTG140O TN Inward rectifier potassium channel Kir1.2 (KCNJ10) TTG140O UP P78508 TTG140O UC KCJ10_HUMAN TTG140O BC Inward rectifier potassium channel TTG140O SN Potassiumchannel, inwardly rectifying, subfamily J, member 10; Potassium channel, inwardly rectifying subfamily J member 10; Inward rectifier K+ channel Kir1.2; Inward rectifier K(+) channel Kir1.2; ATP-sensitive inward rectifier potassium channel 10; ATP-dependent inwardly rectifying potassium channel Kir4.1; ATP dependent K+ channel TTG140O GN KCNJ10 TTG140O FC Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium. In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules. May be responsible for potassium buffering action of glial cells in the brain. TTG140O SQ MTSVAKVYYSQTTQTESRPLMGPGIRRRRVLTKDGRSNVRMEHIADKRFLYLKDLWTTFIDMQWRYKLLLFSATFAGTWFLFGVVWYLVAVAHGDLLELDPPANHTPCVVQVHTLTGAFLFSLESQTTIGYGFRYISEECPLAIVLLIAQLVLTTILEIFITGTFLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANMRKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDTASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVLILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSASGKYIADFSLFDQVVKVASPSGLRDSTVRYGDPEKLKLEESLREQAEKEGSALSVRISNV TTG140O TT Successful TTG140O FM Inward rectifier K(+) channel TTG140O KE hsa04971:Gastric acid secretion TTG140O RC R-HSA-1296041:Activation of G protein gated Potassium channels; R-HSA-997272:Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits TTDTWV0 ID TTDTWV0 TTDTWV0 TN Isocitrate dehydrogenase (IDH) TTDTWV0 UP O75874; P48735; P50213; O43837; P51553 TTDTWV0 UC IDHC_HUMAN; IDHP_HUMAN; IDH3A_HUMAN; IDH3B_HUMAN; IDH3G_HUMAN TTDTWV0 BC CH-OH donor oxidoreductase TTDTWV0 SN Isocitrate dehydrogenase [NAD] TTDTWV0 GN IDH1; IDH2; IDH3A; IDH3B; IDH3G TTDTWV0 FC It may tightly associate or interact with the pyruvate dehydrogenase complex. Plays a role in intermediary metabolism and energy production. TTDTWV0 SQ MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL TTDTWV0 TT Successful TTDTWV0 FM Short-chain dehydrogenases reductases TTDTWV0 KE hsa00020:Citrate cycle (TCA cycle); hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa01210:2-Oxocarboxylic acid metabolism; hsa01230:Biosynthesis of amino acids; hsa04146:Peroxisome TT0ID4A ID TT0ID4A TT0ID4A TN Leutinizing-hormone-releasing hormone (GNRH1) TT0ID4A UP P01148 TT0ID4A UC GON1_HUMAN TT0ID4A BC Gonadotropin-releasing hormone TT0ID4A SN Progonadoliberin-1; Progonadoliberin I; LHRH; GRH; GNRH TT0ID4A GN GNRH1 TT0ID4A FC Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones. TT0ID4A PD 4D5M TT0ID4A SQ MKPIQKLLAGLILLTWCVEGCSSQHWSYGLRPGGKRDAENLIDSFQEIVKEVGQLAETQRFECTTHQPRSPLRDLKGALESLIEEETGQKKI TT0ID4A TT Successful TT0ID4A KE hsa04912:GnRH signaling pathway TT0ID4A RC R-HSA-375281:Hormone ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTXDKTO ID TTXDKTO TTXDKTO TN Long transient receptor potential channel 8 (TRPM8) TTXDKTO UP Q7Z2W7 TTXDKTO UC TRPM8_HUMAN TTXDKTO BC Transient receptor potential catioin channel TTXDKTO SN Trp-p8; Transient receptor potential-p8; Transient receptor potential cation channel subfamily M member 8; TRPP8; TRPM8; LTrpC6 TTXDKTO GN TRPM8 TTXDKTO FC Receptor-activated non-selective cation channel involved in detection of sensations such as coolness, by being activated by cold temperature below 25 degrees Celsius. Activated by icilin, eucalyptol, menthol, cold and modulation of intracellular pH. Involved in menthol sensation. Permeable for monovalent cations sodium, potassium, and cesium and divalent cation calcium. Temperature sensing is tightly linked to voltage-dependent gating. Activated upon depolarization, changes in temperature resulting in graded shifts of its voltage-dependent activation curves. The chemical agonist menthol functions as a gating modifier, shifting activation curves towards physiological membrane potentials. Temperature sensitivity arises from a tenfold difference in the activation energies associated with voltage-dependent opening and closing. In prostate cancer cells, shows strong inward rectification and high calcium selectivity in contrast to its behavior in normal cells which is characterized by outward rectification and poor cationic selectivity. Plays a role in prostate cancer cell migration (PubMed:25559186). Isoform 2 and isoform 3 negatively regulate menthol- and cold-induced channel activity by stabilizing the closed state of the channel. TTXDKTO SQ MSFRAARLSMRNRRNDTLDSTRTLYSSASRSTDLSYSESDLVNFIQANFKKRECVFFTKDSKATENVCKCGYAQSQHMEGTQINQSEKWNYKKHTKEFPTDAFGDIQFETLGKKGKYIRLSCDTDAEILYELLTQHWHLKTPNLVISVTGGAKNFALKPRMRKIFSRLIYIAQSKGAWILTGGTHYGLMKYIGEVVRDNTISRSSEENIVAIGIAAWGMVSNRDTLIRNCDAEGYFLAQYLMDDFTRDPLYILDNNHTHLLLVDNGCHGHPTVEAKLRNQLEKYISERTIQDSNYGGKIPIVCFAQGGGKETLKAINTSIKNKIPCVVVEGSGQIADVIASLVEVEDALTSSAVKEKLVRFLPRTVSRLPEEETESWIKWLKEILECSHLLTVIKMEEAGDEIVSNAISYALYKAFSTSEQDKDNWNGQLKLLLEWNQLDLANDEIFTNDRRWESADLQEVMFTALIKDRPKFVRLFLENGLNLRKFLTHDVLTELFSNHFSTLVYRNLQIAKNSYNDALLTFVWKLVANFRRGFRKEDRNGRDEMDIELHDVSPITRHPLQALFIWAILQNKKELSKVIWEQTRGCTLAALGASKLLKTLAKVKNDINAAGESEELANEYETRAVELFTECYSSDEDLAEQLLVYSCEAWGGSNCLELAVEATDQHFIAQPGVQNFLSKQWYGEISRDTKNWKIILCLFIIPLVGCGFVSFRKKPVDKHKKLLWYYVAFFTSPFVVFSWNVVFYIAFLLLFAYVLLMDFHSVPHPPELVLYSLVFVLFCDEVRQWYVNGVNYFTDLWNVMDTLGLFYFIAGIVFRLHSSNKSSLYSGRVIFCLDYIIFTLRLIHIFTVSRNLGPKIIMLQRMLIDVFFFLFLFAVWMVAFGVARQGILRQNEQRWRWIFRSVIYEPYLAMFGQVPSDVDGTTYDFAHCTFTGNESKPLCVELDEHNLPRFPEWITIPLVCIYMLSTNILLVNLLVAMFGYTVGTVQENNDQVWKFQRYFLVQEYCSRLNIPFPFIVFAYFYMVVKKCFKCCCKEKNMESSVCCFKNEDNETLAWEGVMKENYLVKINTKANDTSEEMRHRFRQLDTKLNDLKGLLKEIANKIK TTXDKTO TT Successful TTXDKTO KE hsa04750:Inflammatory mediator regulation of TRP channels TTXDKTO RC R-HSA-3295583:TRP channels TTS8T1M ID TTS8T1M TTS8T1M TN Lysosomal acid lipase (LIPA) TTS8T1M UP P38571 TTS8T1M UC LICH_HUMAN TTS8T1M BC Carboxylic ester hydrolase TTS8T1M SN Sterol esterase; Lysosomal acid lipase/cholesteryl ester hydrolase; Lipase A; LIPA; LAL; Cholesteryl esterase; Acid cholesteryl ester hydrolase TTS8T1M GN LIPA TTS8T1M FC Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor- mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation. TTS8T1M EC EC 3.1.1.13 TTS8T1M SQ MKMRFLGLVVCLVLWTLHSEGSGGKLTAVDPETNMNVSEIISYWGFPSEEYLVETEDGYILCLNRIPHGRKNHSDKGPKPVVFLQHGLLADSSNWVTNLANSSLGFILADAGFDVWMGNSRGNTWSRKHKTLSVSQDEFWAFSYDEMAKYDLPASINFILNKTGQEQVYYVGHSQGTTIGFIAFSQIPELAKRIKMFFALGPVASVAFCTSPMAKLGRLPDHLIKDLFGDKEFLPQSAFLKWLGTHVCTHVILKELCGNLCFLLCGFNERNLNMSRVDVYTTHSPAGTSVQNMLHWSQAVKFQKFQAFDWGSSAKNYFHYNQSYPPTYNVKDMLVPTAVWSGGHDWLADVYDVNILLTQITNLVFHESIPEWEHLDFIWGLDAPWRLYNKIINLMRKYQ TTS8T1M TT Successful TTS8T1M KE hsa00100:Steroid biosynthesis; hsa04142:Lysosome TT95ICL ID TT95ICL TT95ICL TN Mannose-6-phosphate receptor (M6PR) TT95ICL UP P20645 TT95ICL UC MPRD_HUMAN TT95ICL BC Mannose 6-phosphate receptor TT95ICL SN MPRD; MPR46; MPR 46; Cation-dependent mannose-6-phosphate receptor; CDMan-6-P receptor; CD-MPR; CD Man-6-P receptor; 46kDa mannose 6-phosphate receptor; 46 kDa mannose 6-phosphate receptor TT95ICL GN M6PR TT95ICL FC Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. TT95ICL PD 1JUQ TT95ICL SQ MFPFYSCWRTGLLLLLLAVAVRESWQTEEKTCDLVGEKGKESEKELALVKRLKPLFNKSFESTVGQGSDTYIYIFRVCREAGNHTSGAGLVQINKSNGKETVVGRLNETHIFNGSNWIMLIYKGGDEYDNHCGKEQRRAVVMISCNRHTLADNFNPVSEERGKVQDCFYLFEMDSSLACSPEISHLSVGSILLVTFASLVAVYVVGGFLYQRLVVGAKGMEQFPHLAFWQDLGNLVADGCDFVCRSKPRNVPAAYRGVGDDQLGEESEERDDHLLPM TT95ICL TT Successful TT95ICL KE hsa04142:Lysosome; hsa04145:Phagosome TT95ICL RC R-HSA-432720:Lysosome Vesicle Biogenesis TTLCMWF ID TTLCMWF TTLCMWF TN MHC class II antigen DRB1*1 (HLA-DRB1) TTLCMWF UP P04229 TTLCMWF UC 2B11_HUMAN TTLCMWF BC MHC class II TTLCMWF SN HLA class II histocompatibility antigen, DRB1-1 beta chain; DR1; DR-1 TTLCMWF GN HLA-DRB1 TTLCMWF FC Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route; where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules; and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments; exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides; autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs; other cells of the gastrointestinal tract; such as epithelial cells; express MHC class II molecules and CD74 and act as APCs; which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen; three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs; CD74 undergoes a sequential degradation by various proteases; including CTSS and CTSL; leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells; the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules; increased acidification produces increased proteolysis and efficient peptide loading. TTLCMWF PD 6CQR; 6CQJ; 4X5X; 4X5W; 4OV5 TTLCMWF SQ MVCLKLPGGSCMTALTVTLMVLSSPLALSGDTRPRFLWQPKRECHFFNGTERVRFLDRYFYNQEESVRFDSDVGEFRAVTELGRPDAEYWNSQKDILEQARAAVDTYCRHNYGVVESFTVQRRVQPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFLNGQEEKAGMVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRARSESAQSKMLSGVGGFVLGLLFLGAGLFIYFRNQKGHSGLQPTGFLS TTLCMWF TT Successful TTLCMWF RC R-HSA-202427:Phosphorylation of CD3 and TCR zeta chains; R-HSA-202430:Translocation of ZAP-70 to Immunological synapse; R-HSA-202433:Generation of second messenger molecules; R-HSA-2132295:MHC class II antigen presentation; R-HSA-389948:PD-1 signaling; R-HSA-877300:Interferon gamma signaling TTUS1RD ID TTUS1RD TTUS1RD TN Microsomal triglyceride transfer protein (MTTP) TTUS1RD UP P55157 TTUS1RD UC MTP_HUMAN TTUS1RD SN Microsomal triglyceride transfer protein large subunit; MTP TTUS1RD GN MTTP TTUS1RD FC Required for the secretion of plasma lipoproteins that contain apolipoprotein B. Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces. TTUS1RD SQ MILLAVLFLCFISSYSASVKGHTTGLSLNNDRLYKLTYSTEVLLDRGKGKLQDSVGYRISSNVDVALLWRNPDGDDDQLIQITMKDVNVENVNQQRGEKSIFKGKSPSKIMGKENLEALQRPTLLHLIHGKVKEFYSYQNEAVAIENIKRGLASLFQTQLSSGTTNEVDISGNCKVTYQAHQDKVIKIKALDSCKIARSGFTTPNQVLGVSSKATSVTTYKIEDSFVIAVLAEETHNFGLNFLQTIKGKIVSKQKLELKTTEAGPRLMSGKQAAAIIKAVDSKYTAIPIVGQVFQSHCKGCPSLSELWRSTRKYLQPDNLSKAEAVRNFLAFIQHLRTAKKEEILQILKMENKEVLPQLVDAVTSAQTSDSLEAILDFLDFKSDSSIILQERFLYACGFASHPNEELLRALISKFKGSIGSSDIRETVMIITGTLVRKLCQNEGCKLKAVVEAKKLILGGLEKAEKKEDTRMYLLALKNALLPEGIPSLLKYAEAGEGPISHLATTALQRYDLPFITDEVKKTLNRIYHQNRKVHEKTVRTAAAAIILNNNPSYMDVKNILLSIGELPQEMNKYMLAIVQDILRFEMPASKIVRRVLKEMVAHNYDRFSRSGSSSAYTGYIERSPRSASTYSLDILYSGSGILRRSNLNIFQYIGKAGLHGSQVVIEAQGLEALIAATPDEGEENLDSYAGMSAILFDVQLRPVTFFNGYSDLMSKMLSASGDPISVVKGLILLIDHSQELQLQSGLKANIEVQGGLAIDISGAMEFSLWYRESKTRVKNRVTVVITTDITVDSSFVKAGLETSTETEAGLEFISTVQFSQYPFLVCMQMDKDEAPFRQFEKKYERLSTGRGYVSQKRKESVLAGCEFPLHQENSEMCKVVFAPQPDSTSSGWF TTUS1RD TT Successful TTUS1RD FM Vitellogenin lipid transport TTUS1RD KE hsa04975:Fat digestion and absorption TTUS1RD RC R-HSA-174800:Chylomicron-mediated lipid transport TTUQ7WN ID TTUQ7WN TTUQ7WN TN Mitochondrial rRNA methyltransferase 2 (MRM2) TTUQ7WN UP Q9UI43 TTUQ7WN UC MRM2_HUMAN TTUQ7WN BC Methyltransferase TTUQ7WN SN rRNA methyltransferase 2, mitochondrial; Protein ftsJ homolog 2; 16S rRNA [Um1369] 2'-O-methyltransferase; 16S rRNA (uridine(1369)-2'-O)-methyltransferase TTUQ7WN GN MRM2 TTUQ7WN FC S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. TTUQ7WN EC EC 2.1.1.- TTUQ7WN PD 2NYU TTUQ7WN SQ MAGYLKLVCVSFQRQGFHTVGSRCKNRTGAEHLWLTRHLRDPFVKAAKVESYRCRSAFKLLEVNERHQILRPGLRVLDCGAAPGAWSQVAVQKVNAAGTDPSSPVGFVLGVDLLHIFPLEGATFLCPADVTDPRTSQRILEVLPGRRADVILSDMAPNATGFRDLDHDRLISLCLTLLSVTPDILQPGGTFLCKTWAGSQSRRLQRRLTEEFQNVRIIKPEASRKESSEVYFLATQYHGRKGTVKQ TTUQ7WN TT Successful TT1Q8GP ID TT1Q8GP TT1Q8GP TN Mycobacterium Arabinosyltransferase C (MycB embC) TT1Q8GP UP P9WNL5 TT1Q8GP UC EMBC_MYCTU TT1Q8GP SN Probable arabinosyltransferase C TT1Q8GP GN MycB embC TT1Q8GP FC Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan. TT1Q8GP EC EC 2.4.2.- TT1Q8GP PD 3PTY TT1Q8GP SQ MATEAAPPRIAVRLPSTSVRDAGANYRIARYVAVVAGLLGAVLAIATPLLPVNQTTAQLNWPQNGTFASVEAPLIGYVATDLNITVPCQAAAGLAGSQNTGKTVLLSTVPKQAPKAVDRGLLLQRANDDLVLVVRNVPLVTAPLSQVLGPTCQRLTFTAHADRVAAEFVGLVQGPNAEHPGAPLRGERSGYDFRPQIVGVFTDLAGPAPPGLSFSASVDTRYSSSPTPLKMAAMILGVALTGAALVALHILDTADGMRHRRFLPARWWSTGGLDTLVIAVLVWWHFVGANTSDDGYILTMARVSEHAGYMANYYRWFGTPEAPFGWYYDLLALWAHVSTASIWMRLPTLAMALTCWWVISREVIPRLGHAVKTSRAAAWTAAGMFLAVWLPLDNGLRPEPIIALGILLTWCSVERAVATSRLLPVAIACIIGALTLFSGPTGIASIGALLVAIGPLRTILHRRSRRFGVLPLVAPILAAATVTAIPIFRDQTFAGEIQANLLKRAVGPSLKWFDEHIRYERLFMASPDGSIARRFAVLALVLALAVSVAMSLRKGRIPGTAAGPSRRIIGITIISFLAMMFTPTKWTHHFGVFAGLAGSLGALAAVAVTGAAMRSRRNRTVFAAVVVFVLALSFASVNGWWYVSNFGVPWSNSFPKWRWSLTTALLELTVLVLLLAAWFHFVANGDGRRTARPTRFRARLAGIVQSPLAIATWLLVLFEVVSLTQAMISQYPAWSVGRSNLQALAGKTCGLAEDVLVELDPNAGMLAPVTAPLADALGAGLSEAFTPNGIPADVTADPVMERPGDRSFLNDDGLITGSEPGTEGGTTAAPGINGSRARLPYNLDPARTPVLGSWRAGVQVPAMLRSGWYRLPTNEQRDRAPLLVVTAAGRFDSREVRLQWATDEQAAAGHHGGSMEFADVGAAPAWRNLRAPLSAIPSTATQVRLVADDQDLAPQHWIALTPPRIPRVRTLQNVVGAADPVFLDWLVGLAFPCQRPFGHQYGVDETPKWRILPDRFGAEANSPVMDHNGGGPLGITELLMRATTVASYLKDDWFRDWGALQRLTPYYPDAQPADLNLGTVTRSGLWSPAPLRRG TT1Q8GP TT Successful TTT8SED ID TTT8SED TTT8SED TN Mycobacterium D-alanine-D-alanine ligase (MycB ddl) TTT8SED UP P9WP30 TTT8SED UC DDL_MYCTO TTT8SED BC Carbon-nitrogen ligase TTT8SED SN ddl; D-alanylalanine synthetase; D-alanine:D-alanine ligase; D-Ala-D-Ala ligase TTT8SED GN MycB ddl TTT8SED FC Cell wall formation. TTT8SED EC EC 6.3.2.4 TTT8SED SQ MSANDRRDRRVRVAVVFGGRSNEHAISCVSAGSILRNLDSRRFDVIAVGITPAGSWVLTDANPDALTITNRELPQVKSGSGTELALPADPRRGGQLVSLPPGAGEVLESVDVVFPVLHGPYGEDGTIQGLLELAGVPYVGAGVLASAVGMDKEFTKKLLAADGLPVGAYAVLRPPRSTLHRQECERLGLPVFVKPARGGSSIGVSRVSSWDQLPAAVARARRHDPKVIVEAAISGRELECGVLEMPDGTLEASTLGEIRVAGVRGREDSFYDFATKYLDDAAELDVPAKVDDQVAEAIRQLAIRAFAAIDCRGLARVDFFLTDDGPVINEINTMPGFTTISMYPRMWAASGVDYPTLLATMIETALARGVGLH TTT8SED TT Successful TTT8SED KE mtc00473:D-Alanine metabolism; mtc00550:Peptidoglycan biosynthesis; mtc01100:Metabolic pathways; mtc01502:Vancomycin resistance TTESQTG ID TTESQTG TTESQTG TN N-acetylgalactosamine-4-sulfatase (G4S) TTESQTG UP P15848 TTESQTG UC ARSB_HUMAN TTESQTG BC Sulfuric ester hydrolase TTESQTG SN Nacetylgalactosamine4sulfatase; G4S; ASB; ARSB TTESQTG GN ARSB TTESQTG FC Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (PubMed:19306108). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (PubMed:19306108). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels. TTESQTG EC EC 3.1.6.12 TTESQTG PD 1FSU TTESQTG SQ MGPRGAASLPRGPGPRRLLLPVVLPLLLLLLLAPPGSGAGASRPPHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLPEYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRDPEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM TTESQTG TT Successful TTWNV8U ID TTWNV8U TTWNV8U TN Nicotinic acid receptor (HCAR2) TTWNV8U UP Q8TDS4 TTWNV8U UC HCAR2_HUMAN TTWNV8U BC GPCR rhodopsin TTWNV8U SN Niacin receptor 1; NIACR1; Hydroxycarboxylic acid receptor 2; HM74A; HCA2; GPR109A; G-protein coupled receptor HM74A; G-protein coupled receptor 109A TTWNV8U GN HCAR2 TTWNV8U FC Acts as a high affinity receptor for both nicotinic acid (also known as niacin) and (D)-beta-hydroxybutyrate and mediates increased adiponectin secretion and decreased lipolysis through G(i)-protein-mediated inhibition of adenylyl cyclase. This pharmacological effect requires nicotinic acid doses that are much higher than those provided by a normal diet. Mediates nicotinic acid-induced apoptosis in mature neutrophils. Receptor activation by nicotinic acid results in reduced cAMP levels which may affect activity of cAMP-dependent protein kinase A and phosphorylation of target proteins, leading to neutrophil apoptosis. The rank order of potency for the displacement of nicotinic acid binding is 5-methyl pyrazole-3-carboxylic acid = pyridine-3-acetic acid > acifran > 5-methyl nicotinic acid = acipimox >> nicotinuric acid = nicotinamide. TTWNV8U SQ MNRHHLQDHFLEIDKKNCCVFRDDFIVKVLPPVLGLEFIFGLLGNGLALWIFCFHLKSWKSSRIFLFNLAVADFLLIICLPFLMDNYVRRWDWKFGDIPCRLMLFMLAMNRQGSIIFLTVVAVDRYFRVVHPHHALNKISNRTAAIISCLLWGITIGLTVHLLKKKMPIQNGGANLCSSFSICHTFQWHEAMFLLEFFLPLGIILFCSARIIWSLRQRQMDRHAKIKRAITFIMVVAIVFVICFLPSVVVRIRIFWLLHTSGTQNCEVYRSVDLAFFITLSFTYMNSMLDPVVYYFSSPSFPNFFSTLINRCLQRKMTGEPDNNRSTSVELTGDPNKTRGAPEALMANSGEPWSPSYLGPTSP TTWNV8U TT Successful TTWNV8U KE hsa04024:cAMP signaling pathway TTWNV8U RC R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events TTRANFM ID TTRANFM TTRANFM TN Orphan nuclear receptor NR1I3 (NR1I3) TTRANFM UP Q14994 TTRANFM UC NR1I3_HUMAN TTRANFM BC Nuclear hormone receptor TTRANFM SN Orphan nuclear receptor MB67; Orphan nuclear receptor CAR; Nuclear receptor subfamily 1 group I member 3; Nuclear receptor CAR; Constitutive androstane receptor; Constitutive active response; Constitutive activator of retinoid response; CAR TTRANFM GN NR1I3 TTRANFM FC Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element. Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. TTRANFM PD 1XVP; 1XV9 TTRANFM SQ MASREDELRNCVVCGDQATGYHFNALTCEGCKGFFRRTVSKSIGPTCPFAGSCEVSKTQRRHCPACRLQKCLDAGMRKDMILSAEALALRRAKQAQRRAQQTPVQLSKEQEELIRTLLGAHTRHMGTMFEQFVQFRPPAHLFIHHQPLPTLAPVLPLVTHFADINTFMVLQVIKFTKDLPVFRSLPIEDQISLLKGAAVEICHIVLNTTFCLQTQNFLCGPLRYTIEDGARVSPTVGFQVEFLELLFHFHGTLRKLQLQEPEYVLLAAMALFSPDRPGVTQRDEIDQLQEEMALTLQSYIKGQQRRPRDRFLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEICS TTRANFM TT Successful TTRANFM FM Nuclear hormone receptor family TT2A0DR ID TT2A0DR TT2A0DR TN Oxo-5-alpha-steroid 4-dehydrogenase (SRD5A) TT2A0DR UP P18405; P31213; Q9H8P0 TT2A0DR UC S5A1_HUMAN; S5A2_HUMAN; PORED_HUMAN TT2A0DR BC CH-CH donor oxidoreductase TT2A0DR SN Steroid 5-alpha-reductase; SR; S5AR; 3-oxo-5-alpha-steroid 4-dehydrogenase TT2A0DR GN SRD5A1; SRD5A2; SRD5A3 TT2A0DR FC Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology. TT2A0DR SQ MATATGVAEERLLAALAYLQCAVGCAVFARNRQTNSVYGRHALPSHRLRVPARAAWVVQELPSLALPLYQYASESAPRLRSAPNCILLAMFLVHYGHRCLIYPFLMRGGKPMPLLACTMAIMFCTCNGYLQSRYLSHCAVYADDWVTDPRFLIGFGLWLTGMLINIHSDHILRNLRKPGDTGYKIPRGGLFEYVTAANYFGEIMEWCGYALASWSVQGAAFAFFTFCFLSGRAKEHHEWYLRKFEEYPKFRKIIIPFLF TT2A0DR TT Successful TTSCIUP ID TTSCIUP TTSCIUP TN Oxytocin receptor (OTR) TTSCIUP UP P30559 TTSCIUP UC OXYR_HUMAN TTSCIUP BC GPCR rhodopsin TTSCIUP SN OT-R TTSCIUP GN OXTR TTSCIUP FC The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. Receptor for oxytocin. TTSCIUP SQ MEGALAANWSAEAANASAAPPGAEGNRTAGPPRRNEALARVEVAVLCLILLLALSGNACVLLALRTTRQKHSRLFFFMKHLSIADLVVAVFQVLPQLLWDITFRFYGPDLLCRLVKYLQVVGMFASTYLLLLMSLDRCLAICQPLRSLRRRTDRLAVLATWLGCLVASAPQVHIFSLREVADGVFDCWAVFIQPWGPKAYITWITLAVYIVPVIVLAACYGLISFKIWQNLRLKTAAAAAAEAPEGAAAGDGGRVALARVSSVKLISKAKIRTVKMTFIIVLAFIVCWTPFFFVQMWSVWDANAPKEASAFIIVMLLASLNSCCNPWIYMLFTGHLFHELVQRFLCCSASYLKGRRLGETSASKKSNSSSFVLSHRSSSQRSCSQPSTA TTSCIUP TT Successful TTSCIUP FM GPCR rhodopsin TTSCIUP KE hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04921:Oxytocin signaling pathway TTSCIUP RC R-HSA-388479:Vasopressin-like receptors; R-HSA-416476:G alpha (q) signalling events TT6F7GZ ID TT6F7GZ TT6F7GZ TN Parathyroid hormone (PTH) TT6F7GZ UP P01270 TT6F7GZ UC PTHY_HUMAN TT6F7GZ SN Parathyrin; Parathormone TT6F7GZ GN PTH TT6F7GZ FC Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells. PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. TT6F7GZ PD 3C4M; 2L1X; 1ZWG; 1ZWF; 1ZWE TT6F7GZ SQ MIPAKDMAKVMIVMLAICFLTKSDGKSVKKRSVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFVALGAPLAPRDAGSQRPRKKEDNVLVESHEKSLGEADKADVNVLTKAKSQ TT6F7GZ TT Successful TT6F7GZ FM Parathyroid hormone TT6F7GZ RC R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-418555:G alpha (s) signalling events TTNX2CS ID TTNX2CS TTNX2CS TN Plasmodium Enoyl-ACP reductase (Malaria fabI) TTNX2CS UP Q965D5 TTNX2CS UC Q965D5_PLAFA TTNX2CS BC CH-CH donor oxidoreductase TTNX2CS SN fabI; NADH-dependent enoyl-ACP reductase; Enoyl-acyl-carrier protein reductase; Enoyl-acyl carrier reductase; Enoyl-acyl carrier protein reductase; Enoyl-ACP reductase FabI TTNX2CS GN Malaria fabI TTNX2CS FC Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis. TTNX2CS EC EC 1.3.1.9 TTNX2CS SQ MNKISQRLLFLFLHFYTTVCFIQNNTQKTFHNVLQNEQIRGKEKAFYRKEKRENIFIGNKMKHVHNMNNTHNNNHYMEKEEQDASNINKIKEENKNEDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNGKFDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYPIEDVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSLISLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVLAYHLGRNYNIRINTISAGPLKSRAATAINKLNNTYENNTNQNKNRNSHDVHNIMNNSGEKEEKKNSASQNYTFIDYAIEYSEKYAPLRQKLLSTDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPDDIYRNENE TTNX2CS TT Successful TTAO7YK ID TTAO7YK TTAO7YK TN Plasmodium Glutamate dehydrogenase (Malaria gdh) TTAO7YK UP Q9NGT0 TTAO7YK UC Q9NGT0_PLAFA TTAO7YK BC CH-NH(2) donor oxidoreductase TTAO7YK SN Glutamate dehydrogenase TTAO7YK GN Malaria gdh TTAO7YK FC Catalyses the reversible oxidative deamination of L-glutamate to form -ketoglutarate and ammonia using NADP(H) or NAD(H) as co-factors TTAO7YK EC EC 1.4.1.2 TTAO7YK SQ MDIDRRSALSCSPNNMECGFGSGHFSNNSITWKEKYEQTKELLKSYNLFSDHLINYSIDFYFNKLGFNKFHFEETSPELISKVVVCIITAKINEQYSSDKYFPTFEETHDNVIFIITRVFADDNKTRLNYKMEKKIEEKYFNFSDMSKDCYRLKSFRSVHSVFDKEHTYQEPLRTYILELPTYNDDIIKENETDLKKLMDVNFYNYIKGTRSEQIYYELNKAVLYDLTGQFLQTHYYETSSSTFTLTIAVKRSNVISSIFSLIGDCLNMHRCFSYSKYVEPLKNGVLLIILNVKVIVNNEMEREKQKLDLKDKIYKVVKSLKTLCLFNDSKFIQLSVKRTFTAQESAYLFMIIKFITFFSTFTLSSYKNVEHALNLRNYNNNIMDTTTNSSSSPSSVLNDVYIIKEKLKSSKYTKEEILRCAQSNVRTIKMLFANFEKKLNHQRNKCNQMKYGENNMKNSGDLLKEYSTNNRNVDHPTLSSLASSSSSCSSSFSLHSYLSGSYESPYYHHNKDSKDIIDEIEDNHDKKILQYFYMFEKYALKTNFFLTHKISLAVAFDGALLKDSIYEAQPYSIIMILGLHFVGFHIRFSKISRGGVRIVISNNVNSYMHNSDNLFDEAYNLAYTQNFKNKDIPEGGSKGIILLDADVCNVANTKYIKNLSFYSYVNSILDLLINEDLNEERASSISVHSTKGANNTTITFDNVMSSVENMVDRGGVEGEHLNITLPYDANMACNNNTTNDNLSNMHDTYNLNNSGEATLDHHSVDNRIVSNSSGTNNMNAQKGEGEDEKAKDKEMSNNRKNEENERKRCDNVSNSNYNYVNGTTEDAVQKIMGSKCKGGRNNNGEEKDGDMNGHNNNNNDNNNIDDDEHIEECYKGAGCVINGENKTRKMILQEKMNEEEDLIFLGPDENTGSDQLMDWACIIAKREYIHIGKPFQQGKLRKNGGVPHDMYGMTTLGIETYISKLCEKLNIKEESISRSLVGGPDGDLGSNAILQSKTKIISIIDGSGILYDKQGLNKEELIRLAKRRNNKDKSKAITCCTLYDEKYFSKDGFKISIEDHNVDIFGNKIRNGLDFRNTFFLNPLNKCELFNPCGGRPHSINIFNVNNIIKNGECIYKYIVEGANVFISDDARNILESKNVILFKDAATNKGGVISSSLEVLAGLVLDDKQYIDYMCSPDSDILQVDENEINFVHQNQKMNHSLSFKRGSINNLEEDEKKDTSNNEKNKNIIKTVNKNDTQDNSHHHNNSNKCNEDQQDVSDFYKAYVKEIQKKITHYCELEFESLWKETRRTKTPISKAINILSNKISELKKDILSSDTLCRDYKLLKKVLERVIPPTLLKIVTFEQILERVPYVYIKSLLASARASKLLLFTTILE TTAO7YK TT Successful TTK0943 ID TTK0943 TTK0943 TN Prostaglandin G/H synthase (COX) TTK0943 UP P23219; P35354 TTK0943 UC PGH1_HUMAN; PGH2_HUMAN TTK0943 BC Paired donor oxygen oxidoreductase TTK0943 SN Prostaglandin-endoperoxide synthase; Prostaglandin H2 synthase; PHS; PGHS; PGH synthase; Cyclooxygenase; COX TTK0943 GN PTGS1; PTGS2 TTK0943 FC Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. PTGS1 is involved in the constitutive production of prostanoids in particular in the stomach and platelets. It is a key step in the generation of prostaglandins in gastric epithelial cells and the generation of thromboxane A2 (TXA2) in platelets. PTGS2 is constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. TTK0943 SQ MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWEFVNATFIREMLMRLVLTVRSNLIPSPPTYNSAHDYISWESFSNVSYYTRILPSVPKDCPTPMGTKGKKQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKVGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFNIVKTATLKKLVCLNTKTCPYVSFRVPDASQDDGPAVERPSTEL TTK0943 TT Successful TT958S6 ID TT958S6 TT958S6 TN Ras-related protein Rab-9A (RAB9A) TT958S6 UP P51151 TT958S6 UC RAB9A_HUMAN TT958S6 BC Small GTPase superfamily TT958S6 SN RAB9A TT958S6 GN RAB9A TT958S6 FC Involved in the transport of proteins between the endosomes and the trans Golgi network. TT958S6 PD 1WMS TT958S6 SQ MAGKSSLFKVILLGDGGVGKSSLMNRYVTNKFDTQLFHTIGVEFLNKDLEVDGHFVTMQIWDTAGQERFRSLRTPFYRGSDCCLLTFSVDDSQSFQNLSNWKKEFIYYADVKEPESFPFVILGNKIDISERQVSTEEAQAWCRDNGDYPYFETSAKDATNVAAAFEEAVRRVLATEDRSDHLIQTDTVNLHRKPKPSSSCC TT958S6 TT Successful TT958S6 KE hsa05162:Measles TTKLV96 ID TTKLV96 TTKLV96 TN Retinoic acid receptor RXR-beta (RXRB) TTKLV96 UP P28702 TTKLV96 UC RXRB_HUMAN TTKLV96 BC Nuclear hormone receptor TTKLV96 SN Retinoid X receptor beta; Nuclear receptor subfamily 2 group B member 2; NR2B2 TTKLV96 GN RXRB TTKLV96 FC Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE). Receptor for retinoic acid. TTKLV96 PD 5KYJ; 5KYA; 5I4V; 5HJP; 1UHL TTKLV96 SQ MSWAARPPFLPQRHAAGQCGPVGVRKEMHCGVASRWRRRRPWLDPAAAAAAAVAGGEQQTPEPEPGEAGRDGMGDSGRDSRSPDSSSPNPLPQGVPPPSPPGPPLPPSTAPSLGGSGAPPPPPMPPPPLGSPFPVISSSMGSPGLPPPAPPGFSGPVSSPQINSTVSLPGGGSGPPEDVKPPVLGVRGLHCPPPPGGPGAGKRLCAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLTYSCRDNKDCTVDKRQRNRCQYCRYQKCLATGMKREAVQEERQRGKDKDGDGEGAGGAPEEMPVDRILEAELAVEQKSDQGVEGPGGTGGSGSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSSLPLDDQVILLRAGWNELLIASFSHRSIDVRDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMRMDKTELGCLRAIILFNPDAKGLSNPSEVEVLREKVYASLETYCKQKYPEQQGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQLA TTKLV96 TT Successful TTR40YJ ID TTR40YJ TTR40YJ TN S-mephenytoin 4-hydroxylase (CYP2C9) TTR40YJ UP P11712 TTR40YJ UC CP2C9_HUMAN TTR40YJ BC Paired donor oxygen oxidoreductase TTR40YJ SN Cytochrome P450 PB-1; Cytochrome P450 MP-8; Cytochrome P450 MP-4; Cytochrome P450 2C9; Cytochrome P-450MP; Cholesterol 25-hydroxylase; CYPIIC9; CYP2C10; (S)-limonene 7-monooxygenase; (S)-limonene 6-monooxygenase; (R)-limonene 6-monooxygenase TTR40YJ GN CYP2C9 TTR40YJ FC In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan. Cytochromes P450 are a group of heme-thiolate monooxygenases. TTR40YJ EC EC 1.14.14.- TTR40YJ PD 5XXI; 5X24; 5X23; 5W0C; 5K7K TTR40YJ SQ MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFMKSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYIDLLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFKKSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVPPFYQLCFIPV TTR40YJ TT Successful TTQ38E9 ID TTQ38E9 TTQ38E9 TN Sodium/potassium-transporting ATPase (SPT ATPase) TTQ38E9 UP P05023; P50993; P13637; P05026; P14415; P54709 TTQ38E9 UC AT1A1_HUMAN; AT1A2_HUMAN; AT1A3_HUMAN; AT1B1_HUMAN; AT1B2_HUMAN; AT1B3_HUMAN TTQ38E9 BC Acid anhydrides hydrolase TTQ38E9 SN Na(+)/K(+) ATPase TTQ38E9 GN ATP1A1; ATP1A2; ATP1A3; ATP1B1; ATP1B2; ATP1B3 TTQ38E9 FC Maintain resting potential, affects transport, and regulates cellular volume. Function as a signal transducer/integrator to regulate the MAPK pathway, ROS, as well as intracellular calcium. TTQ38E9 SQ MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY TTQ38E9 TT Successful TTQ38E9 KE hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04911:Insulin secretion; hsa04918:Thyroid hormone synthesis; hsa04919:Thyroid hormone signaling pathway; hsa04960:Aldosterone-regulated sodium reabsorption; hsa04961:Endocrine and other factor-regulated calcium reabsorption; hsa04964:Proximal tubule bicarbonate reclamation; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04973:Carbohydrate digestion and absorption; hsa04974:Protein digestion and absorption; hsa04976:Bile secretion; hsa04978:Mineral absorption TTS087L ID TTS087L TTS087L TN Solute carrier family 12 member 1 (SLC12A1) TTS087L UP Q13621 TTS087L UC S12A1_HUMAN TTS087L BC Cation-chloride cotransporter TTS087L SN Solute carrier family 12 member; SLC12A1; Na+/K+/2CL- co-transporter; NKCC2; Kidney-specific Na-K-Cl symporter; Bumetanide-sensitive sodium-(potassium)Solute carrier family 12 member 1-chloride cotransporter 2; Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 2 TTS087L GN SLC12A1 TTS087L FC Electrically silent transporter system. Mediates sodium and chloride reabsorption. Plays a vital role in the regulation of ionic balance and cell volume. TTS087L SQ MSLNNSSNVFLDSVPSNTNRFQVSVINENHESSAAADDNTDPPHYEETSFGDEAQKRLRISFRPGNQECYDNFLQSGETAKTDASFHAYDSHTNTYYLQTFGHNTMDAVPKIEYYRNTGSISGPKVNRPSLLEIHEQLAKNVAVTPSSADRVANGDGIPGDEQAENKEDDQAGVVKFGWVKGVLVRCMLNIWGVMLFIRLSWIVGEAGIGLGVLIILLSTMVTSITGLSTSAIATNGFVRGGGAYYLISRSLGPEFGGSIGLIFAFANAVAVAMYVVGFAETVVDLLKESDSMMVDPTNDIRIIGSITVVILLGISVAGMEWEAKAQVILLVILLIAIANFFIGTVIPSNNEKKSRGFFNYQASIFAENFGPRFTKGEGFFSVFAIFFPAATGILAGANISGDLEDPQDAIPRGTMLAIFITTVAYLGVAICVGACVVRDATGNMNDTIISGMNCNGSAACGLGYDFSRCRHEPCQYGLMNNFQVMSMVSGFGPLITAGIFSATLSSALASLVSAPKVFQALCKDNIYKALQFFAKGYGKNNEPLRGYILTFLIAMAFILIAELNTIAPIISNFFLASYALINFSCFHASYAKSPGWRPAYGIYNMWVSLFGAVLCCAVMFVINWWAAVITYVIEFFLYVYVTCKKPDVNWGSSTQALSYVSALDNALELTTVEDHVKNFRPQCIVLTGGPMTRPALLDITHAFTKNSGLCICCEVFVGPRKLCVKEMNSGMAKKQAWLIKNKIKAFYAAVAADCFRDGVRSLLQASGLGRMKPNTLVIGYKKNWRKAPLTEIENYVGIIHDAFDFEIGVVIVRISQGFDISQVLQVQEELERLEQERLALEATIKDNECEEESGGIRGLFKKAGKLNITKTTPKKDGSINTSQSMHVGEFNQKLVEASTQFKKKQEKGTIDVWWLFDDGGLTLLIPYILTLRKKWKDCKLRIYVGGKINRIEEEKIVMASLLSKFRIKFADIHIIGDINIRPNKESWKVFEEMIEPYRLHESCKDLTTAEKLKRETPWKITDAELEAVKEKSYRQVRLNELLQEHSRAANLIVLSLPVARKGSISDLLYMAWLEILTKNLPPVLLVRGNHKNVLTFYS TTS087L TT Successful TTS087L KE hsa04970:Salivary secretion; hsa04972:Pancreatic secretion; hsa05110:Vibrio cholerae infection TTS087L RC R-HSA-426117:Cation-coupled Chloride cotransporters TTP362L ID TTP362L TTP362L TN Solute carrier family 12 member 3 (SLC12A3) TTP362L UP P55017 TTP362L UC S12A3_HUMAN TTP362L BC Cation-chloride cotransporter TTP362L SN Thiazide-sensitive sodium-chloride cotransporter; Thiazide-sensitive Na-Cl cotransporter; SLC12A3; Na-Cl symporter TTP362L GN SLC12A3 TTP362L FC Key mediator of sodium and chloride reabsorption in this nephron segment, accounting for a significant fraction of renal sodium reabsorption. TTP362L SQ MAELPTTETPGDATLCSGRFTISTLLSSDEPSPPAAYDSSHPSHLTHSSTFCMRTFGYNTIDVVPTYEHYANSTQPGEPRKVRPTLADLHSFLKQEGRHLHALAFDSRPSHEMTDGLVEGEAGTSSEKNPEEPVRFGWVKGVMIRCMLNIWGVILYLRLPWITAQAGIVLTWIIILLSVTVTSITGLSISAISTNGKVKSGGTYFLISRSLGPELGGSIGLIFAFANAVGVAMHTVGFAETVRDLLQEYGAPIVDPINDIRIIAVVSVTVLLAISLAGMEWESKAQVLFFLVIMVSFANYLVGTLIPPSEDKASKGFFSYRADIFVQNLVPDWRGPDGTFFGMFSIFFPSATGILAGANISGDLKDPAIAIPKGTLMAIFWTTISYLAISATIGSCVVRDASGVLNDTVTPGWGACEGLACSYGWNFTECTQQHSCHYGLINYYQTMSMVSGFAPLITAGIFGATLSSALACLVSAAKVFQCLCEDQLYPLIGFFGKGYGKNKEPVRGYLLAYAIAVAFIIIAELNTIAPIISNFFLCSYALINFSCFHASITNSPGWRPSFQYYNKWAALFGAIISVVIMFLLTWWAALIAIGVVLFLLLYVIYKKPEVNWGSSVQAGSYNLALSYSVGLNEVEDHIKNYRPQCLVLTGPPNFRPALVDFVGTFTRNLSLMICGHVLIGPHKQRMPELQLIANGHTKWLNKRKIKAFYSDVIAEDLRRGVQILMQAAGLGRMKPNILVVGFKKNWQSAHPATVEDYIGILHDAFDFNYGVCVMRMREGLNVSKMMQAHINPVFDPAEDGKEASARVDPKALVKEEQATTIFQSEQGKKTIDIYWLFDDGGLTLLIPYLLGRKRRWSKCKIRVFVGGQINRMDQERKAIISLLSKFRLGFHEVHILPDINQNPRAEHTKRFEDMIAPFRLNDGFKDEATVNEMRRDCPWKISDEEITKNRVKSLRQVRLNEIVLDYSRDAALIVITLPIGRKGKCPSSLYMAWLETLSQDLRPPVILIRGNQENVLTFYCQ TTP362L TT Successful TTP362L RC R-HSA-426117:Cation-coupled Chloride cotransporters TTTQR47 ID TTTQR47 TTTQR47 TN Solute carrier family 22 member 8 (SLC22A8) TTTQR47 UP Q8TCC7 TTTQR47 UC S22A8_HUMAN TTTQR47 BC Major facilitator superfamily TTTQR47 SN hROAT1; hPAHT; hOAT1; Solute carrier family 22 member 6; SLC22A8; SLC22A6; Renal organic anion transporter 1; PAHT; PAH transporter; OAT1 TTTQR47 GN SLC22A8 TTTQR47 FC Involved in the renal elimination of endogenous and exogenous organic anions. Functions as organic anion exchanger when the uptake of one molecule of organic anion is coupled with an efflux of one molecule of endogenous dicarboxylic acid (glutarate, ketoglutarate, etc). TTTQR47 SQ MTFSEILDRVGSMGHFQFLHVAILGLPILNMANHNLLQIFTAATPVHHCRPPHNASTGPWVLPMGPNGKPERCLRFVHPPNASLPNDTQRAMEPCLDGWVYNSTKDSIVTEWDLVCNSNKLKEMAQSIFMAGILIGGLVLGDLSDRFGRRPILTCSYLLLAASGSGAAFSPTFPIYMVFRFLCGFGISGITLSTVILNVEWVPTRMRAIMSTALGYCYTFGQFILPGLAYAIPQWRWLQLTVSIPFFVFFLSSWWTPESIRWLVLSGKSSKALKILRRVAVFNGKKEEGERLSLEELKLNLQKEISLAKAKYTASDLFRIPMLRRMTFCLSLAWFATGFAYYSLAMGVEEFGVNLYILQIIFGGVDVPAKFITILSLSYLGRHTTQAAALLLAGGAILALTFVPLDLQTVRTVLAVFGKGCLSSSFSCLFLYTSELYPTVIRQTGMGVSNLWTRVGSMVSPLVKITGEVQPFIPNIIYGITALLGGSAALFLPETLNQPLPETIEDLENWSLRAKKPKQEPEVEKASQRIPLQPHGPGLGSS TTTQR47 TT Successful TTWF7UG ID TTWF7UG TTWF7UG TN Somatostatin (SST) TTWF7UG UP P61278 TTWF7UG UC SMS_HUMAN TTWF7UG BC Somatostatin cortistatin TTWF7UG SN Somatostatin-28; Somatostatin-14; SST; Growth hormone release-inhibiting factor TTWF7UG GN SST TTWF7UG FC Somatostatin inhibits the release of somatotropin. TTWF7UG PD 2MI1; 1P2W TTWF7UG SQ MLSCRLQCALAALSIVLALGCVTGAPSDPRLRQFLQKSLAAAAGKQELAKYFLAELLSEPNQTENDALEPEDLSQAAEQDEMRLELQRSANSNPAMAPRERKAGCKNFFWKTFTSC TTWF7UG TT Successful TTWF7UG KE hsa04971:Gastric acid secretion TTWF7UG RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTYQWA0 ID TTYQWA0 TTYQWA0 TN Synaptosomal-associated protein 25 (SNAP25) TTYQWA0 UP P60880 TTYQWA0 UC SNP25_HUMAN TTYQWA0 BC Synaptosomal vesicle fusion pore TTYQWA0 SN Synaptosomal-associated 25 kDa protein; Super protein; SUP; SNAP-25; SNAP TTYQWA0 GN SNAP25 TTYQWA0 FC May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells. t-SNARE involved in the molecular regulation of neurotransmitter release. TTYQWA0 PD 5W7J; 5W7I; 3ZUR; 3RL0; 3RK3 TTYQWA0 SQ MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG TTYQWA0 TT Successful TTYQWA0 FM Synaptosomal vesicle fusion pore TTYQWA0 KE hsa04721:Synaptic vesicle cycle; hsa04911:Insulin secretion TTYQWA0 RC R-HSA-181430:Norepinephrine Neurotransmitter Release Cycle; R-HSA-422356:Regulation of insulin secretion TTQ13FT ID TTQ13FT TTQ13FT TN T-cell-specific surface glycoprotein CD28 (CD28) TTQ13FT UP P10747 TTQ13FT UC CD28_HUMAN TTQ13FT SN TP44; CD28-S2 TTQ13FT GN CD28 TTQ13FT FC Enhances the production of IL4 and IL10 in T-cells in conjunction with TCR/CD3 ligation and CD40L costimulation. Isoform 3 enhances CD40L-mediated activation of NF-kappa-B and kinases MAPK8 and PAK2 in T-cells. Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival. TTQ13FT PD 5GJI; 5GJH; 5AUL; 3WA4; 1YJD TTQ13FT SQ MLRLLLALNLFPSIQVTGNKILVKQSPMLVAYDNAVNLSCKYSYNLFSREFRASLHKGLDSAVEVCVVYGNYSQQLQVYSKTGFNCDGKLGNESVTFYLQNLYVNQTDIYFCKIEVMYPPPYLDNEKSNGTIIHVKGKHLCPSPLFPGPSKPFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS TTQ13FT TT Successful TTQ13FT FM Transmembrane protein TTQ13FT KE hsa04514:Cell adhesion molecules (CAMs); hsa04660:T cell receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa04940:Type I diabetes mellitus; hsa05162:Measles; hsa05320:Autoimmune thyroid disease; hsa05322:Systemic lupus erythematosus; hsa05323:Rheumatoid arthritis; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease; hsa05416:Viral myocarditis TTQ13FT RC R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-389356:CD28 co-stimulation; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389359:CD28 dependent Vav1 pathway TTLPJWH ID TTLPJWH TTLPJWH TN Thioredoxin reductase (PRDX5) TTLPJWH UP P30044 TTLPJWH UC PRDX5_HUMAN TTLPJWH BC Peroxide acceptor oxidoreductase TTLPJWH SN Thioredoxin peroxidase PMP20; TPx type VI; SBBI10; PrxV; Prx-V; Peroxisomal antioxidant enzyme; Peroxiredoxin5, mitochondrial; Peroxiredoxin-5, mitochondrial; Peroxiredoxin V; PLP; Liver tissue 2Dpage spot 71B; Liver tissue 2D-page spot 71B; Antioxidant enzyme B166; Alu corepressor 1; AOEB166; ACR1 TTLPJWH GN PRDX5 TTLPJWH FC Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. TTLPJWH EC EC 1.11.1.15 TTLPJWH PD 4MMM; 4K7O; 4K7N; 4K7I; 3MNG TTLPJWH SQ MGLAGVCALRRSAGYILVGGAGGQSAAAAARRYSEGEWASGGVRSFSRAAAAMAPIKVGDAIPAVEVFEGEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLVSIFGNRRLKRFSMVVQDGIVKALNVEPDGTGLTCSLAPNIISQL TTLPJWH TT Successful TTLPJWH FM Class-I pyridine nucleotide-disulfide oxidoreductase family TTP1UKZ ID TTP1UKZ TTP1UKZ TN Thymidylate synthase messenger RNA (TYMS mRNA) TTP1UKZ UP P04818 TTP1UKZ UC TYSY_HUMAN TTP1UKZ BC mRNA target TTP1UKZ SN TSase (mRNA); TS (mRNA); OK/SW-cl.29 (mRNA) TTP1UKZ GN TYMS TTP1UKZ FC Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. TTP1UKZ EC EC 2.1.1.45 TTP1UKZ PD 6R2E; 6QYQ; 6QXH; 6QXG; 5X69 TTP1UKZ SQ MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV TTP1UKZ TT Successful TTP1UKZ FM mRNA target TTIU98M ID TTIU98M TTIU98M TN Trace amine-associated receptor-1 (TAAR1) TTIU98M UP Q96RJ0 TTIU98M UC TAAR1_HUMAN TTIU98M BC GPCR rhodopsin TTIU98M SN Trace amine receptor 1; TaR-1; TAAR1 TTIU98M GN TAAR1 TTIU98M FC Receptor for trace amines, including beta- phenylethylamine (b-PEA), p-tyramine (p-TYR), octopamine and tryptamine, with highest affinity for b-PEA and p-TYR. Unresponsive to classical biogenic amines,such as epinephrine and histamine and only partially activated by dopamine and serotonine. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amineshave clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood. The signal transduced by this receptor is mediated by the G(s)-class of G-proteins which activate adenylate cyclase. TTIU98M SQ MMPFCHNIINISCVKNNWSNDVRASLYSLMVLIILTTLVGNLIVIVSISHFKQLHTPTNWLIHSMATVDFLLGCLVMPYSMVRSAEHCWYFGEVFCKIHTSTDIMLSSASIFHLSFISIDRYYAVCDPLRYKAKMNILVICVMIFISWSVPAVFAFGMIFLELNFKGAEEIYYKHVHCRGGCSVFFSKISGVLTFMTSFYIPGSIMLCVYYRIYLIAKEQARLISDANQKLQIGLEMKNGISQSKERKAVKTLGIVMGVFLICWCPFFICTVMDPFLHYIIPPTLNDVLIWFGYLNSTFNPMVYAFFYPWFRKALKMMLFGKIFQKDSSRCKLFLELSS TTIU98M TT Successful TTIU98M KE hsa04080:Neuroactive ligand-receptor interaction TTIU98M RC R-HSA-418555:G alpha (s) signalling events TTPOYU7 ID TTPOYU7 TTPOYU7 TN Transthyretin messenger RNA (TTR mRNA) TTPOYU7 UP P02766 TTPOYU7 UC TTHY_HUMAN TTPOYU7 BC mRNA target TTPOYU7 SN Transthyretin (mRNA); TBPA (mRNA); Prealbumin (mRNA); PALB (mRNA); ATTR (mRNA) TTPOYU7 GN TTR TTPOYU7 FC Probably transports thyroxine from the bloodstream to the brain. Thyroid hormone-binding protein. TTPOYU7 PD 6IMY; 6IMX; 6GRP; 6GR7; 6FZL TTPOYU7 SQ MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE TTPOYU7 TT Successful TTPOYU7 FM mRNA target TTPOYU7 RC R-HSA-2453864:Retinoid cycle disease events; R-HSA-2453902:The canonical retinoid cycle in rods (twilight vision); R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-975634:Retinoid metabolism and transport; R-HSA-977225:Amyloid formation TTOVYPT ID TTOVYPT TTOVYPT TN Tripeptidyl-peptidase I (TPP1) TTOVYPT UP O14773 TTOVYPT UC TPP1_HUMAN TTOVYPT BC Peptidase TTOVYPT SN TPP1 TTOVYPT GN TPP1 TTOVYPT FC Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus. TTOVYPT EC EC 3.4.14.9 TTOVYPT PD 3EE6; 3EDY; 1R60 TTOVYPT SQ MGLQACLLGLFALILSGKCSYSPEPDQRRTLPPGWVSLGRADPEEELSLTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHSVITQDFLTCWLSIRQAELLLPGAEFHHYVGGPTETHVVRSPHPYQLPQALAPHVDFVGGLHRFPPTSSLRQRPEPQVTGTVGLHLGVTPSVIRKRYNLTSQDVGSGTSNNSQACAQFLEQYFHDSDLAQFMRLFGGNFAHQASVARVVGQQGRGRAGIEASLDVQYLMSAGANISTWVYSSPGRHEGQEPFLQWLMLLSNESALPHVHTVSYGDDEDSLSSAYIQRVNTELMKAAARGLTLLFASGDSGAGCWSVSGRHQFRPTFPASSPYVTTVGGTSFQEPFLITNEIVDYISGGGFSNVFPRPSYQEEAVTKFLSSSPHLPPSSYFNASGRAYPDVAALSDGYWVVSNRVPIPWVSGTSASTPVFGGILSLINEHRILSGRPPLGFLNPRLYQQHGAGLFDVTRGCHESCLDEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLLNP TTOVYPT TT Successful TT8RDXP ID TT8RDXP TT8RDXP TN Troponin C (TN-C) TT8RDXP UP P63316 TT8RDXP UC TNNC1_HUMAN TT8RDXP SN Troponin C, slow skeletal and cardiac muscles; TNNC TT8RDXP GN TNNC1 TT8RDXP FC Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. TT8RDXP PD 6MV3; 5WCL; 5W88; 5VLN; 4Y99 TT8RDXP SQ MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE TT8RDXP TT Successful TT8RDXP FM Troponin TT8RDXP KE hsa04020:Calcium signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05414:Dilated cardiomyopathy TT8RDXP RC R-HSA-390522:Striated Muscle Contraction TTA592U ID TTA592U TTA592U TN Urate anion exchanger 1 (URAT1) TTA592U UP Q96S37 TTA592U UC S22AC_HUMAN TTA592U BC Major facilitator TTA592U SN UNQ6453/PRO34004; Solute carrier family 22 member 12; Renal-specific transporter; RST; Organic anion transporter 4-like protein; OATL4 TTA592U GN SLC22A12 TTA592U FC Regulates blood urate levels. Mediates saturable urate uptake by facilitating the exchange of urate against organic anions. Required for efficient urate re-absorption in the kidney. TTA592U SQ MAFSELLDLVGGLGRFQVLQTMALMVSIMWLCTQSMLENFSAAVPSHRCWAPLLDNSTAQASILGSLSPEALLAISIPPGPNQRPHQCRRFRQPQWQLLDPNATATSWSEADTEPCVDGWVYDRSIFTSTIVAKWNLVCDSHALKPMAQSIYLAGILVGAAACGPASDRFGRRLVLTWSYLQMAVMGTAAAFAPAFPVYCLFRFLLAFAVAGVMMNTGTLLMEWTAARARPLVMTLNSLGFSFGHGLTAAVAYGVRDWTLLQLVVSVPFFLCFLYSWWLAESARWLLTTGRLDWGLQELWRVAAINGKGAVQDTLTPEVLLSAMREELSMGQPPASLGTLLRMPGLRFRTCISTLCWFAFGFTFFGLALDLQALGSNIFLLQMFIGVVDIPAKMGALLLLSHLGRRPTLAASLLLAGLCILANTLVPHEMGALRSALAVLGLGGVGAAFTCITIYSSELFPTVLRMTAVGLGQMAARGGAILGPLVRLLGVHGPWLPLLVYGTVPVLSGLAALLLPETQSLPLPDTIQDVQNQAVKKATHGTLGNSVLKSTQF TTA592U TT Successful TTA592U FM Major facilitator superfamily TT76OLR ID TT76OLR TT76OLR TN Vitamin K-dependent gamma-carboxylase (GGCX) TT76OLR UP P38435 TT76OLR UC VKGC_HUMAN TT76OLR BC Carbon-carbon lyase TT76OLR SN Vitamin K gamma glutamyl carboxylase; Gamma-glutamyl carboxylase; GGCX TT76OLR GN GGCX TT76OLR FC Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. TT76OLR EC EC 4.1.1.90 TT76OLR SQ MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF TT76OLR TT Successful TT76OLR KE hsa00130:Ubiquinone and other terpenoid-quinone biosynthesis TT76OLR RC R-HSA-159740:Gamma-carboxylation of protein precursors TTX4QDJ ID TTX4QDJ TTX4QDJ TN Voltage-gated calcium channel alpha Cav2.1 (CACNA1A) TTX4QDJ UP O00555 TTX4QDJ UC CAC1A_HUMAN TTX4QDJ BC Voltage-gated ion channel TTX4QDJ SN Voltage-gated calcium channel alpha subunit Cav2.1; Voltage-dependent P/Q-type calcium channel; RBA-I; RAT brain class A; Calcium channel, L type, alpha-1 polypeptide, isoform 4; Calcium channel, L type, alpha-1 polypeptide isoform 4; CACNA1A; Brain calcium channel I; BI TTX4QDJ GN CACNA1A TTX4QDJ FC Voltage-sensitive calcium channels (vscc) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release and gene expression. TTX4QDJ PD 3BXK TTX4QDJ SQ MARFGDEMPARYGGGGSGAAAGVVVGSGGGRGAGGSRQGGQPGAQRMYKQSMAQRARTMALYNPIPVRQNCLTVNRSLFLFSEDNVVRKYAKKITEWPPFEYMILATIIANCIVLALEQHLPDDDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFAFHKGSYLRNGWNVMDFVVVLTGILATVGTEFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMIPLLQIGLLLFFAILIFAIIGLEFYMGKFHTTCFEEGTDDIQGESPAPCGTEEPARTCPNGTKCQPYWEGPNNGITQFDNILFAVLTVFQCITMEGWTDLLYNSNDASGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYMEWISKAEEVILAEDETDGEQRHPFDALRRTTIKKSKTDLLNPEEAEDQLADIASVGSPFARASIKSAKLENSTFFHKKERRMRFYIRRMVKTQAFYWTVLSLVALNTLCVAIVHYNQPEWLSDFLYYAEFIFLGLFMSEMFIKMYGLGTRPYFHSSFNCFDCGVIIGSIFEVIWAVIKPGTSFGISVLRALRLLRIFKVTKYWASLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFDEGTPPTNFDTFPAAIMTVFQILTGEDWNEVMYDGIKSQGGVQGGMVFSIYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEQEEEEAANQKLALQKAKEVAEVSPLSAANMSIAVKEQQKNQKPAKSVWEQRTSEMRKQNLLASREALYNEMDPDERWKAAYTRHLRPDMKTHLDRPLVVDPQENRNNNTNKSRAAEPTVDQRLGQQRAEDFLRKQARYHDRARDPSGSAGLDARRPWAGSQEAELSREGPYGRESDHHAREGSLEQPGFWEGEAERGKAGDPHRRHVHRQGGSRESRSGSPRTGADGEHRRHRAHRRPGEEGPEDKAERRARHREGSRPARGGEGEGEGPDGGERRRRHRHGAPATYEGDARREDKERRHRRRKENQGSGVPVSGPNLSTTRPIQQDLGRQDPPLAEDIDNMKNNKLATAESAAPHGSLGHAGLPQSPAKMGNSTDPGPMLAIPAMATNPQNAASRRTPNNPGNPSNPGPPKTPENSLIVTNPSGTQTNSAKTARKPDHTTVDIPPACPPPLNHTVVQVNKNANPDPLPKKEEEKKEEEEDDRGEDGPKPMPPYSSMFILSTTNPLRRLCHYILNLRYFEMCILMVIAMSSIALAAEDPVQPNAPRNNVLRYFDYVFTGVFTFEMVIKMIDLGLVLHQGAYFRDLWNILDFIVVSGALVAFAFTGNSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVFNILIVYMLFMFIFAVVAVQLFKGKFFHCTDESKEFEKDCRGKYLLYEKNEVKARDREWKKYEFHYDNVLWALLTLFTVSTGEGWPQVLKHSVDATFENQGPSPGYRMEMSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKMMEEYSLEKNERACIDFAISAKPLTRHMPQNKQSFQYRMWQFVVSPPFEYTIMAMIALNTIVLMMKFYGASVAYENALRVFNIVFTSLFSLECVLKVMAFGILNYFRDAWNIFDFVTVLGSITDILVTEFGNNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIGIDVEDEDSDEDEFQITEHNNFRTFFQALMLLFRSATGEAWHNIMLSCLSGKPCDKNSGILTRECGNEFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEYVRVWAEYDPAAWGRMPYLDMYQMLRHMSPPLGLGKKCPARVAYKRLLRMDLPVADDNTVHFNSTLMALIRTALDIKIAKGGADKQQMDAELRKEMMAIWPNLSQKTLDLLVTPHKSTDLTVGKIYAAMMIMEYYRQSKAKKLQAMREEQDRTPLMFQRMEPPSPTQEGGPGQNALPSTQLDPGGALMAHESGLKESPSWVTQRAQEMFQKTGTWSPEQGPPTDMPNSQPNSQSVEMREMGRDGYSDSEHYLPMEGQGRAASMPRLPAENQRRRGRPRGNNLSTISDTSPMKRSASVLGPKARRLDDYSLERVPPEENQRHHQRRRDRSHRASERSLGRYTDVDTGLGTDLSMTTQSGDLPSKERDQERGRPKDRKHRQHHHHHHHHHHPPPPDKDRYAQERPDHGRARARDQRWSRSPSEGREHMAHRQGSSSVSGSPAPSTSGTSTPRRGRRQLPQTPSTPRPHVSYSPVIRKAGGSGPPQQQQQQQQQQQQQAVARPGRAATSGPRRYPGPTAEPLAGDRPPTGGHSSGRSPRMERRVPGPARSESPRACRHGGARWPASGPHVSEGPPGPRHHGYYRGSDYDEADGPGSGGGEEAMAGAYDAPPPVRHASSGATGRSPRTPRASGPACASPSRHGRRLPNGYYPAHGLARPRGPGSRKGLHEPYSESDDDWC TTX4QDJ TT Successful TTX4QDJ KE hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04721:Synaptic vesicle cycle; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04727:GABAergic synapse; hsa04728:Dopaminergic synapse; hsa04730:Long-term depression; hsa04742:Taste transduction; hsa04930:Type II diabetes mellitus; hsa05032:Morphine addiction; hsa05033:Nicotine addiction TTX4QDJ RC R-HSA-112308:Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels; R-HSA-422356:Regulation of insulin secretion TTPLQO0 ID TTPLQO0 TTPLQO0 TN Voltage-gated potassium channel Kv4.3 (KCND3) TTPLQO0 UP Q9UK17 TTPLQO0 UC KCND3_HUMAN TTPLQO0 BC Voltage-gated ion channel TTPLQO0 SN Voltage-gated potassium channel subunit Kv4.3; KCND3 TTPLQO0 GN KCND3 TTPLQO0 FC Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits. TTPLQO0 PD 2NZ0; 1S1G TTPLQO0 SQ MAAGVAAWLPFARAAAIGWMPVANCPMPLAPADKNKRQDELIVLNVSGRRFQTWRTTLERYPDTLLGSTEKEFFFNEDTKEYFFDRDPEVFRCVLNFYRTGKLHYPRYECISAYDDELAFYGILPEIIGDCCYEEYKDRKRENAERLMDDNDSENNQESMPSLSFRQTMWRAFENPHTSTLALVFYYVTGFFIAVSVITNVVETVPCGTVPGSKELPCGERYSVAFFCLDTACVMIFTVEYLLRLFAAPSRYRFIRSVMSIIDVVAIMPYYIGLVMTNNEDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSCASELGFLLFSLTMAIIIFATVMFYAEKGSSASKFTSIPASFWYTIVTMTTLGYGDMVPKTIAGKIFGSICSLSGVLVIALPVPVIVSNFSRIYHQNQRADKRRAQKKARLARIRVAKTGSSNAYLHSKRNGLLNEALELTGTPEEEHMGKTTSLIESQHHHLLHCLEKTTGLSYLVDDPLLSVRTSTIKNHEFIDEQMFEQNCMESSMQNYPSTRSPSLSSHPGLTTTCCSRRSKKTTHLPNSNLPATRLRSMQELSTIHIQGSEQPSLTTSRSSLNLKADDGLRPNCKTSQITTAIISIPTPPALTPEGESRPPPASPGPNTNIPSIASNVVKVSAL TTPLQO0 TT Successful TTPLQO0 RC R-HSA-1296072:Voltage gated Potassium channels TTAXZ0K ID TTAXZ0K TTAXZ0K TN Voltage-gated sodium channel alpha Nav1.3 (SCN3A) TTAXZ0K UP Q9NY46 TTAXZ0K UC SCN3A_HUMAN TTAXZ0K BC Voltage-gated ion channel TTAXZ0K SN Voltage-gated sodium channel subunit alpha Nav1.3; Voltage-gated sodium channel subtype III; Sodium channel protein, brain III subunit alpha; Sodium channel protein type III subunit alpha; Sodium channel protein type 3 subunit alpha; Sodium channel protein brain III subunit alpha; NAC3; KIAA1356 TTAXZ0K GN SCN3A TTAXZ0K FC Assuming opened or closed conformations in response to the voltage difference across the membrane, forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. May contribute to the regulation of serotonin/5-hydroxytryptamine release by enterochromaffin cells. In pancreatic endocrine cells, required for both glucagon and glucose-induced insulin secretion. Mediates the voltage-dependent sodium ion permeability of excitable membranes. TTAXZ0K SQ MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDNDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVMNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVSLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPSDSAFETNTTSYFNGTMDSNGTFVNVTMSTFNWKDYIGDDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAVAAASAASRDFSGIGGLGELLESSSEASKLSSKSAKEWRNRRKKRRQREHLEGNNKGERDSFPKSESEDSVKRSSFLFSMDGNRLTSDKKFCSPHQSLLSIRGSLFSPRRNSKTSIFSFRGRAKDVGSENDFADDEHSTFEDSESRRDSLFVPHRHGERRNSNVSQASMSSRMVPGLPANGKMHSTVDCNGVVSLVGGPSALTSPTGQLPPEGTTTETEVRKRRLSSYQISMEMLEDSSGRQRAVSIASILTNTMEELEESRQKCPPCWYRFANVFLIWDCCDAWLKVKHLVNLIVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLTVGNLVFTGIFTAEMVLKIIAMDPYYYFQEGWNIFDGIIVSLSLMELGLSNVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINDDCTLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVFMLVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDYVKNKMRECFQKAFFRKPKVIEIHEGNKIDSCMSNNTGIEISKELNYLRDGNGTTSGVGTGSSVEKYVIDENDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESELEESKEKLNATSSSEGSTVDVVLPREGEQAETEPEEDLKPEACFTEGCIKKFPFCQVSTEEGKGKIWWNLRKTCYSIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQTYFTNAWCWLDFLIVDVSLVSLVANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNMTTGNMFDISDVNNLSDCQALGKQARWKNVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRDVKLQPVYEENLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQGKYMTLVLSRINLVFIVLFTGEFVLKLVSLRHYYFTIGWNIFDFVVVILSIVGMFLAEMIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPDTIHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFSKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEDRFMASNPSKVSYEPITTTLKRKQEEVSAAIIQRNFRCYLLKQRLKNISSNYNKEAIKGRIDLPIKQDMIIDKLNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKESKGKEVRENQK TTAXZ0K TT Successful TTAXZ0K FM Sodium channel TTAXZ0K RC R-HSA-445095:Interaction between L1 and Ankyrins TTCPG9S ID TTCPG9S TTCPG9S TN 5-HT 1E receptor (HTR1E) TTCPG9S UP P28566 TTCPG9S UC 5HT1E_HUMAN TTCPG9S BC GPCR rhodopsin TTCPG9S SN Serotonin receptor 1E; S31; 5-hydroxytryptamine receptor 1E; 5-HT1E; 5-HT-1E; 5-HT 1E TTCPG9S GN HTR1E TTCPG9S FC Functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. G-protein coupled receptor for 5-hydroxytryptamine (serotonin). TTCPG9S SQ MNITNCTTEASMAIRPKTITEKMLICMTLVVITTLTTLLNLAVIMAIGTTKKLHQPANYLICSLAVTDLLVAVLVMPLSIIYIVMDRWKLGYFLCEVWLSVDMTCCTCSILHLCVIALDRYWAITNAIEYARKRTAKRAALMILTVWTISIFISMPPLFWRSHRRLSPPPSQCTIQHDHVIYTIYSTLGAFYIPLTLILILYYRIYHAAKSLYQKRGSSRHLSNRSTDSQNSFASCKLTQTFCVSDFSTSDPTTEFEKFHASIRIPPFDNDLDHPGERQQISSTRERKAARILGLILGAFILSWLPFFIKELIVGLSIYTVSSEVADFLTWLGYVNSLINPLLYTSFNEDFKLAFKKLIRCREHT TTCPG9S TT Successful TTCPG9S KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse TTCPG9S RC R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events TTRJYB6 ID TTRJYB6 TTRJYB6 TN Acid-sensing ion channel 1 (ASIC1) TTRJYB6 UP P78348 TTRJYB6 UC ASIC1_HUMAN TTRJYB6 BC Amiloride-sensitive sodium channel TTRJYB6 SN Brain sodium channel 2; BNaC2; Amiloride-sensitive cation channel 2, neuronal; ASIC1; ACCN2 TTRJYB6 GN ASIC1 TTRJYB6 FC Isoform 1 does not display proton-gated cation channel activity. TTRJYB6 SQ MELKAEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFHYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEVCSAEDFKVVFTRYGKCYTFNSGRDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVACQEQRLIYLPPPWGTCKAVTMDSDLDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHKLCRRGKCQKEAKRSSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC TTRJYB6 TT Successful TTRJYB6 KE hsa04750:Inflammatory mediator regulation of TRP channels TTRJYB6 RC R-HSA-2672351:Stimuli-sensing channels TTU5A6Q ID TTU5A6Q TTU5A6Q TN Adenine nucleotide translocator 1 (SLC25A4) TTU5A6Q UP P12235 TTU5A6Q UC ADT1_HUMAN TTU5A6Q BC Mitochondrial carrier TTU5A6Q SN Solute carrier family 25 member 4; SLC25A4; ANT1; ANT 1; ADP/ATP translocase 1; ADP,ATP carrier protein, heart/skeletal muscle isoform T1; ADP,ATP carrier protein 1 TTU5A6Q GN SLC25A4 TTU5A6Q FC Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. TTU5A6Q SQ MGDHAWSFLKDFLAGGVAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQLFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFHGLGDCIIKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIFVSWMIAQSVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGAKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV TTU5A6Q TT Successful TTU5A6Q KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa05012:Parkinson's disease; hsa05016:Huntington's disease; hsa05166:HTLV-I infection TTU5A6Q RC R-HSA-1268020:Mitochondrial protein import; R-HSA-422356:Regulation of insulin secretion TTG1FXO ID TTG1FXO TTG1FXO TN ALAS1 messenger RNA (ALAS1 mRNA) TTG1FXO UP P13196 TTG1FXO UC HEM1_HUMAN TTG1FXO SN ALAS-H; 5-aminolevulinic acid synthase 1; Delta-ALA synthase 1; Delta-aminolevulinate synthase 1 TTG1FXO GN ALAS1 TTG1FXO EC EC 2.3.1.37 TTG1FXO SQ MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKETPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPERVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLELKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA TTG1FXO TT Successful TT5AHZ0 ID TT5AHZ0 TT5AHZ0 TN Alcohol dehydrogenase 1A (ADH1A) TT5AHZ0 UP P07327 TT5AHZ0 UC ADH1A_HUMAN TT5AHZ0 SN Alcohol dehydrogenase subunit alpha; ADH1 TT5AHZ0 GN ADH1A TT5AHZ0 FC Facilitates the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+) to NADH. TT5AHZ0 EC EC 1.1.1.1 TT5AHZ0 PD 1U3T; 1HSO TT5AHZ0 SQ MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNPQGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTILMF TT5AHZ0 TT Successful TTV0PE2 ID TTV0PE2 TTV0PE2 TN Aspergillus Mannitol-1-phosphate 5-dehydrogenase (Asperg mpdA) TTV0PE2 UP Q4X1A4 TTV0PE2 UC MTLD_ASPFU TTV0PE2 BC Short-chain dehydrogenases reductase TTV0PE2 SN mpdA; MPDH; MPD; M1PDH TTV0PE2 GN Asperg mpdA TTV0PE2 FC Catalyzes the NAD(H)-dependent interconversion of D- fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway. Has a strong preference for NADH over NADPH. TTV0PE2 EC EC 1.1.1.17 TTV0PE2 SQ MGKKAIQFGGGNIGRGFVAEFLHEAGYEVVFIDVVDKIIDALKSTPSYEVTEVSEEGEKTKTITNYRAINSKTNEEDVVKEIGTADVVTCAVGPNVLKFIAPVIAKGIDARTASKPVAVIACENAIGATDTLRGFIEQNTDKDRLSSMSERARFANSAIDRIVPNQPPNAGLNVRIEKFYEWTVEQTPFGEFGHPDIPAIHWVDDLKPYIERKLFTVNTGHATTAYYGHMRGKKMIADALADAEIRQIVHKVLEQTAKLITTKHEITEQEQNEYVDTIVKRMSNPFLEDNVERVGRAPLRKLSRNERFIGPASQLAEKGLPFDALLGSIEMALRFQNVPGDEESAELAKILKEMSAEEATGKLTGLEKHHPLYEPVQNVIAKVQKDSK TTV0PE2 TT Successful TTJME02 ID TTJME02 TTJME02 TN Atrial natriuretic peptide receptor A (NPR1) TTJME02 UP P16066 TTJME02 UC ANPRA_HUMAN TTJME02 BC Phosphorus-oxygen lyase TTJME02 SN NPR1; NPR-A; GC-A; Atrial natriuretic peptide A-type receptor; ANPRA; ANP-A TTJME02 GN NPR1 TTJME02 FC Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand. TTJME02 EC EC 4.6.1.2 TTJME02 SQ MPGPRRPAGSRLRLLLLLLLPPLLLLLRGSHAGNLTVAVVLPLANTSYPWSWARVGPAVELALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAAVDLKWEHNPAVFLGPGCVYAAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWERQALMLYAYRPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGRVIYICSSPDAFRTLMLLALEAGLCGEDYVFFHLDIFGQSLQGGQGPAPRRPWERGDGQDVSARQAFQAAKIITYKDPDNPEYLEFLKQLKHLAYEQFNFTMEDGLVNTIPASFHDGLLLYIQAVTETLAHGGTVTDGENITQRMWNRSFQGVTGYLKIDSSGDRETDFSLWDMDPENGAFRVVLNYNGTSQELVAVSGRKLNWPLGYPPPDIPKCGFDNEDPACNQDHLSTLEVLALVGSLSLLGILIVSFFIYRKMQLEKELASELWRVRWEDVEPSSLERHLRSAGSRLTLSGRGSNYGSLLTTEGQFQVFAKTAYYKGNLVAVKRVNRKRIELTRKVLFELKHMRDVQNEHLTRFVGACTDPPNICILTEYCPRGSLQDILENESITLDWMFRYSLTNDIVKGMLFLHNGAICSHGNLKSSNCVVDGRFVLKITDYGLESFRDLDPEQGHTVYAKKLWTAPELLRMASPPVRGSQAGDVYSFGIILQEIALRSGVFHVEGLDLSPKEIIERVTRGEQPPFRPSLALQSHLEELGLLMQRCWAEDPQERPPFQQIRLTLRKFNRENSSNILDNLLSRMEQYANNLEELVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAVIDNFDVYKVETIGDAYMVVSGLPVRNGRLHACEVARMALALLDAVRSFRIRHRPQEQLRLRIGIHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGEALKIHLSSETKAVLEEFGGFELELRGDVEMKGKGKVRTYWLLGERGSSTRG TTJME02 TT Successful TTHDSE2 ID TTHDSE2 TTHDSE2 TN Bacterial Fumarate reductase flavoprotein (Bact frdA) TTHDSE2 UP O06913 TTHDSE2 UC FRDA_HELPY TTHDSE2 BC CH-CH donor oxidoreductase TTHDSE2 SN Fumarate reductase; FRDA TTHDSE2 GN Bact frdA TTHDSE2 FC Two distinct, membrane-bound, fad-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; The fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. TTHDSE2 EC EC 1.3.5.4 TTHDSE2 SQ MKITYCDALIIGGGLAGLRASIACKQKGLNTIVLSLVPVRRSHSAAAQGGMQASLANAKKSEGDNEDLHFLDTVKGSDWGCDQQVARMFVTTAPKAIRELASWGVPWTRIKKGDRPAVVNGEHVTITERDDRHGYILSRDFGGTKKWRTCFTADATGHTMLYAVANEALHHKVDIQDRKDMLAFIHHDNKCYGAVVRDLITGEISAYVSKGTLLATGGYGRVYKHTTNAVICDGAGAASALETGVAKLGNMEAVQFHPTALVPSGILMTEGCRGDGGVLRDKFGRRFMPAYEPEKKELASRDVVSRRILEHIQKGYGAKSPYGDHVWLDIAILGRNHVEKNLRDVRDIAMTFAGIDPADSKEQTKDNMQGVPANEPEYGQAMAKQKGWIPIKPMQHYSMGGVRTNPKGETHLKGLFCAGEAACWDLHGFNRLGGNSVSEAVVAGMIIGDYFASHCLEAQIEINTQKVEAFIKESQDYMHFLLHNEGKEDVYEIRERMKEVMDEKVGVFREGKRLEEALKELQELYARSKNICVKNKVLHNNPELEDAYRTKKMLKLALCITQGALLRTESRGAHTRIDYPKRDDEKWLNRTLASWPSAEQDMPTIEYEELDVMKMEISPDFRGYGKKGNFIPHPKKEERDAEILKTILELEKLGKDRIEVQHALMPFELQEKYKARNMRLEDEEVRARGEHLYSFNVHELLDQHNANLKGEHHE TTHDSE2 TT Successful TT8RHGB ID TT8RHGB TT8RHGB TN Bacterial Pyruvate decarboxylase (Bact aceE) TT8RHGB UP P0AFG8 TT8RHGB UC ODP1_ECOLI TT8RHGB BC Aldehyde/oxo donor oxidoreductase TT8RHGB SN aceE; Pyruvate decarboxylase E1 component TT8RHGB GN Bact aceE TT8RHGB FC The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-coa and co(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (e1), dihydrolipoamide acetyltransferase (e2) and lipoamide dehydrogenase. TT8RHGB PD 2QTC; 2QTA; 2IEA; 2G67; 2G28 TT8RHGB SQ MSERFPNDVDPIETRDWLQAIESVIREEGVERAQYLIDQLLAEARKGGVNVAAGTGISNYINTIPVEEQPEYPGNLELERRIRSAIRWNAIMTVLRASKKDLELGGHMASFQSSATIYDVCFNHFFRARNEQDGGDLVYFQGHISPGVYARAFLEGRLTQEQLDNFRQEVHGNGLSSYPHPKLMPEFWQFPTVSMGLGPIGAIYQAKFLKYLEHRGLKDTSKQTVYAFLGDGEMDEPESKGAITIATREKLDNLVFVINCNLQRLDGPVTGNGKIINELEGIFEGAGWNVIKVMWGSRWDELLRKDTSGKLIQLMNETVDGDYQTFKSKDGAYVREHFFGKYPETAALVADWTDEQIWALNRGGHDPKKIYAAFKKAQETKGKATVILAHTIKGYGMGDAAEGKNIAHQVKKMNMDGVRHIRDRFNVPVSDADIEKLPYITFPEGSEEHTYLHAQRQKLHGYLPSRQPNFTEKLELPSLQDFGALLEEQSKEISTTIAFVRALNVMLKNKSIKDRLVPIIADEARTFGMEGLFRQIGIYSPNGQQYTPQDREQVAYYKEDEKGQILQEGINELGAGCSWLAAATSYSTNNLPMIPFYIYYSMFGFQRIGDLCWAAGDQQARGFLIGGTSGRTTLNGEGLQHEDGHSHIQSLTIPNCISYDPAYAYEVAVIMHDGLERMYGEKQENVYYYITTLNENYHMPAMPEGAEEGIRKGIYKLETIEGSKGKVQLLGSGSILRHVREAAEILAKDYGVGSDVYSVTSFTELARDGQDCERWNMLHPLETPRVPYIAQVMNDAPAVASTDYMKLFAEQVRTYVPADDYRVLGTDGFGRSDSRENLRHHFEVDASYVVVAALGELAKRGEIDKKVVADAIAKFNIDADKVNPRLA TT8RHGB TT Successful TTVQ6R9 ID TTVQ6R9 TTVQ6R9 TN C1 esterase inhibitor (SERPING1) TTVQ6R9 UP P05155 TTVQ6R9 UC IC1_HUMAN TTVQ6R9 BC Serpin protein TTVQ6R9 SN Serpin G1; SERPING1; Plasma protease C1 inhibitor; C1inhibiting factor; C1Inh; C1 Inh TTVQ6R9 GN SERPING1 TTVQ6R9 FC Activation of the C1 complex is under control of the C1- inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein. {ECO:0000269|PubMed:8495195}. TTVQ6R9 PD 5DUQ; 5DU3; 2OAY; 1M6Q TTVQ6R9 SQ MASRLTLLTLLLLLLAGDRASSNPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTTEPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFVLWDQQHKFPVFMGRVYDPRA TTVQ6R9 TT Successful TTQT5S9 ID TTQT5S9 TTQT5S9 TN Cambridge pathology 1 antigen (CD52) TTQT5S9 UP P31358 TTQT5S9 UC CD52_HUMAN TTQT5S9 SN Epididymal secretory protein E5; CDW52; CD52 antigen; CD52 TTQT5S9 GN CD52 TTQT5S9 FC May play a role in carrying and orienting carbohydrate, as well as having a more specific role. TTQT5S9 SQ MKRFLFLLLTISLLVMVQIQTGLSGQNDTSQTSSPSASSNISGGIFLFFVANAIIHLFCFS TTQT5S9 TT Successful TTPX7I5 ID TTPX7I5 TTPX7I5 TN Carcinoembryonic antigen CGM1 (CD66d) TTPX7I5 UP P40198 TTPX7I5 UC CEAM3_HUMAN TTPX7I5 BC Immunoglobulin TTPX7I5 SN CGM1; CEACAM3; CD66d TTPX7I5 GN CEACAM3 TTPX7I5 FC Major granulocyte receptor mediating recognition and efficient opsonin-independent phagocytosis of CEACAM-binding microorganisms, including Neissiria, Moxarella and Haemophilus species, thus playing an important role in the clearance of pathogens by the innate immune system. Responsible for RAC1 stimulation in the course of pathogen phagocytosis. TTPX7I5 PD 6AW3; 6AW1; 6AW0; 6AVZ TTPX7I5 SQ MGPPSASPHRECIPWQGLLLTASLLNFWNPPTTAKLTIESMPLSVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNSLIVGYVIGTQQATPGAAYSGRETIYTNASLLIQNVTQNDIGFYTLQVIKSDLVNEEATGQFHVYQENAPGLPVGAVAGIVTGVLVGVALVAALVCFLLLAKTGRTSIQRDLKEQQPQALAPGRGPSHSSAFSMSPLSTAQAPLPNPRTAASIYEELLKHDTNIYCRMDHKAEVAS TTPX7I5 TT Successful TTQH65V ID TTQH65V TTQH65V TN Clostridium difficile Toxin B (CD toxB) TTQH65V UP P18177 TTQH65V UC TOXB_CLODI TTQH65V SN Toxin B TTQH65V GN CD toxB TTQH65V FC Cytotoxin. TTQH65V EC EC 3.4.22.- TTQH65V PD 6C0B; 6AR6; 5UQT; 5UQN; 5UQM TTQH65V SQ MSLVNRKQLEKMANVRFRTQEDEYVAILDALEEYHNMSENTVVEKYLKLKDINSLTDIYIDTYKKSGRNKALKKFKEYLVTEVLELKNNNLTPVEKNLHFVWIGGQINDTAINYINQWKDVNSDYNVNVFYDSNAFLINTLKKTVVESAINDTLESFRENLNDPRFDYNKFFRKRMEIIYDKQKNFINYYKAQREENPELIIDDIVKTYLSNEYSKEIDELNTYIEESLNKITQNSGNDVRNFEEFKNGESFNLYEQELVERWNLAAASDILRISALKEIGGMYLDVDMLPGIQPDLFESIEKPSSVTVDFWEMTKLEAIMKYKEYIPEYTSEHFDMLDEEVQSSFESVLASKSDKSEIFSSLGDMEASPLEVKIAFNSKGIINQGLISVKDSYCSNLIVKQIENRYKILNNSLNPAISEDNDFNTTTNTFIDSIMAEANADNGRFMMELGKYLRVGFFPDVKTTINLSGPEAYAAAYQDLLMFKEGSMNIHLIEADLRNFEISKTNISQSTEQEMASLWSFDDARAKAQFEEYKRNYFEGSLGEDDNLDFSQNIVVDKEYLLEKISSLARSSERGYIHYIVQLQGDKISYEAACNLFAKTPYDSVLFQKNIEDSEIAYYYNPGDGEIQEIDKYKIPSIISDRPKIKLTFIGHGKDEFNTDIFAGFDVDSLSTEIEAAIDLAKEDISPKSIEINLLGCNMFSYSINVEETYPGKLLLKVKDKISELMPSISQDSIIVSANQYEVRINSEGRRELLDHSGEWINKEESIIKDISSKEYISFNPKENKITVKSKNLPELSTLLQEIRNNSNSSDIELEEKVMLTECEINVISNIDTQIVEERIEEAKNLTSDSINYIKDEFKLIESISDALCDLKQQNELEDSHFISFEDISETDEGFSIRFINKETGESIFVETEKTIFSEYANHITEEISKIKGTIFDTVNGKLVKKVNLDTTHEVNTLNAAFFIQSLIEYNSSKESLSNLSVAMKVQVYAQLFSTGLNTITDAAKVVELVSTALDETIDLLPTLSEGLPIIATIIDGVSLGAAIKELSETSDPLLRQEIEAKIGIMAVNLTTATTAIITSSLGIASGFSILLVPLAGISAGIPSLVNNELVLRDKATKVVDYFKHVSLVETEGVFTLLDDKIMMPQDDLVISEIDFNNNSIVLGKCEIWRMEGGSGHTVTDDIDHFFSAPSITYREPHLSIYDVLEVQKEELDLSKDLMVLPNAPNRVFAWETGWTPGLRSLENDGTKLLDRIRDNYEGEFYWRYFAFIADALITTLKPRYEDTNIRINLDSNTRSFIVPIITTEYIREKLSYSFYGSGGTYALSLSQYNMGINIELSESDVWIIDVDNVVRDVTIESDKIKKGDLIEGILSTLSIEENKIILNSHEINFSGEVNGSNGFVSLTFSILEGINAIIEVDLLSKSYKLLISGELKILMLNSNHIQQKIDYIGFNSELQKNIPYSFVDSEGKENGFINGSTKEGLFVSELPDVVLISKVYMDDSKPSFGYYSNNLKDVKVITKDNVNILTGYYLKDDIKISLSLTLQDEKTIKLNSVHLDESGVAEILKFMNRKGNTNTSDSLMSFLESMNIKSIFVNFLQSNIKFILDANFIISGTTSIGQFEFICDENDNIQPYFIKFNTLETNYTLYVGNRQNMIVEPNYDLDDSGDISSTVINFSQKYLYGIDSCVNKVVISPNIYTDEINITPVYETNNTYPEVIVLDANYINEKINVNINDLSIRYVWSNDGNDFILMSTSEENKVSQVKIRFVNVFKDKTLANKLSFNFSDKQDVPVSEIILSFTPSYYEDGLIGYDLGLVSLYNEKFYINNFGMMVSGLIYINDSLYYFKPPVNNLITGFVTVGDDKYYFNPINGGAASIGETIIDDKNYYFNQSGVLQTGVFSTEDGFKYFAPANTLDENLEGEAIDFTGKLIIDENIYYFDDNYRGAVEWKELDGEMHYFSPETGKAFKGLNQIGDYKYYFNSDGVMQKGFVSINDNKHYFDDSGVMKVGYTEIDGKHFYFAENGEMQIGVFNTEDGFKYFAHHNEDLGNEEGEEISYSGILNFNNKIYYFDDSFTAVVGWKDLEDGSKYYFDEDTAEAYIGLSLINDGQYYFNDDGIMQVGFVTINDKVFYFSDSGIIESGVQNIDDNYFYIDDNGIVQIGVFDTSDGYKYFAPANTVNDNIYGQAVEYSGLVRVGEDVYYFGETYTIETGWIYDMENESDKYYFNPETKKACKGINLIDDIKYYFDEKGIMRTGLISFENNNYYFNENGEMQFGYINIEDKMFYFGEDGVMQIGVFNTPDGFKYFAHQNTLDENFEGESINYTGWLDLDEKRYYFTDEYIAATGSVIIDGEEYYFDPDTAQLVISE TTQH65V TT Successful TTY4IQ9 ID TTY4IQ9 TTY4IQ9 TN Corynebacterium Mutated CRM197 (Cory mTOX) TTY4IQ9 UP Q6NK15 (mutated) TTY4IQ9 UC Q6NK15_CORDI TTY4IQ9 SN Diphtheria toxin; DIP0222 TTY4IQ9 GN Cory mTOX TTY4IQ9 FC Contains a single base change in the structural gene resulting in the substitution of glutamic acid for glycine which blocks ADP-ribosylation. TTY4IQ9 EC EC 2.4.2.36 TTY4IQ9 PD 5I82 TTY4IQ9 SQ MSRKLFASILIGALLGIGAPPSAHAGADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMYEYMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQVIDSETADNLEKTTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNFVESIINLFQVVHNSYNRPAYSPGHKTQPFLHDGYAVSWNTVEDSIIRTGFQGESGHDIKITAENTPLPIAGVLLPTIPGKLDVNKSKTHISVNGRKIRMRCRAIDGDVTFCRPKSPVYVGNGVHANLHVAFHRSSSEKIHSNEISSDSIGVLGYQKTVDHTKVNSKLSLFFEIKS TTY4IQ9 TT Successful TT0F5P8 ID TT0F5P8 TT0F5P8 TN Cryptosporidium Pyruvate:ferredoxin oxidoreductase (Crypto CpPNO) TT0F5P8 UP Q968X7 TT0F5P8 UC PNO_CRYPV TT0F5P8 BC Aldehyde/oxo donor oxidoreductase TT0F5P8 SN Pyruvate:NADP+ oxidoreductase; PFOR; CpPNO TT0F5P8 GN Crypto CpPNO TT0F5P8 FC May have an important role in respiratorymetabolism. Cryptosporidium have a relic mitochondrion with no function in energy metabolism so it is not known if PFOR has a function. TT0F5P8 EC EC 1.2.1.51 TT0F5P8 SQ MGEKEIVDGCVAACHIAYACSEVAFTYPITPSSTISEVADSWMSRGRRNIFDQVVSVVEMQSEMGSAGALHGSLSVGCSTTTFTASQGLLLMIPNMYKIAGELWPCVFHVTARAIATSSLSIFGDHNDIMAARQTGWAFLGAMTVQEVMDLALVSHVSTFECSVPFVNFFDGFRTSHELQKIDMISYETIKKIFPYEKLKEFRERALNPTHPTLRGTATSSDVYFQLAEARNKYYESTPDIVQSVMDRLAKLIGRSYHLFDYYGHPDAEFLIVVMGSGGLTIEEMIDYLMEKSNEKVGMIKVRLFRPWSIDAFVKKIPKTTKRITVLERCKESGSLGEPLCLDVSTSIMRSELSSNNILVLGGRYGLASKEFTPGMALAVWENMISENPINNFSVGIDDDVTFKSLFVRQPRLDLLTSETKQCLFWGLGSDGTVSANKNAIKIIGESTDLQVQGYFAYDAKKAGGATMSHLRFGPKPIKSAYLLQRCDYVAVHHPSYVHKFDVLENIKQGGCFVLNCPWSTLEELNHELPSKIKHQIASRDVKFYVIDAQRIAQESNLGRRINNILMVVFFSLTNIIPLDLAIKLVKEAIKKTYGKKGDAVVNSNWKAVDLTLESLIQISYDKSQWISKDKCGEKSLPATAVETGNKDQEITKSTVLKQKPEHDVNQFVKDILGPVNALKGDELPVSMFEPTGTVPLGTTAYEKRGIAMSIPIVDMNKCTQCNYCSIVCPHAAIRPFLLDEAEFKNAPETMHIPKAKGGQEFSSYYYRIQVTPLDCTGCELCVHACPDDALHMEGLQKMEAVEKTHWDYLIGLPNKAEKFDRTTVKGSQFQQPLLEFSAACEGCGETPYVKLLTQLFGERMVIANATGCSSIWGASYPSVPYTKNQKGYGPAWGNSLFEDNAEYGLGMVVGYRQRRDRFRELVSNEILKDITEEEEFLKDDNASVQGRNEIITKYDHLKDYLRSWLKNIRNGEACQSLFEEISKLLEDNLINSNNFAQVLKKDRIELLEKLYDSRDLIPKISHWIVGGDGWAYDIGYAGLDHVLSFGEDVNIIILDTEVYSNTGGQASKSTPFGAIAKFAQSGNLRQKKDIGSIAMEYGSVYVASVALGANYSQTIKSLLEAEKYPGTSLIVAYSTCIEHGYTKYNLQQESVKLAVESGYWPLYRYNPELVRTEVVDNLTTIVSSGFTLDSKKVKVDIENFLKRENRFLQLIRSNPELASMAKDKLKAHSDKRFQKMKDMSENVTVTALKDQIKKLKDQLISIQNASKTGELAASGLINADLFIEQEMHVLYGTETGNSEEVAQYIQSQLVSRGYSSSSLNLDDLDIDEFLNPDKFSTVIIVTSTSGQGEFPGSSGILYEALLKKHLENQDDKFCSFMRFGIFGLGDSNYVFFNEAAKKWDKLLLDCGAVRIGAVGMGDDQSEEKYETELIEWLPDYLQLINAPEPKHDEKSEIPKATTFKVTILDSCRNDILNESTGTLCEKLDENNNIGNSHYKPIIPPNSVLLPVIENKRITNQDYDKDVRHIVFKLIGDGGDTPSLSYCLGDSLALYGQNPVNEAIKAIEMFGYNPYSLLRLSINEENEANNTNKVNQRYSSLFGYDITVLQLFVECLDLWGKPNRKFFQEFYRYCSNPEEKIQAKKWAQNEGKKLIEEFSSKTGTYLDVFKMFESARPTLAQLLDIVPFIKSRSYSIASCNKFVNGEKIELCVGIVDWKLESGEIRYGQCTGFLNRLPILDSESKIDSIPRLPSNIKASAFNLPFDYRSPVIMACMGTGIAPFRAFVQNKKYIRDVLKEEIGPVILYFGCRYYDNDYLYREELENYVKEGVITSLNIAFSRDPKGYKTSNCENIRYAQKMYVQHLMLENSQEIYENMIEKCGYFYLCGTKQVPIDIRKAIIQIIIKHSSTTEQVTSEEDANSILNSIQIMGRYNVEAWS TT0F5P8 TT Successful TTOGPL1 ID TTOGPL1 TTOGPL1 TN Cytomegalovirus Terminase UL56 (CMV TRM1) TTOGPL1 UP P16724 TTOGPL1 UC TRM1_HCMVA TTOGPL1 BC Herpesviridae UL28 TTOGPL1 SN UL56; Tripartite terminase subunit UL28 homolog; TRM1; Protein HFLF0 TTOGPL1 GN CMV TRM1 TTOGPL1 FC Component of the terminase, molecular motor that packages genomic DNA in empty capsid during assembly. TTOGPL1 SQ MEMNLLQKLCVVCSKCNEYAMELECLKYCDPNVLLAESTPFKRNAAAIVYLYRKIYPEVVAQNRTQSSLLTLYLEMLLKALHEDTALLDRALMAYSRQPDRAAFYRTVLRLDRCDRHHTVELQFTDNVRFSVSLATLNDIERFLCKMNYVYGILAPEAGLEVCAQLLELLRRLCGISPVARQEVYVEGTTCAQCYEELTIIPNQGRSLNKRLQGLLCNHIAVHRPSSQSDVNIQTVEQDLLDLTTRIPHLAGVLSALKSLFSSSSAYHSYIQEAEEALREYNLFTDIPERIYSLSDFTYWSRTSEVIVKRVGITIQQLNVYHQLCRALMNGISRHLYGEDVEDIFVLGEKALDGEERMFVGSVFAAPNRIIDLITSLSIQAFEDNPVFNKLHESNEMYTKIKHILEEIRRPLPDGTGGDGPEGEAIHLRGREAMSGTGTTLMTASNSSNSSTHSQRNNGGGGRARGGGKKVVGGGVNGQDGDGSENGLRVRNCDEHEALDLVDARSRIHNVTREVNVRKRAYLQKVSEVGYGKVIRCIKTQERLTSKLIDVNLVGPLCLDFISKLMNGFLYRSQYHQDQDVVDVGDQFTYDEHLYVVNNLIHKSLPVESLPLLGQQIYELCNGPLFTHCTDRYPLSHNVDMAYACDNAGVLPHVKDDLVKCAEGTVYPSEWMVVKYMGFFNFSDCQDLNVLQKEMWMHVRELVLSVALYNETFGKQLSIACLRDELHPDRDVILTYNKEWPLLLRHEGSLYKSKDLYLLLYRHLSRPDESGDVPTAPVAKPSTLTAAAAVSGVFREPDRPWLPSPYPSSSTAGVSRRVRATRKRPRRASSLLDLARDEHGIQDLVPGSLR TTOGPL1 TT Successful TTKY2NS ID TTKY2NS TTKY2NS TN Duffy antigen chemokine receptor (ACKR1) TTKY2NS UP Q16570 TTKY2NS UC ACKR1_HUMAN TTKY2NS BC GPCR duffy TTKY2NS SN Plasmodium vivax receptor; GpFy; Glycoprotein D; Fy glycoprotein; Duffy antigen/chemokine receptor; DARC; CD234; ACKR1 TTKY2NS GN ACKR1 TTKY2NS FC Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Has a promiscuous chemokine-binding profile, interacting with inflammatory chemokines of both the CXC and the CC subfamilies but not with homeostatic chemokines. Acts as a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13, CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1, TARC and also for the malaria parasites P.vivax and P.knowlesi. May regulate chemokine bioavailability and, consequently, leukocyte recruitment through two distinct mechanisms: when expressed in endothelial cells, it sustains the abluminal to luminal transcytosis of tissue-derived chemokines and their subsequent presentation to circulating leukocytes; when expressed in erythrocytes, serves as blood reservoir of cognate chemokines but also as a chemokine sink, buffering potential surges in plasma chemokine levels. TTKY2NS PD 4NUV; 4NUU TTKY2NS SQ MGNCLHRAELSPSTENSSQLDFEDVWNSSYGVNDSFPDGDYGANLEAAAPCHSCNLLDDSALPFFILTSVLGILASSTVLFMLFRPLFRWQLCPGWPVLAQLAVGSALFSIVVPVLAPGLGSTRSSALCSLGYCVWYGSAFAQALLLGCHASLGHRLGAGQVPGLTLGLTVGIWGVAALLTLPVTLASGASGGLCTLIYSTELKALQATHTVACLAIFVLLPLGLFGAKGLKKALGMGPGPWMNILWAWFIFWWPHGVVLGLDFLVRSKLLLLSTCLAQQALDLLLNLAEALAILHCVATPLLLALFCHQATRTLLPSLPLPEGWSSHLDTLGSKS TTKY2NS TT Successful TT2F0AU ID TT2F0AU TT2F0AU TN Ebola virus Envelope glycoprotein (EV GP) TT2F0AU UP Q05320 TT2F0AU UC VGP_EBOZM TT2F0AU SN GP1,2; GP TT2F0AU GN EV GP TT2F0AU FC Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, downregulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion. Down-modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1. This decrease in cell adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during infection (cytotoxicity) (Probable). Interacts with host TLR4 and thereby stimulates the differentiation and activation of monocytes leading to bystander death of T-lymphocytes. Downregulates as well the function of host natural killer cells. Counteracts the antiviral effect of host BST2/tetherin that restricts release of progeny virions from infected cells. However, cooperates with VP40 and host BST2 to activate canonical NF-kappa-B pathway in a manner dependent on neddylation. TT2F0AU SQ MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTVVSNGAKNISGQSPARTSSDPGTNTTTEDHKIMASENSSAMVQVHSQGREAAVSHLTTLATISTSPQSLTTKPGPDNSTHNTPVYKLDISEATQVEQHHRRTDNDSTASDTPSATTAAGPPKAENTNTSKSTDFLDPATTTSPQNHSETAGNNNTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRTRREAIVNAQPKCNPNLHYWTTQDEGAAIGLAWIPYFGPAAEGIYIEGLMHNQDGLICGLRQLANETTQALQLFLRATTELRTFSILNRKAIDFLLQRWGGTCHILGPDCCIEPHDWTKNITDKIDQIIHDFVDKTLPDQGDNDNWWTGWRQWIPAGIGVTGVIIAVIALFCICKFVF TT2F0AU TT Successful TT2IZ4K ID TT2IZ4K TT2IZ4K TN Fibroblast growth factor-23 (FGF23) TT2IZ4K UP Q9GZV9 TT2IZ4K UC FGF23_HUMAN TT2IZ4K BC Growth factor TT2IZ4K SN Tumor-derived hypophosphatemia-inducing factor; Phosphatonin; HYPF; Fibroblast growth factor 23; FGF-23 TT2IZ4K GN FGF23 TT2IZ4K FC Regulator of phosphate homeostasis. Inhibits renal tubular phosphate transport by reducing SLC34A1 levels. Upregulates EGR1 expression in the presence of KL (By similarity). Acts directly on the parathyroid to decrease PTH secretion (By similarity). Regulator of vitamin-D metabolism. Negatively regulates osteoblast differentiation and matrix mineralization. TT2IZ4K PD 5W21; 2P39 TT2IZ4K SQ MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARNSYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPGMNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRARMTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRPFAKFI TT2IZ4K TT Successful TTNV1KZ ID TTNV1KZ TTNV1KZ TN Fucosyltransferase IV (CD15) TTNV1KZ UP P22083 TTNV1KZ UC FUT4_HUMAN TTNV1KZ BC Glycosyltransferases TTNV1KZ SN Galactoside 3-L-fucosyltransferase; Fucosyltransferase 4; FucT-IV; Fuc-TIV; FCT3A; ELFT; ELAM-1 ligand fucosyltransferase; Alpha-(1,3)-fucosyltransferase 4 TTNV1KZ GN FUT4 TTNV1KZ FC May catalyze alpha-1,3 glycosidic linkages involved in the expression of Lewis X/SSEA-1 and VIM-2 antigens. TTNV1KZ EC EC 2.4.1.- TTNV1KZ SQ MRRLWGAARKPSGAGWEKEWAEAPQEAPGAWSGRLGPGRSGRKGRAVPGWASWPAHLALAARPARHLGGAGQGPRPLHSGTAPFHSRASGERQRRLEPQLQHESRCRSSTPADAWRAEAALPVRAMGAPWGSPTAAAGGRRGWRRGRGLPWTVCVLAAAGLTCTALITYACWGQLPPLPWASPTPSRPVGVLLWWEPFGGRDSAPRPPPDCRLRFNISGCRLLTDRASYGEAQAVLFHHRDLVKGPPDWPPPWGIQAHTAEEVDLRVLDYEEAAAAAEALATSSPRPPGQRWVWMNFESPSHSPGLRSLASNLFNWTLSYRADSDVFVPYGYLYPRSHPGDPPSGLAPPLSRKQGLVAWVVSHWDERQARVRYYHQLSQHVTVDVFGRGGPGQPVPEIGLLHTVARYKFYLAFENSQHLDYITEKLWRNALLAGAVPVVLGPDRANYERFVPRGAFIHVDDFPSASSLASYLLFLDRNPAVYRRYFHWRRSYAVHITSFWDEPWCRVCQAVQRAGDRPKSIRNLASWFER TTNV1KZ TT Successful TTEX6LM ID TTEX6LM TTEX6LM TN GABA(A) receptor gamma-3 (GABRG3) TTEX6LM UP Q99928 TTEX6LM UC GBRG3_HUMAN TTEX6LM BC Ligand-gated ion channel TTEX6LM SN GABRG3 TTEX6LM GN GABRG3 TTEX6LM FC Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functionsas receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand- gated chloride channel. TTEX6LM SQ MAPKLLLLLCLFSGLHARSRKVEEDEYEDSSSNQKWVLAPKSQDTDVTLILNKLLREYDKKLRPDIGIKPTVIDVDIYVNSIGPVSSINMEYQIDIFFAQTWTDSRLRFNSTMKILTLNSNMVGLIWIPDTIFRNSKTAEAHWITTPNQLLRIWNDGKILYTLRLTINAECQLQLHNFPMDEHSCPLIFSSYGYPKEEMIYRWRKNSVEAADQKSWRLYQFDFMGLRNTTEIVTTSAGDYVVMTIYFELSRRMGYFTIQTYIPCILTVVLSWVSFWIKKDATPARTALGITTVLTMTTLSTIARKSLPRVSYVTAMDLFVTVCFLFVFAALMEYATLNYYSSCRKPTTTKKTTSLLHPDSSRWIPERISLQAPSNYSLLDMRPPPTAMITLNNSVYWQEFEDTCVYECLDGKDCQSFFCCYEECKSGSWRKGRIHIDILELDSYSRVFFPTSFLLFNLVYWVGYLYL TTEX6LM TT Successful TTEX6LM KE hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction TTEX6LM RC R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation TT82EZV ID TT82EZV TT82EZV TN Glutamate receptor AMPA 3 (GRIA3) TT82EZV UP P42263 TT82EZV UC GRIA3_HUMAN TT82EZV BC Glutamate-gated ion channel TT82EZV SN Glutamate receptor ionotropic, AMPA 3; GluRK3; GluRC; GluR3; GluA3; GRIA3; AMPAselective glutamate receptor 3 TT82EZV GN GRIA3 TT82EZV FC Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. TT82EZV SQ MARQKKMGQSVLRAVFFLVLGLLGHSHGGFPNTISIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFSDQQISNDSASSENRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHLEDNNEEPRDPQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILVGGLGLAMMVALIEFCYKSRAESKRMKLTKNTQNFKPAPATNTQNYATYREGYNVYGTESVKI TT82EZV TT Successful TTPJR0G ID TTPJR0G TTPJR0G TN Glutamate receptor AMPA 4 (GRIA4) TTPJR0G UP P48058 TTPJR0G UC GRIA4_HUMAN TTPJR0G BC Glutamate-gated ion channel TTPJR0G SN Glutamate receptor ionotropic, AMPA 4; GluRD; GluR4; GluA4; GRIA4; AMPAselective glutamate receptor 4 TTPJR0G GN GRIA4 TTPJR0G FC Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the centralnervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. TTPJR0G SQ MRIISRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVIKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDVPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLDKLKNKWWYDKGECGPKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEAIRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP TTPJR0G TT Successful TTPJR0G KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04713:Circadian entrainment; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04728:Dopaminergic synapse; hsa05031:Amphetamine addiction; hsa05033:Nicotine addiction TTPJR0G RC R-HSA-399719:Trafficking of AMPA receptors; R-HSA-416993:Trafficking of GluR2-containing AMPA receptors; R-HSA-438066:Unblocking of NMDA receptor, glutamate binding and activation TTDSB34 ID TTDSB34 TTDSB34 TN G-protein coupled estrogen receptor 1 (GPER1) TTDSB34 UP Q99527 TTDSB34 UC GPER1_HUMAN TTDSB34 BC GPCR rhodopsin TTDSB34 SN Membrane estrogen receptor; Lymphocyte-derived G-protein coupled receptor; LYGPR; IL8-related receptor DRY12; GPER1; GPER; GPCR-BR; G-protein coupled receptor 30; Flow-induced endothelial G-protein coupled receptor 1; FEG-1; Chemoattractant receptor-like 2 TTDSB34 GN GPER1 TTDSB34 FC Receptor for estrogen. . TTDSB34 SQ MDVTSQARGVGLEMYPGTAQPAAPNTTSPELNLSHPLLGTALANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHERYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALARAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRVLVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLNPLIYSFLGETFRDKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV TTDSB34 TT Successful TTDSB34 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTNET8J ID TTNET8J TTNET8J TN G-protein coupled receptor 55 (GPR55) TTNET8J UP Q9Y2T6 TTNET8J UC GPR55_HUMAN TTNET8J BC GPCR rhodopsin TTNET8J SN LPIR1 TTNET8J GN GPR55 TTNET8J FC Receptor for L-alpha-lysophosphatidylinositol (LPI). LPI induces Ca(2+) release from intracellular stores via the heterotrimeric G protein GNA13 and RHOA. Putative cannabinoid receptor. May play a role in bone physiology by regulating osteoclast number and function. May be involved in hyperalgesia associated with inflammatory and neuropathic pain. TTNET8J SQ MSQQNTSGDCLFDGVNELMKTLQFAVHIPTFVLGLLLNLLAIHGFSTFLKNRWPDYAATSIYMINLAVFDLLLVLSLPFKMVLSQVQSPFPSLCTLVECLYFVSMYGSVFTICFISMDRFLAIRYPLLVSHLRSPRKIFGICCTIWVLVWTGSIPIYSFHGKVEKYMCFHNMSDDTWSAKVFFPLEVFGFLLPMGIMGFCCSRSIHILLGRRDHTQDWVQQKACIYSIAASLAVFVVSFLPVHLGFFLQFLVRNSFIVECRAKQSISFFLQLSMCFSNVNCCLDVFCYYFVIKEFRMNIRAHRPSRVQLVLQDTTISRG TTNET8J TT Successful TTNET8J FM GPCR rhodopsin TTNET8J RC R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events TTT4SY6 ID TTT4SY6 TTT4SY6 TN Hepatitis B virus Polymerase (HBV P) TTT4SY6 UP Q67889 TTT4SY6 UC Q67889_HBV TTT4SY6 BC DNA-directed DNA polymerase TTT4SY6 SN Protein P TTT4SY6 GN HBV P TTT4SY6 FC Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery. TTT4SY6 SQ MPLSYQHFRKLLLLDDGTGPLEEELPRLADEGLNRRVAEDLNLGNLNVSIPWTHKVGNFTGLYSSTVPVFNPHWKTPSFPNIHLHQDIIKKCEQFVGPLTVNEKRRLQLIMPARFYPKVTKYLPLDKGIKPYYPEHLVNHYFQTRHYLHTLWKAGILYKRETTHSASFCGSPYSWEQDLQHGAESIHQQSSGILSRPPVGSSLQSKHRKSRLGLQSQQGHLARRQQGRSWSIRAGFHPTARRPFGVEPSGSGHTTNFASKSASCLHQSPVRKAAYPSVSTFEKHSSSGHAVELHNLPPNSARSKSERPVFPCWWLQFRNSKPCSDYCLSLIVNLREDWGPCDDHGEHHIRIPRTPARVRGGVFLVDKNPHNTAESRLVVDFSQFSRGNYRVSWPKFAVPNLPSLTNLLSSNLSWLSLDVSAAFYHIPLHPAAMPHLLVGSSGLSRYVARLSSNSRYFNNQHGTMQNLHDSCSRNLYVSLLLLYQTFGRKLHLYSHPIILGFRKIPMAVGLSPFLLAQFTSAICSVVRRAFPHCLGFSYMDDVVLGAKSVQHRESLYTAVTNFLLSLGIHLNPNKTKRWGYSLNFMGYIIGSWGTLPQDHIVQKIKHCFRKLPVNRPIDWKVWQRIVGLLGFAAPFTQCGYPALMPLYACIQAKQAFTFSPTYKAFLSKQYMNLYPVARQRPGLCQVFADATPTGWGLA TTT4SY6 TT Successful TTCJ2X8 ID TTCJ2X8 TTCJ2X8 TN Hepatitis C virus Non-structural 5A (HCV NS5A) TTCJ2X8 UP P26662 (1973-2420) TTCJ2X8 UC POLG_HCV1 TTCJ2X8 BC Hepacivirus polyprotein TTCJ2X8 SN HCV NS5A TTCJ2X8 GN HCV NS5A TTCJ2X8 FC Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). TTCJ2X8 PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TTCJ2X8 SQ SGSWLRDIWDWICEVLSDFKTWLKAKLMPQLPGIPFVSCQRGYKGVWRVDGIMHTRCHCGAEITGHVKNGTMRIVGPRTCRNMWSGTFPINAYTTGPCTPLPAPNYTFALWRVSAEEYVEIRQVGDFHYVTGMTTDNLKCPCQVPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQLPCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSVASSSASQLSAPSLKATCTANHDSPDAELIEANLLWRQEMGGNITRVESENKVVILDSFDPLVAEEDEREISVPAEILRKSRRFAQALPVWARPDYNPPLVETWKKPDYEPPVVHGCPLPPPKSPPVPPPRKKRTVVLTESTLSTALAELATRSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDAESYSSMPPLEGEPGDPDLSDGSWSTVSSEANAEDVVCC TTCJ2X8 TT Successful TTIU7X1 ID TTIU7X1 TTIU7X1 TN Herpes simplex virus DNA polymerase UL30 (HSV UL30) TTIU7X1 UP P04293 TTIU7X1 UC DPOL_HHV11 TTIU7X1 BC DNA polymerase type-B TTIU7X1 SN HSV DNA polymerase catalytic subunit TTIU7X1 GN HSV UL30 TTIU7X1 FC Replicates viral genomic DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein. Additionally, the polymerase contains an intrinsic ribonuclease H (RNase H) activity that specifically degrades RNA/DNA heteroduplexes or duplex DNA substrates in the 5' to 3' direction. Therefore, it can catalyze the excision of the RNA primers that initiate the synthesis of Okazaki fragments at a replication fork during viral DNA replication. TTIU7X1 SQ MFSGGGGPLSPGGKSAARAASGFFAPAGPRGASRGPPPCLRQNFYNPYLAPVGTQQKPTGPTQRHTYYSECDEFRFIAPRVLDEDAPPEKRAGVHDGHLKRAPKVYCGGDERDVLRVGSGGFWPRRSRLWGGVDHAPAGFNPTVTVFHVYDILENVEHAYGMRAAQFHARFMDAITPTGTVITLLGLTPEGHRVAVHVYGTRQYFYMNKEEVDRHLQCRAPRDLCERMAAALRESPGASFRGISADHFEAEVVERTDVYYYETRPALFYRVYVRSGRVLSYLCDNFCPAIKKYEGGVDATTRFILDNPGFVTFGWYRLKPGRNNTLAQPAAPMAFGTSSDVEFNCTADNLAIEGGMSDLPAYKLMCFDIECKAGGEDELAFPVAGHPEDLVIQISCLLYDLSTTALEHVLLFSLGSCDLPESHLNELAARGLPTPVVLEFDSEFEMLLAFMTLVKQYGPEFVTGYNIINFDWPFLLAKLTDIYKVPLDGYGRMNGRGVFRVWDIGQSHFQKRSKIKVNGMVNIDMYGIITDKIKLSSYKLNAVAEAVLKDKKKDLSYRDIPAYYAAGPAQRGVIGEYCIQDSLLVGQLFFKFLPHLELSAVARLAGINITRTIYDGQQIRVFTCLLRLADQKGFILPDTQGRFRGAGGEAPKRPAAAREDEERPEEEGEDEDEREEGGGEREPEGARETAGRHVGYQGARVLDPTSGFHVNPVVVFDFASLYPSIIQAHNLCFSTLSLRADAVAHLEAGKDYLEIEVGGRRLFFVKAHVRESLLSILLRDWLAMRKQIRSRIPQSSPEEAVLLDKQQAAIKVVCNSVYGFTGVQHGLLPCLHVAATVTTIGREMLLATREYVHARWAAFEQLLADFPEAADMRAPGPYSMRIIYGDTDSIFVLCRGLTAAGLTAVGDKMASHISRALFLPPIKLECEKTFTKLLLIAKKKYIGVIYGGKMLIKGVDLVRKNNCAFINRTSRALVDLLFYDDTVSGAAAALAERPAEEWLARPLPEGLQAFGAVLVDAHRRITDPERDIQDFVLTAELSRHPRAYTNKRLAHLTVYYKLMARRAQVPSIKDRIPYVIVAQTREVEETVARLAALRELDAAAPGDEPAPPAALPSPAKRPRETPSPADPPGGASKPRKLLVSELAEDPAYAIAHGVALNTDYYFSHLLGAACVTFKALFGNNAKITESLLKRFIPEVWHPPDDVAARLRTAGFGAVGAGATAEETRRMLHRAFDTLA TTIU7X1 TT Successful TTT3ZC9 ID TTT3ZC9 TTT3ZC9 TN Human immunodeficiency virus Tat protein (HIV tat) TTT3ZC9 UP P04608 TTT3ZC9 UC TAT_HV1H2 TTT3ZC9 BC Lentiviruses Tat family TTT3ZC9 SN Transactivating regulatory protein; TAT protein TTT3ZC9 GN HIV tat TTT3ZC9 FC Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Endosomal low pH allows Tat to cross the endosome membrane to enter the cytosol and eventually further translocate into the nucleus, thereby inducing severe celldysfunctions ranging from cell activation to cell death. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Tat seems toinhibit the HAT activity of KAT5/Tip60 and TAF1, and consequently modify the expression of specific cellular genes. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines (such as IL10) or cytokine receptors. May be involved in the derepression of host interleukin IL2 expression. Mediates the activation of cyclin- dependent kinases and dysregulation of microtubule network. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Host extracellular matrix metalloproteinase MMP1 cleaves Tat and decreases Tat's mediated neurotoxicity. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. Binds to KDR/VEGFR-2. All these Tat-mediated effects enhance angiogenesis in Kaposi's sarcoma lesions. TTT3ZC9 PD 6MCF; 6MCE; 5V61; 4OR5; 3MIA TTT3ZC9 SQ MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAHQNSQTHQASLSKQPTSQPRGDPTGPKE TTT3ZC9 TT Successful TTDGEC0 ID TTDGEC0 TTDGEC0 TN Immunoglobulin epsilon Fc receptor gamma (FCERG) TTDGEC0 UP P30273 TTDGEC0 UC FCERG_HUMAN TTDGEC0 BC Immunoglobulin TTDGEC0 SN IgE Fc receptor subunit gamma; High affinity immunoglobulin epsilon receptor subunit gamma; FceRI gamma; FcRgamma; Fc receptor gamma-chain TTDGEC0 GN FCER1G TTDGEC0 FC As a component of the high-affinity immunoglobulin E (IgE) receptor, mediates allergic inflammatory signaling in mast cells. As a constitutive component of interleukin-3 receptor complex, selectively mediates interleukin 4/IL4 production by basophils, priming T-cells toward effector T-helper 2 subset. Associates with pattern recognition receptors CLEC4D and CLEC4E to form a functional signaling complex in myeloid cells. Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of ITAM, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes. May function cooperatively with other activating receptors. Functionally linked to integrin beta-2/ITGB2-mediated neutrophil activation. Also involved in integrin alpha-2/ITGA2-mediated platelet activation. Adapter protein containing an immunoreceptor tyrosine-based activation motif (ITAM) that transduces activation signals from various immunoreceptors. TTDGEC0 SQ MIPAVVLLLLLLVEQAAALGEPQLCYILDAILFLYGIVLTLLYCRLKIQVRKAAITSYEKSDGVYTGLSTRNQETYETLKHEKPPQ TTDGEC0 TT Successful TTDGEC0 KE hsa04071:Sphingolipid signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa05310:Asthma TTDGEC0 RC R-HSA-2454202:Fc epsilon receptor (FCERI) signaling; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-2871809:FCERI mediated Ca+2 mobilization; R-HSA-2871837:FCERI mediated NF-kB activation TTWORX6 ID TTWORX6 TTWORX6 TN Influenza Polymerase acidic endonuclease (Influ PA) TTWORX6 UP P03433 TTWORX6 UC PA_I34A1 TTWORX6 SN RNA-directed RNA polymerase subunit P2; Polymerase acidic protein TTWORX6 GN Influ PA TTWORX6 FC Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity. TTWORX6 EC EC 3.1.-.- TTWORX6 PD 5JHV; 5JHT; 5I13; 5FDG; 5FDD TTWORX6 SQ MEDFVRQCFNPMIVELAEKTMKEYGEDLKIETNKFAAICTHLEVCFMYSDFHFINEQGESIIVELGDPNALLKHRFEIIEGRDRTMAWTVVNSICNTTGAEKPKFLPDLYDYKENRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRKLADQSLPPNFSSLENFRAYVDGFEPNGYIEGKLSQMSKEVNARIEPFLKTTPRPLRLPNGPPCSQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMRTFFGWKEPNVVKPHEKGINPNYLLSWKQVLAELQDIENEEKIPKTKNMKKTSQLKWALGENMAPEKVDFDDCKDVGDLKQYDSDEPELRSLASWIQNEFNKACELTDSSWIELDEIGEDVAPIEHIASMRRNYFTSEVSHCRATEYIMKGVYINTALLNASCAAMDDFQLIPMISKCRTKEGRRKTNLYGFIIKGRSHLRNDTDVVNFVSMEFSLTDPRLEPHKWEKYCVLEIGDMLIRSAIGQVSRPMFLYVRTNGTSKIKMKWGMEMRRCLLQSLQQIESMIEAESSVKEKDMTKEFFENKSETWPIGESPKGVEESSIGKVCRTLLAKSVFNSLYASPQLEGFSAESRKLLLIVQALRDNLEPGTFDLGGLYEAIEECLINDPWVLLNASWFNSFLTHALS TTWORX6 TT Successful TT69OHW ID TT69OHW TT69OHW TN Interleukin 17 receptor (IL17R) TT69OHW UP Q96F46; Q9NRM6; Q9NRM6; Q8NFM7; Q8NFR9 TT69OHW UC I17RA_HUMAN; I17RB_HUMAN; I17RC_HUMAN; I17RD_HUMAN; I17RE_HUMAN TT69OHW BC Cytokine receptor TT69OHW SN Interleukin-17 receptor; IL-17R; IL-17 receptor TT69OHW GN IL17RA; IL17RB; IL17RC; IL17RD; IL17RE TT69OHW FC Receptor for IL17A, IL17F and, in dimer withIL17RE, for IL17C. Binds its IL17A ligand with low affinity, suggesting that additional components are involved in IL17A-induced signaling. TT69OHW SQ MGAARSPPSAVPGPLLGLLLLLLGVLAPGGASLRLLDHRALVCSQPGLNCTVKNSTCLDDSWIHPRNLTPSSPKDLQIQLHFAHTQQGDLFPVAHIEWTLQTDASILYLEGAELSVLQLNTNERLCVRFEFLSKLRHHHRRWRFTFSHFVVDPDQEYEVTVHHLPKPIPDGDPNHQSKNFLVPDCEHARMKVTTPCMSSGSLWDPNITVETLEAHQLRVSFTLWNESTHYQILLTSFPHMENHSCFEHMHHIPAPRPEEFHQRSNVTLTLRNLKGCCRHQVQIQPFFSSCLNDCLRHSATVSCPEMPDTPEPIPDYMPLWVYWFITGISILLVGSVILLIVCMTWRLAGPGSEKYSDDTKYTDGLPAADLIPPPLKPRKVWIIYSADHPLYVDVVLKFAQFLLTACGTEVALDLLEEQAISEAGVMTWVGRQKQEMVESNSKIIVLCSRGTRAKWQALLGRGAPVRLRCDHGKPVGDLFTAAMNMILPDFKRPACFGTYVVCYFSEVSCDGDVPDLFGAAPRYPLMDRFEEVYFRIQDLEMFQPGRMHRVGELSGDNYLRSPGGRQLRAALDRFRDWQVRCPDWFECENLYSADDQDAPSLDEEVFEEPLLPPGTGIVKRAPLVREPGSQACLAIDPLVGEEGGAAVAKLEPHLQPRGQPAPQPLHTLVLAAEEGALVAAVEPGPLADGAAVRLALAGEGEACPLLGSPGAGRNSVLFLPVDPEDSPLGSSTPMASPDLLPEDVREHLEGLMLSLFEQSLSCQAQGGCSRPAMVLTDPHTPYEEEQRQSVQSDQGYISRSSPQPPEGLTEMEEEEEEEQDPGKPALPLSPEDLESLRSLQRQLLFRQLQKNSGWDTMGSESEGPSA TT69OHW TT Successful TT69OHW KE hsa04060:Cytokine-cytokine receptor interaction TTXH9AD ID TTXH9AD TTXH9AD TN Interleukin 5 receptor alpha (IL5RA) TTXH9AD UP Q01344 TTXH9AD UC IL5RA_HUMAN TTXH9AD BC Cytokine receptor TTXH9AD SN Interleukin-5 receptor subunit alpha; IL5R; IL-5RA; IL-5R-alpha; IL-5R subunit alpha; IL-5 receptor subunit alpha; CDw125; CD125 TTXH9AD GN IL5RA TTXH9AD FC The alpha chain binds to IL5. This is the receptor for interleukin-5. TTXH9AD PD 6H41; 3VA2; 3QT2; 1OBZ; 1OBX TTXH9AD SQ MIIVAHVLLILLGATEILQADLLPDEKISLLPPVNFTIKVTGLAQVLLQWKPNPDQEQRNVNLEYQVKINAPKEDDYETRITESKCVTILHKGFSASVRTILQNDHSLLASSWASAELHAPPGSPGTSIVNLTCTTNTTEDNYSRLRSYQVSLHCTWLVGTDAPEDTQYFLYYRYGSWTEECQEYSKDTLGRNIACWFPRTFILSKGRDWLAVLVNGSSKHSAIRPFDQLFALHAIDQINPPLNVTAEIEGTRLSIQWEKPVSAFPIHCFDYEVKIHNTRNGYLQIEKLMTNAFISIIDDLSKYDVQVRAAVSSMCREAGLWSEWSQPIYVGNDEHKPLREWFVIVIMATICFILLILSLICKICHLWIKLFPPIPAPKSNIKDLFVTTNYEKAGSSETEIEVICYIEKPGVETLEDSVF TTXH9AD TT Successful TTU3X26 ID TTU3X26 TTU3X26 TN Iodothyronine deiodinase type I (DIO1) TTU3X26 UP P49895 TTU3X26 UC IOD1_HUMAN TTU3X26 SN Type-I 5'-deiodinase; Type I iodothyronine deiodinase; Type 1 DI; TXDI1; ITDI1; DIOI; 5DI TTU3X26 GN DIO1 TTU3X26 FC Plays a role in providing a source of plasma T3 by deiodination of T4 in peripheral tissues such as liver and kidney. Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2 (3,3'-diiodothyronine). TTU3X26 EC EC 1.21.99.4 TTU3X26 SQ MGLPQPGLWLKRLWVLLEVAVHVVVGKVLLILFPDRVKRNILAMGEKTGMTRNPHFSHDNWIPTFFSTQYFWFVLKVRWQRLEDTTELGGLAPNCPVVRLSGQRCNIWEFMQGNRPLVLNFGSCTUPSFMFKFDQFKRLIEDFSSIADFLVIYIEEAHASDGWAFKNNMDIRNHQNLQDRLQAAHLLLARSPQCPVVVDTMQNQSSQLYAALPERLYIIQEGRILYKGKSGPWNYNPEEVRAVLEKLHS TTU3X26 TT Successful TTU3X26 KE hsa04919:Thyroid hormone signaling pathway TT2GM5R ID TT2GM5R TT2GM5R TN Lymphocyte activation antigen CD30 (TNFRSF8) TT2GM5R UP P28908 TT2GM5R UC TNR8_HUMAN TT2GM5R SN Tumor necrosis factor receptor superfamily member 8; KI-1 antigen; D1S166E; CD30L receptor; CD30 TT2GM5R GN TNFRSF8 TT2GM5R FC May play a role in the regulation of cellular growth and transformation of activated lymphoblasts. Regulates gene expression through activation of NF-kappa-B. Receptor for TNFSF8/CD30L. TT2GM5R PD 1D01 TT2GM5R SQ MRVLLAALGLLFLGALRAFPQDRPFEDTCHGNPSHYYDKAVRRCCYRCPMGLFPTQQCPQRPTDCRKQCEPDYYLDEADRCTACVTCSRDDLVEKTPCAWNSSRVCECRPGMFCSTSAVNSCARCFFHSVCPAGMIVKFPGTAQKNTVCEPASPGVSPACASPENCKEPSSGTIPQAKPTPVSPATSSASTMPVRGGTRLAQEAASKLTRAPDSPSSVGRPSSDPGLSPTQPCPEGSGDCRKQCEPDYYLDEAGRCTACVSCSRDDLVEKTPCAWNSSRTCECRPGMICATSATNSCARCVPYPICAAETVTKPQDMAEKDTTFEAPPLGTQPDCNPTPENGEAPASTSPTQSLLVDSQASKTLPIPTSAPVALSSTGKPVLDAGPVLFWVILVLVVVVGSSAFLLCHRRACRKRIRQKLHLCYPVQTSQPKLELVDSRPRRSSTQLRSGASVTEPVAEERGLMSQPLMETCHSVGAAYLESLPLQDASPAGGPSSPRDLPEPRVSTEHTNNKIEKIYIMKADTVIVGTVKAELPEGRGLAGPAEPELEEELEADHTPHYPEQETEPPLGSCSDVMLSVEEEGKEDPLPTAASGK TT2GM5R TT Successful TT2GM5R FM Transmembrane protein TT2GM5R KE hsa04060:Cytokine-cytokine receptor interaction TTN6ORK ID TTN6ORK TTN6ORK TN Mcl-1 messenger RNA (MCL-1 mRNA) TTN6ORK UP Q07820 TTN6ORK UC MCL1_HUMAN TTN6ORK BC mRNA target TTN6ORK SN mcl1/EAT (mRNA); Induced myeloid leukemia cell differentiation protein Mcl-1 (mRNA); Bcl2-L-3 (mRNA); Bcl-2-related protein EAT/mcl1 (mRNA); Bcl-2-like protein 3 (mRNA); BCL2L3 (mRNA) TTN6ORK GN MCL1 TTN6ORK FC Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis. Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. TTN6ORK PD 6OVC; 6OQN; 6OQD; 6OQC; 6OQB TTN6ORK SQ MFGLKRNAVIGLNLYCGGAGLGAGSGGATRPGGRLLATEKEASARREIGGGEAGAVIGGSAGASPPSTLTPDSRRVARPPPIGAEVPDVTATPARLLFFAPTRRAAPLEEMEAPAADAIMSPEEELDGYEPEPLGKRPAVLPLLELVGESGNNTSTDGSLPSTPPPAEEEEDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGGIRNVLLAFAGVAGVGAGLAYLIR TTN6ORK TT Successful TTN6ORK FM mRNA target TTPWFDX ID TTPWFDX TTPWFDX TN Melanocortin receptor 2 (MC2R) TTPWFDX UP Q01718 TTPWFDX UC ACTHR_HUMAN TTPWFDX BC GPCR rhodopsin TTPWFDX SN Melanocortin-2 receptor; MC2-R; Adrenocorticotropin receptor; Adrenocorticotropic hormone receptor; ACTHR; ACTH-R; ACTH receptor TTPWFDX GN MC2R TTPWFDX FC Receptor for corticotropin (ACTH). This receptor is mediated by G proteins (G(s)) which activate adenylate cyclase (cAMP). TTPWFDX SQ MKHIINSYENINNTARNNSDCPRVVLPEEIFFTISIVGVLENLIVLLAVFKNKNLQAPMYFFICSLAISDMLGSLYKILENILIILRNMGYLKPRGSFETTADDIIDSLFVLSLLGSIFSLSVIAADRYITIFHALRYHSIVTMRRTVVVLTVIWTFCTGTGITMVIFSHHVPTVITFTSLFPLMLVFILCLYVHMFLLARSHTRKISTLPRANMKGAITLTILLGVFIFCWAPFVLHVLLMTFCPSNPYCACYMSLFQVNGMLIMCNAVIDPFIYAFRSPELRDAFKKMIFCSRYW TTPWFDX TT Successful TTPWFDX FM GPCR rhodopsin TTPWFDX KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTPWFDX RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events TTHQZV7 ID TTHQZV7 TTHQZV7 TN Mothers against decapentaplegic homolog 3 (SMAD3) TTHQZV7 UP P84022 TTHQZV7 UC SMAD3_HUMAN TTHQZV7 SN TGF-beta response effector Smad3; Smad3; SMAD family member 3; SMAD 3; Mothers against DPP homolog 3; Mad3; MMad3; MADH3; MAD homolog 3; JV15-2; HSMAD3; HMAD-3 TTHQZV7 GN SMAD3 TTHQZV7 FC Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. TTHQZV7 PD 5XOC; 5ODG; 5OD6; 2LB2; 2LAJ TTHQZV7 SQ MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS TTHQZV7 TT Successful TTH18TF ID TTH18TF TTH18TF TN Muscarinic acetylcholine receptor M5 (CHRM5) TTH18TF UP P08912 TTH18TF UC ACM5_HUMAN TTH18TF BC GPCR rhodopsin TTH18TF SN CHRM5 TTH18TF GN CHRM5 TTH18TF FC After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. TTH18TF SQ MEGDSYHNATTVNGTPVNHQPLERHRLWEVITIAAVTAVVSLITIVGNVLVMISFKVNSQLKTVNNYYLLSLACADLIIGIFSMNLYTTYILMGRWALGSLACDLWLALDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTPKRAGIMIGLAWLISFILWAPAILCWQYLVGKRTVPLDECQIQFLSEPTITFGTAIAAFYIPVSVMTILYCRIYRETEKRTKDLADLQGSDSVTKAEKRKPAHRALFRSCLRCPRPTLAQRERNQASWSSSRRSTSTTGKPSQATGPSANWAKAEQLTTCSSYPSSEDEDKPATDPVLQVVYKSQGKESPGEEFSAEETEETFVKAETEKSDYDTPNYLLSPAAAHRPKSQKCVAYKFRLVVKADGNQETNNGCHKVKIMPCPFPVAKEPSTKGLNPNPSHQMTKRKRVVLVKERKAAQTLSAILLAFIITWTPYNIMVLVSTFCDKCVPVTLWHLGYWLCYVNSTVNPICYALCNRTFRKTFKMLLLCRWKKKKVEEKLYWQGNSKLP TTH18TF TT Successful TTH18TF KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa04810:Regulation of actin cytoskeleton TTH18TF RC R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-416476:G alpha (q) signalling events TT6TMZU ID TT6TMZU TT6TMZU TN Mycobacterium Biosynthetic alanine racemase (MycB alr) TT6TMZU UP P94967 TT6TMZU UC ALR_MYCSM TT6TMZU BC Racemases and epimerases TT6TMZU SN D-alanine racemase; Alr; Alanine racemase; AlaR TT6TMZU GN MycB alr TT6TMZU FC Catalyzes the interconversion of L-alanine and D- alanine. Overexpression due to a natural mutation in the promoter is responsible for mediating resistance to D-cycloserine (DCS) in mycobacteria. TT6TMZU EC EC 5.1.1.1 TT6TMZU SQ MQTTEPMTPPAPLASAQTVIDLGAIDHNVRVLRELAGSADVMAVVKADAYGHGALPVARTALAAGAAALGVATIPEALALREGGITAPVLAWLHPPGTDFAPAIAADVEVAVSSRRQLEQVTAAAAEVGRTATVTVKVDTGLSRNGVGAADYPEVLDVLRRAQADGAIRVRGLMSHLVHGDDPENPFNGLQGQRLADMRVYAREHGVDYEVAHLCNSPAAMTRPDLAFEMVRPGISLYGLSPIPERGDMGLRPAMTLKCPVALVRSVHAGDGVSYGHRWVADRDTTLGLLPIGYADGVYRALSGRIDVLIKGRRRRAVGRICMDQFVVDLGPDADDVAVGDDAILFGPGANGEPTAQDWAELLDTIHYEVVTSPRGRVTRTYLPAGQQD TT6TMZU TT Successful TT54JVQ ID TT54JVQ TT54JVQ TN Neuronal acetylcholine receptor alpha-1 (CHRNA1) TT54JVQ UP P02708 TT54JVQ UC ACHA_HUMAN TT54JVQ BC Neurotransmitter receptor TT54JVQ SN CHNRA; Acetylcholine receptor subunit alpha; ACHRA TT54JVQ GN CHRNA1 TT54JVQ FC After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. TT54JVQ PD 5HBT; 4ZJS; 1Y6C; 1Y5T; 1Y5P TT54JVQ SQ MEPWPLLLLFSLCSAGLVLGSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQGDMVDLPRPSCVTLGVPLFSHLQNEQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPNWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAAEWKYVAMVMDHILLGVFMLVCIIGTLAVFAGRLIELNQQG TT54JVQ TT Successful TTL1ATN ID TTL1ATN TTL1ATN TN Neuronal acetylcholine receptor alpha-4/beta-2 (CHRNA4/B2) TTL1ATN UP P43681-P17787 TTL1ATN UC ACHA4_HUMAN; ACHB2_HUMAN TTL1ATN BC Neurotransmitter receptor TTL1ATN SN CHRN; nAChR TTL1ATN GN CHRNA4-CHRNB2 TTL1ATN FC After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodiun ions. TTL1ATN SQ MELGGPGAPRLLPPLLLLLGTGLLRASSHVETRAHAEERLLKKLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPADYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFHDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVNMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPTWVRRVFLDIVPRLLLMKRPSVVKDNCRRLIESMHKMASAPRFWPEPEGEPPATSGTQSLHPPSPSFCVPLDVPAEPGPSCKSPSDQLPPQQPLEAEKASPHPSPGPCRPPHGTQAPGLAKARSLSVQHMSSPGEAVEGGVRCRSRSIQYCVPRDDAAPEADGQAAGALASRNTHSAELPPPDQPSPCKCTCKKEPSSVSPSATVKTRSTKAPPPHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAGMI TTL1ATN TT Successful TTNFMS9 ID TTNFMS9 TTNFMS9 TN Protoporphyrinogen oxidase (PPOX) TTNFMS9 UP P50336 TTNFMS9 UC PPOX_HUMAN TTNFMS9 SN PPO TTNFMS9 GN PPOX TTNFMS9 FC Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. TTNFMS9 EC EC 1.3.3.4 TTNFMS9 PD 4IVO; 4IVM; 3NKS TTNFMS9 SQ MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRGIRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQALETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSPPGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS TTNFMS9 TT Successful TTX09M4 ID TTX09M4 TTX09M4 TN Ribonucleotide reductase (RIR) TTX09M4 UP P23921; P31350; Q7LG56 TTX09M4 UC RIR1_HUMAN; RIR2_HUMAN; RIR2B_HUMAN TTX09M4 BC CH/CH(2) oxidoreductase TTX09M4 SN Ribonucleoside diphosphate reductase; RIR1 TTX09M4 GN RIR TTX09M4 FC Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. The N-terminal region confers antiapoptotic activity in differentiated cells such as neurons and is importantfor viral reactivation to increase neural survivability. TTX09M4 SQ MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCSLENRDECLMCGS TTX09M4 TT Successful TTOBVIN ID TTOBVIN TTOBVIN TN Secretin receptor (SCT) TTOBVIN UP P09683 TTOBVIN UC SECR_HUMAN TTOBVIN BC GPCR secretin TTOBVIN SN SCTR; SCT-R; SCT TTOBVIN GN SCT TTOBVIN FC This is a receptor for secretin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. TTOBVIN SQ MAPRPLLLLLLLLGGSAARPAPPRARRHSDGTFTSELSRLREGARLQRLLQGLVGKRSEQDAENSMAWTRLSAGLLCPSGSNMPILQAWMPLDGTWSPWLPPGPMVSEPAGAAAEGTLRPR TTOBVIN TT Successful TTOBVIN KE hsa04080:Neuroactive ligand-receptor interaction; hsa04972:Pancreatic secretion; hsa04976:Bile secretion TTOBVIN RC R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors TT7ILZ1 ID TT7ILZ1 TT7ILZ1 TN SLAM family member 7 SLAMF7 (CS1) TT7ILZ1 UP Q9NQ25 TT7ILZ1 UC SLAF7_HUMAN TT7ILZ1 BC Immunoglobulin TT7ILZ1 SN UNQ576/PRO1138; SLAM family member 7; Protein 19A; Novel Ly9; Membrane protein FOAP-12; CRACC; CD319; CD2-like receptor-activating cytotoxic cells; CD2 subset 1 TT7ILZ1 GN SLAMF7 TT7ILZ1 FC SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Isoform 1 mediates NK cell activation through a SH2D1A-independent extracellular signal-regulated ERK-mediated pathway. Positively regulates NK cell functions by a mechanism dependent on phosphorylated SH2D1B. Downstream signaling implicates PLCG1, PLCG2 and PI3K. In addition to heterotypic NK cells-target cells interactions also homotypic interactions between NK cells may contribute to activation. However, in the absence of SH2D1B, inhibits NK cell function. Acts also inhibitory in T-cells. May play a role in lymphocyte adhesion. In LPS-activated monocytes negatively regulates production of proinflammatory cytokines. Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. TT7ILZ1 SQ MAGSPTCLTLIYILWQLTGSAASGPVKELVGSVGGAVTFPLKSKVKQVDSIVWTFNTTPLVTIQPEGGTIIVTQNRNRERVDFPDGGYSLKLSKLKKNDSGIYYVGIYSSSLQQPSTQEYVLHVYEHLSKPKVTMGLQSNKNGTCVTNLTCCMEHGEEDVIYTWKALGQAANESHNGSILPISWRWGESDMTFICVARNPVSRNFSSPILARKLCEGAADDPDSSMVLLCLLLVPLLLSLFVLGLFLWFLKRERQEEYIEEKKRVDICRETPNICPHSGENTEYDTIPHTNRTILKEDPANTVYSTVEIPKKMENPHSLLTMPDTPRLFAYENVI TT7ILZ1 TT Successful TTLWPVF ID TTLWPVF TTLWPVF TN Sodium/glucose cotransporter 2 (SGLT2) TTLWPVF UP P31639 TTLWPVF UC SC5A2_HUMAN TTLWPVF BC Solute:sodium symporter TTLWPVF SN Solute carrier family 5 member 2; Na(+)/glucose cotransporter 2; Low affinity sodium-glucose cotransporter TTLWPVF GN SLC5A2 TTLWPVF FC Has a Na(+) to glucose coupling ratio of 1:1. Sodium-dependent glucose transporter. TTLWPVF SQ MEEHTEAGSAPEMGAQKALIDNPADILVIAAYFLLVIGVGLWSMCRTNRGTVGGYFLAGRSMVWWPVGASLFASNIGSGHFVGLAGTGAASGLAVAGFEWNALFVVLLLGWLFAPVYLTAGVITMPQYLRKRFGGRRIRLYLSVLSLFLYIFTKISVDMFSGAVFIQQALGWNIYASVIALLGITMIYTVTGGLAALMYTDTVQTFVILGGACILMGYAFHEVGGYSGLFDKYLGAATSLTVSEDPAVGNISSFCYRPRPDSYHLLRHPVTGDLPWPALLLGLTIVSGWYWCSDQVIVQRCLAGKSLTHIKAGCILCGYLKLTPMFLMVMPGMISRILYPDEVACVVPEVCRRVCGTEVGCSNIAYPRLVVKLMPNGLRGLMLAVMLAALMSSLASIFNSSSTLFTMDIYTRLRPRAGDRELLLVGRLWVVFIVVVSVAWLPVVQAAQGGQLFDYIQAVSSYLAPPVSAVFVLALFVPRVNEQGAFWGLIGGLLMGLARLIPEFSFGSGSCVQPSACPAFLCGVHYLYFAIVLFFCSGLLTLTVSLCTAPIPRKHLHRLVFSLRHSKEEREDLDADEQQGSSLPVQNGCPESAMEMNEPQAPAPSLFRQCLLWFCGMSRGGVGSPPPLTQEEAAAAARRLEDISEDPSWARVVNLNALLMMAVAVFLWGFYA TTLWPVF TT Successful TTLWPVF FM Solute:sodium symporter TTLWPVF RC R-HSA-189200:Hexose transport; R-HSA-428808:Na+-dependent glucose transporters; R-HSA-429593:Inositol transporters TTWNFC2 ID TTWNFC2 TTWNFC2 TN Soluble guanylyl cyclase (GUCY2D) TTWNFC2 UP Q02846 TTWNFC2 UC GUC2D_HUMAN TTWNFC2 SN Rod outer segment membrane guanylate cyclase; Retinal guanylyl cyclase 1; ROS-GC; RETGC1; RETGC-1; RETGC; Guanylate cyclase 2D, retinal; GUC2D; GUC1A4; CORD6 TTWNFC2 GN GUCY2D TTWNFC2 FC Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction. TTWNFC2 EC EC 4.6.1.2 TTWNFC2 PD 1AWL TTWNFC2 SQ MTACARRAGGLPDPGLCGPAWWAPSLPRLPRALPRLPLLLLLLLLQPPALSAVFTVGVLGPWACDPIFSRARPDLAARLAAARLNRDPGLAGGPRFEVALLPEPCRTPGSLGAVSSALARVSGLVGPVNPAACRPAELLAEEAGIALVPWGCPWTQAEGTTAPAVTPAADALYALLRAFGWARVALVTAPQDLWVEAGRSLSTALRARGLPVASVTSMEPLDLSGAREALRKVRDGPRVTAVIMVMHSVLLGGEEQRYLLEAAEELGLTDGSLVFLPFDTIHYALSPGPEALAALANSSQLRRAHDAVLTLTRHCPSEGSVLDSLRRAQERRELPSDLNLQQVSPLFGTIYDAVFLLARGVAEARAAAGGRWVSGAAVARHIRDAQVPGFCGDLGGDEEPPFVLLDTDAAGDRLFATYMLDPARGSFLSAGTRMHFPRGGSAPGPDPSCWFDPNNICGGGLEPGLVFLGFLLVVGMGLAGAFLAHYVRHRLLHMQMVSGPNKIILTVDDITFLHPHGGTSRKVAQGSRSSLGARSMSDIRSGPSQHLDSPNIGVYEGDRVWLKKFPGDQHIAIRPATKTAFSKLQELRHENVALYLGLFLARGAEGPAALWEGNLAVVSEHCTRGSLQDLLAQREIKLDWMFKSSLLLDLIKGIRYLHHRGVAHGRLKSRNCIVDGRFVLKITDHGHGRLLEAQKVLPEPPRAEDQLWTAPELLRDPALERRGTLAGDVFSLAIIMQEVVCRSAPYAMLELTPEEVVQRVRSPPPLCRPLVSMDQAPVECILLMKQCWAEQPELRPSMDHTFDLFKNINKGRKTNIIDSMLRMLEQYSSNLEDLIRERTEELELEKQKTDRLLTQMLPPSVAEALKTGTPVEPEYFEQVTLYFSDIVGFTTISAMSEPIEVVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPQRNGQRHAAEIANMSLDILSAVGTFRMRHMPEVPVRIRIGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVNLSTVGILRALDSGYQVELRGRTELKGKGAEDTFWLVGRRGFNKPIPKPPDLQPGSSNHGISLQEIPPERRRKLEKARPGQFS TTWNFC2 TT Successful TTLXAKE ID TTLXAKE TTLXAKE TN Solute carrier family 29 member 1 (SLC29A1) TTLXAKE UP Q99808 TTLXAKE UC S29A1_HUMAN TTLXAKE SN SLC29A1; Nucleoside transporter, es-type; Nucleoside transporter 1; Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter; Equilibrative NBMPR-sensitive nucleoside transporter; ENT1 TTLXAKE GN SLC29A1 TTLXAKE FC Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). It is sensitive to low concentrations of the inhibitor nitrobenzylmercaptopurine riboside (nbmpr) and is sodium-independent. TTLXAKE SQ MTTSHQPQDRYKAVWLIFFMLGLGTLLPWNFFMTATQYFTNRLDMSQNVSLVTAELSKDAQASAAPAAPLPERNSLSAIFNNVMTLCAMLPLLLFTYLNSFLHQRIPQSVRILGSLVAILLVFLITAILVKVQLDALPFFVITMIKIVLINSFGAILQGSLFGLAGLLPASYTAPIMSGQGLAGFFASVAMICAIASGSELSESAFGYFITACAVIILTIICYLGLPRLEFYRYYQQLKLEGPGEQETKLDLISKGEEPRAGKEESGVSVSNSQPTNESHSIKAILKNISVLAFSVCFIFTITIGMFPAVTVEVKSSIAGSSTWERYFIPVSCFLTFNIFDWLGRSLTAVFMWPGKDSRWLPSLVLARLVFVPLLLLCNIKPRRYLTVVFEHDAWFIFFMAAFAFSNGYLASLCMCFGPKKVKPAEAETAGAIMAFFLCLGLALGAVFSFLFRAIV TTLXAKE TT Successful TTQ8KVI ID TTQ8KVI TTQ8KVI TN Staphylococcus 30S ribosomal subunit (Stap-coc pbp2) TTQ8KVI UP F4NA87 TTQ8KVI UC F4NA87_STAAU TTQ8KVI SN Penicillin-binding protein 2; Penicillin-binding protein; Penicillin binding protein PBP 2 TTQ8KVI GN Stap-coc pbp2 TTQ8KVI FC Subunite of bacterial 70s ribosomes. Invovled in protein biosynthesis. TTQ8KVI SQ MTENKGSSQPKKNGNNGGKSNSKKNRNVKRTIIKIIGFMIIAFFVVLLLGILLFAYYAWKAPAFTEAKLQDPIPAKIYDKNGELVKTLDNGQRHEHVNLKDVPKSMKDAVLATEDNRFYEHGALDYKRLFGAIGKNLTGGFGSEGASTLTQQVVKDAFLSQHKSIGRKAQEAYLSYRLEQEYSKDDIFQVYLNKIYYSDGVTGIKAAAKYYFNKDLKDLNLAEEAYLAGLPQVPNNYNIYDHPKAAEDRKNTVLYLMHYHKRITDKQWEDAKKIDLKANLVNRTAEERQNIDTNQDSEYNSYVNFVKSELMNNKAFKDENLGNVLQSGIKIYTNMDKDVQKTLQNDVDNGSFYKNKDQQVGATILDSKTGGLVAISGGRDFKDVVNRNQATDPHPTGSSLKPFLAYGPAIENMKWATNHAIQDESSYQVDGSTFRNYDVKSHGTVSIYDALRQSFNIPALKAWQSVKQNAGNDAPKKFAAKLGLNYEGDIGPSEVLGGSASEFSPTQLASAFAAIANGGTYNNAHSIQKVVTRDGETIEYDHTSHKAMSDYTAYMLAEMLKGTFKPYGSAYGHGVSGVNMGAKTGTGTYGAETYSQYNLPDNAAKDVWINGFTPQYTMSVWMGFSKVKQYGENSFVGHSQQEYPQFLYENVMSKISSRDGEDFKRPSSVSGSIPSINVSGSQDNNTTNRSTHGGSDTSANSSGTAQSNNNTRSQQSRNSGGLTGIFN TTQ8KVI TT Successful TTRVWAT ID TTRVWAT TTRVWAT TN Staphylococcus DNA gyrase A (Stap-coc gyrA) TTRVWAT UP P20831 TTRVWAT UC GYRA_STAAU TTRVWAT SN Stap-coc DNA gyrase subunit A TTRVWAT GN Stap-coc gyrA TTRVWAT FC A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. TTRVWAT EC EC 5.6.2.3 TTRVWAT PD 5BS3; 4PLB TTRVWAT SQ MAELPQSRINERNITSEMRESFLDYAMSVIVARALPDVRDGLKPVHRRILYGLNEQGMTPDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQGNFGSMDGDGAAAMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSVLPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLSKNPDISIAELMEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVIEERGGGRQRIVVTEIPFQVNKARMIEKIAELVRDKKIDGITDLRDETSLRTGVRVVIDVRKDANASVILNNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQKTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAMESLQQRFKLSEKQAQAILDMRLRRLTGLERDKIEAEYNELLNYISELEAILADEEVLLQLVRDELTEIRDRFGDDRRTEIQLGGFEDLEDEDLIPEEQIVITLSHNNYIKRLPVSTYRAQNRGGRGVQGMNTLEEDFVSQLVTLSTHDHVLFFTNKGRVYKLKGYEVPELSRQSKGIPVVNAIELENDEVISTMIAVKDLESEDNFLVFATKRGVVKRSALSNFSRINRNGKIAISFREDDELIAVRLTSGQEDILIGTSHASLIRFPESTLRPLGRTATGVKGITLREGDEVVGLDVAHANSVDEVLVVTENGYGKRTPVNDYRLSNRGGKGIKTATITERNGNVVCITTVTGEEDLMIVTNAGVIIRLDVADISQNGRAAQGVRLIRLGDDQFVSTVAKVKEDAEDETNEDEQSTSTVSEDGTEQQREAVVNDETPGNAIHTEVIDSEENDEDGRIEVRQDFMDRVEEDIQQSLDEDEE TTRVWAT TT Successful TT37GL6 ID TT37GL6 TT37GL6 TN Staphylococcus Leucyl-tRNA synthetase (Stap-coc leuS) TT37GL6 UP A6QHU1 TT37GL6 UC SYL_STAAE TT37GL6 BC Carbon-oxygen ligase TT37GL6 SN Leucyl-tRNA synthetase; Leucine--tRNA ligase; LeuRS TT37GL6 GN Stap-coc leuS TT37GL6 FC Catalyzes the chemical reaction: ATP + L-leucine + Trna = AMP + diphosphate + L-leucyl-tRNALeu TT37GL6 EC EC 6.1.1.4 TT37GL6 SQ MLNYNHNQIEKKWQDYWDENKTFKTNDNLGQKKFYALDMFPYPSGAGLHVGHPEGYTATDIISRYKRMQGYNVLHPMGWDAFGLPAEQYALDTGNDPREFTKKNIQTFKRQIKELGFSYDWDREVNTTDPEYYKWTQWIFIQLYNKGLAYVDEVAVNWCPALGTVLSNEEVIDGVSERGGHPVYRKPMKQWVLKITEYADQLLADLDDLDWPESLKDMQRNWIGRSEGAKVSFDVDNTEGKVEVFTTRPDTIYGASFLVLSPEHALVNSITTDEYKEKVKAYQTEASKKSDLERTDLAKDKSGVFTGAYATNPLSGEKVQIWIADYVLSTYGTGAIMAVPAHDDRDYEFAKKFDLPIIEVIEGGNVEEAAYTGEGKHINSGELDGLENEAAITKAIQLLEQKGAGEKKVNYKLRDWLFSRQRYWGEPIPVIHWEDGTMTTVPEEELPLLLPETDEIKPSGTGESPLANIDSFVNVVDEKTGMKGRRETNTMPQWAGSCWYYLRYIDPKNENMLADPEKLKHWLPVDLYIGGVEHAVLHLLYARFWHKVLYDLAIVPTKEPFQKLFNQGMILGEGNEKMSKSKGNVINPDDIVQSHGADTLRLYEMFMGPLDAAIAWSEKGLDGSRRFLDRVWRLMVNEDGTLSSKIVTTNNKSLDKVYNQTVKKVTEDFETLGFNTAISQLMVFINECYKVDEVYKPYIEGFVKMLAPIAPHIGEELWSKLGHEESITYQPWPTYDEALLVDDEVEIVVQVNGKLRAKIKIAKDTSKEEMQEIALSNDNVKASIEGKDIMKVIAVPQKLVNIVAK TT37GL6 TT Successful TTC1I86 ID TTC1I86 TTC1I86 TN Transthyretin (TTR) TTC1I86 UP P02766 TTC1I86 UC TTHY_HUMAN TTC1I86 SN TBPA; Prealbumin; PALB; ATTR TTC1I86 GN TTR TTC1I86 FC Probably transports thyroxine from the bloodstream to the brain. Thyroid hormone-binding protein. TTC1I86 PD 6IMY; 6IMX; 6GRP; 6GR7; 6FZL TTC1I86 SQ MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE TTC1I86 TT Successful TTC1I86 RC R-HSA-2453864:Retinoid cycle disease events; R-HSA-2453902:The canonical retinoid cycle in rods (twilight vision); R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-975634:Retinoid metabolism and transport; R-HSA-977225:Amyloid formation TTN9VTF ID TTN9VTF TTN9VTF TN Voltage-gated sodium channel alpha Nav1.9 (SCN11A) TTN9VTF UP Q9UI33 TTN9VTF UC SCNBA_HUMAN TTN9VTF BC Voltage-gated ion channel TTN9VTF SN hNaN; Sodium channel protein type XIsubunit alpha; Sodium channel protein type 11subunit alpha; Sensory neuron sodium channel 2; SNS2; SCN12A; SCN11A; Peripheral nerve sodium channel 5; PN5 TTN9VTF GN SCN11A TTN9VTF FC This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant sodium channel isoform. Also involved, with the contribution of the receptor tyrosine kinase NTRK2, in rapid BDNF-evoked neuronal depolarization. TTN9VTF SQ MDDRCYPVIFPDERNFRPFTSDSLAAIEKRIAIQKEKKKSKDQTGEVPQPRPQLDLKASRKLPKLYGDIPRELIGKPLEDLDPFYRNHKTFMVLNRKRTIYRFSAKHALFIFGPFNSIRSLAIRVSVHSLFSMFIIGTVIINCVFMATGPAKNSNSNNTDIAECVFTGIYIFEALIKILARGFILDEFSFLRDPWNWLDSIVIGIAIVSYIPGITIKLLPLRTFRVFRALKAISVVSRLKVIVGALLRSVKKLVNVIILTFFCLSIFALVGQQLFMGSLNLKCISRDCKNISNPEAYDHCFEKKENSPEFKMCGIWMGNSACSIQYECKHTKINPDYNYTNFDNFGWSFLAMFRLMTQDSWEKLYQQTLRTTGLYSVFFFIVVIFLGSFYLINLTLAVVTMAYEEQNKNVAAEIEAKEKMFQEAQQLLKEEKEALVAMGIDRSSLTSLETSYFTPKKRKLFGNKKRKSFFLRESGKDQPPGSDSDEDCQKKPQLLEQTKRLSQNLSLDHFDEHGDPLQRQRALSAVSILTITMKEQEKSQEPCLPCGENLASKYLVWNCCPQWLCVKKVLRTVMTDPFTELAITICIIINTVFLAMEHHKMEASFEKMLNIGNLVFTSIFIAEMCLKIIALDPYHYFRRGWNIFDSIVALLSFADVMNCVLQKRSWPFLRSFRVLRVFKLAKSWPTLNTLIKIIGNSVGALGSLTVVLVIVIFIFSVVGMQLFGRSFNSQKSPKLCNPTGPTVSCLRHWHMGDFWHSFLVVFRILCGEWIENMWECMQEANASSSLCVIVFILITVIGKLVVLNLFIALLLNSFSNEERNGNLEGEARKTKVQLALDRFRRAFCFVRHTLEHFCHKWCRKQNLPQQKEVAGGCAAQSKDIIPLVMEMKRGSETQEELGILTSVPKTLGVRHDWTWLAPLAEEEDDVEFSGEDNAQRITQPEPEQQAYELHQENKKPTSQRVQSVEIDMFSEDEPHLTIQDPRKKSDVTSILSECSTIDLQDGFGWLPEMVPKKQPERCLPKGFGCCFPCCSVDKRKPPWVIWWNLRKTCYQIVKHSWFESFIIFVILLSSGALIFEDVHLENQPKIQELLNCTDIIFTHIFILEMVLKWVAFGFGKYFTSAWCCLDFIIVIVSVTTLINLMELKSFRTLRALRPLRALSQFEGMKVVVNALIGAIPAILNVLLVCLIFWLVFCILGVYFFSGKFGKCINGTDSVINYTIITNKSQCESGNFSWINQKVNFDNVGNAYLALLQVATFKGWMDIIYAAVDSTEKEQQPEFESNSLGYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQQKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKCQGLVFDIVTSQIFDIIIISLIILNMISMMAESYNQPKAMKSILDHLNWVFVVIFTLECLIKIFALRQYYFTNGWNLFDCVVVLLSIVSTMISTLENQEHIPFPPTLFRIVRLARIGRILRLVRAARGIRTLLFALMMSLPSLFNIGLLLFLIMFIYAILGMNWFSKVNPESGIDDIFNFKTFASSMLCLFQISTSAGWDSLLSPMLRSKESCNSSSENCHLPGIATSYFVSYIIISFLIVVNMYIAVILENFNTATEESEDPLGEDDFDIFYEVWEKFDPEATQFIKYSALSDFADALPEPLRVAKPNKYQFLVMDLPMVSEDRLHCMDILFAFTARVLGGSDGLDSMKAMMEEKFMEANPLKKLYEPIVTTTKRKEEERGAAIIQKAFRKYMMKVTKGDQGDQNDLENGPHSPLQTLCNGDLSSFGVAKGKVHCD TTN9VTF TT Successful TTN9VTF RC R-HSA-445095:Interaction between L1 and Ankyrins TTCTAOJ ID TTCTAOJ TTCTAOJ TN Acetaldehyde dehydrogenase (ALDH) TTCTAOJ UP P00352; P05091; P30837 TTCTAOJ UC AL1A1_HUMAN; ALDH2_HUMAN; AL1B1_HUMAN TTCTAOJ BC Aldehyde/oxo donor oxidoreductase TTCTAOJ SN Aldehyde dehydrogenase; ALDH TTCTAOJ GN ALDH1A1; ALDH2; ALDH1B1 TTCTAOJ FC Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta- cleavage pathway for the degradation of 3-phenylpropanoate. Functionsas a chaperone protein for folding of MhpE. TTCTAOJ SQ MSSSGTPDLPVLLTDLKIQYTKIFINNEWHDSVSGKKFPVFNPATEEELCQVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESMNGGKLYSNAYLNDLAGCIKTLRYCAGWADKIQGRTIPIDGNFFTYTRHEPIGVCGQIIPWNFPLVMLIWKIGPALSCGNTVVVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVLADADLDNAVEFAHHGVFYHQGQCCIAASRIFVEESIYDEFVRRSVERAKKYILGNPLTPGVTQGPQIDKEQYDKILDLIESGKKEGAKLECGGGPWGNKGYFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGVFTKDIDKAITISSALQAGTVWVNCYGVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTVKISQKNS TTCTAOJ TT Successful TTPOI4B ID TTPOI4B TTPOI4B TN Acetyl-CoA:lyso-PAF acetyltransferase (PCAT) TTPOI4B UP Q8NF37; Q7L5N7 TTPOI4B UC PCAT1_HUMAN; PCAT2_HUMAN TTPOI4B SN Lysophosphatidylcholine acyltransferase; LysoPC acyltransferase; LysoPAFAT; Lyso-PAF acetyltransferase; LPCAT; LPC acyltransferase; Acyltransferase-like; Acetyl-CoA:lyso-platelet-activating factor acetyltransferase; AYTL; 1-alkylglycerophosphocholine O-acetyltransferase; 1-acylglycerophosphocholine O-acyltransferase TTPOI4B GN LPCAT1; LPCAT2 TTPOI4B FC Possesses both acyltransferase and acetyltransferase activities. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC), a major component of cell membranes and a PAF precursor. TTPOI4B SQ MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLVAAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPNKLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAEALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERARMKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFAEMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD TTPOI4B TT Successful TT037IE ID TT037IE TT037IE TN Aryl hydrocarbon receptor (AHR) TT037IE UP P35869 TT037IE UC AHR_HUMAN TT037IE SN bHLHe76; Class E basic helixloophelix protein 76; Class E basic helix-loop-helix protein 76; AhR; Ah receptor TT037IE GN AHR TT037IE FC Binds to the XRE promoter region of genes it activates. Activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Involved in cell-cycle regulation. Likely to play an important role in the development and maturation of many tissues. Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1. Inhibits PER1 by repressing the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of PER1. The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription. Ligand-activated transcriptional activator. TT037IE PD 5NJ8 TT037IE SQ MNSSSANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSSPTERNGGQDNCRAANFREGLNLQEGEFLLQALNGFVLVVTTDALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPSQCTESGQGIEEATGLPQTVVCYNPDQIPPENSPLMERCFICRLRCLLDNSSGFLAMNFQGKLKYLHGQKKKGKDGSILPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGRIVLGYTEAELCTRGSGYQFIHAADMLYCAESHIRMIKTGESGMIVFRLLTKNNRWTWVQSNARLLYKNGRPDYIIVTQRPLTDEEGTEHLRKRNTKLPFMFTTGEAVLYEATNPFPAIMDPLPLRTKNGTSGKDSATTSTLSKDSLNPSSLLAAMMQQDESIYLYPASSTSSTAPFENNFFNESMNECRNWQDNTAPMGNDTILKHEQIDQPQDVNSFAGGHPGLFQDSKNSDLYSIMKNLGIDFEDIRHMQNEKFFRNDFSGEVDFRDIDLTDEILTYVQDSLSKSPFIPSDYQQQQSLALNSSCMVQEHLHLEQQQQHHQKQVVVEPQQQLCQKMKHMQVNGMFENWNSNQFVPFNCPQQDPQQYNVFTDLHGISQEFPYKSEMDSMPYTQNFISCNQPVLPQHSKCTELDYPMGSFEPSPYPTTSSLEDFVTCLQLPENQKHGLNPQSAIITPQTCYAGAVSMYQCQPEPQHTHVGQMQYNPVLPGQQAFLNKFQNGVLNETYPAELNNINNTQTTTHLQPLHHPSEARPFPDLTSSGFL TT037IE TT Successful TTTX5M8 ID TTTX5M8 TTTX5M8 TN Aspergillus Mannitol 2-dehydrogenase (Asperg M2DH) TTTX5M8 UP Q4WQY4 TTTX5M8 UC M2DH_ASPFU TTTX5M8 BC Short-chain dehydrogenases reductase TTTX5M8 SN MDH; M2DH TTTX5M8 GN Asperg M2DH TTTX5M8 FC Catalyzes the NAD(H)-dependent interconversion of D- fructose and D-mannitol in the mannitol metabolic pathway. Has a preference for NADH over NADPH. TTTX5M8 SQ MAPLKLNSRNLSQIAAAGGALVKIPTYQRGRAVKEGIVHIGVGGFHRAHLAVYIDQLMQKHGVNDYAICGVGLQPFDSAMRDALASQDHLYTLIERSAKGSFAHVIGSINSYLFAPDNREAVIAKMAHPDTKIVSLTITESGYYYNENTHELQSEHPDIQFDLDPANEKAPRTTFGFLYAGLTRRYQQGLKPFTVMSCDNMQKNGSITRHMLESFARLRNPEVAEWIAEEGAFPNAMVDRITPQTSETDKTALAEKFGIVDSWPVVTEPFTQWVIEDQFSDGRPPFEKVGVQVVKDVHAVEQFEKHKLRLLNGSHSALGYPGQLAGFQYVHEVMANPLFRKFVWQMMQEEVKPLLPEIPGVDIDEYCNTLIERFTNPTIMDQLPRICLNASGKIPQFIMPSIAEAIWETGPFRRLCFVAAAWFHYIKGVDDRGKPFEVVDPMREELQAKARAGGNDPSELLSIKSLFGDDLRNDERFLREITTAMNDIARDGIMKTLPKYIN TTTX5M8 TT Successful TTRLPUB ID TTRLPUB TTRLPUB TN Bacillus anthracis Protective antigen (Anthrax PA) TTRLPUB UP P13423 TTRLPUB UC PAG_BACAN TTRLPUB SN Protective antigen; Anthrax toxins translocating protein; Anthrax PA83; Anthrax PA-83; Anthrax PA TTRLPUB GN Anthrax PA TTRLPUB FC One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death when injected, PA associated with EF produces edema. PA induces immunity to infection with anthrax. TTRLPUB PD 5FR3; 4NAM; 4H2A; 4EE2; 3TEZ TTRLPUB SQ MKKRKVLIPLMALSTILVSSTGNLEVIQAEVKQENRLLNESESSSQGLLGYYFSDLNFQAPMVVTSSTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQEVINKASNSNKIRLEKGRLYQIKIQYQRENPTEKGLDFKLYWTDSQNKKEVISSDNLQLPELKQKSSNSRKKRSTSAGPTVPDRDNDGIPDSLEVEGYTVDVKNKRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPLVAAYPIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEVHGNAEVHASFFDIGGSVSAGFSNSNSSTVAIDHSLSLAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPIALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNWSEVLPQIQETTARIIFNGKDLNLVERRIAAVNPSDPLETTKPDMTLKEALKIAFGFNEPNGNLQYQGKDITEFDFNFDQQTSQNIKNQLAELNATNIYTVLDKIKLNAKMNILIRDKRFHYDRNNIAVGADESVVKEAHREVINSSTEGLLLNIDKDIRKILSGYIVEIEDTEGLKEVINDRYDMLNISSLRQDGKTFIDFKKYNDKLPLYISNPNYKVNVYAVTKENTIINPSENGDTSTNGIKKILIFSKKGYEIG TTRLPUB TT Successful TTN6J5F ID TTN6J5F TTN6J5F TN Bacterial DNA gyrase (Bact gyrase) TTN6J5F UP P20831; P0A0K8 TTN6J5F UC GYRA_STAAU; GYRB_STAAU TTN6J5F BC ATP-hydrolyzing DNA topoisomerase TTN6J5F SN DNA gyrase TTN6J5F GN Bact gyrA; Bact gyrB TTN6J5F FC DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. TTN6J5F SQ MAELPQSRINERNITSEMRESFLDYAMSVIVARALPDVRDGLKPVHRRILYGLNEQGMTPDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQGNFGSMDGDGAAAMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSVLPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLSKNPDISIAELMEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVIEERGGGRQRIVVTEIPFQVNKARMIEKIAELVRDKKIDGITDLRDETSLRTGVRVVIDVRKDANASVILNNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQKTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAMESLQQRFKLSEKQAQAILDMRLRRLTGLERDKIEAEYNELLNYISELEAILADEEVLLQLVRDELTEIRDRFGDDRRTEIQLGGFEDLEDEDLIPEEQIVITLSHNNYIKRLPVSTYRAQNRGGRGVQGMNTLEEDFVSQLVTLSTHDHVLFFTNKGRVYKLKGYEVPELSRQSKGIPVVNAIELENDEVISTMIAVKDLESEDNFLVFATKRGVVKRSALSNFSRINRNGKIAISFREDDELIAVRLTSGQEDILIGTSHASLIRFPESTLRPLGRTATGVKGITLREGDEVVGLDVAHANSVDEVLVVTENGYGKRTPVNDYRLSNRGGKGIKTATITERNGNVVCITTVTGEEDLMIVTNAGVIIRLDVADISQNGRAAQGVRLIRLGDDQFVSTVAKVKEDAEDETNEDEQSTSTVSEDGTEQQREAVVNDETPGNAIHTEVIDSEENDEDGRIEVRQDFMDRVEEDIQQSLDEDEE TTN6J5F TT Successful TTR6YA2 ID TTR6YA2 TTR6YA2 TN Bacterial RNA polymerase sigma factor SigA (Bact sigA) TTR6YA2 UP P0A0J0 TTR6YA2 UC SIGA_STAA8 TTR6YA2 SN RNA polymerase sigma factor SigA TTR6YA2 GN Bact sigA TTR6YA2 FC Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. TTR6YA2 PD 4G94; 4G8X; 4G6D TTR6YA2 SQ MSDNTVKIKKQTIDPTLTLEDVKKQLIEKGKKEGHLSHEEIAEKLQNFDIDSDQMDDFFDQLNDNDISLVNEKDSSDTDEKLNPSDLSAPPGVKINDPVRMYLKEIGRVNLLSAQEEIELAKRIEQGDEVAKSRLAEANLRLVVSIAKRYVGRGMLFLDLIQEGNMGLIKAVEKFDFNKGFKFSTYATWWIRQAITRAIADQARTIRIPVHMVETINKLIRVQRQLLQDLGRDPAPEEIGEEMDLPAEKVREILKIAQEPVSLETPIGEEDDSHLGDFIEDQEAQSPSDHAAYELLKEQLEDVLDTLTDREENVLRLRFGLDDGRTRTLEEVGKVFGVTRERIRQIEAKALRKLRHPSRSKRLKDFMD TTR6YA2 TT Successful TTOJI4S ID TTOJI4S TTOJI4S TN Calcium-dependent chloride channel anoctamin (ANO) TTOJI4S UP Q5XXA6 TTOJI4S UC ANO1_HUMAN TTOJI4S SN Tumoramplified and overexpressed sequence 2; Tumor-amplified and overexpressed sequence 2; Transmembrane protein 16A; TMEM16A; TAOS2; Oral cancer overexpressed protein 2; ORAOV2; Discovered on gastrointestinal stromal tumors protein 1; DOG1; Anoctamin1; Anoctamin-1 TTOJI4S GN ANO1 TTOJI4S FC Required for the normal functioning of the interstitial cells of Cajal (ICCs) which generate electrical pacemaker activity in gastrointestinal smooth muscles. Acts as a major contributor to basal and stimulated chloride conductance in airway epithelial cells and plays an important role in tracheal cartilage development. Calcium-activated chloride channel (CaCC) which plays a role in transepithelial anion transport and smooth muscle contraction. TTOJI4S SQ MRVNEKYSTLPAEDRSVHIINICAIEDIGYLPSEGTLLNSLSVDPDAECKYGLYFRDGRRKVDYILVYHHKRPSGNRTLVRRVQHSDTPSGARSVKQDHPLPGKGASLDAGSGEPPMDYHEDDKRFRREEYEGNLLEAGLELERDEDTKIHGVGFVKIHAPWNVLCREAEFLKLKMPTKKMYHINETRGLLKKINSVLQKITDPIQPKVAEHRPQTMKRLSYPFSREKQHLFDLSDKDSFFDSKTRSTIVYEILKRTTCTKAKYSMGITSLLANGVYAAAYPLHDGDYNGENVEFNDRKLLYEEWARYGVFYKYQPIDLVRKYFGEKIGLYFAWLGVYTQMLIPASIVGIIVFLYGCATMDENIPSMEMCDQRHNITMCPLCDKTCSYWKMSSACATARASHLFDNPATVFFSVFMALWAATFMEHWKRKQMRLNYRWDLTGFEEEEEAVKDHPRAEYEARVLEKSLKKESRNKEKRRHIPEESTNKWKQRVKTAMAGVKLTDKVKLTWRDRFPAYLTNLVSIIFMIAVTFAIVLGVIIYRISMAAALAMNSSPSVRSNIRVTVTATAVIINLVVIILLDEVYGCIARWLTKIEVPKTEKSFEERLIFKAFLLKFVNSYTPIFYVAFFKGRFVGRPGDYVYIFRSFRMEECAPGGCLMELCIQLSIIMLGKQLIQNNLFEIGIPKMKKLIRYLKLKQQSPPDHEECVKRKQRYEVDYNLEPFAGLTPEYMEMIIQFGFVTLFVASFPLAPLFALLNNIIEIRLDAKKFVTELRRPVAVRAKDIGIWYNILRGIGKLAVIINAFVISFTSDFIPRLVYLYMYSKNGTMHGFVNHTLSSFNVSDFQNGTAPNDPLDLGYEVQICRYKDYREPPWSENKYDISKDFWAVLAARLAFVIVFQNLVMFMSDFVDWVIPDIPKDISQQIHKEKVLMVELFMREEQDKQQLLETWMEKERQKDEPPCNHHNTKACPDSLGSPAPSHAYHGGVL TTOJI4S TT Successful TTOJI4S FM Calcium-dependent chloride channel TTOJI4S RC R-HSA-2672351:Stimuli-sensing channels TTM9XSU ID TTM9XSU TTM9XSU TN Candida Squalene epoxidase (Candi ERG1) TTM9XSU UP Q92206 TTM9XSU UC ERG1_CANAL TTM9XSU SN Candi Squalene monooxygenase; Candi Squalene epoxidase; Candi SE TTM9XSU GN Candi ERG1 TTM9XSU FC Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis. TTM9XSU SQ MSSVKYDAIIIGAGVIGPTIATAFARQGRKVLIVERDWSKPDRIVGELMQPAGIKALRELGMIKAINNIRAVDCTGYYIKYYDETITIPYPLKKDACITNPVKPVPDAVDGVNDKLDSDSTLNVDDWDFDERVRGAAFHHGDFLMNLRQICRDEPNVTAVEATVTKILRDPSDPNTVIGVQTKQPSGTVDYHAKLTISCDGIYSKFRKELSPTNVPTIGSYFIGLYLKNAELPAKGKGHVLLGGHAPALIYSVSPTETRVLCVYVSSKPPSAANDAVYKYLRDNILPAIPKETVPAFKEALEERKFRIMPNQYLSAMKQGSENHKGFILLGDSLNMRHPLTGGGMTVGLNDSVLLAKLLHPKFVEDFDDHQLIAKRLKTFHRKRKNLDAVINTLSISLYSLFAADKKPLRILRNGCFKYFQRGGECVNGPIGLLSGMLPFPMLLFNHFFSVAFYSVYLNFIERGLLGFPLALFEAFEVLFTAIVIFTPYLWNEIVR TTM9XSU TT Successful TT23XSZ ID TT23XSZ TT23XSZ TN Core proteasome 20S complex (PS 20S) TT23XSZ UP P25786; P25787 TT23XSZ UC PSA1_HUMAN; PSA2_HUMAN TT23XSZ BC Peptidase TT23XSZ SN Proteasome subunit alpha; Proteasome component; PSC; Multicatalytic endopeptidase complex; Macropain; HC TT23XSZ GN PSMA1; PSMA2 TT23XSZ FC Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). TT23XSZ SQ MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH TT23XSZ TT Successful TT4SCBE ID TT4SCBE TT4SCBE TN Cytomegalovirus IE2 region messenger RNA (CMV IE2 mRNA) TT4SCBE UP P19893 TT4SCBE UC VIE2_HCMVA TT4SCBE BC mRNA target TT4SCBE SN Viral transcription factor IE2 (mRNA); UL122 (mRNA); Protein UL122 (mRNA); IE2 (mRNA) TT4SCBE GN CMV IE2 mRNA TT4SCBE FC Stimulates viral early and late gene expression and thus play a crucial role in the regulation of productive infection. In addition, activates quiescent cells to reenter the cell cycle and upregulates several E2F-responsive genes, which are responsible for pushing the cell into S phase. In S-phase, inhibits cellular DNA synthesis and blocks further cell cycle progression. TT4SCBE SQ MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFEQVTEDCNENPEKDVLAELGDILAQAVNHAGIDSSSTGPTLTTHSCSVSSAPLNKPTPTSVAVTNTPLPGASATPELSPRKKPRKTTRPFKVIIKPPVPPAPIMLPLIKQEDIKPEPDFTIQYRNKIIDTAGCIVISDSEEEQGEEVETRGATASSPSTGSGTPRVTSPTHPLSQMNHPPLPDPLGRPDEDSSSSSSSSCSSASDSESESEEMKCSSGGGASVTSSHHGRGGFGGAASSSLLSCGHQSSGGASTGPRKKKSKRISELDNEKVRNIMKDKNTPFCTPNVQTRRGRVKIDEVSRMFRNTNRSLEYKNLPFTIPSMHQVLDEAIKACKTMQVNNKGIQIIYTRNHEVKSEVDAVRCRLGTMCNLALSTPFLMEHTMPVTHPPEVAQRTADACNEGVKAAWSLKELHTHQLCPRSSDYRNMIIHAATPVDLLGALNLCLPLMQKFPKQVMVRIFSTNQGGFMLPIYETAAKAYAVGQFEQPTETPPEDLDTLSLAIEAAIQDLRNKSQ TT4SCBE TT Successful TT4SCBE FM mRNA target TTZCW3T ID TTZCW3T TTZCW3T TN Dihydropyrimidinase related protein 2 (DPYSL2) TTZCW3T UP Q16555 TTZCW3T UC DPYL2_HUMAN TTZCW3T SN Unc33like phosphoprotein 2; Unc-33-like phosphoprotein 2; ULIP2; ULIP-2; N2A3; Dihydropyrimidinaserelated protein 2; Dihydropyrimidinase-related protein 2; DRP2; DRP-2; Collapsin response mediator protein 2; CRMP2; CRMP-2 TTZCW3T GN DPYSL2 TTZCW3T FC Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis. Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. TTZCW3T PD 5YZB; 5YZA; 5YZ5; 5X1D; 5X1C TTZCW3T SQ MSYQGKKNIPRITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAELRGVPRGLYDGPVCEVSVTPKTVTPASSAKTSPAKQQAPPVRNLHQSGFSLSGAQIDDNIPRRTTQRIVAPPGGRANITSLG TTZCW3T TT Successful TTS7G69 ID TTS7G69 TTS7G69 TN Fusion protein Bcr-Abl (Bcr-Abl) TTS7G69 UP P11274-P00519 TTS7G69 UC BCR_HUMAN-ABL1_HUMAN TTS7G69 BC Kinase TTS7G69 SN BCR-ABL fusion protein; BCR-ABL TTS7G69 GN BCR-ABL1 TTS7G69 FC Activates downstream signaling pathways such as STAT5, PI3K/Akt, and Erk1/2 to lead to increased cell transformation, survival, and proliferation. TTS7G69 SQ MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEVMLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR TTS7G69 TT Successful TTLOKXP ID TTLOKXP TTLOKXP TN Gastric H(+)/K(+) ATPase (Proton pump) TTLOKXP UP P20648; P51164 TTLOKXP UC ATP4A_HUMAN; ATP4B_HUMAN TTLOKXP SN Proton pump; Potassium-transporting ATPase TTLOKXP GN ATP4A; ATP4B TTLOKXP FC Proton pump of the stomach. Exchanges potassium from the intestinal lumen with cytoplasmic hydronium and is the enzyme primarily responsible for the acidification of the stomach contents and the activation of the digestive enzyme pepsin. TTLOKXP SQ MGKAENYELYSVELGPGPGGDMAAKMSKKKKAGGGGGKRKEKLENMKKEMEINDHQLSVAELEQKYQTSATKGLSASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLAIALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILAAQGCKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTVQGLVVNTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFIVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQLYLNEKDYPPGYAFDVEAMNFPSSGLCFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPRNPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEGWFPLLCVGLRAQWEDHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEVCQIADVLIRKTRRLSAFQQGFFRNKILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPLPYGILIFVYDEIRKLGVRCCPGSWWDQELYY TTLOKXP TT Successful TTHC7JD ID TTHC7JD TTHC7JD TN Hepatitis C virus Serine protease NS3/4A (HCV NS3/4A) TTHC7JD UP P26664 (1027-1711) TTHC7JD UC POLG_HCV1 TTHC7JD SN HCV Hepacivirin/NS4A; HCV NS3P/NS4A; HCV p70/NS4A TTHC7JD GN HCV NS3/4A TTHC7JD FC Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). TTHC7JD PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TTHC7JD SQ APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCVVIVGRVVLSGKPAIIPDREVLYREFDEMEEC TTHC7JD TT Successful TTG90S6 ID TTG90S6 TTG90S6 TN Human immunodeficiency virus Glycoprotein 41 (HIV gp41) TTG90S6 UP P04578 (33-511) TTG90S6 UC ENV_HV1H2 TTG90S6 SN Env polyprotein gp41 (33-511) TTG90S6 GN HIV gp41 TTG90S6 FC Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C- terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin- dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. TTG90S6 PD 6DLN; 6DE7; 6BXQ; 6BXP; 6B9K TTG90S6 SQ KLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKR TTG90S6 TT Successful TTG8DNU ID TTG8DNU TTG8DNU TN Hyaluronic acid receptor (LYVE1) TTG8DNU UP Q9Y5Y7 TTG8DNU UC LYVE1_HUMAN TTG8DNU SN Lymphatic vessel endothelial hyaluronic acid receptor 1; LYVE1; Extracellular link domaincontaining protein 1; Cell surface retention sequencebindingprotein 1; CRSBP1 TTG8DNU GN LYVE1 TTG8DNU FC Ligand-specific transporter trafficking between intracellular organelles (TGN) and the plasma membrane. Plays a role in autocrine regulation of cell growth mediated by growth regulators containing cell surface retention sequence binding (CRS). May act as a hyaluronan (HA) transporter, either mediating its uptake for catabolism within lymphatic endothelial cells themselves, or its transport into the lumen of afferent lymphatic vessels for subsequent re-uptake and degradation in lymph nodes. TTG8DNU SQ MARCFSLVLLLTSIWTTRLLVQGSLRAEELSIQVSCRIMGITLVSKKANQQLNFTEAKEACRLLGLSLAGKDQVETALKASFETCSYGWVGDGFVVISRISPNPKCGKNGVGVLIWKVPVSRQFAAYCYNSSDTWTNSCIPEIITTKDPIFNTQTATQTTEFIVSDSTYSVASPYSTIPAPTTTPPAPASTSIPRRKKLICVTEVFMETSTMSTETEPFVENKAAFKNEAAGFGGVPTALLVLALLFFGAAAGLGFCYVKRYVKAFPFTNKNQQKEMIETKVVKEEKANDSNPNEESKKTDKNPEESKSPSKTTVRCLEAEV TTG8DNU TT Successful TTG8DNU RC R-HSA-2160916:Hyaluronan uptake and degradation TTC9IZL ID TTC9IZL TTC9IZL TN Inositol 1,4,5-trisphosphate receptor (ITPR) TTC9IZL UP Q14643; Q14571; Q14573 TTC9IZL UC ITPR1_HUMAN; ITPR2_HUMAN; ITPR3_HUMAN TTC9IZL SN InsP3R; InsP3 receptor; IP3R; IP3 receptor TTC9IZL GN ITPR1; ITPR2; ITPR3 TTC9IZL FC Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. TTC9IZL SQ MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENATEELEPSPPLRQLEDHKRGEALRQVLVNRYYGNVRPSGRRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPREELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA TTC9IZL TT Successful TT7ZMI1 ID TT7ZMI1 TT7ZMI1 TN Integrin alpha-4/beta-7 (ITGA4/B7) TT7ZMI1 UP P13612-P26010 TT7ZMI1 UC ITA4_HUMAN-ITB7_HUMAN TT7ZMI1 BC Integrin TT7ZMI1 SN alpha(4)beta(7) integrin; Alpha 4 beta 7 integrin TT7ZMI1 GN ITGA4-ITGB7 TT7ZMI1 FC It is expressed on lymphocytes and is responsible for T-cell homing into gut-associated lymphoid tissues through its binding to mucosal addressin cell adhesion molecule (MAdCAM), which is present on high endothelial venules of mucosal lymphoid organs. TT7ZMI1 SQ MVALPMVLVLLLVLSRGESELDAKIPSTGDATEWRNPHLSMLGSCQPAPSCQKCILSHPSCAWCKQLNFTASGEAEARRCARREELLARGCPLEELEEPRGQQEVLQDQPLSQGARGEGATQLAPQRVRVTLRPGEPQQLQVRFLRAEGYPVDLYYLMDLSYSMKDDLERVRQLGHALLVRLQEVTHSVRIGFGSFVDKTVLPFVSTVPSKLRHPCPTRLERCQSPFSFHHVLSLTGDAQAFEREVGRQSVSGNLDSPEGGFDAILQAALCQEQIGWRNVSRLLVFTSDDTFHTAGDGKLGGIFMPSDGHCHLDSNGLYSRSTEFDYPSVGQVAQALSAANIQPIFAVTSAALPVYQELSKLIPKSAVGELSEDSSNVVQLIMDAYNSLSSTVTLEHSSLPPGVHISYESQCEGPEKREGKAEDRGQCNHVRINQTVTFWVSLQATHCLPEPHLLRLRALGFSEELIVELHTLCDCNCSDTQPQAPHCSDGQGHLQCGVCSCAPGRLGRLCECSVAELSSPDLESGCRAPNGTGPLCSGKGHCQCGRCSCSGQSSGHLCECDDASCERHEGILCGGFGRCQCGVCHCHANRTGRACECSGDMDSCISPEGGLCSGHGRCKCNRCQCLDGYYGALCDQCPGCKTPCERHRDCAECGAFRTGPLATNCSTACAHTNVTLALAPILDDGWCKERTLDNQLFFFLVEDDARGTVVLRVRPQEKGADHTQAIVLGCVGGIVAVGLGLVLAYRLSVEIYDRREYSRFEKEQQQLNWKQDSNPLYKSAITTTINPRFQEADSPTLMAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD TT7ZMI1 TT Successful TT79JGK ID TT79JGK TT79JGK TN Mycobacterium RNA polymerase (MycB RNAP) TT79JGK UP P9WGZ1; P9WGY9; P9WGY7; P9WGY5 TT79JGK UC RPOA_MYCTU; RPOB_MYCTU; RPOC_MYCTU; RPOZ_MYCTU TT79JGK SN Transcriptase; RNAP; RNA polymerase; Mycobacterium DNA-directed RNA polymerase TT79JGK GN MycB rpoA; MycB rpoB; MycB rpoC; MycB rpoZ TT79JGK FC DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. TT79JGK SQ MLISQRPTLSEDVLTDNRSQFVIEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSIRIDGVLHEFTTVPGVKEDVTEIILNLKSLVVSSEEDEPVTMYLRKQGPGEVTAGDIVPPAGVTVHNPGMHIATLNDKGKLEVELVVERGRGYVPAVQNRASGAEIGRIPVDSIYSPVLKVTYKVDATRVEQRTDFDKLILDVETKNSISPRDALASAGKTLVELFGLARELNVEAEGIEIGPSPAEADHIASFALPIDDLDLTVRSYNCLKREGVHTVGELVARTESDLLDIRNFGQKSIDEVKIKLHQLGLSLKDSPPSFDPSEVAGYDVATGTWSTEGAYDEQDYAETEQL TT79JGK TT Successful TT79JGK KE mtu00230:Purine metabolism; mtu00240:Pyrimidine metabolism; mtu01100:Metabolic pathways; mtu03020:RNA polymerase TT35UGH ID TT35UGH TT35UGH TN Neuronal acetylcholine receptor alpha-3/beta-4 (CHRNA3/B4) TT35UGH UP P32297-P30926 TT35UGH UC ACHA3_HUMAN-ACHB4_HUMAN TT35UGH BC Neurotransmitter receptor TT35UGH SN Neuronal acetylcholine receptor TT35UGH GN CHRNA3-CHRNB4 TT35UGH FC A type of nicotinic acetylcholine receptor, consisting of 3 and 4 subunits. TT35UGH SQ MRRAPSLVLFFLVALCGRGNCRVANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIKLQLSLAQLISVNEREQIMTTNVWLKQEWTDYRLTWNSSRYEGVNILRIPAKRIWLPDIVLYNNADGTYEVSVYTNLIVRSNGSVLWLPPAIYKSACKIEVKYFPFDQQNCTLKFRSWTYDHTEIDMVLMTPTASMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLTTLLAILVFYLPSDCGEKMTLCISVLLALTFFLLLISKIVPPTSLDVPLIGKYLMFTMVLVTFSIVTSVCVLNVHHRSPSTHTMAPWVKRCFLHKLPTFLFMKRPGPDSSPARAFPPSKSCVTKPEATATSTSPSNFYGNSMYFVNPASAASKSPAGSTPVAIPRDFWLRSSGRFRQDVQEALEGVSFIAQHMKNDDEDQSVVEDWKYVAMVVDRLFLWVFMFVCVLGTVGLFLPPLFQTHAASEGPYAAQRDMGSGPLSLPLALSPPRLLLLLLLSLLPVARASEAEHRLFERLFEDYNEIIRPVANVSDPVIIHFEVSMSQLVKVDEVNQIMETNLWLKQIWNDYKLKWNPSDYGGAEFMRVPAQKIWKPDIVLYNNAVGDFQVDDKTKALLKYTGEVTWIPPAIFKSSCKIDVTYFPFDYQNCTMKFGSWSYDKAKIDLVLIGSSMNLKDYWESGEWAIIKAPGYKHDIKYNCCEEIYPDITYSLYIRRLPLFYTINLIIPCLLISFLTVLVFYLPSDCGEKVTLCISVLLSLTVFLLVITETIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHYRTPTTHTMPSWVKTVFLNLLPRVMFMTRPTSNEGNAQKPRPLYGAELSNLNCFSRAESKGCKEGYPCQDGMCGYCHHRRIKISNFSANLTRSSSSESVDAVLSLSALSPEIKEAIQSVKYIAENMKAQNEAKEIQDDWKYVAMVIDRIFLWVFTLVCILGTAGLFLQPLMAREDA TT35UGH TT Successful TTSNVHO ID TTSNVHO TTSNVHO TN Onchocerca Glutamate-gated chloride channel (Onchoc GluCl) TTSNVHO UP Q25634 TTSNVHO UC Q25634_ONCVO TTSNVHO BC Ion transport TTSNVHO SN Glutamate-gated chloride channel TTSNVHO GN Onchoc GluCl TTSNVHO FC As postsynaptic receptors within the crustacean stomatogastric ganglion. TTSNVHO SQ MNSFPIVCWNLAFLILVVAKKKLKEQEIIQRTLKDYDWRVRPRGNNLSWPDTGGPVLVSVNIYLRSISKIDDVNMEYSAQFTFREEWNDARLGYERLADENTQVPPFVVLAASEQPDLTQQIWMPDTFFQNEKEARRHLIDKPNVLIRIHPDGQILYSVRLSLVLSCPMSLEYYPLDRQTCLIDLASYAYTTDDIKYEWKVKNPIQQKEGLRQSLPSFELQDVLTEYCTSKTNTGEYSCARVLLLLRREYRFSYYLIQLYIPCIMLVVVSWVSFWLDKDAVPARVSLGVTTLLTMTTQASGINAKLPPVSYIKAVDVWIGVCLAFIFGALLEYALVNYHGRQEFLKKEKKK TTSNVHO TT Successful TTUCK4B ID TTUCK4B TTUCK4B TN Phospholipase A2 inhibitory protein (PA2IP) TTUCK4B UP P04083 TTUCK4B UC ANXA1_HUMAN TTUCK4B SN p35; Lipocortin I; LPC1; Chromobindin-9; Calpactin-2; Calpactin II; Annexin-1; Annexin I; Annexin A1; ANX1 TTUCK4B GN ANXA1 TTUCK4B FC Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (By similarity). Promotes resolution of inflammation and wound healing. Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors. Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells. Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells. Has no effect on unstimulated T cells. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton. Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes. Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). TTUCK4B PD 5VFW; 1QLS; 1BO9; 1AIN TTUCK4B SQ MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN TTUCK4B TT Successful TTZ82MR ID TTZ82MR TTZ82MR TN Plasmodium DNA gyrase (Malaria gyrase) TTZ82MR UP Q8I0X3 TTZ82MR UC Q8I0X3_PLAF7 TTZ82MR SN Malaria DNA gyrase subunit A TTZ82MR GN Malaria gyrase TTZ82MR FC Essential for replication and transcription in prokaryotes. Catalyses ATP-dependent DNA supercoiling activity. TTZ82MR EC EC 5.99.1.3 TTZ82MR SQ MSFKFSIVFVLYLLFLLKFNKRFIFLKSEKITSYINTQIPNYSSSPPFFLKKEAKNNIKKCYFIKREGYRNIGTKNASNAFVLNFKSNRSTYTDNAFSCTSLCSEKKERKKVQDPYDLKAKKKEKTYELNDIKNNEKKKDDIVNASNDITNDKLDNINNNINESRKLIKGEYYDVEICEILSKSFLSYANFLILNRCLCDYRDGLKTVQRRIIWSMYEINKGIDKKGYKKCARIVGEVIGKYHPHGDKSVYDALVRLAQKHHNNNLLIKGYGNFGSVEYNAAAMRYTEAKISSFCYDILLDEINDENVEYIKNFDGNEREPKVLCSKIPLLLINGCSGIAVSILSSIPCHNLIDVANCCINFLINENIRDDELFHIIKGPDFSTGGIIISKYDILKNIYNSGKGNFEIRSNVFFEYIKNDKKVITKHINDLSSIENSDIDKLTKKIIIKNLPPNVKPNELIENIINLLNDKKNEHDNILLRIRDESEKEDMRIVLELKKHSQIEQIHNFLSYLFKYTNMQISYHCNFVCIGYENTYTQFSLKSFIKLWCNNRIKFIKTNYEIKNKNLQKQLNIIDLYLIIQNKILDIITFFQKNQNIEQIQLYLKNNFKLNPEQIKYILSIKLQKLINIKNIDFISQRNKIMHQIKLNDEIINNVQNIKNLIIQELIYIKNKYGIHNLNKQCIIPSTPKYKYSYINSEYHPNFSKNKQIIDTYNTVSTNDNNINHSNYTHDLPNTDNVTKDKNVVETNVHKNIHISSDISNNIKNSDKNSSLTKNQDSDNMMPYRNTYIDSLDNNMKDIYNNDEVLILITYGGYIKKIKINEKLKNHSNNIIKLSNVKYILKENEEKLNENNKRLKFNDLQKGNEQEKYKDNEQKLNNDIGHNINIQNNNNDNNNNNNDNNNVLLLNEEEYNSYKIKKSILVRNRDKILLTDNYNKAFLLNVYDLHLSSYDSKGTPINQIIHSSKNITGITKFQENKKYLIVCSENGKMKVINNDVFLKRKKKGIKLFKNKKNIYFSYCNFNDNCIVGTKNGYIIQFPLSSFKISKKNSLGNKCISLAKNDKVVDLLSYENNEKNLKNYKIIFVTKNGFGKMINLNELKIQKKKGKGHRIMKFKKSKTRKDNKKDIEKKQINAINNKDKDKDIPSNNDDNNILHNTKVDEFLGFKLYDMNKQNEKDILIMITDHAVLIRKNMSLLKEKNKKHSSQIYAKMNKINQLVYFDII TTZ82MR TT Successful TT6NHYC ID TT6NHYC TT6NHYC TN Pneumocystis carinii Dihydropteroate synthase (PC DHPS) TT6NHYC UP P29251 (463-740) TT6NHYC UC FOL1_PNECA TT6NHYC SN PC DHPS TT6NHYC GN PC DHPS TT6NHYC FC Catalyzes three sequential steps of tetrahydrofolate biosynthesis. TT6NHYC EC EC 2.5.1.15 TT6NHYC SQ SFRSYKAPTYIMAILNLTPDSFFDGGIHSYDSVLIDVEKFINAGATIIDIGGQSTRPGSYIIPLEEEIFRVIPAIKYLQKTYPDILISIDTFRSEVAEQAVKAGASLVNDISGGRYDPKMFNTVARLKVPICIMHMRGNFLNMDNLTDYGTDIIEQITIELEKLLNSAEKSGIPRWNIILDPGLGFSKTLHQNIELLRRFNELKSKNCFNGLPWLLGPSRKRFTGFITGDNMPKDRIWGTVAAVVASISGGCDIIRVHDVYEMYKISKMSDAIWKEIY TT6NHYC TT Successful TT57ID8 ID TT57ID8 TT57ID8 TN Respiratory syncytial virus protein F (RSV F) TT57ID8 UP P03420 TT57ID8 UC FUS_HRSVA TT57ID8 SN Protein F; Fusion glycoprotein F1; Fusion glycoprotein F0; F TT57ID8 GN RSV F TT57ID8 FC Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C- terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (protein F) interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between host cell and virion membranes. Notably, RSV fusion protein is able to interact directly with heparan sulfate and therefore actively participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F expressed at the plasma membrane of infected cells mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53- dependent apoptosis. TT57ID8 PD 6OE5; 6OE4; 6APD; 6APB; 5W23 TT57ID8 SQ MELLILKANAITTILTAVTFCFASGQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKNAVTELQLLMQSTPPTNNRARRELPRFMNYTLNNAKKTNVTLSKKRKRRFLGFLLGVGSAIASGVAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPSEINLCNVDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGMDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITTIIIVIIVILLSLIAVGLLLYCKARSTPVTLSKDQLSGINNIAFSN TT57ID8 TT Successful TT23PYC ID TT23PYC TT23PYC TN Soluble guanylate cyclase (GCS) TT23PYC UP Q02108; Q02153 TT23PYC UC GCYA1_HUMAN; GCYB1_HUMAN TT23PYC BC Phosphorus-oxygen lyase TT23PYC SN GUCY1; GUCS; GUC1; GCS TT23PYC GN GUCY1A1; GUCY1B1 TT23PYC FC Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction. TT23PYC SQ MFCTKLKDLKITGECPFSLLAPGQVPNESSEEAAGSSESCKATVPICQDIPEKNIQESLPQRKTSRSRVYLHTLAESICKLIFPEFERLNVALQRTLAKHKIKESRKSLEREDFEKTIAEQAVAAGVPVEVIKESLGEEVFKICYEEDENILGVVGGTLKDFLNSFSTLLKQSSHCQEAGKRGRLEDASILCLDKEDDFLHVYYFFPKRTTSLILPGIIKAAAHVLYETEVEVSLMPPCFHNDCSEFVNQPYLLYSVHMKSTKPSLSPSKPQSSLVIPTSLFCKTFPFHFMFDKDMTILQFGNGIRRLMNRRDFQGKPNFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRRWDNSVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVLIGEQARAQDGLKKRLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQLWQGQVVQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDCPGFVFTPRSREELPPNFPSEIPGICHFLDAYQQGTNSKPCFQKKDVEDGNANFLGKASGID TT23PYC TT Successful TT09I7D ID TT09I7D TT09I7D TN Solute carrier family 19 member 1 (SLC19A1) TT09I7D UP P41440 TT09I7D UC S19A1_HUMAN TT09I7D SN Reduced folate carrier protein; RFC1; RFC; Placental folate transporter; Intestinal folate carrier 1; IFC-1; Folate transporter 1; FOLT; FLOT1 TT09I7D GN SLC19A1 TT09I7D FC Transporter for the intake of folate. Uptake of folate in human placental choriocarcinoma cells occurs by a novel mechanism called potocytosis which functionally couples three components, namely the folate receptor, the folate transporter, and a V-type H(+)-pump. TT09I7D SQ MVPSSPAVEKQVPVEPGPDPELRSWRHLVCYLCFYGFMAQIRPGESFITPYLLGPDKNFTREQVTNEITPVLSYSYLAVLVPVFLLTDYLRYTPVLLLQGLSFVSVWLLLLLGHSVAHMQLMELFYSVTMAARIAYSSYIFSLVRPARYQRVAGYSRAAVLLGVFTSSVLGQLLVTVGRVSFSTLNYISLAFLTFSVVLALFLKRPKRSLFFNRDDRGRCETSASELERMNPGPGGKLGHALRVACGDSVLARMLRELGDSLRRPQLRLWSLWWVFNSAGYYLVVYYVHILWNEVDPTTNSARVYNGAADAASTLLGAITSFAAGFVKIRWARWSKLLIAGVTATQAGLVFLLAHTRHPSSIWLCYAAFVLFRGSYQFLVPIATFQIASSLSKELCALVFGVNTFFATIVKTIITFIVSDVRGLGLPVRKQFQLYSVYFLILSIIYFLGAMLDGLRHCQRGHHPRQPPAQGLRSAAEEKAAQALSVQDKGLGGLQPAQSPPLSPEDSLGAVGPASLEQRQSDPYLAQAPAPQAAEFLSPVTTPSPCTLCSAQASGPEAADETCPQLAVHPPGVSKLGLQCLPSDGVQNVNQ TT09I7D TT Successful TTOP832 ID TTOP832 TTOP832 TN Solute carrier family 23 member 2 (SLC23A2) TTOP832 UP Q9UGH3 TTOP832 UC S23A2_HUMAN TTOP832 BC Nucleobase ascorbate transporter TTOP832 SN hSVCT2; Yolksac permease-like molecule 2; YSPL2; SVCT2; SLC23A2; Nucleobase transporter-like 1 protein; Na(+)/L-ascorbic acid transporter 2; NBTL1; KIAA0238 TTOP832 GN SLC23A2 TTOP832 FC Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate. TTOP832 SQ MMGIGKNTTSKSMEAGSSTEGKYEDEAKHPAFFTLPVVINGGATSSGEQDNEDTELMAIYTTENGIAEKSSLAETLDSTGSLDPQRSDMIYTIEDVPPWYLCIFLGLQHYLTCFSGTIAVPFLLADAMCVGYDQWATSQLIGTIFFCVGITTLLQTTFGCRLPLFQASAFAFLAPARAILSLDKWKCNTTDVSVANGTAELLHTEHIWYPRIREIQGAIIMSSLIEVVIGLLGLPGALLKYIGPLTITPTVALIGLSGFQAAGERAGKHWGIAMLTIFLVLLFSQYARNVKFPLPIYKSKKGWTAYKLQLFKMFPIILAILVSWLLCFIFTVTDVFPPDSTKYGFYARTDARQGVLLVAPWFKVPYPFQWGLPTVSAAGVIGMLSAVVASIIESIGDYYACARLSCAPPPPIHAINRGIFVEGLSCVLDGIFGTGNGSTSSSPNIGVLGITKVGSRRVIQCGAALMLALGMIGKFSALFASLPDPVLGALFCTLFGMITAVGLSNLQFIDLNSSRNLFVLGFSIFFGLVLPSYLRQNPLVTGITGIDQVLNVLLTTAMFVGGCVAFILDNTIPGTPEERGIRKWKKGVGKGNKSLDGMESYNLPFGMNIIKKYRCFSYLPISPTFVGYTWKGLRKSDNSRSSDEDSQATG TTOP832 TT Successful TTP3UTW ID TTP3UTW TTP3UTW TN Steroid hormone receptor ERR (ESRR) TTP3UTW UP P11474; O95718; P62508 TTP3UTW UC ERR1_HUMAN; ERR2_HUMAN; ERR3_HUMAN TTP3UTW BC Nuclear hormone receptor TTP3UTW SN Nuclear receptor subfamily 3 group B; NR3B; ERR TTP3UTW GN ESRRA; ESRRB; ESRRG TTP3UTW FC Intracellular receptors (typically cytoplasmic or nuclear). Initiates signal transduction for steroid hormones which lead to changes in gene expression over a time period of hours to days TTP3UTW SQ MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVALAPGPAPTRCLPGHKEEEDGEGAGPGEQGGGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAAPVNALVSHLLVVEPEKLYAMPDPAGPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD TTP3UTW TT Successful TT6HP1T ID TT6HP1T TT6HP1T TN Streptococcus Elongation factor G (Stre-coc fusA) TT6HP1T UP C1CC62 TT6HP1T UC EFG_STRZJ TT6HP1T BC Acid anhydrides hydrolase TT6HP1T SN fusA; EF-G TT6HP1T GN Stre-coc fusA TT6HP1T FC Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. TT6HP1T SQ MAREFSLEKTRNIGIMAHVDAGKTTTTERILYYTGKIHKIGETHEGASQMDWMEQEQERGITITSAATTAQWNNHRVNIIDTPGHVDFTIEVQRSLRVLDGAVTVLDSQSGVEPQTETVWRQATEYGVPRIVFANKMDKIGADFLYSVSTLHDRLQANAHPIQLPIGSEDDFRGIIDLIKMKAEIYTNDLGTDILEEDIPAEYLDQAQEYREKLIEAVAETDEELMMKYLEGEEITNEELKAGIRKATINVEFFPVLCGSAFKNKGVQLMLDAVIDYLPSPLDIPAIKGINPDTDAEETRPASDEEPFAALAFKIMTDPFVGRLTFFRVYSGVLQSGSYVLNTSKGKRERIGRILQMHANSRQEIDTVYSGDIAAAVGLKDTTTGDSLTDEKAKIILESINVPEPVIQLMVEPKSKADQDKMGIALQKLAEEDPTFRVETNVETGETVISGMGELHLDVLVDRMRREFKVEANVGAPQVSYRETFRASTQARGFFKRQSGGKGQFGDVWIEFTPNEEGKGFEFENAIVGGVVPREFIPAVEKGLVESMANGVLAGYPMVDVKAKLYDGSYHDVDSSETAFKIAASLSLKEAAKSAQPAILEPMMLVTITVPEENLGDVMGHVTARRGRVDGMEAHGNSQIVRAYVPLAEMFGYATVLRSASQGRGTFMMVFDHYEDVPKSVQEEIIKKNKGED TT6HP1T TT Successful TT5KSBY ID TT5KSBY TT5KSBY TN Surface glycoprotein LFA-3 (CD58) TT5KSBY UP P19256 TT5KSBY UC LFA3_HUMAN TT5KSBY SN Surface glycoprotein LFA3; Lymphocyte functionassociated antigen 3; Lymphocyte function-associated antigen 3; LFA3; Ag3 TT5KSBY GN CD58 TT5KSBY FC Ligand of the T-lymphocyte CD2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells, antigen-independent and -dependent interactions of T-lymphocytes with target cells and antigen-presenting cells and the T-lymphocyte rosetting with erythrocytes. In addition, the LFA-3/CD2 interaction may prime response by both the CD2+ and LFA-3+ cells. TT5KSBY PD 1QA9; 1CI5; 1CCZ TT5KSBY SQ MVAGSDAGRALGVLSVVCLLHCFGFISCFSQQIYGVVYGNVTFHVPSNVPLKEVLWKKQKDKVAELENSEFRAFSSFKNRVYLDTVSGSLTIYNLTSSDEDEYEMESPNITDTMKFFLYVLESLPSPTLTCALTNGSIEVQCMIPEHYNSHRGLIMYSWDCPMEQCKRNSTSIYFKMENDLPQKIQCTLSNPLFNTTSSIILTTCIPSSGHSRHRYALIPIPLAVITTCIVLYMNGILKCDRKPDRTNSN TT5KSBY TT Successful TTDJBV3 ID TTDJBV3 TTDJBV3 TN Tryptophan hydroxylase (TPH) TTDJBV3 UP P17752; Q8IWU9 TTDJBV3 UC TPH1_HUMAN; TPH2_HUMAN TTDJBV3 BC Paired donor oxygen oxidoreductase TTDJBV3 SN Tryptophan 5-monooxygenase; TPH TTDJBV3 GN TPH1; TPH2 TTDJBV3 FC Responsible for addition of the -HO group (hydroxylation) to the 5 position to form the amino acid 5-hydroxytryptophan (5-HTP), which is the initial and rate-limiting step in the synthesis of the neurotransmitter serotonin. TTDJBV3 SQ MIEDNKENKDHSLERGRASLIFSLKNEVGGLIKALKIFQEKHVNLLHIESRKSKRRNSEFEIFVDCDINREQLNDIFHLLKSHTNVLSVNLPDNFTLKEDGMETVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQELNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTIKRPFGVKYNPYTRSIQILKDTKSITSAMNELQHDLDVVSDALAKVSRKPSI TTDJBV3 TT Successful TTJ2PTI ID TTJ2PTI TTJ2PTI TN Tubulin beta-2 chain (TUBB2) TTJ2PTI UP Q13885 TTJ2PTI UC TBB2A_HUMAN TTJ2PTI SN Tubulin beta-2A chain; Tubulin beta class IIa; TUBB4B; BetaII-Tubulin; Beta(II)-Tubulin; Beta(II) isotype of Tubulin TTJ2PTI GN TUBB2A TTJ2PTI FC It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Tubulin is the major constituent of microtubules. TTJ2PTI SQ MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYSIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA TTJ2PTI TT Successful TTPRL03 ID TTPRL03 TTPRL03 TN Urokinase plasminogen activator surface receptor (PLAUR) TTPRL03 UP Q03405 TTPRL03 UC UPAR_HUMAN TTPRL03 SN Urokinase-type plasminogen activator receptor; Urokinase plasminogen activator receptor; Monocyte activation antigenMo3; CD87 antigen; CD87 TTPRL03 GN PLAUR TTPRL03 FC Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form. Acts as a receptor for urokinase plasminogen activator. TTPRL03 PD 4QTI; 4K24; 3U74; 3U73; 3BT2 TTPRL03 SQ MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTEVVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNGFHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLWT TTPRL03 TT Successful TTHPJTK ID TTHPJTK TTHPJTK TN Varicella-zoster virus DNA polymerase (VZV ORF28) TTHPJTK UP P09252 TTHPJTK UC DPOL_VZVD TTHPJTK BC Kinase TTHPJTK SN VZV DNA polymerase catalytic subunit; ORF28 TTHPJTK GN VZV ORF28 TTHPJTK FC Replicates viral genomic DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA- binding protein. Additionally, the polymerase contains an intrinsic ribonuclease H (RNase H) activity that specifically degrades RNA/DNA heteroduplexes or duplex DNA substrates in the 5' to 3' direction. Therefore, it can catalyze the excision of the RNA primers that initiate the synthesis of Okazaki fragments at a replication fork during viral DNA replication. TTHPJTK SQ MAIRTGFCNPFLTQASGIKYNPRTGRGSNREFLHSYKTTMSSFQFLAPKCLDEDVPMEERKGVHVGTLSRPPKVYCNGKEVPILDFRCSSPWPRRVNIWGEIDFRGDKFDPRFNTFHVYDIVETTEAASNGDVSRFATATRPLGTVITLLGMSRCGKRVAVHVYGICQYFYINKAEVDTACGIRSGSELSVLLAECLRSSMITQNDATLNGDKNAFHGTSFKSASPESFRVEVIERTDVYYYDTQPCAFYRVYSPSSKFTNYLCDNFHPELKKYEGRVDATTRFLMDNPGFVSFGWYQLKPGVDGERVRVRPASRQLTLSDVEIDCMSDNLQAIPNDDSWPDYKLLCFDIECKSGGSNELAFPDATHLEDLVIQISCLLYSIPRQSLEHILLFSLGSCDLPQRYVQEMKDAGLPEPTVLEFDSEFELLIAFMTLVKQYAPEFATGYNIVNFDWAFIMEKLNSIYSLKLDGYGSINRGGLFKIWDVGKSGFQRRSKVKINGLISLDMYAIATEKLKLSSYKLDSVAREALNESKRDLPYKDIPGYYASGPNTRGIIGEYCIQDSALVGKLFFKYLPHLELSAVARLARITLTKAIYDGQQVRIYTCLLGLASSRGFILPDGGYPATFEYKDVIPDVGDVEEEMDEDESVSPTGTSSGRNVGYKGARVFDPDTGFYIDPVVVLDFASLYPSIIQAHNLCFTTLTLNFETVKRLNPSDYATFTVGGKRLFFVRSNVRESLLGVLLKDWLAMRKAIRARIPGSSSDEAVLLDKQQAAIKVVCNSVYGFTGVAQGFLPCLYVAATVTTIGRQMLLSTRDYIHNNWAAFERFITAFPDIESSVLSQKAYEVKVIYGDTDSVFIRFKGVSVEGIAKIGEKMAHIISTALFCPPIKLECEKTFIKLLLITKKKYIGVIYGGKVLMKGVDLVRKNNCQFINDYARKLVELLLYDDTVSRAAAEASCVSIAEWNRRAMPSGMAGFGRIIADAHRQITSPKLDINKFVMTAELSRPPSAYINRRLAHLTVYYKLVMRQGQIPNVRERIPYVIVAPTDEVEADAKSVALLRGDPLQNTAGKRCGEAKRKLIISDLAEDPIHVTSHGLSLNIDYYFSHLIGTASVTFKALFGNDTKLTERLLKRFIPETRVVNVKMLNRLQAAGFVCIHAPCWDNKMNTEAEITEEEQSHQIMRRVFCIPKAILHQS TTHPJTK TT Successful TTW62OQ ID TTW62OQ TTW62OQ TN Virus Major envelope p37 (Viru p37) TTW62OQ UP P33815 TTW62OQ UC F13_VAR67 TTW62OQ BC Phospholipase D phosphodiesterase TTW62OQ SN Viru p37K; Viru Palmitoylated EV membrane protein; Viru Envelope protein F13; C17L, F13L; 37 kDa protein TTW62OQ GN Viru p37 TTW62OQ FC Envelope protein associated with the inner side of the enveloped virion (EV) membrane. TTW62OQ SQ MWPFTSAPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASEKGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYPPLATDLRRRFDTFKAFNSVKNSWLNLYSSACCLPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLRSAKTSIDIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATAESLDALCVQNDLSVKVFTIQNNTKLLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI TTW62OQ TT Successful TTIB7O8 ID TTIB7O8 TTIB7O8 TN Bacterial Integral membrane LmrP (Bact lmrP) TTIB7O8 UP Q9CDQ3 TTIB7O8 UC Q9CDQ3_LACLA TTIB7O8 SN lmrP; L24511; Integral membrane protein LmrP TTIB7O8 GN Bact lmrP TTIB7O8 FC Major facilitator superfamily multidrug transporter from Lactococcus lactis that mediates the efflux of cationic amphiphilic substrates from the cell in a proton-motive force-dependent fashion. TTIB7O8 SQ MKEFWNLDKNLQLRLGIVFLGAFSYGTVFSSMTIYYNQHLGSAITGILLALSAVATFVAGILSGFFADRNGRKPVMVFGTVIQLLGALLAIDSNLPGHVNPWSTFIAFLLISFGYNLVITAGNAMIIDASNAENRKVVFMLDYWAQNLSVILGAALSAWLFRPAFEALLVILLLTVLVSFFLTTFVMTETFRPIVKAKEEAENIFQAYKTVLQDKTYMIFMGANIATTFIIMQFDNFLPVHLSNSFKTITFFGFEIYGQRMLTIYLILACVLVVLLMTTLNRLTKDWSHQKGFIWGSLFMAIGMIFSFLTTTFTPIFIAGIVYTLGEIVYTPSVQTLGVDLMNPEKIGSYNGVAAIKMPIASILAGLLVSISPMIKATGVSLVLALTEVLAIILVLIAVNRHQKTKIN TTIB7O8 TT Successful TTKANGO ID TTKANGO TTKANGO TN Complement C5 (CO5) TTKANGO UP P01031 TTKANGO UC CO5_HUMAN TTKANGO BC Complement system TTKANGO SN C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4 TTKANGO GN C5 TTKANGO FC Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled. Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes (PubMed:8182049). C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation. TTKANGO SQ MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC TTKANGO TT Successful TTKANGO KE hsa04610:Complement and coagulation cascades; hsa05020:Prion diseases; hsa05133:Pertussis; hsa05150:Staphylococcus aureus infection; hsa05168:Herpes simplex infection; hsa05322:Systemic lupus erythematosus TTKANGO RC R-HSA-174577:Activation of C3 and C5; R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events; R-HSA-977606:Regulation of Complement cascade TTB8JQ7 ID TTB8JQ7 TTB8JQ7 TN Electron transport complex III (Complex III) TTB8JQ7 UP P08574-P00156 TTB8JQ7 UC CY1_HUMAN-CYB_HUMAN TTB8JQ7 SN Cytochrome bc1 complex; CoQH2-cytochrome c reductase TTB8JQ7 GN CYC1-MT-CYB TTB8JQ7 FC Produces a transmembrane proton electrochemical gradient as a result of the redox reactions TTB8JQ7 SQ MTPMRKTNPLMKLINHSFIDLPTPSNISAWWNFGSLLGACLILQITTGLFLAMHYSPDASTAFSSIAHITRDVNYGWIIRYLHANGASMFFICLFLHIGRGLYYGSFLYSETWNIGIILLLATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGYSVDSPTLTRFFTFHFILPFIIAALATLHLLFLHETGSNNPLGITSHSDKITFHPYYTIKDALGLLLFLLSLMTLTLFSPDLLGDPDNYTLANPLNTPPHIKPEWYFLFAYTILRSVPNKLGGVLALLLSILILAMIPILHMSKQQSMMFRPLSQSLYWLLAADLLILTWIGGQPVSYPFTIIGQVASVLYFTTILILMPTISLIENKMLKWAMAAAAASLRGVVLGPRGAGLPGARARGLLCSARPGQLPLRTPQAVALSSKSGLSRGRKVMLSALGMLAAGGAGLAMALHSAVSASDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCASCHSMDFVAYRHLVGVCYTEDEAKELAAEVEVQDGPNEDGEMFMRPGKLFDYFPKPYPNSEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIAMAPPIYTDVLEFDDGTPATMSQIAKDVCTFLRWASEPEHDHRKRMGLKMLMMMALLVPLVYTIKRHKWSVLKSRKLAYRPPK TTB8JQ7 TT Successful TT1JL7D ID TT1JL7D TT1JL7D TN Epstein-Barr virus Envelope glycoprotein gp340 (EBV BLLF1) TT1JL7D UP P68344 TT1JL7D UC VGP3_EBVP3 TT1JL7D SN Membrane antigen; MA; Envelope glycoprotein GP340 TT1JL7D GN EBV BLLF1 TT1JL7D FC Responsible for EBV binding to the CR2 receptor on human B-cells. TT1JL7D SQ MEAALLVCQYTIQSLIQLTRDDPGFFNVEILEFPFYPACNVCTADVNATINFDVGGKKHKLNLDFGLLTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINITTGEEQQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPYIKWDNCNSTNITAVVRAQGLDVTLPLSLPTSAQDSNFSVKTEMLGNEIDIECIMEDGEISQVLPGDNKFNITCSGYESHVPSGGILTSTSPVATPIPGTGYAYSLRLTPRPVSRFLGNNSILYVFYSGNGPKASGGDYCIQSNIVFSDEIPASQDMPTNTTDITYVGDNATYSVPMVTSEDANSPNVTVTAFWAWPNNTETDFKCKWTLTSGTPSGCENISGAFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFSNLSMLVLQWASLAVLTLLLLLVMADCAFRRNLSTSHTYTTPPYDDAETYV TT1JL7D TT Successful TTWODQF ID TTWODQF TTWODQF TN Fibrin (FG) TTWODQF UP P02671 (20-35); P02675 (31-44) TTWODQF UC FIBA_HUMAN; FIBB_HUMAN TTWODQF SN Fibrinogen (31-44) TTWODQF GN FGA; FGB TTWODQF FC A fibrous, non-globular protein involved in the clotting of blood. Formed by the action of the protease thrombin on fibrinogen which causes it to polymerize. TTWODQF SQ MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQ TTWODQF TT Successful TT1EDJZ ID TT1EDJZ TT1EDJZ TN Microtubule-associated protein (MAP) TT1EDJZ UP P78559; P46821 TT1EDJZ UC MAP1A_HUMAN; MAP1B_HUMAN TT1EDJZ SN Microtubule-associated protein 1; MAP-1 TT1EDJZ GN MAP1A; MAP1B TT1EDJZ FC Binds to the tubulin subunits that make up microtubules to regulate their stability. Invovled in stabilizing and destabilizing microtubules, guiding microtubules towards specific cellular locations, cross-linking microtubules and mediating the interactions of microtubules with other proteins in the cell. TT1EDJZ SQ MDGVAEFSEYVSETVDVPSPFDLLEPPTSGGFLKLSKPCCYIFPGGRGDSALFAVNGFNILVDGGSDRKSCFWKLVRHLDRIDSVLLTHIGADNLPGINGLLQRKVAELEEEQSQGSSSYSDWVKNLISPELGVVFFNVPEKLRLPDASRKAKRSIEEACLTLQHLNRLGIQAEPLYRVVSNTIEPLTLFHKMGVGRLDMYVLNPVKDSKEMQFLMQKWAGNSKAKTGIVLPNGKEAEISVPYLTSITALVVWLPANPTEKIVRVLFPGNAPQNKILEGLEKLRHLDFLRYPVATQKDLASGAVPTNLKPSKIKQRADSKESLKATTKTAVSKLAKREEVVEEGAKEARSELAKELAKTEKKAKESSEKPPEKPAKPERVKTESSEALKAEKRKLIKDKVGKKHLKEKISKLEEKKDKEKKEIKKERKELKKDEGRKEEKKDAKKEEKRKDTKPELKKISKPDLKPFTPEVRKTLYKAKVPGRVKIDRSRAIRGEKELSSEPQTPPAQKGTVPLPTISGHRELVLSSPEDLTQDFEEMKREERALLAEQRDTGLGDKPFPLDTAEEGPPSTAIQGTPPSVPGLGQEEHVMKEKELVPEVPEEQGSKDRGLDSGAETEEEKDTWEEKKQREAERLPDRTEAREESEPEVKEDVIEKAELEEMEEVHPSDEEEEDATKAEGFYQKHMQEPLKVTPRSREAFGGRELGLQGKAPEKETSLFLSSLTTPAGATEHVSYIQDETIPGYSETEQTISDEEIHDEPEERPAPPRFHTSTYDLPGPEGAGPFEASQPADSAVPATSGKVYGTPETELTYPTNIVAAPLAEEEHVSSATSITECDKLSSFATSVAEDQSVASLTAPQTEETGKSSLLLDTVTSIPSSRTEATQGLDYVPSAGTISPTSSLEEDKGFKSPPCEDFSVTGESEKRGEIIGKGLSGERAVEEEEEETANVEMSEKLCSQYGTPVFSAPGHALHPGEPALGEAEERCLSPDDSTVKMASPPPSGPPSATHTPFHQSPVEEKSEPQDFQEADSWGDTKRTPGVGKEDAAEETVKPGPEEGTLEKEEKVPPPRSPQAQEAPVNIDEGLTGCTIQLLPAQDKAIVFEIMEAGEPTGPILGAEALPGGLRTLPQEPGKPQKDEVLRYPDRSLSPEDAESLSVLSVPSPDTANQEPTPKSPCGLTEQYLHKDRWPEVSPEDTQSLSLSEESPSKETSLDVSSKQLSPESLGTLQFGELNLGKEEMGHLMQAEDTSHHTAPMSVPEPHAATASPPTDGTTRYSAQTDITDDSLDRKSPASSFSHSTPSGNGKYLPGAITSPDEHILTPDSSFSKSPESLPGPALEDIAIKWEDKVPGLKDRTSEQKKEPEPKDEVLQQKDKTLEHKEVVEPKDTAIYQKDEALHVKNEAVKQQDKALEQKGRDLEQKDTALEQKDKALEPKDKDLEEKDKALEQKDKIPEEKDKALEQKDTALEQKDKALEPKDKDLEQKDRVLEQKEKIPEEKDKALDQKVRSVEHKAPEDTVAEMKDRDLEQTDKAPEQKHQAQEQKDKVSEKKDQALEQKYWALGQKDEALEQNIQALEENHQTQEQESLVQEDKTRKPKMLEEKSPEKVKAMEEKLEALLEKTKALGLEESLVQEGRAREQEEKYWRGQDVVQEWQETSPTREEPAGEQKELAPAWEDTSPEQDNRYWRGREDVALEQDTYWRELSCERKVWFPHELDGQGARPHYTEERESTFLDEGPDDEQEVPLREHATRSPWASDFKDFQESSPQKGLEVERWLAESPVGLPPEEEDKLTRSPFEIISPPASPPEMVGQRVPSAPGQESPIPDPKLMPHMKNEPTTPSWLADIPPWVPKDRPLPPAPLSPAPGPPTPAPESHTPAPFSWGTAEYDSVVAAVQEGAAELEGGPYSPLGKDYRKAEGEREEEGRAEAPDKSSHSSKVPEASKSHATTEPEQTEPEQREPTPYPDERSFQYADIYEQMMLTGLGPACPTREPPLGAAGDWPPCLSTKEAAAGRNTSAEKELSSPISPKSLQSDTPTFSYAALAGPTVPPRPEPGPSMEPSLTPPAVPPRAPILSKGPSPPLNGNILSCSPDRRSPSPKESGRSHWDDSTSDSELEKGAREQPEKEAQSPSPPHPIPMGSPTLWPETEAHVSPPLDSHLGPARPSLDFPASAFGFSSLQPAPPQLPSPAEPRSAPCGSLAFSGDRALALAPGPPTRTRHDEYLEVTKAPSLDSSLPQLPSPSSPGAPLLSNLPRPASPALSEGSSSEATTPVISSVAERFSPSLEAAEQESGELDPGMEPAAHSLWDLTPLSPAPPASLDLALAPAPSLPGDMGDGILPCHLECSEAATEKPSPFQVPSEDCAANGPTETSPNPPGPAPAKAENEEAAACPAWERGAWPEGAERSSRPDTLLSPEQPVCPAGGSGGPPSSASPEVEAGPQGCATEPRPHRGELSPSFLNPPLPPSIDDRDLSTEEVRLVGRGGRRRVGGPGTTGGPCPVTDETPPTSASDSGSSQSDSDVPPETEECPSITAEAALDSDEDGDFLPVDKAGGVSGTHHPRPGHDPPPLPQPDPRPSPPRPDVCMADPEGLSSESGRVERLREKEKVQGRVGRRAPGKAKPASPARRLDLRGKRSPTPGKGPADRASRAPPRPRSTTSQVTPAEEKDGHSPMSKGLVNGLKAGPMALSSKGSSGAPVYVDLAYIPNHCSGKTADLDFFRRVRASYYVVSGNDPANGEPSRAVLDALLEGKAQWGENLQVTLIPTHDTEVTREWYQQTHEQQQQLNVLVLASSSTVVMQDESFPACKIEF TT1EDJZ TT Successful TT19K0L ID TT19K0L TT19K0L TN Mycobacterium Proton pump (MycB Prop) TT19K0L UP A0A1Q4HQH4 TT19K0L UC A0A1Q4HQH4_9MYCO TT19K0L SN Nicotinamide nucleotide transhydrogenase subunit beta; NAD(P) transhydrogenase subunit beta TT19K0L GN MycB Prop TT19K0L FC The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. TT19K0L SQ MNYLVTVLYIISFALFIYGLMGLTGPKTAVRGNLIAAVGMAIAVAATLIKIRHTESWVLIIAGLVVGVALGVPPARYTKMTAMPQLVAFFNGVGGGTVALIALSEFIETKGFSAFQHGESPTVHIVVASLFAAIIGSISFWGSIIAFGKLQEIISGSPIGFGKAQQPINLLLLAAAVAAAVVIGLGAHPGTGGVALWWMIGLLAAAGVLGLMVVLPIGGADMPVVISLLNAMTGLSAAAAGLALNNTAMIVAGMIVGASGSILTNLMAKAMNRSIPAIVAGGFGGGGVAPSGGGGGDKHVKATSAADAAIQMAYANQVIVVPGYGLAVAQAQHAVKDMASLLEDKGVPVKYAIHPVAGRMPGHMNVLLAEAEVDYDAMKDMDDINDEFARTDVAIVIGANDVTNPAARNEQSSPIYGMPILNVDRAKSVIVLKRSMNSGFAGIDNPLFYADGTTMLFGDAKKSVTEVAEELKAL TT19K0L TT Successful TTACFNR ID TTACFNR TTACFNR TN Organic anion transporter M1 (SLCO4C1) TTACFNR UP Q6ZQN7 TTACFNR UC SO4C1_HUMAN TTACFNR SN Solute carrier organic anion transporter family member 4C1; Solute carrier family 21 member 20; OATPX; OATP4C1; OATP-M1; OATP-H TTACFNR GN SLCO4C1 TTACFNR FC Organic anion transporter, capable of transporting pharmacological substances such as digoxin, ouabain, thyroxine, methotrexate and cAMP. May participate in the regulation of membrane transport of ouabain. Involved in the uptake of the dipeptidyl peptidase-4 inhibitor sitagliptin and hence may play a role in its transport into and out of renal proximal tubule cells. May be involved in the first step of the transport pathway of digoxin and various compounds into the urine in the kidney. May be involved in sperm maturation by enabling directed movement of organic anions and compounds within or between cells. This ion-transporting process is important to maintain the strict epididymal homeostasis necessary for sperm maturation. May have a role in secretory functions since seminal vesicle epithelial cells are assumed to secrete proteins involved in decapacitation by modifying surface proteins to facilitate the acquisition of the ability to fertilize the egg. TTACFNR SQ MKSAKGIENLAFVPSSPDILRRLSASPSQIEVSALSSDPQRENSQPQELQKPQEPQKSPEPSLPSAPPNVSEEKLRSLSLSEFEEGSYGWRNFHPQCLQRCNTPGGFLLHYCLLAVTQGIVVNGLVNISISTVEKRYEMKSSLTGLISSSYDISFCLLSLFVSFFGERGHKPRWLAFAAFMIGLGALVFSLPQFFSGEYKLGSLFEDTCVTTRNSTSCTSSTSSLSNYLYVFILGQLLLGAGGTPLYTLGTAFLDDSVPTHKSSLYIGTGYAMSILGPAIGYVLGGQLLTIYIDVAMGESTDVTEDDPRWLGAWWIGFLLSWIFAWSLIIPFSCFPKHLPGTAEIQAGKTSQAHQSNSNADVKFGKSIKDFPAALKNLMKNAVFMCLVLSTSSEALITTGFATFLPKFIENQFGLTSSFAATLGGAVLIPGAALGQILGGFLVSKFRMTCKNTMKFALFTSGVALTLSFVFMYAKCENEPFAGVSESYNGTGELGNLIAPCNANCNCSRSYYYPVCGDGVQYFSPCFAGCSNPVAHRKPKVYYNCSCIERKTEITSTAETFGFEAKAGKCETHCAKLPIFLCIFFIVIIFTFMAGTPITVSILRCVNHRQRSLALGIQFMVLRLLGTIPGPIIFGFTIDSTCILWDINDCGIKGACWIYDNIKMAHMLVAISVTCKVITMFFNGFAIFLYKPPPSATDVSFHKENAVVTNVLAEQDLNKIVKEG TTACFNR TT Successful TT9JZPU ID TT9JZPU TT9JZPU TN Pediculus humanus Nicotinic acetylcholine receptor (Pedhc nAChR) TT9JZPU UP E0VDF4 TT9JZPU UC E0VDF4_PEDHC TT9JZPU SN Acetylcholine receptor protein alpha 1, 2, 3, 4invertebrate, putative; Acetylcholine receptor protein alpha 1, 2, 3, 4 invertebrate, putative TT9JZPU GN Pedhc nAChR TT9JZPU FC Mediates the fast actions ofacetylcholine (ACh) in the nervous system and at neuromuscular junctions. TT9JZPU SQ MCLCLCLTPFLDIPGFKPVQMEANPDAKRLYDDLLSNYNRLIRPVVNNTETLTVRLGLKLSQLIEVNLKSQVMTTNVWVEQKWTDYKLRWNPEEYGGVEMLYVPSEHIWLPDIVLYNNADGNYEVTLMTKATLNYNGEVYWKPPAIYKSSCEINVLYFPFDEQSCYMKFGSWTYHGYQVDLKHMDQKPGTNLVPVGVDLKEFYLSVEWDILEVPARKNEEYYPCCAEPYSDITFNLKMRRKTLFYTVNLIIPCVGITFLTVLVFYLPSDSGEKVTLTVSILLSLTVFFLLLAEIIPPTSLAVPLLGKYLLFTMMLVTLSIFITVCVLNIYFRSPSTHKMSPWVRNVFLNFIPRLLMMRRPPYSVRRDGYDDSGDNGYASALDYRDGIGEPFPPELKGSPEFESVTTVCKSTFGTESDDNLGTTFRHAQPSDSENIIPRNLSSDVLSALQGVCFIAQHIRNADKDNEVIEDWKYVSMVLDRFFLWVFTLACIGGTCAIIFQAPSLYDQRIPIDQEISLIQFGKIFLNIPREQNSD TT9JZPU TT Successful TTY8Z2E ID TTY8Z2E TTY8Z2E TN Proton-coupled folate transporter (SLC46A1) TTY8Z2E UP Q96NT5 TTY8Z2E UC PCFT_HUMAN TTY8Z2E SN Solute carrier family 46 member 1; PCFT/HCP1; PCFT; Heme carrier protein 1; HCP1; G21 TTY8Z2E GN SLC46A1 TTY8Z2E FC Has been shown to act both as an intestinal proton-coupled high-affinity folate transporter and as an intestinal heme transporter which mediates heme uptake from the gut lumen into duodenal epithelial cells. The iron is then released from heme and may be transported into the bloodstream. Dietary heme iron is an important nutritional source of iron. Shows a higher affinity for folate than heme. TTY8Z2E SQ MEGSASPPEKPRARPAAAVLCRGPVEPLVFLANFALVLQGPLTTQYLWHRFSADLGYNGTRQRGGCSNRSADPTMQEVETLTSHWTLYMNVGGFLVGLFSSTLLGAWSDSVGRRPLLVLASLGLLLQALVSVFVVQLQLHVGYFVLGRILCALLGDFGGLLAASFASVADVSSSRSRTFRMALLEASIGVAGMLASLLGGHWLRAQGYANPFWLALALLIAMTLYAAFCFGETLKEPKSTRLFTFRHHRSIVQLYVAPAPEKSRKHLALYSLAIFVVITVHFGAQDILTLYELSTPLCWDSKLIGYGSAAQHLPYLTSLLALKLLQYCLADAWVAEIGLAFNILGMVVFAFATITPLMFTGYGLLFLSLVITPVIRAKLSKLVRETEQGALFSAVACVNSLAMLTASGIFNSLYPATLNFMKGFPFLLGAGLLLIPAVLIGMLEKADPHLEFQQFPQSP TTY8Z2E TT Successful TTZN7RP ID TTZN7RP TTZN7RP TN Rho-associated protein kinase 1 (ROCK1) TTZN7RP UP Q13464 TTZN7RP UC ROCK1_HUMAN TTZN7RP BC Kinase TTZN7RP SN Rok; Rho-associated, coiled-coil containing protein kinase 1; Rho-associated kinase 1; Rho kinase; ROCK1; ROCK; P160ROCK; P160(rock); P160 ROCK-1; Let-502 kinase TTZN7RP GN ROCK1 TTZN7RP FC Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. TTZN7RP SQ MSTGDSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSNRRYLSSANPNDNRTSSNADKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKMKKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLDLSDSTSVASFPSADETDGNLPESRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDVEMEPVQQAEKTNFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIPKNPPSGFVRASPRTLSTRSTANQSFRKVVKNTSGKTS TTZN7RP TT Successful TTZN7RP KE hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04350:TGF-beta signaling pathway; hsa04360:Axon guidance; hsa04510:Focal adhesion; hsa04611:Platelet activation; hsa04670:Leukocyte transendothelial migration; hsa04810:Regulation of actin cytoskeleton; hsa04921:Oxytocin signaling pathway; hsa05130:Pathogenic Escherichia coli infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer TTZN7RP RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-416482:G alpha (12/13) signalling events; R-HSA-416572:Sema4D induced cell migration and growth-cone collapse; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5627117:RHO GTPases Activate ROCKs TT61XTV ID TT61XTV TT61XTV TN Sodium-dependent multivitamin transporter (SLC5A6) TT61XTV UP Q9Y289 TT61XTV UC SC5A6_HUMAN TT61XTV SN Solute carrier family 5 member 6; SMVT; Na(+)-dependent multivitamin transporter TT61XTV GN SLC5A6 TT61XTV FC Transports pantothenate, biotin and lipoate in the presence of sodium. TT61XTV SQ MSVGVSTSAPLSPTSGTSVGMSTFSIMDYVVFVLLLVLSLAIGLYHACRGWGRHTVGELLMADRKMGCLPVALSLLATFQSAVAILGVPSEIYRFGTQYWFLGCCYFLGLLIPAHIFIPVFYRLHLTSAYEYLELRFNKTVRVCGTVTFIFQMVIYMGVVLYAPSLALNAVTGFDLWLSVLALGIVCTVYTALGGLKAVIWTDVFQTLVMFLGQLAVIIVGSAKVGGLGRVWAVASQHGRISGFELDPDPFVRHTFWTLAFGGVFMMLSLYGVNQAQVQRYLSSRTEKAAVLSCYAVFPFQQVSLCVGCLIGLVMFAYYQEYPMSIQQAQAAPDQFVLYFVMDLLKGLPGLPGLFIACLFSGSLSTISSAFNSLATVTMEDLIRPWFPEFSEARAIMLSRGLAFGYGLLCLGMAYISSQMGPVLQAAISIFGMVGGPLLGLFCLGMFFPCANPPGAVVGLLAGLVMAFWIGIGSIVTSMGSSMPPSPSNGSSFSLPTNLTVATVTTLMPLTTFSKPTGLQRFYSLSYLWYSAHNSTTVIVVGLIVSLLTGRMRGRSLNPATIYPVLPKLLSLLPLSCQKRLHCRSYGQDHLDTGLFPEKPRNGVLGDSRDKEAMALDGTAYQGSSSTCILQETSL TT61XTV TT Successful TT6XAGK ID TT6XAGK TT6XAGK TN Solute carrier family 23 member 1 (SLC23A1) TT6XAGK UP Q9UHI7 TT6XAGK UC S23A1_HUMAN TT6XAGK SN hSVCT1; Yolk sac permease-like molecule 3; YSPL3; Sodium-dependent vitamin C transporter 1; SVCT1; Na(+)/L-ascorbic acid transporter 1 TT6XAGK GN SLC23A1 TT6XAGK FC Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate. TT6XAGK SQ MRAQEDLEGRTQHETTRDPSTPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTIAVPFLLAEALCVGHDQHMVSQLIGTIFTCVGITTLIQTTVGIRLPLFQASAFAFLVPAKAILALERWKCPPEEEIYGNWSLPLNTSHIWHPRIREVQGAIMVSSVVEVVIGLLGLPGALLNYIGPLTVTPTVSLIGLSVFQAAGDRAGSHWGISACSILLIILFSQYLRNLTFLLPVYRWGKGLTLLRIQIFKMFPIMLAIMTVWLLCYVLTLTDVLPTDPKAYGFQARTDARGDIMAIAPWIRIPYPCQWGLPTVTAAAVLGMFSATLAGIIESIGDYYACARLAGAPPPPVHAINRGIFTEGICCIIAGLLGTGNGSTSSSPNIGVLGITKVGSRRVVQYGAAIMLVLGTIGKFTALFSSLPDPILGGMFCTLFGMITAVGLSNLQFVDMNSSRNLFVLGFSMFFGLTLPNYLESNPGAINTGILEVDQILIVLLTTEMFVGGCLAFILDNTVPGSPEERGLIQWKAGAHANSDMSSSLKSYDFPIGMGIVKRITFLKYIPICPVFKGFSSSSKDQIAIPEDTPENTETASVCTKV TT6XAGK TT Successful TTMHCGA ID TTMHCGA TTMHCGA TN Solute carrier family 47 member 1 (SLC47A1) TTMHCGA UP Q96FL8 TTMHCGA UC S47A1_HUMAN TTMHCGA SN hMATE-1; Multidrug and toxin extrusion protein 1; MATE1; MATE-1 TTMHCGA GN SLC47A1 TTMHCGA FC Solute transporter for tetraethylammonium (TEA), 1-methyl-4-phenylpyridinium (MPP), cimetidine, N-methylnicotinamide (NMN), metformin, creatinine, guanidine, procainamide, topotecan, estrone sulfate, acyclovir, ganciclovir and also the zwitterionic cephalosporin, cephalexin and cephradin. Seems to also play a role in the uptake of oxaliplatin (a new platinum anticancer agent). Able to transport paraquat (PQ or N,N-dimethyl-4-4'-bipiridinium); a widely used herbicid. Responsible for the secretion of cationic drugs across the brush border membranes. TTMHCGA SQ MEAPEEPAPVRGGPEATLEVRGSRCLRLSAFREELRALLVLAGPAFLVQLMVFLISFISSVFCGHLGKLELDAVTLAIAVINVTGVSVGFGLSSACDTLISQTYGSQNLKHVGVILQRSALVLLLCCFPCWALFLNTQHILLLFRQDPDVSRLTQTYVTIFIPALPATFLYMLQVKYLLNQGIVLPQIVTGVAANLVNALANYLFLHQLHLGVIGSALANLISQYTLALLLFLYILGKKLHQATWGGWSLECLQDWASFLRLAIPSMLMLCMEWWAYEVGSFLSGILGMVELGAQSIVYELAIIVYMVPAGFSVAASVRVGNALGAGDMEQARKSSTVSLLITVLFAVAFSVLLLSCKDHVGYIFTTDRDIINLVAQVVPIYAVSHLFEALACTSGGVLRGSGNQKVGAIVNTIGYYVVGLPIGIALMFATTLGVMGLWSGIIICTVFQAVCFLGFIIQLNWKKACQQAQVHANLKVNNVPRSGNSALPQDPLHPGCPENLEGILTNDVGKTGEPQSDQQMRQEEPLPEHPQDGAKLSRKQLVLRRGLLLLGVFLILLVGILVRFYVRIQ TTMHCGA TT Successful TTLOQ79 ID TTLOQ79 TTLOQ79 TN Taste receptor (TASR) TTLOQ79 UP Q7RTX1; Q8TE23; Q7RTX0 TTLOQ79 UC TS1R1_HUMAN; TS1R2_HUMAN; TS1R3_HUMAN TTLOQ79 SN TR; Sweet taste receptor; G-protein coupled receptor TTLOQ79 GN TAS1R1; TAS1R2; TAS1R3 TTLOQ79 FC Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate). TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. TAS1R3 is essential for the recognition and response to the disaccharide trehalose (By similarity). Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses. TTLOQ79 SQ MLLCTARLVGLQLLISCCWAFACHSTESSPDFTLPGDYLLAGLFPLHSGCLQVRHRPEVTLCDRSCSFNEHGYHLFQAMRLGVEEINNSTALLPNITLGYQLYDVCSDSANVYATLRVLSLPGQHHIELQGDLLHYSPTVLAVIGPDSTNRAATTAALLSPFLVPMISYAASSETLSVKRQYPSFLRTIPNDKYQVETMVLLLQKFGWTWISLVGSSDDYGQLGVQALENQATGQGICIAFKDIMPFSAQVGDERMQCLMRHLAQAGATVVVVFSSRQLARVFFESVVLTNLTGKVWVASEAWALSRHITGVPGIQRIGMVLGVAIQKRAVPGLKAFEEAYARADKKAPRPCHKGSWCSSNQLCRECQAFMAHTMPKLKAFSMSSAYNAYRAVYAVAHGLHQLLGCASGACSRGRVYPWQLLEQIHKVHFLLHKDTVAFNDNRDPLSSYNIIAWDWNGPKWTFTVLGSSTWSPVQLNINETKIQWHGKDNQVPKSVCSSDCLEGHQRVVTGFHHCCFECVPCGAGTFLNKSDLYRCQPCGKEEWAPEGSQTCFPRTVVFLALREHTSWVLLAANTLLLLLLLGTAGLFAWHLDTPVVRSAGGRLCFLMLGSLAAGSGSLYGFFGEPTRPACLLRQALFALGFTIFLSCLTVRSFQLIIIFKFSTKVPTFYHAWVQNHGAGLFVMISSAAQLLICLTWLVVWTPLPAREYQRFPHLVMLECTETNSLGFILAFLYNGLLSISAFACSYLGKDLPENYNEAKCVTFSLLFNFVSWIAFFTTASVYDGKYLPAANMMAGLSSLSSGFGGYFLPKCYVILCRPDLNSTEHFQASIQDYTRRCGST TTLOQ79 TT Successful TTG7UOF ID TTG7UOF TTG7UOF TN Variola virus Envelope phospholipase F13 (VARV p37) TTG7UOF UP P33815 TTG7UOF UC F13_VAR67 TTG7UOF SN Variola 37 kDa protein; VARV p37K; VARV Palmitoylated EV membrane protein; VARV Envelope protein F13 TTG7UOF GN VARV p37 TTG7UOF FC Envelope protein associated with the inner side of the enveloped virion (EV) membrane. TTG7UOF SQ MWPFTSAPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASEKGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYPPLATDLRRRFDTFKAFNSVKNSWLNLYSSACCLPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLRSAKTSIDIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATAESLDALCVQNDLSVKVFTIQNNTKLLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI TTG7UOF TT Successful TTG25NJ ID TTG25NJ TTG25NJ TN Vesicle-associated membrane protein (VAMP) TTG25NJ UP P23763; P63027 TTG25NJ UC VAMP1_HUMAN; VAMP2_HUMAN TTG25NJ SN VAMP; Synaptobrevin; SYB TTG25NJ GN VAMP1; VAMP2 TTG25NJ FC Involved in the targeting and/or fusion of transport vesicles to their target membrane. TTG25NJ SQ MSAPAQPPAEGTEGTAPGGGPPGPPPNMTSNRRLQQTQAQVEEVVDIIRVNVDKVLERDQKLSELDDRADALQAGASQFESSAAKLKRKYWWKNCKMMIMLGAICAIIVVVIVIYFFT TTG25NJ TT Successful TT38DW5 ID TT38DW5 TT38DW5 TN Bacterial 16S ribosomal RNA (Bact 16S rRNA) TT38DW5 UP microRNA/lncRNA TT38DW5 UC NOUNIPROTAC TT38DW5 SN RrnS; Plastid 16S rRNA; 16S rRNA TT38DW5 GN NO-GeName TT38DW5 TT Successful TTLFGBV ID TTLFGBV TTLFGBV TN Bacterial 23S ribosomal RNA (Bact 23S rRNA) TTLFGBV UP microRNA/lncRNA TTLFGBV UC NOUNIPROTAC TTLFGBV SN RrnL; Plastid 23S rRNA TTLFGBV GN NO-GeName TTLFGBV TT Successful TTUWYEA ID TTUWYEA TTUWYEA TN Bacterial 50S ribosomal RNA (Bact 50S rRNA) TTUWYEA UP microRNA/lncRNA TTUWYEA UC NOUNIPROTAC TTUWYEA GN NO-GeName TTUWYEA FC Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. TTUWYEA TT Successful TTOVFH2 ID TTOVFH2 TTOVFH2 TN Bacterial 30S ribosomal RNA (Bact 30S rRNA) TTOVFH2 UP microRNA/lncRNA TTOVFH2 UC NOUNIPROTAC TTOVFH2 GN NO-GeName TTOVFH2 TT Successful TTIA0J5 ID TTIA0J5 TTIA0J5 TN Bacterial 70S ribosomal RNA (Bact 70S rRNA) TTIA0J5 UP microRNA/lncRNA TTIA0J5 UC NOUNIPROTAC TTIA0J5 GN NO-GeName TTIA0J5 TT Successful TTS1W4A ID TTS1W4A TTS1W4A TN Bacterial Deoxyribonucleic acid (Bact DNA) TTS1W4A UP Other molecule TTS1W4A UC NOUNIPROTAC TTS1W4A GN NO-GeName TTS1W4A TT Successful TT8X5NO ID TT8X5NO TT8X5NO TN Calcium (Ca) TT8X5NO UP Other molecule TT8X5NO UC NOUNIPROTAC TT8X5NO GN NO-GeName TT8X5NO TT Successful TTFDXCO ID TTFDXCO TTFDXCO TN Dabigatran (Dabi) TTFDXCO UP Other molecule TTFDXCO UC NOUNIPROTAC TTFDXCO GN NOUNIPROTAC TTFDXCO TT Successful TTQKWA4 ID TTQKWA4 TTQKWA4 TN Fungal Cell membrane ergosterol (Fung CME) TTQKWA4 UP Other molecule TTQKWA4 UC NOUNIPROTAC TTQKWA4 GN NO-GeName TTQKWA4 TT Successful TTUTN1I ID TTUTN1I TTUTN1I TN Human Deoxyribonucleic acid (hDNA) TTUTN1I UP Other molecule TTUTN1I UC NOUNIPROTAC TTUTN1I GN NO-GeName TTUTN1I TT Successful TTY1GPO ID TTY1GPO TTY1GPO TN Human Deoxyribonucleic acid major groove (hDNA maj) TTY1GPO UP Other molecule TTY1GPO UC NOUNIPROTAC TTY1GPO GN NO-GeName TTY1GPO TT Successful TTYTVXF ID TTYTVXF TTYTVXF TN Hyaluronic acid (HA) TTYTVXF UP Other molecule TTYTVXF UC NOUNIPROTAC TTYTVXF GN NO-GeName TTYTVXF TT Successful TTUDR0C ID TTUDR0C TTUDR0C TN Iron (Fe) TTUDR0C UP Other molecule TTUDR0C UC NOUNIPROTAC TTUDR0C GN NO-GeName TTUDR0C TT Successful TTHOTF6 ID TTHOTF6 TTHOTF6 TN Phosphate (PHO) TTHOTF6 UP Other molecule TTHOTF6 UC NOUNIPROTAC TTHOTF6 GN NO-GeName TTHOTF6 TT Successful TTT28H3 ID TTT28H3 TTT28H3 TN Plasmodium 80S ribosome (Malaria 80S) TTT28H3 UP Other molecule TTT28H3 UC NOUNIPROTAC TTT28H3 GN NO-GeName TTT28H3 TT Successful TT698WO ID TT698WO TT698WO TN Plasmodium Deoxyribonucleic acid (Malaria DNA) TT698WO UP Other molecule TT698WO UC NOUNIPROTAC TT698WO GN NO-GeName TT698WO TT Successful TTB0SC6 ID TTB0SC6 TTB0SC6 TN Potassium (K) TTB0SC6 UP Other molecule TTB0SC6 UC NOUNIPROTAC TTB0SC6 GN NO-GeName TTB0SC6 TT Successful TTULV0X ID TTULV0X TTULV0X TN Reactive oxygen species (ROS) TTULV0X UP Other molecule TTULV0X UC NOUNIPROTAC TTULV0X GN NO-GeName TTULV0X TT Successful TTGXKP7 ID TTGXKP7 TTGXKP7 TN Samarium (SAM) TTGXKP7 UP Other molecule TTGXKP7 UC NOUNIPROTAC TTGXKP7 GN NO-GeName TTGXKP7 TT Successful TTB1TZG ID TTB1TZG TTB1TZG TN Schistosoma Deoxyribonucleic acid (Schist DNA) TTB1TZG UP Other molecule TTB1TZG UC NOUNIPROTAC TTB1TZG GN NO-GeName TTB1TZG TT Successful TTX81QL ID TTX81QL TTX81QL TN Toxic methotrexate (TM) TTX81QL UP Other molecule TTX81QL UC NOUNIPROTAC TTX81QL GN NO-GeName TTX81QL TT Successful TT0C9DV ID TT0C9DV TT0C9DV TN Toxic reactive metabolite (TRM) TT0C9DV UP Other molecule TT0C9DV UC NOUNIPROTAC TT0C9DV GN NO-GeName TT0C9DV TT Successful TTZ1SWF ID TTZ1SWF TTZ1SWF TN Uric acid (URA) TTZ1SWF UP Other molecule TTZ1SWF UC NOUNIPROTAC TTZ1SWF GN NO-GeName TTZ1SWF TT Successful TT4823K ID TT4823K TT4823K TN Virus Deoxyribonucleic acid (Viru DNA) TT4823K UP Other molecule TT4823K UC NOUNIPROTAC TT4823K GN NO-GeName TT4823K TT Successful TT5ZKDI ID TT5ZKDI TT5ZKDI TN Histone deacetylase 6 (HDAC6) TT5ZKDI UP Q9UBN7 TT5ZKDI UC HDAC6_HUMAN TT5ZKDI BC Carbon-nitrogen hydrolase TT5ZKDI SN KIAA0901; JM21; HD6 TT5ZKDI GN HDAC6 TT5ZKDI FC Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). TT5ZKDI EC EC 3.5.1.98 TT5ZKDI PD 6CEF; 6CEE; 6CED; 6CEC; 6CEA TT5ZKDI SQ MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH TT5ZKDI TT Clinical trial TT5ZKDI FM Carbon nitrogen hydrolase TT5ZKDI KE hsa05034:Alcoholism; hsa05203:Viral carcinogenesis TT5ZKDI RC R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-5617833:Assembly of the primary cilium TTAIY2U ID TTAIY2U TTAIY2U TN HUMAN clathrin-mediated endocytosis (RME) TTAIY2U UP Pathway/Process TTZGK1R ID TTZGK1R TTZGK1R TN HUMAN glycosylation of host receptor (GHR) TTZGK1R UP Pathway/Process TTD16BI ID TTD16BI TTD16BI TN HUMAN pH-dependent viral fusion/replication (pH-DVF/R) TTD16BI UP Pathway/Process TT3A1EZ ID TT3A1EZ TT3A1EZ TN HUMAN toll-like receptor 7/9 signalling pathway (TLR7/9 pathway) TT3A1EZ UP Pathway/Process TTXV4FI ID TTXV4FI TTXV4FI TN Albendazole monooxygenase (CYP3A4) TTXV4FI UP P08684 TTXV4FI UC CP3A4_HUMAN TTXV4FI BC Paired donor oxygen oxidoreductase TTXV4FI SN Taurochenodeoxycholate 6-alpha-hydroxylase; Quinine 3-monooxygenase; P450-PCN1; Nifedipine oxidase; NF-25; HLp; Cytochrome P450-PCN1; Cytochrome P450 NF-25; Cytochrome P450 HLp; Cytochrome P450 3A4; Cytochrome P450 3A3; CYPIIIA4; CYPIIIA3; CYP3A3; Albendazole sulfoxidase; Albendazole monooxygenase (sulfoxide-forming); 1,8-cineole 2-exo-monooxygenase TTXV4FI GN CYP3A4 TTXV4FI FC In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e. g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4-hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,8-cineole 2-exo-monooxygenase. The enzyme also hydroxylates etoposide. Catalyzes 4-beta-hydroxylation of cholesterol. May catalyze 25-hydroxylation of cholesterol in vitro. Catalyzes sulfoxidation of the anthelmintics albendazole and fenbendazole. Cytochromes P450 are a group of heme-thiolate monooxygenases. TTXV4FI EC EC 1.14.14.- TTXV4FI PD 6BDM; 6BDK; 6BDI; 6BDH; 6BD8 TTXV4FI SQ MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVSGA TTXV4FI TT Clinical trial TTXV4FI FM Paired donor oxidoreductase TTXV4FI KE hsa00140:Steroid hormone biosynthesis; hsa00591:Linoleic acid metabolism; hsa00830:Retinol metabolism; hsa00980:Metabolism of xenobiotics by cytochrome P450; hsa00982:Drug metabolism - cytochrome P450; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways; hsa04976:Bile secretion; hsa05204:Chemical carcinogenesis TTXV4FI RC R-HSA-211981:Xenobiotics; R-HSA-5423646:Aflatoxin activation and detoxification TT2LVK8 ID TT2LVK8 TT2LVK8 TN Carbonic anhydrase IX (CA-IX) TT2LVK8 UP Q16790 TT2LVK8 UC CAH9_HUMAN TT2LVK8 BC Alpha-carbonic anhydrase TT2LVK8 SN Renal cell carcinoma-associated antigen G250; RCC-associated antigen G250; PMW1; P54/58N; Membrane antigen MN; MN; G250 antigen (MN/CA IX/G250); G250; Carbonic anhydrase 9; Carbonate dehydratase IX; CAIX TT2LVK8 GN CA9 TT2LVK8 FC Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia. Reversible hydration of carbon dioxide. TT2LVK8 EC EC 4.2.1.1 TT2LVK8 PD 6G9U; 6G98; 6FE2; 6FE1; 6FE0 TT2LVK8 SQ MAPLCPSPWLPLLIPAPAPGLTVQLLLSLLLLVPVHPQRLPRMQEDSPLGGGSSGEDDPLGEEDLPSEEDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSLKLEDLPTVEAPGDPQEPQNNAHRDKEGDDQSHWRYGGDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLNFRATQPLNGRVIEASFPAGVDSSPRAAEPVQLNSCLAAGDILALVFGLLFAVTSVAFLVQMRRQHRRGTKGGVSYRPAEVAETGA TT2LVK8 TT Clinical trial TT2LVK8 FM Carbon oxygen lyase TT2LVK8 KE hsa00910:Nitrogen metabolism TT2LVK8 RC R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-1475029:Reversible hydration of carbon dioxide TTIDAPM ID TTIDAPM TTIDAPM TN ERK activator kinase 1 (MEK1) TTIDAPM UP Q02750 TTIDAPM UC MP2K1_HUMAN TTIDAPM BC Kinase TTIDAPM SN PRKMK1; Mitogen-activated protein kinase kinase 1; MKK1; MEK 1; MAPKK 1; MAPK/ERKkinase 1; MAPK/ERK kinase 1; MAP kinase kinase 1; Dual specificity mitogen-activated protein kinase kinase 1 TTIDAPM GN MAP2K1 TTIDAPM FC Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator-activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis. Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. TTIDAPM EC EC 2.7.12.2 TTIDAPM PD 5YT3; 5HZE; 5EYM; 5BX0; 4U81 TTIDAPM SQ MPKKKPTPIQLNPAPDGSAVNGTSSAETNLEALQKKLEELELDEQQRKRLEAFLTQKQKVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSRPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGV TTIDAPM TT Clinical trial TTIDAPM FM Kinase TTIDAPM KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04114:Oocyte meiosis; hsa04151:PI3K-Akt signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04320:Dorso-ventral axis formation; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04540:Gap junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04620:Toll-like receptor signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05020:Prion diseases; hsa05034:Alcoholism; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTIDAPM RC R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-5210891:Uptake and function of anthrax toxins; R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5674499:Negative feedback regulation of MAPK pathway; R-HSA-5684264:MAP3K8 (TPL2)-dependent MAPK1/3 activation TTST7KB ID TTST7KB TTST7KB TN Fibroblast growth factor receptor 3 (FGFR3) TTST7KB UP P22607 TTST7KB UC FGFR3_HUMAN TTST7KB BC Kinase TTST7KB SN JTK4; FGFR-3; CD333 TTST7KB GN FGFR3 TTST7KB FC Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Required for normal development of the inner ear. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Plays a role in the regulation of vitamin D metabolism. Mutations that lead to constitutive kinase activation or impair normal FGFR3 maturation, internalization and degradation lead to aberrant signaling. Over-expressed or constitutively activated FGFR3 promotes activation of PTPN11/SHP2, STAT1, STAT5A and STAT5B. Secreted isoform 3 retains its capacity to bind FGF1 and FGF2 and hence may interfere with FGF signaling. Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. TTST7KB EC EC 2.7.10.1 TTST7KB PD 4K33; 2LZL; 1RY7 TTST7KB SQ MGAPACALALCVAVAIVAGASSESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGEDEAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELVEADEAGSVYAGILSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKISRFPLKRQVSLESNASMSSNTPLVRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTPSSSSSGDDSVFAHDLLPPAPPSSGGSRT TTST7KB TT Successful TTST7KB FM Kinase TTST7KB KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05219:Bladder cancer; hsa05230:Central carbon metabolism in cancer TTST7KB RC R-HSA-2033514:FGFR3 mutant receptor activation TTRSMW9 ID TTRSMW9 TTRSMW9 TN Glycogen synthase kinase-3 beta (GSK-3B) TTRSMW9 UP P49841 TTRSMW9 UC GSK3B_HUMAN TTRSMW9 BC Kinase TTRSMW9 SN Serine/threonine-protein kinase GSK3B; GSK-3 beta TTRSMW9 GN GSK3B TTRSMW9 FC Requires primed phosphorylation of the majority of its substrates. In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair. Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin. Is necessary for the establishment of neuronal polarity and axon outgrowth. Phosphorylates MARK2, leading to inhibit its activity. Phosphorylates SIK1 at 'Thr-182', leading to sustain its activity. Phosphorylates ZC3HAV1 which enhances its antiviral activity. Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation. Phosphorylates SFPQ at 'Thr-687' upon T-cell activation. Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including ARNTL/BMAL1, CLOCK and PER2. Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation. Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation. Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation. Regulates the circadian rhythmicity of hippocampal long-term potentiation and ARNTL/BMLA1 and PER2 expression. Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, leading to activate KAT5/TIP60 acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer. Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. TTRSMW9 EC EC 2.7.11.26 TTRSMW9 PD 6NPZ; 6H0U; 6GN1; 6GJO; 6BUU TTRSMW9 SQ MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST TTRSMW9 TT Clinical trial TTRSMW9 FM Kinase TTRSMW9 KE hsa04012:ErbB signaling pathway; hsa04062:Chemokine signaling pathway; hsa04110:Cell cycle; hsa04151:PI3K-Akt signaling pathway; hsa04310:Wnt signaling pathway; hsa04340:Hedgehog signaling pathway; hsa04360:Axon guidance; hsa04390:Hippo signaling pathway; hsa04510:Focal adhesion; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04728:Dopaminergic synapse; hsa04910:Insulin signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05010:Alzheimer's disease; hsa05160:Hepatitis C; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05210:Colorectal cancer; hsa05213:Endometrial cancer; hsa05215:Prostate cancer; hsa05217:Basal cell carcinoma TTRSMW9 RC R-HSA-195253:Degradation of beta-catenin by the destruction complex; R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-3371453:Regulation of HSF1-mediated heat shock response; R-HSA-399956:CRMPs in Sema3A signaling; R-HSA-4641262:Disassembly of the destruction complex and recruitment of AXIN to the membrane; R-HSA-5358747:S33 mutants of beta-catenin aren't phosphorylated; R-HSA-5358749:S37 mutants of beta-catenin aren't phosphorylated; R-HSA-5358751:S45 mutants of beta-catenin aren't phosphorylated; R-HSA-5358752:T41 mutants of beta-catenin aren't phosphorylated; R-HSA-5610783:Degradation of GLI2 by the proteasome; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer TTSHTOI ID TTSHTOI TTSHTOI TN Histone deacetylase 2 (HDAC2) TTSHTOI UP Q92769 TTSHTOI UC HDAC2_HUMAN TTSHTOI BC Carbon-nitrogen hydrolase TTSHTOI SN HD2 TTSHTOI GN HDAC2 TTSHTOI FC Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). TTSHTOI EC EC 3.5.1.98 TTSHTOI PD 6G3O; 5IX0; 5IWG; 4LY1; 4LXZ TTSHTOI SQ MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP TTSHTOI TT Clinical trial TTSHTOI FM Carbon nitrogen hydrolase TTSHTOI KE hsa04110:Cell cycle; hsa04330:Notch signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05016:Huntington's disease; hsa05034:Alcoholism; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05203:Viral carcinogenesis; hsa05220:Chronic myeloid leukemia TTSHTOI RC R-HSA-193670:p75NTR negatively regulates cell cycle via SC1; R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-3214815:HDACs deacetylate histones; R-HSA-427413:NoRC negatively regulates rRNA expression; R-HSA-73762:RNA Polymerase I Transcription Initiation; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTHY57M ID TTHY57M TTHY57M TN Matrix metalloproteinase-13 (MMP-13) TTHY57M UP P45452 TTHY57M UC MMP13_HUMAN TTHY57M BC Peptidase TTHY57M SN Matrix metalloproteinase 13; Collagenase-3; Collagenase 3 TTHY57M GN MMP13 TTHY57M FC Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CTGF. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CTGF. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion. Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. TTHY57M EC EC 3.4.24.- TTHY57M PD 830C; 5UWN; 5UWM; 5UWL; 5UWK TTHY57M SQ MHPGVLAAFLFLSWTHCRALPLPSGGDEDDLSEEDLQFAERYLRSYYHPTNLAGILKENAASSMTERLREMQSFFGLEVTGKLDDNTLDVMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPANSILWC TTHY57M TT Clinical trial TTHY57M FM Peptidase TTHY57M RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures TTGA1IV ID TTGA1IV TTGA1IV TN Matrix metalloproteinase-8 (MMP-8) TTGA1IV UP P22894 TTGA1IV UC MMP8_HUMAN TTGA1IV BC Peptidase TTGA1IV SN PMNL-CL; PMNL collagenase; Neutrophil collagenase; CLG1 TTGA1IV GN MMP8 TTGA1IV FC Can degrade fibrillar type I, II, and III collagens. TTGA1IV EC EC 3.4.24.34 TTGA1IV PD 5H8X; 4QKZ; 3TT4; 3DPF; 3DPE TTGA1IV SQ MFSLKTLPFLLLLHVQISKAFPVSSKEKNTKTVQDYLEKFYQLPSNQYQSTRKNGTNVIVEKLKEMQRFFGLNVTGKPNEETLDMMKKPRCGVPDSGGFMLTPGNPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYGLSSNPIQPTGPSTPKPCDPSLTFDAITTLRGEILFFKDRYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGYDILQGYPKDISNYGFPSSVQAIDAAVFYRSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGIESKVDAVFQQEHFFHVFSGPRYYAFDLIAQRVTRVARGNKWLNCRYG TTGA1IV TT Clinical trial TTGA1IV FM Peptidase TTGA1IV RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases TT6X50U ID TT6X50U TT6X50U TN Matrix metalloproteinase-9 (MMP-9) TT6X50U UP P14780 TT6X50U UC MMP9_HUMAN TT6X50U BC Peptidase TT6X50U SN Matrix metalloproteinase 9; GELB; CLG4B; 92 kDa type IV collagenase; 92 kDa gelatinase TT6X50U GN MMP9 TT6X50U FC Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. TT6X50U EC EC 3.4.24.35 TT6X50U PD 6ESM; 5UE4; 5UE3; 5TH9; 5TH6 TT6X50U SQ MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED TT6X50U TT Clinical trial TT6X50U FM Peptidase TT6X50U KE hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04915:Estrogen signaling pathway; hsa05161:Hepatitis B; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05219:Bladder cancer TT6X50U RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TTWTSCV ID TTWTSCV TTWTSCV TN RAC-alpha serine/threonine-protein kinase (AKT1) TTWTSCV UP P31749 TTWTSCV UC AKT1_HUMAN TTWTSCV BC Kinase TTWTSCV SN RAC-PK-alpha; RAC; Proto-oncogene c-Akt; Protein kinase B alpha; PKB alpha TTWTSCV GN AKT1 TTWTSCV FC AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53. TTWTSCV EC EC 2.7.11.1 TTWTSCV PD 6NPZ; 6HHJ; 6HHI; 6HHH; 6HHG TTWTSCV SQ MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA TTWTSCV TT Clinical trial TTWTSCV FM Kinase TTWTSCV KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04530:Tight junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04728:Dopaminergic synapse; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04922:Glucagon signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04973:Carbohydrate digestion and absorption; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTWTSCV RC R-HSA-111447:Activation of BAD and translocation to mitochondria; R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1445148:Translocation of GLUT4 to the plasma membrane; R-HSA-1474151:Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation; R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-198693:AKT phosphorylates targets in the nucleus; R-HSA-199418:Negative regulation of the PI3K/AKT network; R-HSA-203615:eNOS activation; R-HSA-211163:AKT-mediated inactivation of FOXO1A; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-3769402:Deactivation of the beta-catenin transactivating complex; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-450604:KSRP (KHSRP) binds and destabilizes mRNA; R-HSA-5218920:VEGFR2 mediated vascular permeability; R-HSA-5628897:TP53 Regulates Metabolic Genes; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer TTUJFD0 ID TTUJFD0 TTUJFD0 TN Telomerase reverse transcriptase (TERT) TTUJFD0 UP O14746 TTUJFD0 UC TERT_HUMAN TTUJFD0 BC Kinase TTUJFD0 SN Telomerase-associated protein 2; Telomerase catalytic subunit; TRT; TP2; TCS1; HEST2; EST2 TTUJFD0 GN TERT TTUJFD0 FC Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis. TTUJFD0 EC EC 2.7.7.49 TTUJFD0 PD 5UGW; 5MER; 5MEQ; 5MEP; 5MEO TTUJFD0 SQ MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQVWKNPTFFLRVISDTASLCYSILKAKNAGMSLGAKGAAGPLPSEAVQWLCHQAFLLKLTRHRVTYVPLLGSLRTAQTQLSRKLPGTTLTALEAAANPALPSDFKTILD TTUJFD0 TT Clinical trial TTUJFD0 FM Nucleotidyltransferase TTUJFD0 RC R-HSA-201722:Formation of the beta-catenin:TCF transactivating complex TT6AZXG ID TT6AZXG TT6AZXG TN TNF alpha converting enzyme (ADAM17) TT6AZXG UP P78536 TT6AZXG UC ADA17_HUMAN TT6AZXG BC Peptidase TT6AZXG SN TNFalpha converting enzyme; TNF-alpha-converting enzyme; TNF-alpha converting enzyme; TNF-alpha convertase; TACE; Snake venom-like protease; Disintegrin and metalloproteinase domain-containing protein 17; CSVP; CD156b antigen; CD156b; ADAM 17; A disintegrin and metalloproteinase domain 17 TT6AZXG GN ADAM17 TT6AZXG FC Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2. Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3. Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. TT6AZXG EC EC 3.4.24.86 TT6AZXG PD 3O64; 3LGP; 3LEA; 3LE9; 3L0V TT6AZXG SQ MRQSLLFLTSVVPFVLAPRPPDDPGFGPHQRLEKLDSLLSDYDILSLSNIQQHSVRKRDLQTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQDFFTGHVVGEPDSRVLAHIRDDDVIIRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKNVSRLQSPKVCGYLKVDNEELLPKGLVDREPPEELVHRVKRRADPDPMKNTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNMAKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGNSRVDEGEECDPGIMYLNNDTCCNSDCTLKEGVQCSDRNSPCCKNCQFETAQKKCQEAINATCKGVSYCTGNSSECPPPGNAEDDTVCLDLGKCKDGKCIPFCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWDFIDQLSINTFGKFLADNIVGSVLVFSLIFWIPFSILVHCVDKKLDKQYESLSLFHPSNVEMLSSMDSASVRIIKPFPAPQTPGRLQPAPVIPSAPAAPKLDHQRMDTIQEDPSTDSHMDEDGFEKDPFPNSSTAAKSFEDLTDHPVTRSEKAASFKLQRQNRVDSKETEC TT6AZXG TT Clinical trial TT6AZXG FM Peptidase TT6AZXG KE hsa04330:Notch signaling pathway; hsa05010:Alzheimer's disease; hsa05120:Epithelial cell signaling in Helicobacter pylori infection TT6AZXG RC R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-1442490:Collagen degradation; R-HSA-193692:Regulated proteolysis of p75NTR; R-HSA-2122948:Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2660826:Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant; R-HSA-2691232:Constitutive Signaling by NOTCH1 HD Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-75893:TNF signaling; R-HSA-982772:Growth hormone receptor signaling TT2Q6G1 ID TT2Q6G1 TT2Q6G1 TN Vascular endothelial growth factor receptor 1 (FLT-1) TT2Q6G1 UP P17948 TT2Q6G1 UC VGFR1_HUMAN TT2Q6G1 BC Kinase TT2Q6G1 SN Vascular permeability factor receptor; VEGFR1; VEGFR-1; VEGF-1 receptor; Tyrosine-protein kinase receptor FLT; Tyrosine-protein kinase FRT; Fms-like tyrosine kinase 1; FRT; FLT TT2Q6G1 GN FLT1 TT2Q6G1 FC May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Likewise, isoforms lacking a transmembrane domain, such as isoform 2, isoform 3 and isoform 4, may function as decoy receptors for VEGFA. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Isoform 1 phosphorylates PLCG. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1. Isoform 7 has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion. Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. TT2Q6G1 EC EC 2.7.10.1 TT2Q6G1 PD 5T89; 5EX3; 5ABD; 4CL7; 4CKV TT2Q6G1 SQ MVSYWDTGVLLCALLSCLLLTGSSSGSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNTSVHIYDKAFITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTATLIVNVKPQIYEKAVSSFPDPALYPLGSRQILTCTAYGIPQPTIKWFWHPCNHNHSEARCDFCSNNEESFILDADSNMGNRIESITQRMAIIEGKNKMASTLVVADSRISGIYICIASNKVGTVGRNISFYITDVPNGFHVNLEKMPTEGEDLKLSCTVNKFLYRDVTWILLRTVNNRTMHYSISKQKMAITKEHSITLNLTIMNVSLQDSGTYACRARNVYTGEEILQKKEITIRDQEAPYLLRNLSDHTVAISSSTTLDCHANGVPEPQITWFKNNHKIQQEPGIILGPGSSTLFIERVTEEDEGVYHCKATNQKGSVESSAYLTVQGTSDKSNLELITLTCTCVAATLFWLLLTLFIRKMKRSSSEIKTDYLSIIMDPDEVPLDEQCERLPYDASKWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRTVAVKMLKEGATASEYKALMTELKILTHIGHHLNVVNLLGACTKQGGPLMVIVEYCKYGNLSNYLKSKRDLFFLNKDAALHMEPKKEKMEPGLEQGKKPRLDSVTSSESFASSGFQEDKSLSDVEEEEDSDGFYKEPITMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDTRLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGGSPYPGVQMDEDFCSRLREGMRMRAPEYSTPEIYQIMLDCWHRDPKERPRFAELVEKLGDLLQANVQQDGKDYIPINAILTGNSGFTYSTPAFSEDFFKESISAPKFNSGSSDDVRYVNAFKFMSLERIKTFEELLPNATSMFDDYQGDSSTLLASPMLKRFTWTDSKPKASLKIDLRVTSKSKESGLSDVSRPSFCHSSCGHVSEGKRRFTYDHAELERKIACCSPPPDYNSVVLYSTPPI TT2Q6G1 TT Successful TT2Q6G1 FM Kinase TT2Q6G1 KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa05202:Transcriptional misregulation in cancer; hsa05323:Rheumatoid arthritis TT2Q6G1 RC R-HSA-194306:Neurophilin interactions with VEGF and VEGFR; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization TT140V6 ID TT140V6 TT140V6 TN HUMAN vascular endothelial growth factor (VEGF) TT140V6 UP P15692; P49765; P49767; O43915 TT140V6 UC VEGFA_HUMAN; VEGFB_HUMAN; VEGFC_HUMAN; VEGFD_HUMAN TT140V6 BC Growth factor TT140V6 SN Vascular endothelial cell growth factor TT140V6 FC Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development. TT140V6 SQ MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPHPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR TTDJB68 ID TTDJB68 TTDJB68 TN HUMAN MYD88NF-kappa-B proinflammatory pathway (MYD88-NFKB pathway) TTDJB68 UP Pathway/Process TTK3C21 ID TTK3C21 TTK3C21 TN Acetoacetyl-CoA thiolase (ACAT1) TTK3C21 UP P24752 TTK3C21 UC THIL_HUMAN TTK3C21 BC Acyltransferase TTK3C21 SN T2; MAT; Acetyl-CoA acetyltransferase, mitochondrial TTK3C21 GN ACAT1 TTK3C21 FC Plays a major role in ketone body metabolism. TTK3C21 EC EC 2.3.1.9 TTK3C21 PD 2IBY; 2IBW; 2IBU; 2IB9; 2IB8 TTK3C21 SQ MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL TTK3C21 TT Clinical trial TTK3C21 FM Acyltransferase TTK3C21 KE hsa00071:Fatty acid degradation; hsa00072:Synthesis and degradation of ketone bodies; hsa00280:Valine, leucine and isoleucine degradation; hsa00310:Lysine degradation; hsa00380:Tryptophan metabolism; hsa00620:Pyruvate metabolism; hsa00630:Glyoxylate and dicarboxylate metabolism; hsa00640:Propanoate metabolism; hsa00650:Butanoate metabolism; hsa00900:Terpenoid backbone biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa01212:Fatty acid metabolism TTJFY5U ID TTJFY5U TTJFY5U TN Adenosine A3 receptor (ADORA3) TTJFY5U UP P0DMS8 TTJFY5U UC AA3R_HUMAN TTJFY5U BC GPCR rhodopsin TTJFY5U SN Adenosine receptor A3A; Adenosine receptor A3; Adenosine 3 receptor; A3AR; A3 Adenosine receptor TTJFY5U GN ADORA3 TTJFY5U FC The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. Isoform 2: Receptor for adenosine. TTJFY5U PD 1R7N; 1OEA TTJFY5U SQ MPNNSTALSLANVTYITMEIFIGLCAIVGNVLVICVVKLNPSLQTTTFYFIVSLALADIAVGVLVMPLAIVVSLGITIHFYSCLFMTCLLLIFTHASIMSLLAIAVDRYLRVKLTVRYKRVTTHRRIWLALGLCWLVSFLVGLTPMFGWNMKLTSEYHRNVTFLSCQFVSVMRMDYMVYFSFLTWIFIPLVVMCAIYLDIFYIIRNKLSLNLSNSKETGAFYGREFKTAKSLFLVLFLFALSWLPLSIINCIIYFNGEVPQLVLYMGILLSHANSMMNPIVYAYKIKKFKETYLLILKACVVCHPSDSLDTSIEKNSE TTJFY5U TT Clinical trial TTJFY5U RC R-HSA-417973:Adenosine P1 receptors; R-HSA-418594:G alpha (i) signalling events TTL732K ID TTL732K TTL732K TN Adenosine kinase (ADK) TTL732K UP P55263 TTL732K UC ADK_HUMAN TTL732K BC Kinase TTL732K SN Adenosine 5'-phosphotransferase; AK TTL732K GN ADK TTL732K FC Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides. ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. TTL732K EC EC 2.7.1.20 TTL732K PD 4O1L; 2I6B; 2I6A; 1BX4 TTL732K SQ MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPDFH TTL732K TT Clinical trial TTL732K KE hsa00230:Purine metabolism; hsa01100:Metabolic pathways TTL732K RC R-HSA-74217:Purine salvage TTXSU2Y ID TTXSU2Y TTXSU2Y TN Aggrecanase (ADAMTS5) TTXSU2Y UP Q9UNA0 TTXSU2Y UC ATS5_HUMAN TTXSU2Y BC Peptidase TTXSU2Y SN Aggrecanase-2; ADMP-2; ADAMTS5; ADAMTS-5; ADAM-TS5; ADAM-TS 5; ADAM-TS 11; A disintegrin and metalloproteinase with thrombospondinmotifs 5 TTXSU2Y GN ADAMTS5 TTXSU2Y FC Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period. TTXSU2Y EC EC 3.4.24.- TTXSU2Y PD 3LJT; 3HYG; 3HY9; 3HY7; 3B8Z TTXSU2Y SQ MLLGWASLLLCAFRLPLAAVGPAATPAQDKAGQPPTAAAAAQPRRRQGEEVQERAEPPGHPHPLAQRRRSKGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDGSVGIAGFVPAGGGTSAPWRHRSHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEKGRVYGDGSARILHVYTREGFSFEALPPRASCETPASTPEAHEHAPAHSNPSGRAALASQLLDQSALSPAGGSGPQTWWRRRRRSISRARQVELLLVADASMARLYGRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYDAAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDSKFCEETFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQILGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGTPCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSLMPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVLPADVCKLTCRAKGTGYYVVFSPKVTDGTECRLYSNSVCVRGKCVRTGCDGIIGSKLQYDKCGVCGGDNSSCTKIVGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPTKPLDVRYSFFVPKKSTPKVNSVTSHGSNKVGSHTSQPQWVTGPWLACSRTCDTGWHTRTVQCQDGNRKLAKGCPLSQRPSAFKQCLLKKC TTXSU2Y TT Clinical trial TTXSU2Y RC R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-5173214:O-glycosylation of TSR domain-containing proteins TTPHMWB ID TTPHMWB TTPHMWB TN Aminopeptidase N (ANPEP) TTPHMWB UP P15144 TTPHMWB UC AMPN_HUMAN TTPHMWB BC Peptidase TTPHMWB SN Myeloid plasma membrane glycoprotein CD13; Microsomal aminopeptidase; HAPN; Gp150; Aminopeptidase M; Alanyl aminopeptidase; ANPEP TTPHMWB GN ANPEP TTPHMWB FC Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection. TTPHMWB EC EC 3.4.11.2 TTPHMWB PD 6ATK; 5LHD; 4FYT; 4FYS; 4FYR TTPHMWB SQ MAKGFYISKSLGILGILLGVAAVCTIIALSVVYSQEKNKNANSSPVASTTPSASATTNPASATTLDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCKEATDVIIIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVVHLKGSLVKDSQYEMDSEFEGELADDLAGFYRSEYMEGNVRKVVATTQMQAADARKSFPCFDEPAMKAEFNITLIHPKDLTALSNMLPKGPSTPLPEDPNWNVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLIRIWARPSAIAAGHGDYALNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLVTYRENSLLFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEINTPAQISELFDAISYSKGASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTIYLNLWDHLQEAVNNRSIQLPTTVRDIMNRWTLQMGFPVITVDTSTGTLSQEHFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDYWLIDVRAQNDLFSTSGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQIINDAFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNGVPECEEMVSGLFKQWMENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWEQFRNATLVNEADKLRAALACSKELWILNRYLSYTLNPDLIRKQDATSTIISITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSNLIQAVTRRFSTEYELQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQWFTENSK TTPHMWB TT Clinical trial TTPHMWB KE hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways; hsa04614:Renin-angiotensin system; hsa04640:Hematopoietic cell lineage TTPHMWB RC R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins TT9VGXW ID TT9VGXW TT9VGXW TN Angiopoietin 1 receptor (TEK) TT9VGXW UP Q02763 TT9VGXW UC TIE2_HUMAN TT9VGXW BC Kinase TT9VGXW SN hTIE2; VMCM1; VMCM; Tyrosine-protein kinase receptor TIE-2; Tyrosine-protein kinase receptor TEK; Tyrosine kinase with Ig and EGF homology domains-2; Tunica interna endothelial cell kinase; TIE2; P140 TEK; Endothelial tyrosine kinase; Endothelial Cell-Specific Receptor TIE-2; CD202b antigen; CD202b TT9VGXW GN TEK TT9VGXW FC Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1. Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. TT9VGXW EC EC 2.7.10.1 TT9VGXW PD 6MWE; 5UTK; 5MYB; 5MYA; 4X3J TT9VGXW SQ MDSLASLVLCGVSLLLSGTVEGAMDLILINSLPLVSDAETSLTCIASGWRPHEPITIGRDFEALMNQHQDPLEVTQDVTREWAKKVVWKREKASKINGAYFCEGRVRGEAIRIRTMKMRQQASFLPATLTMTVDKGDNVNISFKKVLIKEEDAVIYKNGSFIHSVPRHEVPDILEVHLPHAQPQDAGVYSARYIGGNLFTSAFTRLIVRRCEAQKWGPECNHLCTACMNNGVCHEDTGECICPPGFMGRTCEKACELHTFGRTCKERCSGQEGCKSYVFCLPDPYGCSCATGWKGLQCNEACHPGFYGPDCKLRCSCNNGEMCDRFQGCLCSPGWQGLQCEREGIQRMTPKIVDLPDHIEVNSGKFNPICKASGWPLPTNEEMTLVKPDGTVLHPKDFNHTDHFSVAIFTIHRILPPDSGVWVCSVNTVAGMVEKPFNISVKVLPKPLNAPNVIDTGHNFAVINISSEPYFGDGPIKSKKLLYKPVNHYEAWQHIQVTNEIVTLNYLEPRTEYELCVQLVRRGEGGEGHPGPVRRFTTASIGLPPPRGLNLLPKSQTTLNLTWQPIFPSSEDDFYVEVERRSVQKSDQQNIKVPGNLTSVLLNNLHPREQYVVRARVNTKAQGEWSEDLTAWTLSDILPPQPENIKISNITHSSAVISWTILDGYSISSITIRYKVQGKNEDQHVDVKIKNATITQYQLKGLEPETAYQVDIFAENNIGSSNPAFSHELVTLPESQAPADLGGGKMLLIAILGSAGMTCLTVLLAFLIILQLKRANVQRRMAQAFQNVREEPAVQFNSGTLALNRKVKNNPDPTIYPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKFTYAGIDCSAEEAA TT9VGXW TT Clinical trial TT9VGXW FM Kinase TT9VGXW KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa05323:Rheumatoid arthritis TT9VGXW RC R-HSA-210993:Tie2 Signaling; R-HSA-5673001:RAF/MAP kinase cascade TT9RTBL ID TT9RTBL TT9RTBL TN Aurora B messenger RNA (AURKB mRNA) TT9RTBL UP Q96GD4 TT9RTBL UC AURKB_HUMAN TT9RTBL BC mRNA target TT9RTBL SN Serine/threonine-protein kinase aurora-B (mRNA); Serine/threonine-protein kinase 5 (mRNA); Serine/threonine-protein kinase 12 (mRNA); Serine/threonine protein kinase 12 (mRNA); STK5 (mRNA); STK12 (mRNA); Aurora/IPL1-related kinase 2 (mRNA); Aurora-related kinase 2 (mRNA); Aurora-B (mRNA); Aurora-2 kinase (mRNA); Aurora-2 (mRNA); Aurora- and Ipl1-like midbody-associated protein 1 (mRNA); Aurora 1 (mRNA); ARK2 (mRNA); ARK-2 (mRNA); AIRK2 (mRNA); AIM1 (mRNA); AIM-1 (mRNA); AIK2 (mRNA) TT9RTBL GN AURKB TT9RTBL FC The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, HASPIN, and histone H3. A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). A positive feedback between HASPIN and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGO1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. TT9RTBL EC EC 2.7.11.1 TT9RTBL PD 4AF3 TT9RTBL SQ MAQKENSYPWPYGRQTAPSGLSTLPQRVLRKEPVTPSALVLMSRSNVQPTAAPGQKVMENSSGTPDILTRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA TT9RTBL TT Clinical trial TT9RTBL FM mRNA target TT9RTBL RC R-HSA-174178:APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1; R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-68877:Mitotic Prometaphase TTPS3C0 ID TTPS3C0 TTPS3C0 TN Aurora kinase A (AURKA) TTPS3C0 UP O14965 TTPS3C0 UC AURKA_HUMAN TTPS3C0 BC Kinase TTPS3C0 SN hARK1; Serine/threonine-protein kinase aurora-A; Serine/threonine-protein kinase 6; Serine/threonine-protein kinase 15; Serine/threonine kinase 15; STK6; STK15; IAK1; Breast tumor-amplified kinase; BTAK; Aurora/IPL1-related kinase 1; Aurora-related kinase 1; Aurora-A; Aurora 2; AYK1; AURA; ARK1; ARK-1; AIRK1; AIK TTPS3C0 GN AURKA TTPS3C0 FC Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis. Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression. TTPS3C0 EC EC 2.7.11.1 TTPS3C0 PD 6R4D; 6R4C; 6R4B; 6R4A; 6R49 TTPS3C0 SQ MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRVPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS TTPS3C0 TT Clinical trial TTPS3C0 FM Kinase TTPS3C0 KE hsa04114:Oocyte meiosis TTPS3C0 RC R-HSA-174178:APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1; R-HSA-2565942:Regulation of PLK1 Activity at G2/M Transition TT5LS6T ID TT5LS6T TT5LS6T TN Aurora kinase B (AURKB) TT5LS6T UP Q96GD4 TT5LS6T UC AURKB_HUMAN TT5LS6T BC Kinase TT5LS6T SN Serine/threonine-protein kinase aurora-B; Serine/threonine-protein kinase 5; Serine/threonine-protein kinase 12; Serine/threonine protein kinase 12; STK5; STK12; Aurora/IPL1-related kinase 2; Aurora-related kinase 2; Aurora-B; Aurora-2 kinase; Aurora-2; Aurora- and Ipl1-like midbody-associated protein 1; Aurora 1; ARK2; ARK-2; AIRK2; AIM1; AIM-1; AIK2 TT5LS6T GN AURKB TT5LS6T FC The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, HASPIN, and histone H3. A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). A positive feedback between HASPIN and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGO1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. TT5LS6T EC EC 2.7.11.1 TT5LS6T PD 4AF3 TT5LS6T SQ MAQKENSYPWPYGRQTAPSGLSTLPQRVLRKEPVTPSALVLMSRSNVQPTAAPGQKVMENSSGTPDILTRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA TT5LS6T TT Clinical trial TT5LS6T FM Kinase TT5LS6T RC R-HSA-174178:APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1; R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-68877:Mitotic Prometaphase TTLYXIT ID TTLYXIT TTLYXIT TN Aurora kinase C (AURKC) TTLYXIT UP Q9UQB9 TTLYXIT UC AURKC_HUMAN TTLYXIT BC Kinase TTLYXIT SN Serine/threonine-protein kinase aurora-C; STK13; Aurora/Ipl1/Eg2 protein 2; Aurora/Ipl1-related kinase 3; Aurora-related kinase 3; Aurora-C; Aurora 3; ARK3; ARK-3; AIRK3; AIK3; AIE2 TTLYXIT GN AURKC TTLYXIT FC The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin and INCENP leading to increased AURKC activity. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'. Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. TTLYXIT EC EC 2.7.11.1 TTLYXIT PD 6GR9; 6GR8 TTLYXIT SQ MSSPRAVVQLGKAQPAGEELATANQTAQQPSSPAMRRLTVDDFEIGRPLGKGKFGNVYLARLKESHFIVALKVLFKSQIEKEGLEHQLRREIEIQAHLQHPNILRLYNYFHDARRVYLILEYAPRGELYKELQKSEKLDEQRTATIIEELADALTYCHDKKVIHRDIKPENLLLGFRGEVKIADFGWSVHTPSLRRKTMCGTLDYLPPEMIEGRTYDEKVDLWCIGVLCYELLVGYPPFESASHSETYRRILKVDVRFPLSMPLGARDLISRLLRYQPLERLPLAQILKHPWVQAHSRRVLPPCAQMAS TTLYXIT TT Clinical trial TTLYXIT KE hsa04114:Oocyte meiosis TTLYXIT RC R-HSA-174178:APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1; R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-5663220:RHO GTPases Activate Formins TT0EOB8 ID TT0EOB8 TT0EOB8 TN B-Raf messenger RNA (BRAF mRNA) TT0EOB8 UP P15056 TT0EOB8 UC BRAF_HUMAN TT0EOB8 BC mRNA target TT0EOB8 SN V-Raf murine sarcoma viral oncogene homolog B1 (mRNA); Serine/threonine-protein kinase B-raf (mRNA); RAFB1 (mRNA); Proto-oncogene B-Raf (mRNA); P94 (mRNA); BRAF1 (mRNA); BRAF(V599E) (mRNA); BRAF serine/threonine kinase (mRNA); B-raf protein (mRNA); B-Raf (mRNA) TT0EOB8 GN BRAF TT0EOB8 FC May play a role in the postsynaptic responses of hippocampal neuron. Phosphorylates MAP2K1, and thereby contributes to the MAP kinase signal transduction pathway. Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus. TT0EOB8 EC EC 2.7.11.1 TT0EOB8 PD 6CAD; 6B8U; 5VYK; 5VR3; 5VAM TT0EOB8 SQ MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH TT0EOB8 TT Clinical trial TT0EOB8 FM mRNA target TT0EOB8 KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04015:Rap1 signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04068:FoxO signaling pathway; hsa04150:mTOR signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04510:Focal adhesion; hsa04650:Natural killer cell mediated cytotoxicity; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa05034:Alcoholism; hsa05160:Hepatitis C; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer TT0EOB8 RC R-HSA-1295596:Spry regulation of FGF signaling; R-HSA-170968:Frs2-mediated activation; R-HSA-170984:ARMS-mediated activation; R-HSA-442742:CREB phosphorylation through the activation of Ras; R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5674499:Negative feedback regulation of MAPK pathway; R-HSA-5675221:Negative regulation of MAPK pathway TTER6YH ID TTER6YH TTER6YH TN Casein kinase II alpha (CSNK2A1) TTER6YH UP P68400 TTER6YH UC CSK21_HUMAN TTER6YH BC Kinase TTER6YH SN Protein kinase CK2; Casein kinase II subunit alpha; CK2A1; CK II alpha; CK II TTER6YH GN CSNK2A1 TTER6YH FC Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry. Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue. Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. TTER6YH EC EC 2.7.11.1 TTER6YH PD 6Q4Q; 6Q38; 6HME; 6HBN; 6GMD TTER6YH SQ MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAAAGAQQ TTER6YH TT Clinical trial TTER6YH FM Kinase TTER6YH KE hsa03008:Ribosome biogenesis in eukaryotes; hsa04064:NF-kappa B signaling pathway; hsa04310:Wnt signaling pathway; hsa04520:Adherens junction; hsa04530:Tight junction; hsa05162:Measles; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection TTER6YH RC R-HSA-2514853:Condensation of Prometaphase Chromosomes TTPT2QI ID TTPT2QI TTPT2QI TN Cathepsin D (CTSD) TTPT2QI UP P07339 TTPT2QI UC CATD_HUMAN TTPT2QI BC Peptidase TTPT2QI SN CPSD; CD TTPT2QI GN CTSD TTPT2QI FC Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease. Acid protease active in intracellular protein breakdown. TTPT2QI EC EC 3.4.23.5 TTPT2QI PD 4OD9; 4OC6; 4OBZ; 1LYW; 1LYB TTPT2QI SQ MQPSSLLPLALCLLAAPASALVRIPLHKFTSIRRTMSEVGGSVEDLIAKGPVSKYSQAVPAVTEGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQSASSASALGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNRVGFAEAARL TTPT2QI TT Clinical trial TTPT2QI FM Peptidase TTPT2QI KE hsa04071:Sphingolipid signaling pathway; hsa04142:Lysosome; hsa05152:Tuberculosis TTPT2QI RC R-HSA-1442490:Collagen degradation; R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins; R-HSA-2132295:MHC class II antigen presentation TTQAJF1 ID TTQAJF1 TTQAJF1 TN Cathepsin G (CTSG) TTQAJF1 UP P08311 TTQAJF1 UC CATG_HUMAN TTQAJF1 BC Peptidase TTQAJF1 SN CG TTQAJF1 GN CTSG TTQAJF1 FC Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P. aeruginosa, antibacterial activity is inhibited by LPS from P. aeruginosa, Z-Gly-Leu-Phe-CH2Cl and phenylmethylsulfonyl fluoride. Serine protease with trypsin- and chymotrypsin-like specificity. TTQAJF1 EC EC 3.4.21.20 TTQAJF1 PD 1T32; 1KYN; 1CGH; 1AU8 TTQAJF1 SQ MQPLLLLLAFLLPTGAEAGEIIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQRRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGDSGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKLLDQMETPL TTQAJF1 TT Clinical trial TTQAJF1 FM Peptidase TTQAJF1 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04142:Lysosome; hsa04614:Renin-angiotensin system; hsa05146:Amoebiasis; hsa05322:Systemic lupus erythematosus TTQAJF1 RC R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins; R-HSA-381426:Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) TTDZN01 ID TTDZN01 TTDZN01 TN Cathepsin K (CTSK) TTDZN01 UP P43235 TTDZN01 UC CATK_HUMAN TTDZN01 BC Peptidase TTDZN01 SN Cathepsin X; Cathepsin O2; Cathepsin O; CTSO2; CTSO TTDZN01 GN CTSK TTDZN01 FC Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. TTDZN01 EC EC 3.4.22.38 TTDZN01 PD 7PCK; 6QBS; 6ASH; 5Z5O; 5TUN TTDZN01 SQ MWGLKVLLLPVVSFALYPEEILDTHWELWKKTHRKQYNNKVDEISRRLIWEKNLKYISIHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPLSHSRSNDTLYIPEWEGRAPDSVDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGGYMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNKNNACGIANLASFPKM TTDZN01 TT Clinical trial TTDZN01 FM Peptidase TTDZN01 KE hsa04142:Lysosome; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa05323:Rheumatoid arthritis TTDZN01 RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-2132295:MHC class II antigen presentation TTTU902 ID TTTU902 TTTU902 TN Checkpoint kinase-1 (CHK1) TTTU902 UP O14757 TTTU902 UC CHK1_HUMAN TTTU902 BC Kinase TTTU902 SN Serine/threonine-protein kinase Chk1; Chk1; Cell cycle checkpoint kinase; CHK1 checkpoint homolog TTTU902 GN CHEK1 TTTU902 FC May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A. Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Also phosphorylates NEK6. Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination. Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation. Also promotes repair of DNA cross-links through phosphorylation of FANCE. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may enhance chromatin assembly both in the presence or absence of DNA damage. May also play a role in replication fork maintenance through regulation of PCNA. May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones. Phosphorylates histone H3. 1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes. May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest. Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. TTTU902 EC EC 2.7.11.1 TTTU902 PD 6FCK; 6FCF; 6FC8; 5WI2; 5OQ8 TTTU902 SQ MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKMLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGFSKHIQSNLDFSPVNSASSEENVKYSSSQPEPRTGLSLWDTSPSYIDKLVQGISFSQPTCPDHMLLNSQLLGTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETCEKLGYQWKKSCMNQVTISTTDRRNNKLIFKVNLLEMDDKILVDFRLSKGDGLEFKRHFLKIKGKLIDIVSSQKIWLPAT TTTU902 TT Clinical trial TTTU902 FM Kinase TTTU902 KE hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa05166:HTLV-I infection; hsa05203:Viral carcinogenesis TTTU902 RC R-HSA-176187:Activation of ATR in response to replication stress; R-HSA-5693607:Processing of DNA double-strand break ends; R-HSA-5693616:Presynaptic phase of homologous DNA pairing and strand exchange; R-HSA-69473:G2/M DNA damage checkpoint; R-HSA-69601:Ubiquitin Mediated Degradation of Phosphorylated Cdc25A; R-HSA-75035:Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex TTCG0AL ID TTCG0AL TTCG0AL TN Cholecystokinin receptor type A (CCKAR) TTCG0AL UP P32238 TTCG0AL UC CCKAR_HUMAN TTCG0AL BC GPCR rhodopsin TTCG0AL SN CCKAR; CCK-AR; CCK-A receptor TTCG0AL GN CCKAR TTCG0AL FC Receptor forcholecystokinin. Mediates pancreatic growth and enzyme secretion, smooth muscle contraction of the gall bladder and stomach. Has a 1000-fold higher affinity for CCK rather than for gastrin. It modulates feeding and dopamine-induced behavior in the central and peripheral nervous system. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. TTCG0AL PD 1PB2; 1HZN; 1D6G TTCG0AL SQ MDVVDSLLVNGSNITPPCELGLENETLFCLDQPRPSKEWQPAVQILLYSLIFLLSVLGNTLVITVLIRNKRMRTVTNIFLLSLAVSDLMLCLFCMPFNLIPNLLKDFIFGSAVCKTTTYFMGTSVSVSTFNLVAISLERYGAICKPLQSRVWQTKSHALKVIAATWCLSFTIMTPYPIYSNLVPFTKNNNQTANMCRFLLPNDVMQQSWHTFLLLILFLIPGIVMMVAYGLISLELYQGIKFEASQKKSAKERKPSTTSSGKYEDSDGCYLQKTRPPRKLELRQLSTGSSSRANRIRSNSSAANLMAKKRVIRMLIVIVVLFFLCWMPIFSANAWRAYDTASAERRLSGTPISFILLLSYTSSCVNPIIYCFMNKRFRLGFMATFPCCPNPGPPGARGEVGEEEEGGTTGASLSRFSYSHMSASVPPQ TTCG0AL TT Clinical trial TTCG0AL KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04911:Insulin secretion; hsa04972:Pancreatic secretion TTCG0AL RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TT10AWB ID TT10AWB TT10AWB TN Choline kinase (CHKA) TT10AWB UP P35790 TT10AWB UC CHKA_HUMAN TT10AWB BC Kinase TT10AWB SN ChoK; CHKA; CHETK-alpha TT10AWB GN CHKA TT10AWB FC Has a key role in phospholipid biosynthesis and may contribute to tumor cell growth. Catalyzes the first step in phosphatidylcholine biosynthesis. Contributes to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine. Has higher activity with choline. TT10AWB EC EC 2.7.1.32 TT10AWB PD 5W6O; 5FUT; 5FTG; 5EQY; 5EQP TT10AWB SQ MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPPPPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQMRSCNKEGSEQAQKENEFQGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV TT10AWB TT Clinical trial TT10AWB KE hsa00564:Glycerophospholipid metabolism; hsa01100:Metabolic pathways; hsa05231:Choline metabolism in cancer TT8VUE0 ID TT8VUE0 TT8VUE0 TN Chymase (CYM) TT8VUE0 UP P23946 TT8VUE0 UC CMA1_HUMAN TT8VUE0 BC Peptidase TT8VUE0 SN Mast cell protease I; CYH; Alpha-chymase TT8VUE0 GN CMA1 TT8VUE0 FC Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion. TT8VUE0 EC EC 3.4.21.39 TT8VUE0 PD 5YJP; 5YJM; 4KP0; 4K69; 4K60 TT8VUE0 SQ MLLLPLPLLLFLLCSRAEAGEIIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN TT8VUE0 TT Clinical trial TT8VUE0 FM Peptidase TT8VUE0 KE hsa04614:Renin-angiotensin system TT8VUE0 RC R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins TTN7BL9 ID TTN7BL9 TTN7BL9 TN Corticosteroid 11-beta-dehydrogenase 1 (HSD11B1) TTN7BL9 UP P28845 TTN7BL9 UC DHI1_HUMAN TTN7BL9 BC Short-chain dehydrogenases reductase TTN7BL9 SN HSD11B1; 11beta-HSD1A; 11HSD1; 11-beta-hydroxysteroid dehydrogenase 1; 11-beta-HSD1; 11-DH; 11 beta-hydroxysteroid dehydrogenase type 1 TTN7BL9 GN HSD11B1 TTN7BL9 FC Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7- ketocholesterol to 7-beta-hydroxycholesterol. TTN7BL9 EC EC 1.1.1.146 TTN7BL9 PD 5QII; 5PGY; 5PGX; 5PGW; 5PGV TTN7BL9 SQ MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK TTN7BL9 TT Clinical trial TTN7BL9 KE hsa00140:Steroid hormone biosynthesis; hsa00980:Metabolism of xenobiotics by cytochrome P450; hsa01100:Metabolic pathways; hsa05204:Chemical carcinogenesis TTN7BL9 RC R-HSA-194002:Glucocorticoid biosynthesis TTH6V3D ID TTH6V3D TTH6V3D TN Cyclin-dependent kinase 1 (CDK1) TTH6V3D UP P06493 TTH6V3D UC CDK1_HUMAN TTH6V3D BC Kinase TTH6V3D SN P34CDC2; P34 protein kinase; CDKN1; CDC28A; CDC2 TTH6V3D GN CDK1 TTH6V3D FC Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, LMNA, LMNB, LMNC, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, UL40/R2, RAB4A, RAP1GAP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SAMHD1, SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-mediated dephosphorylation and restoring cell cycle progression. In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. CDK1-cyclin-B complex phosphorylates NCKAP5L and mediates its dissociation from centrosomes during mitosis. Regulates the amplitude of the cyclic expression of the core clock gene ARNTL/BMAL1 by phosphorylating its transcriptional repressor NR1D1, and this phosphorylation is necessary for SCF(FBXW7)-mediated ubiquitination and proteasomal degradation of NR1D1. Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. TTH6V3D EC EC 2.7.11.22 TTH6V3D PD 6GU7; 6GU6; 6GU4; 6GU3; 6GU2 TTH6V3D SQ MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQIKKM TTH6V3D TT Clinical trial TTH6V3D FM Kinase TTH6V3D KE hsa04110:Cell cycle; hsa04114:Oocyte meiosis; hsa04115:p53 signaling pathway; hsa04540:Gap junction; hsa04914:Progesterone-mediated oocyte maturation; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05203:Viral carcinogenesis TTH6V3D RC R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-1538133:G0 and Early G1; R-HSA-157881:Cyclin B2 mediated events; R-HSA-162658:Golgi Cisternae Pericentriolar Stack Reorganization; R-HSA-174184:Cdc20:Phospho-APC/C mediated degradation of Cyclin A; R-HSA-176408:Regulation of APC/C activators between G1/S and early anaphase; R-HSA-176412:Phosphorylation of the APC/C; R-HSA-176417:Phosphorylation of Emi1; R-HSA-2299718:Condensation of Prophase Chromosomes; R-HSA-2465910:MASTL Facilitates Mitotic Progression; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-2514853:Condensation of Prometaphase Chromosomes; R-HSA-2565942:Regulation of PLK1 Activity at G2/M Transition; R-HSA-2980767:Activation of NIMA Kinases NEK9, NEK6, NEK7; R-HSA-380259:Loss of Nlp from mitotic centrosomes; R-HSA-380270:Recruitment of mitotic centrosome proteins and complexes; R-HSA-380284:Loss of proteins required for interphase microtubule organization?from the centrosome; R-HSA-380320:Recruitment of NuMA to mitotic centrosomes; R-HSA-4419969:Depolymerisation of the Nuclear Lamina; R-HSA-5620912:Anchoring of the basal body to the plasma membrane; R-HSA-5687128:MAPK6/MAPK4 signaling; R-HSA-69205:G1/S-Specific Transcription; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition; R-HSA-69478:G2/M DNA replication checkpoint; R-HSA-75035:Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex TT7HF4W ID TT7HF4W TT7HF4W TN Cyclin-dependent kinase 2 (CDK2) TT7HF4W UP P24941 TT7HF4W UC CDK2_HUMAN TT7HF4W BC Kinase TT7HF4W SN Sin3 associated polypeptide; SIN3-associated protein; P33 protein kinase; Cell division protein kinase 2; CDKN2 TT7HF4W GN CDK2 TT7HF4W FC Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1. Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability. Phosphorylates CDK2AP2. Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. TT7HF4W EC EC 2.7.11.22 TT7HF4W PD 6Q4K; 6Q4J; 6Q4I; 6Q4H; 6Q4G TT7HF4W SQ MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL TT7HF4W TT Clinical trial TT7HF4W FM Kinase TT7HF4W KE hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04114:Oocyte meiosis; hsa04115:p53 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa05161:Hepatitis B; hsa05162:Measles; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05215:Prostate cancer; hsa05222:Small cell lung cancer TT7HF4W RC R-HSA-1538133:G0 and Early G1; R-HSA-176187:Activation of ATR in response to replication stress; R-HSA-176408:Regulation of APC/C activators between G1/S and early anaphase; R-HSA-187577:SCF(Skp2)-mediated degradation of p27/p21; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-2559586:DNA Damage/Telomere Stress Induced Senescence; R-HSA-5693607:Processing of DNA double-strand break ends; R-HSA-68911:G2 Phase; R-HSA-68949:Orc1 removal from chromatin; R-HSA-69202:Cyclin E associated events during G1/S transition; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition; R-HSA-69563:p53-Dependent G1 DNA Damage Response; R-HSA-69656:Cyclin A:Cdk2-associated events at S phase entry; R-HSA-912446:Meiotic recombination; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TT1LVF2 ID TT1LVF2 TT1LVF2 TN Cyclin-dependent kinase 9 (CDK9) TT1LVF2 UP P50750 TT1LVF2 UC CDK9_HUMAN TT1LVF2 BC Kinase TT1LVF2 SN Tat-associated kinase complex catalytic subunit; TAK; Similar to cyclin-dependent kinase 9; Serine/threonine-protein kinase PITALRE; Cyclin-dependent protein kinase Cdk9; Cell division protein kinase 9; Cell division cycle 2-like protein kinase 4; CDC2L4; CDC2-related kinase; C-2K TT1LVF2 GN CDK9 TT1LVF2 FC Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e. g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement. RPB1/POLR2A phosphorylation on 'Ser-2' in CTD activates transcription. AR phosphorylation modulates AR transcription factor promoter selectivity and cell growth. DSIF and NELF phosphorylation promotes transcription by inhibiting their negative effect. The phosphorylation of MYOD1 enhances its transcriptional activity and thus promotes muscle differentiation. Protein kinase involved in the regulation of transcription. TT1LVF2 EC EC 2.7.11.22 TT1LVF2 PD 6GZH; 6CYT; 5L1Z; 4OR5; 4OGR TT1LVF2 SQ MAKQYDSVECPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVLVKFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLALISQLCGSITPEVWPNVDNYELYEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKGMLSTHLTSMFEYLAPPRRKGSQITQQSTNQSRNPATTNQTEFERVF TT1LVF2 TT Clinical trial TT1LVF2 FM Kinase TT1LVF2 KE hsa05202:Transcriptional misregulation in cancer TT1LVF2 RC R-HSA-2173796:SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription TTK0O6Y ID TTK0O6Y TTK0O6Y TN Ecto-5'-nucleotidase (CD73) TTK0O6Y UP P21589 TTK0O6Y UC 5NTD_HUMAN TTK0O6Y BC Phosphoric monoester hydrolase TTK0O6Y SN NT5; CD73 antigen; 5'-nucleotidase; 5'-NT TTK0O6Y GN NT5E TTK0O6Y FC Exhibits AMP-, NAD-, and NMN-nucleosidase activities. Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. TTK0O6Y EC EC 3.1.3.5 TTK0O6Y PD 4H2I; 4H2G; 4H2F; 4H2B; 4H1Y TTK0O6Y SQ MCPRAARAPATLLLALGAVLWPAAGAWELTILHTNDVHSRLEQTSEDSSKCVNASRCMGGVARLFTKVQQIRRAEPNVLLLDAGDQYQGTIWFTVYKGAEVAHFMNALRYDAMALGNHEFDNGVEGLIEPLLKEAKFPILSANIKAKGPLASQISGLYLPYKVLPVGDEVVGIVGYTSKETPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVVGGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKIEFDERGNVISSHGNPILLNSSIPEDPSIKADINKWRIKLDNYSTQELGKTIVYLDGSSQSCRFRECNMGNLICDAMINNNLRHTDEMFWNHVSMCILNGGGIRSPIDERNNGTITWENLAAVLPFGGTFDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDLSRKPGDRVVKLDVLCTKCRVPSYDPLKMDEVYKVILPNFLANGGDGFQMIKDELLRHDSGDQDINVVSTYISKMKVIYPAVEGRIKFSTGSHCHGSFSLIFLSLWAVIFVLYQ TTK0O6Y TT Clinical trial TTK0O6Y FM Phosphoric monoester hydrolase TTK0O6Y KE hsa00230:Purine metabolism; hsa00240:Pyrimidine metabolism; hsa00760:Nicotinate and nicotinamide metabolism; hsa01100:Metabolic pathways TTK0O6Y RC R-HSA-74259:Purine catabolism TTI4ZX2 ID TTI4ZX2 TTI4ZX2 TN Ephrin type-B receptor 4 (EPHB4) TTI4ZX2 UP P54760 TTI4ZX2 UC EPHB4_HUMAN TTI4ZX2 BC Kinase TTI4ZX2 SN Tyrosine-protein kinase TYRO11; TYRO11; MYK1; Hepatoma transmembrane kinase; HTK TTI4ZX2 GN EPHB4 TTI4ZX2 FC Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 it is involved in the regulation of cell adhesion and migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. TTI4ZX2 EC EC 2.7.10.1 TTI4ZX2 PD 6FNM; 6FNL; 6FNK; 6FNJ; 6FNI TTI4ZX2 SQ MELRVLLCWASLAAALEETLLNTKLETADLKWVTFPQVDGQWEELSGLDEEQHSVRTYEVCDVQRAPGQAHWLRTGWVPRRGAVHVYATLRFTMLECLSLPRAGRSCKETFTVFYYESDADTATALTPAWMENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYLAFQDQGACMALLSLHLFYKKCAQLTVNLTRFPETVPRELVVPVAGSCVVDAVPAPGPSPSLYCREDGQWAEQPVTGCSCAPGFEAAEGNTKCRACAQGTFKPLSGEGSCQPCPANSHSNTIGSAVCQCRVGYFRARTDPRGAPCTTPPSAPRSVVSRLNGSSLHLEWSAPLESGGREDLTYALRCRECRPGGSCAPCGGDLTFDPGPRDLVEPWVVVRGLRPDFTYTFEVTALNGVSSLATGPVPFEPVNVTTDREVPPAVSDIRVTRSSPSSLSLAWAVPRAPSGAVLDYEVKYHEKGAEGPSSVRFLKTSENRAELRGLKRGASYLVQVRARSEAGYGPFGQEHHSQTQLDESEGWREQLALIAGTAVVGVVLVLVVIVVAVLCLRKQSNGREAEYSDKHGQYLIGHGTKVYIDPFTYEDPNEAVREFAKEIDVSYVKIEEVIGAGEFGEVCRGRLKAPGKKESCVAIKTLKGGYTERQRREFLSEASIMGQFEHPNIIRLEGVVTNSMPVMILTEFMENGALDSFLRLNDGQFTVIQLVGMLRGIASGMRYLAEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLEENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDAWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTSLHQLMLDCWQKDRNARPRFPQVVSALDKMIRNPASLKIVARENGGASHPLLDQRQPHYSAFGSVGEWLRAIKMGRYEESFAAAGFGSFELVSQISAEDLLRIGVTLAGHQKKILASVQHMKSQAKPGTPGGTGGPAPQY TTI4ZX2 TT Clinical trial TTI4ZX2 FM Kinase TTI4ZX2 KE hsa04360:Axon guidance TTI4ZX2 RC R-HSA-2682334:EPH-Ephrin signaling; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TTR5TV4 ID TTR5TV4 TTR5TV4 TN ERBB2 messenger RNA (HER2 mRNA) TTR5TV4 UP P04626 TTR5TV4 UC ERBB2_HUMAN TTR5TV4 BC mRNA target TTR5TV4 SN Tyrosine kinase-type cell surface receptor HER2 (mRNA); Tyrosine kinase receptor ErbB2 (mRNA); Receptor tyrosine-protein kinase erbB-2 (mRNA); Proto-oncogene c-ErbB-2 (mRNA); Proto-oncogene Neu (mRNA); P185erbB2 (mRNA); NGL (mRNA); NEU proto-oncogene (mRNA); NEU (mRNA); Metastatic lymph node gene 19 protein (mRNA); MLN19 (mRNA); MLN 19 (mRNA); HER2/neu (mRNA); HER2 (erbB2/neu) (mRNA); HER-2 (mRNA); Erb2 (mRNA); Epidermal growth factor receptor 2 (mRNA); CD340 (mRNA); C-erbB-2 oncoprotein (mRNA); C-erbB-2 (mRNA) TTR5TV4 GN ERBB2 TTR5TV4 FC Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. TTR5TV4 EC EC 2.7.10.1 TTR5TV4 PD 6OGE; 6J71; 6BGT; 6ATT; 5TQS TTR5TV4 SQ MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV TTR5TV4 TT Clinical trial TTR5TV4 FM mRNA target TTR5TV4 KE hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05215:Prostate cancer; hsa05219:Bladder cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer TTR5TV4 RC R-HSA-1250196:SHC1 events in ERBB2 signaling; R-HSA-1251932:PLCG1 events in ERBB2 signaling; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1963640:GRB2 events in ERBB2 signaling; R-HSA-1963642:PI3K events in ERBB2 signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-416572:Sema4D induced cell migration and growth-cone collapse; R-HSA-5673001:RAF/MAP kinase cascade TTTW2NY ID TTTW2NY TTTW2NY TN ERK activator kinase 2 (MEK2) TTTW2NY UP P36507 TTTW2NY UC MP2K2_HUMAN TTTW2NY BC Kinase TTTW2NY SN PRKMK2; MKK2; MEK 2; MAPKK 2; MAPK/ERK kinase 2; MAP kinase kinase 2; Dual specificity mitogenactivated protein kinase kinase 2; Dual specificity mitogen-activated protein kinase kinase 2 TTTW2NY GN MAP2K2 TTTW2NY FC Activates the ERK1 and ERK2 MAP kinases. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. TTTW2NY EC EC 2.7.12.2 TTTW2NY PD 4H3Q; 1S9I TTTW2NY SQ MLARRKPVLPALTINPTIAEGPSPTSEGASEANLVDLQKKLEELELDEQQKKRLEAFLTQKAKVGELKDDDFERISELGAGNGGVVTKVQHRPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMAPERLQGTHYSVQSDIWSMGLSLVELAVGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISPRPRPPGRPVSGHGMDSRPAMAIFELLDYIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERADLKMLTNHTFIKRSEVEEVDFAGWLCKTLRLNQPGTPTRTAV TTTW2NY TT Clinical trial TTTW2NY FM Kinase TTTW2NY KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04370:VEGF signaling pathway; hsa04540:Gap junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04620:Toll-like receptor signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05020:Prion diseases; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTTW2NY RC R-HSA-112411:MAPK1 (ERK2) activation; R-HSA-5210891:Uptake and function of anthrax toxins; R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5674499:Negative feedback regulation of MAPK pathway TTIWB6L ID TTIWB6L TTIWB6L TN Estradiol 17 beta-dehydrogenase 1 (17-beta-HSD1) TTIWB6L UP P14061 TTIWB6L UC DHB1_HUMAN TTIWB6L BC CH-OH donor oxidoreductase TTIWB6L SN Short chain dehydrogenase/reductase family 28C member 1; SDR28C1; Placental 17-beta-hydroxysteroid dehydrogenase; Estradiol 17-beta-dehydrogenase 1; EDHB17; EDH17B2; EDH17B1; E2DH; E17KSR; 20-alpha-HSD; 20 alpha-hydroxysteroid dehydrogenase; 17-beta-Hydroxysteroid dehydrogenase type 1; 17-beta-HSD 1 TTIWB6L GN HSD17B1 TTIWB6L FC Has 20-alpha-HSD activity. Uses preferentially NADH. Favors the reduction of estrogens and androgens. TTIWB6L EC EC 1.1.1.62 TTIWB6L PD 6MNE; 6MNC; 6DTP; 6CGE; 6CGC TTIWB6L SQ MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ TTIWB6L TT Clinical trial TTIWB6L FM Short-chain dehydrogenases reductases TTIWB6L KE hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways; hsa04913:Ovarian steroidogenesis TTIWB6L RC R-HSA-2453902:The canonical retinoid cycle in rods (twilight vision) TT4TQBX ID TT4TQBX TT4TQBX TN Extracellular signal-regulated kinase 2 (ERK2) TT4TQBX UP P28482 TT4TQBX UC MK01_HUMAN TT4TQBX BC Kinase TT4TQBX SN PRKM2; PRKM1; P42-MAPK; P42 Mitogen-activated protein kinase; Mitogen-activated protein kinase 2; Mitogen-activated protein kinase 1; MAPK 2; MAPK 1; MAP kinase isoform p42; MAP kinase 2; MAP kinase 1; ERT1; ERK-2 TT4TQBX GN MAPK1 TT4TQBX FC MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation. Phosphorylates CDK2AP2. Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. TT4TQBX EC EC 2.7.11.24 TT4TQBX PD 6QAW; 6QAQ; 6QAL; 6QAG; 6Q7K TT4TQBX SQ MAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS TT4TQBX TT Clinical trial TT4TQBX FM Kinase TT4TQBX KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04114:Oocyte meiosis; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04320:Dorso-ventral axis formation; hsa04350:TGF-beta signaling pathway; hsa04360:Axon guidance; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04540:Gap junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04930:Type II diabetes mellitus; hsa04960:Aldosterone-regulated sodium reabsorption; hsa05010:Alzheimer's disease; hsa05020:Prion diseases; hsa05034:Alcoholism; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TT4TQBX RC R-HSA-112409:RAF-independent MAPK1/3 activation; R-HSA-112411:MAPK1 (ERK2) activation; R-HSA-162658:Golgi Cisternae Pericentriolar Stack Reorganization; R-HSA-198753:ERK/MAPK targets; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-2559585:Oncogene Induced Senescence; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-3371453:Regulation of HSF1-mediated heat shock response; R-HSA-375165:NCAM signaling for neurite out-growth; R-HSA-437239:Recycling pathway of L1; R-HSA-442742:CREB phosphorylation through the activation of Ras; R-HSA-450341:Activation of the AP-1 family of transcription factors; R-HSA-456926:Thrombin signalling through proteinase activated receptors (PARs); R-HSA-5654726:Negative regulation of FGFR1 signaling; R-HSA-5654727:Negative regulation of FGFR2 signaling; R-HSA-5654732:Negative regulation of FGFR3 signaling; R-HSA-5654733:Negative regulation of FGFR4 signaling; R-HSA-5663213:RHO GTPases Activate WASPs and WAVEs; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5674499:Negative feedback regulation of MAPK pathway; R-HSA-5675221:Negative regulation of MAPK pathway; R-HSA-74749:Signal attenuation; R-HSA-879415:Advanced glycosylation endproduct receptor signaling; R-HSA-881907:Gastrin-CREB signalling pathway via PKC and MAPK; R-HSA-982772:Growth hormone receptor signaling TTDLNGZ ID TTDLNGZ TTDLNGZ TN Glucokinase (GCK) TTDLNGZ UP P35557 TTDLNGZ UC HXK4_HUMAN TTDLNGZ BC Kinase TTDLNGZ SN Hexokinase type IV; Hexokinase D; HK4; HK IV TTDLNGZ GN GCK TTDLNGZ FC Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting asan insulin-sensitive determinant of hepatic glucose usage. TTDLNGZ EC EC 2.7.1.2 TTDLNGZ PD 5V4X; 5V4W; 4RCH; 4NO7; 4MLH TTDLNGZ SQ MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ TTDLNGZ TT Clinical trial TTDLNGZ KE hsa00010:Glycolysis / Gluconeogenesis; hsa00052:Galactose metabolism; hsa00500:Starch and sucrose metabolism; hsa00520:Amino sugar and nucleotide sugar metabolism; hsa00524:Butirosin and neomycin biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa04910:Insulin signaling pathway; hsa04911:Insulin secretion; hsa04917:Prolactin signaling pathway; hsa04922:Glucagon signaling pathway; hsa04930:Type II diabetes mellitus; hsa04950:Maturity onset diabetes of the young; hsa05230:Central carbon metabolism in cancer TTDLNGZ RC R-HSA-210745:Regulation of gene expression in beta cells; R-HSA-70153:Glucose transport; R-HSA-70171:Glycolysis TTO8QRU ID TTO8QRU TTO8QRU TN Group IIA phospholipase A2 (GIIA sPLA2) TTO8QRU UP P14555 TTO8QRU UC PA2GA_HUMAN TTO8QRU BC Carboxylic ester hydrolase TTO8QRU SN RASF-A; Phospholipase A2, membrane associated; Phosphatidylcholine 2-acylhydrolase 2A; PLA2L; PLA2B; Non-pancreatic secretory phospholipase A2; NPS-PLA2; GIIC sPLA2 TTO8QRU GN PLA2G2A TTO8QRU FC Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Thought to participate in the regulation of phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Independent of its catalytic activity, acts as a ligand for integrins. Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1. Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1. Induces cell proliferation in an integrin-dependent manner. TTO8QRU EC EC 3.1.1.4 TTO8QRU PD 5G3N; 3U8I; 3U8H; 3U8D; 3U8B TTO8QRU SQ MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFARNKTTYNKKYQYYSNKHCRGSTPRC TTO8QRU TT Clinical trial TTO8QRU FM Carboxylic ester hydrolase TTO8QRU KE hsa00564:Glycerophospholipid metabolism; hsa00565:Ether lipid metabolism; hsa00590:Arachidonic acid metabolism; hsa00591:Linoleic acid metabolism; hsa00592:alpha-Linolenic acid metabolism; hsa01100:Metabolic pathways; hsa04014:Ras signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04972:Pancreatic secretion; hsa04975:Fat digestion and absorption TTO8QRU RC R-HSA-1482788:Acyl chain remodelling of PC; R-HSA-1482839:Acyl chain remodelling of PE; R-HSA-1482922:Acyl chain remodelling of PI TTV9GOF ID TTV9GOF TTV9GOF TN Histidine decarboxylase (HDC) TTV9GOF UP P19113 TTV9GOF UC DCHS_HUMAN TTV9GOF BC Carbon-carbon lyase TTV9GOF SN Human histidine decarboxylase TTV9GOF GN HDC TTV9GOF FC Catalyzes the biosynthesis of histamine from histidine. TTV9GOF EC EC 4.1.1.22 TTV9GOF PD 4E1O TTV9GOF SQ MMEPEEYRERGREMVDYICQYLSTVRERRVTPDVQPGYLRAQLPESAPEDPDSWDSIFGDIERIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNVMDWLAKMLGLPEHFLHHHPSSQGGGVLQSTVSESTLIALLAARKNKILEMKTSEPDADESCLNARLVAYASDQAHSSVEKAGLISLVKMKFLPVDDNFSLRGEALQKAIEEDKQRGLVPVFVCATLGTTGVCAFDCLSELGPICAREGLWLHIDAAYAGTAFLCPEFRGFLKGIEYADSFTFNPSKWMMVHFDCTGFWVKDKYKLQQTFSVNPIYLRHANSGVATDFMHWQIPLSRRFRSVKLWFVIRSFGVKNLQAHVRHGTEMAKYFESLVRNDPSFEIPAKRHLGLVVFRLKGPNCLTENVLKEIAKAGRLFLIPATIQDKLIIRFTVTSQFTTRDDILRDWNLIRDAATLILSQHCTSQPSPRVGNLISQIRGARAWACGTSLQSVSGAGDDPVQARKIIKQPQRVGAGPMKRENGLHLETLLDPVDDCFSEEAPDATKHKLSSFLFSYLSVQTKKKTVRSLSCNSVPVSAQKPLPTEASVKNGGSSRVRIFSRFPEDMMMLKKSAFKKLIKFYSVPSFPECSSQCGLQLPCCPLQAMV TTV9GOF TT Clinical trial TTV9GOF FM Carbon-carbon lyase TTV9GOF KE hsa00340:Histidine metabolism; hsa01100:Metabolic pathways TTTQGH8 ID TTTQGH8 TTTQGH8 TN Histone deacetylase 4 (HDAC4) TTTQGH8 UP P56524 TTTQGH8 UC HDAC4_HUMAN TTTQGH8 BC Carbon-nitrogen hydrolase TTTQGH8 SN KIAA0288; HD4 TTTQGH8 GN HDAC4 TTTQGH8 FC Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). TTTQGH8 EC EC 3.5.1.98 TTTQGH8 PD 6FYZ; 5ZOP; 5ZOO; 5A2S; 4CBY TTTQGH8 SQ MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL TTTQGH8 TT Clinical trial TTTQGH8 FM Carbon nitrogen hydrolase TTTQGH8 KE hsa05034:Alcoholism; hsa05169:Epstein-Barr virus infection; hsa05203:Viral carcinogenesis; hsa05206:MicroRNAs in cancer TTTQGH8 RC R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants TTJ3E9X ID TTJ3E9X TTJ3E9X TN Inhibitor of nuclear factor kappa-B kinase beta (IKKB) TTJ3E9X UP O14920 TTJ3E9X UC IKKB_HUMAN TTJ3E9X BC Kinase TTJ3E9X SN Nuclear factor NF-kappa-B inhibitor kinase beta; NFKBIKB; Inhibitor of nuclear factor kappa-B kinase subunit beta; IkBKB; IKKB; IKK2; IKK-beta; IKK-B; I-kappa-B-kinase beta; I-kappa-B kinase 2 TTJ3E9X GN IKBKB TTJ3E9X FC Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation. Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation. TTJ3E9X EC EC 2.7.11.10 TTJ3E9X PD 4KIK; 4E3C; 3BRV; 3BRT TTJ3E9X SQ MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMRRLTHPNVVAARDVPEGMQNLAPNDLPLLAMEYCQGGDLRKYLNQFENCCGLREGAILTLLSDIASALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHSKVRQKSEVDIVVSEDLNGTVKFSSSLPYPNNLNSVLAERLEKWLQLMLMWHPRQRGTDPTYGPNGCFKALDDILNLKLVHILNMVTGTIHTYPVTEDESLQSLKARIQQDTGIPEEDQELLQEAGLALIPDKPATQCISDGKLNEGHTLDMDLVFLFDNSKITYETQISPRPQPESVSCILQEPKRNLAFFQLRKVWGQVWHSIQTLKEDCNRLQQGQRAAMMNLLRNNSCLSKMKNSMASMSQQLKAKLDFFKTSIQIDLEKYSEQTEFGITSDKLLLAWREMEQAVELCGRENEVKLLVERMMALQTDIVDLQRSPMGRKQGGTLDDLEEQARELYRRLREKPRDQRTEGDSQEMVRLLLQAIQSFEKKVRVIYTQLSKTVVCKQKALELLPKVEEVVSLMNEDEKTVVRLQEKRQKELWNLLKIACSKVRGPVSGSPDSMNASRLSQPGQLMSQPSTASNSLPEPAKKSEELVAEAHNLCTLLENAIQDTVREQDQSFTALDWSWLQTEEEEHSCLEQAS TTJ3E9X TT Clinical trial TTJ3E9X FM Kinase TTJ3E9X KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04062:Chemokine signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04068:FoxO signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04910:Insulin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05215:Prostate cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer TTJ3E9X RC R-HSA-1169091:Activation of NF-kappaB in B cells; R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-1810476:RIP-mediated NFkB activation via ZBP1; R-HSA-209543:p75NTR recruits signalling complexes; R-HSA-209560:NF-kB is activated and signals survival; R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-446652:Interleukin-1 signaling; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5602636:IKBKB deficiency causes SCID; R-HSA-5603027:IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR); R-HSA-5603029:IkBA variant leads to EDA-ID; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-5684264:MAP3K8 (TPL2)-dependent MAPK1/3 activation; R-HSA-933542:TRAF6 mediated NF-kB activation; R-HSA-933543:NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10; R-HSA-937039:IRAK1 recruits IKK complex; R-HSA-937041:IKK complex recruitment mediated by RIP1; R-HSA-975144:IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation TTUS45N ID TTUS45N TTUS45N TN Leukocyte common antigen (PTPRC) TTUS45N UP P08575 TTUS45N UC PTPRC_HUMAN TTUS45N BC Phosphoric monoester hydrolase TTUS45N SN T200; Receptor-type tyrosine-protein phosphatase C; L-CA; CD45 antigen; CD45 TTUS45N GN PTPRC TTUS45N FC Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity. Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. TTUS45N EC EC 3.1.3.48 TTUS45N PD 5FN7; 5FN6; 5FMV; 1YGU; 1YGR TTUS45N SQ MTMYLWLKLLAFGFAFLDTEVFVTGQSPTPSPTGLTTAKMPSVPLSSDPLPTHTTAFSPASTFERENDFSETTTSLSPDNTSTQVSPDSLDNASAFNTTGVSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDPVSPLTTTLSLAHHSSAALPARTSNTTITANTSDAYLNASETTTLSPSGSAVISTTTIATTPSKPTCDEKYANITVDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTLILDVPPGVEKFQLHDCTQVEKADTTICLKWKNIETFTCDTQNITYRFQCGNMIFDNKEIKLENLEPEHEYKCDSEILYNNHKFTNASKIIKTDFGSPGEPQIIFCRSEAAHQGVITWNPPQRSFHNFTLCYIKETEKDCLNLDKNLIKYDLQNLKPYTKYVLSLHAYIIAKVQRNGSAAMCHFTTKSAPPSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGNTLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGDYPGEPFILHHSTSYNSKALIAFLAFLIIVTSIALLVVLYKIYDLHKKRSCNLDEQQELVERDDEKQLMNVEPIHADILLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEYNQFGETEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEMSKESEHDSDESSDDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTYPAQNGQVKKNNHQEDKIEFDNEVDKVKQDANCVNPLGAPEKLPEAKEQAEGSEPTSGTEGPEHSVNGPASPALNQGS TTUS45N TT Clinical trial TTUS45N FM Phosphoric monoester hydrolases TTUS45N KE hsa04514:Cell adhesion molecules (CAMs); hsa04660:T cell receptor signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa05340:Primary immunodeficiency TTUS45N RC R-HSA-202427:Phosphorylation of CD3 and TCR zeta chains; R-HSA-416700:Other semaphorin interactions TTLPC70 ID TTLPC70 TTLPC70 TN Lysosomal alpha-glucosidase (GAA) TTLPC70 UP P10253 TTLPC70 UC LYAG_HUMAN TTLPC70 BC Glycosylase TTLPC70 SN GAA; Aglucosidase alfa; Acid maltase TTLPC70 GN GAA TTLPC70 FC Essential for the degradation of glygogen to glucose in lysosomes. TTLPC70 EC EC 3.2.1.20 TTLPC70 PD 5NN8; 5NN6; 5NN5; 5NN4; 5NN3 TTLPC70 SQ MGVRHPPCSHRLLAVCALVSLATAALLGHILLHDFLLVPRELSGSSPVLEETHPAHQQGASRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLFFADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPVEALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQPMALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQLQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC TTLPC70 TT Clinical trial TTLPC70 KE hsa00052:Galactose metabolism; hsa00500:Starch and sucrose metabolism; hsa01100:Metabolic pathways; hsa04142:Lysosome TTXZ0KQ ID TTXZ0KQ TTXZ0KQ TN Matrix metalloproteinase-12 (MMP-12) TTXZ0KQ UP P39900 TTXZ0KQ UC MMP12_HUMAN TTXZ0KQ BC Peptidase TTXZ0KQ SN Macrophage metalloelastase; Macrophage elastase; MME; ME; HME TTXZ0KQ GN MMP12 TTXZ0KQ FC Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3. May be involved in tissue injury and remodeling. TTXZ0KQ EC EC 3.4.24.65 TTXZ0KQ PD 6EOX; 6ENM; 6ELA; 6EKN; 5N5K TTXZ0KQ SQ MKFLLILLLQATASGALPLNSSTSLEKNNVLFGERYLEKFYGLEINKLPVTKMKYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMMHAPRCGVPDVHHFREMPGGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNLRPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNKYYYFFQGSNQFEYDFLLQRITKTLKSNSWFGC TTXZ0KQ TT Clinical trial TTXZ0KQ FM Peptidase TTXZ0KQ RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix TTJ4QE7 ID TTJ4QE7 TTJ4QE7 TN Matrix metalloproteinase-14 (MMP-14) TTJ4QE7 UP P50281 TTJ4QE7 UC MMP14_HUMAN TTJ4QE7 BC Peptidase TTJ4QE7 SN Membrane-type-1 matrix metalloproteinase; Membrane-type matrix metalloproteinase 1; MTMMP1; MT1MMP; MT1-MMP; MT-MMP 1; MMP-X1 TTJ4QE7 GN MMP14 TTJ4QE7 FC Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis. Endopeptidase that degrades various components of the extracellular matrix such as collagen. TTJ4QE7 EC EC 3.4.24.80 TTJ4QE7 PD 6CM1; 6CLZ; 5H0U; 4QXU; 4P3D TTJ4QE7 SQ MSPAPRPPRCLLLPLLTLGTALASLGSAQSSSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTTSRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGGGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPRRLLYCQRSLLDKV TTJ4QE7 TT Clinical trial TTJ4QE7 FM Peptidase TTJ4QE7 KE hsa04668:TNF signaling pathway; hsa04912:GnRH signaling pathway TTJ4QE7 RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases TT3DCYJ ID TT3DCYJ TT3DCYJ TN Microtubule affinity regulating kinase 3 (MARK3) TT3DCYJ UP P27448 TT3DCYJ UC MARK3_HUMAN TT3DCYJ BC Kinase TT3DCYJ SN cTAK1; Serine/threonine-protein kinase p78; Ser/Thr protein kinase PAR-1; Protein kinase STK10); Protein kinase STK10; Par-1a; MAP/microtubule affinity-regulating kinase 3; EMK2; EMK-2; ELKL motif kinase 2; Cdc25C-associated protein kinase 1; C-TAK1 TT3DCYJ GN MARK3 TT3DCYJ FC Involved in the specific phosphorylation of microtubule-associated proteins for MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU. Phosphorylates CDC25C on 'Ser-216'. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Negatively regulates the Hippo signaling pathway and antagonizes the phosphorylation of LATS1. Cooperates with DLG5 to inhibit the kinase activity of STK3/MST2 toward LATS1. Serine/threonine-protein kinase. TT3DCYJ EC EC 2.7.11.1 TT3DCYJ PD 3FE3; 2QNJ TT3DCYJ SQ MSTRTPLPTVNERDTENHTSHGDGRQEVTSRTSRSGARCRNSIASCADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLIMEYASGGEVFDYLVAHGRMKEKEARSKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGGKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKRFLVLNPIKRGTLEQIMKDRWINAGHEEDELKPFVEPELDISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLGRKSSELDASDSSSSSNLSLAKVRPSSDLNNSTGQSPHHKVQRSVSSSQKQRRYSDHAGPAIPSVVAYPKRSQTSTADSDLKEDGISSRKSSGSAVGGKGIAPASPMLGNASNPNKADIPERKKSSTVPSSNTASGGMTRRNTYVCSERTTADRHSVIQNGKENSTIPDQRTPVASTHSISSAATPDRIRFPRGTASRSTFHGQPRERRTATYNGPPASPSLSHEATPLSQTRSRGSTNLFSKLTSKLTRRNMSFRFIKRLPTEYERNGRYEGSSRNVSAEQKDENKEAKPRSLRFTWSMKTTSSMDPGDMMREIRKVLDANNCDYEQRERFLLFCVHGDGHAENLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL TT3DCYJ TT Clinical trial TT3DCYJ FM Kinase TT3DCYJ RC R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5675221:Negative regulation of MAPK pathway TTUNSIX ID TTUNSIX TTUNSIX TN Mixed lineage kinase 1 (MAP3K9) TTUNSIX UP P80192 TTUNSIX UC M3K9_HUMAN TTUNSIX BC Kinase TTUNSIX SN PRKE1; Mitogen-activated protein kinase kinase kinase 9; MLK1 TTUNSIX GN MAP3K9 TTUNSIX FC Plays an important role in the cascades of cellular responses evoked by changes in the environment. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade through the phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7 which in turn activate the JNKs. The MKK/JNK signaling pathway regulates stress response via activator protein-1 (JUN) and GATA4 transcription factors. Plays also a role in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. TTUNSIX EC EC 2.7.11.25 TTUNSIX PD 4UY9; 3DTC TTUNSIX SQ MEPSRALLGCLASAAAAAPPGEDGAGAGAEEEEEEEEEAAAAVGPGELGCDAPLPYWTAVFEYEAAGEDELTLRLGDVVEVLSKDSQVSGDEGWWTGQLNQRVGIFPSNYVTPRSAFSSRCQPGGEDPSCYPPIQLLEIDFAELTLEEIIGIGGFGKVYRAFWIGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHDEAIVPIIHRDLKSSNILILQKVENGDLSNKILKITDFGLAREWHRTTKMSAAGTYAWMAPEVIRASMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLALPIPSTCPEPFAKLMEDCWNPDPHSRPSFTNILDQLTTIEESGFFEMPKDSFHCLQDNWKHEIQEMFDQLRAKEKELRTWEEELTRAALQQKNQEELLRRREQELAEREIDILERELNIIIHQLCQEKPRVKKRKGKFRKSRLKLKDGNRISLPSDFQHKFTVQASPTMDKRKSLINSRSSPPASPTIIPRLRAIQLTPGESSKTWGRSSVVPKEEGEEEEKRAPKKKGRTWGPGTLGQKELASGDEGSPQRREKANGLSTPSESPHFHLGLKSLVDGYKQWSSSAPNLVKGPRSSPALPGFTSLMEMEDEDSEGPGSGESRLQHSPSQSYLCIPFPRGEDGDGPSSDGIHEEPTPVNSATSTPQLTPTNSLKRGGAHHRRCEVALLGCGAVLAATGLGFDLLEAGKCQLLPLEEPEPPAREEKKRREGLFQRSSRPRRSTSPPSRKLFKKEEPMLLLGDPSASLTLLSLSSISECNSTRSLLRSDSDEIVVYEMPVSPVEAPPLSPCTHNPLVNVRVERFKRDPNQSLTPTHVTLTTPSQPSSHRRTPSDGALKPETLLASRSPSSNGLSPSPGAGMLKTPSPSRDPGEFPRLPDPNVVFPPTPRRWNTQQDSTLERPKTLEFLPRPRPSANRQRLDPWWFVSPSHARSTSPANSSSTETPSNLDSCFASSSSTVEERPGLPALLPFQAGPLPPTERTLLDLDAEGQSQDSTVPLCRAELNTHRPAPYEIQQEFWS TTUNSIX TT Clinical trial TTUNSIX FM Kinase TTVCZPI ID TTVCZPI TTVCZPI TN Myeloperoxidase (MPO) TTVCZPI UP P05164 TTVCZPI UC PERM_HUMAN TTVCZPI BC Peroxidases TTVCZPI SN MPO TTVCZPI GN MPO TTVCZPI FC Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acidin physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity. TTVCZPI EC EC 1.11.2.2 TTVCZPI PD 6BMT; 6AZP; 5UZU; 5MFA; 5FIW TTVCZPI SQ MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTSLVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLHVALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFVNCSTLPALNLASWREAS TTVCZPI TT Clinical trial TTVCZPI KE hsa04145:Phagosome; hsa05202:Transcriptional misregulation in cancer TTUF2HO ID TTUF2HO TTUF2HO TN NAD-dependent deacetylase sirtuin-1 (SIRT1) TTUF2HO UP Q96EB6 TTUF2HO UC SIR1_HUMAN TTUF2HO BC Carbon-nitrogen hydrolase TTUF2HO SN hSIRT1; hSIR2; SIR2L1; SIR2-like protein 1; Regulatory protein SIR2 homolog 1; NAD-dependent protein deacetylase sirtuin-1 TTUF2HO GN SIRT1 TTUF2HO FC Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of HIST1H1E. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A-mediated transcription. Required for the repression of ESRRG by CREBZF. Deacetylates NR1H3 and NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteosomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates p300/EP300 and PRMT1. Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation. Involved in liver and muscle metabolism. Through deacteylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletel muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and faciliting recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacteylates MECOM/EVI1. Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, repress selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including ARNTL/BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates ARNTL/BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteosome. Protects cardiomyocytes against palmitate-induced apoptosis. Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity. Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis. Involved in the CCAR2-mediated regulation of PCK1 and NR1D1. Deacetylates CTNB1 at 'Lys-49'. In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling. NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metobolism, apoptosis and autophagy. TTUF2HO EC EC 3.5.1.- TTUF2HO PD 5BTR; 4ZZJ; 4ZZI; 4ZZH; 4KXQ TTUF2HO SQ MADEAALALQPGGSPSAAGADREAASSPAGEPLRKRPRRDGPGLERSPGEPGGAAPEREVPAAARGCPGAAAAALWREAEAEAAAAGGEQEAQATAAAGEGDNGPGLQGPSREPPLADNLYDEDDDDEGEEEEEAAAAAIGYRDNLLFGDEIITNGFHSCESDEEDRASHASSSDWTPRPRIGPYTFVQQHLMIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDINTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRIIQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRTQKELAYLSELPPTPLHVSEDSSSPERTSPPDSSVIVTLLDQAAKSNDDLDVSESKGCMEEKPQEVQTSRNVESIAEQMENPDLKNVGSSTGEKNERTSVAGTVRKCWPNRVAKEQISRRLDGNQYLFLPPNRYIFHGAEVYSDSEDDVLSSSSCGSNSDSGTCQSPSLEEPMEDESEIEEFYNGLEDEPDVPERAGGAGFGTDGDDQEAINEAISVKQEVTDMNYPSNKS TTUF2HO TT Clinical trial TTUF2HO FM Carbon nitrogen hydrolase TTUF2HO KE hsa04068:FoxO signaling pathway; hsa04152:AMPK signaling pathway; hsa04922:Glucagon signaling pathway; hsa05031:Amphetamine addiction; hsa05206:MicroRNAs in cancer TTUF2HO RC R-HSA-1368082:RORA activates gene expression; R-HSA-3371453:Regulation of HSF1-mediated heat shock response; R-HSA-400253:Circadian Clock TTPLTSQ ID TTPLTSQ TTPLTSQ TN Neutrophil elastase (NE) TTPLTSQ UP P08246 TTPLTSQ UC ELNE_HUMAN TTPLTSQ BC Peptidase TTPLTSQ SN PMN elastase; Medullasin; Human leukocyte elastase; HLE; Elastase-2; ELA2; Bone marrow serine protease TTPLTSQ GN ELANE TTPLTSQ FC Inhibits C5a-dependent neutrophil enzyme release and chemotaxis. Modifies the functions of natural killer cells, monocytes and granulocytes. TTPLTSQ EC EC 3.4.21.37 TTPLTSQ PD 6F5M; 5ABW; 5A8Z; 5A8Y; 5A8X TTPLTSQ SQ MTLGRRLACLFLACVLPALLLGGTALASEIVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQRSEDNPCPHPRDPDPASRTH TTPLTSQ TT Clinical trial TTPLTSQ FM Peptidase TTPLTSQ KE hsa05202:Transcriptional misregulation in cancer; hsa05322:Systemic lupus erythematosus TTPLTSQ RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases TTZUFI5 ID TTZUFI5 TTZUFI5 TN Nitric-oxide synthase brain (NOS1) TTZUFI5 UP P29475 TTZUFI5 UC NOS1_HUMAN TTZUFI5 BC Paired donor oxygen oxidoreductase TTZUFI5 SN Peptidyl-cysteine S-nitrosylase NOS1; Nitric oxide synthase, brain; Neuronal NOS; NOS, type I; NOS type I; NNOS; NC-NOS; N-NOS; BNOS TTZUFI5 GN NOS1 TTZUFI5 FC In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. TTZUFI5 EC EC 1.14.13.39 TTZUFI5 PD 6NHC; 6NHB; 6NGI; 6NGH; 6NGF TTZUFI5 SQ MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTIRVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAPRPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQVDRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPSKCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCEIFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQEERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGVISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREPDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS TTZUFI5 TT Clinical trial TTZUFI5 FM Paired donor oxidoreductase TTZUFI5 KE hsa00330:Arginine and proline metabolism; hsa01100:Metabolic pathways; hsa04020:Calcium signaling pathway; hsa04145:Phagosome; hsa04713:Circadian entrainment; hsa04730:Long-term depression; hsa04970:Salivary secretion; hsa05010:Alzheimer's disease; hsa05014:Amyotrophic lateral sclerosis (ALS) TTZUFI5 RC R-HSA-1222556:ROS production in response to bacteria; R-HSA-392154:Nitric oxide stimulates guanylate cyclase TTCM4B3 ID TTCM4B3 TTCM4B3 TN Nitric-oxide synthase endothelial (NOS3) TTCM4B3 UP P29474 TTCM4B3 UC NOS3_HUMAN TTCM4B3 BC Paired donor oxygen oxidoreductase TTCM4B3 SN Nitric oxide synthase, endothelial; NOSIII; NOS,type III; NOS type III; Endothelial nitric oxide synthase; Endothelial NOS; ENOS; EC-NOS; Constitutive NOS; CNOS TTCM4B3 GN NOS3 TTCM4B3 FC NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets. Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. TTCM4B3 EC EC 1.14.13.39 TTCM4B3 PD 6CIF; 6CIE; 6AV7; 6AV6; 5XOF TTCM4B3 SQ MGNLKSVAQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPASLLPPAPEHSPPSSPLTQPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPAPEQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDDPPELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPWKGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSSPRPEQHKSYKIRFNSISCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAARDIFSPKRSWKRQRYRLSAQAEGLQLLPGLIHVHRRKMFQATIRSVENLQSSKSTRATILVRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPAPTEPVAVEQLEKGSPGGPPPGWVRDPRLPPCTLRQALTFFLDITSPPSPQLLRLLSTLAEEPREQQELEALSQDPRRYEEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSTHPGEIHLTVAVLAYRTQDGLGPLHYGVCSTWLSQLKPGDPVPCFIRGAPSFRLPPDPSLPCILVGPGTGIAPFRGFWQERLHDIESKGLQPTPMTLVFGCRCSQLDHLYRDEVQNAQQRGVFGRVLTAFSREPDNPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATNVLQTVQRILATEGDMELDEAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWAFDPPGSDTNSP TTCM4B3 TT Clinical trial TTCM4B3 FM Oxidoreductases acting on paired donors TTCM4B3 KE hsa00330:Arginine and proline metabolism; hsa01100:Metabolic pathways; hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04370:VEGF signaling pathway; hsa04611:Platelet activation; hsa04915:Estrogen signaling pathway; hsa04921:Oxytocin signaling pathway TTCM4B3 RC R-HSA-1222556:ROS production in response to bacteria; R-HSA-1474151:Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation; R-HSA-203615:eNOS activation; R-HSA-392154:Nitric oxide stimulates guanylate cyclase; R-HSA-5218920:VEGFR2 mediated vascular permeability TTF10I9 ID TTF10I9 TTF10I9 TN Nitric-oxide synthase inducible (NOS2) TTF10I9 UP P35228 TTF10I9 UC NOS2_HUMAN TTF10I9 BC Paired donor oxygen oxidoreductase TTF10I9 SN iNOS; Peptidyl-cysteine S-nitrosylase NOS2; Nitric oxide synthase, inducible; NOS2A; NOS type II; Inducible NOS; Inducible NO synthase; Hepatocyte NOS; HEP-NOS TTF10I9 GN NOS2 TTF10I9 FC Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (By similarity). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH on 'Cys-247' implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of proinflammatory mediators such as IL6 and IL8. TTF10I9 EC EC 1.14.13.39 TTF10I9 PD 5XN3; 5TP6; 4NOS; 4CX7; 3HR4 TTF10I9 SQ MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPLVETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVTILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGDELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDLSKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQPALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCFVRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDRVAVQPSSLEMSAL TTF10I9 TT Clinical trial TTF10I9 FM Paired donor oxidoreductase TTF10I9 KE hsa00220:Arginine biosynthesis; hsa00330:Arginine and proline metabolism; hsa01100:Metabolic pathways; hsa04020:Calcium signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04146:Peroxisome; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05200:Pathways in cancer; hsa05222:Small cell lung cancer TTF10I9 RC R-HSA-1222556:ROS production in response to bacteria; R-HSA-392154:Nitric oxide stimulates guanylate cyclase TTJ8DV7 ID TTJ8DV7 TTJ8DV7 TN O-6-methylguanine-DNA-alkyltransferase (MGMT) TTJ8DV7 UP P16455 TTJ8DV7 UC MGMT_HUMAN TTJ8DV7 BC Methyltransferase TTJ8DV7 SN Methylated-DNA--protein-cysteine methyltransferase; Human O(6)-alkylguanine-DNA alkyltransferase; 6-O-methylguanine-DNA methyltransferase TTJ8DV7 GN MGMT TTJ8DV7 FC Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. TTJ8DV7 EC EC 2.1.1.63 TTJ8DV7 PD 1YFH; 1T39; 1T38; 1QNT; 1EH8 TTJ8DV7 SQ MDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPAAVLGGPEPLMQCTAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLWKLLKVVKFGEVISYQQLAALAGNPKAARAVGGAMRGNPVPILIPCHRVVCSSGAVGNYSGGLAVKEWLLAHEGHRLGKPGLGGSSGLAGAWLKGAGATSGSPPAGRN TTJ8DV7 TT Clinical trial TTJ8DV7 FM Methyltransferase TTVIAT9 ID TTVIAT9 TTVIAT9 TN Phosphodiesterase 4B (PDE4B) TTVIAT9 UP Q07343 TTVIAT9 UC PDE4B_HUMAN TTVIAT9 BC Phosphoric diester hydrolase TTVIAT9 SN cAMP-specific 3',5'-cyclic phosphodiesterase 4B; Type 4B cAMP phosphodiesterase; Type 4 cyclic adenosine monophosphate phosphodiesterase (type 4 PDE); PDE32; DPDE4 TTVIAT9 GN PDE4B TTVIAT9 FC May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents. Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. TTVIAT9 EC EC 3.1.4.53 TTVIAT9 PD 6BOJ; 5OHJ; 5LAQ; 5K6J; 4X0F TTVIAT9 SQ MKKSRSVMTVMADDNVKDYFECSLSKSYSSSSNTLGIDLWRGRRCCSGNLQLPPLSQRQSERARTPEGDGISRPTTLPLTTLPSIAITTVSQECFDVENGPSPGRSPLDPQASSSAGLVLHATFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRSVRNNFTILTNLHGTSNKRSPAASQPPVSRVNPQEESYQKLAMETLEELDWCLDQLETIQTYRSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKKKQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSHNRPLTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDVAYHNSLHAADVAQSTHVLLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTSSGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSPSPPLDEQNRDCQGLMEKFQFELTLDEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLGETDIDIATEDKSPVDT TTVIAT9 TT Clinical trial TTVIAT9 FM Phosphoric diester hydrolase TTVIAT9 KE hsa00230:Purine metabolism; hsa04024:cAMP signaling pathway; hsa05032:Morphine addiction TTVIAT9 RC R-HSA-180024:DARPP-32 events; R-HSA-418555:G alpha (s) signalling events TTDNFMT ID TTDNFMT TTDNFMT TN Platelet-activating factor acetylhydrolase (PLA2G7) TTDNFMT UP Q13093 TTDNFMT UC PAFA_HUMAN TTDNFMT BC Carboxylic ester hydrolase TTDNFMT SN gVIIA-PLA2; PAFAH; PAF acetylhydrolase; PAF 2-acylhydrolase; Lipoprotein-associated phospholipase A2; LDL-associated phospholipase A2; LDL-PLA(2); Group-VIIA phospholipase A2; 2-acetyl-1-alkylglycerophosphocholine esterase; 1-alkyl-2-acetylglycerophosphocholine esterase TTDNFMT GN PLA2G7 TTDNFMT FC Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids. Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. TTDNFMT EC EC 3.1.1.47 TTDNFMT PD 5YEA; 5YE9; 5YE8; 5YE7; 5LZ9 TTDNFMT SQ MVPPKLHVLFCLCGCLAVVYPFDWQYINPVAHMKSSAWVNKIQVLMAAASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPSQDNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNILRLLFGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWLYLRTLKQEEETHIRNEQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLSEDQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFATGKIIGHMLKLKGDIDSNVAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENLIPGTNINTTNQHIMLQNSSGIEKYN TTDNFMT TT Clinical trial TTDNFMT FM Carboxylic ester hydrolase TTDNFMT KE hsa00565:Ether lipid metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics TTIYVQP ID TTIYVQP TTIYVQP TN Polo-like kinase 1 (PLK1) TTIYVQP UP P53350 TTIYVQP UC PLK1_HUMAN TTIYVQP BC Kinase TTIYVQP SN Serine/threonine-protein kinase PLK1; Serine/threonine-protein kinase 13; Serine-threonine protein kinase 13; STPK13; Plk1; PLK-1; PLK; Mitoticserine-threonine kinase polo-like kinase 1 TTIYVQP GN PLK1 TTIYVQP FC Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning. Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage. Phosphorylates CEP68 and is required for its degradation. Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope. Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock. Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression. Regulates mitotic progression by phosphorylating RIOK2. Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. TTIYVQP EC EC 2.7.11.21 TTIYVQP PD 6AX4; 5TA8; 5TA6; 5NN2; 5NN1 TTIYVQP SQ MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERPREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS TTIYVQP TT Clinical trial TTIYVQP FM Kinase TTIYVQP KE hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04114:Oocyte meiosis; hsa04914:Progesterone-mediated oocyte maturation TTIYVQP RC R-HSA-156711:Polo-like kinase mediated events; R-HSA-162658:Golgi Cisternae Pericentriolar Stack Reorganization; R-HSA-174178:APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1; R-HSA-176412:Phosphorylation of the APC/C; R-HSA-176417:Phosphorylation of Emi1; R-HSA-2299718:Condensation of Prophase Chromosomes; R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-2565942:Regulation of PLK1 Activity at G2/M Transition; R-HSA-2980767:Activation of NIMA Kinases NEK9, NEK6, NEK7; R-HSA-380259:Loss of Nlp from mitotic centrosomes; R-HSA-380270:Recruitment of mitotic centrosome proteins and complexes; R-HSA-380284:Loss of proteins required for interphase microtubule organization?from the centrosome; R-HSA-5620912:Anchoring of the basal body to the plasma membrane; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-68877:Mitotic Prometaphase; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition TTNGKET ID TTNGKET TTNGKET TN Prolyl endopeptidase (PREP) TTNGKET UP P48147 TTNGKET UC PPCE_HUMAN TTNGKET BC Peptidase TTNGKET SN Post-proline cleaving enzyme; PREP; PE TTNGKET GN PREP TTNGKET FC Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. TTNGKET EC EC 3.4.21.26 TTNGKET PD 3DDU TTNGKET SQ MLSLQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLSIREGCDPVNRLWYCDLQQESSGIAGILKWVKLIDNFEGEYDYVTNEGTVFTFKTNRQSPNYRVINIDFRDPEESKWKVLVPEHEKDVLEWIACVRSNFLVLCYLHDVKNILQLHDLTTGALLKTFPLDVGSIVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPRVFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGILAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYGCSDSKQHFEWLVKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNVDWIP TTNGKET TT Clinical trial TTNGKET KE hsa04614:Renin-angiotensin system TTYLQ8V ID TTYLQ8V TTYLQ8V TN Prostaglandin E synthase (PTGES) TTYLQ8V UP O14684 TTYLQ8V UC PTGES_HUMAN TTYLQ8V BC Intramolecular oxidoreductase TTYLQ8V SN p53-induced gene 12 protein; PIG12; PGES; PGE synthase; P53-induced apoptosis protein 12; Microsomal prostaglandin E synthase 1; Microsomal glutathione S-transferase 1-like 1; MPGES1; MPGES-1; MGST1L1; MGST1-L1 TTYLQ8V GN PTGES TTYLQ8V FC Catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). TTYLQ8V EC EC 5.3.99.3 TTYLQ8V PD 5TL9; 5T37; 5T36; 5K0I; 5BQI TTYLQ8V SQ MPAHSLVMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCRSDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVAWMHFLVFLVGRVAHTVAYLGKLRAPIRSVTYTLAQLPCASMALQILWEAARHL TTYLQ8V TT Clinical trial TTYLQ8V FM Intramolecular oxidoreductases TTYLQ8V KE hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways TT9WJ8U ID TT9WJ8U TT9WJ8U TN Protein kinase C delta (PRKCD) TT9WJ8U UP Q05655 TT9WJ8U UC KPCD_HUMAN TT9WJ8U BC Kinase TT9WJ8U SN nPKC-delta; Tyrosine-protein kinase PRKCD; SDK1; Protein kinase C delta type catalytic subunit; Protein kinase C delta type; PKC-delta TT9WJ8U GN PRKCD TT9WJ8U FC Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion. Phosphorylates ELAVL1 in response to angiotensin-2 treatment. Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. TT9WJ8U EC EC 2.7.11.13 TT9WJ8U PD 2YUU; 1YRK TT9WJ8U SQ MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED TT9WJ8U TT Clinical trial TT9WJ8U FM Kinase TT9WJ8U KE hsa04062:Chemokine signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04530:Tight junction; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04722:Neurotrophin signaling pathway; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa04930:Type II diabetes mellitus TT9WJ8U RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-111933:Calmodulin induced events; R-HSA-114508:Effects of PIP2 hydrolysis; R-HSA-1489509:DAG and IP3 signaling; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-418597:G alpha (z) signalling events; R-HSA-450520:HuR (ELAVL1) binds and stabilizes mRNA; R-HSA-5218921:VEGFR2 mediated cell proliferation; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-877300:Interferon gamma signaling TT8QL1J ID TT8QL1J TT8QL1J TN Protein kinase C theta (PRKCQ) TT8QL1J UP Q04759 TT8QL1J UC KPCT_HUMAN TT8QL1J BC Kinase TT8QL1J SN Protein kinase C theta type; PRKCT; NPKC-theta TT8QL1J GN PRKCQ TT8QL1J FC In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates in the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1. Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. TT8QL1J EC EC 2.7.11.13 TT8QL1J PD 5F9E; 4RA5; 4Q9Z; 2JED; 2ENZ TT8QL1J SQ MSPFLRIGLSNFDCGSCQSCQGEAVNPYCAVLVKEYVESENGQMYIQKKPTMYPPWDSTFDAHINKGRVMQIIVKGKNVDLISETTVELYSLAERCRKNNGKTEIWLELKPQGRMLMNARYFLEMSDTKDMNEFETEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFVWGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYKSPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARCLRDTEQIFREGPVEIGLPCSIKNEARPPCLPTPGKREPQGISWESPLDEVDKMCHLPEPELNKERPSLQIKLKIEDFILHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSRATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTNTFCGTPDYIAPEILLGQKYNHSVDWWSFGVLLYEMLIGQSPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFDCSNFDKEFLNEKPRLSFADRALINSMDQNMFRNFSFMNPGMERLIS TT8QL1J TT Clinical trial TT8QL1J FM Kinase TT8QL1J KE hsa04064:NF-kappa B signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04530:Tight junction; hsa04660:T cell receptor signaling pathway; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04920:Adipocytokine signaling pathway; hsa05162:Measles TT8QL1J RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-114508:Effects of PIP2 hydrolysis; R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade; R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-418597:G alpha (z) signalling events TTMCF1Y ID TTMCF1Y TTMCF1Y TN Purine nucleoside phosphorylase (PNP) TTMCF1Y UP P00491 TTMCF1Y UC PNPH_HUMAN TTMCF1Y BC Pentosyltransferase TTMCF1Y SN PNP; Inosine phosphorylase TTMCF1Y GN PNP TTMCF1Y FC The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. TTMCF1Y EC EC 2.4.2.1 TTMCF1Y PD 5UGF; 5ETJ; 4GKA; 4ECE; 4EB8 TTMCF1Y SQ MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQMGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS TTMCF1Y TT Clinical trial TTMCF1Y KE hsa00230:Purine metabolism; hsa00240:Pyrimidine metabolism; hsa00760:Nicotinate and nicotinamide metabolism; hsa01100:Metabolic pathways TTMCF1Y RC R-HSA-74217:Purine salvage; R-HSA-74259:Purine catabolism TT8XK6L ID TT8XK6L TT8XK6L TN Quinone reductase 1 (NQO1) TT8XK6L UP P15559 TT8XK6L UC NQO1_HUMAN TT8XK6L BC NADH/NADPH oxidoreductase TT8XK6L SN Qui reductase 1; QR1; Phylloquinone reductase; Phylloqui reductase; NMOR1; NAD(P)H:quinone oxidoreductase 1; NAD(P)H dehydrogenase [quinone] 1; Menadione reductase; DTD; DT-diaphorase 1; DT-diaphorase; DIA4; Azoreductase TT8XK6L GN NQO1 TT8XK6L FC The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. TT8XK6L EC EC 1.6.5.2 TT8XK6L PD 6FY4; 5FUQ; 5EAI; 5EA2; 5A4K TT8XK6L SQ MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVFIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKKEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK TT8XK6L TT Clinical trial TT8XK6L FM Oxidoreductases acting on NADH or NADPH TT8XK6L KE hsa00130:Ubiquinone and other terpenoid-quinone biosynthesis TTAZ05C ID TTAZ05C TTAZ05C TN RAC-gamma serine/threonine-protein kinase (AKT3) TTAZ05C UP Q9Y243 TTAZ05C UC AKT3_HUMAN TTAZ05C BC Kinase TTAZ05C SN STK-2; RAC-PK-gamma; Protein kinase B gamma; Protein kinase Akt-3; PKBG; PKB gamma TTAZ05C GN AKT3 TTAZ05C FC AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. TTAZ05C EC EC 2.7.11.1 TTAZ05C PD 2X18 TTAZ05C SQ MSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE TTAZ05C TT Clinical trial TTAZ05C FM Kinase TTAZ05C KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04530:Tight junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04728:Dopaminergic synapse; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04922:Glucagon signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04973:Carbohydrate digestion and absorption; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTW38KT ID TTW38KT TTW38KT TN Retinoic acid receptor alpha (RARA) TTW38KT UP P10276 TTW38KT UC RARA_HUMAN TTW38KT BC Nuclear hormone receptor TTW38KT SN RAR-alpha; RAR alpha; Nuclear receptor subfamily 1 group B member 1; NR1B1 TTW38KT GN RARA TTW38KT FC Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function. Receptor for retinoic acid. TTW38KT PD 5K13; 4DQM; 3KMZ; 3KMR; 3A9E TTW38KT SQ MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGALTTLQHQLPVSGYSTPSPATIETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEVPKPECSESYTLTPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLICGDRQDLEQPDRVDMLQEPLLEALKVYVRKRRPSRPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGLDTLSGQPGGGGRDGGGLAPPPGSCSPSLSPSSNRSSPATHSP TTW38KT TT Clinical trial TTW38KT FM Nuclear hormone receptor TTW38KT KE hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05221:Acute myeloid leukemia TTW38KT RC R-HSA-383280:Nuclear Receptor transcription pathway TTG0U4H ID TTG0U4H TTG0U4H TN Ribosomal protein S6 kinase beta-1 (S6K1) TTG0U4H UP P23443 TTG0U4H UC KS6B1_HUMAN TTG0U4H BC Kinase TTG0U4H SN p70-S6K 1; p70 ribosomal S6 kinase alpha; p70 S6KA; p70 S6K-alpha; p70 S6 kinase alpha; Serine/threonine-protein kinase 14A; STK14A; S6K-beta-1; S6K; Ribosomal protein S6 kinase I; P70S6K1; P70-S6K; 70 kDa ribosomal protein S6 kinase 1 TTG0U4H GN RPS6KB1 TTG0U4H FC Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B. May be involved in cytoskeletal rearrangement through binding to neurabin. Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR. Following activation by mTORC1, phosphorylates EPRS and thereby plays a key role in fatty acid uptake by adipocytes and also most probably in interferon-gamma-induced translation inhibition. Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. TTG0U4H EC EC 2.7.11.1 TTG0U4H PD 5WBK; 5WBH; 4RLP; 4RLO; 4L46 TTG0U4H SQ MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVKFSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTMSGEASAPLPIRQPNSGPYKKQAFPMISKRPEHLRMNL TTG0U4H TT Clinical trial TTG0U4H FM Kinase TTG0U4H KE hsa04012:ErbB signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04350:TGF-beta signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04910:Insulin signaling pathway; hsa05205:Proteoglycans in cancer; hsa05221:Acute myeloid leukemia; hsa05231:Choline metabolism in cancer TTG0U4H RC R-HSA-166208:mTORC1-mediated signalling TTQBR95 ID TTQBR95 TTQBR95 TN Stress-activated protein kinase 2a (p38 alpha) TTQBR95 UP Q16539 TTQBR95 UC MK14_HUMAN TTQBR95 BC Kinase TTQBR95 SN SAPK2A; P38 mitogen activatedprotein kinase; P38 Mitogen-activatedprotein kinase alpha; Mitogen-activated protein kinase p38 alpha; Mitogen-activated protein kinase 14; MXI2; MAX-interacting protein 2; MAPK 14; MAP kinase p38alpha; MAP kinase p38 alpha; MAP kinase MXI2; MAP kinase 14; Cytokine suppressive anti-inflammatory drug-binding protein; Cytokine suppressive anti-inflammatory drug binding protein; CSPB1; CSBP2; CSBP1; CSBP; CSAID-binding protein; CSAID binding protein; CRK1 TTQBR95 GN MAPK14 TTQBR95 FC MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression. Isoform MXI2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role in the early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113'. Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. TTQBR95 EC EC 2.7.11.24 TTQBR95 PD 6M9L; 6M95; 6HWV; 6HWU; 6HWT TTQBR95 SQ MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES TTQBR95 TT Clinical trial TTQBR95 FM Kinase TTQBR95 KE hsa04010:MAPK signaling pathway; hsa04015:Rap1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04723:Retrograde endocannabinoid signaling; hsa04728:Dopaminergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04917:Prolactin signaling pathway; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05164:Influenza A; hsa05169:Epstein-Barr virus infection; hsa05205:Proteoglycans in cancer TTQBR95 RC R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-171007:p38MAPK events; R-HSA-198753:ERK/MAPK targets; R-HSA-2151209:Activation of PPARGC1A (PGC-1alpha) by phosphorylation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-375170:CDO in myogenesis; R-HSA-376172:DSCAM interactions; R-HSA-418592:ADP signalling through P2Y purinoceptor 1; R-HSA-432142:Platelet sensitization by LDL; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-450302:activated TAK1 mediates p38 MAPK activation; R-HSA-450341:Activation of the AP-1 family of transcription factors; R-HSA-450604:KSRP (KHSRP) binds and destabilizes mRNA TT73U6C ID TT73U6C TT73U6C TN Stress-activated protein kinase 2b (p38 beta) TT73U6C UP Q15759 TT73U6C UC MK11_HUMAN TT73U6C BC Kinase TT73U6C SN Stress-activated protein kinase-2; SAPK2b; SAPK2; PRKM11; P38b; P38-2; P38 Mitogen-activated protein kinase beta; Mitogen-activated protein kinase p38 beta; Mitogen-activated protein kinase 11; MAPK 11; MAP kinase p38 beta; MAP kinase 11 TT73U6C GN MAPK11 TT73U6C FC MAPK11 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK11 functions are mostly redundant with those of MAPK14. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Additional examples of p38 MAPK substrates are the FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. TT73U6C EC EC 2.7.11.24 TT73U6C PD 3GP0; 3GC9; 3GC8 TT73U6C SQ MSGPRAGFYRQELNKTVWEVPQRLQGLRPVGSGAYGSVCSAYDARLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHLKHENVIGLLDVFTPATSIEDFSEVYLVTTLMGADLNNIVKCQALSDEHVQFLVYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADEEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLQGKALFPGSDYIDQLKRIMEVVGTPSPEVLAKISSEHARTYIQSLPPMPQKDLSSIFRGANPLAIDLLGRMLVLDSDQRVSAAEALAHAYFSQYHDPEDEPEAEPYDESVEAKERTLEEWKELTYQEVLSFKPPEPPKPPGSLEIEQ TT73U6C TT Clinical trial TT73U6C FM Kinase TT73U6C KE hsa04010:MAPK signaling pathway; hsa04015:Rap1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04723:Retrograde endocannabinoid signaling; hsa04728:Dopaminergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04917:Prolactin signaling pathway; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05164:Influenza A; hsa05169:Epstein-Barr virus infection; hsa05205:Proteoglycans in cancer TT73U6C RC R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-171007:p38MAPK events; R-HSA-198753:ERK/MAPK targets; R-HSA-2151209:Activation of PPARGC1A (PGC-1alpha) by phosphorylation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-375170:CDO in myogenesis; R-HSA-376172:DSCAM interactions; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-450302:activated TAK1 mediates p38 MAPK activation; R-HSA-450341:Activation of the AP-1 family of transcription factors; R-HSA-450604:KSRP (KHSRP) binds and destabilizes mRNA TT0K6EO ID TT0K6EO TT0K6EO TN Stress-activated protein kinase JNK1 (JNK1) TT0K6EO UP P45983 TT0K6EO UC MK08_HUMAN TT0K6EO BC Kinase TT0K6EO SN Stress-activated protein kinase 1c; SAPK1c; PRKM8; Mitogen-activated protein kinase 8; MAPK 8; MAP kinase 8; JNK-46; C-Jun N-terminal kinase 1 TT0K6EO GN MAPK8 TT0K6EO FC Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates the heat shock transcription factor HSF1, suppressing HSF1-induced transcriptional activity. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation. Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. TT0K6EO EC EC 2.7.11.24 TT0K6EO PD 6F5E; 5LW1; 4YR8; 4UX9; 4QTD TT0K6EO SQ MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEERTKNGVIRGQPSPLGAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR TT0K6EO TT Clinical trial TT0K6EO FM Kinase TT0K6EO KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04024:cAMP signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04141:Protein processing in endoplasmic reticulum; hsa04310:Wnt signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04723:Retrograde endocannabinoid signaling; hsa04728:Dopaminergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04917:Prolactin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05210:Colorectal cancer; hsa05212:Pancreatic cancer; hsa05231:Choline metabolism in cancer TT0K6EO RC R-HSA-193648:NRAGE signals death through JNK; R-HSA-205043:NRIF signals cell death from the nucleus; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-376172:DSCAM interactions; R-HSA-450321:JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1; R-HSA-450341:Activation of the AP-1 family of transcription factors; R-HSA-5693565:Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks TTP4520 ID TTP4520 TTP4520 TN TGF-beta receptor type I (TGFBR1) TTP4520 UP P36897 TTP4520 UC TGFR1_HUMAN TTP4520 BC Kinase TTP4520 SN Type I TGFbeta receptor kinase; Transforming growth factor-beta receptor type I; TbetaRI; TbetaR-I; TGFR-1; TGF-beta type I receptor; TGF-beta receptor type-1; Serine/threonine-protein kinase receptor R4; SKR4; Activin receptor-like kinase 5; Activin A receptor type II-like protein kinase of 53kD; ALK5; ALK-5 TTP4520 GN TGFBR1 TTP4520 FC Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation. Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. TTP4520 EC EC 2.7.11.30 TTP4520 PD 6B8Y; 5USQ; 5QIM; 5QIL; 5QIK TTP4520 SQ MEAAVAAPRPRLLLLVLAAAAAAAAALLPGATALQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEGIKM TTP4520 TT Clinical trial TTP4520 FM Kinase TTP4520 KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04068:FoxO signaling pathway; hsa04144:Endocytosis; hsa04350:TGF-beta signaling pathway; hsa04380:Osteoclast differentiation; hsa04390:Hippo signaling pathway; hsa04520:Adherens junction; hsa05142:Chagas disease (American trypanosomiasis); hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05210:Colorectal cancer; hsa05212:Pancreatic cancer; hsa05220:Chronic myeloid leukemia TTP4520 RC R-HSA-2173789:TGF-beta receptor signaling activates SMADs; R-HSA-2173791:TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition); R-HSA-3304356:SMAD2/3 Phosphorylation Motif Mutants in Cancer; R-HSA-3315487:SMAD2/3 MH2 Domain Mutants in Cancer; R-HSA-3645790:TGFBR2 Kinase Domain Mutants in Cancer; R-HSA-3656532:TGFBR1 KD Mutants in Cancer; R-HSA-3656535:TGFBR1 LBD Mutants in Cancer TTJLNAW ID TTJLNAW TTJLNAW TN Tissue kallikrein (KLK2) TTJLNAW UP P20151 TTJLNAW UC KLK2_HUMAN TTJLNAW BC Peptidase TTJLNAW SN hGK-1; Tissue kallikrein-2; Kallikrein-2; Glandular kallikrein-1 TTJLNAW GN KLK2 TTJLNAW FC Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. TTJLNAW EC EC 3.4.21.35 TTJLNAW PD 4NFF; 4NFE TTJLNAW SQ MWDLVLSIALSVGCTGAVPLIQSRIVGGWECEKHSQPWQVAVYSHGWAHCGGVLVHPQWVLTAAHCLKKNSQVWLGRHNLFEPEDTGQRVPVSHSFPHPLYNMSLLKHQSLRPDEDSSHDLMLLRLSEPAKITDVVKVLGLPTQEPALGTTCYASGWGSIEPEEFLRPRSLQCVSLHLLSNDMCARAYSEKVTEFMLCAGLWTGGKDTCGGDSGGPLVCNGVLQGITSWGPEPCALPEKPAVYTKVVHYRKWIKDTIAANP TTJLNAW TT Clinical trial TTJLNAW FM Peptidase TTJLNAW KE hsa04961:Endocrine and other factor-regulated calcium reabsorption TTJLNAW RC R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-381426:Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-5625886:Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 TT08GJW ID TT08GJW TT08GJW TN Ubiquitin-protein ligase E3 Mdm2 (MDM2) TT08GJW UP Q00987 TT08GJW UC MDM2_HUMAN TT08GJW BC Acyltransferase TT08GJW SN RING-type E3 ubiquitin transferase Mdm2; P53-binding protein Mdm2; Oncoprotein Mdm2; MDM2 protein; Hdm2; E3 ubiquitin-protein ligase Mdm2; Double minute 2 protein TT08GJW GN MDM2 TT08GJW FC Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation. Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells. Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis. E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. TT08GJW EC EC 2.3.2.27 TT08GJW PD 6Q9O; 6Q9L; 6Q9H; 6Q96; 6IM9 TT08GJW SQ MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP TT08GJW TT Clinical trial TT08GJW FM Peptide synthase TT08GJW KE hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia TT08GJW RC R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559585:Oncogene Induced Senescence; R-HSA-399719:Trafficking of AMPA receptors; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer; R-HSA-69541:Stabilization of p53 TTDCBX5 ID TTDCBX5 TTDCBX5 TN Vascular endothelial growth factor receptor 3 (FLT-4) TTDCBX5 UP P35916 TTDCBX5 UC VGFR3_HUMAN TTDCBX5 BC Kinase TTDCBX5 SN VEGFR3; VEGFR-3; VEGF-3 receptor; Tyrosine-protein kinase receptor FLT4; Fms-like tyrosine kinase 4 TTDCBX5 GN FLT4 TTDCBX5 FC Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. The secreted isoform 3 may function as a decoy receptor for VEGFC and/or VEGFD and play an important role as a negative regulator of VEGFC-mediated lymphangiogenesis and angiogenesis. Binding of vascular growth factors to isoform 1 or isoform 2 leads to the activation of several signaling cascades; isoform 2 seems to be less efficient in signal transduction, because it has a truncated C-terminus and therefore lacks several phosphorylation sites. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'. Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. TTDCBX5 EC EC 2.7.10.1 TTDCBX5 PD 4BSK; 4BSJ TTDCBX5 SQ MQRGAALCLRLWLCLGLLDGLVSGYSMTPPTLNITEESHVIDTGDSLSISCRGQHPLEWAWPGAQEAPATGDKDSEDTGVVRDCEGTDARPYCKVLLLHEVHANDTGSYVCYYKYIKARIEGTTAASSYVFVRDFEQPFINKPDTLLVNRKDAMWVPCLVSIPGLNVTLRSQSSVLWPDGQEVVWDDRRGMLVSTPLLHDALYLQCETTWGDQDFLSNPFLVHITGNELYDIQLLPRKSLELLVGEKLVLNCTVWAEFNSGVTFDWDYPGKQAERGKWVPERRSQQTHTELSSILTIHNVSQHDLGSYVCKANNGIQRFRESTEVIVHENPFISVEWLKGPILEATAGDELVKLPVKLAAYPPPEFQWYKDGKALSGRHSPHALVLKEVTEASTGTYTLALWNSAAGLRRNISLELVVNVPPQIHEKEASSPSIYSRHSRQALTCTAYGVPLPLSIQWHWRPWTPCKMFAQRSLRRRQQQDLMPQCRDWRAVTTQDAVNPIESLDTWTEFVEGKNKTVSKLVIQNANVSAMYKCVVSNKVGQDERLIYFYVTTIPDGFTIESKPSEELLEGQPVLLSCQADSYKYEHLRWYRLNLSTLHDAHGNPLLLDCKNVHLFATPLAASLEEVAPGARHATLSLSIPRVAPEHEGHYVCEVQDRRSHDKHCHKKYLSVQALEAPRLTQNLTDLLVNVSDSLEMQCLVAGAHAPSIVWYKDERLLEEKSGVDLADSNQKLSIQRVREEDAGRYLCSVCNAKGCVNSSASVAVEGSEDKGSMEIVILVGTGVIAVFFWVLLLLIFCNMRRPAHADIKTGYLSIIMDPGEVPLEEQCEYLSYDASQWEFPRERLHLGRVLGYGAFGKVVEASAFGIHKGSSCDTVAVKMLKEGATASEHRALMSELKILIHIGNHLNVVNLLGACTKPQGPLMVIVEFCKYGNLSNFLRAKRDAFSPCAEKSPEQRGRFRAMVELARLDRRRPGSSDRVLFARFSKTEGGARRASPDQEAEDLWLSPLTMEDLVCYSFQVARGMEFLASRKCIHRDLAARNILLSESDVVKICDFGLARDIYKDPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLRDGTRMRAPELATPAIRRIMLNCWSGDPKARPAFSELVEILGDLLQGRGLQEEEEVCMAPRSSQSSEEGSFSQVSTMALHIAQADAEDSPPSLQRHSLAARYYNWVSFPGCLARGAETRGSSRMKTFEEFPMTPTTYKGSVDNQTDSGMVLASEEFEQIESRHRQESGFSCKGPGQNVAVTRAHPDSQGRRRRPERGARGGQVFYNSEYGELSEPSEEDHCSPSARVTFFTDNSY TTDCBX5 TT Successful TTDCBX5 FM Kinase TTDCBX5 KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion TTDCBX5 RC R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization TT4G2JS ID TT4G2JS TT4G2JS TN Voltage-gated sodium channel alpha Nav1.7 (SCN9A) TT4G2JS UP Q15858 TT4G2JS UC SCN9A_HUMAN TT4G2JS BC Voltage-gated ion channel TT4G2JS SN hNE-Na; Voltage-gated sodium channel subunit alpha Nav1.7; Sodium channel proteintype IX subunit alpha; Sodium channel proteintype 9 subunit alpha; Sodium channel protein type IX subunit alpha; Sodium channel protein type 9 subunit alpha; Peripheral sodium channel 1; PN1; Neuroendocrine sodium channel; NENA TT4G2JS GN SCN9A TT4G2JS FC Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-sensitive Na(+) channel isoform. Plays a role in pain mechanisms, especially in the development of inflammatory pain. Mediates the voltage-dependent sodium ion permeability of excitable membranes. TT4G2JS PD 6NT4; 6NT3; 6N4R; 6N4Q; 6J8J TT4G2JS SQ MAMLPPPGPQSFVHFTKQSLALIEQRIAERKSKEPKEEKKDDDEEAPKPSSDLEAGKQLPFIYGDIPPGMVSEPLEDLDPYYADKKTFIVLNKGKTIFRFNATPALYMLSPFSPLRRISIKILVHSLFSMLIMCTILTNCIFMTMNNPPDWTKNVEYTFTGIYTFESLVKILARGFCVGEFTFLRDPWNWLDFVVIVFAYLTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLKHKCFRNSLENNETLESIMNTLESEEDFRKYFYYLEGSKDALLCGFSTDSGQCPEGYTCVKIGRNPDYGYTSFDTFSWAFLALFRLMTQDYWENLYQQTLRAAGKTYMIFFVVVIFLGSFYLINLILAVVAMAYEEQNQANIEEAKQKELEFQQMLDRLKKEQEEAEAIAAAAAEYTSIRRSRIMGLSESSSETSKLSSKSAKERRNRRKKKNQKKLSSGEEKGDAEKLSKSESEDSIRRKSFHLGVEGHRRAHEKRLSTPNQSPLSIRGSLFSARRSSRTSLFSFKGRGRDIGSETEFADDEHSIFGDNESRRGSLFVPHRPQERRSSNISQASRSPPMLPVNGKMHSAVDCNGVVSLVDGRSALMLPNGQLLPEVIIDKATSDDSGTTNQIHKKRRCSSYLLSEDMLNDPNLRQRAMSRASILTNTVEELEESRQKCPPWWYRFAHKFLIWNCSPYWIKFKKCIYFIVMDPFVDLAITICIVLNTLFMAMEHHPMTEEFKNVLAIGNLVFTGIFAAEMVLKLIAMDPYEYFQVGWNIFDSLIVTLSLVELFLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINDDCTLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVYMMVMVIGNLVVLNLFLALLLSSFSSDNLTAIEEDPDANNLQIAVTRIKKGINYVKQTLREFILKAFSKKPKISREIRQAEDLNTKKENYISNHTLAEMSKGHNFLKEKDKISGFGSSVDKHLMEDSDGQSFIHNPSLTVTVPIAPGESDLENMNAEELSSDSDSEYSKVRLNRSSSSECSTVDNPLPGEGEEAEAEPMNSDEPEACFTDGCVWRFSCCQVNIESGKGKIWWNIRKTCYKIVEHSWFESFIVLMILLSSGALAFEDIYIERKKTIKIILEYADKIFTYIFILEMLLKWIAYGYKTYFTNAWCWLDFLIVDVSLVTLVANTLGYSDLGPIKSLRTLRALRPLRALSRFEGMRVVVNALIGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYECINTTDGSRFPASQVPNRSECFALMNVSQNVRWKNLKVNFDNVGLGYLSLLQVATFKGWTIIMYAAVDSVNVDKQPKYEYSLYMYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKIQGCIFDLVTNQAFDISIMVLICLNMVTMMVEKEGQSQHMTEVLYWINVVFIILFTGECVLKLISLRHYYFTVGWNIFDFVVVIISIVGMFLADLIETYFVSPTLFRVIRLARIGRILRLVKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEDGINDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPKKVHPGSSVEGDCGNPSVGIFYFVSYIIISFLVVVNMYIAVILENFSVATEESTEPLSEDDFEMFYEVWEKFDPDATQFIEFSKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDSLRSQMEERFMSANPSKVSYEPITTTLKRKQEDVSATVIQRAYRRYRLRQNVKNISSIYIKDGDRDDDLLNKKDMAFDNVNENSSPEKTDATSSTTSPPSYDSVTKPDKEKYEQDRTEKEDKGKDSKESKK TT4G2JS TT Clinical trial TT4G2JS FM Voltage gated ion channel TT4G2JS RC R-HSA-445095:Interaction between L1 and Ankyrins TTJFOAL ID TTJFOAL TTJFOAL TN Wee1-like protein kinase (WEE1) TTJFOAL UP P30291 TTJFOAL UC WEE1_HUMAN TTJFOAL BC Kinase TTJFOAL SN Wee1A kinase; WEE1hu TTJFOAL GN WEE1 TTJFOAL FC Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation. Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. TTJFOAL EC EC 2.7.10.2 TTJFOAL PD 5VDA; 5VD9; 5VD8; 5VD7; 5VD5 TTJFOAL SQ MSFLSRQQPPPPRRAGAACTLRQKLIFSPCSDCEEEEEEEEEEGSGHSTGEDSAFQEPDSPLPPARSPTEPGPERRRSPGPAPGSPGELEEDLLLPGACPGADEAGGGAEGDSWEEEGFGSSSPVKSPAAPYFLGSSFSPVRCGGPGDASPRGCGARRAGEGRRSPRPDHPGTPPHKTFRKLRLFDTPHTPKSLLSKARGIDSSSVKLRGSSLFMDTEKSGKREFDVRQTPQVNINPFTPDSLLLHSSGQCRRRKRTYWNDSCGEDMEASDYELEDETRPAKRITITESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYFSAWAEDDHMLIQNEYCNGGSLADAISENYRIMSYFKEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDDWASNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIPQVLSQEFTELLKVMIHPDPERRPSAMALVKHSVLLSASRKSAEQLRIELNAEKFKNSLLQKELKKAQMAKAAAEERALFTDRMATRSTTQSNRTSRLIGKKMNRSVSLTIY TTJFOAL TT Clinical trial TTJFOAL FM Kinase TTJFOAL KE hsa04110:Cell cycle TTJFOAL RC R-HSA-156711:Polo-like kinase mediated events; R-HSA-69202:Cyclin E associated events during G1/S transition; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition; R-HSA-69478:G2/M DNA replication checkpoint; R-HSA-69656:Cyclin A:Cdk2-associated events at S phase entry; R-HSA-75035:Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TT0SQ8J ID TT0SQ8J TT0SQ8J TN Yes tyrosine kinase (YES) TT0SQ8J UP P07947 TT0SQ8J UC YES_HUMAN TT0SQ8J BC Kinase TT0SQ8J SN p61-Yes; Yes p59-Fyn; Yes Protooncogene Syn; Tyrosine-protein kinase Yes; Proto-oncogene c-Yes TT0SQ8J GN YES1 TT0SQ8J FC Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis. Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. TT0SQ8J EC EC 2.7.10.2 TT0SQ8J PD 2HDA TT0SQ8J SQ MGCIKSKENKSPAIKYRPENTPEPVSTSVSHYGAEPTTVSPCPSSSAKGTAVNFSSLSMTPFGGSSGVTPFGGASSSFSVVPSSYPAGLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGENL TT0SQ8J TT Clinical trial TT0SQ8J FM Kinase TT0SQ8J KE hsa04520:Adherens junction; hsa04530:Tight junction TT0SQ8J RC R-HSA-1433559:Regulation of KIT signaling; R-HSA-2029481:FCGR activation; R-HSA-210990:PECAM1 interactions; R-HSA-2682334:EPH-Ephrin signaling; R-HSA-389356:CD28 co-stimulation; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-3928665:EPH-ephrin mediated repulsion of cells; R-HSA-912631:Regulation of signaling by CBL TTJS8PY ID TTJS8PY TTJS8PY TN 5-HT 6 receptor (HTR6) TTJS8PY UP P50406 TTJS8PY UC 5HT6R_HUMAN TTJS8PY BC GPCR rhodopsin TTJS8PY SN Serotonin receptor 6; 5-hydroxytryptamine receptor 6; 5-HT6 receptor; 5-HT6; 5-HT-6 TTJS8PY GN HTR6 TTJS8PY FC The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. It has a high affinity for tricyclic psychotropic drugs. Controls pyramidal neurons migration during corticogenesis, through the regulation of CDK5 activity. Is an activator of TOR signaling. This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. TTJS8PY SQ MVPEPGPTANSTPAWGAGPPSAPGGSGWVAAALCVVIALTAAANSLLIALICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTPLRALALVLGAWSLAALASFLPLLLGWHELGHARPPVPGQCRLLASLPFVLVASGLTFFLPSGAICFTYCRILLAARKQAVQVASLTTGMASQASETLQVPRTPRPGVESADSRRLATKHSRKALKASLTLGILLGMFFVTWLPFFVANIVQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFLPCPRCPRERQASLASPSLRTSHSGPRPGLSLQQVLPLPLPPDSDSDSDAGSGGSSGLRLTAQLLLPGEATQDPPLPTRAAAAVNFFNIDPAEPELRPHPLGIPTN TTJS8PY TT Clinical trial TTJS8PY FM GPCR rhodopsin TTJS8PY KE hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse TTJS8PY RC R-HSA-390666:Serotonin receptors; R-HSA-418555:G alpha (s) signalling events TTKPW01 ID TTKPW01 TTKPW01 TN Androgen receptor messenger RNA (AR mRNA) TTKPW01 UP P10275 TTKPW01 UC ANDR_HUMAN TTKPW01 BC mRNA target TTKPW01 SN Testosterone receptor (mRNA); Nuclear receptor subfamily 3 group C member 4 (mRNA); NR3C4 (mRNA); Dihydrotestosterone receptor (mRNA); DHTR (mRNA); Androgen receptor (mRNA) TTKPW01 GN AR TTKPW01 FC Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. TTKPW01 PD 5VO4; 5V8Q; 5T8J; 5T8E; 5JJM TTKPW01 SQ MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSALECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPYGYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ TTKPW01 TT Clinical trial TTKPW01 FM mRNA target TTKPW01 KE hsa04114:Oocyte meiosis; hsa05200:Pathways in cancer; hsa05215:Prostate cancer TTKPW01 RC R-HSA-383280:Nuclear Receptor transcription pathway; R-HSA-5625886:Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 TTWNQ1T ID TTWNQ1T TTWNQ1T TN Angiopoietin-1 (ANGPT1) TTWNQ1T UP Q15389 TTWNQ1T UC ANGP1_HUMAN TTWNQ1T BC Fibrinogen protein TTWNQ1T SN Angiopoietin1; ANGPT1; ANG1; ANG-1 TTWNQ1T GN ANGPT1 TTWNQ1T FC Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes laterand distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. TTWNQ1T PD 4K0V; 4JYO; 4EPU TTWNQ1T SQ MTVFLSFAFLAAILTHIGCSNQRRSPENSGRRYNRIQHGQCAYTFILPEHDGNCRESTTDQYNTNALQRDAPHVEPDFSSQKLQHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVTRQTYIIQELEKQLNRATTNNSVLQKQQLELMDTVHNLVNLCTKEGVLLKGGKREEEKPFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF TTWNQ1T TT Clinical trial TTWNQ1T KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa05323:Rheumatoid arthritis TTWNQ1T RC R-HSA-210993:Tie2 Signaling; R-HSA-5673001:RAF/MAP kinase cascade TTKLQTJ ID TTKLQTJ TTKLQTJ TN Angiopoietin-2 (ANGPT2) TTKLQTJ UP O15123 TTKLQTJ UC ANGP2_HUMAN TTKLQTJ BC Fibrinogen protein TTKLQTJ SN ANG-2 TTKLQTJ GN ANGPT2 TTKLQTJ FC Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal. Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. TTKLQTJ PD 4ZFG; 4JZC; 2GY7; 1Z3U; 1Z3S TTKLQTJ SQ MWQIVFFTLSCDLVLAAAYNNFRKSMDSIGKKQYQVQHGSCSYTFLLPEMDNCRSSSSPYVSNAVQRDAPLEYDDSVQRLQVLENIMENNTQWLMKLENYIQDNMKKEMVEIQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEINKLQDKNSFLEKKVLAMEDKHIIQLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVNNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQISFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGGGWTIIQRREDGSVDFQRTWKEYKVGFGNPSGEYWLGNEFVSQLTNQQRYVLKIHLKDWEGNEAYSLYEHFYLSSEELNYRIHLKGLTGTAGKISSISQPGNDFSTKDGDNDKCICKCSQMLTGGWWFDACGPSNLNGMYYPQRQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF TTKLQTJ TT Clinical trial TTKLQTJ FM Fibrinogen TTKLQTJ KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04151:PI3K-Akt signaling pathway TTKLQTJ RC R-HSA-210993:Tie2 Signaling TTUI5H7 ID TTUI5H7 TTUI5H7 TN Angiotensin-converting enzyme 2 (ACE2) TTUI5H7 UP Q9BYF1 TTUI5H7 UC ACE2_HUMAN TTUI5H7 BC Peptidase TTUI5H7 SN Processed angiotensinconverting enzyme 2; Metalloprotease MPROT15; Angiotensinconverting enzyme homolog; Angiotensinconverting enzyme 2; ACErelated carboxypeptidase; ACEH; ACE2 TTUI5H7 GN ACE2 TTUI5H7 FC Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin- 13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses. TTUI5H7 EC EC 3.4.17.23 TTUI5H7 PD 6CS2; 6ACK; 6ACJ; 6ACG; 3SCL TTUI5H7 SQ MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKGENNPGFQNTDDVQTSF TTUI5H7 TT Clinical trial TTUI5H7 KE hsa04614:Renin-angiotensin system; hsa04974:Protein digestion and absorption TTUI5H7 RC R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins TTTPU1G ID TTTPU1G TTTPU1G TN Apoptosis inhibitor survivin (BIRC5) TTTPU1G UP O15392 TTTPU1G UC BIRC5_HUMAN TTTPU1G BC Acyltransferase TTTPU1G SN Survivin; IAP4; Baculoviral IAP repeat-containing protein 5; Apoptosis inhibitor 4; API4 TTTPU1G GN BIRC5 TTTPU1G FC Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform. Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. TTTPU1G PD 4A0N; 4A0J; 4A0I; 3UIK; 3UIJ TTTPU1G SQ MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD TTTPU1G TT Clinical trial TTTPU1G FM Inhibitor of apoptosis TTTPU1G KE hsa04390:Hippo signaling pathway; hsa05161:Hepatitis B; hsa05200:Pathways in cancer; hsa05210:Colorectal cancer TTTPU1G RC R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-68877:Mitotic Prometaphase TTQ79W8 ID TTQ79W8 TTQ79W8 TN Apoptosis regulator Bcl-W (BCL-W) TTQ79W8 UP Q92843 TTQ79W8 UC B2CL2_HUMAN TTQ79W8 BC B-cell lymphoma Bcl-2 TTQ79W8 SN KIAA0271; Bcl2-L-2; Bcl-2-like protein 2; BCLW TTQ79W8 GN BCL2L2 TTQ79W8 FC Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. Promotes cell survival. TTQ79W8 PD 4CIM; 2Y6W; 1ZY3; 1O0L; 1MK3 TTQ79W8 SQ MATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQEWMVAYLETQLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK TTQ79W8 TT Clinical trial TTQ79W8 FM BCL2 family TTQ79W8 KE hsa05206:MicroRNAs in cancer TTU1E82 ID TTU1E82 TTU1E82 TN Apoptosis regulator Bcl-xL (BCL-xL) TTU1E82 UP Q07817 TTU1E82 UC B2CL1_HUMAN TTU1E82 BC B-cell lymphoma Bcl-2 TTU1E82 SN Bcl2like protein 1; Bcl2L1; Bcl2-L-1; Bcl-XL; Bcl-2-like protein 1; BCLX; BCL2L; Apoptosis regulator Bcl-X TTU1E82 GN BCL2L1 TTU1E82 FC Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Potent inhibitor of cell death. TTU1E82 PD 6IJQ; 6F46; 6DCO; 6DCN; 6BF2 TTU1E82 SQ MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK TTU1E82 TT Clinical trial TTU1E82 FM BCL2 family TTU1E82 KE hsa04014:Ras signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04630:Jak-STAT signaling pathway; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05145:Toxoplasmosis; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05212:Pancreatic cancer; hsa05220:Chronic myeloid leukemia; hsa05222:Small cell lung cancer TTU1E82 RC R-HSA-111453:BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members; R-HSA-844455:The NLRP1 inflammasome TTKBM7V ID TTKBM7V TTKBM7V TN ATM serine/threonine kinase (ATM) TTKBM7V UP Q13315 TTKBM7V UC ATM_HUMAN TTKBM7V BC Kinase TTKBM7V SN Serine-protein kinase ATM; Ataxia telangiectasia mutated; A-T mutated TTKBM7V GN ATM TTKBM7V FC Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9, UBQLN4 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response. TTKBM7V EC EC 2.7.11.1 TTKBM7V PD 6HKA; 5NP1; 5NP0 TTKBM7V SQ MSLVLNDLLICCRQLEHDRATERKKEVEKFKRLIRDPETIKHLDRHSDSKQGKYLNWDAVFRFLQKYIQKETECLRIAKPNVSASTQASRQKKMQEISSLVKYFIKCANRRAPRLKCQELLNYIMDTVKDSSNGAIYGADCSNILLKDILSVRKYWCEISQQQWLELFSVYFRLYLKPSQDVHRVLVARIIHAVTKGCCSQTDGLNSKFLDFFSKAIQCARQEKSSSGLNHILAALTIFLKTLAVNFRIRVCELGDEILPTLLYIWTQHRLNDSLKEVIIELFQLQIYIHHPKGAKTQEKGAYESTKWRSILYNLYDLLVNEISHIGSRGKYSSGFRNIAVKENLIELMADICHQVFNEDTRSLEISQSYTTTQRESSDYSVPCKRKKIELGWEVIKDHLQKSQNDFDLVPWLQIATQLISKYPASLPNCELSPLLMILSQLLPQQRHGERTPYVLRCLTEVALCQDKRSNLESSQKSDLLKLWNKIWCITFRGISSEQIQAENFGLLGAIIQGSLVEVDREFWKLFTGSACRPSCPAVCCLTLALTTSIVPGTVKMGIEQNMCEVNRSFSLKESIMKWLLFYQLEGDLENSTEVPPILHSNFPHLVLEKILVSLTMKNCKAAMNFFQSVPECEHHQKDKEELSFSEVEELFLQTTFDKMDFLTIVRECGIEKHQSSIGFSVHQNLKESLDRCLLGLSEQLLNNYSSEITNSETLVRCSRLLVGVLGCYCYMGVIAEEEAYKSELFQKAKSLMQCAGESITLFKNKTNEEFRIGSLRNMMQLCTRCLSNCTKKSPNKIASGFFLRLLTSKLMNDIADICKSLASFIKKPFDRGEVESMEDDTNGNLMEVEDQSSMNLFNDYPDSSVSDANEPGESQSTIGAINPLAEEYLSKQDLLFLDMLKFLCLCVTTAQTNTVSFRAADIRRKLLMLIDSSTLEPTKSLHLHMYLMLLKELPGEEYPLPMEDVLELLKPLSNVCSLYRRDQDVCKTILNHVLHVVKNLGQSNMDSENTRDAQGQFLTVIGAFWHLTKERKYIFSVRMALVNCLKTLLEADPYSKWAILNVMGKDFPVNEVFTQFLADNHHQVRMLAAESINRLFQDTKGDSSRLLKALPLKLQQTAFENAYLKAQEGMREMSHSAENPETLDEIYNRKSVLLTLIAVVLSCSPICEKQALFALCKSVKENGLEPHLVKKVLEKVSETFGYRRLEDFMASHLDYLVLEWLNLQDTEYNLSSFPFILLNYTNIEDFYRSCYKVLIPHLVIRSHFDEVKSIANQIQEDWKSLLTDCFPKILVNILPYFAYEGTRDSGMAQQRETATKVYDMLKSENLLGKQIDHLFISNLPEIVVELLMTLHEPANSSASQSTDLCDFSGDLDPAPNPPHFPSHVIKATFAYISNCHKTKLKSILEILSKSPDSYQKILLAICEQAAETNNVYKKHRILKIYHLFVSLLLKDIKSGLGGAWAFVLRDVIYTLIHYINQRPSCIMDVSLRSFSLCCDLLSQVCQTAVTYCKDALENHLHVIVGTLIPLVYEQVEVQKQVLDLLKYLVIDNKDNENLYITIKLLDPFPDHVVFKDLRITQQKIKYSRGPFSLLEEINHFLSVSVYDALPLTRLEGLKDLRRQLELHKDQMVDIMRASQDNPQDGIMVKLVVNLLQLSKMAINHTGEKEVLEAVGSCLGEVGPIDFSTIAIQHSKDASYTKALKLFEDKELQWTFIMLTYLNNTLVEDCVKVRSAAVTCLKNILATKTGHSFWEIYKMTTDPMLAYLQPFRTSRKKFLEVPRFDKENPFEGLDDINLWIPLSENHDIWIKTLTCAFLDSGGTKCEILQLLKPMCEVKTDFCQTVLPYLIHDILLQDTNESWRNLLSTHVQGFFTSCLRHFSQTSRSTTPANLDSESEHFFRCCLDKKSQRTMLAVVDYMRRQKRPSSGTIFNDAFWLDLNYLEVAKVAQSCAAHFTALLYAEIYADKKSMDDQEKRSLAFEEGSQSTTISSLSEKSKEETGISLQDLLLEIYRSIGEPDSLYGCGGGKMLQPITRLRTYEHEAMWGKALVTYDLETAIPSSTRQAGIIQALQNLGLCHILSVYLKGLDYENKDWCPELEELHYQAAWRNMQWDHCTSVSKEVEGTSYHESLYNALQSLRDREFSTFYESLKYARVKEVEEMCKRSLESVYSLYPTLSRLQAIGELESIGELFSRSVTHRQLSEVYIKWQKHSQLLKDSDFSFQEPIMALRTVILEILMEKEMDNSQRECIKDILTKHLVELSILARTFKNTQLPERAIFQIKQYNSVSCGVSEWQLEEAQVFWAKKEQSLALSILKQMIKKLDASCAANNPSLKLTYTECLRVCGNWLAETCLENPAVIMQTYLEKAVEVAGNYDGESSDELRNGKMKAFLSLARFSDTQYQRIENYMKSSEFENKQALLKRAKEEVGLLREHKIQTNRYTVKVQRELELDELALRALKEDRKRFLCKAVENYINCLLSGEEHDMWVFRLCSLWLENSGVSEVNGMMKRDGMKIPTYKFLPLMYQLAARMGTKMMGGLGFHEVLNNLISRISMDHPHHTLFIILALANANRDEFLTKPEVARRSRITKNVPKQSSQLDEDRTEAANRIICTIRSRRPQMVRSVEALCDAYIILANLDATQWKTQRKGINIPADQPITKLKNLEDVVVPTMEIKVDHTGEYGNLVTIQSFKAEFRLAGGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDGAHKRYRPNDFSAFQCQKKMMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCMEKFLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTMNPLKALYLQQRPEDETELHPTLNADDQECKRNLSDIDQSFNKVAERVLMRLQEKLKGVEEGTVLSVGGQVNLLIQQAIDPKNLSRLFPGWKAWV TTKBM7V TT Clinical trial TTIQSC1 ID TTIQSC1 TTIQSC1 TN Bacterial Lethal factor (Bact lef) TTIQSC1 UP P15917 TTIQSC1 UC LEF_BACAN TTIQSC1 BC Peptidase TTIQSC1 SN lef; Anthrax lethal toxin endopeptidase component; Anthrax lethal factor; ALF TTIQSC1 GN Bact lef TTIQSC1 FC One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. LF is the lethal factor that, when associated with PA, causes death. LF is not toxic by itself. It is a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5). Cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LeTx intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates. TTIQSC1 EC EC 3.4.24.83 TTIQSC1 PD 5D1U; 5D1T; 5D1S; 4XM8; 4XM7 TTIQSC1 SQ MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS TTIQSC1 TT Clinical trial TTIQSC1 RC R-HSA-5210891:Uptake and function of anthrax toxins TTVSFJW ID TTVSFJW TTVSFJW TN Calcitonin gene-related peptide 1 (CALCA) TTVSFJW UP P06881 TTVSFJW UC CALCA_HUMAN TTVSFJW BC Cytotoxic amylin family TTVSFJW SN Calcitonin gene-related peptide I; CGRP-I; CALCA; CALC1; Alpha-type CGRP TTVSFJW GN CALCA TTVSFJW FC CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role. It also elevates platelet cAMP. TTVSFJW PD 6E3Y; 1LS7 TTVSFJW SQ MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSRIIAQKRACDTATCVTHRLAGLLSRSGGVVKNNFVPTNVGSKAFGRRRRDLQA TTVSFJW TT Clinical trial TTVSFJW RC R-HSA-418555:G alpha (s) signalling events; R-HSA-419812:Calcitonin-like ligand receptors TTG5QB7 ID TTG5QB7 TTG5QB7 TN Calpain-2 (CAPN2) TTG5QB7 UP P17655 TTG5QB7 UC CAN2_HUMAN TTG5QB7 BC Peptidase TTG5QB7 SN Millimolar-calpain; M-calpain; Calpain-2 large subunit; Calpain-2 catalytic subunit; Calpain large polypeptide L2; Calpain M-type; Calcium-activated neutral proteinase 2; Calcium-activated neutral proteinase; CANPL2; CANP 2; CANP TTG5QB7 GN CAPN2 TTG5QB7 FC Proteolytically cleaves MYOC at 'Arg-226'. Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs. Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. TTG5QB7 EC EC 3.4.22.53 TTG5QB7 SQ MAGIAAKLAKDREAAEGLGSHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDNCPSWNTIDPEERERLTRRHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELSGQTNIHLSKNFFLTNRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL TTG5QB7 TT Clinical trial TTG5QB7 FM Peptidase C2 family TTG5QB7 KE hsa04141:Protein processing in endoplasmic reticulum; hsa04210:Apoptosis; hsa05010:Alzheimer's disease TTG5QB7 RC R-HSA-1474228:Degradation of the extracellular matrix TTP18AY ID TTP18AY TTP18AY TN Carboxypeptidase B2 (CPB2) TTP18AY UP Q96IY4 TTP18AY UC CBPB2_HUMAN TTP18AY BC Peptidase TTP18AY SN Thrombin-activable fibrinolysis inhibitor; TAFI; Plasma carboxypeptidase B; Carboxypeptidase U; CPU; CPB2 TTP18AY GN CPB2 TTP18AY FC Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down- regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. TTP18AY EC EC 3.4.17.20 TTP18AY PD 5HVH; 5HVG; 5HVF; 4P10; 3LMS TTP18AY SQ MKLCSLAVLVPIVLFCEQHVFAFQSGQVLAALPRTSRQVQVLQNLTTTYEIVLWQPVTADLIVKKKQVHFFVNASDVDNVKAHLNVSGIPCSVLLADVEDLIQQQISNDTVSPRASASYYEQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKEQAAKNAIWIDCGIHAREWISPAFCLWFIGHITQFYGIIGQYTNLLRLVDFYVMPVVNVDGYDYSWKKNRMWRKNRSFYANNHCIGTDLNRNFASKHWCEEGASSSSCSETYCGLYPESEPEVKAVASFLRRNINQIKAYISMHSYSQHIVFPYSYTRSKSKDHEELSLVASEAVRAIEKISKNTRYTHGHGSETLYLAPGGGDDWIYDLGIKYSFTIELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVIRNV TTP18AY TT Clinical trial TTP18AY KE hsa04610:Complement and coagulation cascades; hsa04972:Pancreatic secretion; hsa04974:Protein digestion and absorption TTP18AY RC R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins TTCQIBE ID TTCQIBE TTCQIBE TN Caspase-1 (CASP1) TTCQIBE UP P29466 TTCQIBE UC CASP1_HUMAN TTCQIBE BC Peptidase TTCQIBE SN P45; Interleukin-1 beta-converting enzyme; Interleukin-1 beta converting enzyme; Interleukin-1 beta convertase; IL1BCE; IL1BC; IL-1BC; IL-1 beta-converting enzyme; IL-1 beta converting enzyme; ICE; CASP-1 TTCQIBE GN CASP1 TTCQIBE FC Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive. Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. TTCQIBE EC EC 3.4.22.36 TTCQIBE SQ MADKVLKEKRKLFIRSMGEGTINGLLDELLQTRVLNKEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLAGTLGLSADQTSGNYLNMQDSQGVLSSFPAPQAVQDNPAMPTSSGSEGNVKLCSLEEAQRIWKQKSAEIYPIMDKSSRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFMSHGIREGICGKKHSEQVPDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKDSVGVSGNLSLPTTEEFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDGRAQMPTTERVTLTRCFYLFPGH TTCQIBE TT Clinical trial TTCQIBE FM Peptidase TTCQIBE KE hsa04621:NOD-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05164:Influenza A TTCQIBE RC R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-448706:Interleukin-1 processing; R-HSA-844456:The NLRP3 inflammasome TTPF2QI ID TTPF2QI TTPF2QI TN Caspase-3 (CASP3) TTPF2QI UP P42574 TTPF2QI UC CASP3_HUMAN TTPF2QI BC Peptidase TTPF2QI SN Yama protein; SREBP cleavage activity 1; SCA-1; Protein Yama; Cysteine protease CPP32; Caspase 3; CPP32; CPP-32; CASP-3; Apopain TTPF2QI GN CASP3 TTPF2QI FC At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. Involved in the activation cascade of caspases responsible for apoptosis execution. TTPF2QI EC EC 3.4.22.56 TTPF2QI SQ MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH TTPF2QI TT Clinical trial TTPF2QI FM Peptidase TTPF2QI KE hsa04010:MAPK signaling pathway; hsa04115:p53 signaling pathway; hsa04210:Apoptosis; hsa04650:Natural killer cell mediated cytotoxicity; hsa04668:TNF signaling pathway; hsa04726:Serotonergic synapse; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05010:Alzheimer's disease; hsa05012:Parkinson's disease; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05016:Huntington's disease; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05168:Herpes simplex infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05416:Viral myocarditis TTPF2QI RC R-HSA-111463:SMAC binds to IAPs; R-HSA-111464:SMAC-mediated dissociation of IAP:caspase complexes; R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-205025:NADE modulates death signalling; R-HSA-211227:Activation of DNA fragmentation factor; R-HSA-264870:Caspase-mediated cleavage of cytoskeletal proteins TT36ETB ID TT36ETB TT36ETB TN Cathepsin L (CTSL) TT36ETB UP P07711 TT36ETB UC CATL1_HUMAN TT36ETB BC Peptidase TT36ETB SN Major excreted protein; MEP; Cathepsin L1; CTSL1 TT36ETB GN CTSL TT36ETB FC Important for the overall degradation of proteins in lysosomes. TT36ETB EC EC 3.4.22.15 TT36ETB PD 6F06; 6EZX; 6EZP; 5MQY; 5MAJ TT36ETB SQ MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV TT36ETB TT Clinical trial TT36ETB FM Peptidase TT36ETB KE hsa04142:Lysosome; hsa04145:Phagosome; hsa04612:Antigen processing and presentation; hsa05205:Proteoglycans in cancer; hsa05323:Rheumatoid arthritis TT36ETB RC R-HSA-1236977:Endosomal/Vacuolar pathway; R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures; R-HSA-2132295:MHC class II antigen presentation TTUMQVO ID TTUMQVO TTUMQVO TN Cathepsin S (CTSS) TTUMQVO UP P25774 TTUMQVO UC CATS_HUMAN TTUMQVO BC Peptidase TTUMQVO SN Cysteine protease cathepsin S TTUMQVO GN CTSS TTUMQVO FC Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L. Thiol protease. TTUMQVO EC EC 3.4.22.27 TTUMQVO PD 5QCJ; 5QCI; 5QCH; 5QCG; 5QCF TTUMQVO SQ MKRLVCVLLVCSSAVAQLHKDPTLDHHWHLWKKTYGKQYKEKNEEAVRRLIWEKNLKFVMLHNLEHSMGMHSYDLGMNHLGDMTSEEVMSLMSSLRVPSQWQRNITYKSNPNRILPDSVDWREKGCVTEVKYQGSCGACWAFSAVGALEAQLKLKTGKLVSLSAQNLVDCSTEKYGNKGCNGGFMTTAFQYIIDNKGIDSDASYPYKAMDQKCQYDSKYRAATCSKYTELPYGREDVLKEAVANKGPVSVGVDARHPSFFLYRSGVYYEPSCTQNVNHGVLVVGYGDLNGKEYWLVKNSWGHNFGEEGYIRMARNKGNHCGIASFPSYPEI TTUMQVO TT Clinical trial TTUMQVO FM Peptidase TTUMQVO KE hsa04142:Lysosome; hsa04145:Phagosome; hsa04612:Antigen processing and presentation; hsa05152:Tuberculosis TTUMQVO RC R-HSA-1236977:Endosomal/Vacuolar pathway; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures; R-HSA-2132295:MHC class II antigen presentation TTC24WT ID TTC24WT TTC24WT TN C-C chemokine receptor type 1 (CCR1) TTC24WT UP P32246 TTC24WT UC CCR1_HUMAN TTC24WT BC GPCR rhodopsin TTC24WT SN SCYAR1; RANTES-R; Macrophage inflammatory protein-1 alpha receptor; Macrophage inflammatory protein 1-alpha receptor; MIP-1alpha-R; LD78 receptor; HM145; Chemokine receptor CCR1; CMKR1; CMKBR1; CD191; CCR-1; CC-CKR-1; C-C CKR-1 TTC24WT GN CCR1 TTC24WT FC Binds to MIP-1-alpha, MIP-1-delta, RANTES, and MCP-3 and, less efficiently, to MIP-1-beta or MCP-1 and subsequently transduces a signal by increasing the intracellular calcium ions level. Responsible for affecting stem cell proliferation. Receptor for a C-C type chemokine. TTC24WT PD 1Y5D TTC24WT SQ METPNTTEDYDTTTEFDYGDATPCQKVNERAFGAQLLPPLYSLVFVIGLVGNILVVLVLVQYKRLKNMTSIYLLNLAISDLLFLFTLPFWIDYKLKDDWVFGDAMCKILSGFYYTGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGVITSIIIWALAILASMPGLYFSKTQWEFTHHTCSLHFPHESLREWKLFQALKLNLFGLVLPLLVMIICYTGIIKILLRRPNEKKSKAVRLIFVIMIIFFLFWTPYNLTILISVFQDFLFTHECEQSRHLDLAVQVTEVIAYTHCCVNPVIYAFVGERFRKYLRQLFHRRVAVHLVKWLPFLSVDRLERVSSTSPSTGEHELSAGF TTC24WT TT Clinical trial TTC24WT FM GPCR rhodopsin TTC24WT KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway TTC24WT RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTFZYTO ID TTFZYTO TTFZYTO TN C-C chemokine receptor type 2 (CCR2) TTFZYTO UP P41597 TTFZYTO UC CCR2_HUMAN TTFZYTO BC GPCR rhodopsin TTFZYTO SN Monocyte chemoattractant protein 1 receptor; MCP-1-R; Chemokine receptor CCR2B; CMKBR2; CD192; CCR-2; CC-CKR-2; C-C CKR-2 TTFZYTO GN CCR2 TTFZYTO FC Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion. Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B. Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation. Faciltates the export of mature thymocytes by enhancing directional movement of thymocytes to sphingosine-1-phosphate stimulation and up-regulation of S1P1R expression; signals through the JAK-STAT pathway to regulate FOXO1 activity leading to an increased expression of S1P1R. Plays an important role in mediating peripheral nerve injury-induced neuropathic pain. Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B. Mediates the recruitment of macrophages and monocytes to the injury site following brain injury. Key functional receptor for CCL2 but can also bind CCL7 and CCL12. TTFZYTO PD 5T1A; 2MLQ; 2MLO; 1KP1; 1KAD TTFZYTO SQ MLSTSRSRFIRNTNESGEEVTTFFDYDYGAPCHKFDVKQIGAQLLPPLYSLVFIFGFVGNMLVVLILINCKKLKCLTDIYLLNLAISDLLFLITLPLWAHSAANEWVFGNAMCKLFTGLYHIGYFGGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWLVAVFASVPGIIFTKCQKEDSVYVCGPYFPRGWNNFHTIMRNILGLVLPLLIMVICYSGILKTLLRCRNEKKRHRAVRVIFTIMIVYFLFWTPYNIVILLNTFQEFFGLSNCESTSQLDQATQVTETLGMTHCCINPIIYAFVGEKFRSLFHIALGCRIAPLQKPVCGGPGVRPGKNVKVTTQGLLDGRGKGKSIGRAPEASLQDKEGA TTFZYTO TT Clinical trial TTFZYTO KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway TTFZYTO RC R-HSA-1461957:Beta defensins; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTN6Y9A ID TTN6Y9A TTN6Y9A TN CD40L receptor (CD40) TTN6Y9A UP P25942 TTN6Y9A UC TNR5_HUMAN TTN6Y9A BC Cytokine receptor TTN6Y9A SN Tumor necrosis factor receptor superfamily member 5; TNFRSF5; CDw40; Bp50; B-cell surfaceantigen CD40; B-cell surface antigen CD40 TTN6Y9A GN CD40 TTN6Y9A FC Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion. Receptor for TNFSF5/CD40LG. TTN6Y9A PD 6FAX; 5IHL; 5DMJ; 5DMI; 3QD6 TTN6Y9A SQ MVRLPLQCVLWGCLLTAVHPEPPTACREKQYLINSQCCSLCQPGQKLVSDCTEFTETECLPCGESEFLDTWNRETHCHQHKYCDPNLGLRVQQKGTSETDTICTCEEGWHCTSEACESCVLHRSCSPGFGVKQIATGVSDTICEPCPVGFFSNVSSAFEKCHPWTSCETKDLVVQQAGTNKTDVVCGPQDRLRALVVIPIIFGILFAILLVLVFIKKVAKKPTNKAPHPKQEPQEINFPDDLPGSNTAAPVQETLHGCQPVTQEDGKESRISVQERQ TTN6Y9A TT Clinical trial TTN6Y9A FM Cytokine receptor TTN6Y9A KE hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04514:Cell adhesion molecules (CAMs); hsa04620:Toll-like receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05202:Transcriptional misregulation in cancer; hsa05310:Asthma; hsa05320:Autoimmune thyroid disease; hsa05322:Systemic lupus erythematosus; hsa05330:Allograft rejection; hsa05340:Primary immunodeficiency; hsa05416:Viral myocarditis TT7SBF5 ID TT7SBF5 TT7SBF5 TN Cellular tumor antigen p53 (TP53) TT7SBF5 UP P04637 TT7SBF5 UC P53_HUMAN TT7SBF5 SN Tumor suppressor p53; Phosphoprotein p53; P53; Antigen NY-CO-13 TT7SBF5 GN TP53 TT7SBF5 FC Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2. Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. TT7SBF5 PD 6GGF; 6GGE; 6GGD; 6GGC; 6GGB TT7SBF5 SQ MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD TT7SBF5 TT Clinical trial TT7SBF5 FM Zinc finger TT7SBF5 KE hsa04010:MAPK signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04310:Wnt signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05016:Huntington's disease; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05217:Basal cell carcinoma; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer TT7SBF5 RC R-HSA-111448:Activation of NOXA and translocation to mitochondria; R-HSA-139915:Activation of PUMA and translocation to mitochondria; R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559584:Formation of Senescence-Associated Heterochromatin Foci (SAHF); R-HSA-2559585:Oncogene Induced Senescence; R-HSA-2559586:DNA Damage/Telomere Stress Induced Senescence; R-HSA-349425:Autodegradation of the E3 ubiquitin ligase COP1; R-HSA-5628897:TP53 Regulates Metabolic Genes; R-HSA-5693565:Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks; R-HSA-69541:Stabilization of p53; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTFQAYR ID TTFQAYR TTFQAYR TN Cholesteryl ester transfer protein (CETP) TTFQAYR UP P11597 TTFQAYR UC CETP_HUMAN TTFQAYR BC Bactericidal permeability increasing protein TTFQAYR SN Lipid transfer protein I; Cholesterol ester transfer protein TTFQAYR GN CETP TTFQAYR FC Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL. Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination. Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. TTFQAYR PD 4F2A; 4EWS; 2OBD TTFQAYR SQ MLAATVLTLALLGNAHACSKGTSHEAGIVCRITKPALLVLNHETAKVIQTAFQRASYPDITGEKAMMLLGQVKYGLHNIQISHLSIASSQVELVEAKSIDVSIQNVSVVFKGTLKYGYTTAWWLGIDQSIDFEIDSAIDLQINTQLTCDSGRVRTDAPDCYLSFHKLLLHLQGEREPGWIKQLFTNFISFTLKLVLKGQICKEINVISNIMADFVQTRAASILSDGDIGVDISLTGDPVITASYLESHHKGHFIYKNVSEDLPLPTFSPTLLGDSRMLYFWFSERVFHSLAKVAFQDGRLMLSLMGDEFKAVLETWGFNTNQEIFQEVVGGFPSQAQVTVHCLKMPKISCQNKGVVVNSSVMVKFLFPRPDQQHSVAYTFEEDIVTTVQASYSKKKLFLSLLDFQITPKTVSNLTESSSESVQSFLQSMITAVGIPEVMSRLEVVFTALMNSKGVSLFDIINPEIITRDGFLLLQMDFGFPEHLLVDFLQSLS TTFQAYR TT Clinical trial TTFQAYR FM Bactericidal permeability increasing protein TTFQAYR RC R-HSA-171052:LDL-mediated lipid transport; R-HSA-194223:HDL-mediated lipid transport TT9H85R ID TT9H85R TT9H85R TN Corticosteroid 11-beta-dehydrogenase 2 (HSD11B2) TT9H85R UP P80365 TT9H85R UC DHI2_HUMAN TT9H85R BC Short-chain dehydrogenases reductase TT9H85R SN NAD-dependent 11-beta-hydroxysteroid dehydrogenase; HSD11B2; 11-beta-hydroxysteroid dehydrogenase type 2; 11-beta-HSD2; 11-DH2; 11 beta-hydroxysteroid dehydrogenase type 2; 11 beta-HSD2 TT9H85R GN HSD11B2 TT9H85R FC Catalyzes the conversion of cortisol to the inactive metabolite cortisone. modulates intracellular glucocorticoid levels, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids. TT9H85R EC EC 1.1.1.- TT9H85R SQ MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALAVLAAAGWIALSRLARPQRLPVATRAVLITGCDSGFGKETAKKLDSMGFTVLATVLELNSPGAIELRTCCSPRLRLLQMDLTKPGDISRVLEFTKAHTTSTGLWGLVNNAGHNEVVADAELSPVATFRSCMEVNFFGALELTKGLLPLLRSSRGRIVTVGSPAGDMPYPCLGAYGTSKAAVALLMDTFSCELLPWGVKVSIIQPGCFKTESVRNVGQWEKRKQLLLANLPQELLQAYGKDYIEHLHGQFLHSLRLAMSDLTPVVDAITDALLAARPRRRYYPGQGLGLMYFIHYYLPEGLRRRFLQAFFISHCLPRALQPGQPGTTPPQDAAQDPNLSPGPSPAVAR TT9H85R TT Clinical trial TT9H85R KE hsa00140:Steroid hormone biosynthesis; hsa04960:Aldosterone-regulated sodium reabsorption TT9H85R RC R-HSA-194002:Glucocorticoid biosynthesis TTZF0K2 ID TTZF0K2 TTZF0K2 TN C-X-C motif chemokine 2 (CXCL2) TTZF0K2 UP P19875 TTZF0K2 UC CXCL2_HUMAN TTZF0K2 BC Cytokine: CXC chemokine TTZF0K2 SN SCYB2; Macrophage inflammatory protein 2-alpha; MIP2A; MIP2-alpha; Growth-regulated protein beta; Growth regulatedprotein beta; Gro-beta; GROB; GRO2 TTZF0K2 GN CXCL2 TTZF0K2 FC Hematoregulatory chemokine, which, in vitro, suppresses hematopoietic progenitor cell proliferation. GRO-beta(5-73) shows a highly enhanced hematopoietic activity. Produced by activated monocytes and neutrophils and expressed at sites of inflammation. TTZF0K2 PD 5OB5; 1QNK TTZF0K2 SQ MARATLSAAPSNPRLLRVALLLLLLVAASRRAAGAPLATELRCQCLQTLQGIHLKNIQSVKVKSPGPHCAQTEVIATLKNGQKACLNPASPMVKKIIEKMLKNGKSN TTZF0K2 TT Clinical trial TTZF0K2 FM Intercrine-alpha family TTZF0K2 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa05132:Salmonella infection; hsa05134:Legionellosis TTZF0K2 RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTQYF7G ID TTQYF7G TTQYF7G TN Cyclin-dependent kinase 7 (CDK7) TTQYF7G UP P50613 TTQYF7G UC CDK7_HUMAN TTQYF7G BC Kinase TTQYF7G SN TFIIH basal transcription factor complex kinase subunit; Serine/threonine-protein kinase 1; P39 Mo15; MO15; Cell division protein kinase 7; CDKN7; CDK-activating kinase 1; CDK-activating kinase; CAK1; CAK; 39 kDa protein kinase TTQYF7G GN CDK7 TTQYF7G FC Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition. Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. TTQYF7G EC EC 2.7.11.22 TTQYF7G PD 2HIC; 1UA2; 1PA8; 1LG3 TTQYF7G SQ MALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSNRPGPTPGCQLPRPNCPVETLKEQSNPALAIKRKRTEALEQGGLPKKLIF TTQYF7G TT Clinical trial TTQYF7G FM Kinase TTQYF7G KE hsa03022:Basal transcription factors; hsa03420:Nucleotide excision repair; hsa04110:Cell cycle TTQYF7G RC R-HSA-427413:NoRC negatively regulates rRNA expression; R-HSA-6781823:Formation of TC-NER Pre-Incision Complex; R-HSA-6782135:Dual incision in TC-NER; R-HSA-6782210:Gap-filling DNA repair synthesis and ligation in TC-NER; R-HSA-69202:Cyclin E associated events during G1/S transition; R-HSA-69231:Cyclin D associated events in G1; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition; R-HSA-69656:Cyclin A:Cdk2-associated events at S phase entry; R-HSA-73762:RNA Polymerase I Transcription Initiation TTI84H7 ID TTI84H7 TTI84H7 TN Cytochrome P450 1B1 (CYP1B1) TTI84H7 UP Q16678 TTI84H7 UC CP1B1_HUMAN TTI84H7 BC Paired donor oxygen oxidoreductase TTI84H7 SN CYPIB1 TTI84H7 GN CYP1B1 TTI84H7 FC In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression. Cytochromes P450 are a group of heme-thiolate monooxygenases. TTI84H7 EC EC 1.14.14.- TTI84H7 PD 6IQ5; 3PM0 TTI84H7 SQ MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLIGNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAFASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVALLVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSLVDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSAEKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAELDQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVVFVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQLFLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKETCQ TTI84H7 TT Clinical trial TTI84H7 FM Oxidoreductases acting on paired donors TTI84H7 KE hsa00140:Steroid hormone biosynthesis; hsa00380:Tryptophan metabolism; hsa00980:Metabolism of xenobiotics by cytochrome P450; hsa04913:Ovarian steroidogenesis; hsa05204:Chemical carcinogenesis; hsa05206:MicroRNAs in cancer TTI84H7 RC R-HSA-211976:Endogenous sterols TT4H0V2 ID TT4H0V2 TT4H0V2 TN Dipeptidyl peptidase I (CTSC) TT4H0V2 UP P53634 TT4H0V2 UC CATC_HUMAN TT4H0V2 BC Peptidase TT4H0V2 SN Dipeptidyl transferase; Dipeptidyl peptidase 1; DPPI; DPP-I; Cysteine protease dipeptidyl peptidase I; Cathepsin J; Cathepsin C; CPPI TT4H0V2 GN CTSC TT4H0V2 FC Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII. Thiol protease. TT4H0V2 EC EC 3.4.14.1 TT4H0V2 PD 4OEM; 4OEL; 4CDF; 4CDE; 4CDD TT4H0V2 SQ MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL TT4H0V2 TT Clinical trial TT4H0V2 FM Peptidase TT4H0V2 KE hsa04142:Lysosome TT4H0V2 RC R-HSA-204005:COPII (Coat Protein 2) Mediated Vesicle Transport; R-HSA-2132295:MHC class II antigen presentation; R-HSA-5694530:Cargo concentration in the ER TT6S2FE ID TT6S2FE TT6S2FE TN DNA [cytosine-5]-methyltransferase 1 (DNMT1) TT6S2FE UP P26358 TT6S2FE UC DNMT1_HUMAN TT6S2FE BC Methyltransferase TT6S2FE SN MCMT; M.HsaI; Dnmt1; DNMT; DNA methyltransferase HsaI; DNA MTase HsaI; DNA (cytosine5)methyltransferase 1; DNA (cytosine-5)-methyltransferase 1; CXXCtype zinc finger protein 9; CXXC9; CXXC-type zinc finger protein 9; AIM TT6S2FE GN DNMT1 TT6S2FE FC Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. Promotes tumor growth. Methylates CpG residues. TT6S2FE EC EC 2.1.1.37 TT6S2FE PD 5YDR; 5WVO; 4Z97; 4Z96; 4YOC TT6S2FE SQ MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQLCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEKEEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD TT6S2FE TT Clinical trial TT6S2FE FM Methyltransferase superfamily TT6S2FE KE hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways; hsa05206:MicroRNAs in cancer TT6S2FE RC R-HSA-212300:PRC2 methylates histones and DNA; R-HSA-427413:NoRC negatively regulates rRNA expression; R-HSA-5334118:DNA methylation TT6VZ78 ID TT6VZ78 TT6VZ78 TN DNA [cytosine-5]-methyltransferase 3B (DNMT3B) TT6VZ78 UP Q9UBC3 TT6VZ78 UC DNM3B_HUMAN TT6VZ78 BC Methyltransferase TT6VZ78 SN M.HsaIIIB; Dnmt3b; DNA methyltransferase HsaIIIB; DNA methyltransferase 3B; DNA MTase HsaIIIB; DNA (cytosine-5)-methyltransferase 3B TT6VZ78 GN DNMT3B TT6VZ78 FC DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing. In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs. Function as transcriptional corepressor by associating with ZHX1. Required for DUX4 silencing in somatic cells. Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. TT6VZ78 EC EC 2.1.1.37 TT6VZ78 PD 5NVO; 5NV7; 5NV2; 5NV0; 5NRV TT6VZ78 SQ MKGDTRHLNGEEDAGGREDSILVNGACSDQSSDSPPILEAIRTPEIRGRRSSSRLSKREVSSLLSYTQDLTGDGDGEDGDGSDTPVMPKLFRETRTRSESPAVRTRNNNSVSSRERHRPSPRSTRGRQGRNHVDESPVEFPATRSLRRRATASAGTPWPSPPSSYLTIDLTDDTEDTHGTPQSSSTPYARLAQDSQQGGMESPQVEADSGDGDSSEYQDGKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRKAMYHALEKARVRAGKTFPSSPGDSLEDQLKPMLEWAHGGFKPTGIEGLKPNNTQPVVNKSKVRRAGSRKLESRKYENKTRRRTADDSATSDYCPAPKRLKTNCYNNGKDRGDEDQSREQMASDVANNKSSLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGTGTAAEAKLQEPWSCYMCLPQRCHGVLRRRKDWNVRLQAFFTSDTGLEYEAPKLYPAIPAARRRPIRVLSLFDGIATGYLVLKELGIKVGKYVASEVCEESIAVGTVKHEGNIKYVNDVRNITKKNIEEWGPFDLVIGGSPCNDLSNVNPARKGLYEGTGRLFFEFYHLLNYSRPKEGDDRPFFWMFENVVAMKVGDKRDISRFLECNPVMIDAIKVSAAHRARYFWGNLPGMNRPVIASKNDKLELQDCLEYNRIAKLKKVQTITTKSNSIKQGKNQLFPVVMNGKEDVLWCTELERIFGFPVHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE TT6VZ78 TT Clinical trial TT6VZ78 FM Methyltransferase superfamily TT6VZ78 KE hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways; hsa05206:MicroRNAs in cancer TT6VZ78 RC R-HSA-212300:PRC2 methylates histones and DNA; R-HSA-427413:NoRC negatively regulates rRNA expression; R-HSA-5334118:DNA methylation TTK3PY9 ID TTK3PY9 TTK3PY9 TN DNA-dependent protein kinase catalytic (PRKDC) TTK3PY9 UP P78527 TTK3PY9 UC PRKDC_HUMAN TTK3PY9 BC Kinase TTK3PY9 SN p460; HYRC1; HYRC; DNPK1; DNA-dependent protein kinase catalytic subunit; DNA-PKcs; DNA-PK catalytic subunit TTK3PY9 GN PRKDC TTK3PY9 FC Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D. Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. TTK3PY9 EC EC 2.7.11.1 TTK3PY9 PD 5Y3R; 5W1R; 5LUQ TTK3PY9 SQ MAGSGAGVRCSLLRLQETLSAADRCGAALAGHQLIRGLGQECVLSSSPAVLALQTSLVFSRDFGLLVFVRKSLNSIEFRECREEILKFLCIFLEKMGQKIAPYSVEIKNTCTSVYTKDRAAKCKIPALDLLIKLLQTFRSSRLMDEFKIGELFSKFYGELALKKKIPDTVLEKVYELLGLLGEVHPSEMINNAENLFRAFLGELKTQMTSAVREPKLPVLAGCLKGLSSLLCNFTKSMEEDPQTSREIFNFVLKAIRPQIDLKRYAVPSAGLRLFALHASQFSTCLLDNYVSLFEVLLKWCAHTNVELKKAALSALESFLKQVSNMVAKNAEMHKNKLQYFMEQFYGIIRNVDSNNKELSIAIRGYGLFAGPCKVINAKDVDFMYVELIQRCKQMFLTQTDTGDDRVYQMPSFLQSVASVLLYLDTVPEVYTPVLEHLVVMQIDSFPQYSPKMQLVCCRAIVKVFLALAAKGPVLRNCISTVVHQGLIRICSKPVVLPKGPESESEDHRASGEVRTGKWKVPTYKDYVDLFRHLLSSDQMMDSILADEAFFSVNSSSESLNHLLYDEFVKSVLKIVEKLDLTLEIQTVGEQENGDEAPGVWMIPTSDPAANLHPAKPKDFSAFINLVEFCREILPEKQAEFFEPWVYSFSYELILQSTRLPLISGFYKLLSITVRNAKKIKYFEGVSPKSLKHSPEDPEKYSCFALFVKFGKEVAVKMKQYKDELLASCLTFLLSLPHNIIELDVRAYVPALQMAFKLGLSYTPLAEVGLNALEEWSIYIDRHVMQPYYKDILPCLDGYLKTSALSDETKNNWEVSALSRAAQKGFNKVVLKHLKKTKNLSSNEAISLEEIRIRVVQMLGSLGGQINKNLLTVTSSDEMMKSYVAWDREKRLSFAVPFREMKPVIFLDVFLPRVTELALTASDRQTKVAACELLHSMVMFMLGKATQMPEGGQGAPPMYQLYKRTFPVLLRLACDVDQVTRQLYEPLVMQLIHWFTNNKKFESQDTVALLEAILDGIVDPVDSTLRDFCGRCIREFLKWSIKQITPQQQEKSPVNTKSLFKRLYSLALHPNAFKRLGASLAFNNIYREFREEESLVEQFVFEALVIYMESLALAHADEKSLGTIQQCCDAIDHLCRIIEKKHVSLNKAKKRRLPRGFPPSASLCLLDLVKWLLAHCGRPQTECRHKSIELFYKFVPLLPGNRSPNLWLKDVLKEEGVSFLINTFEGGGCGQPSGILAQPTLLYLRGPFSLQATLCWLDLLLAALECYNTFIGERTVGALQVLGTEAQSSLLKAVAFFLESIAMHDIIAAEKCFGTGAAGNRTSPQEGERYNYSKCTVVVRIMEFTTTLLNTSPEGWKLLKKDLCNTHLMRVLVQTLCEPASIGFNIGDVQVMAHLPDVCVNLMKALKMSPYKDILETHLREKITAQSIEELCAVNLYGPDAQVDRSRLAAVVSACKQLHRAGLLHNILPSQSTDLHHSVGTELLSLVYKGIAPGDERQCLPSLDLSCKQLASGLLELAFAFGGLCERLVSLLLNPAVLSTASLGSSQGSVIHFSHGEYFYSLFSETINTELLKNLDLAVLELMQSSVDNTKMVSAVLNGMLDQSFRERANQKHQGLKLATTILQHWKKCDSWWAKDSPLETKMAVLALLAKILQIDSSVSFNTSHGSFPEVFTTYISLLADTKLDLHLKGQAVTLLPFFTSLTGGSLEELRRVLEQLIVAHFPMQSREFPPGTPRFNNYVDCMKKFLDALELSQSPMLLELMTEVLCREQQHVMEELFQSSFRRIARRGSCVTQVGLLESVYEMFRKDDPRLSFTRQSFVDRSLLTLLWHCSLDALREFFSTIVVDAIDVLKSRFTKLNESTFDTQITKKMGYYKILDVMYSRLPKDDVHAKESKINQVFHGSCITEGNELTKTLIKLCYDAFTENMAGENQLLERRRLYHCAAYNCAISVICCVFNELKFYQGFLFSEKPEKNLLIFENLIDLKRRYNFPVEVEVPMERKKKYIEIRKEAREAANGDSDGPSYMSSLSYLADSTLSEEMSQFDFSTGVQSYSYSSQDPRPATGRFRRREQRDPTVHDDVLELEMDELNRHECMAPLTALVKHMHRSLGPPQGEEDSVPRDLPSWMKFLHGKLGNPIVPLNIRLFLAKLVINTEEVFRPYAKHWLSPLLQLAASENNGGEGIHYMVVEIVATILSWTGLATPTGVPKDEVLANRLLNFLMKHVFHPKRAVFRHNLEIIKTLVECWKDCLSIPYRLIFEKFSGKDPNSKDNSVGIQLLGIVMANDLPPYDPQCGIQSSEYFQALVNNMSFVRYKEVYAAAAEVLGLILRYVMERKNILEESLCELVAKQLKQHQNTMEDKFIVCLNKVTKSFPPLADRFMNAVFFLLPKFHGVLKTLCLEVVLCRVEGMTELYFQLKSKDFVQVMRHRDDERQKVCLDIIYKMMPKLKPVELRELLNPVVEFVSHPSTTCREQMYNILMWIHDNYRDPESETDNDSQEIFKLAKDVLIQGLIDENPGLQLIIRNFWSHETRLPSNTLDRLLALNSLYSPKIEVHFLSLATNFLLEMTSMSPDYPNPMFEHPLSECEFQEYTIDSDWRFRSTVLTPMFVETQASQGTLQTRTQEGSLSARWPVAGQIRATQQQHDFTLTQTADGRSSFDWLTGSSTDPLVDHTSPSSDSLLFAHKRSERLQRAPLKSVGPDFGKKRLGLPGDEVDNKVKGAAGRTDLLRLRRRFMRDQEKLSLMYARKGVAEQKREKEIKSELKMKQDAQVVLYRSYRHGDLPDIQIKHSSLITPLQAVAQRDPIIAKQLFSSLFSGILKEMDKFKTLSEKNNITQKLLQDFNRFLNTTFSFFPPFVSCIQDISCQHAALLSLDPAAVSAGCLASLQQPVGIRLLEEALLRLLPAELPAKRVRGKARLPPDVLRWVELAKLYRSIGEYDVLRGIFTSEIGTKQITQSALLAEARSDYSEAAKQYDEALNKQDWVDGEPTEAEKDFWELASLDCYNHLAEWKSLEYCSTASIDSENPPDLNKIWSEPFYQETYLPYMIRSKLKLLLQGEADQSLLTFIDKAMHGELQKAILELHYSQELSLLYLLQDDVDRAKYYIQNGIQSFMQNYSSIDVLLHQSRLTKLQSVQALTEIQEFISFISKQGNLSSQVPLKRLLNTWTNRYPDAKMDPMNIWDDIITNRCFFLSKIEEKLTPLPEDNSMNVDQDGDPSDRMEVQEQEEDISSLIRSCKFSMKMKMIDSARKQNNFSLAMKLLKELHKESKTRDDWLVSWVQSYCRLSHCRSRSQGCSEQVLTVLKTVSLLDENNVSSYLSKNILAFRDQNILLGTTYRIIANALSSEPACLAEIEEDKARRILELSGSSSEDSEKVIAGLYQRAFQHLSEAVQAAEEEAQPPSWSCGPAAGVIDAYMTLADFCDQQLRKEEENASVIDSAELQAYPALVVEKMLKALKLNSNEARLKFPRLLQIIERYPEETLSLMTKEISSVPCWQFISWISHMVALLDKDQAVAVQHSVEEITDNYPQAIVYPFIISSESYSFKDTSTGHKNKEFVARIKSKLDQGGVIQDFINALDQLSNPELLFKDWSNDVRAELAKTPVNKKNIEKMYERMYAALGDPKAPGLGAFRRKFIQTFGKEFDKHFGKGGSKLLRMKLSDFNDITNMLLLKMNKDSKPPGNLKECSPWMSDFKVEFLRNELEIPGQYDGRGKPLPEYHVRIAGFDERVTVMASLRRPKRIIIRGHDEREHPFLVKGGEDLRQDQRVEQLFQVMNGILAQDSACSQRALQLRTYSVVPMTSRLGLIEWLENTVTLKDLLLNTMSQEEKAAYLSDPRAPPCEYKDWLTKMSGKHDVGAYMLMYKGANRTETVTSFRKRESKVPADLLKRAFVRMSTSPEAFLALRSHFASSHALICISHWILGIGDRHLNNFMVAMETGGVIGIDFGHAFGSATQFLPVPELMPFRLTRQFINLMLPMKETGLMYSIMVHALRAFRSDPGLLTNTMDVFVKEPSFDWKNFEQKMLKKGGSWIQEINVAEKNWYPRQKICYAKRKLAGANPAVITCDELLLGHEKAPAFRDYVAVARGSKDHNIRAQEPESGLSEETQVKCLMDQATDPNILGRTWEGWEPWM TTK3PY9 TT Clinical trial TTK3PY9 FM Kinase TTK3PY9 KE hsa03450:Non-homologous end-joining; hsa04110:Cell cycle TTK3PY9 RC R-HSA-5693571:Nonhomologous End-Joining (NHEJ) TTG8HIM ID TTG8HIM TTG8HIM TN Dual specificity protein phosphatase 1 (DUSP1) TTG8HIM UP P28562 TTG8HIM UC DUS1_HUMAN TTG8HIM BC Phosphoric monoester hydrolase TTG8HIM SN VH1; Protein-tyrosine phosphatase CL100; PTPN10; Mitogen-activated protein kinase phosphatase 1; MKP1; MKP-1; MAP kinase phosphatase-1; MAP kinase phosphatase 1; Dual specificity protein phosphatase hVH1; CL100 TTG8HIM GN DUSP1 TTG8HIM FC Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle. TTG8HIM EC EC 3.1.3.16 TTG8HIM PD 6D67; 6D66; 6D65; 6APX TTG8HIM SQ MVMEVGTLDAGGLRALLGERAAQCLLLDCRSFFAFNAGHIAGSVNVRFSTIVRRRAKGAMGLEHIVPNAELRGRLLAGAYHAVVLLDERSAALDGAKRDGTLALAAGALCREARAAQVFFLKGGYEAFSASCPELCSKQSTPMGLSLPLSTSVPDSAESGCSSCSTPLYDQGGPVEILPFLYLGSAYHASRKDMLDALGITALINVSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDFIDSIKNAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAPHCSAEAGSPAMAVLDRGTSTTTVFNFPVSIPVHSTNSALSYLQSPITTSPSC TTG8HIM TT Clinical trial TTG8HIM FM Phosphoric monoester hydrolases TTG8HIM KE hsa04010:MAPK signaling pathway; hsa04726:Serotonergic synapse TTG8HIM RC R-HSA-112409:RAF-independent MAPK1/3 activation; R-HSA-5675221:Negative regulation of MAPK pathway TTW26OG ID TTW26OG TTW26OG TN Endoplasmic reticulum chaperone BiP (HSPA5) TTW26OG UP P11021 TTW26OG UC BIP_HUMAN TTW26OG BC Acid anhydride hydrolase TTW26OG SN Immunoglobulin heavy chainbinding protein; Immunoglobulin heavy chain-binding protein; Heat shock protein family A member 5; Heat shock protein 70 family protein 5; Heat shock 70 kDa protein 5; HSP70 family protein 5; GRP78; GRP-78; Endoplasmic reticulum lumenal Ca(2+)binding protein grp78; Binding-immunoglobulin protein; BiP; 78 kDa glucose-regulated protein TTW26OG GN HSPA5 TTW26OG FC Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1. Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. TTW26OG EC EC 3.6.4.10 TTW26OG PD 6DFO; 6DFM; 6CZ1; 6ASY; 5F2R TTW26OG SQ MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL TTW26OG TT Clinical trial TTW26OG FM Heat shock protein TTW26OG KE hsa03060:Protein export; hsa04141:Protein processing in endoplasmic reticulum; hsa04612:Antigen processing and presentation; hsa04918:Thyroid hormone synthesis; hsa05020:Prion diseases TTW26OG RC R-HSA-114608:Platelet degranulation; R-HSA-3371453:Regulation of HSF1-mediated heat shock response TTTO43N ID TTTO43N TTTO43N TN Endothelial plasminogen activator inhibitor (SERPINE1) TTTO43N UP P05121 TTTO43N UC PAI1_HUMAN TTTO43N BC Serpin protein TTTO43N SN Serpin E1; Plasminogen activator inhibitor type 1; Plasminogen activator inhibitor 1; PLANH1; PAI1; PAI-1 TTTO43N GN SERPINE1 TTTO43N FC Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair. It is involved in cellular and replicative senescence. Plays a role in alveolar type 2 cells senescence in the lung. Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis. Serine protease inhibitor. TTTO43N PD 9PAI; 6I8S; 5ZLZ; 5BRR; 4IC0 TTTO43N SQ MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP TTTO43N TT Clinical trial TTTO43N FM Serpin family TTTO43N KE hsa04066:HIF-1 signaling pathway; hsa04115:p53 signaling pathway; hsa04390:Hippo signaling pathway; hsa04610:Complement and coagulation cascades; hsa05142:Chagas disease (American trypanosomiasis) TTTO43N RC R-HSA-114608:Platelet degranulation; R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-2173796:SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription; R-HSA-3000178:ECM proteoglycans; R-HSA-75205:Dissolution of Fibrin Clot TT9MZCQ ID TT9MZCQ TT9MZCQ TN Enhancer of zeste homolog 2 (EZH2) TT9MZCQ UP Q15910 TT9MZCQ UC EZH2_HUMAN TT9MZCQ BC Methyltransferase TT9MZCQ SN Lysine Nmethyltransferase 6; Lysine N-methyltransferase 6; KMT6; Histonelysine Nmethyltransferase EZH2; Histone-lysine N-methyltransferase EZH2; EZH2; ENX1; ENX-1 TT9MZCQ GN EZH2 TT9MZCQ FC Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2. Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-ARNTL/BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription. Polycomb group (PcG) protein. TT9MZCQ EC EC 2.1.1.43 TT9MZCQ PD 6C24; 6C23; 5WUK; 5WG6; 5U62 TT9MZCQ SQ MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP TT9MZCQ TT Successful TT9MZCQ FM Methyltransferase superfamily TT9MZCQ KE hsa05206:MicroRNAs in cancer TT9MZCQ RC R-HSA-212300:PRC2 methylates histones and DNA; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-3214841:PKMTs methylate histone lysines TTKPV6O ID TTKPV6O TTKPV6O TN Ephrin type-B receptor 2 (EPHB2) TTKPV6O UP P29323 TTKPV6O UC EPHB2_HUMAN TTKPV6O BC Kinase TTKPV6O SN hEK5; Tyrosine-protein kinase receptor EPH-3; Tyrosine-protein kinase TYRO5; TYRO5; Renal carcinoma antigen NY-REN-47; Receptor protein-tyrosine kinase HEK5; EphB2 receptor tyrosine kinase; EphB2; EPTH3; EPHT3; EPH-like kinase 5; EPH tyrosine kinase 3; ELK-related tyrosine kinase; EK5; Developmentally-regulated Eph-related tyrosine kinase; DRT TTKPV6O GN EPHB2 TTKPV6O FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Functions in axon guidance during development. Involved in the guidance of commissural axons, that form a major interhemispheric connection between the 2 temporal lobes of the cerebral cortex. Also involved in guidance of contralateral inner ear efferent growth cones at the midline and of retinal ganglion cell axons to the optic disk. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses. Upon activation by EFNB1, abolishes the ARHGEF15-mediated negative regulation on excitatory synapse formation. Controls other aspects of development including angiogenesis, palate development and in inner ear development through regulation of endolymph production. Forward and reverse signaling through the EFNB2/EPHB2 complex regulate movement and adhesion of cells that tubularize the urethra and septate the cloaca. May function as a tumor suppressor. Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TTKPV6O EC EC 2.7.10.1 TTKPV6O PD 3ZFM; 2QBX; 1F0M; 1B4F TTKPV6O SQ MALRRLGAALLLLPLLAAVEETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKFIRRRGAHRIHVEMKFSVRDCSSIPSVPGSCKETFNLYYYEADFDSATKTFPNWMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRSGFYLAFQDYGGCMSLIAVRVFYRKCPRIIQNGAIFQETLSGAESTSLVAARGSCIANAEEVDVPIKLYCNGDGEWLVPIGRCMCKAGFEAVENGTVCRGCPSGTFKANQGDEACTHCPINSRTTSEGATNCVCRNGYYRADLDPLDMPCTTIPSAPQAVISSVNETSLMLEWTPPRDSGGREDLVYNIICKSCGSGRGACTRCGDNVQYAPRQLGLTEPRIYISDLLAHTQYTFEIQAVNGVTDQSPFSPQFASVNITTNQAAPSAVSIMHQVSRTVDSITLSWSQPDQPNGVILDYELQYYEKELSEYNATAIKSPTNTVTVQGLKAGAIYVFQVRARTVAGYGRYSGKMYFQTMTEAEYQTSIQEKLPLIIGSSAAGLVFLIAVVVIAIVCNRRGFERADSEYTDKLQHYTSGHMTPGMKIYIDPFTYEDPNEAVREFAKEIDISCVKIEQVIGAGEFGEVCSGHLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNVIHLEGVVTKSTPVMIITEFMENGSLDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLADMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYTSALGGKIPIRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMTNQDVINAIEQDYRLPPPMDCPSALHQLMLDCWQKDRNHRPKFGQIVNTLDKMIRNPNSLKAMAPLSSGINLPLLDRTIPDYTSFNTVDEWLEAIKMGQYKESFANAGFTSFDVVSQMMMEDILRVGVTLAGHQKKILNSIQVMRAQMNQIQSVEGQPLARRPRATGRTKRCQPRDVTKKTCNSNDGKKKGMGKKKTDPGRGREIQGIFFKEDSHKESNDCSCGG TTKPV6O TT Clinical trial TTKPV6O FM Kinase TTKPV6O KE hsa04360:Axon guidance TTKPV6O RC R-HSA-2682334:EPH-Ephrin signaling; R-HSA-373760:L1CAM interactions; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TTDC8N2 ID TTDC8N2 TTDC8N2 TN Erbb3 tyrosine kinase receptor (Erbb-3) TTDC8N2 UP P21860 TTDC8N2 UC ERBB3_HUMAN TTDC8N2 BC Kinase TTDC8N2 SN Tyrosine kinase-type cell surface receptor HER3; Receptor tyrosine-protein kinase erbB-3; Proto-oncogene-like protein c-ErbB-3; HER3; C-erbB3; C-erbB-3 protein TTDC8N2 GN ERBB3 TTDC8N2 FC Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5. Involved in the regulation of myeloid cell differentiation. Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. TTDC8N2 EC EC 2.7.10.1 TTDC8N2 PD 5O7P; 5O4O; 5CUS; 4RIY; 4RIX TTDC8N2 SQ MRANDALQVLGLLFSLARGSEVGNSQAVCPGTLNGLSVTGDAENQYQTLYKLYERCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNGRSCPPCHEVCKGRCWGPGSEDCQTLTKTICAPQCNGHCFGPNPNQCCHDECAGGCSGPQDTDCFACRHFNDSGACVPRCPQPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTSCVRACPPDKMEVDKNGLKMCEPCGGLCPKACEGTGSGSRFQTVDSSNIDGFVNCTKILGNLDFLITGLNGDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRIYISANRQLCYHHSLNWTKVLRGPTEERLDIKHNRPRRDCVAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSRGGVCVTHCNFLNGEPREFAHEAECFSCHPECQPMEGTATCNGSGSDTCAQCAHFRDGPHCVSSCPHGVLGAKGPIYKYPDVQNECRPCHENCTQGCKGPELQDCLGQTLVLIGKTHLTMALTVIAGLVVIFMMLGGTFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFGVADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRESGPGIAPGPEPHGLTNKKLEEVELEPELDLDLDLEAEEDNLATTTLGSALSLPVGTLNRPRGSQSLLSPSSGYMPMNQGNLGESCQESAVSGSSERCPRPVSLHPMPRGCLASESSEGHVTGSEAELQEKVSMCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDVNGYVMPDTHLKGTPSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRRRRHSPPHPPRPSSLEELGYEYMDVGSDLSASLGSTQSCPLHPVPIMPTAGTTPDEDYEYMNRQRDGGGPGGDYAAMGACPASEQGYEEMRAFQGPGHQAPHVHYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT TTDC8N2 TT Clinical trial TTDC8N2 FM Kinase TTDC8N2 KE hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04144:Endocytosis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer TTDM4ZU ID TTDM4ZU TTDM4ZU TN Factor XI messenger RNA (F11 mRNA) TTDM4ZU UP P03951 TTDM4ZU UC FA11_HUMAN TTDM4ZU BC mRNA target TTDM4ZU SN Plasma thromboplastin antecedent (mRNA); PTA (mRNA); FXI (mRNA); Coagulation factor XI (mRNA) TTDM4ZU GN F11 TTDM4ZU FC Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. TTDM4ZU EC EC 3.4.21.27 TTDM4ZU PD 6R8X; 6I58; 6C0S; 6AOD; 5WB6 TTDM4ZU SQ MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV TTDM4ZU TT Clinical trial TTDM4ZU FM mRNA target TTDM4ZU KE hsa04610:Complement and coagulation cascades TTDM4ZU RC R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation TTRJSMV ID TTRJSMV TTRJSMV TN Factor XII messenger RNA (FA12 mRNA) TTRJSMV UP P00748 TTRJSMV UC FA12_HUMAN TTRJSMV BC mRNA target TTRJSMV SN Hageman factor (mRNA); HAF (mRNA); Coagulation factor XII (mRNA) TTRJSMV GN F12 TTRJSMV FC Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa. Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. TTRJSMV EC EC 3.4.21.38 TTRJSMV PD 6B77; 6B74; 4XE4; 4XDE; 4BDX TTRJSMV SQ MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS TTRJSMV TT Clinical trial TTRJSMV FM mRNA target TTRJSMV KE hsa04610:Complement and coagulation cascades TTRJSMV RC R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation TT1KX2S ID TT1KX2S TT1KX2S TN FGFR4 messenger RNA (FGFR4 mRNA) TT1KX2S UP P22455 TT1KX2S UC FGFR4_HUMAN TT1KX2S BC mRNA target TT1KX2S SN TKF (mRNA); JTK2 (mRNA); FGFR-4 (mRNA); CD334 (mRNA) TT1KX2S GN FGFR4 TT1KX2S FC Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling. Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. TT1KX2S EC EC 2.7.10.1 TT1KX2S PD 6JPJ; 5XFJ; 5XFF; 5NWZ; 5NUD TT1KX2S SQ MRLLLALLGVLLSVPGPPVLSLEASEEVELEPCLAPSLEQQEQELTVALGQPVRLCCGRAERGGHWYKEGSRLAPAGRVRGWRGRLEIASFLPEDAGRYLCLARGSMIVLQNLTLITGDSLTSSNDDEDPKSHRDPSNRHSYPQQAPYWTHPQRMEKKLHAVPAGNTVKFRCPAAGNPTPTIRWLKDGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENAVGSIRYNYLLDVLERSPHRPILQAGLPANTTAVVGSDVELLCKVYSDAQPHIQWLKHIVINGSSFGADGFPYVQVLKTADINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVLPEEDPTWTAAAPEARYTDIILYASGSLALAVLLLLAGLYRGQALHGRHPRPPATVQKLSRFPLARQFSLESGSSGKSSSSLVRGVRLSSSGPALLAGLVSLDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVRAEAFGMDPARPDQASTVAVKMLKDNASDKDLADLVSEMEVMKLIGRHKNIINLLGVCTQEGPLYVIVECAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPVLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDNVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMDRPPHCPPELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPSGGDASSTCSSSDSVFSHDPLPLGSSSFPFGSGVQT TT1KX2S TT Clinical trial TT1KX2S FM mRNA target TT1KX2S KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04810:Regulation of actin cytoskeleton TT1KX2S RC R-HSA-109704:PI3K Cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-190322:FGFR4 ligand binding and activation; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5654228:Phospholipase C-mediated cascade; R-HSA-5654712:FRS-mediated FGFR4 signaling; R-HSA-5654719:SHC-mediated cascade:FGFR4; R-HSA-5654720:PI-3K cascade:FGFR4; R-HSA-5654733:Negative regulation of FGFR4 signaling; R-HSA-5673001:RAF/MAP kinase cascade TTPJ921 ID TTPJ921 TTPJ921 TN Fibronectin (FN1) TTPJ921 UP P02751 TTPJ921 UC FINC_HUMAN TTPJ921 BC Fibronectin protein TTPJ921 SN FN; Cold-insoluble globulin; CIG TTPJ921 GN FN1 TTPJ921 FC Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts. TTPJ921 PD 6HNF; 5N48; 5N47; 5M0A; 5J7C TTPJ921 SQ MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHPQPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTRGGNSNGALCHFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDMGHMMRCTCVGNGRGEWTCIAYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDSWEKYVHGVRYQCYCYGRGIGEWHCQPLQTYPSSSGPVEVFITETPSQPNSHPIQWNAPQPSHISKYILRWRPKNSVGRWKEATIPGHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTSTPVTSNTVTGETTPFSPLVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDTTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPRDLQFVEVTDVKVTIMWTPPESAVTGYRVDVIPVNLPGEHGQRLPISRNTFAEVTGLSPGVTYYFKVFAVSHGRESKPLTAQQTTKLDAPTNLQFVNETDSTVLVRWTPPRAQITGYRLTVGLTRRGQPRQYNVGPSVSKYPLRNLQPASEYTVSLVAIKGNQESPKATGVFTTLQPGSSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYVYTIQVLRDGQERDAPIVNKVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGNSLEEVVHADQSSCTFDNLSPGLEYNVSVYTVKDDKESVPISDTIIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYVVSVSSVYEQHESTPLRGRQKTGLDSPTGIDFSDITANSFTVHWIAPRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTNLTPGTEYVVSIVALNGREESPLLIGQQSTVSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIDKPSQMQVTDVQDNSISVKWLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGEEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAIPAPTDLKFTQVTPTSLSAQWTPPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAVPANGQTPIQRTIKPDVRSYTITGLQPGTDYKIYLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLLVSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTSGQQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYPHGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLTGLTRGATYNVIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDEWERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGGEPSPEGTTGQSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE TTPJ921 TT Clinical trial TTPJ921 FM Fibronectin TTPJ921 KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04810:Regulation of actin cytoskeleton; hsa05100:Bacterial invasion of epithelial cells; hsa05146:Amoebiasis; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05222:Small cell lung cancer TTPJ921 RC R-HSA-114608:Platelet degranulation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1566977:Fibronectin matrix formation; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-354194:GRB2:SOS provides linkage to MAPK signaling for Integrins; R-HSA-372708:p130Cas linkage to MAPK signaling for integrins; R-HSA-5674135:MAP2K and MAPK activation TTON5IT ID TTON5IT TTON5IT TN Focal adhesion kinase 1 (FAK) TTON5IT UP Q05397 TTON5IT UC FAK1_HUMAN TTON5IT BC Kinase TTON5IT SN pp125FAK; p125FAK; Protein-tyrosine kinase 2; Protein phosphatase 1 regulatory subunit 71; PPP1R71; Focal adhesion kinase-related nonkinase; FRNK; FAK1; FADK 1; FADK TTON5IT GN PTK2 TTON5IT FC Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. TTON5IT EC EC 2.7.10.2 TTON5IT PD 6I8Z; 4Q9S; 4NY0; 4KAO; 4KAB TTON5IT SQ MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH TTON5IT TT Clinical trial TTON5IT FM Protein kinase superfamily. Tyr protein kinase family TTON5IT KE hsa04012:ErbB signaling pathway; hsa04062:Chemokine signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04360:Axon guidance; hsa04370:VEGF signaling pathway; hsa04510:Focal adhesion; hsa04670:Leukocyte transendothelial migration; hsa04810:Regulation of actin cytoskeleton; hsa05100:Bacterial invasion of epithelial cells; hsa05146:Amoebiasis; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05205:Proteoglycans in cancer; hsa05222:Small cell lung cancer TTON5IT RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-354194:GRB2:SOS provides linkage to MAPK signaling for Integrins; R-HSA-372708:p130Cas linkage to MAPK signaling for integrins; R-HSA-375165:NCAM signaling for neurite out-growth; R-HSA-391160:Signal regulatory protein (SIRP) family interactions; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-418885:DCC mediated attractive signaling; R-HSA-418886:Netrin mediated repulsion signals; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5663213:RHO GTPases Activate WASPs and WAVEs; R-HSA-5673001:RAF/MAP kinase cascade TTB8FUC ID TTB8FUC TTB8FUC TN Free fatty acid receptor 1 (GPR40) TTB8FUC UP O14842 TTB8FUC UC FFAR1_HUMAN TTB8FUC BC GPCR rhodopsin TTB8FUC SN Gprotein coupled receptor 40; FFAR1 TTB8FUC GN FFAR1 TTB8FUC FC G-protein coupled receptor for medium and long chain saturated and unsaturated fatty acids that plays an important role in glucose homeostasis. Fatty acid binding increases glucose- stimulated insulin secretion, and may also enhance the secretion of glucagon-like peptide 1 (GLP-1). May also play a role in bone homeostasis; receptor signaling activates pathways that inhibit osteoclast differentiation. Ligand binding leads to a conformation change that triggers signaling via G-proteins that activate phospholipase C, leading to an increase of the intracellular calcium concentration. Seems to act through a G(q) and G(i)-mediated pathway. TTB8FUC PD 5TZY; 5TZR; 5KW2; 4PHU TTB8FUC SQ MDLPPQLSFGLYVAAFALGFPLNVLAIRGATAHARLRLTPSLVYALNLGCSDLLLTVSLPLKAVEALASGAWPLPASLCPVFAVAHFFPLYAGGGFLAALSAGRYLGAAFPLGYQAFRRPCYSWGVCAAIWALVLCHLGLVFGLEAPGGWLDHSNTSLGINTPVNGSPVCLEAWDPASAGPARFSLSLLLFFLPLAITAFCYVGCLRALARSGLTHRRKLRAAWVAGGALLTLLLCVGPYNASNVASFLYPNLGGSWRKLGLITGAWSVVLNPLVTGYLGRGPGLKTVCAARTQGGKSQK TTB8FUC TT Clinical trial TTB8FUC KE hsa04911:Insulin secretion TTB8FUC RC R-HSA-416476:G alpha (q) signalling events; R-HSA-434316:Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion TTZMS1L ID TTZMS1L TTZMS1L TN Fungal Papulacandin B resistance protein 1 (Fung FKS1) TTZMS1L UP P38631 TTZMS1L UC FKS1_YEAST TTZMS1L BC Hexosyltransferase TTZMS1L SN UDP-glucose-1,3-beta-D-glucan glucosyltransferase; Papulacandin B sensitivity protein 1 of Saccharomyces cerevisiae; Glucan synthase; FKS1 protein of Saccharomyces cerevisiae; FKS1; CWN53 protein of Saccharomyces cerevisiae; CND1 protein of Saccharomyces cerevisiae; Beta-1,3-glucan synthetase; Beta-1,3-glucan synthase; 1,3-beta-D-glucan-UDP glucosyltransferase of Saccharomyces cerevisiae; (1,3)-beta-D-glucan synthase TTZMS1L GN Fung FKS1 TTZMS1L FC Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Involved in cell wall synthesis, maintenance and cell wall remodeling. TTZMS1L EC EC 2.4.1.34 TTZMS1L SQ MNTDQQPYQGQTDYTQGPGNGQSQEQDYDQYGQPLYPSQADGYYDPNVAAGTEADMYGQQPPNESYDQDYTNGEYYGQPPNMAAQDGENFSDFSSYGPPGTPGYDSYGGQYTASQMSYGEPNSSGTSTPIYGNYDPNAIAMALPNEPYPAWTADSQSPVSIEQIEDIFIDLTNRLGFQRDSMRNMFDHFMVLLDSRSSRMSPDQALLSLHADYIGGDTANYKKWYFAAQLDMDDEIGFRNMSLGKLSRKARKAKKKNKKAMEEANPEDTEETLNKIEGDNSLEAADFRWKAKMNQLSPLERVRHIALYLLCWGEANQVRFTAECLCFIYKCALDYLDSPLCQQRQEPMPEGDFLNRVITPIYHFIRNQVYEIVDGRFVKRERDHNKIVGYDDLNQLFWYPEGIAKIVLEDGTKLIELPLEERYLRLGDVVWDDVFFKTYKETRTWLHLVTNFNRIWVMHISIFWMYFAYNSPTFYTHNYQQLVDNQPLAAYKWASCALGGTVASLIQIVATLCEWSFVPRKWAGAQHLSRRFWFLCIIFGINLGPIIFVFAYDKDTVYSTAAHVVAAVMFFVAVATIIFFSIMPLGGLFTSYMKKSTRRYVASQTFTAAFAPLHGLDRWMSYLVWVTVFAAKYSESYYFLVLSLRDPIRILSTTAMRCTGEYWWGAVLCKVQPKIVLGLVIATDFILFFLDTYLWYIIVNTIFSVGKSFYLGISILTPWRNIFTRLPKRIYSKILATTDMEIKYKPKVLISQVWNAIIISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRDSEAERRISFFAQSLSTPIPEPLPVDNMPTFTVLTPHYAERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWECFVKDTKILAEETAAYEGNENEAEKEDALKSQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNAEGLERELEKMARRKFKFLVSMQRLAKFKPHELENAEFLLRAYPDLQIAYLDEEPPLTEGEEPRIYSALIDGHCEILDNGRRRPKFRVQLSGNPILGDGKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELNVEQVNPYAPGLRYEEQTTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLSQIGGKLHYGHPDFINATFMTTRGGVSKAQKGLHLNEDIYAGMNAMLRGGRIKHCEYYQCGKGRDLGFGTILNFTTKIGAGMGEQMLSREYYYLGTQLPVDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLSSLAHESIMCIYDRNKPKTDVLVPIGCYNFQPAVDWVRRYTLSIFIVFWIAFVPIVVQELIERGLWKATQRFFCHLLSLSPMFEVFAGQIYSSALLSDLAIGGARYISTGRGFATSRIPFSILYSRFAGSAIYMGARSMLMLLFGTVAHWQAPLLWFWASLSSLIFAPFVFNPHQFAWEDFFLDYRDYIRWLSRGNNQYHRNSWIGYVRMSRARITGFKRKLVGDESEKAAGDASRAHRTNLIMAEIIPCAIYAAGCFIAFTFINAQTGVKTTDDDRVNSVLRIIICTLAPIAVNLGVLFFCMGMSCCSGPLFGMCCKKTGSVMAGIAHGVAVIVHIAFFIVMWVLESFNFVRMLIGVVTCIQCQRLIFHCMTALMLTREFKNDHANTAFWTGKWYGKGMGYMAWTQPSRELTAKVIELSEFAADFVLGHVILICQLPLIIIPKIDKFHSIMLFWLKPSRQIRPPIYSLKQTRLRKRMVKKYCSLYFLVLAIFAGCIIGPAVASAKIHKHIGDSLDGVVHNLFQPINTTNNDTGSQMSTYQSHYYTHTPSLKTWSTIK TTZMS1L TT Clinical trial TTZMS1L KE sce00500:Starch and sucrose metabolism; sce04011:MAPK signaling pathway - yeast TTLMJSC ID TTLMJSC TTLMJSC TN Glucagon receptor messenger RNA (GCGR mRNA) TTLMJSC UP P47871 TTLMJSC UC GLR_HUMAN TTLMJSC BC mRNA target TTLMJSC SN Glucagon receptor (mRNA); GLR (mRNA); GL-R (mRNA) TTLMJSC GN GCGR TTLMJSC FC Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system. G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. TTLMJSC PD 5XEZ; 5EE7; 4LF3; 4L6R; 4ERS TTLMJSC SQ MPPCQPQRPLLLLLLLLACQPQVPSAQVMDFLFEKWKLYGDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPANTTANISCPWYLPWHHKVQHRFVFKRCGPDGQWVRGPRGQPWRDASQCQMDGEEIEVQKEVAKMYSSFQVMYTVGYSLSLGALLLALAILGGLSKLHCTRNAIHANLFASFVLKASSVLVIDGLLRTRYSQKIGDDLSVSTWLSDGAVAGCRVAAVFMQYGIVANYCWLLVEGLYLHNLLGLATLPERSFFSLYLGIGWGAPMLFVVPWAVVKCLFENVQCWTSNDNMGFWWILRFPVFLAILINFFIFVRIVQLLVAKLRARQMHHTDYKFRLAKSTLTLIPLLGVHEVVFAFVTDEHAQGTLRSAKLFFDLFLSSFQGLLVAVLYCFLNKEVQSELRRRWHRWRLGKVLWEERNTSNHRASSSPGHGPPSKELQFGRGGGSQDSSAETPLAGGLPRLAESPF TTLMJSC TT Clinical trial TTLMJSC FM mRNA target TTLMJSC RC R-HSA-163359:Glucagon signaling in metabolic regulation; R-HSA-416476:G alpha (q) signalling events; R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors TTOZRK6 ID TTOZRK6 TTOZRK6 TN Glucocorticoid receptor messenger RNA (GCR mRNA) TTOZRK6 UP P04150 TTOZRK6 UC GCR_HUMAN TTOZRK6 BC mRNA target TTOZRK6 SN Nuclear receptor subfamily 3 group C member 1 (mRNA); Glucocorticoid receptor (mRNA); GRL (mRNA); GR (mRNA); Alpha-A (mRNA) TTOZRK6 GN NR3C1 TTOZRK6 FC Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Receptor for glucocorticoids (GC). TTOZRK6 PD 6EL9; 6EL7; 6EL6; 6DXK; 6CFN TTOZRK6 SQ MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK TTOZRK6 TT Clinical trial TTOZRK6 FM mRNA target TTOZRK6 KE hsa04080:Neuroactive ligand-receptor interaction TTOZRK6 RC R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression TT9PBIL ID TT9PBIL TT9PBIL TN Glutamyl aminopeptidase (ENPEP) TT9PBIL UP Q07075 TT9PBIL UC AMPE_HUMAN TT9PBIL BC Peptidase TT9PBIL SN ENPEP; EAP; Differentiation antigen gp160; Aminopeptidase A; APA TT9PBIL GN ENPEP TT9PBIL FC Appears to have a role in the catabolicpathway of the renin-angiotensin system. Probably plays a role in regulating growth and differentiation of early B-lineage cells. TT9PBIL EC EC 3.4.11.7 TT9PBIL PD 4KXD; 4KXC; 4KXB; 4KXA; 4KX9 TT9PBIL SQ MNFAEREGSKRYCIQTKHVAILCAVVVGVGLIVGLAVGLTRSCDSSGDGGPGTAPAPSHLPSSTASPSGPPAQDQDICPASEDESGQWKNFRLPDFVNPVHYDLHVKPLLEEDTYTGTVSISINLSAPTRYLWLHLRETRITRLPELKRPSGDQVQVRRCFEYKKQEYVVVEAEEELTPSSGDGLYLLTMEFAGWLNGSLVGFYRTTYTENGQVKSIVATDHEPTDARKSFPCFDEPNKKATYTISITHPKEYGALSNMPVAKEESVDDKWTRTTFEKSVPMSTYLVCFAVHQFDSVKRISNSGKPLTIYVQPEQKHTAEYAANITKSVFDYFEEYFAMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDPKESASSNQQRVATVVAHELVHQWFGNIVTMDWWEDLWLNEGFASFFEFLGVNHAETDWQMRDQMLLEDVLPVQEDDSLMSSHPIIVTVTTPDEITSVFDGISYSKGSSILRMLEDWIKPENFQKGCQMYLEKYQFKNAKTSDFWAALEEASRLPVKEVMDTWTRQMGYPVLNVNGVKNITQKRFLLDPRANPSQPPSDLGYTWNIPVKWTEDNITSSVLFNRSEKEGITLNSSNPSGNAFLKINPDHIGFYRVNYEVATWDSIATALSLNHKTFSSADRASLIDDAFALARAQLLDYKVALNLTKYLKREENFLPWQRVISAVTYIISMFEDDKELYPMIEEYFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVLETVKNNIEWLKQHRNTIREWFFNLLESG TT9PBIL TT Clinical trial TT9PBIL KE hsa04614:Renin-angiotensin system TT9PBIL RC R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins TT40K12 ID TT40K12 TT40K12 TN Glutathione S-transferase P (GSTP1) TT40K12 UP P09211 TT40K12 UC GSTP1_HUMAN TT40K12 BC Alkyl aryl transferase TT40K12 SN GSTP11; GSTP1-1; GST3; GST classpi; GST class-pi; FAEES3 TT40K12 GN GSTP1 TT40K12 FC Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. TT40K12 EC EC 2.5.1.18 TT40K12 PD 9GSS; 8GSS; 7GSS; 6GSS; 6AP9 TT40K12 SQ MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ TT40K12 TT Clinical trial TT40K12 FM Alkyl aryl transferase TT40K12 KE hsa00480:Glutathione metabolism; hsa00980:Metabolism of xenobiotics by cytochrome P450; hsa00982:Drug metabolism - cytochrome P450; hsa05200:Pathways in cancer; hsa05204:Chemical carcinogenesis; hsa05215:Prostate cancer TTUGSWA ID TTUGSWA TTUGSWA TN Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) TTUGSWA UP P04406 TTUGSWA UC G3P_HUMAN TTUGSWA BC Aldehyde/oxo donor oxidoreductase TTUGSWA SN Peptidyl-cysteine S-nitrosylase GAPDH; OK/SW-cl.12; GAPD; D-glyceraldehyde-3-phosphate dehydrogenase; CDABP0047 TTUGSWA GN GAPDH TTUGSWA FC Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. TTUGSWA EC EC 1.2.1.12 TTUGSWA PD 6ADE; 4WNI; 4WNC; 3GPD; 2FEH TTUGSWA SQ MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE TTUGSWA TT Clinical trial TTUGSWA FM Glyceraldehyde-3-phosphate TTUGSWA KE hsa00010:Glycolysis / Gluconeogenesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa01230:Biosynthesis of amino acids; hsa04066:HIF-1 signaling pathway; hsa05010:Alzheimer's disease TTUGSWA RC R-HSA-70171:Glycolysis; R-HSA-70263:Gluconeogenesis TT37XV9 ID TT37XV9 TT37XV9 TN Growth/differentiation factor 5 (GDF-5) TT37XV9 UP P43026 TT37XV9 UC GDF5_HUMAN TT37XV9 BC Growth factor TT37XV9 SN Radotermin; Lipopolysaccharide-associated protein 4; LPS-associated protein 4; LAP-4; Cartilagederived morphogenetic protein 1; Cartilage-derived morphogenetic protein 1; CDMP1; CDMP-1; Bone morphogenetic protein 14; BMP14; BMP-14 TT37XV9 GN GDF5 TT37XV9 FC During cartilage development regulates differentiation of chondrogenic tissue through two pathways. Firstly, positively regulates differentiation of chondrogenic tissue through its binding of high affinity with BMPR1B and of less affinity with BMPR1A, leading to induction of SMAD1-SMAD5-SMAD8 complex phosphorylation and then SMAD protein signaling transduction. Secondly, negatively regulates chondrogenic differentiation through its interaction with NOG. Required to prevent excessive muscle loss upon denervation. This function requires SMAD4 and is mediated by phosphorylated SMAD1/5/8. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Growth factor involved in bone and cartilage formation. TT37XV9 PD 5HK5; 3QB4; 3EVS; 2BHK; 1WAQ TT37XV9 SQ MRLPKLLTFLLWYLAWLDLEFICTVLGAPDLGQRPQGTRPGLAKAEAKERPPLARNVFRPGGHSYGGGATNANARAKGGTGQTGGLTQPKKDEPKKLPPRPGGPEPKPGHPPQTRQATARTVTPKGQLPGGKAPPKAGSVPSSFLLKKAREPGPPREPKEPFRPPPITPHEYMLSLYRTLSDADRKGGNSSVKLEAGLANTITSFIDKGQDDRGPVVRKQRYVFDISALEKDGLLGAELRILRKKPSDTAKPAAPGGGRAAQLKLSSCPSGRQPASLLDVRSVPGLDGSGWEVFDIWKLFRNFKNSAQLCLELEAWERGRAVDLRGLGFDRAARQVHEKALFLVFGRTKKRDLFFNEIKARSGQDDKTVYEYLFSQRRKRRAPLATRQGKRPSKNLKARCSRKALHVNFKDMGWDDWIIAPLEYEAFHCEGLCEFPLRSHLEPTNHAVIQTLMNSMDPESTPPTCCVPTRLSPISILFIDSANNVVYKQYEDMVVESCGCR TT37XV9 TT Clinical trial TT37XV9 FM Growth factor TT37XV9 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway TT37XV9 RC R-HSA-2129379:Molecules associated with elastic fibres TTLSWP6 ID TTLSWP6 TTLSWP6 TN GTP cyclohydrolase-I (GCH1) TTLSWP6 UP P30793 TTLSWP6 UC GCH1_HUMAN TTLSWP6 BC Carbon-nitrogen hydrolase TTLSWP6 SN Guanosine triphosphate cyclohydrolase I; GTP-CH-I; GTP cyclohydrolase I; GTP cyclohydrolase 1; GCH; DYT5 TTLSWP6 GN GCH1 TTLSWP6 FC May be involved in dopamine synthesis. May modify pain sensitivity and persistence. Isoform GCH-1 is the functional enzyme, the potential function of the enzymatically inactive isoforms remains unknown. Positively regulates nitric oxide synthesis in umbilical vein endothelial cells (HUVECs). TTLSWP6 EC EC 3.5.4.16 TTLSWP6 PD 1FB1 TTLSWP6 SQ MEKGPVRAPAEKPRGARCSNGFPERDPPRPGPSRPAEKPPRPEAKSAQPADGWKGERPRSEEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS TTLSWP6 TT Clinical trial TTLSWP6 FM Carbon nitrogen hydrolase TTLSWP6 RC R-HSA-1474151:Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation TTI6V2A ID TTI6V2A TTI6V2A TN Heme oxygenase 1 (HMOX1) TTI6V2A UP P09601 TTI6V2A UC HMOX1_HUMAN TTI6V2A BC Paired donor oxygen oxidoreductase TTI6V2A SN HO1; HO-1; HO TTI6V2A GN HMOX1 TTI6V2A FC Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. TTI6V2A EC EC 1.14.14.18 TTI6V2A PD 6EHA; 5BTQ; 4WD4; 3TGM; 3K4F TTI6V2A SQ MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM TTI6V2A TT Clinical trial TTI6V2A FM Oxidoreductases acting on paired donors TTI6V2A KE hsa00860:Porphyrin and chlorophyll metabolism; hsa04066:HIF-1 signaling pathway; hsa04978:Mineral absorption; hsa05206:MicroRNAs in cancer TTI6V2A RC R-HSA-917937:Iron uptake and transport TT4V2JM ID TT4V2JM TT4V2JM TN Hepatocyte growth factor (HGF) TT4V2JM UP P14210 TT4V2JM UC HGF_HUMAN TT4V2JM BC Peptidase TT4V2JM SN Scatter factor; SF; Hepatopoietin-A; Hepatopoeitin A; HPTA TT4V2JM GN HGF TT4V2JM FC Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization. Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. TT4V2JM PD 5CT3; 5CT2; 5CT1; 5CSQ; 5CS9 TT4V2JM SQ MWVTKLLPALLLQHVLLHLLLLPIAIPYAEGQRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYENKDYIRNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDGSESPWCFTTDPNIRVGYCSQIPNCDMSHGQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPISRCEGDTTPTIVNLDHPVISCAKTKQLRVVNGIPTRTNIGWMVSLRYRNKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDEKCKQVLNVSQLVYGPEGSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLRVAHLYIMGNEKCSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKIILTYKVPQS TT4V2JM TT Clinical trial TT4V2JM FM Peptidase TT4V2JM KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa05144:Malaria; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05211:Renal cell carcinoma; hsa05218:Melanoma TT4V2JM RC R-HSA-114608:Platelet degranulation; R-HSA-1266695:Interleukin-7 signaling TTMHFRY ID TTMHFRY TTMHFRY TN HIF-prolyl hydroxylase 1 (HPH-1) TTMHFRY UP Q96KS0 TTMHFRY UC EGLN2_HUMAN TTMHFRY BC Paired donor oxygen oxidoreductase TTMHFRY SN Prolyl hydroxylase domain-containing protein 1; PHD1; Hypoxia-inducible factor prolyl hydroxylase 1; HPH-3; HIF-PH1; HIF-PH; Estrogen-induced tag6; Estrogen-induced tag 6; Egl nine homolog 2; EIT6; EIT-6 TTMHFRY GN EGLN2 TTMHFRY FC Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death. Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappaB activation in hypoxic conditions. Target proteins are preferentially recognized via a LXXLAP motif. Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. TTMHFRY EC EC 1.14.11.29 TTMHFRY PD 5V1B TTMHFRY SQ MDSPCQPQPLSQALPQLPGSSSEPLEPEPGRARMGVESYLPCPLLPSYHCPGVPSEASAGSGTPRATATSTTASPLRDGFGGQDGGELRPLQSEGAAALVTKGCQRLAAQGARPEAPKRKWAEDGGDAPSPSKRPWARQENQEAEREGGMSCSCSSGSGEASAGLMEEALPSAPERLALDYIVPCMRYYGICVKDSFLGAALGGRVLAEVEALKRGGRLRDGQLVSQRAIPPRSIRGDQIAWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGSYVINGRTKAMVACYPGNGLGYVRHVDNPHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEVKPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT TTMHFRY TT Clinical trial TTMHFRY FM Oxidoreductases acting on paired donors TTMHFRY KE hsa04066:HIF-1 signaling pathway; hsa05200:Pathways in cancer; hsa05211:Renal cell carcinoma TTMHFRY RC R-HSA-1234176:Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha TT9JNIC ID TT9JNIC TT9JNIC TN Histamine H3 receptor (H3R) TT9JNIC UP Q9Y5N1 TT9JNIC UC HRH3_HUMAN TT9JNIC BC GPCR rhodopsin TT9JNIC SN Histamine receptor 3; HH3R; GPCR97; G-protein coupled receptor 97; G protein-coupled receptor 97 TT9JNIC GN HRH3 TT9JNIC FC Signals through the inhibition of adenylate cyclase and displays high constitutive activity (spontaneous activity in the absence of agonist). Agonist stimulation of isoform 3 neither modified adenylate cyclase activity nor induced intracellular calcium mobilization. The H3 subclass of histamine receptors could mediate the histamine signals in CNS and peripheral nervous system. TT9JNIC SQ MERAPPDGPLNASGALAGEAAAAGGARGFSAAWTAVLAALMALLIVATVLGNALVMLAFVADSSLRTQNNFFLLNLAISDFLVGAFCIPLYVPYVLTGRWTFGRGLCKLWLVVDYLLCTSSAFNIVLISYDRFLSVTRAVSYRAQQGDTRRAVRKMLLVWVLAFLLYGPAILSWEYLSGGSSIPEGHCYAEFFYNWYFLITASTLEFFTPFLSVTFFNLSIYLNIQRRTRLRLDGAREAAGPEPPPEAQPSPPPPPGCWGCWQKGHGEAMPLHRYGVGEAAVGAEAGEATLGGGGGGGSVASPTSSSGSSSRGTERPRSLKRGSKPSASSASLEKRMKMVSQSFTQRFRLSRDRKVAKSLAVIVSIFGLCWAPYTLLMIIRAACHGHCVPDYWYETSFWLLWANSAVNPVLYPLCHHSFRRAFTKLLCPQKLKIQPHSSLEHCWK TT9JNIC TT Successful TT9JNIC FM GPCR rhodopsin TT9JNIC KE hsa04080:Neuroactive ligand-receptor interaction TT9JNIC RC R-HSA-390650:Histamine receptors; R-HSA-418594:G alpha (i) signalling events TTXJ178 ID TTXJ178 TTXJ178 TN Histamine H4 receptor (H4R) TTXJ178 UP Q9H3N8 TTXJ178 UC HRH4_HUMAN TTXJ178 BC GPCR rhodopsin TTXJ178 SN SP9144; Pfi-013; HH4R; H4 receptor; GPRv53; GPCR105; G protein-coupled receptor 105; AXOR35 TTXJ178 GN HRH4 TTXJ178 FC Displays a significant level of constitutive activity (spontaneous activity in the absence of agonist). The H4 subclass of histamine receptors could mediate the histamine signals in peripheral tissues. TTXJ178 SQ MPDTNSTINLSLSTRVTLAFFMSLVAFAIMLGNALVILAFVVDKNLRHRSSYFFLNLAISDFFVGVISIPLYIPHTLFEWDFGKEICVFWLTTDYLLCTASVYNIVLISYDRYLSVSNAVSYRTQHTGVLKIVTLMVAVWVLAFLVNGPMILVSESWKDEGSECEPGFFSEWYILAITSFLEFVIPVILVAYFNMNIYWSLWKRDHLSRCQSHPGLTAVSSNICGHSFRGRLSSRRSLSASTEVPASFHSERQRRKSSLMFSSRTKMNSNTIASKMGSFSQSDSVALHQREHVELLRARRLAKSLAILLGVFAVCWAPYSLFTIVLSFYSSATGPKSVWYRIAFWLQWFNSFVNPLLYPLCHKRFQKAFLKIFCIKKQPLPSQHSRSVSS TTXJ178 TT Clinical trial TTXJ178 KE hsa04080:Neuroactive ligand-receptor interaction TTXJ178 RC R-HSA-390650:Histamine receptors; R-HSA-418594:G alpha (i) signalling events TTSZ8T1 ID TTSZ8T1 TTSZ8T1 TN Histone-lysine N-methyltransferase (HLNM) TTSZ8T1 UP Q8TEK3 TTSZ8T1 UC DOT1L_HUMAN TTSZ8T1 BC Methyltransferase TTSZ8T1 SN Lysine N-methyltransferase 4; KMT4; KIAA1814; Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone H3-K79 methyltransferase; H3-K79-HMTase; DOT1-like protein TTSZ8T1 GN DOT1L TTSZ8T1 FC Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA. TTSZ8T1 EC EC 2.1.1.43 TTSZ8T1 PD 6O96; 6NQA; 6NOG; 6NN6; 6NJ9 TTSZ8T1 SQ MGEKLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMNTANPERKPKKNQTALDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQRHSPNPLLVAPTPPALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKSCVPPDDALSLHLRGKGALGRELEPDASRLHLELDCTKFSLPHLSSMSPELSMNGQAAGYELCGVLSRPSSKQNTPQYLASPLDQEVVPCTPSHVGRPRLEKLSGLAAPDYTRLSPAKIVLRRHLSQDHTVPGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRERAYGSSGELITSLPISIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVLQPRDPSSTLEKQIGANAHGAGSRSLALAPAGFSYAGSVAISGALAGSPASLTPGAEPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRIVFTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSPLNLNSMVSNINQPLEITAISSPETSLKSSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKSTFSPISDIGLAKSADSPLQASSALSQNSLFTFRPALEEPSADAKLAAHPRKGFPGSLSGADGLSPGTNPANGCTFGGGLAADLSLHSFSDGASLPHKGPEAAGLSSPLSFPSQRGKEGSDANPFLSKRQLDGLAGLKGEGSRGKEAGEGGLPLCGPTDKTPLLSGKAAKARDREVDLKNGHNLFISAAAVPPGSLLSGPGLAPAASSAGGAASSAQTHRSFLGPFPPGPQFALGPMSLQANLGSVAGSSVLQSLFSSVPAAAGLVHVSSAATRLTNSHAMGSFSGVAGGTVGGN TTSZ8T1 TT Clinical trial TTSZ8T1 FM Methyltransferase superfamily TTSZ8T1 KE hsa00310:Lysine degradation; hsa05202:Transcriptional misregulation in cancer TTSZ8T1 RC R-HSA-3214841:PKMTs methylate histone lysines TTL53M6 ID TTL53M6 TTL53M6 TN Induced myeloid leukemia cell differentiation protein Mcl-1 (MCL1) TTL53M6 UP Q07820 TTL53M6 UC MCL1_HUMAN TTL53M6 BC B-cell lymphoma Bcl-2 TTL53M6 SN mcl1/EAT; Bcl2-L-3; Bcl-2-related protein EAT/mcl1; Bcl-2-like protein 3; BCL2L3 TTL53M6 GN MCL1 TTL53M6 FC Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis. Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. TTL53M6 PD 6OVC; 6OQN; 6OQD; 6OQC; 6OQB TTL53M6 SQ MFGLKRNAVIGLNLYCGGAGLGAGSGGATRPGGRLLATEKEASARREIGGGEAGAVIGGSAGASPPSTLTPDSRRVARPPPIGAEVPDVTATPARLLFFAPTRRAAPLEEMEAPAADAIMSPEEELDGYEPEPLGKRPAVLPLLELVGESGNNTSTDGSLPSTPPPAEEEEDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGGIRNVLLAFAGVAGVGAGLAYLIR TTL53M6 TT Clinical trial TTL53M6 FM BCL2 family TTL53M6 KE hsa04151:PI3K-Akt signaling pathway; hsa05206:MicroRNAs in cancer TTHIZP9 ID TTHIZP9 TTHIZP9 TN Integrin alpha-5 (ITGA5) TTHIZP9 UP P08648 TTHIZP9 UC ITA5_HUMAN TTHIZP9 BC Integrin TTHIZP9 SN VLA-5; Integrin alpha-F; Integrin alpha-5 light chain; Integrin alpha-5 heavy chain; Fibronectin receptor subunit alpha; FNRA; CD49e antigen; CD49e; CD49 antigen-like family member E TTHIZP9 GN ITGA5 TTHIZP9 FC It recognizes the sequence R-G-D in its ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling. Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for fibronectin and fibrinogen. TTHIZP9 PD 4WK4; 4WK2; 4WK0; 4WJK; 3VI4 TTHIZP9 SQ MGSRTPESPLHAVQLRWGPRRRPPLLPLLLLLLPPPPRVGGFNLDAEAPAVLSGPPGSFFGFSVEFYRPGTDGVSVLVGAPKANTSQPGVLQGGAVYLCPWGASPTQCTPIEFDSKGSRLLESSLSSSEGEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKEPLSDPVGTCYLSTDNFTRILEYAPCRSDFSWAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQIAESYYPEYLINLVQGQLQTRQASSIYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTILNGSDIRSLYNFSGEQMASYFGYAVAATDVNGDGLDDLLVGAPLLMDRTPDGRPQEVGRVYVYLQHPAGIEPTPTLTLTGHDEFGRFGSSLTPLGDLDQDGYNDVAIGAPFGGETQQGVVFVFPGGPGGLGSKPSQVLQPLWAASHTPDFFGSALRGGRDLDGNGYPDLIVGSFGVDKAVVYRGRPIVSASASLTIFPAMFNPEERSCSLEGNPVACINLSFCLNASGKHVADSIGFTVELQLDWQKQKGGVRRALFLASRQATLTQTLLIQNGAREDCREMKIYLRNESEFRDKLSPIHIALNFSLDPQAPVDSHGLRPALHYQSKSRIEDKAQILLDCGEDNICVPDLQLEVFGEQNHVYLGDKNALNLTFHAQNVGEGGAYEAELRVTAPPEAEYSGLVRHPGNFSSLSCDYFAVNQSRLLVCDLGNPMKAGASLWGGLRFTVPHLRDTKKTIQFDFQILSKNLNNSQSDVVSFRLSVEAQAQVTLNGVSKPEAVLFPVSDWHPRDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQALEGQQLLYVTRVTGLNCTTNHPINPKGLELDPEGSLHHQQKREAPSRSSASSGPQILKCPEAECFRLRCELGPLHQQESQSLQLHFRVWAKTFLQREHQPFSLQCEAVYKALKMPYRILPRQLPQKERQVATAVQWTKAEGSYGVPLWIIILAILFGLLLLGLLIYILYKLGFFKRSLPYGTAMEKAQLKPPATSDA TTHIZP9 TT Clinical trial TTHIZP9 FM Integrin TTHIZP9 KE hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04640:Hematopoietic cell lineage; hsa04810:Regulation of actin cytoskeleton; hsa05100:Bacterial invasion of epithelial cells; hsa05131:Shigellosis; hsa05133:Pertussis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTHIZP9 RC R-HSA-1566948:Elastic fibre formation; R-HSA-1566977:Fibronectin matrix formation; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-216083:Integrin cell surface interactions TTT1R2L ID TTT1R2L TTT1R2L TN Integrin alpha-V (ITGAV) TTT1R2L UP P06756 TTT1R2L UC ITAV_HUMAN TTT1R2L BC Integrin TTT1R2L SN Vitronectin receptor subunit alpha; Vitronectin receptor alpha subunit; Vitronectin receptor; VTNR; VNRA; MSK8; CD51 antigen; CD51 TTT1R2L GN ITGAV TTT1R2L FC The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling. ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling. ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling. ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling. ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGAV:ITGB3 and ITGAV:ITGB6 act as a receptor for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1. Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6 or ITGAV:ITGB8) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation. TTT1R2L PD 6DJP; 6AVU; 6AVR; 6AVQ; 5NEU TTT1R2L SQ MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET TTT1R2L TT Clinical trial TTT1R2L FM Integrin TTT1R2L KE hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04514:Cell adhesion molecules (CAMs); hsa04810:Regulation of actin cytoskeleton; hsa04919:Thyroid hormone signaling pathway; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05222:Small cell lung cancer; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTT1R2L RC R-HSA-1236973:Cross-presentation of particulate exogenous antigens (phagosomes); R-HSA-1566948:Elastic fibre formation; R-HSA-210990:PECAM1 interactions; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000157:Laminin interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-4420097:VEGFA-VEGFR2 Pathway TTBVIQC ID TTBVIQC TTBVIQC TN Integrin beta-1 (ITGB1) TTBVIQC UP P05556 TTBVIQC UC ITB1_HUMAN TTBVIQC BC Integrin TTBVIQC SN VLA-4 subunit beta; MSK12; MDF2; Integrin VLA-4 beta subunit; Glycoprotein IIa; GPIIA; Fibronectin receptor subunit beta; Fibronectin receptor beta subunit; FNRB; CD29 antigen; CD29; Beta(1) integrin TTBVIQC GN ITGB1 TTBVIQC FC Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion. Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. Isoform 2 interferes with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro). When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling. Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. TTBVIQC PD 4WK4; 4WK2; 4WK0; 4WJK; 4DX9 TTBVIQC SQ MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK TTBVIQC TT Clinical trial TTBVIQC FM Integrin TTBVIQC KE hsa04015:Rap1 signaling pathway; hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04360:Axon guidance; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04514:Cell adhesion molecules (CAMs); hsa04611:Platelet activation; hsa04670:Leukocyte transendothelial migration; hsa04810:Regulation of actin cytoskeleton; hsa05100:Bacterial invasion of epithelial cells; hsa05130:Pathogenic Escherichia coli infection; hsa05131:Shigellosis; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05145:Toxoplasmosis; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05222:Small cell lung cancer; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTBVIQC RC R-HSA-1566948:Elastic fibre formation; R-HSA-1566977:Fibronectin matrix formation; R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-210991:Basigin interactions; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000157:Laminin interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-416700:Other semaphorin interactions; R-HSA-446343:Localization of the PINCH-ILK-PARVIN complex to focal adhesions; R-HSA-447041:CHL1 interactions; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-75892:Platelet Adhesion to exposed collagen TT51DEV ID TT51DEV TT51DEV TN Interleukin 1 receptor type 2 (IL1R2) TT51DEV UP P27930 TT51DEV UC IL1R2_HUMAN TT51DEV BC Cytokine receptor TT51DEV SN Interleukin-1 receptor type II; Interleukin-1 receptor type 2; Interleukin-1 receptor beta; Interleukin 1 receptor type II; IL1RB; IL-1RT2; IL-1RT-2; IL-1R-beta; IL-1R-2; IL-1 type II receptor; CDw121b; CD121b; CD121 antigen-like family member B; Antigen CDw121b TT51DEV GN IL1R2 TT51DEV FC Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Non-signaling receptor for IL1A, IL1B and IL1RN. TT51DEV PD 3O4O TT51DEV SQ MLRLYVLVMGVSAFTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPYWLWASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFLPFISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRIKKKKEETIPVIISPLKTISASLGSRLTIPCKVFLGTGTPLTTMLWWTANDTHIESAYPGGRVTEGPRQEYSENNENYIEVPLIFDPVTREDLHMDFKCVVHNTLSFQTLRTTVKEASSTFSWGIVLAPLSLAFLVLGGIWMHRRCKHRTGKADGLTVLWPHHQDFQSYPK TT51DEV TT Clinical trial TT51DEV KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04640:Hematopoietic cell lineage; hsa05146:Amoebiasis; hsa05166:HTLV-I infection; hsa05202:Transcriptional misregulation in cancer TT51DEV RC R-HSA-446652:Interleukin-1 signaling TT9721Y ID TT9721Y TT9721Y TN Interleukin 2 receptor beta (IL2RB) TT9721Y UP P14784 TT9721Y UC IL2RB_HUMAN TT9721Y BC Cytokine receptor TT9721Y SN P70-75; Interleukin-2 receptor subunit beta; Interleukin-15 receptor subunit beta; IL15RB; IL-2RB; IL-2R subunit beta; IL-2 receptor subunit beta; IL-2 receptor; High affinity IL-2 receptor subunit beta; CD122 TT9721Y GN IL2RB TT9721Y FC Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15. TT9721Y PD 6E8K; 5M5E; 4GS7; 3QAZ; 2ERJ TT9721Y SQ MAAPALSWRLPLLILLLPLATSWASAAVNGTSQFTCFYNSRANISCVWSQDGALQDTSCQVHAWPDRRRWNQTCELLPVSQASWACNLILGAPDSQKLTTVDIVTLRVLCREGVRWRVMAIQDFKPFENLRLMAPISLQVVHVETHRCNISWEISQASHYFERHLEFEARTLSPGHTWEEAPLLTLKQKQEWICLETLTPDTQYEFQVRVKPLQGEFTTWSPWSQPLAFRTKPAALGKDTIPWLGHLLVGLSGAFGFIILVYLLINCRNTGPWLKKVLKCNTPDPSKFFSQLSSEHGGDVQKWLSSPFPSSSFSPGGLAPEISPLEVLERDKVTQLLLQQDKVPEPASLSSNHSLTSCFTNQGYFFFHLPDALEIEACQVYFTYDPYSEEDPDEGVAGAPTGSSPQPLQPLSGEDDAYCTFPSRDDLLLFSPSLLGGPSPPSTAPGGSGAGEERMPPSLQERVPRDWDPQPLGPPTPGVPDLVDFQPPPELVLREAGEEVPDAGPREGVSFPWSRPPGQGEFRALNARLPLNTDAYLSLQELQGQDPTHLV TT9721Y TT Clinical trial TT9721Y FM Cytokine receptor TT9721Y KE hsa04060:Cytokine-cytokine receptor interaction; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa05162:Measles; hsa05166:HTLV-I infection; hsa05202:Transcriptional misregulation in cancer TT9721Y RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-451927:Interleukin-2 signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-912526:Interleukin receptor SHC signaling TT0GVCH ID TT0GVCH TT0GVCH TN Interleukin-13 (IL13) TT0GVCH UP P35225 TT0GVCH UC IL13_HUMAN TT0GVCH BC Cytokine: interleukin TT0GVCH SN NC30; IL-13 TT0GVCH GN IL13 TT0GVCH FC Inhibits inflammatory cytokine production. Synergizes with IL2 in regulating interferon-gamma synthesis. May be critical in regulating inflammatory and immune responses. Positively regulates IL31RA expression in macrophages. Cytokine. TT0GVCH PD 5L6Y; 5E4E; 4PS4; 4I77; 3LB6 TT0GVCH SQ MHPLLNPLLLALGLMALLLTTVIALTCLGGFASPGPVPPSTALRELIEELVNITQNQKAPLCNGSMVWSINLTAGMYCAALESLINVSGCSAIEKTQRMLSGFCPHKVSAGQFSSLHVRDTKIEVAQFVKDLLLHLKKLFREGRFN TT0GVCH TT Clinical trial TT0GVCH FM Interleukin TT0GVCH KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa05162:Measles; hsa05310:Asthma; hsa05321:Inflammatory bowel disease (IBD) TTJFA35 ID TTJFA35 TTJFA35 TN Interleukin-15 (IL15) TTJFA35 UP P40933 TTJFA35 UC IL15_HUMAN TTJFA35 BC Cytokine: interleukin TTJFA35 SN IL-15 TTJFA35 GN IL15 TTJFA35 FC Stimulation by IL15 requires interaction of IL15 with components of the IL2 receptor, including IL2RB and probably IL2RG but not IL2RA. In neutrophils, stimulates phagocytosis probably by signaling through the IL15 receptor, composed of the subunits IL15RA, IL2RB and IL2RG, which results in kinase SYK activation. Cytokine that stimulates the proliferation of T-lymphocytes. TTJFA35 PD 4GS7; 2Z3R; 2Z3Q; 2XQB TTJFA35 SQ MRISKPHLRSISIQCYLCLLLNSHFLTEAGIHVFILGCFSAGLPKTEANWVNVISDLKKIEDLIQSMHIDATLYTESDVHPSCKVTAMKCFLLELQVISLESGDASIHDTVENLIILANNSLSSNGNVTESGCKECEELEEKNIKEFLQSFVHIVQMFINTS TTJFA35 TT Clinical trial TTJFA35 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04668:TNF signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05323:Rheumatoid arthritis TTRICUF ID TTRICUF TTRICUF TN Interleukin-18 (IL18) TTRICUF UP Q14116 TTRICUF UC IL18_HUMAN TTRICUF BC Cytokine: interleukin TTRICUF SN Interleukin-1 gamma; Interferon-gamma inducing factor; Interferon gamma-inducing factor; Iboctadekin; IL1F4; IL-18; IL-1 gamma; IGIF; IFN-gamma-inducing factor TTRICUF GN IL18 TTRICUF FC Upon binding to IL18R1 and IL18RAP, forms a signaling ternary complex which activates NF-kappa-B, triggering synthesis of inflammatory mediators. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells and natural killer (NK) cells. A proinflammatory cytokine primarily involved in polarized T-helper 1 (Th1) cell and natural killer (NK) cell immune responses. TTRICUF PD 4XFU; 4XFT; 4XFS; 4R6U; 4HJJ TTRICUF SQ MAAEPVEDNCINFVAMKFIDNTLYFIAEDDENLESDYFGKLESKLSVIRNLNDQVLFIDQGNRPLFEDMTDSDCRDNAPRTIFIISMYKDSQPRGMAVTISVKCEKISTLSCENKIISFKEMNPPDNIKDTKSDIIFFQRSVPGHDNKMQFESSSYEGYFLACEKERDLFKLILKKEDELGDRSIMFTVQNED TTRICUF TT Clinical trial TTRICUF FM Interleukin TTRICUF KE hsa04060:Cytokine-cytokine receptor interaction; hsa04621:NOD-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa05132:Salmonella infection; hsa05134:Legionellosis; hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05152:Tuberculosis; hsa05164:Influenza A; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis TTRICUF RC R-HSA-448706:Interleukin-1 processing TTEO25X ID TTEO25X TTEO25X TN Inward rectifier potassium channel Kir3.4 (KCNJ5) TTEO25X UP P48544 TTEO25X UC KCNJ5_HUMAN TTEO25X BC Inward rectifier potassium channel TTEO25X SN Potassium channel, inwardly rectifying, subfamily J, member 5; KCNJ5; KATP-1; KATP channel; Inward rectifier K+ channel Kir3.4; Heart KATP channel; GIRK4; Cardiac inward rectifier; CIR TTEO25X GN KCNJ5 TTEO25X FC This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium. TTEO25X SQ MAGDSRNAMNQDMEIGVTPWDPKKIPKQARDYVPIATDRTRLLAEGKKPRQRYMEKSGKCNVHHGNVQETYRYLSDLFTTLVDLKWRFNLLVFTMVYTVTWLFFGFIWWLIAYIRGDLDHVGDQEWIPCVENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIILLLVQAILGSIVNAFMVGCMFVKISQPKKRAETLMFSNNAVISMRDEKLCLMFRVGDLRNSHIVEASIRAKLIKSRQTKEGEFIPLNQTDINVGFDTGDDRLFLVSPLIISHEINQKSPFWEMSQAQLHQEEFEVVVILEGMVEATGMTCQARSSYMDTEVLWGHRFTPVLTLEKGFYEVDYNTFHDTYETNTPSCCAKELAEMKREGRLLQYLPSPPLLGGCAEAGLDAEAEQNEEDEPKGLGGSREARGSV TTEO25X TT Clinical trial TTEO25X KE hsa04713:Circadian entrainment; hsa04723:Retrograde endocannabinoid signaling; hsa04726:Serotonergic synapse; hsa04728:Dopaminergic synapse; hsa04915:Estrogen signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05032:Morphine addiction TTEO25X RC R-HSA-1296041:Activation of G protein gated Potassium channels; R-HSA-997272:Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits TTTRP0H ID TTTRP0H TTTRP0H TN Kinesin-like protein KIF11 (KIF11) TTTRP0H UP P52732 TTTRP0H UC KIF11_HUMAN TTTRP0H BC Kinesin-like protein family TTTRP0H SN Thyroid receptor interacting protein 5; TRIP5; Kinesin-related motor protein Eg5; Kinesin-like spindle protein HKSP; Kinesin-like protein 1; KIF11; Eg5 TTTRP0H GN KIF11 TTTRP0H FC Motor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays. TTTRP0H PD 6G6Z; 6G6Y; 5ZO9; 5ZO8; 5ZO7 TTTRP0H SQ MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKSSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNILNKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIVELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEYITSALESTEEKLHDAASKLLNTVEETTKDVSGLHSKLDRKKAVDQHNAEAQDIFGKNLNSLFNNMEELIKDGSSKQKAMLEVHKTLFGNLLSSSVSALDTITTVALGSLTSIPENVSTHVSQIFNMILKEQSLAAESKTVLQELINVLKTDLLSSLEMILSPTVVSILKINSQLKHIFKTSLTVADKIEDQKKELDGFLSILCNNLHELQENTICSLVESQKQCGNLTEDLKTIKQTHSQELCKLMNLWTERFCALEEKCENIQKPLSSVQENIQQKSKDIVNKMTFHSQKFCADSDGFSQELRNFNQEGTKLVEESVKHSDKLNGNLEKISQETEQRCESLNTRTVYFSEQWVSSLNEREQELHNLLEVVSQCCEASSSDITEKSDGRKAAHEKQHNIFLDQMTIDEDKLIAQNLELNETIKIGLTKLNCFLEQDLKLDIPTGTTPQRKSYLYPSTLVRTEPREHLLDQLKRKQPELLMMLNCSENNKEETIPDVDVEEAVLGQYTEEPLSQEPSVDAGVDCSSIGGVPFFQHKKSHGKDKENRGINTLERSKVEETTEHLVTKSRLPLRAQINL TTTRP0H TT Clinical trial TTTRP0H RC R-HSA-2132295:MHC class II antigen presentation; R-HSA-983189:Kinesins TTV9A7R ID TTV9A7R TTV9A7R TN Lactoylglutathione lyase (GLO1) TTV9A7R UP Q04760 TTV9A7R UC LGUL_HUMAN TTV9A7R BC Carbon-sulfur lyases TTV9A7R SN S-D-lactoylglutathione methylglyoxal lyase; Methylglyoxalase; Ketone-aldehyde mutase; Glyoxalase I; GlxI; Glx I; GLO1; Aldoketomutase TTV9A7R GN GLO1 TTV9A7R FC Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF- kappa-B. Required for normal osteoclastogenesis. TTV9A7R EC EC 4.4.1.5 TTV9A7R PD 3W0U; 3W0T; 3VW9; 1QIP; 1QIN TTV9A7R SQ MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM TTV9A7R TT Clinical trial TTV9A7R KE hsa00620:Pyruvate metabolism TTV9A7R RC R-HSA-70268:Pyruvate metabolism TT5MLC4 ID TT5MLC4 TT5MLC4 TN Leukocyte proteinase-3 (PRTN3) TT5MLC4 UP P24158 TT5MLC4 UC PRTN3_HUMAN TT5MLC4 BC Peptidase TT5MLC4 SN Wegener autoantigen; PR3; PR-3; P29; Neutrophil proteinase 4; NP4; NP-4; Myeloblastin; MBN; Leukocyte proteinase 3; CANCA antigen; C-ANCA antigen; AGP7 TT5MLC4 GN PRTN3 TT5MLC4 FC By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177. Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). TT5MLC4 EC EC 3.4.21.76 TT5MLC4 PD 1FUJ TT5MLC4 SQ MAHRPPSPALASVLLALLLSGAARAAEIVGGHEAQPHSRPYMASLQMRGNPGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQQHFSVAQVFLNNYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPAQVLQELNVTVVTFFCRPHNICTFVPRRKAGICFGDSGGPLICDGIIQGIDSFVIWGCATRLFPDFFTRVALYVDWIRSTLRRVEAKGRP TT5MLC4 TT Clinical trial TT5MLC4 RC R-HSA-140875:Common Pathway of Fibrin Clot Formation TTVJX54 ID TTVJX54 TTVJX54 TN Leukotriene B4 receptor 2 (LTB4R2) TTVJX54 UP Q9NPC1 TTVJX54 UC LT4R2_HUMAN TTVJX54 BC GPCR rhodopsin TTVJX54 SN Seven transmembrane receptor BLTR2; Leukotriene B4 receptor BLT2; Leukotriene B(4) receptor BLT2; LTB4-R2; LTB4-R 2; LTB4 receptor JULF2; BLTR2; BLT2R TTVJX54 GN LTB4R2 TTVJX54 FC Mediates chemotaxis of granulocytes and macrophages. The response is mediated via G-proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTB4 > 12-epi-LTB4 > LTB5 > LTB3. Low-affinity receptor for leukotrienes including leukotriene B4. TTVJX54 SQ MSVCYRPPGNETLLSWKTSRATGTAFLLLAALLGLPGNGFVVWSLAGWRPARGRPLAATLVLHLALADGAVLLLTPLFVAFLTRQAWPLGQAGCKAVYYVCALSMYASVLLTGLLSLQRCLAVTRPFLAPRLRSPALARRLLLAVWLAALLLAVPAAVYRHLWRDRVCQLCHPSPVHAAAHLSLETLTAFVLPFGLMLGCYSVTLARLRGARWGSGRHGARVGRLVSAIVLAFGLLWAPYHAVNLLQAVAALAPPEGALAKLGGAGQAARAGTTALAFFSSSVNPVLYVFTAGDLLPRAGPRFLTRLFEGSGEARGGGRSREGTMELRTTPQLKVVGQGRGNGDPGGGMEKDGPEWDL TTVJX54 TT Clinical trial TTVJX54 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTVJX54 RC R-HSA-391906:Leukotriene receptors; R-HSA-416476:G alpha (q) signalling events TTNR0UQ ID TTNR0UQ TTNR0UQ TN Lysine-specific histone demethylase 1 (LSD) TTNR0UQ UP O60341 TTNR0UQ UC KDM1A_HUMAN TTNR0UQ BC CH-NH(2) donor oxidoreductase TTNR0UQ SN Lysine-specific histone demethylase 1A; LSD1; KIAA0601; KDM1; Flavin-containing amine oxidase domain-containing protein 2; BRAF35-HDAC complex protein BHC110; AOF2 TTNR0UQ GN KDM1A TTNR0UQ FC Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. TTNR0UQ EC EC 1.-.-.- TTNR0UQ PD 6NQU; 6NQM; 5YJB; 5X60; 5LHI TTNR0UQ SQ MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM TTNR0UQ TT Clinical trial TTNR0UQ FM Paired donor oxidoreductase TTNR0UQ RC R-HSA-3214815:HDACs deacetylate histones; R-HSA-5625886:Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTQ6S1K ID TTQ6S1K TTQ6S1K TN Lysophosphatidic acid receptor 1 (LPAR1) TTQ6S1K UP Q92633 TTQ6S1K UC LPAR1_HUMAN TTQ6S1K BC GPCR rhodopsin TTQ6S1K SN Lysophosphatidic acid receptor Edg-2; LPA1; LPA-1; LPA receptor 1; EDG2; EDG 2 receptor TTQ6S1K GN LPAR1 TTQ6S1K FC Plays a role in the reorganization of the actin cytoskeleton, cell migration, differentiation and proliferation, and thereby contributes to the responses to tissue damage and infectious agents. Activates downstream signaling cascades via the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Signaling inhibits adenylyl cyclase activity and decreases cellular cAMP levels. Signaling triggers an increase of cytoplasmic Ca(2+) levels. Activates RALA; this leads to the activation of phospholipase C (PLC) and the formation of inositol 1,4,5-trisphosphate. Signaling mediates activation of down-stream MAP kinases. Contributes to the regulation of cell shape. Promotes Rho-dependent reorganization of the actin cytoskeleton in neuronal cells and neurite retraction. Promotes the activation of Rho and the formation of actin stress fibers. Promotes formation of lamellipodia at the leading edge of migrating cells via activation of RAC1. Through its function as lysophosphatidic acid receptor, plays a role in chemotaxis and cell migration, including responses to injury and wounding. Plays a role in triggering inflammation in response to bacterial lipopolysaccharide (LPS) via its interaction with CD14. Promotes cell proliferation in response to lysophosphatidic acid. Required for normal skeleton development. May play a role in osteoblast differentiation. Required for normal brain development. Required for normal proliferation, survival and maturation of newly formed neurons in the adult dentate gyrus. Plays a role in pain perception and in the initiation of neuropathic pain. Receptor for lysophosphatidic acid (LPA). TTQ6S1K PD 4Z36; 4Z35; 4Z34 TTQ6S1K SQ MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVCIFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVSTWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGAIPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMSRHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLAEFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSNDHSVV TTQ6S1K TT Clinical trial TTQ6S1K FM GPCR rhodopsin TTQ6S1K KE hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04540:Gap junction; hsa05200:Pathways in cancer TTQ6S1K RC R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events; R-HSA-419408:Lysosphingolipid and LPA receptors TT2AST1 ID TT2AST1 TT2AST1 TN Macrophage migration inhibitory factor (MIF) TT2AST1 UP P14174 TT2AST1 UC MIF_HUMAN TT2AST1 BC Intramolecular oxidoreductase TT2AST1 SN Phenylpyruvate tautomerase; MMIF; L-dopachrome tautomerase; L-dopachrome isomerase; Glycosylation-inhibiting factor; GLIF; GIF TT2AST1 GN MIF TT2AST1 FC Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity. Pro-inflammatory cytokine. TT2AST1 EC EC 5.3.2.1 TT2AST1 PD 6FVH; 6FVE; 6CBH; 6CBG; 6CBF TT2AST1 SQ MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA TT2AST1 TT Clinical trial TT2AST1 FM Intramolecular oxidoreductases TT2AST1 KE hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism TTBQ3OC ID TTBQ3OC TTBQ3OC TN Macrophage-stimulating protein receptor (RON) TTBQ3OC UP Q04912 TTBQ3OC UC RON_HUMAN TTBQ3OC BC Kinase TTBQ3OC SN p185Ron; Proteintyrosine kinase 8; Macrophagestimulating protein receptor beta chain; Macrophagestimulating protein receptor; MST1R; MSP receptor; CDw136; CD136 TTBQ3OC GN MST1R TTBQ3OC FC Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Plays also a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand. TTBQ3OC EC EC 2.7.10.1 TTBQ3OC PD 4QT8; 4FWW; 3PLS TTBQ3OC SQ MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVASPLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVTDDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGVGPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAWHFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRPVPRKDFVEEFECELEPLGTQAVGPTNVSLTVTNMPPGKHFRVDGTSVLRGFSFMEPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVNGTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWTFQYREDPVVLSISPNCGYINSHITICGQHLTSAWHLVLSFHDGLRAVESRCERQLPEQQLCRLPEYVVRDPQGWVAGNLSARGDGAAGFTLPGFRFLPPPHPPSANLVPLKPEEHAIKFEYIGLGAVADCVGINVTVGGESCQHEFRGDMVVCPLPPSLQLGQDGAPLQVCVDGECHILGRVVRPGPDGVPQSTLLGILLPLLLLVAALATALVFSYWWRRKQLVLPPNLNDLASLDQTAGATPLPILYSGSDYRSGLALPAIDGLDSTTCVHGASFSDSEDESCVPLLRKESIQLRDLDSALLAEVKDVLIPHERVVTHSDRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSALLGDHYVQLPATYMNLGPSTSHEMNVRPEQPQFSPMPGNVRRPRPLSEPPRPT TTBQ3OC TT Clinical trial TTOMWSY ID TTOMWSY TTOMWSY TN Mammalian disintegrin-metalloprotease (ADAM10) TTOMWSY UP O14672 TTOMWSY UC ADA10_HUMAN TTOMWSY BC Peptidase TTOMWSY SN Mammalian disintegrinmetalloprotease; MADM; Kuzbanian protein homolog; KUZ; Disintegrin and metalloproteinase domaincontaining protein 10; Disintegrin and metalloproteinase domain-containing protein 10; CDw156; CD156c; ADAM 10 TTOMWSY GN ADAM10 TTOMWSY FC Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3. May regulate the EFNA5-EPHA3 signaling. Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. TTOMWSY EC EC 3.4.24.81 TTOMWSY PD 6BE6; 6BDZ; 1M1I TTOMWSY SQ MVLLRVLILLLSWAAGMGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLRLDFHAHGRHFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIQTRGGTFYVEPAERYIKDRTLPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEVTQIPQEEHAANGPELLRKKRTTSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMDPSTCASTGSVQWSRHFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPQRQRPRESYQMGHMRR TTOMWSY TT Clinical trial TTOMWSY FM Peptidase TTOMWSY KE hsa05010:Alzheimer's disease; hsa05120:Epithelial cell signaling in Helicobacter pylori infection TTOMWSY RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-2122948:Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2660826:Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant; R-HSA-2691232:Constitutive Signaling by NOTCH1 HD Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-2979096:NOTCH2 Activation and Transmission of Signal to the Nucleus; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TTFRV98 ID TTFRV98 TTFRV98 TN Melanoma antigen gp75 (TYRP1) TTFRV98 UP P17643 TTFRV98 UC TYRP1_HUMAN TTFRV98 BC Tyrosinase TTFRV98 SN Tyrosinaserelated protein 1; TYRP1; TRP; Glycoprotein 75; Catalase B; 5,6dihydroxyindole2carboxylic acid oxidase TTFRV98 GN TYRP1 TTFRV98 FC Oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA)into indole-5,6-quinone-2-carboxylic acid. May regulate or influence the type of melanin synthesized. TTFRV98 EC EC 1.14.18.- TTFRV98 PD 5M8T; 5M8S; 5M8R; 5M8Q; 5M8P TTFRV98 SQ MSAPKLLSLGCIFFPLLLFQQARAQFPRQCATVEALRSGMCCPDLSPVSGPGTDRCGSSSGRGRCEAVTADSRPHSPQYPHDGRDDREVWPLRFFNRTCHCNGNFSGHNCGTCRPGWRGAACDQRVLIVRRNLLDLSKEEKNHFVRALDMAKRTTHPLFVIATRRSEEILGPDGNTPQFENISIYNYFVWTHYYSVKKTFLGVGQESFGEVDFSHEGPAFLTWHRYHLLRLEKDMQEMLQEPSFSLPYWNFATGKNVCDICTDDLMGSRSNFDSTLISPNSVFSQWRVVCDSLEDYDTLGTLCNSTEDGPIRRNPAGNVARPMVQRLPEPQDVAQCLEVGLFDTPPFYSNSTNSFRNTVEGYSDPTGKYDPAVRSLHNLAHLFLNGTGGQTHLSPNDPIFVLLHTFTDAVFDEWLRRYNADISTFPLENAPIGHNRQYNMVPFWPPVTNTEMFVTAPDNLGYTYEIQWPSREFSVPEIIAIAVVGALLLVALIFGTASYLIRARRSMDEANQPLLTDQYQCYAEEYEKLQNPNQSVV TTFRV98 TT Clinical trial TTFRV98 KE hsa00350:Tyrosine metabolism; hsa01100:Metabolic pathways; hsa04916:Melanogenesis TTXJ47W ID TTXJ47W TTXJ47W TN Metabotropic glutamate receptor 2 (mGluR2) TTXJ47W UP Q14416 TTXJ47W UC GRM2_HUMAN TTXJ47W BC GPCR glutamate TTXJ47W SN mGLUR2; Group II metabotropic glutamate receptor; Glutamate receptor mGLU2; GPRC1B TTXJ47W GN GRM2 TTXJ47W FC Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. May mediate suppression of neurotransmission or may be involved in synaptogenesis or synaptic stabilization. G-protein coupled receptor for glutamate. TTXJ47W PD 5KZQ; 5KZN; 5CNJ; 5CNI; 4XAS TTXJ47W SQ MGSLLALLALLLLWGAVAEGPAKKVLTLEGDLVLGGLFPVHQKGGPAEDCGPVNEHRGIQRLEAMLFALDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATHGDAPTAITGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAASQRLNASFTWVASDGWGALESVVAGSEGAAEGAITIELASYPISDFASYFQSLDPWNNSRNPWFREFWEQRFRCSFRQRDCAAHSLRAVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADTHNEVRFDRFGDGIGRYNIFTYLRAGSGRYRYQKVGYWAEGLTLDTSLIPWASPSAGPLPASRCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNASLTGCFELPQEYIRWGDAWAVGPVTIACLGALATLFVLGVFVRHNATPVVKASGRELCYILLGGVFLCYCMTFIFIAKPSTAVCTLRRLGLGTAFSVCYSALLTKTNRIARIFGGAREGAQRPRFISPASQVAICLALISGQLLIVVAWLVVEAPGTGKETAPERREVVTLRCNHRDASMLGSLAYNVLLIALCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCVSVSLSGSVVLGCLFAPKLHIILFQPQKNVVSHRAPTSRFGSAAARASSSLGQGSGSQFVPTVCNGREVVDSTTSSL TTXJ47W TT Clinical trial TTXJ47W FM GPCR glutamate TTXJ47W KE hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse; hsa05030:Cocaine addiction TTXJ47W RC R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors) TT8A9EF ID TT8A9EF TT8A9EF TN Metabotropic glutamate receptor 3 (mGluR3) TT8A9EF UP Q14832 TT8A9EF UC GRM3_HUMAN TT8A9EF BC GPCR glutamate TT8A9EF SN mGLUR3; Group III metabotropic glutamate receptor; GPRC1C TT8A9EF GN GRM3 TT8A9EF FC Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. G-protein coupled receptor for glutamate. TT8A9EF PD 6B7H; 5CNM; 5CNK; 4XAR; 3SM9 TT8A9EF SQ MKMLTRLQVLTLALFSKGFLLSLGDHNFLRREIKIEGDLVLGGLFPINEKGTGTEECGRINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEFVRASLTKVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNICIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRANASFTWVASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFRDFWEQKFQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLCPNTTKLCDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNFQNVGGKYSYLKVGHWAETLSLDVNSIHWSRNSVPTSQCSDPCAPNEMKNMQPGDVCCWICIPCEPYEYLADEFTCMDCGSGQWPTADLTGCYDLPEDYIRWEDAWAIGPVTIACLGFMCTCMVVTVFIKHNNTPLVKASGRELCYILLFGVGLSYCMTFFFIAKPSPVICALRRLGLGSSFAICYSALLTKTNCIARIFDGVKNGAQRPKFISPSSQVFICLGLILVQIVMVSVWLILEAPGTRRYTLAEKRETVILKCNVKDSSMLISLTYDVILVILCTVYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCISVSLSGFVVLGCLFAPKVHIILFQPQKNVVTHRLHLNRFSVSGTGTTYSQSSASTYVPTVCNGREVLDSTTSSL TT8A9EF TT Clinical trial TT8A9EF FM GPCR glutamate TT8A9EF KE hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse; hsa05030:Cocaine addiction TT8A9EF RC R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors) TTHS256 ID TTHS256 TTHS256 TN Metabotropic glutamate receptor 5 (mGluR5) TTHS256 UP P41594 TTHS256 UC GRM5_HUMAN TTHS256 BC GPCR glutamate TTHS256 SN MGLUR5; GPRC1E TTHS256 GN GRM5 TTHS256 FC G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current. Plays an important role in the regulation of synaptic plasticity and the modulation of the neural network activity. TTHS256 PD 6N52; 6N51; 6N50; 6N4Y; 6N4X TTHS256 SQ MVLLLILSVLLLKEDVRGSAQSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRDSLISSEEEEGLVRCVDGSSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNHRNPWFQEFWQHRFQCRLEGFPQENSKYNKTCNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAMKPIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDDEVWSKKSNIIRSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYVFDEYTCKACQLGSWPTDDLTGCDLIPVQYLRWGDPEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCMFVPKVYIILAKPERNVRSAFTTSTVVRMHVGDGKSSSAASRSSSLVNLWKRRGSSGETLRYKDRRLAQHKSEIECFTPKGSMGNGGRATMSSSNGKSVTWAQNEKSSRGQHLWQRLSIHINKKENPNQTAVIKPFPKSTESRGLGAGAGAGGSAGGVGATGGAGCAGAGPGGPESPDAGPKALYDVAEAEEHFPAPARPRSPSPISTLSHRAGSASRTDDDVPSLHSEPVARSSSSQGSLMEQISSVVTRFTANISELNSMMLSTAAPSPGVGAPLCSSYLIPKEIQLPTTMTTFAEIQPLPAIEVTGGAQPAAGAQAAGDAARESPAAGPEAAAAKPDLEELVALTPPSPFRDSVDSGSTTPNSPVSESALCIPSSPKYDTLIIRDYTQSSSSL TTHS256 TT Clinical trial TTHS256 FM GPCR glutamate TTHS256 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04720:Long-term potentiation; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa05016:Huntington's disease TTHS256 RC R-HSA-416476:G alpha (q) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors) TTZL0OI ID TTZL0OI TTZL0OI TN Methionine aminopeptidase 2 (METAP2) TTZL0OI UP P50579 TTZL0OI UC MAP2_HUMAN TTZL0OI BC Peptidase TTZL0OI SN Peptidase M 2; P67eIF2; P67; MetAP 2; METAP2; Initiation factor 2 associated 67 kDa glycoprotein; (MetAP)-2 TTZL0OI GN METAP2 TTZL0OI FC Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). TTZL0OI EC EC 3.4.11.18 TTZL0OI PD 6QEJ; 6QEI; 6QEH; 6QEG; 6QEF TTZL0OI SQ MAGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSAAGEQEPDKESGASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY TTZL0OI TT Clinical trial TTZL0OI RC R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade TTFLN4T ID TTFLN4T TTFLN4T TN Mitochondrial aldehyde dehydrogenase (ALDH2) TTFLN4T UP P05091 TTFLN4T UC ALDH2_HUMAN TTFLN4T BC Aldehyde/oxo donor oxidoreductase TTFLN4T SN Aldehyde dehydrogenase, mitochondrial; ALDM; ALDHI; ALDH-E2; ALDH class 2 TTFLN4T GN ALDH2 TTFLN4T FC Second enzyme of the major oxidative pathway of alcohol metabolism. Catalyzes the chemical transformation from acetaldehyde to acetic acid. Additionally, functions as a protector against oxidative stress. TTFLN4T EC EC 1.2.1.3 TTFLN4T PD 5L13; 4KWG; 4KWF; 4FR8; 4FQF TTFLN4T SQ MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS TTFLN4T TT Clinical trial TTFLN4T KE hsa00010:Glycolysis / Gluconeogenesis; hsa00040:Pentose and glucuronate interconversions; hsa00053:Ascorbate and aldarate metabolism; hsa00071:Fatty acid degradation; hsa00280:Valine, leucine and isoleucine degradation; hsa00310:Lysine degradation; hsa00330:Arginine and proline metabolism; hsa00340:Histidine metabolism; hsa00380:Tryptophan metabolism; hsa00410:beta-Alanine metabolism; hsa00561:Glycerolipid metabolism; hsa00620:Pyruvate metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics TTNAY0P ID TTNAY0P TTNAY0P TN Monocyte chemotactic and activating factor (CCL2) TTNAY0P UP P13500 TTNAY0P UC CCL2_HUMAN TTNAY0P BC Cytokine: CC chemokine TTNAY0P SN Small-inducible cytokine A2; SCYA2; Monocyte secretory protein JE; Monocyte chemotactic protein 1; Monocyte chemoattractant protein-1; Monocyte Chemoattractant Protein 1; MCP1; MCP-1; MCAF; HC11; C-C motif chemokine 2 TTNAY0P GN CCL2 TTNAY0P FC Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions. Exhibits a chemotactic activity for monocytes and basophils but not neutrophils or eosinophils. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis. Acts as a ligand for C-C chemokine receptor CCR2. TTNAY0P PD 4ZK9; 4R8I; 4DN4; 3IFD; 2NZ1 TTNAY0P SQ MKVSAALLCLLLIAATFIPQGLAQPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWVQDSMDHLDKQTQTPKT TTNAY0P TT Clinical trial TTNAY0P FM Cytokine: CC chemokine TTNAY0P KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa05142:Chagas disease (American trypanosomiasis); hsa05144:Malaria; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05323:Rheumatoid arthritis TTNAY0P RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-380994:ATF4 activates genes TTR0SWN ID TTR0SWN TTR0SWN TN M-phase inducer phosphatase 2 (MPIP2) TTR0SWN UP P30305 TTR0SWN UC MPIP2_HUMAN TTR0SWN BC Phosphoric monoester hydrolase TTR0SWN SN Dual specificity phosphatase Cdc25B; Cdc25B phosphatase; CDC25HU2 TTR0SWN GN CDC25B TTR0SWN FC Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Directly dephosphorylates CDK1 and stimulates its kinase activity. The three isoforms seem to have a different level of activity. Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. TTR0SWN EC EC 3.1.3.48 TTR0SWN PD 4WH9; 4WH7; 3FQU; 3FQT; 2UZQ TTR0SWN SQ MEVPQPEPAPGSALSPAGVCGGAQRPGHLPGLLLGSHGLLGSPVRAAASSPVTTLTQTMHDLAGLGSETPKSQVGTLLFRSRSRLTHLSLSRRASESSLSSESSESSDAGLCMDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHSPVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ TTR0SWN TT Clinical trial TTR0SWN FM Phosphoric monoester hydrolases TTR0SWN KE hsa04010:MAPK signaling pathway; hsa04110:Cell cycle; hsa04914:Progesterone-mediated oocyte maturation; hsa05206:MicroRNAs in cancer TTR0SWN RC R-HSA-157881:Cyclin B2 mediated events; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition; R-HSA-69656:Cyclin A:Cdk2-associated events at S phase entry TT5KPZR ID TT5KPZR TT5KPZR TN Neuronal acetylcholine receptor beta-2 (CHRNB2) TT5KPZR UP P17787 TT5KPZR UC ACHB2_HUMAN TT5KPZR BC Neurotransmitter receptor TT5KPZR SN Nicotinic acetylcholine receptor beta2; Nicotinic acetylcholine receptor beta 2-subunit protein; CHRNB2; Beta-2 nAChR; Alpha-4/beta-2 nicotinic receptor TT5KPZR GN CHRNB2 TT5KPZR FC After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodiun ions. TT5KPZR PD 6CNK; 6CNJ; 5KXI; 2LM2; 2KSR TT5KPZR SQ MARRCGPVALLLGFGLLRLCSGVWGTDTEERLVEHLLDPSRYNKLIRPATNGSELVTVQLMVSLAQLISVHEREQIMTTNVWLTQEWEDYRLTWKPEEFDNMKKVRLPSKHIWLPDVVLYNNADGMYEVSFYSNAVVSYDGSIFWLPPAIYKSACKIEVKHFPFDQQNCTMKFRSWTYDRTEIDLVLKSEVASLDDFTPSGEWDIVALPGRRNENPDDSTYVDITYDFIIRRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTVFLLLISKIVPPTSLDVPLVGKYLMFTMVLVTFSIVTSVCVLNVHHRSPTTHTMAPWVKVVFLEKLPALLFMQQPRHHCARQRLRLRRRQREREGAGALFFREAPGADSCTCFVNRASVQGLAGAFGAEPAPVAGPGRSGEPCGCGLREAVDGVRFIADHMRSEDDDQSVSEDWKYVAMVIDRLFLWIFVFVCVFGTIGMFLQPLFQNYTTTTFLHSDHSAPSSK TT5KPZR TT Clinical trial TT5KPZR KE hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa05033:Nicotine addiction TT5KPZR RC R-HSA-629587:Highly sodium permeable acetylcholine nicotinic receptors; R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors; R-HSA-629597:Highly calcium permeable nicotinic acetylcholine receptors TTTVAFQ ID TTTVAFQ TTTVAFQ TN Neuronal acetylcholine receptor beta-4 (CHRNB4) TTTVAFQ UP P30926 TTTVAFQ UC ACHB4_HUMAN TTTVAFQ BC Neurotransmitter receptor TTTVAFQ SN CHRNB4; Beta-4 nAChR TTTVAFQ GN CHRNB4 TTTVAFQ FC After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. TTTVAFQ PD 2ASG TTTVAFQ SQ MRRAPSLVLFFLVALCGRGNCRVANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIKLQLSLAQLISVNEREQIMTTNVWLKQEWTDYRLTWNSSRYEGVNILRIPAKRIWLPDIVLYNNADGTYEVSVYTNLIVRSNGSVLWLPPAIYKSACKIEVKYFPFDQQNCTLKFRSWTYDHTEIDMVLMTPTASMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLTTLLAILVFYLPSDCGEKMTLCISVLLALTFFLLLISKIVPPTSLDVPLIGKYLMFTMVLVTFSIVTSVCVLNVHHRSPSTHTMAPWVKRCFLHKLPTFLFMKRPGPDSSPARAFPPSKSCVTKPEATATSTSPSNFYGNSMYFVNPASAASKSPAGSTPVAIPRDFWLRSSGRFRQDVQEALEGVSFIAQHMKNDDEDQSVVEDWKYVAMVVDRLFLWVFMFVCVLGTVGLFLPPLFQTHAASEGPYAAQRD TTTVAFQ TT Clinical trial TTTVAFQ KE hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse TTTVAFQ RC R-HSA-629587:Highly sodium permeable acetylcholine nicotinic receptors; R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors; R-HSA-629597:Highly calcium permeable nicotinic acetylcholine receptors TT5TKPM ID TT5TKPM TT5TKPM TN Neutral endopeptidase (MME) TT5TKPM UP P08473 TT5TKPM UC NEP_HUMAN TT5TKPM BC Peptidase TT5TKPM SN Skin fibroblast elastase; SFE; Neutral endopeptidase 24.11; Neprilysin; NEP protein; Enkephalinase; EPN; Common acute lymphocytic leukemia antigen; CD10; CALLA; Atriopeptidase TT5TKPM GN MME TT5TKPM FC Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers. Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. TT5TKPM EC EC 3.4.24.11 TT5TKPM PD 6GID; 5JMY; 4CTH; 2YB9; 2QPJ TT5TKPM SQ MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW TT5TKPM TT Clinical trial TT5TKPM FM Peptidase TT5TKPM KE hsa04614:Renin-angiotensin system; hsa04640:Hematopoietic cell lineage; hsa04974:Protein digestion and absorption; hsa05010:Alzheimer's disease TT5TKPM RC R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins TTD1WIG ID TTD1WIG TTD1WIG TN Nicotinamide phosphoribosyltransferase (NAMPT) TTD1WIG UP P43490 TTD1WIG UC NAMPT_HUMAN TTD1WIG BC Glycosyltransferases TTD1WIG SN Visfatin; PreBcell colonyenhancing factor 1; PreB cellenhancing factor; Pre-B-cell colony-enhancing factor 1; Pre-B cell-enhancing factor; PBEF1; PBEF; Nampt; NAmPRTase TTD1WIG GN NAMPT TTD1WIG FC It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-ARNTL/BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression. Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. TTD1WIG EC EC 2.4.2.12 TTD1WIG PD 6B76; 6B75; 6AZJ; 6ATB; 6.00E+68 TTD1WIG SQ MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFYGLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIVSRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINTLQEIVEGMKQKMWSIENIAFGSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVADPNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHTVFKNGKVTKSYSFDEIRKNAQLNIELEAAHH TTD1WIG TT Clinical trial TTD1WIG FM Pentosyltransferase TTD1WIG KE hsa00760:Nicotinate and nicotinamide metabolism; hsa01100:Metabolic pathways TTD1WIG RC R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression TTNT7K8 ID TTNT7K8 TTNT7K8 TN Nociceptin receptor (OPRL1) TTNT7K8 UP P41146 TTNT7K8 UC OPRX_HUMAN TTNT7K8 BC GPCR rhodopsin TTNT7K8 SN Orphanin FQ receptor; Opioid-receptor-like 1; Opioid receptor like-1 receptor; Opioid receptor 4; ORL-1 receptor; ORL-1; OPRL1; OP(4); Kappa-type 3 opioid receptor; KOR-3 TTNT7K8 GN OPRL1 TTNT7K8 FC G-protein coupled opioid receptor that functions as receptor for the endogenous neuropeptide nociceptin. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling via G proteins mediates inhibition of adenylate cyclase activity and calcium channel activity. Arrestins modulate signaling via G proteins and mediate the activation of alternative signaling pathways that lead to the activation of MAP kinases. Plays a role in modulating nociception and the perception of pain. Plays a role in the regulation of locomotor activity by the neuropeptide nociceptin. TTNT7K8 PD 5DHH; 5DHG; 4EA3 TTNT7K8 SQ MEPLFPAPFWEVIYGSHLQGNLSLLSPNHSLLPPHLLLNASHGAFLPLGLKVTIVGLYLAVCVGGLLGNCLVMYVILRHTKMKTATNIYIFNLALADTLVLLTLPFQGTDILLGFWPFGNALCKTVIAIDYYNMFTSTFTLTAMSVDRYVAICHPIRALDVRTSSKAQAVNVAIWALASVVGVPVAIMGSAQVEDEEIECLVEIPTPQDYWGPVFAICIFLFSFIVPVLVISVCYSLMIRRLRGVRLLSGSREKDRNLRRITRLVLVVVAVFVGCWTPVQVFVLAQGLGVQPSSETAVAILRFCTALGYVNSCLNPILYAFLDENFKACFRKFCCASALRRDVQVSDRVRSIAKDVALACKTSETVPRPA TTNT7K8 TT Clinical trial TTNT7K8 KE hsa04080:Neuroactive ligand-receptor interaction TTNT7K8 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTOZHQC ID TTOZHQC TTOZHQC TN P2Y purinoceptor 2 (P2RY2) TTOZHQC UP P41231 TTOZHQC UC P2RY2_HUMAN TTOZHQC BC GPCR rhodopsin TTOZHQC SN P2Y2; P2U1; P2U receptor; P2U purinoceptor 1; P2U nucleotide receptor; P2RY2; Adenosine P2Y2 receptor TTOZHQC GN P2RY2 TTOZHQC FC Receptor for ATP and UTP coupled to G-proteins thatactivate a phosphatidylinositol-calcium second messenger system. The affinity range is UTP = ATP > ATP-gamma-S >> 2-methylthio-ATP = ADP. TTOZHQC PD 1Z8E TTOZHQC SQ MAADLGPWNDTINGTWDGDELGYRCRFNEDFKYVLLPVSYGVVCVPGLCLNAVALYIFLCRLKTWNASTTYMFHLAVSDALYAASLPLLVYYYARGDHWPFSTVLCKLVRFLFYTNLYCSILFLTCISVHRCLGVLRPLRSLRWGRARYARRVAGAVWVLVLACQAPVLYFVTTSARGGRVTCHDTSAPELFSRFVAYSSVMLGLLFAVPFAVILVCYVLMARRLLKPAYGTSGGLPRAKRKSVRTIAVVLAVFALCFLPFHVTRTLYYSFRSLDLSCHTLNAINMAYKVTRPLASANSCLDPVLYFLAGQRLVRFARDAKPPTGPSPATPARRRLGLRRSDRTDMQRIEDVLGSSEDSRRTESTPAGSENTKDIRL TTOZHQC TT Clinical trial TTOZHQC KE hsa04080:Neuroactive ligand-receptor interaction; hsa04750:Inflammatory mediator regulation of TRP channels TTOZHQC RC R-HSA-416476:G alpha (q) signalling events; R-HSA-417957:P2Y receptors; R-HSA-5683826:Surfactant metabolism TTNIZ2B ID TTNIZ2B TTNIZ2B TN PCSK9 messenger RNA (PCSK9 mRNA) TTNIZ2B UP Q8NBP7 TTNIZ2B UC PCSK9_HUMAN TTNIZ2B BC mRNA target TTNIZ2B SN Subtilisin/kexin-like protease PC9 (mRNA); Proprotein convertase subtilisin/kexin type 9 (mRNA); Proprotein convertase 9 (mRNA); PSEC0052 (mRNA); PC9 (mRNA); Neural apoptosis-regulated convertase 1 (mRNA); NARC1 (mRNA); NARC-1 (mRNA) TTNIZ2B GN PCSK9 TTNIZ2B FC Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways. Crucial player in the regulation of plasma cholesterol homeostasis. TTNIZ2B EC EC 3.4.21.- TTNIZ2B PD 6MV5; 6F5G; 6E4Z; 6E4Y; 5VLP TTNIZ2B SQ MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEGAVTAVAICCRSRHLAQASQELQ TTNIZ2B TT Clinical trial TTNIZ2B FM mRNA target TT2JWF6 ID TT2JWF6 TT2JWF6 TN Peroxisome proliferator-activated receptor delta (PPARD) TT2JWF6 UP Q03181 TT2JWF6 UC PPARD_HUMAN TT2JWF6 BC Nuclear hormone receptor TT2JWF6 SN Peroxisomeproliferator-activated receptor beta; Peroxisomeproliferator activated receptor beta/delta; Peroxisome proliferator-activated receptor beta; PPARdelta; PPARB; PPAR-delta; PPAR-beta; Nuclear receptor subfamily 1 group C member 2; Nuclear hormone receptor 1; NUCI; NUC1; NR1C2 TT2JWF6 GN PPARD TT2JWF6 FC Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Has a preference for poly-unsaturated fatty acids, such as gamma-linoleic acid and eicosapentanoic acid. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene. Decreases expression of NPC1L1 once activated by a ligand. Ligand-activated transcription factor. TT2JWF6 PD 5ZXI; 5Y7X; 5XMX; 5U46; 5U45 TT2JWF6 SQ MEQPQEEAPEVREEEEKEEVAEAEGAPELNGGPQHALPSSSYTDLSRSSSPPSLLDQLQMGCDGASCGSLNMECRVCGDKASGFHYGVHACEGCKGFFRRTIRMKLEYEKCERSCKIQKKNRNKCQYCRFQKCLALGMSHNAIRFGRMPEAEKRKLVAGLTANEGSQYNPQVADLKAFSKHIYNAYLKNFNMTKKKARSILTGKASHTAPFVIHDIETLWQAEKGLVWKQLVNGLPPYKEISVHVFYRCQCTTVETVRELTEFAKSIPSFSSLFLNDQVTLLKYGVHEAIFAMLASIVNKDGLLVANGSGFVTREFLRSLRKPFSDIIEPKFEFAVKFNALELDDSDLALFIAAIILCGDRPGLMNVPRVEAIQDTILRALEFHLQANHPDAQYLFPKLLQKMADLRQLVTEHAQMMQRIKKTETETSLHPLLQEIYKDMY TT2JWF6 TT Clinical trial TT2JWF6 FM Zinc finger TT2JWF6 KE hsa03320:PPAR signaling pathway; hsa04310:Wnt signaling pathway; hsa05200:Pathways in cancer; hsa05221:Acute myeloid leukemia TT2JWF6 RC R-HSA-200425:Import of palmitoyl-CoA into the mitochondrial matrix; R-HSA-204174:Regulation of pyruvate dehydrogenase (PDH) complex; R-HSA-383280:Nuclear Receptor transcription pathway TTJW4LU ID TTJW4LU TTJW4LU TN Phosphodiesterase 10A (PDE10) TTJW4LU UP Q9Y233 TTJW4LU UC PDE10_HUMAN TTJW4LU BC Phosphoric diester hydrolase TTJW4LU SN cAMP and cAMPinhibited cGMP 3',5'cyclic phosphodiesterase 10A; cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A TTJW4LU GN PDE10A TTJW4LU FC Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate. May play a critical role in regulating cAMP and cGMP levels in the striatum, a region of the brain that contributes to the control of movement and cognition. Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. TTJW4LU EC EC 3.1.4.17 TTJW4LU PD 6MSC; 6MSA; 6IJI; 6IJH; 5ZNL TTJW4LU SQ MRIEERKSQHLTGLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKNNKSEDESAPKEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGDERFPRGTGLESGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVCRGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIRHSECIYRVTMEKLSYHSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIFVYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED TTJW4LU TT Clinical trial TTJW4LU FM Phosphoric diester hydrolases TTJW4LU KE hsa00230:Purine metabolism; hsa05032:Morphine addiction TTJW4LU RC R-HSA-418457:cGMP effects; R-HSA-418555:G alpha (s) signalling events TTJGW1Z ID TTJGW1Z TTJGW1Z TN Phosphodiesterase 2A (PDE2A) TTJGW1Z UP O00408 TTJGW1Z UC PDE2A_HUMAN TTJGW1Z BC Phosphoric diester hydrolase TTJGW1Z SN cGMP-dependent 3',5'-cyclic phosphodiesterase; PDE-II; Cyclic-GMP phosphodiesterase; Cyclic GMP-stimulated phosphodiesterase; Cyclic GMP stimulated phosphodiesterase; CGSPDE; CGS-PDE TTJGW1Z GN PDE2A TTJGW1Z FC Plays an important role in growth and invasion of malignant melanoma cells (e. g. pseudomyxoma peritonei (PMP) cell line). Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. TTJGW1Z EC EC 3.1.4.17 TTJGW1Z PD 6CYD; 6CYC; 6CYB; 6C7J; 6C7I TTJGW1Z SQ MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDISGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCNGLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAVEKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDLDASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVVEDKKSIQLKDLTSEDVQQLQSMLGCELQAMLCVPVISRATDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNFASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMHAFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSHKFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPINGCCSLDAE TTJGW1Z TT Clinical trial TTJGW1Z FM Phosphoric diester hydrolases TTJGW1Z KE hsa00230:Purine metabolism; hsa04022:cGMP-PKG signaling pathway; hsa05032:Morphine addiction TTJGW1Z RC R-HSA-418457:cGMP effects; R-HSA-418555:G alpha (s) signalling events TTZOEBC ID TTZOEBC TTZOEBC TN Phosphodiesterase 9 (PDE9) TTZOEBC UP O76083 TTZOEBC UC PDE9A_HUMAN TTZOEBC BC Phosphoric diester hydrolase TTZOEBC SN High affinity cGMPspecific 3',5'cyclic phosphodiesterase 9A; High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A TTZOEBC GN PDE9A TTZOEBC FC Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein. In brain, involved in cognitive function, such as learning and long-term memory. Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. TTZOEBC EC EC 3.1.4.35 TTZOEBC PD 6A3N; 4Y8C; 4Y87; 4Y86; 4GH6 TTZOEBC SQ MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA TTZOEBC TT Clinical trial TTZOEBC KE hsa00230:Purine metabolism TTZOEBC RC R-HSA-418457:cGMP effects TTTHBCA ID TTTHBCA TTTHBCA TN PI3-kinase beta (PIK3CB) TTTHBCA UP P42338 TTTHBCA UC PK3CB_HUMAN TTTHBCA BC Kinase TTTHBCA SN p110beta; PtdIns3kinase subunit p110beta; PtdIns3kinase subunit beta; PtdIns-3-kinase subunit p110-beta; PtdIns-3-kinase subunit beta; Phosphatidylinositol 4,5bisphosphate 3kinase catalytic subunitbeta isoform; Phosphatidylinositol 4,5bisphosphate 3kinase 110 kDa catalyticsubunit beta; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform; Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta; PIK3C1; PI3kinase subunit beta; PI3Kbeta; PI3K-beta; PI3-kinase subunit beta TTTHBCA GN PIK3CB TTTHBCA FC Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Involved in the activation of AKT1 upon stimulation by G-protein coupled receptors (GPCRs) ligands such as CXCL12, sphingosine 1-phosphate, and lysophosphatidic acid. May also act downstream receptor tyrosine kinases. Required in different signaling pathways for stable platelet adhesion and aggregation. Plays a role in platelet activation signaling triggered by GPCRs, alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) and ITAM (immunoreceptor tyrosine-based activation motif)-bearing receptors such as GP6. Regulates the strength of adhesion of ITGA2B/ ITGB3 activated receptors necessary for the cellular transmission of contractile forces. Required for platelet aggregation induced by F2 (thrombin) and thromboxane A2 (TXA2). Has a role in cell survival. May have a role in cell migration. Involved in the early stage of autophagosome formation. Modulates the intracellular level of PtdIns3P (Phosphatidylinositol 3-phosphate) and activates PIK3C3 kinase activity. May act as a scaffold, independently of its lipid kinase activity to positively regulate autophagy. May have a role in insulin signaling as scaffolding protein in which the lipid kinase activity is not required. May have a kinase-independent function in regulating cell proliferation and in clathrin-mediated endocytosis. Mediator of oncogenic signal in cell lines lacking PTEN. The lipid kinase activity is necessary for its role in oncogenic transformation. Required for the growth of ERBB2 and RAS driven tumors. TTTHBCA EC EC 2.7.1.153 TTTHBCA SQ MCFSFIMPPAMADILDIWAVDSQIASDGSIPVDFLLPTGIYIQLEVPREATISYIKQMLWKQVHNYPMFNLLMDIDSYMFACVNQTAVYEELEDETRRLCDVRPFLPVLKLVTRSCDPGEKLDSKIGVLIGKGLHEFDSLKDPEVNEFRRKMRKFSEEKILSLVGLSWMDWLKQTYPPEHEPSIPENLEDKLYGGKLIVAVHFENCQDVFSFQVSPNMNPIKVNELAIQKRLTIHGKEDEVSPYDYVLQVSGRVEYVFGDHPLIQFQYIRNCVMNRALPHFILVECCKIKKMYEQEMIAIEAAINRNSSNLPLPLPPKKTRIISHVWENNNPFQIVLVKGNKLNTEETVKVHVRAGLFHGTELLCKTIVSSEVSGKNDHIWNEPLEFDINICDLPRMARLCFAVYAVLDKVKTKKSTKTINPSKYQTIRKAGKVHYPVAWVNTMVFDFKGQLRTGDIILHSWSSFPDELEEMLNPMGTVQTNPYTENATALHVKFPENKKQPYYYPPFDKIIEKAAEIASSDSANVSSRGGKKFLPVLKEILDRDPLSQLCENEMDLIWTLRQDCREIFPQSLPKLLLSIKWNKLEDVAQLQALLQIWPKLPPREALELLDFNYPDQYVREYAVGCLRQMSDEELSQYLLQLVQVLKYEPFLDCALSRFLLERALGNRRIGQFLFWHLRSEVHIPAVSVQFGVILEAYCRGSVGHMKVLSKQVEALNKLKTLNSLIKLNAVKLNRAKGKEAMHTCLKQSAYREALSDLQSPLNPCVILSELYVEKCKYMDSKMKPLWLVYNNKVFGEDSVGVIFKNGDDLRQDMLTLQMLRLMDLLWKEAGLDLRMLPYGCLATGDRSGLIEVVSTSETIADIQLNSSNVAAAAAFNKDALLNWLKEYNSGDDLDRAIEEFTLSCAGYCVASYVLGIGDRHSDNIMVKKTGQLFHIDFGHILGNFKSKFGIKRERVPFILTYDFIHVIQQGKTGNTEKFGRFRQCCEDAYLILRRHGNLFITLFALMLTAGLPELTSVKDIQYLKDSLALGKSEEEALKQFKQKFDEALRESWTTKVNWMAHTVRKDYRS TTTHBCA TT Clinical trial TTTHBCA FM Kinase TTTHBCA KE hsa00562:Inositol phosphate metabolism; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04070:Phosphatidylinositol signaling system; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04960:Aldosterone-regulated sodium reabsorption; hsa04973:Carbohydrate digestion and absorption; hsa05100:Bacterial invasion of epithelial cells; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTTHBCA RC R-HSA-109704:PI3K Cascade; R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-198203:PI3K/AKT activation; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-210993:Tie2 Signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-2424491:DAP12 signaling; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-373753:Nephrin interactions; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-912526:Interleukin receptor SHC signaling; R-HSA-912631:Regulation of signaling by CBL TTZ3S8C ID TTZ3S8C TTZ3S8C TN Presenilin 1 (PSEN1) TTZ3S8C UP P49768 TTZ3S8C UC PSN1_HUMAN TTZ3S8C BC Peptidase TTZ3S8C SN S182 protein; Protein S182; Presenilin-1; PSNL1; PS1; PS-1; AD3 TTZ3S8C GN PSEN1 TTZ3S8C FC Requires the presence of the other members of the gamma-secretase complex for protease activity. Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels. Stimulates cell-cell adhesion via its interaction with CDH1; this stabilizes the complexes between CDH1 (E-cadherin) and its interaction partners CTNNB1 (beta-catenin), CTNND1 and JUP (gamma-catenin). Under conditions of apoptosis or calcium influx, cleaves CDH1. This promotes the disassembly of the complexes between CDH1 and CTNND1, JUP and CTNNB1, increases the pool of cytoplasmic CTNNB1, and thereby negatively regulates Wnt signaling. Required for normal embryonic brain and skeleton development, and for normal angiogenesis. Mediates the proteolytic cleavage of EphB2/CTF1 into EphB2/CTF2. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is therefore involved in calcium homeostasis. Involved in the regulation of neurite outgrowth. Is a regulator of presynaptic facilitation, spike transmission and synaptic vesicles replenishment in a process that depends on gamma-secretase activity. It acts through the control of SYT7 presynaptic expression. Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). TTZ3S8C EC EC 3.4.23.- TTZ3S8C PD 6IYC; 6IDF; 5FN5; 5FN4; 5FN3 TTZ3S8C SQ MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI TTZ3S8C TT Clinical trial TTZ3S8C FM Peptidase TTZ3S8C KE hsa04310:Wnt signaling pathway; hsa04330:Notch signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa05010:Alzheimer's disease TTZ3S8C RC R-HSA-1474228:Degradation of the extracellular matrix TTGPQ0F ID TTGPQ0F TTGPQ0F TN Prolyl endopeptidase FAP (FAP) TTGPQ0F UP Q12884 TTGPQ0F UC SEPR_HUMAN TTGPQ0F BC Peptidase TTGPQ0F SN Integral membrane serine protease; Fibroblast activation protein alpha; FAP; Antiplasmin-cleaving enzyme; APCE; 170-kDa melanoma membrane-bound gelatinase TTGPQ0F GN FAP TTGPQ0F FC Cell surface glycoprotein serine protease that participatesin extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble formsexhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2 (PubMed:14751930, PubMed:16223769, PubMed:16480718, PubMed:16410248, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:9065413, PubMed:2172980, PubMed:7923219, PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711). Have also dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16651416, PubMed:16410248, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner. TTGPQ0F EC EC 3.4.21.26 TTGPQ0F PD 1Z68 TTGPQ0F SQ MKTWVKIVFGVATSAVLALLVMCIVLRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD TTGPQ0F TT Clinical trial TTQDMX5 ID TTQDMX5 TTQDMX5 TN Prostaglandin D2 receptor 2 (PTGDR2) TTQDMX5 UP Q9Y5Y4 TTQDMX5 UC PD2R2_HUMAN TTQDMX5 BC GPCR rhodopsin TTQDMX5 SN PTGDR2; Chemoattractant receptor-homologous molecule expressed on Th2 cells; CD294 TTQDMX5 GN PTGDR2 TTQDMX5 FC Receptor for prostaglandin D2 (PGD2). Coupled to the G(i)-protein. Receptor activation may result in pertussis toxin- sensitive decreases in cAMP levels and Ca(2+) mobilization. PI3K signaling is also implicated in mediating PTGDR2 effects. PGD2 induced receptor internalization. CRTH2 internalization can be regulated by diverse kinases such as, PKC, PKA, ADRBK1/GRK2, GPRK5/GRK5 and GRK6. Receptoractivation is responsible, at least in part, in immune regulation and allergic/inflammation responses. TTQDMX5 PD 6D27; 6D26 TTQDMX5 SQ MSANATLKPLCPILEQMSRLQSHSNTSIRYIDHAAVLLHGLASLLGLVENGVILFVVGCRMRQTVVTTWVLHLALSDLLASASLPFFTYFLAVGHSWELGTTFCKLHSSIFFLNMFASGFLLSAISLDRCLQVVRPVWAQNHRTVAAAHKVCLVLWALAVLNTVPYFVFRDTISRLDGRIMCYYNVLLLNPGPDRDATCNSRQVALAVSKFLLAFLVPLAIIASSHAAVSLRLQHRGRRRPGRFVRLVAAVVAAFALCWGPYHVFSLLEARAHANPGLRPLVWRGLPFVTSLAFFNSVANPVLYVLTCPDMLRKLRRSLRTVLESVLVDDSELGGAGSSRRRRTSSTARSASPLALCSRPEEPRGPARLLGWLLGSCAASPQTGPLNRALSSTSS TTQDMX5 TT Clinical trial TTQDMX5 RC R-HSA-391908:Prostanoid ligand receptors; R-HSA-418594:G alpha (i) signalling events TTPNGDE ID TTPNGDE TTPNGDE TN Prostaglandin E2 receptor EP3 (PTGER3) TTPNGDE UP P43115 TTPNGDE UC PE2R3_HUMAN TTPNGDE BC GPCR rhodopsin TTPNGDE SN Prostanoid EP3 receptor; Prostaglandin E2 receptor EP3 subtype; PGE2-R; PGE2 receptor EP3 subtype; PGE receptor, EP3 subtype; PGE receptor EP3 subtype TTPNGDE GN PTGER3 TTPNGDE FC The activity of this receptor can couple to both the inhibition of adenylate cyclase mediated by G(i) proteins, and to an elevation of intracellular calcium. Required for normal development of fever in response to pyrinogens, including IL1B, prostaglandin E2 and bacterial lipopolysaccharide (LPS). Required for normal potentiation of platelet aggregation by prostaglandin E2, and thus plays a role in the regulation of blood coagulation. Required for increased HCO3(-) secretion in the duodenum in response to mucosal acidification, and thereby contributes to the protection of the mucosa against acid-induced ulceration. Not required for normal kidney function, normal urine volume and osmolality. Receptor for prostaglandin E2 (PGE2). TTPNGDE PD 6M9T; 6AK3 TTPNGDE SQ MKETRGYGGDAPFCTRLNHSYTGMWAPERSAEARGNLTRPPGSGEDCGSVSVAFPITMLLTGFVGNALAMLLVSRSYRRRESKRKKSFLLCIGWLALTDLVGQLLTTPVVIVVYLSKQRWEHIDPSGRLCTFFGLTMTVFGLSSLFIASAMAVERALAIRAPHWYASHMKTRATRAVLLGVWLAVLAFALLPVLGVGQYTVQWPGTWCFISTGRGGNGTSSSHNWGNLFFASAFAFLGLLALTVTFSCNLATIKALVSRCRAKATASQSSAQWGRITTETAIQLMGIMCVLSVCWSPLLIMMLKMIFNQTSVEHCKTHTEKQKECNFFLIAVRLASLNQILDPWVYLLLRKILLRKFCQIRYHTNNYASSSTSLPCQCSSTLMWSDHLER TTPNGDE TT Clinical trial TTPNGDE FM GPCR rhodopsin TTPNGDE KE hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04923:Regulation of lipolysis in adipocytes; hsa05200:Pathways in cancer TTPNGDE RC R-HSA-391908:Prostanoid ligand receptors; R-HSA-418594:G alpha (i) signalling events TT79WV3 ID TT79WV3 TT79WV3 TN Prostaglandin E2 receptor EP4 (PTGER4) TT79WV3 UP P35408 TT79WV3 UC PE2R4_HUMAN TT79WV3 BC GPCR rhodopsin TT79WV3 SN Prostanoid EP4 receptor; Prostaglandin E2 receptor EP4 subtype; PTGER2; PGE2 receptor EP4 subtype; PGE receptor EP4 subtype TT79WV3 GN PTGER4 TT79WV3 FC Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function. TT79WV3 PD 5YWY; 5YHL TT79WV3 SQ MSTPGVNSSASLSPDRLNSPVTIPAVMFIFGVVGNLVAIVVLCKSRKEQKETTFYTLVCGLAVTDLLGTLLVSPVTIATYMKGQWPGGQPLCEYSTFILLFFSLSGLSIICAMSVERYLAINHAYFYSHYVDKRLAGLTLFAVYASNVLFCALPNMGLGSSRLQYPDTWCFIDWTTNVTAHAAYSYMYAGFSSFLILATVLCNVLVCGALLRMHRQFMRRTSLGTEQHHAAAAASVASRGHPAASPALPRLSDFRRRRSFRRIAGAEIQMVILLIATSLVVLICSIPLVVRVFVNQLYQPSLEREVSKNPDLQAIRIASVNPILDPWIYILLRKTVLSKAIEKIKCLFCRIGGSRRERSGQHCSDSQRTSSAMSGHSRSFISRELKEISSTSQTLLPDLSLPDLSENGLGGRNLLPGVPGMGLAQEDTTSLRTLRISETSDSSQGQDSESVLLVDEAGGSGRAGPAPKGSSLQVTFPSETLNLSEKCI TT79WV3 TT Clinical trial TT79WV3 FM GPCR rhodopsin TT79WV3 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04924:Renin secretion; hsa05200:Pathways in cancer TT79WV3 RC R-HSA-391908:Prostanoid ligand receptors; R-HSA-418555:G alpha (s) signalling events TTS78AZ ID TTS78AZ TTS78AZ TN Prostate specific antigen (KLK3) TTS78AZ UP P07288 TTS78AZ UC KLK3_HUMAN TTS78AZ BC Peptidase TTS78AZ SN Seminin; Semenogelase; Prostate-specific antigen; PSA; P-30 antigen; Kallikrein-3; Gamma-seminoprotein; APS TTS78AZ GN KLK3 TTS78AZ FC Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum. TTS78AZ EC EC 3.4.21.77 TTS78AZ PD 3QUM; 2ZCL; 2ZCK; 2ZCH; 2PSA TTS78AZ SQ MWVPVVFLTLSVTWIGAAPLILSRIVGGWECEKHSQPWQVLVASRGRAVCGGVLVHPQWVLTAAHCIRNKSVILLGRHSLFHPEDTGQVFQVSHSFPHPLYDMSLLKNRFLRPGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQEPALGTTCYASGWGSIEPEEFLTPKKLQCVDLHVISNDVCAQVHPQKVTKFMLCAGRWTGGKSTCSGDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVANP TTS78AZ TT Clinical trial TTS78AZ FM Peptidase TTS78AZ KE hsa05200:Pathways in cancer; hsa05215:Prostate cancer TTS78AZ RC R-HSA-381426:Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-5625886:Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 TTYPXQF ID TTYPXQF TTYPXQF TN Protein kinase C beta (PRKCB) TTYPXQF UP P05771 TTYPXQF UC KPCB_HUMAN TTYPXQF BC Kinase TTYPXQF SN Protein kinase C beta type; PRKCB1; PKCB; PKC-beta; PKC-B TTYPXQF GN PRKCB TTYPXQF FC Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. TTYPXQF EC EC 2.7.11.13 TTYPXQF PD 2I0E TTYPXQF SQ MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV TTYPXQF TT Clinical trial TTYPXQF FM Kinase TTYPXQF KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04062:Chemokine signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04070:Phosphatidylinositol signaling system; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04310:Wnt signaling pathway; hsa04370:VEGF signaling pathway; hsa04510:Focal adhesion; hsa04530:Tight junction; hsa04540:Gap junction; hsa04650:Natural killer cell mediated cytotoxicity; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04670:Leukocyte transendothelial migration; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04727:GABAergic synapse; hsa04728:Dopaminergic synapse; hsa04730:Long-term depression; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04911:Insulin secretion; hsa04912:GnRH signaling pathway; hsa04916:Melanogenesis; hsa04918:Thyroid hormone synthesis; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04960:Aldosterone-regulated sodium reabsorption; hsa04961:Endocrine and other factor-regulated calcium reabsorption; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04973:Carbohydrate digestion and absorption; hsa05031:Amphetamine addiction; hsa05032:Morphine addiction; hsa05110:Vibrio cholerae infection; hsa05140:Leishmaniasis; hsa05143:African trypanosomiasis; hsa05146:Amoebiasis; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05214:Glioma; hsa05223:Non-small cell lung cancer; hsa05231:Choline metabolism in cancer TTYPXQF RC R-HSA-114516:Disinhibition of SNARE formation; R-HSA-1169091:Activation of NF-kappaB in B cells; R-HSA-416993:Trafficking of GluR2-containing AMPA receptors; R-HSA-418597:G alpha (z) signalling events; R-HSA-4419969:Depolymerisation of the Nuclear Lamina; R-HSA-5099900:WNT5A-dependent internalization of FZD4; R-HSA-5218921:VEGFR2 mediated cell proliferation; R-HSA-76005:Response to elevated platelet cytosolic Ca2+ TTMS7KP ID TTMS7KP TTMS7KP TN Protein-tyrosine phosphatase 1B (PTP1B) TTMS7KP UP P18031 TTMS7KP UC PTN1_HUMAN TTMS7KP BC Phosphoric monoester hydrolase TTMS7KP SN Tyrosine-protein phosphatase non-receptor type 1; PTP-1B TTMS7KP GN PTPN1 TTMS7KP FC Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET. Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. TTMS7KP EC EC 3.1.3.48 TTMS7KP PD 6CWV; 6CWU; 6BAI; 6B95; 6B90 TTMS7KP SQ MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHNGKCREFFPNHQWVKEETQEDKDCPIKEEKGSPLNAAPYGIESMSQDTEVRSRVVGGSLRGAQAASPAKGEPSLPEKDEDHALSYWKPFLVNMCVATVLTAGAYLCYRFLFNSNT TTMS7KP TT Clinical trial TTMS7KP FM Phosphoric monoester hydrolases TTMS7KP KE hsa04520:Adherens junction; hsa04910:Insulin signaling pathway TTMS7KP RC R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-877312:Regulation of IFNG signaling; R-HSA-912694:Regulation of IFNA signaling; R-HSA-982772:Growth hormone receptor signaling TT7WUAV ID TT7WUAV TT7WUAV TN Protein-tyrosine phosphatase SHP-2 (PTPN11) TT7WUAV UP Q06124 TT7WUAV UC PTN11_HUMAN TT7WUAV BC Phosphoric monoester hydrolase TT7WUAV SN Tyrosine-protein phosphatase non-receptor type 11; SHPTP2; SHP2; SHP-2; SH-PTP3; SH-PTP2; Protein-tyrosine phosphatase SHP2; Protein-tyrosine phosphatase 2C; Protein-tyrosine phosphatase 1D; PTP2C; PTP-2C; PTP-1D TT7WUAV GN PTPN11 TT7WUAV FC Positively regulates MAPK signal transduction pathway. Dephosphorylates GAB1, ARHGAP35 and EGFR. Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulatation of its RhoA binding activity. Dephosphorylates CDC73. Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. TT7WUAV EC EC 3.1.3.48 TT7WUAV PD 6MDD; 6MDC; 6MDB; 6MDA; 6MD9 TT7WUAV SQ MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLADQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQKSFR TT7WUAV TT Clinical trial TT7WUAV FM Phosphoric monoester hydrolases TT7WUAV KE hsa04014:Ras signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05168:Herpes simplex infection; hsa05205:Proteoglycans in cancer; hsa05211:Renal cell carcinoma; hsa05220:Chronic myeloid leukemia TT7WUAV RC R-HSA-1059683:Interleukin-6 signaling; R-HSA-109704:PI3K Cascade; R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-112411:MAPK1 (ERK2) activation; R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1170546:Prolactin receptor signaling; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1295596:Spry regulation of FGF signaling; R-HSA-180292:GAB1 signalosome; R-HSA-210990:PECAM1 interactions; R-HSA-210993:Tie2 Signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-388841:Costimulation by the CD28 family; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-389948:PD-1 signaling; R-HSA-391160:Signal regulatory protein (SIRP) family interactions; R-HSA-418886:Netrin mediated repulsion signals; R-HSA-432142:Platelet sensitization by LDL; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-5654689:PI-3K cascade:FGFR1; R-HSA-5654693:FRS-mediated FGFR1 signaling; R-HSA-5654695:PI-3K cascade:FGFR2; R-HSA-5654699:SHC-mediated cascade:FGFR2; R-HSA-5654700:FRS-mediated FGFR2 signaling; R-HSA-5654706:FRS-mediated FGFR3 signaling; R-HSA-5654710:PI-3K cascade:FGFR3; R-HSA-5654712:FRS-mediated FGFR4 signaling; R-HSA-5654719:SHC-mediated cascade:FGFR4; R-HSA-5654720:PI-3K cascade:FGFR4; R-HSA-5654726:Negative regulation of FGFR1 signaling; R-HSA-5654727:Negative regulation of FGFR2 signaling; R-HSA-5654732:Negative regulation of FGFR3 signaling; R-HSA-5654733:Negative regulation of FGFR4 signaling; R-HSA-877312:Regulation of IFNG signaling; R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912694:Regulation of IFNA signaling; R-HSA-936964:Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon TT371QC ID TT371QC TT371QC TN Puromycin-sensitive aminopeptidase (NPEPPS) TT371QC UP P55786 TT371QC UC PSA_HUMAN TT371QC BC Peptidase TT371QC SN NPEPPS TT371QC GN NPEPPS TT371QC FC Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain moreefficiently than tau from Alzheimer disease brain. TT371QC EC EC 3.4.11.14 TT371QC SQ MWLAAAAPSLARRLLFLGPPPPPLLLLVFSRSSRRRLHSLGLAAMPEKRPFERLPADVSPINYSLCLKPDLLDFTFEGKLEAAAQVRQATNQIVMNCADIDIITASYAPEGDEEIHATGFNYQNEDEKVTLSFPSTLQTGTGTLKIDFVGELNDKMKGFYRSKYTTPSGEVRYAAVTQFEATDARRAFPCWDEPAIKATFDISLVVPKDRVALSNMNVIDRKPYPDDENLVEVKFARTPVMSTYLVAFVVGEYDFVETRSKDGVCVRVYTPVGKAEQGKFALEVAAKTLPFYKDYFNVPYPLPKIDLIAIADFAAGAMENWGLVTYRETALLIDPKNSCSSSRQWVALVVGHELAHQWFGNLVTMEWWTHLWLNEGFASWIEYLCVDHCFPEYDIWTQFVSADYTRAQELDALDNSHPIEVSVGHPSEVDEIFDAISYSKGASVIRMLHDYIGDKDFKKGMNMYLTKFQQKNAATEDLWESLENASGKPIAAVMNTWTKQMGFPLIYVEAEQVEDDRLLRLSQKKFCAGGSYVGEDCPQWMVPITISTSEDPNQAKLKILMDKPEMNVVLKNVKPDQWVKLNLGTVGFYRTQYSSAMLESLLPGIRDLSLPPVDRLGLQNDLFSLARAGIISTVEVLKVMEAFVNEPNYTVWSDLSCNLGILSTLLSHTDFYEEIQEFVKDVFSPIGERLGWDPKPGEGHLDALLRGLVLGKLGKAGHKATLEEARRRFKDHVEGKQILSADLRSPVYLTVLKHGDGTTLDIMLKLHKQADMQEEKNRIERVLGATLLPDLIQKVLTFALSEEVRPQDTVSVIGGVAGGSKHGRKAAWKFIKDNWEELYNRYQGGFLISRLIKLSVEGFAVDKMAGEVKAFFESHPAPSAERTIQQCCENILLNAAWLKRDAESIHQYLLQRKASPPTV TT371QC TT Clinical trial TT371QC RC R-HSA-983168:Antigen processing: Ubiquitination & Proteasome degradation TTGWKQJ ID TTGWKQJ TTGWKQJ TN Rho-associated protein kinase 2 (ROCK2) TTGWKQJ UP O75116 TTGWKQJ UC ROCK2_HUMAN TTGWKQJ BC Kinase TTGWKQJ SN p164 ROCK-2; Rho-associated, coiled-coil-containing protein kinase II; Rho-associated, coiled-coil-containing protein kinase 2; Rho kinase 2; ROCK-II; KIAA0619 TTGWKQJ GN ROCK2 TTGWKQJ FC Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation. Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. TTGWKQJ EC EC 2.7.11.1 TTGWKQJ PD 6ED6; 5U7R; 5U7Q; 4WOT; 4L6Q TTGWKQJ SQ MSRPPPTGKMPGAPETAPGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGFYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIRQHPFFKNDQWHWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENLLLSDSPSCRETDSIQSRKNEESQEIQKKLYTLEEHLSNEMQAKEELEQKCKSVNTRLEKTAKELEEEITLRKSVESALRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKEFINLQSALESERRDRTHGSEIINDLQGRICGLEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDAEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISTAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAPNKPS TTGWKQJ TT Clinical trial TTGWKQJ FM Kinase TTGWKQJ KE hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04310:Wnt signaling pathway; hsa04360:Axon guidance; hsa04510:Focal adhesion; hsa04611:Platelet activation; hsa04670:Leukocyte transendothelial migration; hsa04810:Regulation of actin cytoskeleton; hsa04921:Oxytocin signaling pathway; hsa05130:Pathogenic Escherichia coli infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer TTGWKQJ RC R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-416482:G alpha (12/13) signalling events; R-HSA-416572:Sema4D induced cell migration and growth-cone collapse; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5627117:RHO GTPases Activate ROCKs TTCQ2E5 ID TTCQ2E5 TTCQ2E5 TN RIP2 messenger RNA (RIP2 mRNA) TTCQ2E5 UP O43353 TTCQ2E5 UC RIPK2_HUMAN TTCQ2E5 BC mRNA target TTCQ2E5 SN UNQ277/PRO314/PRO34092 (mRNA); Tyrosine-protein kinase RIPK2 (mRNA); Receptor-interacting serine/threonine-protein kinase 2 (mRNA); Receptor-interacting protein 2 (mRNA); RIP2 (mRNA); RIP-like-interacting CLARP kinase (mRNA); RIP-2 (mRNA); RICK (mRNA); CARDIAK (mRNA); CARD-containing interleukin-1 beta-converting enzyme-associated kinase (mRNA); CARD-containing IL-1 beta ICE-kinase (mRNA) TTCQ2E5 GN RIPK2 TTCQ2E5 FC Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and induces 'Lys-63'-linked polyubiquitination of IKBKG/NEMO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation. Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. TTCQ2E5 EC EC 2.7.11.1 TTCQ2E5 PD 6HMX; 6GGS; 6GFJ; 6FU5; 6ES0 TTCQ2E5 SQ MNGEAICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLHIHTPLLDSERKDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKTEYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHVKIADFGLSKWRMMSLSQSRSSKSAPEGGTIIYMPPENYEPGQKSRASIKHDIYSYAVITWEVLSRKQPFEDVTNPLQIMYSVSQGHRPVINEESLPYDIPHRARMISLIESGWAQNPDERPSFLKCLIELEPVLRTFEEITFLEAVIQLKKTKLQSVSSAIHLCDKKKMELSLNIPVNHGPQEESCGSSQLHENSGSPETSRSLPAPQDNDFLSRKAQDCYFMKLHHCPGNHSWDSTISGSQRAAFCDHKTTPCSSAIINPLSTAGNSERLQPGIAQQWIQSKREDIVNQMTEACLNQSLDALLSRDLIMKEDYELVSTKPTRTSKVRQLLDTTDIQGEEFAKVIVQKLKDNKQMGLQPYPEILVVSRSPSLNLLQNKSM TTCQ2E5 TT Clinical trial TTCQ2E5 FM mRNA target TTCQ2E5 KE hsa04621:NOD-like receptor signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa05131:Shigellosis; hsa05152:Tuberculosis TTCQ2E5 RC R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-209543:p75NTR recruits signalling complexes; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-446652:Interleukin-1 signaling; R-HSA-450302:activated TAK1 mediates p38 MAPK activation; R-HSA-450321:JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 TTJNTSI ID TTJNTSI TTJNTSI TN Rotamase Pin1 (PIN1) TTJNTSI UP Q13526 TTJNTSI UC PIN1_HUMAN TTJNTSI BC Cis-trans-isomerase TTJNTSI SN Prolyl isomerase Pin1; Peptidyl-prolyl cis-trans isomerase Pin1; Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl prolyl cis/trans isomerase Pin1; PPIase Pin1 TTJNTSI GN PIN1 TTJNTSI FC By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (, Ref. 21). Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN. May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR). Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. TTJNTSI EC EC 5.2.1.8 TTJNTSI PD 6DUN; 5VTK; 5VTJ; 5VTI; 5UY9 TTJNTSI SQ MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE TTJNTSI TT Clinical trial TTJNTSI FM Cis-trans-isomerases TTJNTSI KE hsa04622:RIG-I-like receptor signaling pathway TTJNTSI RC R-HSA-1169408:ISG15 antiviral mechanism; R-HSA-936440:Negative regulators of RIG-I/MDA5 signaling TT9ABMF ID TT9ABMF TT9ABMF TN Serine/threonine-protein kinase Chk2 (RAD53) TT9ABMF UP O96017 TT9ABMF UC CHK2_HUMAN TT9ABMF BC Kinase TT9ABMF SN hCds1; Hucds1; Checkpoint kinase 2; Cds1 homolog; Cds1; CHK2 checkpoint homolog; CHK2 TT9ABMF GN CHEK2 TT9ABMF FC May also negatively regulate cell cycle progression during unperturbed cell cycles. Following activation, phosphorylates numerous effectors preferentially at the consensus sequence [L-X-R-X-X-S/T]. Regulates cell cycle checkpoint arrest through phosphorylation of CDC25A, CDC25B and CDC25C, inhibiting their activity. Inhibition of CDC25 phosphatase activity leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. May also phosphorylate NEK6 which is involved in G2/M cell cycle arrest. Regulates DNA repair through phosphorylation of BRCA2, enhancing the association of RAD51 with chromatin which promotes DNA repair by homologous recombination. Also stimulates the transcription of genes involved in DNA repair (including BRCA2) through the phosphorylation and activation of the transcription factor FOXM1. Regulates apoptosis through the phosphorylation of p53/TP53, MDM4 and PML. Phosphorylation of p53/TP53 at 'Ser-20' by CHEK2 may alleviate inhibition by MDM2, leading to accumulation of active p53/TP53. Phosphorylation of MDM4 may also reduce degradation of p53/TP53. Also controls the transcription of pro-apoptotic genes through phosphorylation of the transcription factor E2F1. Tumor suppressor, it may also have a DNA damage-independent function in mitotic spindle assembly by phosphorylating BRCA1. Its absence may be a cause of the chromosomal instability observed in some cancer cells. Promotes the CCAR2-SIRT1 association and is required for CCAR2-mediated SIRT1 inhibition. Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest, activation of DNA repair and apoptosis in response to the presence of DNA double-strand breaks. TT9ABMF EC EC 2.7.11.1 TT9ABMF PD 4BDK; 4BDJ; 4BDI; 4BDH; 4BDG TT9ABMF SQ MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAETTKRPAVCAAVL TT9ABMF TT Clinical trial TT9ABMF FM Kinase TT9ABMF KE hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa05166:HTLV-I infection TT9ABMF RC R-HSA-5693565:Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks; R-HSA-69473:G2/M DNA damage checkpoint; R-HSA-69601:Ubiquitin Mediated Degradation of Phosphorylated Cdc25A TTTN5QW ID TTTN5QW TTTN5QW TN Serine/threonine-protein kinase pim-1 (PIM1) TTTN5QW UP P11309 TTTN5QW UC PIM1_HUMAN TTTN5QW BC Kinase TTTN5QW SN Pim-1 proto-oncogene, serine/threonine kinase; PIM TTTN5QW GN PIM1 TTTN5QW FC Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis. Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. TTTN5QW EC EC 2.7.11.1 TTTN5QW PD 6QXK; 6NO9; 6MT0; 6BSK; 6AYD TTTN5QW SQ MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK TTTN5QW TT Clinical trial TTTN5QW FM Kinase TTTN5QW KE hsa04630:Jak-STAT signaling pathway; hsa05206:MicroRNAs in cancer; hsa05221:Acute myeloid leukemia TT69J2Z ID TT69J2Z TT69J2Z TN Serine/threonine-protein kinase pim-2 (PIM2) TT69J2Z UP Q9P1W9 TT69J2Z UC PIM2_HUMAN TT69J2Z BC Kinase TT69J2Z SN Pim-2h; PIM2 TT69J2Z GN PIM2 TT69J2Z FC Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti- apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Isoform 1 is less active in this respect. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate. TT69J2Z EC EC 2.7.11.1 TT69J2Z PD 4X7Q; 2IWI TT69J2Z SQ MLTKPLQGPPAPPGTPTPPPGGKDREAFEAEYRLGPLLGKGGFGTVFAGHRLTDRLQVAIKVIPRNRVLGWSPLSDSVTCPLEVALLWKVGAGGGHPGVIRLLDWFETQEGFMLVLERPLPAQDLFDYITEKGPLGEGPSRCFFGQVVAAIQHCHSRGVVHRDIKDENILIDLRRGCAKLIDFGSGALLHDEPYTDFDGTRVYSPPEWISRHQYHALPATVWSLGILLYDMVCGDIPFERDQEILEAELHFPAHVSPDCCALIRRCLAPKPSSRPSLEEILLDPWMQTPAEDVPLNPSKGGPAPLAWSLLP TT69J2Z TT Clinical trial TT69J2Z KE hsa05221:Acute myeloid leukemia TTTV8EJ ID TTTV8EJ TTTV8EJ TN Serine/threonine-protein kinase Sgk1 (SGK1) TTTV8EJ UP O00141 TTTV8EJ UC SGK1_HUMAN TTTV8EJ BC Kinase TTTV8EJ SN Serum/glucocorticoid-regulated kinase 1; SGK1 TTTV8EJ GN SGK1 TTTV8EJ FC Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Isoform 2 exhibited a greater effect on cell plasma membrane expression of SCNN1A/ENAC and Na(+) transport than isoform 1. Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. TTTV8EJ EC EC 2.7.11.1 TTTV8EJ PD 3HDN; 3HDM; 2R5T TTTV8EJ SQ MTVKTEAAKGTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKISQPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEVFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNSTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFMEIKSHVFFSLINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTEEPVPNSIGKSPDSVLVTASVKEAAEAFLGFSYAPPTDSFL TTTV8EJ TT Clinical trial TTTV8EJ FM Kinase TTTV8EJ KE hsa04068:FoxO signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04960:Aldosterone-regulated sodium reabsorption TTTV8EJ RC R-HSA-2672351:Stimuli-sensing channels TTTP2Z1 ID TTTP2Z1 TTTP2Z1 TN SH2 domain inositol 5'-phosphatase 1 (INPP5D) TTTP2Z1 UP Q92835 TTTP2Z1 UC SHIP1_HUMAN TTTP2Z1 BC Phosphoric monoester hydrolase TTTP2Z1 SN p150Ship; hp51CN; SIP145; SIP-145; SHIP1; SHIP-1; SHIP; SH2 domaincontaining inositol phosphatase 1; SH2 domaincontaining inositol 5'phosphatase 1; SH2 domain-containing inositol phosphatase 1; SH2 domain-containing inositol 5'-phosphatase 1; Phosphatidylinositol 3,4,5trisphosphate 5phosphatase 1; Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1; Inositol polyphosphate5phosphatase of 145 kDa; Inositol polyphosphate-5-phosphatase of 145 kDa TTTP2Z1 GN INPP5D TTTP2Z1 FC Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. TTTP2Z1 EC EC 3.1.3.86 TTTP2Z1 PD 6IBD; 2YSX TTTP2Z1 SQ MVPCWNHGNITRSKAEELLSRTGKDGSFLVRASESISRAYALCVLYRNCVYTYRILPNEDDKFTVQASEGVSMRFFTKLDQLIEFYKKENMGLVTHLQYPVPLEEEDTGDDPEEDTVESVVSPPELPPRNIPLTASSCEAKEVPFSNENPRATETSRPSLSETLFQRLQSMDTSGLPEEHLKAIQDYLSTQLAQDSEFVKTGSSSLPHLKKLTTLLCKELYGEVIRTLPSLESLQRLFDQQLSPGLRPRPQVPGEANPINMVSKLSQLTSLLSSIEDKVKALLHEGPESPHRPSLIPPVTFEVKAESLGIPQKMQLKVDVESGKLIIKKSKDGSEDKFYSHKKILQLIKSQKFLNKLVILVETEKEKILRKEYVFADSKKREGFCQLLQQMKNKHSEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAETIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHHGELTGHFQGEIKLQTSQGKTREKLYDFVKTERDESSGPKTLKSLTSHDPMKQWEVTSRAPPCSGSSITEIINPNYMGVGPFGPPMPLHVKQTLSPDQQPTAWSYDQPPKDSPLGPCRGESPPTPPGQPPISPKKFLPSTANRGLPPRTQESRPSDLGKNAGDTLPQEDLPLTKPEMFENPLYGSLSSFPKPAPRKDQESPKMPRKEPPPCPEPGILSPSIVLTKAQEADRGEGPGKQVPAPRLRSFTCSSSAEGRAAGGDKSQGKPKTPVSSQAPVPAKRPIKPSRSEINQQTPPTPTPRPPLPVKSPAVLHLQHSKGRDYRDNTELPHHGKHRPEEGPPGPLGRTAMQ TTTP2Z1 TT Clinical trial TTTP2Z1 FM Phosphoric monoester hydrolases TTTP2Z1 KE hsa00562:Inositol phosphate metabolism; hsa04070:Phosphatidylinositol signaling system; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis TTTP2Z1 RC R-HSA-210990:PECAM1 interactions; R-HSA-912526:Interleukin receptor SHC signaling TTP9K3Q ID TTP9K3Q TTP9K3Q TN SOD1 messenger RNA (SOD1 mRNA) TTP9K3Q UP P00441 TTP9K3Q UC SODC_HUMAN TTP9K3Q BC mRNA target TTP9K3Q SN hSod1 (mRNA); Superoxide dismutase [Cu-Zn] (mRNA); Superoxide dismutase 1 (mRNA); Superoxide dismutase (mRNA) TTP9K3Q GN SOD1 TTP9K3Q FC Destroys radicals which are normally produced within the cells and which are toxic to biological systems. TTP9K3Q EC EC 1.15.1.1 TTP9K3Q PD 6FP6; 6FON; 6FOL; 6FOI; 6FLH TTP9K3Q SQ MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ TTP9K3Q TT Clinical trial TTP9K3Q FM mRNA target TTP9K3Q KE hsa04146:Peroxisome; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05016:Huntington's disease; hsa05020:Prion diseases TTP9K3Q RC R-HSA-114608:Platelet degranulation; R-HSA-3299685:Detoxification of Reactive Oxygen Species TTGSEFH ID TTGSEFH TTGSEFH TN Sodium/hydrogen exchanger 1 (SLC9A1) TTGSEFH UP P19634 TTGSEFH UC SL9A1_HUMAN TTGSEFH BC Monovalent cation:proton antiporter-1 TTGSEFH SN Solute carrier family 9 member 1; Na+/H+ antiporter, amiloride-sensitive; Na(+)Sodium/hydrogen exchanger 1/H(+) exchanger 1; Na(+)/H(+) exchanger 1; Na(+)/H(+) antiporter, amiloride-sensitive; NHE1; NHE-1; Myocardial Na+/H+ exchanger; APNH1; APNH TTGSEFH GN SLC9A1 TTGSEFH FC Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. TTGSEFH PD 6BJF; 2YGG; 2MDF; 2L0E; 2KBV TTGSEFH SQ MVLRSGICGLSPHRIFPSLLVVVALVGLLPVLRSHGLQLSPTASTIRSSEPPRERSIGDVTTAPPEVTPESRPVNHSVTDHGMKPRKAFPVLGIDYTHVRTPFEISLWILLACLMKIGFHVIPTISSIVPESCLLIVVGLLVGGLIKGVGETPPFLQSDVFFLFLLPPIILDAGYFLPLRQFTENLGTILIFAVVGTLWNAFFLGGLMYAVCLVGGEQINNIGLLDNLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLNDAVTVVLYHLFEEFANYEHVGIVDIFLGFLSFFVVALGGVLVGVVYGVIAAFTSRFTSHIRVIEPLFVFLYSYMAYLSAELFHLSGIMALIASGVVMRPYVEANISHKSHTTIKYFLKMWSSVSETLIFIFLGVSTVAGSHHWNWTFVISTLLFCLIARVLGVLGLTWFINKFRIVKLTPKDQFIIAYGGLRGAIAFSLGYLLDKKHFPMCDLFLTAIITVIFFTVFVQGMTIRPLVDLLAVKKKQETKRSINEEIHTQFLDHLLTGIEDICGHYGHHHWKDKLNRFNKKYVKKCLIAGERSKEPQLIAFYHKMEMKQAIELVESGGMGKIPSAVSTVSMQNIHPKSLPSERILPALSKDKEEEIRKILRNNLQKTRQRLRSYNRHTLVADPYEEAWNQMLLRRQKARQLEQKINNYLTVPAHKLDSPTMSRARIGSDPLAYEPKEDLPVITIDPASPQSPESVDLVNEELKGKVLGLSRDPAKVAEEDEDDDGGIMMRSKETSSPGTDDVFTPAPSDSPSSQRIQRCLSDPGPHPEPGEGEPFFPKGQ TTGSEFH TT Clinical trial TTGSEFH FM Monovalent cation:proton antiporter TTGSEFH KE hsa04024:cAMP signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04810:Regulation of actin cytoskeleton; hsa04919:Thyroid hormone signaling pathway; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04976:Bile secretion; hsa05205:Proteoglycans in cancer TTGSEFH RC R-HSA-2160916:Hyaluronan uptake and degradation TT7WVHI ID TT7WVHI TT7WVHI TN Soluble epoxide hydrolase (EPHX2) TT7WVHI UP P34913 TT7WVHI UC HYES_HUMAN TT7WVHI BC Ether bond hydrolase TT7WVHI SN Bifunctional epoxide hydrolase 2 TT7WVHI GN EPHX2 TT7WVHI FC Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid and 12-phosphonooxy-octadec-9E-enoic acid. TT7WVHI PD 6AUM; 5MWA; 5FP0; 5AM5; 5AM4 TT7WVHI SQ MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM TT7WVHI TT Clinical trial TT7WVHI FM Ether hydrolase TT7WVHI KE hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04146:Peroxisome TTOHFIY ID TTOHFIY TTOHFIY TN Sphingosine kinase 1 (SPHK1) TTOHFIY UP Q9NYA1 TTOHFIY UC SPHK1_HUMAN TTOHFIY BC Kinase TTOHFIY SN SPK 1; SPK; SPHK1; SK 1; Acetyltransferase SPHK1 TTOHFIY GN SPHK1 TTOHFIY FC Acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol. In contrast to proapoptotic SPHK2, has a negative effect on intracellular ceramide levels, enhances cell growth and inhibits apoptosis. Involved in the regulation of inflammatory response and neuroinflammation. Via the product sphingosine 1-phosphate, stimulates TRAF2 E3 ubiquitin ligase activity, and promotes activation of NF-kappa-B in response to TNF signaling leading to IL17 secretion. In response to TNF and in parallel to NF-kappa-B activation, negatively regulates RANTES inducion through p38 MAPK signaling pathway. Involved in endocytic membrane trafficking induced by sphingosine, recruited to dilate endosomes, also plays a role on later stages of endosomal maturation and membrane fusion independently of its kinase activity. In Purkinje cells, seems to be also involved in the regulation of autophagosome-lysosome fusion upon VEGFA. Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. TTOHFIY EC EC 2.7.1.91 TTOHFIY PD 4V24; 4L02; 3VZD; 3VZC; 3VZB TTOHFIY SQ MDPAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAEISFTLMLTERRNHARELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPAGSGNALAASLNHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSVLSLAWGFIADVDLESEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASPVVVQQGPVDAHLVPLEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMHLFYVRAGVSRAMLLRLFLAMEKGRHMEYECPYLVYVPVVAFRLEPKDGKGVFAVDGELMVSEAVQGQVHPNYFWMVSGCVEPPPSWKPQQMPPPEEPL TTOHFIY TT Clinical trial TTOHFIY FM Kinase TTOHFIY KE hsa00600:Sphingolipid metabolism; hsa01100:Metabolic pathways; hsa04020:Calcium signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04370:VEGF signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa05152:Tuberculosis TTOHFIY RC R-HSA-1660661:Sphingolipid de novo biosynthesis; R-HSA-5218921:VEGFR2 mediated cell proliferation TT618Q2 ID TT618Q2 TT618Q2 TN Sphingosine-1-phosphate lyase 1 (SGPL1) TT618Q2 UP O95470 TT618Q2 UC SGPL1_HUMAN TT618Q2 BC Carbon-carbon lyase TT618Q2 SN hSPL; Sphingosine-1-phosphate aldolase; SPL 1; SP-lyase 1; S1PL; KIAA1252 TT618Q2 GN SGPL1 TT618Q2 FC Elevates stress-induced ceramide production and apoptosis. Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro-inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP. Seems to play a role in establishing neuronal contact sites and axonal maintenance. Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. TT618Q2 EC EC 4.1.2.27 TT618Q2 PD 4Q6R TT618Q2 SQ MPSTDLLMLKAFEPYLEILEVYSTKAKNYVNGHCTKYEPWQLIAWSVVWTLLIVWGYEFVFQPESLWSRFKKKCFKLTRKMPIIGRKIQDKLNKTKDDISKNMSFLKVDKEYVKALPSQGLSSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTELLVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEKGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLEHPFDFRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVDTDWQGGIYASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIALGSRDFDIYRLSNLMTAKGWNLNQLQFPPSIHFCITLLHARKRVAIQFLKDIRESVTQIMKNPKAKTTGMGAIYGMAQTTVDRNMVAELSSVFLDSLYSTDTVTQGSQMNGSPKPH TT618Q2 TT Clinical trial TT618Q2 FM Carbon-carbon lyase TT618Q2 KE hsa00600:Sphingolipid metabolism; hsa01100:Metabolic pathways; hsa04071:Sphingolipid signaling pathway TT618Q2 RC R-HSA-1660661:Sphingolipid de novo biosynthesis TT6RVLG ID TT6RVLG TT6RVLG TN Superoxide dismutase Cu-Zn (SOD Cu-Zn) TT6RVLG UP P00441 TT6RVLG UC SODC_HUMAN TT6RVLG BC Superoxide dismutase/reductase TT6RVLG SN hSod1; Superoxide dismutase [Cu-Zn]; Superoxide dismutase 1; Superoxide dismutase TT6RVLG GN SOD1 TT6RVLG FC Destroys radicals which are normally produced within the cells and which are toxic to biological systems. TT6RVLG EC EC 1.15.1.1 TT6RVLG PD 6FP6; 6FON; 6FOL; 6FOI; 6FLH TT6RVLG SQ MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ TT6RVLG TT Clinical trial TT6RVLG FM Superoxide acceptor oxidoreductase TT6RVLG KE hsa04146:Peroxisome; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05016:Huntington's disease; hsa05020:Prion diseases TT6RVLG RC R-HSA-114608:Platelet degranulation; R-HSA-3299685:Detoxification of Reactive Oxygen Species TT2HUPM ID TT2HUPM TT2HUPM TN SYK messenger RNA (SYK mRNA) TT2HUPM UP P43405 TT2HUPM UC KSYK_HUMAN TT2HUPM BC mRNA target TT2HUPM SN p72-Syk (mRNA); Spleen tyrosine kinase (mRNA) TT2HUPM GN SYK TT2HUPM FC Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development. Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. It also phosphorylates and activates PLCG1 and the PKC signaling pathway. It also phosphorylates BTK and regulates its activity in B-cell antigen receptor (BCR)-coupled signaling. In addition to its function downstream of BCR plays also a role in T-cell receptor signaling. Plays also a crucial role in the innate immune response to fungal, bacterial and viral pathogens. It is for instance activated by the membrane lectin CLEC7A. Upon stimulation by fungal proteins, CLEC7A together with SYK activates immune cells inducing the production of ROS. Also activates the inflammasome and NF-kappa-B-mediated transcription of chemokines and cytokines in presence of pathogens. Regulates neutrophil degranulation and phagocytosis through activation of the MAPK signaling cascade. Required for the stimulation of neutrophil phagocytosis by IL15. Also mediates the activation of dendritic cells by cell necrosis stimuli. Also involved in mast cells activation. Involved in interleukin-3/IL3-mediated signaling pathway in basophils. Also functions downstream of receptors mediating cell adhesion. Relays for instance, integrin-mediated neutrophils and macrophages activation and P-selectin receptor/SELPG-mediated recruitment of leukocytes to inflammatory loci. Plays also a role in non-immune processes. It is for instance involved in vascular development where it may regulate blood and lymphatic vascular separation. It is also required for osteoclast development and function. Functions in the activation of platelets by collagen, mediating PLCG2 phosphorylation and activation. May be coupled to the collagen receptor by the ITAM domain-containing FCER1G. Also activated by the membrane lectin CLEC1B that is required for activation of platelets by PDPN/podoplanin. Involved in platelet adhesion being activated by ITGB3 engaged by fibrinogen. Together with CEACAM20, enhances production of the cytokine CXCL8/IL-8 via the NFKB pathway and may thus have a role in the intestinal immune response. Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). TT2HUPM EC EC 2.7.10.2 TT2HUPM PD 6HM7; 6HM6; 5Y5U; 5Y5T; 5TT7 TT2HUPM SQ MASSGMADSANHLPFFFGNITREEAEDYLVQGGMSDGLYLLRQSRNYLGGFALSVAHGRKAHHYTIERELNGTYAIAGGRTHASPADLCHYHSQESDGLVCLLKKPFNRPQGVQPKTGPFEDLKENLIREYVKQTWNLQGQALEQAIISQKPQLEKLIATTAHEKMPWFHGKISREESEQIVLIGSKTNGKFLIRARDNNGSYALCLLHEGKVLHYRIDKDKTGKLSIPEGKKFDTLWQLVEHYSYKADGLLRVLTVPCQKIGTQGNVNFGGRPQLPGSHPATWSAGGIISRIKSYSFPKPGHRKSSPAQGNRQESTVSFNPYEPELAPWAADKGPQREALPMDTEVYESPYADPEEIRPKEVYLDRKLLTLEDKELGSGNFGTVKKGYYQMKKVVKTVAVKILKNEANDPALKDELLAEANVMQQLDNPYIVRMIGICEAESWMLVMEMAELGPLNKYLQQNRHVKDKNIIELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGKWPVKWYAPECINYYKFSSKSDVWSFGVLMWEAFSYGQKPYRGMKGSEVTAMLEKGERMGCPAGCPREMYDLMNLCWTYDVENRPGFAAVELRLRNYYYDVVN TT2HUPM TT Clinical trial TT2HUPM FM mRNA target TT2HUPM KE hsa04064:NF-kappa B signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04380:Osteoclast differentiation; hsa04611:Platelet activation; hsa04650:Natural killer cell mediated cytotoxicity; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa05152:Tuberculosis; hsa05169:Epstein-Barr virus infection; hsa05203:Viral carcinogenesis TT2HUPM RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-2029481:FCGR activation; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-2424491:DAP12 signaling; R-HSA-2454202:Fc epsilon receptor (FCERI) signaling; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-2871809:FCERI mediated Ca+2 mobilization; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-451927:Interleukin-2 signaling; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-5621480:Dectin-2 family; R-HSA-912631:Regulation of signaling by CBL; R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTKNWZ4 ID TTKNWZ4 TTKNWZ4 TN Thromboxane-A synthase (TBXAS1) TTKNWZ4 UP P24557 TTKNWZ4 UC THAS_HUMAN TTKNWZ4 BC Intramolecular oxidoreductase TTKNWZ4 SN Thromboxane A2 synthase; TXS; TXA synthase; Cytochrome P450 5A1; CYP5A1; CYP5 TTKNWZ4 GN TBXAS1 TTKNWZ4 FC endoplasmic reticulum membrane, 12-hydroxyheptadecatrienoic acid synthase activity, thromboxane-A synthase activity, cyclooxygenase pathway, icosanoid metabolic process. TTKNWZ4 EC EC 5.3.99.5 TTKNWZ4 SQ MEALGFLKLEVNGPMVTVALSVALLALLKWYSTSAFSRLEKLGLRHPKPSPFIGNLTFFRQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFPSIMVPLARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDIVRDVFSSTGCKPNPSRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVYIKIVSR TTKNWZ4 TT Clinical trial TTKNWZ4 FM Intramolecular oxidoreductase TTKNWZ4 KE hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04611:Platelet activation TTD24Y0 ID TTD24Y0 TTD24Y0 TN Toll-like receptor 3 (TLR3) TTD24Y0 UP O15455 TTD24Y0 UC TLR3_HUMAN TTD24Y0 BC Toll-like receptor TTD24Y0 SN CD283 TTD24Y0 GN TLR3 TTD24Y0 FC Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response. TTD24Y0 PD 5GS0; 3ULV; 3ULU; 2MKA; 2MK9 TTD24Y0 SQ MRQTLPCIYFWGGLLPFGMLCASSTTKCTVSHEVADCSHLKLTQVPDDLPTNITVLNLTHNQLRRLPAANFTRYSQLTSLDVGFNTISKLEPELCQKLPMLKVLNLQHNELSQLSDKTFAFCTNLTELHLMSNSIQKIKNNPFVKQKNLITLDLSHNGLSSTKLGTQVQLENLQELLLSNNKIQALKSEELDIFANSSLKKLELSSNQIKEFSPGCFHAIGRLFGLFLNNVQLGPSLTEKLCLELANTSIRNLSLSNSQLSTTSNTTFLGLKWTNLTMLDLSYNNLNVVGNDSFAWLPQLEYFFLEYNNIQHLFSHSLHGLFNVRYLNLKRSFTKQSISLASLPKIDDFSFQWLKCLEHLNMEDNDIPGIKSNMFTGLINLKYLSLSNSFTSLRTLTNETFVSLAHSPLHILNLTKNKISKIESDAFSWLGHLEVLDLGLNEIGQELTGQEWRGLENIFEIYLSYNKYLQLTRNSFALVPSLQRLMLRRVALKNVDSSPSPFQPLRNLTILDLSNNNIANINDDMLEGLEKLEILDLQHNNLARLWKHANPGGPIYFLKGLSHLHILNLESNGFDEIPVEVFKDLFELKIIDLGLNNLNTLPASVFNNQVSLKSLNLQKNLITSVEKKVFGPAFRNLTELDMRFNPFDCTCESIAWFVNWINETHTNIPELSSHYLCNTPPHYHGFPVRLFDTSSCKDSAPFELFFMINTSILLIFIFIVLLIHFEGWRISFYWNVSVHRVLGFKEIDRQTEQFEYAAYIIHAYKDKDWVWEHFSSMEKEDQSLKFCLEERDFEAGVFELEAIVNSIKRSRKIIFVITHHLLKDPLCKRFKVHHAVQQAIEQNLDSIILVFLEEIPDYKLNHALCLRRGMFKSHCILNWPVQKERIGAFRHKLQVALGSKNSVH TTD24Y0 TT Clinical trial TTD24Y0 FM Toll-like receptor family TTD24Y0 KE hsa04620:Toll-like receptor signaling pathway; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05168:Herpes simplex infection TTD24Y0 RC R-HSA-140534:Ligand-dependent caspase activation; R-HSA-166166:MyD88-independent TLR3/TLR4 cascade; R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-1810476:RIP-mediated NFkB activation via ZBP1; R-HSA-2562578:TRIF-mediated programmed cell death; R-HSA-936964:Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon; R-HSA-937041:IKK complex recruitment mediated by RIP1; R-HSA-937072:TRAF6 mediated induction of TAK1 complex TTISGCA ID TTISGCA TTISGCA TN Toll-like receptor 4 (TLR4) TTISGCA UP O00206 TTISGCA UC TLR4_HUMAN TTISGCA BC Toll-like receptor TTISGCA SN TLR-4; HToll; CD284 TTISGCA GN TLR4 TTISGCA FC Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni(2+). Responses triggered by Ni(2+) require non-conserved histidines and are, therefore, species-specific. Both M. tuberculosis HSP70 (dnaK) and HSP65 (groEL-2) act via this protein to stimulate NF-kappa-B expression. In complex with TLR6, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-). Stimulation of monocytes in vitro with M. tuberculosis PstS1 induces p38 MAPK and ERK1/2 activation primarily via TLR2, but also partially via this receptor. Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). TTISGCA PD 5NAO; 5NAM; 4G8A; 3ULA; 3UL9 TTISGCA SQ MMSASRLAGTLIPAMAFLSCVRPESWEPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNEGNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFPTLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEHLDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQCQLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNKTIIGVSVLSVLVVSVVAVLVYKFYFHLMLLAGCIKYGRGENIYDAFVIYSSQDEDWVRNELVKNLEEGVPPFQLCLHYRDFIPGVAIAANIIHEGFHKSRKVIVVVSQHFIQSRWCIFEYEIAQTWQFLSSRAGIIFIVLQKVEKTLLRQQVELYRLLSRNTYLEWEDSVLGRHIFWRRLRKALLDGKSWNPEGTVGTGCNWQEATSI TTISGCA TT Clinical trial TTISGCA FM Toll like receptor TTISGCA KE hsa04064:NF-kappa B signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa05130:Pathogenic Escherichia coli infection; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05205:Proteoglycans in cancer; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis TTISGCA RC R-HSA-140534:Ligand-dependent caspase activation; R-HSA-166016:Toll Like Receptor 4 (TLR4) Cascade; R-HSA-166058:MyD88:Mal cascade initiated on plasma membrane; R-HSA-166166:MyD88-independent TLR3/TLR4 cascade; R-HSA-2562578:TRIF-mediated programmed cell death; R-HSA-5602498:MyD88 deficiency (TLR2/4); R-HSA-5603041:IRAK4 deficiency (TLR2/4); R-HSA-936964:Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon; R-HSA-937041:IKK complex recruitment mediated by RIP1; R-HSA-937072:TRAF6 mediated induction of TAK1 complex TT5WLRX ID TT5WLRX TT5WLRX TN TRAIL receptor 1 (TRAIL-R1) TT5WLRX UP O00220 TT5WLRX UC TR10A_HUMAN TT5WLRX BC Cytokine receptor TT5WLRX SN Tumor necrosis factor receptor superfamily member 10A; TRAILR1; TNF-related apoptosis-inducing ligand receptor 1; Death receptor 4; DR4; CD261; APO2 TT5WLRX GN TNFRSF10A TT5WLRX FC The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Receptor for the cytotoxic ligand TNFSF10/TRAIL. TT5WLRX PD 5CIR TT5WLRX SQ MAPPPARVHLGAFLAVTPNPGSAASGTEAAAATPSKVWGSSAGRIEPRGGGRGALPTSMGQHGPSARARAGRAPGPRPAREASPRLRVHKTFKFVVVGVLLQVVPSSAATIKLHDQSIGTQQWEHSPLGELCPPGSHRSEHPGACNRCTEGVGYTNASNNLFACLPCTACKSDEEERSPCTTTRNTACQCKPGTFRNDNSAEMCRKCSRGCPRGMVKVKDCTPWSDIECVHKESGNGHNIWVILVVTLVVPLLLVAVLIVCCCIGSGCGGDPKCMDRVCFWRLGLLRGPGAEDNAHNEILSNADSLSTFVSEQQMESQEPADLTGVTVQSPGEAQCLLGPAEAEGSQRRRLLVPANGADPTETLMLFFDKFANIVPFDSWDQLMRQLDLTKNEIDVVRAGTAGPGDALYAMLMKWVNKTGRNASIHTLLDALERMEERHAREKIQDLLVDSGKFIYLEDGTGSAVSLE TT5WLRX TT Clinical trial TT5WLRX FM Cytokine receptor TT5WLRX KE hsa04060:Cytokine-cytokine receptor interaction; hsa04210:Apoptosis; hsa04650:Natural killer cell mediated cytotoxicity; hsa05162:Measles; hsa05164:Influenza A TT5WLRX RC R-HSA-140534:Ligand-dependent caspase activation; R-HSA-3371378:Regulation by c-FLIP; R-HSA-5213460:RIPK1-mediated regulated necrosis; R-HSA-5218900:CASP8 activity is inhibited; R-HSA-69416:Dimerization of procaspase-8; R-HSA-75158:TRAIL signaling TTW20TU ID TTW20TU TTW20TU TN TRAIL receptor 2 (TRAIL-R2) TTW20TU UP O14763 TTW20TU UC TR10B_HUMAN TTW20TU BC Cytokine receptor TTW20TU SN ZTNFR9; UNQ160/PRO186; Tumor necrosis factor receptor superfamily member 10B; TRICK2; TRAILR2; TNF-related apoptosis-inducing ligand receptor 2; KILLER; Death receptor 5; DR5; CD262 TTW20TU GN TNFRSF10B TTW20TU FC The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis. Receptor for the cytotoxic ligand TNFSF10/TRAIL. TTW20TU PD 6NHY; 6NHW; 4OD2; 4N90; 4I9X TTW20TU SQ MEQRGQNAPAASGARKRHGPGPREARGARPGPRVPKTLVLVVAAVLLLVSAESALITQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCDSGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVHKESGTKHSGEVPAVEETVTSSPGTPASPCSLSGIIIGVTVAAVVLIVAVFVCKSLLWKKVLPYLKGICSGGGGDPERVDRSSQRPGAEDNVLNEIVSILQPTQVPEQEMEVQEPAEPTGVNMLSPGESEHLLEPAEAERSQRRRLLVPANEGDPTETLRQCFDDFADLVPFDSWEPLMRKLGLMDNEIKVAKAEAAGHRDTLYTMLIKWVNKTGRDASVHTLLDALETLGERLAKQKIEDHLLSSGKFMYLEGNADSAMS TTW20TU TT Clinical trial TTW20TU FM Cytokine receptor TTW20TU KE hsa04060:Cytokine-cytokine receptor interaction; hsa04115:p53 signaling pathway; hsa04210:Apoptosis; hsa04650:Natural killer cell mediated cytotoxicity; hsa05162:Measles; hsa05164:Influenza A TTW20TU RC R-HSA-140534:Ligand-dependent caspase activation; R-HSA-3371378:Regulation by c-FLIP; R-HSA-5213460:RIPK1-mediated regulated necrosis; R-HSA-5218900:CASP8 activity is inhibited; R-HSA-69416:Dimerization of procaspase-8; R-HSA-75158:TRAIL signaling TTY9TWO ID TTY9TWO TTY9TWO TN Transforming growth factor beta 2 (TGFB2) TTY9TWO UP P61812 TTY9TWO UC TGFB2_HUMAN TTY9TWO BC Growth factor TTY9TWO SN Transforming growth factor beta-2 proprotein; TGF-beta 2; Polyergin; Glioblastoma-derived T-cell suppressor factor; G-TSF; Cetermin; BSC-1 cell growth inhibitor TTY9TWO GN TGFB2 TTY9TWO FC Transforming growth factor beta-2 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively. TTY9TWO PD 5TY4; 5TX4; 4KXZ; 2TGI; 1TFG TTY9TWO SQ MHYCVLSAFLILHLVTVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPEEVPPEVISIYNSTRDLLQEKASRRAAACERERSDEEYYAKEVYKIDMPPFFPSENAIPPTFYRPYFRIVRFDVSAMEKNASNLVKAEFRVFRLQNPKARVPEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVHEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYTSGDQKTIKSTRKKNSGKTPHLLLMLLPSYRLESQQTNRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS TTY9TWO TT Clinical trial TTY9TWO FM Growth factor TTY9TWO KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04144:Endocytosis; hsa04350:TGF-beta signaling pathway; hsa04380:Osteoclast differentiation; hsa04390:Hippo signaling pathway; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05220:Chronic myeloid leukemia; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05414:Dilated cardiomyopathy TTY9TWO RC R-HSA-114608:Platelet degranulation; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-3000178:ECM proteoglycans TT1RWNJ ID TT1RWNJ TT1RWNJ TN Tyrosine-protein kinase Lyn (JTK8) TT1RWNJ UP P07948 TT1RWNJ UC LYN_HUMAN TT1RWNJ BC Kinase TT1RWNJ SN p56Lyn; p53Lyn; V-yes-1 Yamaguchi sarcoma viral related oncogene homolog; Lck/Yes-related novel protein tyrosine kinase TT1RWNJ GN LYN TT1RWNJ FC Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Mediates phosphorylation of the BCR-ABL fusion protein. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. TT1RWNJ EC EC 2.7.10.2 TT1RWNJ PD 6NMW; 5XY1; 3A4O; 1WA7; 1W1F TT1RWNJ SQ MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP TT1RWNJ TT Clinical trial TT1RWNJ FM Kinase TT1RWNJ KE hsa04062:Chemokine signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04611:Platelet activation; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04730:Long-term depression; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05169:Epstein-Barr virus infection; hsa05203:Viral carcinogenesis TT1RWNJ RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1433559:Regulation of KIT signaling; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-2029481:FCGR activation; R-HSA-210990:PECAM1 interactions; R-HSA-2454202:Fc epsilon receptor (FCERI) signaling; R-HSA-2682334:EPH-Ephrin signaling; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-2871809:FCERI mediated Ca+2 mobilization; R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-389356:CD28 co-stimulation; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-3928665:EPH-ephrin mediated repulsion of cells; R-HSA-5621480:Dectin-2 family; R-HSA-5621575:CD209 (DC-SIGN) signaling; R-HSA-75892:Platelet Adhesion to exposed collagen; R-HSA-912631:Regulation of signaling by CBL; R-HSA-982772:Growth hormone receptor signaling; R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTO7LKR ID TTO7LKR TTO7LKR TN Tyrosine-protein kinase Mer (MERTK) TTO7LKR UP Q12866 TTO7LKR UC MERTK_HUMAN TTO7LKR BC Kinase TTO7LKR SN Receptor tyrosine kinase MerTK; Proto-oncogene c-Mer TTO7LKR GN MERTK TTO7LKR FC Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. TTO7LKR EC EC 2.7.10.1 TTO7LKR PD 5U6C; 5TD2; 5TC0; 5K0X; 5K0K TTO7LKR SQ MGPAPLPLLLGLFLPALWRRAITEAREEAKPYPLFPGPFPGSLQTDHTPLLSLPHASGYQPALMFSPTQPGRPHTGNVAIPQVTSVESKPLPPLAFKHTVGHIILSEHKGVKFNCSISVPNIYQDTTISWWKDGKELLGAHHAITQFYPDDEVTAIIASFSITSVQRSDNGSYICKMKINNEEIVSDPIYIEVQGLPHFTKQPESMNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNEQPEKSPSVLTVPGLTEMAVFSCEAHNDKGLTVSKGVQINIKAIPSPPTEVSIRNSTAHSILISWVPGFDGYSPFRNCSIQVKEADPLSNGSVMIFNTSALPHLYQIKQLQALANYSIGVSCMNEIGWSAVSPWILASTTEGAPSVAPLNVTVFLNESSDNVDIRWMKPPTKQQDGELVGYRISHVWQSAGISKELLEEVGQNGSRARISVQVHNATCTVRIAAVTRGGVGPFSDPVKIFIPAHGWVDYAPSSTPAPGNADPVLIIFGCFCGFILIGLILYISLAIRKRVQETKFGNAFTEEDSELVVNYIAKKSFCRRAIELTLHSLGVSEELQNKLEDVVIDRNLLILGKILGEGEFGSVMEGNLKQEDGTSLKVAVKTMKLDNSSQREIEEFLSEAACMKDFSHPNVIRLLGVCIEMSSQGIPKPMVILPFMKYGDLHTYLLYSRLETGPKHIPLQTLLKFMVDIALGMEYLSNRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYEIMYSCWRTDPLDRPTFSVLRLQLEKLLESLPDVRNQADVIYVNTQLLESSEGLAQGSTLAPLDLNIDPDSIIASCTPRAAISVVTAEVHDSKPHEGRYILNGGSEEWEDLTSAPSAAVTAEKNSVLPGERLVRNGVSWSHSSMLPLGSSLPDELLFADDSSEGSEVLM TTO7LKR TT Clinical trial TTO7LKR FM Kinase TTO7LKR RC R-HSA-202733:Cell surface interactions at the vascular wall TTHNLSB ID TTHNLSB TTHNLSB TN Valosin-containing protein p97 (VCP) TTHNLSB UP P55072 TTHNLSB UC TERA_HUMAN TTHNLSB BC Acid anhydride hydrolase TTHNLSB SN Valosin-containing protein; Transitional endoplasmic reticulum ATPase; TER ATPase; 15S Mg(2+)-ATPase p97 subunit TTHNLSB GN VCP TTHNLSB FC Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. Plays a role in the regulation of stress granules (SGs) clearance process upon arsenite-induced response. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage. Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation. Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy. Acts as a negative regulator of type I interferon production by interacting with DDX58/RIG-I: interaction takes place when DDX58/RIG-I is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of DDX58/RIG-I. May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation. May more particularly play a role in caveolins sorting in cells. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. TTHNLSB EC EC 3.6.4.6 TTHNLSB PD 6MCK; 6G30; 6G2Z; 6G2Y; 6G2X TTHNLSB SQ MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGSVYTEDNDDDLYG TTHNLSB TT Clinical trial TTHNLSB FM Acid anhydrides hydrolase TTHNLSB KE hsa04141:Protein processing in endoplasmic reticulum; hsa05134:Legionellosis TTHNLSB RC R-HSA-5358346:Hedgehog ligand biogenesis; R-HSA-5362768:Hh mutants that don't undergo autocatalytic processing are degraded by ERAD TTCL30I ID TTCL30I TTCL30I TN Vasoactive intestinal polypeptide receptor 1 (VIPR1) TTCL30I UP P32241 TTCL30I UC VIPR1_HUMAN TTCL30I BC GPCR secretin TTCL30I SN Vasoactive intestinal peptide/pituitary adenylate cyclase activating polypeptide receptor-1; Vasoactive intestinal peptide receptor 1; VPAC1; VPAC-1; VIPR1; VIP-R-1; Pituitary adenylate cyclase activating polypeptide type II receptor; PACAP-R-2; PACAP type II receptor TTCL30I GN VIPR1 TTCL30I FC This is a receptor for vip. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The affinity is vip = pacap-27 > pacap-38. TTCL30I PD 5IB5; 5IB4; 5IB3; 5IB2; 5IB1 TTCL30I SQ MRPPSPLPARWLCVLAGALAWALGPAGGQAARLQEECDYVQMIEVQHKQCLEEAQLENETIGCSKMWDNLTCWPATPRGQVVVLACPLIFKLFSSIQGRNVSRSCTDEGWTHLEPGPYPIACGLDDKAASLDEQQTMFYGSVKTGYTIGYGLSLATLLVATAILSLFRKLHCTRNYIHMHLFISFILRAAAVFIKDLALFDSGESDQCSEGSVGCKAAMVFFQYCVMANFFWLLVEGLYLYTLLAVSFFSERKYFWGYILIGWGVPSTFTMVWTIARIHFEDYGCWDTINSSLWWIIKGPILTSILVNFILFICIIRILLQKLRPPDIRKSDSSPYSRLARSTLLLIPLFGVHYIMFAFFPDNFKPEVKMVFELVVGSFQGFVVAILYCFLNGEVQAELRRKWRRWHLQGVLGWNPKYRHPSGGSNGATCSTQVSMLTRVSPGARRSSSFQAEVSLV TTCL30I TT Clinical trial TTCL30I KE hsa04080:Neuroactive ligand-receptor interaction TTCL30I RC R-HSA-418555:G alpha (s) signalling events TTIVDM3 ID TTIVDM3 TTIVDM3 TN Voltage-gated potassium channel Kv7.3 (KCNQ3) TTIVDM3 UP O43525 TTIVDM3 UC KCNQ3_HUMAN TTIVDM3 BC Voltage-gated ion channel TTIVDM3 SN Voltage-gated potassium channel subunit Kv7.3; Potassium channel alpha subunit KvLQT3; Potassium channel KQT-like 3; KQT-like 3; KCNQ3; K+ channel KCNQ3 TTIVDM3 GN KCNQ3 TTIVDM3 FC Probably important in the regulation of neuronal excitability. Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. TTIVDM3 PD 5J03 TTIVDM3 SQ MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQEQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAASSQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPRNEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPTKGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNLPRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDTDTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI TTIVDM3 TT Clinical trial TTIVDM3 KE hsa04725:Cholinergic synapse TTIVDM3 RC R-HSA-1296072:Voltage gated Potassium channels; R-HSA-445095:Interaction between L1 and Ankyrins TT84DRB ID TT84DRB TT84DRB TN Voltage-gated sodium channel alpha Nav1.4 (SCN4A) TT84DRB UP P35499 TT84DRB UC SCN4A_HUMAN TT84DRB BC Voltage-gated ion channel TT84DRB SN Voltage-gated sodium channel subunit alpha Nav1.4; Sodium channel protein type IV subunit alpha; Sodium channel protein skeletal muscle subunit alpha; SkM1; SCN4A TT84DRB GN SCN4A TT84DRB FC This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. This sodium channel may be present in both denervated and innervated skeletal muscle. TT84DRB PD 6MC9; 6MBA; 6AGF TT84DRB SQ MARPSLCTLVPLGPECLRPFTRESLAAIEQRAVEEEARLQRNKQMEIEEPERKPRSDLEAGKNLPMIYGDPPPEVIGIPLEDLDPYYSNKKTFIVLNKGKAIFRFSATPALYLLSPFSVVRRGAIKVLIHALFSMFIMITILTNCVFMTMSDPPPWSKNVEYTFTGIYTFESLIKILARGFCVDDFTFLRDPWNWLDFSVIMMAYLTEFVDLGNISALRTFRVLRALKTITVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALVGLQLFMGNLRQKCVRWPPPFNDTNTTWYSNDTWYGNDTWYGNEMWYGNDSWYANDTWNSHASWATNDTFDWDAYISDEGNFYFLEGSNDALLCGNSSDAGHCPEGYECIKTGRNPNYGYTSYDTFSWAFLALFRLMTQDYWENLFQLTLRAAGKTYMIFFVVIIFLGSFYLINLILAVVAMAYAEQNEATLAEDKEKEEEFQQMLEKFKKHQEELEKAKAAQALEGGEADGDPAHGKDCNGSLDTSQGEKGAPRQSSSGDSGISDAMEELEEAHQKCPPWWYKCAHKVLIWNCCAPWLKFKNIIHLIVMDPFVDLGITICIVLNTLFMAMEHYPMTEHFDNVLTVGNLVFTGIFTAEMVLKLIAMDPYEYFQQGWNIFDSIIVTLSLVELGLANVQGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKIALDCNLPRWHMHDFFHSFLIVFRILCGEWIETMWDCMEVAGQAMCLTVFLMVMVIGNLVVLNLFLALLLSSFSADSLAASDEDGEMNNLQIAIGRIKLGIGFAKAFLLGLLHGKILSPKDIMLSLGEADGAGEAGEAGETAPEDEKKEPPEEDLKKDNHILNHMGLADGPPSSLELDHLNFINNPYLTIQVPIASEESDLEMPTEEETDTFSEPEDSKKPPQPLYDGNSSVCSTADYKPPEEDPEEQAEENPEGEQPEECFTEACVQRWPCLYVDISQGRGKKWWTLRRACFKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRRVIRTILEYADKVFTYIFIMEMLLKWVAYGFKVYFTNAWCWLDFLIVDVSIISLVANWLGYSELGPIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYYCINTTTSERFDISEVNNKSECESLMHTGQVRWLNVKVNYDNVGLGYLSLLQVATFKGWMDIMYAAVDSREKEEQPQYEVNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGKDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPQNKIQGMVYDLVTKQAFDITIMILICLNMVTMMVETDNQSQLKVDILYNINMIFIIIFTGECVLKMLALRQYYFTVGWNIFDFVVVILSIVGLALSDLIQKYFVSPTLFRVIRLARIGRVLRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMSNFAYVKKESGIDDMFNFETFGNSIICLFEITTSAGWDGLLNPILNSGPPDCDPNLENPGTSVKGDCGNPSIGICFFCSYIIISFLIVVNMYIAIILENFNVATEESSEPLGEDDFEMFYETWEKFDPDATQFIAYSRLSDFVDTLQEPLRIAKPNKIKLITLDLPMVPGDKIHCLDILFALTKEVLGDSGEMDALKQTMEEKFMAANPSKVSYEPITTTLKRKHEEVCAIKIQRAYRRHLLQRSMKQASYMYRHSHDGSGDDAPEKEGLLANTMSKMYGHENGNSSSPSPEEKGEAGDAGPTMGLMPISPSDTAWPPAPPPGQTVRPGVKESLV TT84DRB TT Clinical trial TT84DRB RC R-HSA-445095:Interaction between L1 and Ankyrins TTK3WBU ID TTK3WBU TTK3WBU TN XIAP messenger RNA (XIAP mRNA) TTK3WBU UP P98170 TTK3WBU UC XIAP_HUMAN TTK3WBU BC mRNA target TTK3WBU SN hILP (mRNA); hIAP3 (mRNA); hIAP-3 (mRNA); Xlinked IAP (mRNA); X-linked IAP (mRNA); RING-type E3 ubiquitin transferase XIAP (mRNA); Inhibitor of apoptosis protein 3 (mRNA); ILP (mRNA); IAPlike protein (mRNA); IAP3 (mRNA); IAP-like protein (mRNA); IAP-3 (mRNA); E3 ubiquitinprotein ligase XIAP (mRNA); E3 ubiquitin-protein ligase XIAP (mRNA); Baculoviral IAP repeatcontaining protein 4 (mRNA); Baculoviral IAP repeat-containing protein 4 (mRNA); BIRC4 (mRNA); API3 (mRNA) TTK3WBU GN XIAP TTK3WBU FC Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinationg COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program. Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. TTK3WBU EC EC 2.3.2.27 TTK3WBU PD 6QCI; 6EY2; 5OQW; 5O6T; 5M6M TTK3WBU SQ MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS TTK3WBU TT Clinical trial TTK3WBU FM mRNA target TTK3WBU KE hsa04064:NF-kappa B signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa04210:Apoptosis; hsa04510:Focal adhesion; hsa05145:Toxoplasmosis; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05222:Small cell lung cancer TTK3WBU RC R-HSA-111463:SMAC binds to IAPs; R-HSA-111464:SMAC-mediated dissociation of IAP:caspase complexes; R-HSA-3769402:Deactivation of the beta-catenin transactivating complex; R-HSA-5213460:RIPK1-mediated regulated necrosis; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5675482:Regulation of necroptotic cell death TTO9X1H ID TTO9X1H TTO9X1H TN 5-HT 7 receptor (HTR7) TTO9X1H UP P34969 TTO9X1H UC 5HT7R_HUMAN TTO9X1H BC GPCR rhodopsin TTO9X1H SN Serotonin receptor 7; 5HT7; 5-hydroxytryptamine receptor 7; 5-HT7 receptor; 5-HT7; 5-HT-X; 5-HT-7 TTO9X1H GN HTR7 TTO9X1H FC The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. TTO9X1H SQ MMDVNSSGRPDLYGHLRSFLLPEVGRGLPDLSPDGGADPVAGSWAPHLLSEVTASPAPTWDAPPDNASGCGEQINYGRVEKVVIGSILTLITLLTIAGNCLVVISVCFVKKLRQPSNYLIVSLALADLSVAVAVMPFVSVTDLIGGKWIFGHFFCNVFIAMDVMCCTASIMTLCVISIDRYLGITRPLTYPVRQNGKCMAKMILSVWLLSASITLPPLFGWAQNVNDDKVCLISQDFGYTIYSTAVAFYIPMSVMLFMYYQIYKAARKSAAKHKFPGFPRVEPDSVIALNGIVKLQKEVEECANLSRLLKHERKNISIFKREQKAATTLGIIVGAFTVCWLPFFLLSTARPFICGTSCSCIPLWVERTFLWLGYANSLINPFIYAFFNRDLRTTYRSLLQCQYRNINRKLSAAGMHEALKLAERPERPEFVLRACTRRVLLRPEKRPPVSVWVLQSPDHHNWLADKMLTTVEKKVMIHD TTO9X1H TT Clinical trial TTO9X1H FM GPCR rhodopsin TTO9X1H KE hsa04014:Ras signaling pathway; hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse TTO9X1H RC R-HSA-390666:Serotonin receptors; R-HSA-418555:G alpha (s) signalling events TTGYPTC ID TTGYPTC TTGYPTC TN Activin receptor-like kinase-1 (ACVRL1) TTGYPTC UP P37023 TTGYPTC UC ACVL1_HUMAN TTGYPTC BC Kinase TTGYPTC SN Serine/threonine-protein kinase receptor R3; SKR3; Activin receptor-like kinase 1; ALK-1; ACVRLK1; ACVRL1 TTGYPTC GN ACVRL1 TTGYPTC FC Type I receptor for TGF-beta family ligands BMP9/GDF2 and BMP10 and important regulator of normal blood vessel development. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. May bindactivin as well. TTGYPTC EC EC 2.7.11.30 TTGYPTC PD 4FAO; 3MY0; 2LCR TTGYPTC SQ MTLGSPRKGLLMLLMALVTQGDPVKPSRGPLVTCTCESPHCKGPTCRGAWCTVVLVREEGRHPQEHRGCGNLHRELCRGRPTEFVNHYCCDSHLCNHNVSLVLEATQPPSEQPGTDGQLALILGPVLALLALVALGVLGLWHVRRRQEKQRGLHSELGESSLILKASEQGDSMLGDLLDSDCTTGSGSGLPFLVQRTVARQVALVECVGKGRYGEVWRGLWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSLYDFLQRQTLEPHLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDFKSRNVLVKSNLQCCIADLGLAVMHSQGSDYLDIGNNPRVGTKRYMAPEVLDEQIRTDCFESYKWTDIWAFGLVLWEIARRTIVNGIVEDYRPPFYDVVPNDPSFEDMKKVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKISNSPEKPKVIQ TTGYPTC TT Clinical trial TT92EIB ID TT92EIB TT92EIB TN ADORA1 messenger RNA (ADORA1 mRNA) TT92EIB UP P30542 TT92EIB UC AA1R_HUMAN TT92EIB BC mRNA target TT92EIB SN Adenosine receptor A1 (mRNA); A(1) adenosine receptor (mRNA) TT92EIB GN ADORA1 TT92EIB FC The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Receptor for adenosine. TT92EIB PD 6D9H; 5UEN; 5N2S TT92EIB SQ MPPSISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGALVIPLAILINIGPQTYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKMVVTPRRAAVAIAGCWILSFVVGLTPMFGWNNLSAVERAWAANGSMGEPVIKCEFEKVISMEYMVYFNFFVWVLPPLLLMVLIYLEVFYLIRKQLNKKVSASSGDPQKYYGKELKIAKSLALILFLFALSWLPLHILNCITLFCPSCHKPSILTYIAIFLTHGNSAMNPIVYAFRIQKFRVTFLKIWNDHFRCQPAPPIDEDLPEERPDD TT92EIB TT Clinical trial TT92EIB FM mRNA target TT92EIB RC R-HSA-417973:Adenosine P1 receptors; R-HSA-418594:G alpha (i) signalling events TTG8ZWP ID TTG8ZWP TTG8ZWP TN ADRB2 messenger RNA (ADRB2 mRNA) TTG8ZWP UP P07550 TTG8ZWP UC ADRB2_HUMAN TTG8ZWP BC mRNA target TTG8ZWP SN Beta-2 adrenoreceptor (mRNA); Beta-2 adrenoceptor (mRNA); Beta-2 adrenergic receptor (mRNA); B2AR (mRNA); ADRB2R (mRNA) TTG8ZWP GN ADRB2 TTG8ZWP FC The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. TTG8ZWP PD 6MXT; 5X7D; 5JQH; 5D6L; 5D5B TTG8ZWP SQ MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL TTG8ZWP TT Clinical trial TTG8ZWP FM mRNA target TTG8ZWP KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04144:Endocytosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04970:Salivary secretion TTG8ZWP RC R-HSA-390696:Adrenoceptors; R-HSA-418555:G alpha (s) signalling events TTMO9HF ID TTMO9HF TTMO9HF TN Advanced glycosylation end product receptor (AGER) TTMO9HF UP Q15109 TTMO9HF UC RAGE_HUMAN TTMO9HF BC Immunoglobulin TTMO9HF SN Receptor foradvanced glycosylation end products; RAGESEC; RAGE; AGER TTMO9HF GN AGER TTMO9HF FC Mediates interactions of advanced glycosylation end products (age). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Receptor for amyloid beta peptide. TTMO9HF PD 5D7F; 4YBH; 4XYN; 4P2Y; 4OI8 TTMO9HF SQ MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP TTMO9HF TT Clinical trial TTMO9HF RC R-HSA-1810476:RIP-mediated NFkB activation via ZBP1; R-HSA-3134963:DEx/H-box helicases activate type I IFN and inflammatory cytokines production; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-879415:Advanced glycosylation endproduct receptor signaling; R-HSA-933542:TRAF6 mediated NF-kB activation TT9MNE2 ID TT9MNE2 TT9MNE2 TN Aldosterone synthase (CYP11B2) TT9MNE2 UP P19099 TT9MNE2 UC C11B2_HUMAN TT9MNE2 BC Paired donor oxygen oxidoreductase TT9MNE2 SN Steroid 18hydroxylase; Cytochrome P450C18; Cytochrome P450Aldo; Cytochrome P450 11B2, mitochondrial; CYPXIB2; CYP11B2; Aldosteronesynthesizing enzyme; ALDOS TT9MNE2 GN CYP11B2 TT9MNE2 FC Preferentially catalyzes the conversion of 11- deoxycorticosterone to aldosterone via corticosterone and 18- hydroxycorticosterone. TT9MNE2 EC EC 1.14.15.4 TT9MNE2 PD 4ZGX; 4FDH; 4DVQ TT9MNE2 SQ MALRAKAEVCVAAPWLSLQRARALGTRAARAPRTVLPFEAMPQHPGNRWLRLLQIWREQGYEHLHLEMHQTFQELGPIFRYNLGGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGIVAELLLKAELSLEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQILRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRPERYNPQRWLDIRGSGRNFHHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQEDIKMVYSFILRPGTSPLLTFRAIN TT9MNE2 TT Literature-reported TT9MNE2 KE hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways TT9MNE2 RC R-HSA-194002:Glucocorticoid biosynthesis; R-HSA-211976:Endogenous sterols TTHGL48 ID TTHGL48 TTHGL48 TN AP endonuclease 1 (APEX1) TTHGL48 UP P27695 TTHGL48 UC APEX1_HUMAN TTHGL48 BC Alpha-carbonic anhydrase TTHGL48 SN Redox factor-1; REF1; REF-1; HAP1; DNA-(apurinic or apyrimidinic site) lyase; Apurinic-apyrimidinic endonuclease 1; APX; APEX nuclease; APEX; APEN; APE1; APE-1; APE TTHGL48 GN APEX1 TTHGL48 FC Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA. TTHGL48 EC EC 3.1.-.- TTHGL48 PD 6MKO; 6MKM; 6MKK; 6MK3; 6BOW TTHGL48 SQ MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL TTHGL48 TT Clinical trial TTHGL48 KE hsa03410:Base excision repair TTXOZQ1 ID TTXOZQ1 TTXOZQ1 TN ApoC-III messenger RNA (APOC3 mRNA) TTXOZQ1 UP P02656 TTXOZQ1 UC APOC3_HUMAN TTXOZQ1 BC mRNA target TTXOZQ1 SN Apolipoprotein CIII (mRNA); Apolipoprotein C3 (mRNA); Apolipoprotein C-III (mRNA); ApoC-III (mRNA); Apo-CIII (mRNA) TTXOZQ1 GN APOC3 TTXOZQ1 FC Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners. Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. TTXOZQ1 PD 2JQ3 TTXOZQ1 SQ MQPRVLLVVALLALLASARASEAEDASLLSFMQGYMKHATKTAKDALSSVQESQVAQQARGWVTDGFSSLKDYWSTVKDKFSEFWDLDPEVRPTSAVAA TTXOZQ1 TT Successful TTXOZQ1 FM mRNA target TTXOZQ1 KE hsa03320:PPAR signaling pathway TTXOZQ1 RC R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-194223:HDL-mediated lipid transport; R-HSA-975634:Retinoid metabolism and transport TTU9LGY ID TTU9LGY TTU9LGY TN Apolipoprotein A messenger RNA (LPA mRNA) TTU9LGY UP P08519 TTU9LGY UC APOA_HUMAN TTU9LGY BC mRNA target TTU9LGY SN Lp(a) (mRNA); Apolipoprotein(a) (mRNA); Apo(a) (mRNA) TTU9LGY GN LPA TTU9LGY FC It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330. Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). TTU9LGY EC EC 3.4.21.- TTU9LGY PD 4KIV; 4BVW; 4BVV; 4BVD; 4BVC TTU9LGY SQ MEHKEVVLLLLLFLKSAAPEQSHVVQDCYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNRTTENYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDPVAAPYCYTRDPSVRWEYCNLTQCSDAEGTAVAPPTITPIPSLEAPSEQAPTEQRPGVQECYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSRTPAYYPNAGLIKNYCRNPDPVAAPWCYTTDPSVRWEYCNLTRCSDAEWTAFVPPNVILAPSLEAFFEQALTEETPGVQDCYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSRTPENYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQCLVTESSVLATLTVVPDPSTEASSEEAPTEQSPGVQDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEISPWCYTMDPNVRWEYCNLTQCPVTESSVLATSTAVSEQAPTEQSPTVQDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQCPVMESTLLTTPTVVPVPSTELPSEEAPTENSTGVQDCYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRIPLYYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTRCPVTESSVLTTPTVAPVPSTEAPSEQAPPEKSPVVQDCYHGDGRSYRGISSTTVTGRTCQSWSSMIPHWHQRTPENYPNAGLTENYCRNPDSGKQPWCYTTDPCVRWEYCNLTQCSETESGVLETPTVVPVPSMEAHSEAAPTEQTPVVRQCYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQRTPENYPNDGLTMNYCRNPDADTGPWCFTMDPSIRWEYCNLTRCSDTEGTVVAPPTVIQVPSLGPPSEQDCMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHSTFIPGTNKWAGLEKNYCRNPDGDINGPWCYTMNPRKLFDYCDIPLCASSSFDCGKPQVEPKKCPGSIVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLKKSSRPSSYKVILGAHQEVNLESHVQEIEVSRLFLEPTQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGETQGTFGTGLLKEAQLLVIENEVCNHYKYICAEHLARGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWIEGMMRNN TTU9LGY TT Clinical trial TTU9LGY FM mRNA target TTU9LGY RC R-HSA-171052:LDL-mediated lipid transport TT7GN3U ID TT7GN3U TT7GN3U TN Apolipoprotein A-I (APOA1) TT7GN3U UP P02647 TT7GN3U UC APOA1_HUMAN TT7GN3U BC Apolipoprotein TT7GN3U SN Truncated apolipoprotein AI; Apolipoprotein A1; ApoAI; ApoA-I; Apo-AI TT7GN3U GN APOA1 TT7GN3U FC As part of the SPAP complex, activates spermatozoa motility. Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). TT7GN3U PD 6CM1; 6CLZ; 6CCX; 6CCH; 6CC9 TT7GN3U SQ MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ TT7GN3U TT Clinical trial TT7GN3U FM Apolipoprotein TT7GN3U KE hsa03320:PPAR signaling pathway; hsa04975:Fat digestion and absorption; hsa04977:Vitamin digestion and absorption; hsa05143:African trypanosomiasis TT7GN3U RC R-HSA-114608:Platelet degranulation; R-HSA-1369062:ABC transporters in lipid homeostasis; R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-194223:HDL-mediated lipid transport; R-HSA-1989781:PPARA activates gene expression; R-HSA-2168880:Scavenging of heme from plasma; R-HSA-3000471:Scavenging by Class B Receptors; R-HSA-3000480:Scavenging by Class A Receptors; R-HSA-975634:Retinoid metabolism and transport; R-HSA-977225:Amyloid formation TTGUMYS ID TTGUMYS TTGUMYS TN Apolipoprotein(a) (LPA) TTGUMYS UP P08519 TTGUMYS UC APOA_HUMAN TTGUMYS BC Apolipoprotein TTGUMYS SN Lp(a); Lipoprotein(a); LPA; Apo(a) TTGUMYS GN LPA TTGUMYS FC Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330. TTGUMYS EC EC 3.4.21.- TTGUMYS PD 4KIV; 4BVW; 4BVV; 4BVD; 4BVC TTGUMYS SQ MEHKEVVLLLLLFLKSAAPEQSHVVQDCYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNRTTENYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDPVAAPYCYTRDPSVRWEYCNLTQCSDAEGTAVAPPTITPIPSLEAPSEQAPTEQRPGVQECYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSRTPAYYPNAGLIKNYCRNPDPVAAPWCYTTDPSVRWEYCNLTRCSDAEWTAFVPPNVILAPSLEAFFEQALTEETPGVQDCYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSRTPENYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQCLVTESSVLATLTVVPDPSTEASSEEAPTEQSPGVQDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEISPWCYTMDPNVRWEYCNLTQCPVTESSVLATSTAVSEQAPTEQSPTVQDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQCPVMESTLLTTPTVVPVPSTELPSEEAPTENSTGVQDCYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRIPLYYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTRCPVTESSVLTTPTVAPVPSTEAPSEQAPPEKSPVVQDCYHGDGRSYRGISSTTVTGRTCQSWSSMIPHWHQRTPENYPNAGLTENYCRNPDSGKQPWCYTTDPCVRWEYCNLTQCSETESGVLETPTVVPVPSMEAHSEAAPTEQTPVVRQCYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQRTPENYPNDGLTMNYCRNPDADTGPWCFTMDPSIRWEYCNLTRCSDTEGTVVAPPTVIQVPSLGPPSEQDCMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHSTFIPGTNKWAGLEKNYCRNPDGDINGPWCYTMNPRKLFDYCDIPLCASSSFDCGKPQVEPKKCPGSIVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLKKSSRPSSYKVILGAHQEVNLESHVQEIEVSRLFLEPTQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGETQGTFGTGLLKEAQLLVIENEVCNHYKYICAEHLARGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWIEGMMRNN TTGUMYS TT Clinical trial TTGUMYS RC R-HSA-171052:LDL-mediated lipid transport TTF0RCZ ID TTF0RCZ TTF0RCZ TN Apoptosis mediating surface antigen FAS (FAS) TTF0RCZ UP P25445 TTF0RCZ UC TNR6_HUMAN TTF0RCZ BC Cytokine receptor TTF0RCZ SN Tumor necrosis factor receptor superfamily member 6; TNFRSF6; FASLG receptor; FAS1; CD95; Apoptosis-mediating surface antigen FAS; Apo-1 antigen; APT1 TTF0RCZ GN FAS TTF0RCZ FC The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (in vitro). Receptor for TNFSF6/FASLG. TTF0RCZ PD 3TJE; 3THM; 3EZQ; 3EWT; 2NA7 TTF0RCZ SQ MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCRKHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKKANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV TTF0RCZ TT Clinical trial TTF0RCZ FM Cytokine receptor TTF0RCZ KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04115:p53 signaling pathway; hsa04210:Apoptosis; hsa04650:Natural killer cell mediated cytotoxicity; hsa04668:TNF signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04940:Type I diabetes mellitus; hsa05010:Alzheimer's disease; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05320:Autoimmune thyroid disease; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease TTF0RCZ RC R-HSA-75157:FasL/ CD95L signaling TTOQCD8 ID TTOQCD8 TTOQCD8 TN Apoptosis signal-regulating kinase 1 (MAP3K5) TTOQCD8 UP Q99683 TTOQCD8 UC M3K5_HUMAN TTOQCD8 BC Kinase TTOQCD8 SN Mitogen-activated protein kinase kinase kinase 5; MEKK5; MEKK 5; MEK kinase 5; MAPKKK5; MAPK/ERK kinase kinase 5; ASK1; ASK-1 TTOQCD8 GN MAP3K5 TTOQCD8 FC Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1). Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. TTOQCD8 EC EC 2.7.11.25 TTOQCD8 PD 6EJL; 6E2O; 6E2N; 6E2M; 5VIO TTOQCD8 SQ MSTEADEGITFSVPPFAPSGFCTIPEGGICRRGGAAAVGEGEEHQLPPPPPGSFWNVESAAAPGIGCPAATSSSSATRGRGSSVGGGSRRTTVAYVINEASQGQLVVAESEALQSLREACETVGATLETLHFGKLDFGETTVLDRFYNADIAVVEMSDAFRQPSLFYHLGVRESFSMANNIILYCDTNSDSLQSLKEIICQKNTMCTGNYTFVPYMITPHNKVYCCDSSFMKGLTELMQPNFELLLGPICLPLVDRFIQLLKVAQASSSQYFRESILNDIRKARNLYTGKELAAELARIRQRVDNIEVLTADIVINLLLSYRDIQDYDSIVKLVETLEKLPTFDLASHHHVKFHYAFALNRRNLPGDRAKALDIMIPMVQSEGQVASDMYCLVGRIYKDMFLDSNFTDTESRDHGASWFKKAFESEPTLQSGINYAVLLLAAGHQFESSFELRKVGVKLSSLLGKKGNLEKLQSYWEVGFFLGASVLANDHMRVIQASEKLFKLKTPAWYLKSIVETILIYKHFVKLTTEQPVAKQELVDFWMDFLVEATKTDVTVVRFPVLILEPTKIYQPSYLSINNEVEEKTISIWHVLPDDKKGIHEWNFSASSVRGVSISKFEERCCFLYVLHNSDDFQIYFCTELHCKKFFEMVNTITEEKGRSTEEGDCESDLLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIKEIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGFIKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILEGLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRLAGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGCTIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSAEAKAFILKCFEPDPDKRACANDLLVDEFLKVSSKKKKTQPKLSALSAGSNEYLRSISLPVPVLVEDTSSSSEYGSVSPDTELKVDPFSFKTRAKSCGERDVKGIRTLFLGIPDENFEDHSAPPSPEEKDSGFFMLRKDSERRATLHRILTEDQDKIVRNLMESLAQGAEEPKLKWEHITTLIASLREFVRSTDRKIIATTLSKLKLELDFDSHGISQVQVVLFGFQDAVNKVLRNHNIKPHWMFALDSIIRKAVQTAITILVPELRPHFSLASESDTADQEDLDVEDDHEEQPSNQTVRRPQAVIEDAVATSGVSTLSSTVSHDSQSAHRSLNVQLGRMKIETNRLLEELVRKEKELQALLHRAIEEKDQEIKHLKLKSQPIEIPELPVFHLNSSGTNTEDSELTDWLRVNGADEDTISRFLAEDYTLLDVLYYVTRDDLKCLRLRGGMLCTLWKAIIDFRNKQT TTOQCD8 TT Clinical trial TTOQCD8 FM Kinase TTOQCD8 KE hsa04010:MAPK signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04141:Protein processing in endoplasmic reticulum; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05014:Amyotrophic lateral sclerosis (ALS) TTOQCD8 RC R-HSA-2559580:Oxidative Stress Induced Senescence TT5TURO ID TT5TURO TT5TURO TN A-Raf messenger RNA (ARAF mRNA) TT5TURO UP P10398 TT5TURO UC ARAF_HUMAN TT5TURO BC mRNA target TT5TURO SN Serine/threonine-protein kinase A-Raf (mRNA); Proto-oncogene Pks (mRNA); Proto-oncogene A-Raf-1 (mRNA); Proto-oncogene A-Raf (mRNA); PKS2 (mRNA); PKS (mRNA); ARAF1 (mRNA) TT5TURO GN ARAF TT5TURO FC May also regulate the TOR signaling cascade. Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. TT5TURO EC EC 2.7.11.1 TT5TURO PD 2MSE; 1WXM TT5TURO SQ MEPPRGPPANGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRQQFYHSVQDLSGGSRQHEAPSNRPLNELLTPQGPSPRTQHCDPEHFPFPAPANAPLQRIRSTSTPNVHMVSTTAPMDSNLIQLTGQSFSTDAAGSRGGSDGTPRGSPSPASVSSGRKSPHSKSPAEQRERKSLADDKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGSFGTVFRGRWHGDVAVKVLKVSQPTAEQAQAFKNEMQVLRKTRHVNILLFMGFMTRPGFAIITQWCEGSSLYHHLHVADTRFDMVQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGAQPLEQPSGSVLWMAAEVIRMQDPNPYSFQSDVYAYGVVLYELMTGSLPYSHIGCRDQIIFMVGRGYLSPDLSKISSNCPKAMRRLLSDCLKFQREERPLFPQILATIELLQRSLPKIERSASEPSLHRTQADELPACLLSAARLVP TT5TURO TT Clinical trial TT5TURO FM mRNA target TT5TURO KE hsa04012:ErbB signaling pathway; hsa04068:FoxO signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04650:Natural killer cell mediated cytotoxicity; hsa04720:Long-term potentiation; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa05034:Alcoholism; hsa05160:Hepatitis C; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer TT5TURO RC R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5675221:Negative regulation of MAPK pathway TTG5QIA ID TTG5QIA TTG5QIA TN B1 bradykinin receptor (BDKRB1) TTG5QIA UP P46663 TTG5QIA UC BKRB1_HUMAN TTG5QIA BC GPCR rhodopsin TTG5QIA SN BRADYB1; BK-1 receptor; B1R TTG5QIA GN BDKRB1 TTG5QIA FC This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation. TTG5QIA SQ MASSWPPLELQSSNQSQLFPQNATACDNAPEAWDLLHRVLPTFIISICFFGLLGNLFVLLVFLLPRRQLNVAEIYLANLAASDLVFVLGLPFWAENIWNQFNWPFGALLCRVINGVIKANLFISIFLVVAISQDRYRVLVHPMASRRQQRRRQARVTCVLIWVVGGLLSIPTFLLRSIQAVPDLNITACILLLPHEAWHFARIVELNILGFLLPLAAIVFFNYHILASLRTREEVSRTRCGGRKDSKTTALILTLVVAFLVCWAPYHFFAFLEFLFQVQAVRGCFWEDFIDLGLQLANFFAFTNSSLNPVIYVFVGRLFRTKVWELYKQCTPKSLAPISSSHRKEIFQLFWRN TTG5QIA TT Clinical trial TTG5QIA KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04610:Complement and coagulation cascades; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer TTG5QIA RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events TT5UJWD ID TT5UJWD TT5UJWD TN Basigin (BSG) TT5UJWD UP P35613 TT5UJWD UC BASI_HUMAN TT5UJWD BC Basigin protein TT5UJWD SN UNQ6505/PRO21383; Tumor cell-derived collagenase stimulatory factor; TCSF; OK blood group antigen; Leukocyte activation antigen M6; Extracellular matrix metalloproteinase inducer; EMMPRIN; 5F7 TT5UJWD GN BSG TT5UJWD FC Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes. Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3, SLC16A8, SLC16A11 and SLC16A12 to the plasma membrane. TT5UJWD PD 5XF0; 5X0T; 4U0Q; 3QR2; 3QQN TT5UJWD SQ MAAALFVLLGFALLGTHGASGAAGFVQAPLSQQRWVGGSVELHCEAVGSPVPEIQWWFEGQGPNDTCSQLWDGARLDRVHIHATYHQHAASTISIDTLVEEDTGTYECRASNDPDRNHLTRAPRVKWVRAQAVVLVLEPGTVFTTVEDLGSKILLTCSLNDSATEVTGHRWLKGGVVLKEDALPGQKTEFKVDSDDQWGEYSCVFLPEPMGTANIQLHGPPRVKAVKSSEHINEGETAMLVCKSESVPPVTDWAWYKITDSEDKALMNGSESRFFVSSSQGRSELHIENLNMEADPGQYRCNGTSSKGSDQAIITLRVRSHLAALWPFLGIVAEVLVLVTIIFIYEKRRKPEDVLDDDDAGSAPLKSSGQHQNDKGKNVRQRNSS TT5UJWD TT Clinical trial TT5UJWD FM Basigin family TT5UJWD RC R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-210991:Basigin interactions; R-HSA-216083:Integrin cell surface interactions; R-HSA-70268:Pyruvate metabolism TTFOUV4 ID TTFOUV4 TTFOUV4 TN BCL-2 messenger RNA (BCL2 mRNA) TTFOUV4 UP P10415 TTFOUV4 UC BCL2_HUMAN TTFOUV4 BC mRNA target TTFOUV4 SN Bcl-2 (mRNA); Apoptosis regulator Bcl-2 (mRNA) TTFOUV4 GN BCL2 TTFOUV4 FC Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release. Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. TTFOUV4 PD 6GL8; 5VAY; 5VAX; 5VAU; 5JSN TTFOUV4 SQ MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK TTFOUV4 TT Clinical trial TTFOUV4 FM mRNA target TTFOUV4 KE hsa04064:NF-kappa B signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04141:Protein processing in endoplasmic reticulum; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04510:Focal adhesion; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05215:Prostate cancer; hsa05222:Small cell lung cancer TTFOUV4 RC R-HSA-111447:Activation of BAD and translocation to mitochondria; R-HSA-111453:BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members; R-HSA-844455:The NLRP1 inflammasome TTJUNZF ID TTJUNZF TTJUNZF TN Beta-secretase 1 (BACE1) TTJUNZF UP P56817 TTJUNZF UC BACE1_HUMAN TTJUNZF BC Peptidase TTJUNZF SN Membrane-associated aspartic protease 2; Memapsin-2; KIAA1149; Beta-site amyloid precursor protein cleaving enzyme 1; Beta-site APP cleaving enzyme 1; BACE; Aspartyl protease 2; Asp 2; ASP2 TTJUNZF GN BACE1 TTJUNZF FC Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves APP with much more catalytic efficiency than for the wild-type. Responsible for the proteolytic processing of the amyloid precursor protein (APP). TTJUNZF EC EC 3.4.23.46 TTJUNZF PD 6FGY; 6EQM; 6EJ3; 6EJ2; 6DMI TTJUNZF SQ MAQALPWLLLWMGAGVLPAHGTQHGIRLPLRSGLGGAPLGLRLPRETDEEPEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQWRCLRCLRQQHDDFADDISLLK TTJUNZF TT Clinical trial TTJUNZF FM Peptidase A1 family TTJUNZF KE hsa05010:Alzheimer disease TTXYCDZ ID TTXYCDZ TTXYCDZ TN Bifunctional aminoacyl-tRNA synthetase (EPRS) TTXYCDZ UP P07814 TTXYCDZ UC SYEP_HUMAN TTXYCDZ BC Carbon-oxygen ligase TTXYCDZ SN QPRS; QARS; ProlinetRNA ligase; PIG32; GlutamatylprolyltRNA synthetase; Glutamatyl-prolyl-tRNA synthetase; GluRS; EPRS; Cell proliferationinducing gene 32 protein; Cell proliferation-inducing gene 32 protein; Bifunctional glutamate/prolinetRNA ligase; Bifunctional glutamate/proline--tRNA ligase; Bifunctional aminoacyltRNA synthetase TTXYCDZ GN EPRS TTXYCDZ FC The phosphorylation of EPRS, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it to the GAIT complex that binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin), suppressing their translation. Interferon-gamma can therefore redirect, in specific cells, the EPRS function from protein synthesis to translation inhibition. Also functions as an effector of the mTORC1 signaling pathway by promoting, through SLC27A1, the uptake of long-chain fatty acid by adipocytes. Thereby, it also plays a role in fat metabolism and more indirectly influences lifespan. Multifunctional protein which is primarily part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. TTXYCDZ PD 5Y6L; 5VAD; 5V58; 5BMU; 5A5H TTXYCDZ SQ MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLARVATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENKDYKKTTKVTWLAETTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPFKERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKSEKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY TTXYCDZ TT Clinical trial TTXYCDZ FM Carbon oxygen ligase TTXYCDZ KE hsa00860:Porphyrin and chlorophyll metabolism; hsa00970:Aminoacyl-tRNA biosynthesis; hsa01100:Metabolic pathways TTTRNQW ID TTTRNQW TTTRNQW TN Bile-salt-activated lipase (CEL) TTTRNQW UP P19835 TTTRNQW UC CEL_HUMAN TTTRNQW BC Carboxylic ester hydrolase TTTRNQW SN Pancreatic lysophospholipase; Pancreatic cholesterol esterase; Cholesterol esterase; Carboxyl ester lipase; CEL; Bile-salt-stimulated lipase; BSSL; BAL TTTRNQW GN CEL TTTRNQW FC Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides. TTTRNQW EC EC 3.1.1.13 TTTRNQW PD 6H1A; 6H19; 6H18; 6H0V; 6H0T TTTRNQW SQ MGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTKALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPVMIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPGNYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQSGVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYPMLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVTEEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIALAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTVSKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLRYWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDSGAPPVPPTGDSEAAPVPPTDDSKEAQMPAVIRF TTTRNQW TT Clinical trial TT7CPI5 ID TT7CPI5 TT7CPI5 TN Bromodomain testis-specific protein (BRDT) TT7CPI5 UP Q58F21 TT7CPI5 UC BRDT_HUMAN TT7CPI5 BC Bromodomain TT7CPI5 SN Cancer/testis antigen 9; CT9 TT7CPI5 GN BRDT TT7CPI5 FC Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of specific meiotic and post-meiotic genes, facilitating their activation at the appropriate time. In the post-meiotic phase of spermatogenesis, binds to hyperacetylated histones and participates in their general removal from DNA. Also recognizes and binds a subset of butyrylated histones: able to bind histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-5' (H4K5ac). Also acts as a component of the splicing machinery in pachytene spermatocytes and round spermatids and participates in 3'-UTR truncation of specific mRNAs in post-meiotic spermatids. Required for chromocenter organization, a structure comprised of peri-centromeric heterochromatin. Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. TT7CPI5 PD 5VBR; 5VBQ; 4KCX; 4FLP; 2RFJ TT7CPI5 SQ MSLPSRQTAIIVNPPPPEYINTKKNGRLTNQLQYLQKVVLKDLWKHSFSWPFQRPVDAVKLQLPDYYTIIKNPMDLNTIKKRLENKYYAKASECIEDFNTMFSNCYLYNKPGDDIVLMAQALEKLFMQKLSQMPQEEQVVGVKERIKKGTQQNIAVSSAKEKSSPSATEKVFKQQEIPSVFPKTSISPLNVVQGASVNSSSQTAAQVTKGVKRKADTTTPATSAVKASSEFSPTFTEKSVALPPIKENMPKNVLPDSQQQYNVVKTVKVTEQLRHCSEILKEMLAKKHFSYAWPFYNPVDVNALGLHNYYDVVKNPMDLGTIKEKMDNQEYKDAYKFAADVRLMFMNCYKYNPPDHEVVTMARMLQDVFETHFSKIPIEPVESMPLCYIKTDITETTGRENTNEASSEGNSSDDSEDERVKRLAKLQEQLKAVHQQLQVLSQVPFRKLNKKKEKSKKEKKKEKVNNSNENPRKMCEQMRLKEKSKRNQPKKRKQQFIGLKSEDEDNAKPMNYDEKRQLSLNINKLPGDKLGRVVHIIQSREPSLSNSNPDEIEIDFETLKASTLRELEKYVSACLRKRPLKPPAKKIMMSKEELHSQKKQELEKRLLDVNNQLNSRKRQTKSDKTQPSKAVENVSRLSESSSSSSSSSESESSSSDLSSSDSSDSESEMFPKFTEVKPNDSPSKENVKKMKNECIPPEGRTGVTQIGYCVQDTTSANTTLVHQTTPSHVMPPNHHQLAFNYQELEHLQTVKNISPLQILPPSGDSEQLSNGITVMHPSGDSDTTMLESECQAPVQKDIKIKNADSWKSLGKPVKPSGVMKSSDELFNQFRKAAIEKEVKARTQELIRKHLEQNTKELKASQENQRDLGNGLTVESFSNKIQNKCSGEEQKEHQQSSEAQDKSKLWLLKDRDLARQKEQERRRREAMVGTIDMTLQSDIMTMFENNFD TT7CPI5 TT Clinical trial TT7CPI5 FM Bromodomain TTDP48B ID TTDP48B TTDP48B TN Bromodomain-containing protein 2 (BRD2) TTDP48B UP P25440 TTDP48B UC BRD2_HUMAN TTDP48B BC Bromodomain TTDP48B SN Really interesting new gene 3 protein; RING3; O27.1.1; KIAA9001 TTDP48B GN BRD2 TTDP48B FC Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly. May play a role in spermatogenesis or folliculogenesis. TTDP48B PD 6MOA; 6MO9; 6MO8; 6MO7; 6FFG TTDP48B SQ MLQNVTPHNKLPGEGNAGLLGLGPEAAAPGKRIRKPSLLYEGFESPTMASVPALQLTPANPPPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPMDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMPQEEQELVVTIPKNSHKKGAKLAALQGSVTSAHQVPAVSSVSHTALYTPPPEIPTTVLNIPHPSVISSPLLKSLHSAGPPLLAVTAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGSPASPPGSLEPKAARLPPMRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKELLSKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRLMFSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTAMPPGLAKSSSESSSEESSSESSSEEEEEEDEEDEEEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQGPISKPKRKREKKEKKKKRKAEKHRGRAGADEDDKGPRAPRPPQPKKSKKASGSGGGSAALGPSGFGPSGGSGTKLPKKATKTAPPALPTGYDSEEEEESRPMSYDEKRQLSLDINKLPGEKLGRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIKKPVGKTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKANEKTESSSAQQVAVSRLSASSSSSDSSSSSSSSSSSDTSDSDSG TTDP48B TT Clinical trial TTDP48B FM Bromodomain TTHE657 ID TTHE657 TTHE657 TN Bromodomain-containing protein 3 (BRD3) TTHE657 UP Q15059 TTHE657 UC BRD3_HUMAN TTHE657 BC Bromodomain TTHE657 SN RING3like protein; RING3L; RING3-like protein; KIAA0043 TTHE657 GN BRD3 TTHE657 FC Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets. Chromatin reader that recognizes and binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. TTHE657 PD 6I7A; 6I68; 6I5P; 6I41; 6BGH TTHE657 SQ MSTATTVAPAGIPATPGPVNPPPPEVSNPSKPGRKTNQLQYMQNVVVKTLWKHQFAWPFYQPVDAIKLNLPDYHKIIKNPMDMGTIKKRLENNYYWSASECMQDFNTMFTNCYIYNKPTDDIVLMAQALEKIFLQKVAQMPQEEVELLPPAPKGKGRKPAAGAQSAGTQQVAAVSSVSPATPFQSVPPTVSQTPVIAATPVPTITANVTSVPVPPAAAPPPPATPIVPVVPPTPPVVKKKGVKRKADTTTPTTSAITASRSESPPPLSDPKQAKVVARRESGGRPIKPPKKDLEDGEVPQHAGKKGKLSEHLRYCDSILREMLSKKHAAYAWPFYKPVDAEALELHDYHDIIKHPMDLSTVKRKMDGREYPDAQGFAADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPVEAPALPAPAAPMVSKGAESSRSSEESSSDSGSSDSEEERATRLAELQEQLKAVHEQLAALSQAPVNKPKKKKEKKEKEKKKKDKEKEKEKHKVKAEEEKKAKVAPPAKQAQQKKAPAKKANSTTTAGRQLKKGGKQASASYDSEEEEEGLPMSYDEKRQLSLDINRLPGEKLGRVVHIIQSREPSLRDSNPDEIEIDFETLKPTTLRELERYVKSCLQKKQRKPFSASGKKQAAKSKEELAQEKKKELEKRLQDVSGQLSSSKKPARKEKPGSAPSGGPSRLSSSSSSESGSSSSSGSSSDSSDSE TTHE657 TT Clinical trial TTHE657 FM Bromodomain TTRA6BO ID TTRA6BO TTRA6BO TN Bromodomain-containing protein 4 (BRD4) TTRA6BO UP O60885 TTRA6BO UC BRD4_HUMAN TTRA6BO BC Bromodomain TTRA6BO SN Protein HUNK1; HUNK1 TTRA6BO GN BRD4 TTRA6BO FC Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters. Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6. BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II. Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II. According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo. In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B. Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters. TTRA6BO PD 6Q3Z; 6Q3Y; 6MNL; 6MAU; 6HDQ TTRA6BO SQ MSAESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQATPHPFPAVTPDLIVQTPVMTVVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLPPEPKTTKLGQRRESSRPVKPPKKDVPDSQQHPAPEKSSKVSEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLEAREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVAVSSPAVPPPTKVVAPPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKEKDKKEKKKEKHKRKEEVEENKKSKAKEPPPKKTKKNNSSNSNVSKKEPAPMKSKPPPTYESEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESSSESSSSDSEDSETEMAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQQQQQPPPPPPPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPAVSPALTQTPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPPPPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTHIQQPPPPQGQQPPHPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPLMIHSPQMSQFQSLTHQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPFSPSLRPEPPKHPESIKAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKAQAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAAAVAAAATPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF TTRA6BO TT Clinical trial TTRA6BO FM Bromodomain TTHXFA1 ID TTHXFA1 TTHXFA1 TN C5a anaphylatoxin chemotactic receptor (C5AR1) TTHXFA1 UP P21730 TTHXFA1 UC C5AR1_HUMAN TTHXFA1 BC GPCR rhodopsin TTHXFA1 SN CD88; C5aR; C5a-R; C5a anaphylatoxin chemotactic receptor 1; C5R1 TTHXFA1 GN C5AR1 TTHXFA1 FC The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production. Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a. TTHXFA1 PD 6C1R; 6C1Q; 5O9H TTHXFA1 SQ MDSFNYTTPDYGHYDDKDTLDLNTPVDKTSNTLRVPDILALVIFAVVFLVGVLGNALVVWVTAFEAKRTINAIWFLNLAVADFLSCLALPILFTSIVQHHHWPFGGAACSILPSLILLNMYASILLLATISADRFLLVFKPIWCQNFRGAGLAWIACAVAWGLALLLTIPSFLYRVVREEYFPPKVLCGVDYSHDKRRERAVAIVRLVLGFLWPLLTLTICYTFILLRTWSRRATRSTKTLKVVVAVVASFFIFWLPYQVTGIMMSFLEPSSPTFLLLKKLDSLCVSFAYINCCINPIIYVVAGQGFQGRLRKSLPSLLRNVLTEESVVRESKSFTRSTVDTMAQKTQAV TTHXFA1 TT Clinical trial TTHXFA1 FM GPCR rhodopsin TTHXFA1 KE hsa04080:Neuroactive ligand-receptor interaction; hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection TTHXFA1 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTY6O0Q ID TTY6O0Q TTY6O0Q TN Calcitonin gene-related peptide receptor (CGRPR) TTY6O0Q UP Q16602 TTY6O0Q UC CALRL_HUMAN TTY6O0Q BC GPCR secretin TTY6O0Q SN Calcitonin receptor-like receptor; Calcitonin gene-related peptide type 1 receptor; CGRPR; CGRP type 1 receptor TTY6O0Q GN CALCRL TTY6O0Q FC Receptor for calcitonin-gene-related peptide (CGRP) together with RAMP1 and receptor for adrenomedullin together with RAMP3 (By similarity). Receptor for adrenomedullin together with RAMP2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. TTY6O0Q PD 6E3Y; 6D1U; 5V6Y; 4RWG; 4RWF TTY6O0Q SQ MEKKCTLNFLVLLPFFMILVTAELEESPEDSIQLGVTRNKIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLTIIGHGLSIASLLISLGIFFYFKSLSCQRITLHKNLFFSFVCNSVVTIIHLTAVANNQALVATNPVSCKVSQFIHLYLMGCNYFWMLCEGIYLHTLIVVAVFAEKQHLMWYYFLGWGFPLIPACIHAIARSLYYNDNCWISSDTHLLYIIHGPICAALLVNLFFLLNIVRVLITKLKVTHQAESNLYMKAVRATLILVPLLGIEFVLIPWRPEGKIAEEVYDYIMHILMHFQGLLVSTIFCFFNGEVQAILRRNWNQYKIQFGNSFSNSEALRSASYTVSTISDGPGYSHDCPSEHLNGKSIHDIENVLLKPENLYN TTY6O0Q TT Successful TTY6O0Q FM GPCR secretin TTY6O0Q KE hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction TTY6O0Q RC R-HSA-418555:G alpha (s) signalling events; R-HSA-419812:Calcitonin-like ligand receptors TT0TMQG ID TT0TMQG TT0TMQG TN Calgranulin B (S100A9) TT0TMQG UP P06702 TT0TMQG UC S10A9_HUMAN TT0TMQG BC S100 calcium-binding protein TT0TMQG SN S100 calcium-binding protein A9; Protein S100-A9; P14; Myeloid-related protein 14; Migration inhibitory factor-related protein 14; MRP14; MRP-14; Leukocyte L1 complex heavy chain; Calprotectin L1H subunit; Calgranulin-B; CAGB TT0TMQG GN S100A9 TT0TMQG FC It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. Has transnitrosylase activity; in oxidatively-modified low-densitity lipoprotein (LDL(ox))-induced S-nitrosylation of GAPDH on 'Cys-247' proposed to transfer the NO moiety from NOS2/iNOS to GAPDH via its own S-nitrosylated Cys-3. The iNOS-S100A8/A9 transnitrosylase complex is proposed to also direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif. S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. TT0TMQG PD 6DS2; 5W1F; 5I8N; 4XJK; 4GGF TT0TMQG SQ MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP TT0TMQG TT Clinical trial TTY6DTE ID TTY6DTE TTY6DTE TN Carcinoembryonic antigen CEA (CD66e) TTY6DTE UP P06731 TTY6DTE UC CEAM5_HUMAN TTY6DTE BC Immunoglobulin TTY6DTE SN Meconium antigen 100; Carcinoembryonic antigen-related cell adhesion molecule 5; CEA; CD66e antigen TTY6DTE GN CEACAM5 TTY6DTE FC Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6. Plays a role as an oncogene by promoting tumor progression; induces resistance to anoikis of colorectal carcinoma cells. Cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. TTY6DTE PD 2VER; 2QST; 2QSQ; 1.00E+07 TTY6DTE SQ MESPSAPPHRWCIPWQRLLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPELPKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILNVLYGPDAPTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTTITVYAEPPKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNKLSVDHSDPVILNVLYGPDDPTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTITVSAELPKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLDVLYGPDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVSASGTSPGLSAGATVGIMIGVLVGVALI TTY6DTE TT Clinical trial TTB6T7O ID TTB6T7O TTB6T7O TN Caspase-9 (CASP9) TTB6T7O UP P55211 TTB6T7O UC CASP9_HUMAN TTB6T7O BC Peptidase TTB6T7O SN MCH6; ICE-like apoptotic protease 6; ICE-LAP6; CASP-9; Apoptotic protease-activating factor 3; Apoptotic protease activating factor 3; Apoptotic protease Mch-6; APAF-3 TTB6T7O GN CASP9 TTB6T7O FC Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Involved in the activation cascade of caspases responsible for apoptosis execution. TTB6T7O EC EC 3.4.22.62 TTB6T7O PD 5WVE; 5WVC; 5JUY; 4RHW; 3YGS TTB6T7O SQ MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMIEDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDTGQDMLASFLRTNRQAAKLSKPTLENLTPVVLRPEIRKPEVLRPETPRPVDIGSGGFGDVGALESLRGNADLAYILSMEPCGHCLIINNVNFCRESGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQQDHGALDCCVVVILSHGCQASHLQFPGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSNPEPDATPFQEGLRTFDQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAVSVKGIYKQMPGCFNFLRKKLFFKTS TTB6T7O TT Clinical trial TTB6T7O FM Peptidase TTB6T7O KE hsa04115:p53 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04370:VEGF signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05010:Alzheimer's disease; hsa05012:Parkinson's disease; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05016:Huntington's disease; hsa05134:Legionellosis; hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05210:Colorectal cancer; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05215:Prostate cancer; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05416:Viral myocarditis TTB6T7O RC R-HSA-111463:SMAC binds to IAPs; R-HSA-111464:SMAC-mediated dissociation of IAP:caspase complexes; R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer TTPS279 ID TTPS279 TTPS279 TN Catalase (CAT) TTPS279 UP P04040 TTPS279 UC CATA_HUMAN TTPS279 BC Peroxide acceptor oxidoreductase TTPS279 SN Human catalase TTPS279 GN CAT TTPS279 FC Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells. Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. TTPS279 EC EC 1.11.1.6 TTPS279 PD 1QQW; 1F4J; 1DGH; 1DGG; 1DGF TTPS279 SQ MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL TTPS279 TT Clinical trial TTPS279 FM Peroxidases TTPS279 KE hsa00380:Tryptophan metabolism; hsa00630:Glyoxylate and dicarboxylate metabolism; hsa01130:Biosynthesis of antibiotics; hsa04068:FoxO signaling pathway; hsa04146:Peroxisome; hsa05014:Amyotrophic lateral sclerosis (ALS) TTPS279 RC R-HSA-3299685:Detoxification of Reactive Oxygen Species; R-HSA-74259:Purine catabolism TT5NILS ID TT5NILS TT5NILS TN Cathepsin A (CTSA) TT5NILS UP P10619 TT5NILS UC PPGB_HUMAN TT5NILS BC Peptidase TT5NILS SN Protective protein for betagalactosidase; Protective protein cathepsin A; PPCA; Lysosomal protective protein 20 kDa chain; Lysosomal protective protein; Carboxypeptidase L; Carboxypeptidase C; CTSA TT5NILS GN CTSA TT5NILS FC Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins. TT5NILS EC EC 3.4.16.5 TT5NILS PD 4MWT; 4MWS; 4CIB; 4CIA; 4CI9 TT5NILS SQ MIRAAPPPLFLLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY TT5NILS TT Clinical trial TT5NILS KE hsa04142:Lysosome; hsa04614:Renin-angiotensin system TT5NILS RC R-HSA-1660662:Glycosphingolipid metabolism; R-HSA-2132295:MHC class II antigen presentation; R-HSA-4085001:Sialic acid metabolism TTIPS8B ID TTIPS8B TTIPS8B TN C-C chemokine receptor type 9 (CCR9) TTIPS8B UP P51686 TTIPS8B UC CCR9_HUMAN TTIPS8B BC GPCR rhodopsin TTIPS8B SN Gprotein coupled receptor 28; GPR96; GPR28; GPR-9-6; G-protein coupled receptor 28; CDw199; CCR-9; CCCKR9; CC-CKR-9; CC chemokine receptor type 9; CC CKR9; C-C CKR-9 TTIPS8B GN CCR9 TTIPS8B FC Subsequently transduces a signal by increasing the intracellular calcium ions level. Receptor for chemokine SCYA25/TECK. TTIPS8B PD 5LWE TTIPS8B SQ MTPTDFTSPIPNMADDYGSESTSSMEDYVNFNFTDFYCEKNNVRQFASHFLPPLYWLVFIVGALGNSLVILVYWYCTRVKTMTDMFLLNLAIADLLFLVTLPFWAIAAADQWKFQTFMCKVVNSMYKMNFYSCVLLIMCISVDRYIAIAQAMRAHTWREKRLLYSKMVCFTIWVLAAALCIPEILYSQIKEESGIAICTMVYPSDESTKLKSAVLTLKVILGFFLPFVVMACCYTIIIHTLIQAKKSSKHKALKVTITVLTVFVLSQFPYNCILLVQTIDAYAMFISNCAVSTNIDICFQVTQTIAFFHSCLNPVLYVFVGERFRRDLVKTLKNLGCISQAQWVSFTRREGSLKLSSMLLETTSGALSL TTIPS8B TT Clinical trial TTIPS8B KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04672:Intestinal immune network for IgA production TTIPS8B RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTSMTDI ID TTSMTDI TTSMTDI TN CDC7-related kinase (CDC7) TTSMTDI UP O00311 TTSMTDI UC CDC7_HUMAN TTSMTDI BC Kinase TTSMTDI SN huCdc7; HsCdc7; Cell division cycle 7related protein kinase; Cell division cycle 7-related protein kinase; CDC7related kinase; CDC7L1 TTSMTDI GN CDC7 TTSMTDI FC Can phosphorylates MCM2 and MCM3. Seems to phosphorylate critical substrates that regulate the G1/S phase transition and/or DNA replication. TTSMTDI EC EC 2.7.11.1 TTSMTDI PD 5UWR; 5UWQ; 4F9C; 4F9B; 4F9A TTSMTDI SQ MEASLGIQMDEPMAFSPQRDRFQAEGSLKKNEQNFKLAGVKKDIEKLYEAVPQLSNVFKIEDKIGEGTFSSVYLATAQLQVGPEEKIALKHLIPTSHPIRIAAELQCLTVAGGQDNVMGVKYCFRKNDHVVIAMPYLEHESFLDILNSLSFQEVREYMLNLFKALKRIHQFGIVHRDVKPSNFLYNRRLKKYALVDFGLAQGTHDTKIELLKFVQSEAQQERCSQNKSHIITGNKIPLSGPVPKELDQQSTTKASVKRPYTNAQIQIKQGKDGKEGSVGLSVQRSVFGERNFNIHSSISHESPAVKLMKQSKTVDVLSRKLATKKKAISTKVMNSAVMRKTASSCPASLTCDCYATDKVCSICLSRRQQVAPRAGTPGFRAPEVLTKCPNQTTAIDMWSAGVIFLSLLSGRYPFYKASDDLTALAQIMTIRGSRETIQAAKTFGKSILCSKEVPAQDLRKLCERLRGMDSSTPKLTSDIQGHASHQPAISEKTDHKASCLVQTPPGQYSGNSFKKGDSNSCEHCFDEYNTNLEGWNEVPDEAYDLLDKLLDLNPASRITAEEALLHPFFKDMSL TTSMTDI TT Clinical trial TTSMTDI FM Kinase TTQ5LRD ID TTQ5LRD TTQ5LRD TN Cellular inhibitor of apoptosis 1 (BIRC2) TTQ5LRD UP Q13490 TTQ5LRD UC BIRC2_HUMAN TTQ5LRD BC Acyltransferase TTQ5LRD SN hIAP2; hIAP-2; TNFR2TRAFsignaling complex protein 2; TNFR2-TRAF-signaling complex protein 2; RNF48; RING-type E3 ubiquitin transferase BIRC2; RING finger protein 48; MIHB; Inhibitor of apoptosis protein 2; IAP2; IAP homolog B; CIAP1; C-IAP1; Baculoviral IAP repeatcontaining protein 2; Baculoviral IAP repeat-containing protein 2; API1 TTQ5LRD GN BIRC2 TTQ5LRD FC Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle. Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. TTQ5LRD EC EC 2.3.2.27 TTQ5LRD PD 6HPR; 6EXW; 5M6N; 4MU7; 4MTI TTQ5LRD SQ MHKTASQRLFPGPSYQNIKSIMEDSTILSDWTNSNKQKMKYDFSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKLGDSPIQKHKQLYPSCSFIQNLVSASLGSTSKNTSPMRNSFAHSLSPTLEHSSLFSGSYSSLSPNPLNSRAVEDISSSRTNPYSYAMSTEEARFLTYHMWPLTFLSPSELARAGFYYIGPGDRVACFACGGKLSNWEPKDDAMSEHRRHFPNCPFLENSLETLRFSISNLSMQTHAARMRTFMYWPSSVPVQPEQLASAGFYYVGRNDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEFLIRMKGQEFVDEIQGRYPHLLEQLLSTSDTTGEENADPPIIHFGPGESSSEDAVMMNTPVVKSALEMGFNRDLVKQTVQSKILTTGENYKTVNDIVSALLNAEDEKREEEKEKQAEEMASDDLSLIRKNRMALFQQLTCVLPILDNLLKANVINKQEHDIIKQKTQIPLQARELIDTILVKGNAAANIFKNCLKEIDSTLYKNLFVDKNMKYIPTEDVSGLSLEEQLRRLQEERTCKVCMDKEVSVVFIPCGHLVVCQECAPSLRKCPICRGIIKGTVRTFLS TTQ5LRD TT Clinical trial TTQ5LRD FM Carbon-nitrogen ligase TTQ5LRD KE hsa04064:NF-kappa B signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa04210:Apoptosis; hsa04390:Hippo signaling pathway; hsa04510:Focal adhesion; hsa04621:NOD-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa05145:Toxoplasmosis; hsa05200:Pathways in cancer; hsa05222:Small cell lung cancer TTQ5LRD RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-5213460:RIPK1-mediated regulated necrosis; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5675482:Regulation of necroptotic cell death; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway; R-HSA-937041:IKK complex recruitment mediated by RIP1 TTIRY6K ID TTIRY6K TTIRY6K TN Cellular inhibitor of apoptosis 2 (BIRC3) TTIRY6K UP Q13489 TTIRY6K UC BIRC3_HUMAN TTIRY6K BC Acyltransferase TTIRY6K SN hIAP1; hIAP-1; TNFR2TRAFsignaling complex protein 1; TNFR2-TRAF-signaling complex protein 1; RNF49; RING-type E3 ubiquitin transferase BIRC3; RING finger protein 49; MIHC; Inhibitor of apoptosis protein 1; IAP1; IAP homolog C; CIAP2; C-IAP2; Baculoviral IAP repeatcontaining protein3; Baculoviral IAP repeat-containing protein 3; Apoptosis inhibitor 2; API2 TTIRY6K GN BIRC3 TTIRY6K FC Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. TTIRY6K EC EC 2.3.2.27 TTIRY6K PD 3M0D; 3M0A; 3EB6; 3EB5; 2UVL TTIRY6K SQ MNIVENSIFLSNLMKSANTFELKYDLSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKRGDSPTEKHKKLYPSCRFVQSLNSVNNLEATSQPTFPSSVTNSTHSLLPGTENSGYFRGSYSNSPSNPVNSRANQDFSALMRSSYHCAMNNENARLLTFQTWPLTFLSPTDLAKAGFYYIGPGDRVACFACGGKLSNWEPKDNAMSEHLRHFPKCPFIENQLQDTSRYTVSNLSMQTHAARFKTFFNWPSSVLVNPEQLASAGFYYVGNSDDVKCFCCDGGLRCWESGDDPWVQHAKWFPRCEYLIRIKGQEFIRQVQASYPHLLEQLLSTSDSPGDENAESSIIHFEPGEDHSEDAIMMNTPVINAAVEMGFSRSLVKQTVQRKILATGENYRLVNDLVLDLLNAEDEIREEERERATEEKESNDLLLIRKNRMALFQHLTCVIPILDSLLTAGIINEQEHDVIKQKTQTSLQARELIDTILVKGNIAATVFRNSLQEAEAVLYEHLFVQQDIKYIPTEDVSDLPVEEQLRRLQEERTCKVCMDKEVSIVFIPCGHLVVCKDCAPSLRKCPICRSTIKGTVRTFLS TTIRY6K TT Clinical trial TTIRY6K FM Carbon-nitrogen ligase TTIRY6K KE hsa04064:NF-kappa B signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa04210:Apoptosis; hsa04510:Focal adhesion; hsa04621:NOD-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa05145:Toxoplasmosis; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05222:Small cell lung cancer TTIRY6K RC R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-5213460:RIPK1-mediated regulated necrosis; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5675482:Regulation of necroptotic cell death; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway; R-HSA-937041:IKK complex recruitment mediated by RIP1 TTYQANR ID TTYQANR TTYQANR TN Cerebroside-sulfatase (ARSA) TTYQANR UP P15289 TTYQANR UC ARSA_HUMAN TTYQANR BC Sulfuric ester hydrolase TTYQANR SN Cerebrosidesulfatase; Arylsulfatase A component C; ASA; ARSA TTYQANR GN ARSA TTYQANR FC Hydrolyzes cerebroside sulfate. TTYQANR EC EC 3.1.6.8 TTYQANR PD 2HI8; 2AIK; 2AIJ; 1N2L; 1N2K TTYQANR SQ MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSLTAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPACCHCPDPHA TTYQANR TT Successful TTYQANR KE hsa00600:Sphingolipid metabolism; hsa04142:Lysosome TTYQANR RC R-HSA-1660662:Glycosphingolipid metabolism TT4VQZX ID TT4VQZX TT4VQZX TN Cholestenol delta-isomerase (EBP) TT4VQZX UP Q15125 TT4VQZX UC EBP_HUMAN TT4VQZX BC Intramolecular oxidoreductases TT4VQZX SN Emopamilbinding protein; EBP; Delta(8)Delta(7) sterol isomerase; D8D7 sterol isomerase; 3betahydroxysteroidDelta(8),Delta(7)isomerase TT4VQZX GN EBP TT4VQZX FC Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. TT4VQZX EC EC 5.3.3.5 TT4VQZX SQ MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN TT4VQZX TT Clinical trial TT4VQZX KE hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways TT4EB85 ID TT4EB85 TT4EB85 TN Cholesterol 24-hydroxylase (CYP46A1) TT4EB85 UP Q9Y6A2 TT4EB85 UC CP46A_HUMAN TT4EB85 BC Paired donor oxygen oxidoreductase TT4EB85 SN Cytochrome P450 46A1; CYP46; Cholesterol 24S-hydroxylase; Cholesterol 24-monooxygenase; CH24H TT4EB85 GN CYP46A1 TT4EB85 FC Primarily catalyzes the hydroxylation (with S stereochemistry) at C-24 of cholesterol side chain, triggering cholesterol diffusion out of neurons and its further degradation. By promoting constant cholesterol elimination in neurons, may activate the mevalonate pathway and coordinate the synthesis of new cholesterol and nonsterol isoprenoids involved in synaptic activity and learning. Further hydroxylates cholesterol derivatives and hormone steroids on both the ring and side chain of these molecules, converting them into active oxysterols involved in lipid signaling and biosynthesis. Acts as an epoxidase converting cholesta-5,24-dien-3beta-ol/desmosterol into (24S),25-epoxycholesterol, an abundant lipid ligand of nuclear NR1H2 and NR1H3 receptors shown to promote neurogenesis in developing brain. May also catalyze the oxidative metabolism of xenobiotics, such as clotrimazole. P450 monooxygenase that plays a major role in cholesterol homeostasis in the brain. TT4EB85 EC EC 1.14.14.25 TT4EB85 PD 4J14; 4FIA; 4ENH; 3MDV; 3MDT TT4EB85 SQ MSPGLLLLGSAVLLAFGLCCTFVHRARSRYEHIPGPPRPSFLLGHLPCFWKKDEVGGRVLQDVFLDWAKKYGPVVRVNVFHKTSVIVTSPESVKKFLMSTKYNKDSKMYRALQTVFGERLFGQGLVSECNYERWHKQRRVIDLAFSRSSLVSLMETFNEKAEQLVEILEAKADGQTPVSMQDMLTYTAMDILAKAAFGMETSMLLGAQKPLSQAVKLMLEGITASRNTLAKFLPGKRKQLREVRESIRFLRQVGRDWVQRRREALKRGEEVPADILTQILKAEEGAQDDEGLLDNFVTFFIAGHETSANHLAFTVMELSRQPEIVARLQAEVDEVIGSKRYLDFEDLGRLQYLSQVLKESLRLYPPAWGTFRLLEEETLIDGVRVPGNTPLLFSTYVMGRMDTYFEDPLTFNPDRFGPGAPKPRFTYFPFSLGHRSCIGQQFAQMEVKVVMAKLLQRLEFRLVPGQRFGLQEQATLKPLDPVLCTLRPRGWQPAPPPPPC TT4EB85 TT Clinical trial TT4EB85 FM Oxidoreductases acting on paired donors TT4EB85 KE hsa00120:Primary bile acid biosynthesis TT4EB85 RC R-HSA-211976:Endogenous sterols TTGEM5Q ID TTGEM5Q TTGEM5Q TN Ciliary neurotrophic factor (CNTF) TTGEM5Q UP P26441 TTGEM5Q UC CNTF_HUMAN TTGEM5Q BC Ciliary neurotrophic factor TTGEM5Q SN CNTF TTGEM5Q GN CNTF TTGEM5Q FC CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. TTGEM5Q PD 1CNT TTGEM5Q SQ MAFTEHSPLTPHRRDLCSRSIWLARKIRSDLTALTESYVKHQGLNKNINLDSADGMPVASTDQWSELTEAERLQENLQAYRTFHVLLARLLEDQQVHFTPTEGDFHQAIHTLLLQVAAFAYQIEELMILLEYKIPRNEADGMPINVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRFISSHQTGIPARGSHYIANNKKM TTGEM5Q TT Clinical trial TTGEM5Q KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway TTT2F9E ID TTT2F9E TTT2F9E TN Ciliary neurotrophic factor receptor alpha (CNTFR) TTT2F9E UP P26992 TTT2F9E UC CNTFR_HUMAN TTT2F9E BC Cytokine receptor TTT2F9E SN Ciliary neurotrophic factor receptor subunit alpha; CNTFR-alpha; CNTFR alpha; CNTF receptor subunit alpha TTT2F9E GN CNTFR TTT2F9E FC The alpha subunit provides the receptor specificity. Binds to CNTF. TTT2F9E PD 1UC6 TTT2F9E SQ MAAPVPWACCAVLAAAAAVVYAQRHSPQEAPHVQYERLGSDVTLPCGTANWDAAVTWRVNGTDLAPDLLNGSQLVLHGLELGHSGLYACFHRDSWHLRHQVLLHVGLPPREPVLSCRSNTYPKGFYCSWHLPTPTYIPNTFNVTVLHGSKIMVCEKDPALKNRCHIRYMHLFSTIKYKVSISVSNALGHNATAITFDEFTIVKPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQHVELSDGTAHTITDAYAGKEYIIQVAAKDNEIGTWSDWSVAAHATPWTEEPRHLTTEAQAAETTTSTTSSLAPPPTTKICDPGELGSGGGPSAPFLVSVPITLALAAAAATASSLLI TTT2F9E TT Clinical trial TTT2F9E FM Cytokine receptor TTT2F9E KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway TTRL76H ID TTRL76H TTRL76H TN Clusterin messenger RNA (Clusterin mRNA) TTRL76H UP P10909 TTRL76H UC CLUS_HUMAN TTRL76H BC mRNA target TTRL76H SN Testosteronerepressed prostate message 2 (mRNA); Testosterone-repressed prostate message 2 (mRNA); TRPM-2 (mRNA); NA1/NA2 (mRNA); Ku70binding protein 1 (mRNA); Ku70-binding protein 1 (mRNA); KUB1 (mRNA); Complementassociated protein SP40,40 (mRNA); Complement-associated protein SP-40,40 (mRNA); Complement cytolysis inhibitor (mRNA); Clusterin alpha chain (mRNA); Clusterin (mRNA); CLI (mRNA); Apolipoprotein J (mRNA); ApoJ (mRNA); Apo-J (mRNA); Agingassociated gene 4 protein (mRNA); Aging-associated gene 4 protein (mRNA); AAG4 (mRNA) TTRL76H GN CLU TTRL76H FC Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. TTRL76H SQ MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE TTRL76H TT Clinical trial TTRL76H FM mRNA target TTRL76H RC R-HSA-114608:Platelet degranulation TTJGY7A ID TTJGY7A TTJGY7A TN Complement C3 (CO3) TTJGY7A UP P01024 TTJGY7A UC CO3_HUMAN TTJGY7A BC Complement system TTJGY7A SN C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1; C3 TTJGY7A GN C3 TTJGY7A FC Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2 (PubMed:8376604, PubMed:2909530, PubMed:9059512, PubMed:10432298, PubMed:15833747, PubMed:16333141, PubMed:19615750). TTJGY7A PD 6EHG; 5O35; 5O32; 5NBQ; 5M6W TTJGY7A SQ MGPTSGPSLLLLLLTHLPLALGSPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAARRRRSVQLTEKRMDKVGKYPKELRKCCEDGMRENPMRFSCQRRTRFISLGEACKKVFLDCCNYITELRRQHARASHLGLARSNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPERLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMTEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDAKNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN TTJGY7A TT Clinical trial TTJGY7A KE hsa04145:Phagosome; hsa04610:Complement and coagulation cascades; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05150:Staphylococcus aureus infection; hsa05152:Tuberculosis; hsa05168:Herpes simplex infection; hsa05203:Viral carcinogenesis; hsa05322:Systemic lupus erythematosus TTJGY7A RC R-HSA-173736:Alternative complement activation; R-HSA-174577:Activation of C3 and C5; R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events; R-HSA-977606:Regulation of Complement cascade TT8D13I ID TT8D13I TT8D13I TN Complement factor D (CFD) TT8D13I UP P00746 TT8D13I UC CFAD_HUMAN TT8D13I BC Peptidase TT8D13I SN Properdin factor D; PFD; DF; C3 convertase activator; Adipsin TT8D13I GN CFD TT8D13I FC Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway. TT8D13I EC EC 3.4.21.46 TT8D13I PD 6QMT; 6QMR; 6FUT; 6FUJ; 6FUI TT8D13I SQ MHSWERLAVLVLLGAAACAAPPRGRILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGKVQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSGSRVCGNRKKPGIYTRVASYAAWIDSVLA TT8D13I TT Clinical trial TT8D13I KE hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection TT8D13I RC R-HSA-114608:Platelet degranulation; R-HSA-173736:Alternative complement activation TTIY658 ID TTIY658 TTIY658 TN Corticotropin-releasing factor receptor 2 (CRHR2) TTIY658 UP Q13324 TTIY658 UC CRFR2_HUMAN TTIY658 BC GPCR secretin TTIY658 SN Corticotropin-releasinghormone receptor 2; CRHR2; CRH2 receptor; CRH-R 2; CRF2; CRF-R 2 TTIY658 GN CRHR2 TTIY658 FC This is a receptor for corticotropin releasing factor. Shows high-affinity crf binding. Also binds to urocortin i, ii and iii. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. TTIY658 PD 3N96; 3N95; 3N93 TTIY658 SQ MDAALLHSLLEANCSLALAEELLLDGWGPPLDPEGPYSYCNTTLDQIGTCWPRSAAGALVERPCPEYFNGVKYNTTRNAYRECLENGTWASKINYSQCEPILDDKQRKYDLHYRIALVVNYLGHCVSVAALVAAFLLFLALRSIRCLRNVIHWNLITTFILRNVMWFLLQLVDHEVHESNEVWCRCITTIFNYFVVTNFFWMFVEGCYLHTAIVMTYSTERLRKCLFLFIGWCIPFPIIVAWAIGKLYYENEQCWFGKEPGDLVDYIYQGPIILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDDLSQIMFIYFNSFLQSFQGFFVSVFYCFFNGEVRSAVRKRWHRWQDHHSLRVPMARAMSIPTSPTRISFHSIKQTAAV TTIY658 TT Clinical trial TTIY658 KE hsa04080:Neuroactive ligand-receptor interaction TTIY658 RC R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-418555:G alpha (s) signalling events TTFRCTK ID TTFRCTK TTFRCTK TN CREB-binding protein (CREBBP) TTFRCTK UP Q92793 TTFRCTK UC CBP_HUMAN TTFRCTK BC Acyltransferase TTFRCTK SN CREBbinding protein; CBP TTFRCTK GN CREBBP TTFRCTK FC Acetylates non-histone proteins, like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway. Acetylates histones, giving a specific tag for transcriptional activation. TTFRCTK EC EC 2.3.1.48 TTFRCTK PD 6FRF; 6FR0; 6FQU; 6FQT; 6FQO TTFRCTK SQ MAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELGLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANMASLSAMGKSPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQGASSSVLAETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATGVNPQLASKQSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGTGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEMMEEDLQGASQVKEETDIAEQKSEPMEVDEKKPEVKVEVKEEEESSSNGTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIIHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETTEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVINTLPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVSMSPAGFPSVARTQPPTTVSTGKPTSQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRVNINNSMPPGRTGMGTPGSQMAPVSLNVPRPNQVSGPVMPSMPPGQWQQAPLPQQQPMPGLPRPVISMQAQAAVAGPRMPSVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQAMGGLNPQGQALNIMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQHLPLQGSSMGQMAAQMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSIDQGHLGNPEQSAMLPQLNTPSRSALSSELSLVGDTTGDTLEKFVEGL TTFRCTK TT Clinical trial TTFRCTK FM Acyltransferase TTFRCTK KE hsa04024:cAMP signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04310:Wnt signaling pathway; hsa04330:Notch signaling pathway; hsa04350:TGF-beta signaling pathway; hsa04520:Adherens junction; hsa04630:Jak-STAT signaling pathway; hsa04720:Long-term potentiation; hsa04916:Melanogenesis; hsa04919:Thyroid hormone signaling pathway; hsa04922:Glucagon signaling pathway; hsa05016:Huntington's disease; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma; hsa05215:Prostate cancer TTFRCTK RC R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-1368082:RORA activates gene expression; R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-1989781:PPARA activates gene expression; R-HSA-201722:Formation of the beta-catenin:TCF transactivating complex; R-HSA-2032785:YAP1- and WWTR1 (TAZ)-stimulated gene expression; R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2151201:Transcriptional activation of mitochondrial biogenesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP); R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-3134973:LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production; R-HSA-3214847:HATs acetylate histones; R-HSA-3371568:Attenuation phase; R-HSA-350054:Notch-HLH transcription pathway; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-400206:Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha); R-HSA-400253:Circadian Clock; R-HSA-5621575:CD209 (DC-SIGN) signaling; R-HSA-918233:TRAF3-dependent IRF activation pathway; R-HSA-933541:TRAF6 mediated IRF7 activation; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTWRN6M ID TTWRN6M TTWRN6M TN CRP messenger RNA (CRP mRNA) TTWRN6M UP P02741 TTWRN6M UC CRP_HUMAN TTWRN6M BC mRNA target TTWRN6M SN PTX1 (mRNA); C-reactive protein (mRNA) TTWRN6M GN CRP TTWRN6M FC Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. TTWRN6M PD 3PVO; 3PVN; 3L2Y; 1LJ7; 1GNH TTWRN6M SQ MEKLLCFLVLTSLSHAFGQTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP TTWRN6M TT Clinical trial TTWRN6M FM mRNA target TTN12BZ ID TTN12BZ TTN12BZ TN CTP synthase (CTPS1) TTN12BZ UP P17812 TTN12BZ UC PYRG1_HUMAN TTN12BZ BC Carbon-nitrogen ligase TTN12BZ SN Uridine triphosphate aminase; UTP:ammonia ligase (ADP-forming); UTP--ammonia ligase; Cytidine triphosphate synthetase; Cytidine 5'-triphosphate synthetase; CTPS1; CTP synthetase TTN12BZ GN CTPS1 TTN12BZ FC This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP- dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity. TTN12BZ EC EC 6.3.4.2 TTN12BZ PD 5U03; 2VO1 TTN12BZ SQ MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD TTN12BZ TT Clinical trial TTN12BZ KE hsa00240:Pyrimidine metabolism; hsa01100:Metabolic pathways TTQOVYA ID TTQOVYA TTQOVYA TN C-X-C motif chemokine 10 (CXCL10) TTQOVYA UP P02778 TTQOVYA UC CXL10_HUMAN TTQOVYA BC Cytokine: CXC chemokine TTQOVYA SN Small-inducible cytokine B10; SCYB10; IP-10; INP10; Gamma-IP10; 10 kDa interferon gamma-induced protein TTQOVYA GN CXCL10 TTQOVYA FC Pro-inflammatory cytokine that is involved in a wide variety of processes such as chemotaxis, differentiation, and activation of peripheral immune cells, regulation of cell growth, apoptosis and modulation of angiostatic effects. Plays thereby an important role during viral infections by stimulating the activation and migration of immune cells to the infected sites (By similarity). Mechanistically, binding of CXCL10 to the CXCR3 receptor activates G protein-mediated signaling and results in downstream activation of phospholipase C-dependent pathway, an increase in intracellular calcium production and actin reorganization. In turn, recruitment of activated Th1 lymphocytes occurs at sites of inflammation. Activation of the CXCL10/CXCR3 axis plays also an important role in neurons in response to brain injury for activating microglia, the resident macrophage population of the central nervous system, and directing them to the lesion site. This recruitment is an essential element for neuronal reorganization (By similarity). TTQOVYA PD 1O80; 1O7Z; 1O7Y; 1LV9 TTQOVYA SQ MNQTAILICCLIFLTLSGIQGVPLSRTVRCTCISISNQPVNPRSLEKLEIIPASQFCPRVEIIATMKKKGEKRCLNPESKAIKNLLKAVSKERSKRSP TTQOVYA TT Clinical trial TTQOVYA FM Cytokine: CXC chemokine TTQOVYA KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04668:TNF signaling pathway; hsa05164:Influenza A TTQOVYA RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTWP7HQ ID TTWP7HQ TTWP7HQ TN CYP3A4 messenger RNA (CYP3A4 mRNA) TTWP7HQ UP P08684 TTWP7HQ UC CP3A4_HUMAN TTWP7HQ BC mRNA target TTWP7HQ SN Taurochenodeoxycholate 6-alpha-hydroxylase (mRNA); Quinine 3-monooxygenase (mRNA); P450-PCN1 (mRNA); Nifedipine oxidase (mRNA); NF-25 (mRNA); HLp (mRNA); Cytochrome P450-PCN1 (mRNA); Cytochrome P450 NF-25 (mRNA); Cytochrome P450 HLp (mRNA); Cytochrome P450 3A4 (mRNA); Cytochrome P450 3A3 (mRNA); CYPIIIA4 (mRNA); CYPIIIA3 (mRNA); CYP3A3 (mRNA); Albendazole sulfoxidase (mRNA); Albendazole monooxygenase (sulfoxide-forming) (mRNA); 1,8-cineole 2-exo-monooxygenase (mRNA) TTWP7HQ GN CYP3A4 TTWP7HQ FC In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e. g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4-hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,8-cineole 2-exo-monooxygenase. The enzyme also hydroxylates etoposide. Catalyzes 4-beta-hydroxylation of cholesterol. May catalyze 25-hydroxylation of cholesterol in vitro. Catalyzes sulfoxidation of the anthelmintics albendazole and fenbendazole. Cytochromes P450 are a group of heme-thiolate monooxygenases. TTWP7HQ EC EC 1.14.14.- TTWP7HQ PD 6BDM; 6BDK; 6BDI; 6BDH; 6BD8 TTWP7HQ SQ MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVSGA TTWP7HQ TT Clinical trial TTWP7HQ FM mRNA target TTWP7HQ KE hsa00140:Steroid hormone biosynthesis; hsa00591:Linoleic acid metabolism; hsa00830:Retinol metabolism; hsa00980:Metabolism of xenobiotics by cytochrome P450; hsa00982:Drug metabolism - cytochrome P450; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways; hsa04976:Bile secretion; hsa05204:Chemical carcinogenesis TTWP7HQ RC R-HSA-211981:Xenobiotics; R-HSA-5423646:Aflatoxin activation and detoxification TTQ12RK ID TTQ12RK TTQ12RK TN Cytidine deaminase (CDA) TTQ12RK UP P32320 TTQ12RK UC CDD_HUMAN TTQ12RK BC Carbon-nitrogen hydrolase TTQ12RK SN Cytidine aminohydrolase; CDA TTQ12RK GN CDA TTQ12RK FC This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. TTQ12RK EC EC 3.5.4.5 TTQ12RK PD 1MQ0 TTQ12RK SQ MAQKRPACTLKPECVQQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMQDDFISPCGACRQVMREFGTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDLQKTQ TTQ12RK TT Clinical trial TTQ12RK KE hsa00240:Pyrimidine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways TT82UI1 ID TT82UI1 TT82UI1 TN Cytochrome P450 24 (CYP24A1) TT82UI1 UP Q07973 TT82UI1 UC CP24A_HUMAN TT82UI1 BC Paired donor oxygen oxidoreductase TT82UI1 SN Vitamin D(3) 24hydroxylase; Cytochrome P450CC24; CYP24A1; 24OHase; 1,25dihydroxyvitamin D(3) 24hydroxylase, mitochondrial TT82UI1 GN CYP24A1 TT82UI1 FC Has a role in maintaining calcium homeostasis. Catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25- hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3)). The enzyme can perform up to 6 rounds of hydroxylation of calcitriol leading to calcitroic acid. It also shows 23- hydroxylating activity leading to 1-alpha,25-dihydroxyvitamin D(3)-26,23-lactone as end product. TT82UI1 EC EC 1.14.15.16 TT82UI1 SQ MSSPISKSRSLAAFLQQLRSPRQPPRLVTSTAYTSPQPREVPVCPLTAGGETQNAAALPGPTSWPLLGSLLQILWKGGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGEVMKLDNKINEVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGTVLMLNTQVLGSSEDNFEDSSQFRPERWLQEKEKINPFAHLPFGVGKRMCIGRRLAELQLHLALCWIVRKYDIQATDNEPVEMLHSGTLVPSRELPIAFCQR TT82UI1 TT Clinical trial TT82UI1 KE hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways; hsa05206:MicroRNAs in cancer TT82UI1 RC R-HSA-196791:Vitamin D (calciferol) metabolism TTD7Q0R ID TTD7Q0R TTD7Q0R TN Cytochrome P450 26 (CYP26A1) TTD7Q0R UP O43174 TTD7Q0R UC CP26A_HUMAN TTD7Q0R BC Paired donor oxygen oxidoreductase TTD7Q0R SN Retinoic acid-metabolizing cytochrome; Retinoic acid inducible enzyme; Retinoic acid 4-hydroxylase; P450RAI; P450 retinoic acid-inactivating 1; HP450RAI; Cytochrome P450RAI; CYP26A1 TTD7Q0R GN CYP26A1 TTD7Q0R FC Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18- hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. TTD7Q0R EC EC 1.14.13.- TTD7Q0R SQ MGLPALLASALCTFVLPLLLFLAAIKLWDLYCVSGRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGSGCLSNLHDSSHKQRKKVIMRAFSREALECYVPVITEEVGSSLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPQLAGDGDSEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGMKARNLIHARIEQNIRAKICGLRASEAGQGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYPHVLQKVREELKSKGLLCKSNQDNKLDMEILEQLKYIGCVIKETLRLNPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVAEIFTNKEEFNPDRFMLPHPEDASRFSFIPFGGGLRSCVGKEFAKILLKIFTVELARHCDWQLLNGPPTMKTSPTVYPVDNLPARFTHFHGEI TTD7Q0R TT Clinical trial TTD7Q0R KE hsa00830:Retinol metabolism; hsa01100:Metabolic pathways TT1U2YM ID TT1U2YM TT1U2YM TN Cytomegalovirus DNA polymerase (CMV UL54) TT1U2YM UP P08546 TT1U2YM UC DPOL_HCMVA TT1U2YM BC DNA polymerase type-B family TT1U2YM SN UL54; DNA polymerase of Human herpesvirus 5 TT1U2YM GN CMV UL54 TT1U2YM FC Replicates viral genomic DNA in the late phase of lytic infection, producing long concatemeric DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein. TT1U2YM EC EC 2.7.7.7 TT1U2YM PD 1YYP TT1U2YM SQ MFFNPYLSGGVTGGAVAGGRRQRSQPGSAQGSGKRPPQKQFLQIVPRGVMFDGQTGLIKHKTGRLPLMFYREIKHLLSHDMVWPCPWRETLVGRVVGPIRFHTYDQTDAVLFFDSPENVSPRYRQHLVPSGNVLRFFGATEHGYSICVNVFGQRSYFYCEYSDTDRLREVIASVGELVPEPRTPYAVSVTPATKTSIYGYGTRPVPDLQCVSISNWTMARKIGEYLLEQGFPVYEVRVDPLTRLVIDRRITTFGWCSVNRYDWRQQGRASTCDIEVDCDVSDLVAVPDDSSWPRYRCLSFDIECMSGEGGFPCAEKSDDIVIQISCVCYETGGNTAVDQGIPNGNDGRGCTSEGVIFGHSGLHLFTIGTCGQVGPDVDVYEFPSEYELLLGFMLFFQRYAPAFVTGYNINSFDLKYILTRLEYLYKVDSQRFCKLPTAQGGRFFLHSPAVGFKRQYAAAFPSASHNNPASTAATKVYIAGSVVIDMYPVCMAKTNSPNYKLNTMAELYLRQRKDDLSYKDIPRCFVANAEGRAQVGRYCLQDAVLVRDLFNTINFHYEAGAIARLAKIPLRRVIFDGQQIRIYTSLLDECACRDFILPNHYSKGTTVPETNSVAVSPNAAIISTAAVPGDAGSVAAMFQMSPPLQSAPSSQDGVSPGSGSNSSSSVGVFSVGSGSSGGVGVSNDNHGAGGTAAVSYQGATVFEPEVGYYNDPVAVFDFASLYPSIIMAHNLCYSTLLVPGGEYPVDPADVYSVTLENGVTHRFVRASVRVSVLSELLNKWVSQRRAVRECMRECQDPVRRMLLDKEQMALKVTCNAFYGFTGVVNGMMPCLPIAASITRIGRDMLERTARFIKDNFSEPCFLHNFFNQEDYVVGTREGDSEESSALPEGLETSSGGSNERRVEARVIYGDTDSVFVRFRGLTPQALVARGPSLAHYVTACLFVEPVKLEFEKVFVSLMMICKKRYIGKVEGASGLSMKGVDLVRKTACEFVKGVTRDVLSLLFEDREVSEAAVRLSRLSLDEVKKYGVPRGFWRILRRLVQARDDLYLHRVRVEDLVLSSVLSKDISLYRQSNLPHIAVIKRLAARSEELPSVGDRVFYVLTAPGVRTAPQGSSDNGDSVTAGVVSRSDAIDGTDDDADGGGVEESNRRGGEPAKKRARKPPSAVCNYEVAEDPSYVREHGVPIHADKYFEQVLKAVTNVLSPVFPGGETARKDKFLHMVLPRRLHLEPAFLPYSVKAHECC TT1U2YM TT Clinical trial TTKRTP6 ID TTKRTP6 TTKRTP6 TN Cytosine deaminase (AICDA) TTKRTP6 UP Q9GZX7 TTKRTP6 UC AICDA_HUMAN TTKRTP6 BC Carbon-nitrogen hydrolase TTKRTP6 SN Activationinduced cytidine deaminase; AICDA TTKRTP6 GN AICDA TTKRTP6 FC Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation, gene conversion, and class- switch recombination in B-lymphocytes. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. TTKRTP6 EC EC 3.5.4.38 TTKRTP6 PD 5W1C; 5W0Z; 5W0U; 5W0R; 5JJ4 TTKRTP6 SQ MDSLLMNRRKFLYQFKNVRWAKGRRETYLCYVVKRRDSATSFSLDFGYLRNKNGCHVELLFLRYISDWDLDPGRCYRVTWFTSWSPCYDCARHVADFLRGNPNLSLRIFTARLYFCEDRKAEPEGLRRLHRAGVQIAIMTFKDYFYCWNTFVENHERTFKAWEGLHENSVRLSRQLRRILLPLYEVDDLRDAFRTLGL TTKRTP6 TT Clinical trial TTKRTP6 KE hsa04672:Intestinal immune network for IgA production; hsa05340:Primary immunodeficiency TTT1JVS ID TTT1JVS TTT1JVS TN Cytosolic phospholipase A2 (GIVA cPLA2) TTT1JVS UP P47712 TTT1JVS UC PA24A_HUMAN TTT1JVS BC Carboxylic ester hydrolase TTT1JVS SN Phospholipase A2 group IVA; PLA2G4; CPLA2 TTT1JVS GN PLA2G4A TTT1JVS FC Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response. Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. TTT1JVS PD 1RLW; 1CJY; 1BCI TTT1JVS SQ MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEVPFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEGLHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEELENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYRAPGVPRETEEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRRQNPSRCSVSLSNVEARRFFNKEFLSKPKA TTT1JVS TT Clinical trial TTT1JVS FM Carboxylic ester hydrolase TTT1JVS KE hsa00564:Glycerophospholipid metabolism; hsa00565:Ether lipid metabolism; hsa00590:Arachidonic acid metabolism; hsa00591:Linoleic acid metabolism; hsa00592:alpha-Linolenic acid metabolism; hsa01100:Metabolic pathways; hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04370:VEGF signaling pathway; hsa04611:Platelet activation; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04724:Glutamatergic synapse; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04912:GnRH signaling pathway; hsa04913:Ovarian steroidogenesis; hsa04921:Oxytocin signaling pathway; hsa05231:Choline metabolism in cancer TTT1JVS RC R-HSA-1482788:Acyl chain remodelling of PC; R-HSA-1482839:Acyl chain remodelling of PE; R-HSA-1482922:Acyl chain remodelling of PI; R-HSA-418592:ADP signalling through P2Y purinoceptor 1; R-HSA-432142:Platelet sensitization by LDL TT7Y3EJ ID TT7Y3EJ TT7Y3EJ TN D-amino acid oxidase (DAO) TT7Y3EJ UP P14920 TT7Y3EJ UC OXDA_HUMAN TT7Y3EJ BC CH-NH(2) donor oxidoreductase TT7Y3EJ SN Daminoacid oxidase; DAMOX; DAAO TT7Y3EJ GN DAO TT7Y3EJ FC Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids. TT7Y3EJ EC EC 1.4.3.3 TT7Y3EJ PD 5ZJA; 5ZJ9; 4QFD; 4QFC; 3ZNQ TT7Y3EJ SQ MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPNNPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPRELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVNCTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGGIFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGPSNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL TT7Y3EJ TT Clinical trial TT7Y3EJ KE hsa00260:Glycine, serine and threonine metabolism; hsa00330:Arginine and proline metabolism; hsa00472:D-Arginine and D-ornithine metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa04146:Peroxisome TTE3RAC ID TTE3RAC TTE3RAC TN Dickkopf-related protein 1 (DKK1) TTE3RAC UP O94907 TTE3RAC UC DKK1_HUMAN TTE3RAC BC Dickkopf protein TTE3RAC SN hDkk1; hDkk-1; UNQ492/PRO1008; Dkk1; Dkk-1; Dickkopfrelated protein 1; Dickkopf1; Dickkopf-1 TTE3RAC GN DKK1 TTE3RAC FC DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity. Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. TTE3RAC PD 5GJE; 5FWW; 3SOQ; 3S8V; 3S2K TTE3RAC SQ MMALGAAGATRVFVAMVAAALGGHPLLGVSATLNSVLNSNAIKNLPPPLGGAAGHPGSAVSAAPGILYPGGNKYQTIDNYQPYPCAEDEECGTDEYCASPTRGGDAGVQICLACRKRRKRCMRHAMCCPGNYCKNGICVSSDQNHFRGEIEETITESFGNDHSTLDGYSRRTTLSSKMYHTKGQEGSVCLRSSDCASGLCCARHFWSKICKPVLKEGQVCTKHRRKGSHGLEIFQRCYCGEGLSCRIQKDHHQASNSSRLHTCQRH TTE3RAC TT Clinical trial TTE3RAC FM Dickkopf family TTE3RAC KE hsa04310:Wnt signaling pathway TTE3RAC RC R-HSA-201681:TCF dependent signaling in response to WNT; R-HSA-3772470:Negative regulation of TCF-dependent signaling by WNT ligand antagonists TTCGY2K ID TTCGY2K TTCGY2K TN DNA topoisomerase II alpha (TOP2A) TTCGY2K UP P11388 TTCGY2K UC TOP2A_HUMAN TTCGY2K BC Topoisomerase TTCGY2K SN DNA topoisomerase II, alpha isozyme; DNA topoisomerase 2alpha; DNA topoisomerase 2-alpha TTCGY2K GN TOP2A TTCGY2K FC Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation. Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. TTCGY2K EC EC 5.6.2.3 TTCGY2K PD 5NNE; 5GWK; 4R1F; 4FM9; 1ZXN TTCGY2K SQ MEVSPLQPVNENMQVNKIKKNEDAKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVKGFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKNKGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQVQLNKKCSAVKHNRIKGIPKLDDANDAGGRNSTECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEMAFYSLPEFEEWKSSTPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQIDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQTTTYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSSLARLLFPPKDDHTLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREIVNNIRRLMDGEEPLPMLPSYKNFKGTIEELAPNQYVISGEVAILNSTTIEISELPVRTWTQTYKEQVLEPMLNGTEKTPPLITDYREYHTDTTVKFVVKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESAKLNNQARFILEKIDGKIIIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPDEEENEESDNEKETEKSDSVTDSGPTFNYLLDMPLWYLTKEKKDELCRLRNEKEQELDTLKRKSPSDLWKEDLATFIEELEAVEAKEKQDEQVGLPGKGGKAKGKKTQMAEVLPSPRGQRVIPRITIEMKAEAEKKNKKKIKNENTEGSPQEDGVELEGLKQRLEKKQKREPGTKTKKQTTLAFKPIKKGKKRNPWSDSESDRSSDESNFDVPPRETEPRRAATKTKFTMDLDSDEDFSDFDEKTDDEDFVPSDASPPKTKTSPKLSNKELKPQKSVVSDLEADDVKGSVPLSSSPPATHFPDETEITNPVPKKNVTVKKTAAKSQSSTSTTGAKKRAAPKGTKRDPALNSGVSQKPDPAKTKNRRKRKPSTSDDSDSNFEKIVSKAVTSKKSKGESDDFHMDFDSAVAPRAKSVRAKKPIKYLEESDEDDLF TTCGY2K TT Clinical trial TTCGY2K FM ATP-hydrolyzing DNA topoisomerase TTCGY2K RC R-HSA-1538133:G0 and Early G1 TTYIP79 ID TTYIP79 TTYIP79 TN Dopamine beta hydroxylase (DBH) TTYIP79 UP P09172 TTYIP79 UC DOPO_HUMAN TTYIP79 BC Paired donor oxygen oxidoreductase TTYIP79 SN Soluble dopamine betahydroxylase; Dopamine betamonooxygenase; Dopamine betahydroxylase; Dopamine beta-monooxygenase; Dopamine beta-hydroxylase TTYIP79 GN DBH TTYIP79 FC Conversion of dopamine to noradrenaline. TTYIP79 EC EC 1.14.17.1 TTYIP79 PD 4ZEL TTYIP79 SQ MPALSRWASLPGPSMREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQDYQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQRVQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVTKGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIVNQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNSFNRDVLKALYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCPTSQGRSPAGPTVVSIGGGKG TTYIP79 TT Clinical trial TTYIP79 FM Oxidoreductases acting on paired donors TTYIP79 KE hsa00350:Tyrosine metabolism; hsa01100:Metabolic pathways TTP7EGM ID TTP7EGM TTP7EGM TN Dual specificity protein kinase TTK (MPS1) TTP7EGM UP P33981 TTP7EGM UC TTK_HUMAN TTP7EGM BC Kinase TTP7EGM SN Tyrosine threonine kinase; Phosphotyrosine picked threonine-protein kinase; PYT; MPS1L1 TTP7EGM GN TTK TTP7EGM FC Probably associated with cell proliferation. Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint. Phosphorylates proteins on serine, threonine, and tyrosine. TTP7EGM EC EC 2.7.12.1 TTP7EGM PD 6N6O; 6H3K; 6GVJ; 6B4W; 5O91 TTP7EGM SQ MESEDLSGRELTIDSIMNKVRDIKNKFKNEDLTDELSLNKISADTTDNSGTVNQIMMMANNPEDWLSLLLKLEKNSVPLSDALLNKLIGRYSQAIEALPPDKYGQNESFARIQVRFAELKAIQEPDDARDYFQMARANCKKFAFVHISFAQFELSQGNVKKSKQLLQKAVERGAVPLEMLEIALRNLNLQKKQLLSEEEKKNLSASTVLTAQESFSGSLGHLQNRNNSCDSRGQTTKARFLYGENMPPQDAEIGYRNSLRQTNKTKQSCPFGRVPVNLLNSPDCDVKTDDSVVPCFMKRQTSRSECRDLVVPGSKPSGNDSCELRNLKSVQNSHFKEPLVSDEKSSELIITDSITLKNKTESSLLAKLEETKEYQEPEVPESNQKQWQSKRKSECINQNPAASSNHWQIPELARKVNTEQKHTTFEQPVFSVSKQSPPISTSKWFDPKSICKTPSSNTLDDYMSCFRTPVVKNDFPPACQLSTPYGQPACFQQQQHQILATPLQNLQVLASSSANECISVKGRIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENGKSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAKGTTEEMKYVLGQLVGLNSPNSILKAAKTLYEHYSGGESHNSSSSKTFEKKRGKK TTP7EGM TT Clinical trial TTP7EGM FM Kinase TTP7EGM KE hsa04110:Cell cycle TT48MP6 ID TT48MP6 TT48MP6 TN Dystrophin (DMD) TT48MP6 UP P11532 TT48MP6 UC DMD_HUMAN TT48MP6 BC Dystrophin protein TT48MP6 SN Dystrophin TT48MP6 GN DMD TT48MP6 FC Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. TT48MP6 PD 3UUN; 1EG4; 1EG3; 1DXX TT48MP6 SQ MLWWEEVEDCYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQVLPQQVSIEAIQEVEMLPRPPKVTKEEHFQLHHQMHYSQQITVSLAQGYERTSSPKPRFKSYAYTQAAYVTTSDPTRSPFPSQHLEAPEDKSFGSSLMESEVNLDRYQTALEEVLSWLLSAEDTLQAQGEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIGTGKLSEDEETEVQEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQNQKLKELNDWLTKTEERTRKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDILLKWQRLTEEQCLFSAWLSEKEDAVNKIHTTGFKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSVTQKTEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQEELPPPPPQKKRQITVDSEIRKRLDVDITELHSWITRSEAVLQSPEFAIFRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEGVNADSIKQASEQLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIALKEKGQGPMFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETKLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNEVEFKLKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVREETMMVMTEDMPLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRSVEKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPVVTKETAISKLEMPSSLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKLYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLQELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRDFGPASQHFLSTSVQGPWERAISPNKVPYYINHETQTTCWDHPKMTELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEYCTPTTSGEDVRDFAKVLKNKFRTKRYFAKHPRMGYLPVQTVLEGDNMETPVTLINFWPVDSAPASSPQLSHDDTHSRIEHYASRLAEMENSNGSYLNDSISPNESIDDEHLLIQHYCQSLNQDSPLSQPRSPAQILISLESEERGELERILADLEEENRNLQAEYDRLKQQHEHKGLSPLPSPPEMMPTSPQSPRDAELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPQAEAKVNGTTVSSPSTSLQRSDSSQPMLLRVVGSQTSDSMGEEDLLSPPQDTSTGLEEVMEQLNNSFPSSRGRNTPGKPMREDTM TT48MP6 TT Clinical trial TT48MP6 FM Zinc-finger TT48MP6 KE hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy; hsa05416:Viral myocarditis TT48MP6 RC R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-390522:Striated Muscle Contraction TTWLFXU ID TTWLFXU TTWLFXU TN Dystrophin messenger RNA (DMD mRNA) TTWLFXU UP P11532 TTWLFXU UC DMD_HUMAN TTWLFXU BC mRNA target TTWLFXU SN Dystrophin mRNA TTWLFXU GN DMD TTWLFXU FC Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. TTWLFXU PD 3UUN; 1EG4; 1EG3; 1DXX TTWLFXU SQ MLWWEEVEDCYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQVLPQQVSIEAIQEVEMLPRPPKVTKEEHFQLHHQMHYSQQITVSLAQGYERTSSPKPRFKSYAYTQAAYVTTSDPTRSPFPSQHLEAPEDKSFGSSLMESEVNLDRYQTALEEVLSWLLSAEDTLQAQGEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIGTGKLSEDEETEVQEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQNQKLKELNDWLTKTEERTRKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDILLKWQRLTEEQCLFSAWLSEKEDAVNKIHTTGFKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSVTQKTEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQEELPPPPPQKKRQITVDSEIRKRLDVDITELHSWITRSEAVLQSPEFAIFRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEGVNADSIKQASEQLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIALKEKGQGPMFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETKLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNEVEFKLKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVREETMMVMTEDMPLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRSVEKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPVVTKETAISKLEMPSSLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKLYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLQELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRDFGPASQHFLSTSVQGPWERAISPNKVPYYINHETQTTCWDHPKMTELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEYCTPTTSGEDVRDFAKVLKNKFRTKRYFAKHPRMGYLPVQTVLEGDNMETPVTLINFWPVDSAPASSPQLSHDDTHSRIEHYASRLAEMENSNGSYLNDSISPNESIDDEHLLIQHYCQSLNQDSPLSQPRSPAQILISLESEERGELERILADLEEENRNLQAEYDRLKQQHEHKGLSPLPSPPEMMPTSPQSPRDAELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPQAEAKVNGTTVSSPSTSLQRSDSSQPMLLRVVGSQTSDSMGEEDLLSPPQDTSTGLEEVMEQLNNSFPSSRGRNTPGKPMREDTM TTWLFXU TT Clinical trial TTWLFXU FM mRNA target TTWLFXU KE hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy; hsa05416:Viral myocarditis TTWLFXU RC R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-390522:Striated Muscle Contraction TT0A1R8 ID TT0A1R8 TT0A1R8 TN E2 ubiquitin-conjugating enzyme T (UBE2T) TT0A1R8 UP Q9NPD8 TT0A1R8 UC UBE2T_HUMAN TT0A1R8 BC Ubiquitin-conjugating enzyme family TT0A1R8 SN Ubiquitin-protein ligase T; Ubiquitin carrier protein T; Cell proliferation-inducing gene 50 protein TT0A1R8 GN UBE2T TT0A1R8 FC Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair. Acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway (PubMed:16916645, PubMed:17938197, PubMed:19111657, PubMed:19589784, PubMed:28437106). Also mediates monoubiquitination of FANCL and FANCI (PubMed:16916645, PubMed:17938197, PubMed:19111657, PubMed:19589784). May contribute to ubiquitination and degradation of BRCA1 (PubMed:19887602). In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination (PubMed:20061386). TT0A1R8 EC EC 2.3.2.23 TT0A1R8 PD 5OJJ; 5NGZ; 4CCG; 1YH2 TT0A1R8 SQ MQRASRLKRELHMLATEPPPGITCWQDKDQMDDLRAQILGGANTPYEKGVFKLEVIIPERYPFEPPQIRFLTPIYHPNIDSAGRICLDVLKLPPKGAWRPSLNIATVLTSIQLLMSEPNPDDPLMADISSEFKYNKPAFLKNARQWTEKHARQKQKADEEEMLDNLPEAGDSRVHNSTQKRKASQLVGIEKKFHPDV TT0A1R8 TT Clinical trial TT0A1R8 KE hsa03460:Fanconi anemia pathway TTG96HZ ID TTG96HZ TTG96HZ TN EGFR messenger RNA (EGFR mRNA) TTG96HZ UP P00533 TTG96HZ UC EGFR_HUMAN TTG96HZ BC mRNA target TTG96HZ SN Receptor tyrosine-protein kinase erbB-1 (mRNA); Proto-oncogene c-ErbB-1 (mRNA); HER1 (mRNA); Epidermal growth factor receptor (mRNA); ERBB1 (mRNA); ERBB (mRNA); EGFR (mRNA) TTG96HZ GN EGFR TTG96HZ FC Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Plays a role in enhancing learning and memory performance. TTG96HZ EC EC 2.7.10.1 TTG96HZ PD 6D8E; 6B3S; 6ARU; 5ZWJ; 5YU9 TTG96HZ SQ MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA TTG96HZ TT Clinical trial TTG96HZ FM mRNA target TTFPKXQ ID TTFPKXQ TTFPKXQ TN Endoplasmin (HSP90B1) TTFPKXQ UP P14625 TTFPKXQ UC ENPL_HUMAN TTFPKXQ BC Heat shock protein TTFPKXQ SN gp96 homolog; Tumor rejection antigen 1; TRA1; Heat shock protein 90 kDa beta member 1; GRP94; GRP-94; 94 kDa glucoseregulated protein; 94 kDa glucose-regulated protein TTFPKXQ GN HSP90B1 TTFPKXQ FC When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Molecular chaperone that functions in the processing and transport of secreted proteins. TTFPKXQ PD 4NH9 TTFPKXQ SQ MRALWVLGLCCVLLTFGSVRADDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVLDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEEETAKESTAEKDEL TTFPKXQ TT Clinical trial TTFPKXQ FM Heat shock protein TTFPKXQ KE hsa04141:Protein processing in endoplasmic reticulum; hsa04151:PI3K-Akt signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04915:Estrogen signaling pathway; hsa04918:Thyroid hormone synthesis; hsa05200:Pathways in cancer; hsa05215:Prostate cancer TTFPKXQ RC R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-3000480:Scavenging by Class A Receptors TTRJB2G ID TTRJB2G TTRJB2G TN Ephrin type-A receptor 2 (EPHA2) TTRJB2G UP P29317 TTRJB2G UC EPHA2_HUMAN TTRJB2G BC Kinase TTRJB2G SN Tyrosine-protein kinase receptor ECK; Epithelial cell kinase; EphA2receptor; ECK TTRJB2G GN EPHA2 TTRJB2G FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis. Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TTRJB2G EC EC 2.7.10.1 TTRJB2G PD 6NKP; 6NK2; 6NK1; 6NK0; 6NJZ TTRJB2G SQ MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI TTRJB2G TT Clinical trial TTRJB2G FM Kinase TTRJB2G KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04360:Axon guidance TTRJB2G RC R-HSA-2682334:EPH-Ephrin signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TTHS2LR ID TTHS2LR TTHS2LR TN Ephrin type-A receptor 3 (EPHA3) TTHS2LR UP P29320 TTHS2LR UC EPHA3_HUMAN TTHS2LR BC Kinase TTHS2LR SN hEK4; Tyrosineprotein kinase receptor ETK1; Tyrosineprotein kinase TYRO4; Tyrosine-protein kinase receptor ETK1; Tyrosine-protein kinase TYRO4; TYRO4; Human embryo kinase; HEK; Ephrin typeA receptor 3; Ephlike tyrosine kinase 1; Eph-like tyrosine kinase 1; ETK1; ETK protein; EPHlike kinase 4; EPH-like kinase 4; EK4 TTHS2LR GN EPHA3 TTHS2LR FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development. Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TTHS2LR EC EC 2.7.10.1 TTHS2LR PD 4TWO; 4TWN; 4P5Z; 4P5Q; 4P4C TTHS2LR SQ MDCQLSILLLLSCSVLDSFGELIPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCSCNAGYEERGFMCQACRPGFYKALDGNMKCAKCPPHSSTQEDGSMNCRCENNYFRADKDPPSMACTRPPSSPRNVISNINETSVILDWSWPLDTGGRKDVTFNIICKKCGWNIKQCEPCSPNVRFLPRQFGLTNTTVTVTDLLAHTNYTFEIDAVNGVSELSSPPRQFAAVSITTNQAAPSPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISSLKPDTIYVFQIRARTAAGYGTNSRKFEFETSPDSFSISGESSQVVMIAISAAVAIILLTVVIYVLIGRFCGYKSKHGADEKRLHFGNGHLKLPGLRTYVDPHTYEDPTQAVHEFAKELDATNISIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTSPEAIAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPPPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPGSLKIITSAAARPSNLLLDQSNVDITTFRTTGDWLNGVWTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETQSKNGPVPV TTHS2LR TT Clinical trial TTHS2LR KE hsa04360:Axon guidance TTHS2LR RC R-HSA-2682334:EPH-Ephrin signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TTAU4D6 ID TTAU4D6 TTAU4D6 TN E-selectin (SELE) TTAU4D6 UP P16581 TTAU4D6 UC LYAM2_HUMAN TTAU4D6 SN Leukocyte-endothelial cell adhesion molecule 2; LECAM2; Endothelial leukocyte adhesion molecule 1; ELAM1; ELAM-1; CD62E antigen; CD62E; CD62 antigen-like family member E TTAU4D6 GN SELE TTAU4D6 FC Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis. Cell-surface glycoprotein having a role in immunoadhesion. TTAU4D6 PD 6EYK; 6EYJ; 6EYI; 4CSY; 4C16 TTAU4D6 SQ MIASQFLSALTLVLLIKESGAWSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVWVWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCYTAACTNTSCSGHGECVETINNYTCKCDPGFSGLKCEQIVNCTALESPEHGSLVCSHPLGNFSYNSSCSISCDRGYLPSSMETMQCMSSGEWSAPIPACNVVECDAVTNPANGFVECFQNPGSFPWNTTCTFDCEEGFELMGAQSLQCTSSGNWDNEKPTCKAVTCRAVRQPQNGSVRCSHSPAGEFTFKSSCNFTCEEGFMLQGPAQVECTTQGQWTQQIPVCEAFQCTALSNPERGYMNCLPSASGSFRYGSSCEFSCEQGFVLKGSKRLQCGPTGEWDNEKPTCEAVRCDAVHQPPKGLVRCAHSPIGEFTYKSSCAFSCEEGFELHGSTQLECTSQGQWTEEVPSCQVVKCSSLAVPGKINMSCSGEPVFGTVCKFACPEGWTLNGSAARTCGATGHWSGLLPTCEAPTESNIPLVAGLSAAGLSLLTLAPFLLWLRKCLRKAKKFVPASSCQSLESDGSYQKPSYIL TTAU4D6 TT Clinical trial TTAU4D6 FM Selectin TTAU4D6 KE hsa04514:Cell adhesion molecules (CAMs); hsa04668:TNF signaling pathway; hsa05143:African trypanosomiasis; hsa05144:Malaria TTAU4D6 RC R-HSA-202733:Cell surface interactions at the vascular wall TTCJUR4 ID TTCJUR4 TTCJUR4 TN Exportin-1 (XPO1) TTCJUR4 UP O14980 TTCJUR4 UC XPO1_HUMAN TTCJUR4 BC Eukaryotic nuclear pore complex TTCJUR4 SN Exp1; Chromosome region maintenance 1 protein homolog; CRM1 TTCJUR4 GN XPO1 TTCJUR4 FC In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. TTCJUR4 PD 5DIS; 4BSN; 4BSM; 3GB8; 2L1L TTCJUR4 SQ MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTEKLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD TTCJUR4 TT Clinical trial TTCJUR4 FM Exportin TTCJUR4 KE hsa03008:Ribosome biogenesis in eukaryotes; hsa03013:RNA transport; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection TTCJUR4 RC R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-3769402:Deactivation of the beta-catenin transactivating complex; R-HSA-450520:HuR (ELAVL1) binds and stabilizes mRNA; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-68877:Mitotic Prometaphase; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition TT1MG9E ID TT1MG9E TT1MG9E TN Extracellular signal-regulated kinase 1 (ERK1) TT1MG9E UP P27361 TT1MG9E UC MK03_HUMAN TT1MG9E BC Kinase TT1MG9E SN PRKM3; P44-MAPK; P44-ERK1; P44 Mitogen-activated protein kinase; Mitogen-activated protein kinase 3; Microtubule-associated protein-2 kinase; Microtubule-associated protein 2 kinase; MAPK 3; MAP kinase isoform p44; MAP kinase 3; Insulin-stimulated MAP2 kinase; ERT2; ERK-1 TT1MG9E GN MAPK3 TT1MG9E FC MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. TT1MG9E EC EC 2.7.11.24 TT1MG9E PD 6GES; 4QTB; 2ZOQ TT1MG9E SQ MAAAAAQGGGGGEPRRTEGVGPGVPGEVEMVKGQPFDVGPRYTQLQYIGEGAYGMVSSAYDHVRKTRVAIKKISPFEHQTYCQRTLREIQILLRFRHENVIGIRDILRASTLEAMRDVYIVQDLMETDLYKLLKSQQLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLINTTCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINMKARNYLQSLPSKTKVAWAKLFPKSDSKALDLLDRMLTFNPNKRITVEEALAHPYLEQYYDPTDEPVAEEPFTFAMELDDLPKERLKELIFQETARFQPGVLEAP TT1MG9E TT Clinical trial TT1MG9E FM Kinase TT1MG9E KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04114:Oocyte meiosis; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04320:Dorso-ventral axis formation; hsa04350:TGF-beta signaling pathway; hsa04360:Axon guidance; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04540:Gap junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04930:Type II diabetes mellitus; hsa04960:Aldosterone-regulated sodium reabsorption; hsa05010:Alzheimer's disease; hsa05020:Prion diseases; hsa05034:Alcoholism; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TT1MG9E RC R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-112409:RAF-independent MAPK1/3 activation; R-HSA-1169408:ISG15 antiviral mechanism; R-HSA-198753:ERK/MAPK targets; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-2559585:Oncogene Induced Senescence; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-3371453:Regulation of HSF1-mediated heat shock response; R-HSA-375165:NCAM signaling for neurite out-growth; R-HSA-450341:Activation of the AP-1 family of transcription factors; R-HSA-456926:Thrombin signalling through proteinase activated receptors (PARs); R-HSA-5654726:Negative regulation of FGFR1 signaling; R-HSA-5654727:Negative regulation of FGFR2 signaling; R-HSA-5654732:Negative regulation of FGFR3 signaling; R-HSA-5654733:Negative regulation of FGFR4 signaling; R-HSA-5663213:RHO GTPases Activate WASPs and WAVEs; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5674499:Negative feedback regulation of MAPK pathway; R-HSA-5675221:Negative regulation of MAPK pathway; R-HSA-74749:Signal attenuation; R-HSA-879415:Advanced glycosylation endproduct receptor signaling; R-HSA-881907:Gastrin-CREB signalling pathway via PKC and MAPK; R-HSA-982772:Growth hormone receptor signaling TTXQKM3 ID TTXQKM3 TTXQKM3 TN Farnesyl protein transferase (Ftase) TTXQKM3 UP P49354; P49356 TTXQKM3 UC FNTA_HUMAN; FNTB_HUMAN TTXQKM3 BC Alkyl aryl transferase TTXQKM3 SN Ras proteins prenyltransferase; Protein farnesyltransferase; Ftase; CAAX farnesyltransferase TTXQKM3 GN FNTB; FNTA TTXQKM3 FC Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1prenylation and activation. TTXQKM3 SQ MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDSPSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRDPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQRYFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIGRSLQSKHSTENDSPTNVQQ TTXQKM3 TT Successful TTXQKM3 KE hsa00900:Terpenoid backbone biosynthesis; hsa01130:Biosynthesis of antibiotics TTXQKM3 RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade TT975ZT ID TT975ZT TT975ZT TN Ferritin (FTH1) TT975ZT UP P02794 TT975ZT UC FRIH_HUMAN TT975ZT BC Metal ion oxidoreductase TT975ZT SN PIG15; OK/SW-cl.84; Ferritin heavy chain; Ferritin H subunit; FTHL6; FTH; Cell proliferationinducing gene 15 protein; Cell proliferation-inducing gene 15 protein TT975ZT GN FTH1 TT975ZT FC Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney. Stores iron in a soluble, non-toxic, readily available form. TT975ZT EC EC 1.16.3.1 TT975ZT PD 6IPQ; 6IPP; 6IPO; 6IPC; 6H5I TT975ZT SQ MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES TT975ZT TT Clinical trial TT975ZT FM Metal ion oxidoreductase TT975ZT KE hsa04978:Mineral absorption TT975ZT RC R-HSA-3000480:Scavenging by Class A Receptors; R-HSA-432722:Golgi Associated Vesicle Biogenesis; R-HSA-917937:Iron uptake and transport TT5BR7T ID TT5BR7T TT5BR7T TN Fibroblast growth factor receptor 4 (FGFR4) TT5BR7T UP P22455 TT5BR7T UC FGFR4_HUMAN TT5BR7T BC Kinase TT5BR7T SN TKF; JTK2; FGFR-4; CD334 TT5BR7T GN FGFR4 TT5BR7T FC Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling. Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. TT5BR7T EC EC 2.7.10.1 TT5BR7T PD 6JPJ; 5XFJ; 5XFF; 5NWZ; 5NUD TT5BR7T SQ MRLLLALLGVLLSVPGPPVLSLEASEEVELEPCLAPSLEQQEQELTVALGQPVRLCCGRAERGGHWYKEGSRLAPAGRVRGWRGRLEIASFLPEDAGRYLCLARGSMIVLQNLTLITGDSLTSSNDDEDPKSHRDPSNRHSYPQQAPYWTHPQRMEKKLHAVPAGNTVKFRCPAAGNPTPTIRWLKDGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENAVGSIRYNYLLDVLERSPHRPILQAGLPANTTAVVGSDVELLCKVYSDAQPHIQWLKHIVINGSSFGADGFPYVQVLKTADINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVLPEEDPTWTAAAPEARYTDIILYASGSLALAVLLLLAGLYRGQALHGRHPRPPATVQKLSRFPLARQFSLESGSSGKSSSSLVRGVRLSSSGPALLAGLVSLDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVRAEAFGMDPARPDQASTVAVKMLKDNASDKDLADLVSEMEVMKLIGRHKNIINLLGVCTQEGPLYVIVECAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPVLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDNVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMDRPPHCPPELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPSGGDASSTCSSSDSVFSHDPLPLGSSSFPFGSGVQT TT5BR7T TT Clinical trial TT5BR7T FM Kinase TT5BR7T KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04810:Regulation of actin cytoskeleton TT5BR7T RC R-HSA-109704:PI3K Cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-190322:FGFR4 ligand binding and activation; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5654228:Phospholipase C-mediated cascade; R-HSA-5654712:FRS-mediated FGFR4 signaling; R-HSA-5654719:SHC-mediated cascade:FGFR4; R-HSA-5654720:PI-3K cascade:FGFR4; R-HSA-5654733:Negative regulation of FGFR4 signaling; R-HSA-5673001:RAF/MAP kinase cascade TTQ916P ID TTQ916P TTQ916P TN Fibroblast growth factor-21 (FGF21) TTQ916P UP Q9NSA1 TTQ916P UC FGF21_HUMAN TTQ916P BC Growth factor TTQ916P SN UNQ3115/PRO10196; Fibroblast growth factor 21; FGF-21 TTQ916P GN FGF21 TTQ916P FC Activity requires the presence of KLB. Stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). TTQ916P PD 5VAQ TTQ916P SQ MDSDETGFEHSGLWVSVLAGLLLGACQAHPIPDSSPLLQFGGQVRQRYLYTDDAQQTEAHLEIREDGTVGGAADQSPESLLQLKALKPGVIQILGVKTSRFLCQRPDGALYGSLHFDPEACSFRELLLEDGYNVYQSEAHGLPLHLPGNKSPHRDPAPRGPARFLPLPGLPPALPEPPGILAPQPPDVGSSDPLSMVGPSQGRSPSYAS TTQ916P TT Clinical trial TTQ916P FM Growth factor TTQ916P KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer; hsa05218:Melanoma TTQ916P RC R-HSA-428790:Facilitative Na+-independent glucose transporters; R-HSA-70153:Glucose transport TTFCJ7S ID TTFCJ7S TTFCJ7S TN G1/S-specific cyclin-D1 (CCND1) TTFCJ7S UP P24385 TTFCJ7S UC CCND1_HUMAN TTFCJ7S SN PRAD1 oncogene; PRAD1; Cyclin D1; BCL1; BCL-1 oncogene; BCL-1; B-cell lymphoma 1 protein TTFCJ7S GN CCND1 TTFCJ7S FC Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner. Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. TTFCJ7S PD 5VZU; 2W9Z; 2W9F; 2W99; 2W96 TTFCJ7S SQ MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI TTFCJ7S TT Clinical trial TTFCJ7S KE hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04310:Wnt signaling pathway; hsa04390:Hippo signaling pathway; hsa04510:Focal adhesion; hsa04630:Jak-STAT signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05161:Hepatitis B; hsa05162:Measles; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05416:Viral myocarditis TTFCJ7S RC R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-3214858:RMTs methylate histone arginines; R-HSA-69229:Ubiquitin-dependent degradation of Cyclin D1; R-HSA-69231:Cyclin D associated events in G1 TTYMKBE ID TTYMKBE TTYMKBE TN Gastric inhibitory polypeptide receptor (GIPR) TTYMKBE UP P48546 TTYMKBE UC GIPR_HUMAN TTYMKBE BC GPCR secretin TTYMKBE SN Glucosedependent insulinotropic polypeptide receptor; GIPR TTYMKBE GN GIPR TTYMKBE FC This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. TTYMKBE PD 6DKJ; 4HJ0; 2QKH TTYMKBE SQ MTTSPILQLLLRLSLCGLLLQRAETGSKGQTAGELYQRWERYRRECQETLAAAEPPSGLACNGSFDMYVCWDYAAPNATARASCPWYLPWHHHVAAGFVLRQCGSDGQWGLWRDHTQCENPEKNEAFLDQRLILERLQVMYTVGYSLSLATLLLALLILSLFRRLHCTRNYIHINLFTSFMLRAAAILSRDRLLPRPGPYLGDQALALWNQALAACRTAQIVTQYCVGANYTWLLVEGVYLHSLLVLVGGSEEGHFRYYLLLGWGAPALFVIPWVIVRYLYENTQCWERNEVKAIWWIIRTPILMTILINFLIFIRILGILLSKLRTRQMRCRDYRLRLARSTLTLVPLLGVHEVVFAPVTEEQARGALRFAKLGFEIFLSSFQGFLVSVLYCFINKEVQSEIRRGWHHCRLRRSLGEEQRQLPERAFRALPSGSGPGEVPTSRGLSSGTLPGPGNEASRELESYC TTYMKBE TT Clinical trial TTYMKBE KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTYMKBE RC R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors TTKYZA9 ID TTKYZA9 TTKYZA9 TN Gastric triacylglycerol lipase (LIPF) TTKYZA9 UP P07098 TTKYZA9 UC LIPG_HUMAN TTKYZA9 BC Carboxylic ester hydrolase TTKYZA9 SN Gastric lipase; GL TTKYZA9 GN LIPF TTKYZA9 FC An acidic lipase secreted by the gastric chief cells in the fundic mucosa in the stomach. Makes up 30% of lipid hydrolysis occurring during digestion in the human adult, TTKYZA9 EC EC 3.1.1.3 TTKYZA9 PD 1HLG TTKYZA9 SQ MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPNLIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK TTKYZA9 TT Clinical trial TTKYZA9 KE hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways; hsa04975:Fat digestion and absorption TT4LRVO ID TT4LRVO TT4LRVO TN Gastrin (GAST) TT4LRVO UP P01350 TT4LRVO UC GAST_HUMAN TT4LRVO BC Gastrin cholecystokinin TT4LRVO SN Gastrin6; GAST; G52; G34; G14 TT4LRVO GN GAST TT4LRVO FC Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine. TT4LRVO PD 5WRJ TT4LRVO SQ MQRLCVYVLIFALALAAFSEASWKPRSQQPDAPLGTGANRDLELPWLEQQGPASHHRRQLGPQGPPHLVADPSKKQGPWLEEEEEAYGWMDFGRRSAEDEN TT4LRVO TT Clinical trial TT4LRVO KE hsa04971:Gastric acid secretion TT4LRVO RC R-HSA-416476:G alpha (q) signalling events; R-HSA-881907:Gastrin-CREB signalling pathway via PKC and MAPK TTC1MVT ID TTC1MVT TTC1MVT TN Gastrin-releasing peptide receptor (GRPR) TTC1MVT UP P30550 TTC1MVT UC GRPR_HUMAN TTC1MVT BC GPCR rhodopsin TTC1MVT SN GRPR; GRP-preferring bombesin receptor; GRP-R; Bombesin/gastrin-releasing peptide receptor TTC1MVT GN GRPR TTC1MVT FC Receptor for gastrin-releasing peptide (GRP). Signals via association with G proteins that activate a phosphatidylinositol-calcium second messenger system, resulting in Akt phosphorylation. Contributes to the regulation of food intake. Contributes to the perception of prurient stimuli and transmission of itch signals in the spinal cord that promote scratching behavior, but does not play a role in the perception of pain. Contributes primarily to nonhistaminergic itch sensation. Contributes to long-term fear memory, but not normal spatial memory. TTC1MVT SQ MALNDCFLLNLEVDHFMHCNISSHSADLPVNDDWSHPGILYVIPAVYGVIILIGLIGNITLIKIFCTVKSMRNVPNLFISSLALGDLLLLITCAPVDASRYLADRWLFGRIGCKLIPFIQLTSVGVSVFTLTALSADRYKAIVRPMDIQASHALMKICLKAAFIWIISMLLAIPEAVFSDLHPFHEESTNQTFISCAPYPHSNELHPKIHSMASFLVFYVIPLSIISVYYYFIAKNLIQSAYNLPVEGNIHVKKQIESRKRLAKTVLVFVGLFAFCWLPNHVIYLYRSYHYSEVDTSMLHFVTSICARLLAFTNSCVNPFALYLLSKSFRKQFNTQLLCCQPGLIIRSHSTGRSTTCMTSLKSTNPSVATFSLINGNICHERYV TTC1MVT TT Clinical trial TTC1MVT KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTC1MVT RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTEQF1O ID TTEQF1O TTEQF1O TN Glioma pathogenesis-related protein 1 (GLIPR1) TTEQF1O UP P48060 TTEQF1O UC GLIP1_HUMAN TTEQF1O BC Cysteine-rich secretory protein TTEQF1O SN RTVP1; Protein RTVP-1; GliPR 1; GLIPR TTEQF1O GN GLIPR1 TTEQF1O FC Similarity to both the pathogenesis-related protein (PR) superfamily and the cysteine-rich secretory protein (CRISP) family TTEQF1O PD 3Q2U; 3Q2R TTEQF1O SQ MRVTLATIAWMVSFVSNYSHTANILPDIENEDFIKDCVRIHNKFRSEVKPTASDMLYMTWDPALAQIAKAWASNCQFSHNTRLKPPHKLHPNFTSLGENIWTGSVPIFSVSSAITNWYDEIQDYDFKTRICKKVCGHYTQVVWADSYKVGCAVQFCPKVSGFDALSNGAHFICNYGPGGNYPTWPYKRGATCSACPNNDKCLDNLCVNRQRDQVKRYYSVVYPGWPIYPRNRYTSLFLIVNSVILILSVIITILVQHKYPNLVLLD TTEQF1O TT Clinical trial TTEQF1O RC R-HSA-1989781:PPARA activates gene expression TT7UY6K ID TT7UY6K TT7UY6K TN Glutamate decarboxylase 2 (GAD2) TT7UY6K UP Q05329 TT7UY6K UC DCE2_HUMAN TT7UY6K BC Carbon-carbon lyase TT7UY6K SN Glutamate decarboxylase 65 kDa isoform; GAD65; GAD2; 65 kDa glutamic acid decarboxylase TT7UY6K GN GAD2 TT7UY6K FC Catalyzes the production of GABA. TT7UY6K EC EC 4.1.1.15 TT7UY6K PD 2OKK; 1ES0 TT7UY6K SQ MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGGSQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEYLYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL TT7UY6K TT Clinical trial TT7UY6K KE hsa00250:Alanine, aspartate and glutamate metabolism; hsa00410:beta-Alanine metabolism; hsa00430:Taurine and hypotaurine metabolism; hsa00650:Butanoate metabolism; hsa01100:Metabolic pathways; hsa04727:GABAergic synapse; hsa04940:Type I diabetes mellitus TTJ7YTV ID TTJ7YTV TTJ7YTV TN Glutaminyl cyclase (QPCT) TTJ7YTV UP Q16769 TTJ7YTV UC QPCT_HUMAN TTJ7YTV BC Acyltransferase TTJ7YTV SN sQC; QPCT; QC; Glutamyl cyclase; GlutaminyltRNA cyclotransferase; Glutaminylpeptide cyclotransferase; EC TTJ7YTV GN QPCT TTJ7YTV FC Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides. TTJ7YTV EC EC 2.3.2.5 TTJ7YTV PD 6GBX; 4YWY; 4YU9; 3SI0; 3PBE TTJ7YTV SQ MAGGRHRRVVGTLHLLLLVAALPWASRGVSPSASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLHL TTJ7YTV TT Clinical trial TTEXB9Z ID TTEXB9Z TTEXB9Z TN Glycinamide ribonucleotide formyltransferase (GART) TTEXB9Z UP P22102 TTEXB9Z UC PUR2_HUMAN TTEXB9Z BC Carbon-nitrogen ligase TTEXB9Z SN Trifunctional purine biosynthetic protein adenosine-3; PRGS; PGFT TTEXB9Z GN GART TTEXB9Z FC A trifunctional polypeptide. Has Phosphoribosylamineglycine ligase, Phosphoribosylglycinamide formyltransferase, AIR synthetase (FGAM cyclase) activity which is required for de novo purine biosynthesis. TTEXB9Z PD 5J9F; 4ZZ3; 4ZZ2; 4ZZ1; 4ZZ0 TTEXB9Z SQ MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQFCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAFGAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEAQALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKDVGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLPHLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTRIYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEGHLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKNLIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE TTEXB9Z TT Clinical trial TTEXB9Z KE hsa00230:Purine metabolism; hsa00670:One carbon pool by folate; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics TTEXB9Z RC R-HSA-73817:Purine ribonucleoside monophosphate biosynthesis TTHJTF7 ID TTHJTF7 TTHJTF7 TN Glycine transporter GlyT-1 (SLC6A9) TTHJTF7 UP P48067 TTHJTF7 UC SC6A9_HUMAN TTHJTF7 BC Neurotransmitter:sodium symporter TTHJTF7 SN Solute carrier family 6 member 9; Sodium- and chloride-dependent glycine transporter 1; Glycine type-1 transporter; Glycine transporter type 1; GlyT1; GlyT-1 TTHJTF7 GN SLC6A9 TTHJTF7 FC May play a role in regulation of glycine levels in NMDA receptor-mediated neurotransmission. Terminates the action of glycine by its high affinity sodium-dependent reuptake into presynaptic terminals. TTHJTF7 SQ MSGGDTRAAIARPRMAAAHGPVAPSSPEQVTLLPVQRSFFLPPFSGATPSTSLAESVLKVWHGAYNSGLLPQLMAQHSLAMAQNGAVPSEATKRDQNLKRGNWGNQIEFVLTSVGYAVGLGNVWRFPYLCYRNGGGAFMFPYFIMLIFCGIPLFFMELSFGQFASQGCLGVWRISPMFKGVGYGMMVVSTYIGIYYNVVICIAFYYFFSSMTHVLPWAYCNNPWNTHDCAGVLDASNLTNGSRPAALPSNLSHLLNHSLQRTSPSEEYWRLYVLKLSDDIGNFGEVRLPLLGCLGVSWLVVFLCLIRGVKSSGKVVYFTATFPYVVLTILFVRGVTLEGAFDGIMYYLTPQWDKILEAKVWGDAASQIFYSLGCAWGGLITMASYNKFHNNCYRDSVIISITNCATSVYAGFVIFSILGFMANHLGVDVSRVADHGPGLAFVAYPEALTLLPISPLWSLLFFFMLILLGLGTQFCLLETLVTAIVDEVGNEWILQKKTYVTLGVAVAGFLLGIPLTSQAGIYWLLLMDNYAASFSLVVISCIMCVAIMYIYGHRNYFQDIQMMLGFPPPLFFQICWRFVSPAIIFFILVFTVIQYQPITYNHYQYPGWAVAIGFLMALSSVLCIPLYAMFRLCRTDGDTLLQRLKNATKPSRDWGPALLEHRTGRYAPTIAPSPEDGFEVQPLHPDKAQIPIVGSNGSSRLQDSRI TTHJTF7 TT Clinical trial TTHJTF7 FM Neurotransmitter:sodium symporter TTHJTF7 RC R-HSA-442660:Na+/Cl- dependent neurotransmitter transporters TTSDVTR ID TTSDVTR TTSDVTR TN G-protein coupled bile acid receptor 1 (GPBAR1) TTSDVTR UP Q8TDU6 TTSDVTR UC GPBAR_HUMAN TTSDVTR BC GPCR rhodopsin TTSDVTR SN hGPCR19; hBG37; TGR5; Membrane-type receptor for bile acids; M-BAR; G-protein coupled receptor GPCR19; BG37 TTSDVTR GN GPBAR1 TTSDVTR FC Bile acid-binding induces its internalization, activation of extracellular signal-regulated kinase and intracellular cAMP production. May be involved in the suppression of macrophage functions by bile acids. Receptor for bile acid. TTSDVTR SQ MTPNSTGEVPSPIPKGALGLSLALASLIITANLLLALGIAWDRRLRSPPAGCFFLSLLLAGLLTGLALPTLPGLWNQSRRGYWSCLLVYLAPNFSFLSLLANLLLVHGERYMAVLRPLQPPGSIRLALLLTWAGPLLFASLPALGWNHWTPGANCSSQAIFPAPYLYLEVYGLLLPAVGAAAFLSVRVLATAHRQLQDICRLERAVCRDEPSALARALTWRQARAQAGAMLLFGLCWGPYVATLLLSVLAYEQRPPLGPGTLLSLLSLGSASAAAVPVAMGLGDQRYTAPWRAAAQRCLQGLWGRASRDSPGPSIAYHPSSQSSVDLDLN TTSDVTR TT Clinical trial TTSDVTR FM GPCR rhodopsin TTSDVTR RC R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418555:G alpha (s) signalling events TTEYRJ9 ID TTEYRJ9 TTEYRJ9 TN GRB2 messenger RNA (GRB2 mRNA) TTEYRJ9 UP P62993 TTEYRJ9 UC GRB2_HUMAN TTEYRJ9 BC mRNA target TTEYRJ9 SN SH2/SH3 adapter GRB2 (mRNA); Protein Ash (mRNA); Growth factor receptor-bound protein 2 (mRNA); Adapter protein GRB2 (mRNA); ASH (mRNA) TTEYRJ9 GN GRB2 TTEYRJ9 FC Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway. TTEYRJ9 PD 5CDW; 4P9Z; 4P9V; 3WA4; 3S8O TTEYRJ9 SQ MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV TTEYRJ9 TT Clinical trial TTEYRJ9 FM mRNA target TTSWPH8 ID TTSWPH8 TTSWPH8 TN Growth/differentiation factor 8 (GDF-8) TTSWPH8 UP O14793 TTSWPH8 UC GDF8_HUMAN TTSWPH8 BC Growth factor TTSWPH8 SN GDF8 TTSWPH8 GN MSTN TTSWPH8 FC Acts specifically as a negative regulator of skeletal muscle growth. TTSWPH8 PD 5NXS; 5NTU; 5F3H; 5F3B TTSWPH8 SQ MQKLQLCVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS TTSWPH8 TT Clinical trial TTSWPH8 FM Growth factor TTW2R9X ID TTW2R9X TTW2R9X TN GTPase NRas (NRAS) TTW2R9X UP P01111 TTW2R9X UC RASN_HUMAN TTW2R9X BC Small GTPase TTW2R9X SN Transforming protein N-Ras; HRAS1 TTW2R9X GN NRAS TTW2R9X FC Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. TTW2R9X PD 5UHV; 3CON; 2N9C TTW2R9X SQ MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLNSSDDGTQGCMGLPCVVM TTW2R9X TT Clinical trial TTW2R9X FM Ras family TTW2R9X RC R-HSA-112412:SOS-mediated signalling; R-HSA-1169092:Activation of RAS in B cells; R-HSA-1236382:Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1250196:SHC1 events in ERBB2 signaling; R-HSA-1250347:SHC1 events in ERBB4 signaling; R-HSA-171007:p38MAPK events; R-HSA-179812:GRB2 events in EGFR signaling; R-HSA-180336:SHC1 events in EGFR signaling; R-HSA-1963640:GRB2 events in ERBB2 signaling; R-HSA-210993:Tie2 Signaling; R-HSA-2179392:EGFR Transactivation by Gastrin; R-HSA-2424491:DAP12 signaling; R-HSA-2428933:SHC-related events triggered by IGF1R; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-375165:NCAM signaling for neurite out-growth; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-5218921:VEGFR2 mediated cell proliferation; R-HSA-5621575:CD209 (DC-SIGN) signaling; R-HSA-5637810:Constitutive Signaling by EGFRvIII; R-HSA-5654688:SHC-mediated cascade:FGFR1; R-HSA-5654693:FRS-mediated FGFR1 signaling; R-HSA-5654699:SHC-mediated cascade:FGFR2; R-HSA-5654700:FRS-mediated FGFR2 signaling; R-HSA-5654704:SHC-mediated cascade:FGFR3; R-HSA-5654706:FRS-mediated FGFR3 signaling; R-HSA-5654712:FRS-mediated FGFR4 signaling; R-HSA-5654719:SHC-mediated cascade:FGFR4; R-HSA-5658442:Regulation of RAS by GAPs; R-HSA-5673000:RAF activation; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5675221:Negative regulation of MAPK pathway; R-HSA-74751:Insulin receptor signalling cascade TTLBYH1 ID TTLBYH1 TTLBYH1 TN Guanylate cyclase soluble beta-1 (GUCY1B1) TTLBYH1 UP Q02153 TTLBYH1 UC GCYB1_HUMAN TTLBYH1 BC Phosphorus-oxygen lyase TTLBYH1 SN Soluble guanylate cyclase small subunit; Guanylate cyclase soluble subunit beta-3; Guanylate cyclase soluble subunit beta-1; GUCY1B3; GUCSB3; GUC1B3; GCS-beta-3; GCS-beta-1 TTLBYH1 GN GUCY1B1 TTLBYH1 FC Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP. TTLBYH1 EC EC 4.6.1.2 TTLBYH1 PD 5MNW; 4NI2; 3UVJ; 2WZ1 TTLBYH1 SQ MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDAEKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFLIEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRDLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKLECEDELTGTEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVLLGEQFREEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHKRPVPAKRYDNVTILFSGIVGFNAFCSKHASGEGAMKIVNLLNDLYTRFDTLTDSRKNPFVYKVETVGDKYMTVSGLPEPCIHHARSICHLALDMMEIAGQVQVDGESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLMSPENSDPQFHLEHRGPVSMKGKKEPMQVWFLSRKNTGTEETKQDDD TTLBYH1 TT Clinical trial TTLBYH1 KE hsa00230:Purine metabolism; hsa04022:cGMP-PKG signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04540:Gap junction; hsa04611:Platelet activation; hsa04713:Circadian entrainment; hsa04730:Long-term depression; hsa04921:Oxytocin signaling pathway; hsa04970:Salivary secretion TTLBYH1 RC R-HSA-392154:Nitric oxide stimulates guanylate cyclase TT4O5P0 ID TT4O5P0 TT4O5P0 TN Helodermin-preferring VIP receptor (VIPR2) TT4O5P0 UP P41587 TT4O5P0 UC VIPR2_HUMAN TT4O5P0 BC GPCR secretin TT4O5P0 SN Vasoactive intestinal polypeptide receptor 2; VPAC2; VIPR2; VIP-R-2; Pituitary adenylate cyclase-activating polypeptide typeIII receptor; PACAP-R3; PACAP-R-3; PACAP type III receptor TT4O5P0 GN VIPR2 TT4O5P0 FC This is a receptor for VIP as well as PACAP-38 and -27,the activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Can be coupled to phospholipase C. TT4O5P0 PD 2X57 TT4O5P0 SQ MRTLLPPALLTCWLLAPVNSIHPECRFHLEIQEEETKCAELLRSQTEKHKACSGVWDNITCWRPANVGETVTVPCPKVFSNFYSKAGNISKNCTSDGWSETFPDFVDACGYSDPEDESKITFYILVKAIYTLGYSVSLMSLATGSIILCLFRKLHCTRNYIHLNLFLSFILRAISVLVKDDVLYSSSGTLHCPDQPSSWVGCKLSLVFLQYCIMANFFWLLVEGLYLHTLLVAMLPPRRCFLAYLLIGWGLPTVCIGAWTAARLYLEDTGCWDTNDHSVPWWVIRIPILISIIVNFVLFISIIRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAVFPISISSKYQILFELCLGSFQGLVVAVLYCFLNSEVQCELKRKWRSRCPTPSASRDYRVCGSSFSRNGSEGALQFHRGSRAQSFLQTETSVI TT4O5P0 TT Clinical trial TT4O5P0 KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TT4O5P0 RC R-HSA-418555:G alpha (s) signalling events TTMY81X ID TTMY81X TTMY81X TN Heparin-binding growth factor 1 (FGF1) TTMY81X UP P05230 TTMY81X UC FGF1_HUMAN TTMY81X BC Growth factor TTMY81X SN HBGF-1; Fibroblast growth factor 1; FGFA; FGF-1; Endothelial cell growth factor; ECGF-beta; ECGF; Beta-endothelial cell growth factor; Acidic fibroblast growth factor; AFGF TTMY81X GN FGF1 TTMY81X FC Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1. Can induce angiogenesis. Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. TTMY81X PD 4YOL; 4XKI; 4QO3; 4QC4; 4QBV TTMY81X SQ MAEGEITTFTALTEKFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD TTMY81X TT Clinical trial TTMY81X FM Growth factor TTMY81X KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04390:Hippo signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer; hsa05218:Melanoma TTMY81X RC R-HSA-109704:PI3K Cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-190322:FGFR4 ligand binding and activation; R-HSA-190372:FGFR3c ligand binding and activation; R-HSA-190375:FGFR2c ligand binding and activation; R-HSA-190377:FGFR2b ligand binding and activation; R-HSA-2033514:FGFR3 mutant receptor activation; R-HSA-2033519:Activated point mutants of FGFR2; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5654219:Phospholipase C-mediated cascade: FGFR1; R-HSA-5654221:Phospholipase C-mediated cascade; R-HSA-5654227:Phospholipase C-mediated cascade; R-HSA-5654228:Phospholipase C-mediated cascade; R-HSA-5654688:SHC-mediated cascade:FGFR1; R-HSA-5654689:PI-3K cascade:FGFR1; R-HSA-5654693:FRS-mediated FGFR1 signaling; R-HSA-5654695:PI-3K cascade:FGFR2; R-HSA-5654699:SHC-mediated cascade:FGFR2; R-HSA-5654700:FRS-mediated FGFR2 signaling; R-HSA-5654704:SHC-mediated cascade:FGFR3; R-HSA-5654706:FRS-mediated FGFR3 signaling; R-HSA-5654710:PI-3K cascade:FGFR3; R-HSA-5654712:FRS-mediated FGFR4 signaling; R-HSA-5654719:SHC-mediated cascade:FGFR4; R-HSA-5654720:PI-3K cascade:FGFR4; R-HSA-5654726:Negative regulation of FGFR1 signaling; R-HSA-5654727:Negative regulation of FGFR2 signaling; R-HSA-5654732:Negative regulation of FGFR3 signaling; R-HSA-5654733:Negative regulation of FGFR4 signaling; R-HSA-5673001:RAF/MAP kinase cascade TTPCG5T ID TTPCG5T TTPCG5T TN Hepcidin (HAMP) TTPCG5T UP P81172 TTPCG5T UC HEPC_HUMAN TTPCG5T BC Hepcidin family TTPCG5T SN Putative liver tumor regressor; PLTR; Liverexpressed antimicrobial peptide 1; LEAP1; Hepcidin20; Hepc25; Hepc20; HAMP TTPCG5T GN HAMP TTPCG5T FC Has strong antimicrobial activity against E.coli ML35P N.cinereaand weaker against S.epidermidis, S.aureus and group b streptococcus bacteria. Active against the fungus C.albicans. No activity against P.aeruginosa (PubMed:11113131, PubMed:11034317). TTPCG5T PD 4QAE; 3H0T; 2KEF; 1M4F; 1M4E TTPCG5T SQ MALSSQIWAACLLLLLLLASLTSGSVFPQQTGQLAELQPQDRAGARASWMPMFQRRRRRDTHFPICIFCCGCCHRSKCGMCCKT TTPCG5T TT Clinical trial TTK02H8 ID TTK02H8 TTK02H8 TN Hexokinase-2 (HK2) TTK02H8 UP P52789 TTK02H8 UC HXK2_HUMAN TTK02H8 BC Hexokinase family TTK02H8 SN Muscle form hexokinase; Hexokinase type II; HK II TTK02H8 GN HK2 TTK02H8 FC cytosol, membrane, mitochondrial outer membrane, fructokinase activity, glucokinase activity, hexokinase activity, mannokinase activity, apoptotic mitochondrial changes, canonical glycolysis, cellular glucose homeostasis. TTK02H8 EC EC 2.7.1.1 TTK02H8 PD 5HG1; 5HFU; 5HEX; 2NZT TTK02H8 SQ MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIREAGQR TTK02H8 TT Clinical trial TTK02H8 KE hsa00010:Glycolysis/Gluconeogenesis; hsa00051:Fructose and mannose metabolism; hsa00052:Galactose metabolism; hsa00500:Starch and sucrose metabolism; hsa00520:Amino sugar and nucleotide sugar metabolism; hsa00524:Neomycin, kanamycin and gentamicin biosynthesis; hsa01100:Metabolic pathways; hsa01200:Carbon metabolism; hsa04066:HIF-1 signaling pathway; hsa04910:Insulin signaling pathway; hsa04930:Type II diabetes mellitus; hsa04973:Carbohydrate digestion and absorption; hsa05230:Central carbon metabolism in cancer TTSN6QU ID TTSN6QU TTSN6QU TN HIF1-alpha messenger RNA (HIF1A mRNA) TTSN6QU UP Q16665 TTSN6QU UC HIF1A_HUMAN TTSN6QU BC mRNA target TTSN6QU SN bHLHe78 (mRNA); Transcription factor HIF-1 (mRNA); PASD8 (mRNA); PAS domain-containing protein 8 (mRNA); Member of PAS protein 1 (mRNA); MOP1 (mRNA); Hypoxia-inducible transcription factor (HIF)-1 (mRNA); Hypoxia-inducible factor 1-alpha (mRNA); Hypoxia-inducible factor 1 (mRNA); Hypoxia inducible factor 1 (mRNA); HIF1-alpha (mRNA); HIF1 alpha (mRNA); HIF-1alpha (mRNA); HIF-1-alpha (mRNA); HIF-1 alpha (mRNA); Class E basic helix-loop-helix protein 78 (mRNA); Basic-helix-loop-helix-PAS protein MOP1 (mRNA); ARNT-interacting protein (mRNA); ARNT interacting protein (mRNA) TTSN6QU GN HIF1A TTSN6QU FC Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia. Functions as a master transcriptional regulator of the adaptive response to hypoxia. TTSN6QU PD 6GMR; 6GFX; 5LAS; 5LA9; 5L9V TTSN6QU SQ MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN TTSN6QU TT Clinical trial TTSN6QU FM mRNA target TTSN6QU KE hsa04066:HIF-1 signaling pathway; hsa04150:mTOR signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05211:Renal cell carcinoma; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTSN6QU RC R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-1234176:Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha; R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-400253:Circadian Clock TT4YWTO ID TT4YWTO TT4YWTO TN Histone deacetylase 3 (HDAC3) TT4YWTO UP O15379 TT4YWTO UC HDAC3_HUMAN TT4YWTO BC Carbon-nitrogen hydrolase TT4YWTO SN SMAP45; RPD32; RPD3-2; HD3 TT4YWTO GN HDAC3 TT4YWTO FC Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation. Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress. Regulates both the transcriptional activation and repression phases of the circadian clock in a deacetylase activity-independent manner. During the activation phase, promotes the accumulation of ubiquitinated ARNTL/BMAL1 at the E-boxes and during the repression phase, blocks FBXL3-mediated CRY1/2 ubiquitination and promotes the interaction of CRY1 and ARNTL/BMAL1. The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. TT4YWTO EC EC 3.5.1.98 TT4YWTO PD 4A69 TT4YWTO SQ MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI TT4YWTO TT Clinical trial TT4YWTO FM Carbon-nitrogen hydrolase TT4YWTO KE hsa04919:Thyroid hormone signaling pathway; hsa05034:Alcoholism; hsa05203:Viral carcinogenesis TTSJ542 ID TTSJ542 TTSJ542 TN Integrin alpha-2 (ITGA2) TTSJ542 UP P17301 TTSJ542 UC ITA2_HUMAN TTSJ542 BC Integrin TTSJ542 SN VLA-2 subunit alpha; VLA-2 alphachain; VLA-2; Platelet membrane glycoprotein Ia; Platelet glycoprotein Ia/IIa; Glycoprotein Ia-IIa; GPIa/IIa; GPIa; Collagen receptor; CD49b; CD49 antigen-like family member B; Adhesive platelet receptor alpha1 beta2 TTSJ542 GN ITGA2 TTSJ542 FC It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix. Integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. TTSJ542 PD 6NDH; 6NDG; 6NDF; 6NDE; 6NDD TTSJ542 SQ MGPERTGAAPLPLLLVLALSQGILNCCLAYNVGLPEAKIFSGPSSEQFGYAVQQFINPKGNWLLVGSPWSGFPENRMGDVYKCPVDLSTATCEKLNLQTSTSIPNVTEMKTNMSLGLILTRNMGTGGFLTCGPLWAQQCGNQYYTTGVCSDISPDFQLSASFSPATQPCPSLIDVVVVCDESNSIYPWDAVKNFLEKFVQGLDIGPTKTQVGLIQYANNPRVVFNLNTYKTKEEMIVATSQTSQYGGDLTNTFGAIQYARKYAYSAASGGRRSATKVMVVVTDGESHDGSMLKAVIDQCNHDNILRFGIAVLGYLNRNALDTKNLIKEIKAIASIPTERYFFNVSDEAALLEKAGTLGEQIFSIEGTVQGGDNFQMEMSQVGFSADYSSQNDILMLGAVGAFGWSGTIVQKTSHGHLIFPKQAFDQILQDRNHSSYLGYSVAAISTGESTHFVAGAPRANYTGQIVLYSVNENGNITVIQAHRGDQIGSYFGSVLCSVDVDKDTITDVLLVGAPMYMSDLKKEEGRVYLFTIKKGILGQHQFLEGPEGIENTRFGSAIAALSDINMDGFNDVIVGSPLENQNSGAVYIYNGHQGTIRTKYSQKILGSDGAFRSHLQYFGRSLDGYGDLNGDSITDVSIGAFGQVVQLWSQSIADVAIEASFTPEKITLVNKNAQIILKLCFSAKFRPTKQNNQVAIVYNITLDADGFSSRVTSRGLFKENNERCLQKNMVVNQAQSCPEHIIYIQEPSDVVNSLDLRVDISLENPGTSPALEAYSETAKVFSIPFHKDCGEDGLCISDLVLDVRQIPAAQEQPFIVSNQNKRLTFSVTLKNKRESAYNTGIVVDFSENLFFASFSLPVDGTEVTCQVAASQKSVACDVGYPALKREQQVTFTINFDFNLQNLQNQASLSFQALSESQEENKADNLVNLKIPLLYDAEIHLTRSTNINFYEISSDGNVPSIVHSFEDVGPKFIFSLKVTTGSVPVSMATVIIHIPQYTKEKNPLMYLTGVQTDKAGDISCNADINPLKIGQTSSSVSFKSENFRHTKELNCRTASCSNVTCWLKDVHMKGEYFVNVTTRIWNGTFASSTFQTVQLTAAAEINTYNPEIYVIEDNTVTIPLMIMKPDEKAEVPTGVIIGSIIAGILLLLALVAILWKLGFFKRKYEKMTKNPDEIDETTELSS TTSJ542 TT Clinical trial TTSJ542 FM Integrin TTSJ542 KE hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04611:Platelet activation; hsa04640:Hematopoietic cell lineage; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05222:Small cell lung cancer; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTSJ542 RC R-HSA-216083:Integrin cell surface interactions; R-HSA-3000157:Laminin interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-447041:CHL1 interactions; R-HSA-75892:Platelet Adhesion to exposed collagen TTMPZ7V ID TTMPZ7V TTMPZ7V TN Interleukin 13 receptor alpha-2 (IL13RA2) TTMPZ7V UP Q14627 TTMPZ7V UC I13R2_HUMAN TTMPZ7V BC Cytokine receptor TTMPZ7V SN Interleukin-13-binding protein; Interleukin-13 receptor subunit alpha-2; Interleukin-13 binding protein; IL-13RA2; IL-13R-alpha-2; IL-13R subunit alpha-2; IL-13R alpha-2 chain; IL-13 receptor subunit alpha-2; CD213a2 TTMPZ7V GN IL13RA2 TTMPZ7V FC Binds as a monomer with high affinity to interleukin-13 (IL13), but not to interleukin-4 (IL4). TTMPZ7V PD 3LB6 TTMPZ7V SQ MAFVCLAIGCLYTFLISTTFGCTSSSDTEIKVNPPQDFEIVDPGYLGYLYLQWQPPLSLDHFKECTVEYELKYRNIGSETWKTIITKNLHYKDGFDLNKGIEAKIHTLLPWQCTNGSEVQSSWAETTYWISPQGIPETKVQDMDCVYYNWQYLLCSWKPGIGVLLDTNYNLFYWYEGLDHALQCVDYIKADGQNIGCRFPYLEASDYKDFYICVNGSSENKPIRSSYFTFQLQNIVKPLPPVYLTFTRESSCEIKLKWSIPLGPIPARCFDYEIEIREDDTTLVTATVENETYTLKTTNETRQLCFVVRSKVNIYCSDDGIWSEWSDKQCWEGEDLSKKTLLRFWLPFGFILILVIFVTGLLLRKPNTYPKMIPEFFCDT TTMPZ7V TT Clinical trial TTMPZ7V KE hsa04630:Jak-STAT signaling pathway TTAWI51 ID TTAWI51 TTAWI51 TN Interleukin 7 receptor alpha (IL7R) TTAWI51 UP P16871 TTAWI51 UC IL7RA_HUMAN TTAWI51 BC Cytokine receptor TTAWI51 SN Interleukin-7 receptor subunit alpha; IL-7RA; IL-7R-alpha; IL-7R subunit alpha; IL-7R alpha chain; IL-7 receptor subunit alpha; CDw127; CD127 antigen; CD127 TTAWI51 GN IL7R TTAWI51 FC Acts as a receptor for thymic stromal lymphopoietin (TSLP). Receptor for interleukin-7. TTAWI51 PD 5J11; 3UP1; 3DI3; 3DI2 TTAWI51 SQ MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVEVKCLNFRKLQEIYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVYREGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTHVNLSSTKLTLLQRKLQPAAMYEIKVRSIPDHYFKGFWSEWSPSYYFRTPEINNSSGEMDPILLTISILSFFSVALLVILACVLWKKRIKPIVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSSSRSLDCRESGKNGPHVYQDLLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSNQEEAYVTMSSFYQNQ TTAWI51 TT Clinical trial TTAWI51 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04068:FoxO signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05340:Primary immunodeficiency TTAWI51 RC R-HSA-1266695:Interleukin-7 signaling TTPM6HI ID TTPM6HI TTPM6HI TN Interleukin-1 alpha (IL1A) TTPM6HI UP P01583 TTPM6HI UC IL1A_HUMAN TTPM6HI BC Cytokine: interleukin TTPM6HI SN IL1F1; IL-1 alpha; Hematopoietin-1 TTPM6HI GN IL1A TTPM6HI FC Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. TTPM6HI PD 5UC6; 2L5X; 2KKI; 2ILA; 1ITA TTPM6HI SQ MAKVPDMFEDLKNCYSENEEDSSSIDHLSLNQKSFYHVSYGPLHEGCMDQSVSLSISETSKTSKLTFKESMVVVATNGKVLKKRRLSLSQSITDDDLEAIANDSEEEIIKPRSAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA TTPM6HI TT Clinical trial TTPM6HI FM Interleukin TTPM6HI KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04210:Apoptosis; hsa04380:Osteoclast differentiation; hsa04640:Hematopoietic cell lineage; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04940:Type I diabetes mellitus; hsa05020:Prion diseases; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05152:Tuberculosis; hsa05162:Measles; hsa05164:Influenza A; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis; hsa05332:Graft-versus-host disease TTPM6HI RC R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-446652:Interleukin-1 signaling; R-HSA-448706:Interleukin-1 processing TTT0Q1F ID TTT0Q1F TTT0Q1F TN Interleukin-10 (IL10) TTT0Q1F UP P22301 TTT0Q1F UC IL10_HUMAN TTT0Q1F BC Cytokine: interleukin TTT0Q1F SN IL-10; Cytokine synthesis inhibitory factor; CSIF TTT0Q1F GN IL10 TTT0Q1F FC Mechanistically, IL10 binds to its heterotetrameric receptor comprising IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of STAT3. In turn, STAT3 translocates to the nucleus where it drives expression of anti-inflammatory mediators. Targets antigen-presenting cells (APCs) such as macrophages and monocytes and inhibits their release of pro-inflammatory cytokines including granulocyte-macrophage colony-stimulating factor /GM-CSF, granulocyte colony-stimulating factor/G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha. Interferes also with antigen presentation by reducing the expression of MHC-class II and co-stimulatory molecules, thereby inhibiting their ability to induce T cell activation. In addition, controls the inflammatory response of macrophages by reprogramming essential metabolic pathways including mTOR signaling. Major immune regulatory cytokine that acts on many cells of the immune system where it has profound anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. TTT0Q1F PD 2ILK; 2H24; 1Y6K; 1LK3; 1J7V TTT0Q1F SQ MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN TTT0Q1F TT Clinical trial TTT0Q1F FM Cytokine: interleukin TTT0Q1F KE hsa04060:Cytokine-cytokine receptor interaction; hsa04068:FoxO signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05150:Staphylococcus aureus infection; hsa05152:Tuberculosis; hsa05169:Epstein-Barr virus infection; hsa05310:Asthma; hsa05320:Autoimmune thyroid disease; hsa05321:Inflammatory bowel disease (IBD); hsa05322:Systemic lupus erythematosus; hsa05330:Allograft rejection TTGUYTR ID TTGUYTR TTGUYTR TN Interleukin-11 (IL11) TTGUYTR UP P20809 TTGUYTR UC IL11_HUMAN TTGUYTR BC Cytokine: interleukin TTGUYTR SN Oprelvekin; IL-11; Adipogenesis inhibitory factor; AGIF TTGUYTR GN IL11 TTGUYTR FC Promotes the proliferation of hepatocytes in response to liver damage. Binding to its receptor formed by IL6ST and either IL11RA1 or IL11RA2 activates a signaling cascade that promotes cell proliferation. Signaling leads to the activation of intracellular protein kinases and the phosphorylation of STAT3. Cytokine that stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production. TTGUYTR PD 4MHL TTGUYTR SQ MNCVCRLVLVVLSLWPDTAVAPGPPPGPPRVSPDPRAELDSTVLLTRSLLADTRQLAAQLRDKFPADGDHNLDSLPTLAMSAGALGALQLPGVLTRLRADLLSYLRHVQWLRRAGGSSLKTLEPELGTLQARLDRLLRRLQLLMSRLALPQPPPDPPAPPLAPPSSAWGGIRAAHAILGGLHLTLDWAVRGLLLLKTRL TTGUYTR TT Clinical trial TTGUYTR FM Cytokine: interleukin TTGUYTR KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05323:Rheumatoid arthritis TTNZMY2 ID TTNZMY2 TTNZMY2 TN Interleukin-20 (IL20) TTNZMY2 UP Q9NYY1 TTNZMY2 UC IL20_HUMAN TTNZMY2 BC Cytokine: interleukin TTNZMY2 SN ZCYTO10; UNQ852/PRO1801; IL-20; Four alpha helix cytokine ZCYTO10; Cytokine Zcyto10 TTNZMY2 GN IL20 TTNZMY2 FC Angiogenic and proliferative activities are antagonized by IL10. May act through STAT3. Proinflammatory and angiogenic cytokine that may be involved in epidermal function and psoriasis. TTNZMY2 PD 4DOH TTNZMY2 SQ MKASSLAFSLLSAAFYLLWTPSTGLKTLNLGSCVIATNLQEIRNGFSEIRGSVQAKDGNIDIRILRRTESLQDTKPANRCCLLRHLLRLYLDRVFKNYQTPDHYTLRKISSLANSFLTIKKDLRLCHAHMTCHCGEEAMKKYSQILSHFEKLEPQAAVVKALGELDILLQWMEETE TTNZMY2 TT Clinical trial TTNZMY2 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway TT9QEJ6 ID TT9QEJ6 TT9QEJ6 TN Interleukin-21 (IL21) TT9QEJ6 UP Q9HBE4 TT9QEJ6 UC IL21_HUMAN TT9QEJ6 BC Cytokine: interleukin TT9QEJ6 SN Za11; Interleukin21; IL-21 TT9QEJ6 GN IL21 TT9QEJ6 FC May promote the transition between innate and adaptive immunity. Induces the production of IgG(1) and IgG(3) in B-cells. May play a role in proliferation and maturation of natural killer (NK) cells in synergy with IL15. May regulate proliferation of mature B- and T-cells in response to activating stimuli. In synergy with IL15 and IL18 stimulates interferon gamma production in T-cells and NK cells. During T-cell mediated immune response may inhibit dendritic cells (DC) activation and maturation. Cytokine with immunoregulatory activity. TT9QEJ6 PD 3TGX; 2OQP TT9QEJ6 SQ MRSSPGNMERIVICLMVIFLGTLVHKSSSQGQDRHMIRMRQLIDIVDQLKNYVNDLVPEFLPAPEDVETNCEWSAFSCFQKAQLKSANTGNNERIINVSIKKLKRKPPSTNAGRRQKHRLTCPSCDSYEKKPPKEFLERFKSLLQKMIHQHLSSRTHGSEDS TT9QEJ6 TT Clinical trial TT9QEJ6 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa05321:Inflammatory bowel disease (IBD) TTLDX4N ID TTLDX4N TTLDX4N TN Interleukin-22 (IL22) TTLDX4N UP Q9GZX6 TTLDX4N UC IL22_HUMAN TTLDX4N BC Cytokine: interleukin TTLDX4N SN ZCYTO18; UNQ3099/PRO10096; Interleukin22; ILTIF; IL10related Tcellderivedinducible factor; IL-TIF; IL-22; IL-10-related T-cell-derived-inducible factor; Cytokine Zcyto18 TTLDX4N GN IL22 TTLDX4N FC Cytokine that contributes to the inflammatory response in vivo. TTLDX4N PD 3Q1S; 3G9V; 3DLQ; 3DGC; 1YKB TTLDX4N SQ MAALQKSVSSFLMGTLATSCLLLLALLVQGGAAAPISSHCRLDKSNFQQPYITNRTFMLAKEASLADNNTDVRLIGEKLFHGVSMSERCYLMKQVLNFTLEEVLFPQSDRFQPYMQEVVPFLARLSNRLSTCHIEGDDLHIQRNVQKLKDTVKKLGESGEIKAIGELDLLFMSLRNACI TTLDX4N TT Clinical trial TTM624L ID TTM624L TTM624L TN Interleukin-29 (IL29) TTM624L UP Q8IU54 TTM624L UC IFNL1_HUMAN TTM624L BC Cytokine: interleukin TTM624L SN ZCYTO21; Interleukin29; Interferon lambda1; Interferon lambda-1; IL-29; IFNlambda1; IFN-lambda-1; Cytokine Zcyto21 TTM624L GN IFNL1 TTM624L FC Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression. Cytokine with antiviral, antitumour and immunomodulatory activities. TTM624L PD 3OG6; 3OG4 TTM624L SQ MAAAWTVVLVTLVLGLAVAGPVPTSKPTTTGKGCHIGRFKSLSPQELASFKKARDALEESLKLKNWSCSSPVFPGNWDLRLLQVRERPVALEAELALTLKVLEAAAGPALEDVLDQPLHTLHHILSQLQACIQPQPTAGPRPRGRLHHWLHRLQEAPKKESAGCLEASVTFNLFRLLTRDLKYVADGNLCLRTSTHPEST TTM624L TT Clinical trial TTM624L KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway TT5MD4P ID TT5MD4P TT5MD4P TN Interleukin-33 (IL33) TT5MD4P UP O95760 TT5MD4P UC IL33_HUMAN TT5MD4P BC Cytokine: interleukin TT5MD4P SN Nuclear factor from high endothelial venules; NFHEV; NF-HEV; Interleukin1 family member 11; Interleukin-1 family member 11; IL1F11; IL-33; IL-1F11; C9orf26 TT5MD4P GN IL33 TT5MD4P FC Involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines. Also involved in activation of mast cells, basophils, eosinophils and natural killer cells. Acts as a chemoattractant for Th2 cells, and may function as an "alarmin", that amplifies immune responses during tissue injury. Cytokine that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells. TT5MD4P PD 4KC3; 2KLL TT5MD4P SQ MKPKMKYSTNKISTAKWKNTASKALCFKLGKSQQKAKEVCPMYFMKLRSGLMIKKEACYFRRETTKRPSLKTGRKHKRHLVLAACQQQSTVECFAFGISGVQKYTRALHDSSITGISPITEYLASLSTYNDQSITFALEDESYEIYVEDLKKDEKKDKVLLSYYESQHPSNESGDGVDGKMLMVTLSPTKDFWLHANNKEHSVELHKCEKPLPDQAFFVLHNMHSNCVSFECKTDPGVFIGVKDNHLALIKVDSSENLCTENILFKLSET TT5MD4P TT Clinical trial TT5MD4P KE hsa04623:Cytosolic DNA-sensing pathway; hsa05164:Influenza A TT8FRMO ID TT8FRMO TT8FRMO TN Interleukin-7 (IL7) TT8FRMO UP P13232 TT8FRMO UC IL7_HUMAN TT8FRMO BC Cytokine: interleukin TT8FRMO SN Interleukin7; IL-7 TT8FRMO GN IL7 TT8FRMO FC It is important for proliferation during certain stages of B-cell maturation. Hematopoietic growth factor capable of stimulating the proliferation of lymphoid progenitors. TT8FRMO PD 3DI3; 3DI2; 1IL7 TT8FRMO SQ MFHVSFRYIFGLPPLILVLLPVASSDCDIEGKDGKQYESVLMVSIDQLLDSMKEIGSNCLNNEFNFFKRHICDANKEGMFLFRAARKLRQFLKMNSTGDFDLHLLKVSEGTTILLNCTGQVKGRKPAALGEAQPTKSLEENKSLKEQKKLNDLCFLKRLLQEIKTCWNKILMGTKEH TT8FRMO TT Clinical trial TT8FRMO FM Interleukin receptor family TT8FRMO KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage TT8FRMO RC R-HSA-1266695:Interleukin-7 signaling TT0JTFD ID TT0JTFD TT0JTFD TN Interleukin-9 (IL9) TT0JTFD UP P15248 TT0JTFD UC IL9_HUMAN TT0JTFD BC Cytokine: interleukin TT0JTFD SN T-cell growth factor P40; P40 cytokine; IL-9; Cytokine P40 TT0JTFD GN IL9 TT0JTFD FC Supports IL-2 independent and IL-4 independent growth of helper T-cells. TT0JTFD SQ MLLAMVLTSALLLCSVAGQGCPTLAGILDINFLINKMQEDPASKCHCSANVTSCLCLGIPSDNCTRPCFSERLSQMTNTTMQTRYPLIFSRVKKSVEVLKNNKCPYFSCEQPCNQTTAGNALTFLKSLLEIFQKEKMRGMRGKI TT0JTFD TT Clinical trial TT0JTFD KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa05310:Asthma TTJMF9P ID TTJMF9P TTJMF9P TN ITGA4 messenger RNA (ITGA4 mRNA) TTJMF9P UP P13612 TTJMF9P UC ITA4_HUMAN TTJMF9P BC mRNA target TTJMF9P SN VLA4 subunit alpha (mRNA); VLA-4 subunit alpha (mRNA); Integrin alphaIV (mRNA); Integrin alpha4 (mRNA); Integrin alpha-IV (mRNA); Integrin alpha-4 (mRNA); CD49d (mRNA); CD49 antigenlike family member D (mRNA); CD49 antigen-like family member D (mRNA) TTJMF9P GN ITGA4 TTJMF9P FC Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. TTJMF9P PD 5FPI; 5C7Z; 4HKC; 3V4V; 3V4P TTJMF9P SQ MAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD TTJMF9P TT Clinical trial TTJMF9P FM mRNA target TTJMF9P KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04514:Cell adhesion molecules (CAMs); hsa04640:Hematopoietic cell lineage; hsa04670:Leukocyte transendothelial migration; hsa04672:Intestinal immune network for IgA production; hsa04810:Regulation of actin cytoskeleton; hsa05140:Leishmaniasis; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTJMF9P RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-216083:Integrin cell surface interactions TTV1AG6 ID TTV1AG6 TTV1AG6 TN Kidney-type arginase (ARG2) TTV1AG6 UP P78540 TTV1AG6 UC ARGI2_HUMAN TTV1AG6 BC Carbon-nitrogen hydrolase TTV1AG6 SN Non-hepatic arginase; Human penile arginase; Arginase II; ARG2 TTV1AG6 GN ARG2 TTV1AG6 FC May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, arginase II plays a role in both male and female sexual arousal. It is therefore a potential target for the treatment of male and female sexual arousal disorders. TTV1AG6 EC EC 3.5.3.1 TTV1AG6 PD 4IXV; 4IXU; 4IE3; 4IE2; 4I06 TTV1AG6 SQ MSLRGSLSRLLQTRVHSILKKSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSFTPVPKDDLYNNLIVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDHSLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQDKVPQLPGFSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIGKRQRPIHLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSFGQTREGGHIVYDQLPTPSSPDESENQARVRI TTV1AG6 TT Clinical trial TTV1AG6 KE hsa00330:Arginine and proline metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01230:Biosynthesis of amino acids; hsa05146:Amoebiasis TTBGTCW ID TTBGTCW TTBGTCW TN Kinesin spindle messenger RNA (KIF11 mRNA) TTBGTCW UP P52732 TTBGTCW UC KIF11_HUMAN TTBGTCW BC mRNA target TTBGTCW SN Thyroid receptor-interacting protein 5 (mRNA); TRIP5 (mRNA); TRIP-5 (mRNA); TR-interacting protein 5 (mRNA); Kinesin-related motor protein Eg5 (mRNA); Kinesin-like spindle protein HKSP (mRNA); Kinesin-like protein KIF11 (mRNA); Kinesin-like protein 1 (mRNA); KNSL1 (mRNA); EG5 (mRNA) TTBGTCW GN KIF11 TTBGTCW FC Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface. Motor protein required for establishing a bipolar spindle during mitosis. TTBGTCW PD 6G6Z; 6G6Y; 5ZO9; 5ZO8; 5ZO7 TTBGTCW SQ MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKSSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNILNKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIVELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEYITSALESTEEKLHDAASKLLNTVEETTKDVSGLHSKLDRKKAVDQHNAEAQDIFGKNLNSLFNNMEELIKDGSSKQKAMLEVHKTLFGNLLSSSVSALDTITTVALGSLTSIPENVSTHVSQIFNMILKEQSLAAESKTVLQELINVLKTDLLSSLEMILSPTVVSILKINSQLKHIFKTSLTVADKIEDQKKELDGFLSILCNNLHELQENTICSLVESQKQCGNLTEDLKTIKQTHSQELCKLMNLWTERFCALEEKCENIQKPLSSVQENIQQKSKDIVNKMTFHSQKFCADSDGFSQELRNFNQEGTKLVEESVKHSDKLNGNLEKISQETEQRCESLNTRTVYFSEQWVSSLNEREQELHNLLEVVSQCCEASSSDITEKSDGRKAAHEKQHNIFLDQMTIDEDKLIAQNLELNETIKIGLTKLNCFLEQDLKLDIPTGTTPQRKSYLYPSTLVRTEPREHLLDQLKRKQPELLMMLNCSENNKEETIPDVDVEEAVLGQYTEEPLSQEPSVDAGVDCSSIGGVPFFQHKKSHGKDKENRGINTLERSKVEETTEHLVTKSRLPLRAQINL TTBGTCW TT Clinical trial TTBGTCW FM mRNA target TTBGTCW RC R-HSA-2132295:MHC class II antigen presentation; R-HSA-983189:Kinesins TTSZDQU ID TTSZDQU TTSZDQU TN Lactotransferrin (LTF) TTSZDQU UP P02788 TTSZDQU UC TRFL_HUMAN TTSZDQU BC Transferrin TTSZDQU SN Talalactoferrin; Lactoferrin; LF; Growth-inhibiting protein 12; GIG12 TTSZDQU GN LTF TTSZDQU FC Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. TTSZDQU EC EC 3.4.21.- TTSZDQU PD 2PMS; 2HD4; 2GMD; 2GMC; 2DP4 TTSZDQU SQ MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK TTSZDQU TT Clinical trial TTSZDQU FM Peptidase TTSZDQU RC R-HSA-1222556:ROS production in response to bacteria; R-HSA-977225:Amyloid formation TT67TDP ID TT67TDP TT67TDP TN Lanosterol 14-alpha demethylase (CYP51A1) TT67TDP UP Q16850 TT67TDP UC CP51A_HUMAN TT67TDP BC Cytochrome P450 family TT67TDP SN Cytochrome P450LI; Cytochrome P45014DM; Cytochrome P450-14DM; Cytochrome P450 51A1 TT67TDP GN CYP51A1 TT67TDP FC Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. TT67TDP EC EC 1.14.14.154 TT67TDP PD 4UHL; 4UHI; 3LD6; 3JUV; 3JUS TT67TDP SQ MLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQLPAGVKSPPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETKEYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWLLPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDLNLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFPTVNYTTMIHTPENPVIRYKRRSK TT67TDP TT Clinical trial TT67TDP KE hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways TTGZ91P ID TTGZ91P TTGZ91P TN Lecithin-cholesterol acyltransferase (LCAT) TTGZ91P UP P04180 TTGZ91P UC LCAT_HUMAN TTGZ91P BC Acyltransferase TTGZ91P SN Phospholipidcholesterolacyltransferase; Phospholipid-cholesterol acyltransferase; Phosphatidylcholinesterol acyltransferase; Phosphatidylcholine-sterol acyltransferase TTGZ91P GN LCAT TTGZ91P FC Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs). The cholesterol ester is then transported back to the liver. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines. Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms. Central enzyme in the extracellular metabolism of plasma lipoproteins. TTGZ91P EC EC 2.3.1.43 TTGZ91P PD 6MVD; 5TXF; 5BV7; 4XX1; 4XWG TTGZ91P SQ MGPPGSPWQWVTLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDPVGVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLGAYRQGPPASPTASPEPPPPE TTGZ91P TT Clinical trial TTGZ91P FM Acyltransferase TTGZ91P KE hsa00564:Glycerophospholipid metabolism TTGZ91P RC R-HSA-194223:HDL-mediated lipid transport TTPTWV5 ID TTPTWV5 TTPTWV5 TN Legumain (LGMN) TTPTWV5 UP Q99538 TTPTWV5 UC LGMN_HUMAN TTPTWV5 BC Peptidase TTPTWV5 SN Protease, cysteine 1; PRSC1; Asparaginyl endopeptidase TTPTWV5 GN LGMN TTPTWV5 FC Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. Has a strict specificity for hydrolysis of asparaginyl bonds. TTPTWV5 EC EC 3.4.22.34 TTPTWV5 PD 5LUB; 5LUA; 5LU9; 5LU8; 4N6O TTPTWV5 SQ MVWKVAVFLSVALGIGAVPIDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIVVMMYDDIAYSEDNPTPGIVINRPNGTDVYQGVPKDYTGEDVTPQNFLAVLRGDAEAVKGIGSGKVLKSGPQDHVFIYFTDHGSTGILVFPNEDLHVKDLNETIHYMYKHKMYRKMVFYIEACESGSMMNHLPDNINVYATTAANPRESSYACYYDEKRSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKTISTMKVMQFQGMKRKASSPVPLPPVTHLDLTPSPDVPLTIMKRKLMNTNDLEESRQLTEEIQRHLDARHLIEKSVRKIVSLLAASEAEVEQLLSERAPLTGHSCYPEALLHFRTHCFNWHSPTYEYALRHLYVLVNLCEKPYPLHRIKLSMDHVCLGHY TTPTWV5 TT Clinical trial TTPTWV5 FM Peptidase TTPTWV5 KE hsa04142:Lysosome; hsa04612:Antigen processing and presentation TTPTWV5 RC R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-196791:Vitamin D (calciferol) metabolism; R-HSA-2132295:MHC class II antigen presentation TTZYQ80 ID TTZYQ80 TTZYQ80 TN Leucine-rich repeat neuronal protein 1 (LINGO1) TTZYQ80 UP Q96FE5 TTZYQ80 UC LIGO1_HUMAN TTZYQ80 BC Immunoglobulin TTZYQ80 SN Leucinerich repeat neuronal protein 6A; Leucinerich repeat and immunoglobulinlike domaincontaining nogo receptorinteracting protein 1; Leucinerich repeat and immunoglobulin domaincontaining protein 1; LINGO1 TTZYQ80 GN LINGO1 TTZYQ80 FC Functional component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. Is also an important negative regulator of oligodentrocyte differentiation and axonal myelination. Acts in conjunction with RTN4 and RTN4R in regulating neuronal precursor cell motility during cortical development. {ECO:0000250}. TTZYQ80 PD 4OQT; 2ID5 TTZYQ80 SQ MQVSKRMLAGGVRSMPSPLLACWQPILLLVLGSVLSGSATGCPPRCECSAQDRAVLCHRKRFVAVPEGIPTETRLLDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRLKLIPLGVFTGLSNLTKLDISENKIVILLDYMFQDLYNLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLTSIPTEALSHLHGLIVLRLRHLNINAIRDYSFKRLYRLKVLEISHWPYLDTMTPNCLYGLNLTSLSITHCNLTAVPYLAVRHLVYLRFLNLSYNPISTIEGSMLHELLRLQEIQLVGGQLAVVEPYAFRGLNYLRVLNVSGNQLTTLEESVFHSVGNLETLILDSNPLACDCRLLWVFRRRWRLNFNRQQPTCATPEFVQGKEFKDFPDVLLPNYFTCRRARIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHVRSYSPDWPHQPNKTFAFISNQPGEGEANSTRATVPFPFDIKTLIIATTMGFISFLGVVLFCLVLLFLWSRGKGNTKHNIEIEYVPRKSDAGISSADAPRKFNMKMI TTZYQ80 TT Clinical trial TTZYQ80 RC R-HSA-193634:Axonal growth inhibition (RHOA activation) TTN53ZF ID TTN53ZF TTN53ZF TN Leukotriene B4 receptor 1 (LTB4R) TTN53ZF UP Q15722 TTN53ZF UC LT4R1_HUMAN TTN53ZF BC GPCR rhodopsin TTN53ZF SN P2Y7; P2Y purinoceptor 7; P2RY7; Leukotriene B(4) receptor BLT1; LTB4-R1; LTB4-R 1; LTB4-R; GPR16; G-protein coupled receptor 16; Chemoattractant receptor-like 1; CMKRL1; BLTR; BLT1; BLT TTN53ZF GN LTB4R TTN53ZF FC The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. May be the cardiac P2Y receptor involved in the regulation of cardiac muscle contraction through modulation of L-type calcium currents. Is a receptor for leukotriene B4, a potent chemoattractant involved in inflammation and immune response. Receptor for extracellular ATP > UTP and ADP. TTN53ZF SQ MNTTSSAAPPSLGVEFISLLAIILLSVALAVGLPGNSFVVWSILKRMQKRSVTALMVLNLALADLAVLLTAPFFLHFLAQGTWSFGLAGCRLCHYVCGVSMYASVLLITAMSLDRSLAVARPFVSQKLRTKAMARRVLAGIWVLSFLLATPVLAYRTVVPWKTNMSLCFPRYPSEGHRAFHLIFEAVTGFLLPFLAVVASYSDIGRRLQARRFRRSRRTGRLVVLIILTFAAFWLPYHVVNLAEAGRALAGQAAGLGLVGKRLSLARNVLIALAFLSSSVNPVLYACAGGGLLRSAGVGFVAKLLEGTGSEASSTRRGGSLGQTARSGPAALEPGPSESLTASSPLKLNELN TTN53ZF TT Clinical trial TTN53ZF FM GPCR rhodopsin TTN53ZF KE hsa04080:Neuroactive ligand-receptor interaction TTN53ZF RC R-HSA-391906:Leukotriene receptors; R-HSA-416476:G alpha (q) signalling events TT2IYXF ID TT2IYXF TT2IYXF TN L-selectin (SELL) TT2IYXF UP P14151 TT2IYXF UC LYAM1_HUMAN TT2IYXF SN TQ1; SELL; Lymph node homing receptor; Leukocyte-endothelial cell adhesion molecule 1; Leukocyte surface antigen Leu-8; Leukocyte adhesion molecule-1; LECAM1; LAM-1; Gp90-MEL; CD62L TT2IYXF GN SELL TT2IYXF FC Cell surface adhesion protein. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia. TT2IYXF PD 5VC1; 3CFW; 2LGF; 1KJB TT2IYXF SQ MIFPWKCQSTQRDLWNIFKLWGWTMLCCDFLAHHGTDCWTYHYSEKPMNWQRARRFCRDNYTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPNNKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALCYTASCQPWSCSGHGECVEIINNYTCNCDVGYYGPQCQFVIQCEPLEAPELGTMDCTHPLGNFSFSSQCAFSCSEGTNLTGIEETTCGPFGNWSSPEPTCQVIQCEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKKTICESSGIWSNPSPICQKLDKSFSMIKEGDYNPLFIPVAVMVTAFSGLAFIIWLARRLKKGKKSKRSMNDPY TT2IYXF TT Clinical trial TT2IYXF KE hsa04514:Cell adhesion molecules (CAMs) TT2IYXF RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202733:Cell surface interactions at the vascular wall TTCH6MU ID TTCH6MU TTCH6MU TN Lymphocyte IgE receptor (CD23) TTCH6MU UP P06734 TTCH6MU UC FCER2_HUMAN TTCH6MU BC Immunoglobulin TTCH6MU SN Low affinity immunoglobulin epsilon Fc receptor soluble form; Low affinity immunoglobulin epsilon Fc receptor; Immunoglobulin Ebinding factor; FcepsilonRII; FCER2; Ctype lectin domain family 4 member J; CD23; BLAST2 TTCH6MU GN FCER2 TTCH6MU FC Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen). TTCH6MU PD 5LGK; 4KI1; 4J6Q; 4J6P; 4J6N TTCH6MU SQ MEEGQYSEIEELPRRRCCRRGTQIVLLGLVTAALWAGLLTLLLLWHWDTTQSLKQLEERAARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQELNERNEASDLLERLREEVTKLRMELQVSSGFVCNTCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATCTPPASEGSAESMGPDSRPDPDGRLPTPSAPLHS TTCH6MU TT Clinical trial TTCH6MU KE hsa04640:Hematopoietic cell lineage; hsa05169:Epstein-Barr virus infection TTCH6MU RC R-HSA-2197563:NOTCH2 intracellular domain regulates transcription TTFO0PM ID TTFO0PM TTFO0PM TN Lymphotoxin beta receptor (LTBR) TTFO0PM UP P36941 TTFO0PM UC TNR3_HUMAN TTFO0PM BC Cytokine receptor TTFO0PM SN Tumor necrosis factor receptor type III; Tumor necrosis factor receptor superfamily member 3; Tumor necrosis factor receptor 2-related protein; Tumor necrosis factor C receptor; TNFRSF3; TNFR3; TNFR-III; TNFCR; TNF-RIII; Lymphotoxin-beta receptor; D12S370 TTFO0PM GN LTBR TTFO0PM FC Promotes apoptosis via TRAF3 and TRAF5. May play a role in the development of lymphoid organs. Receptor for the heterotrimeric lymphotoxin containing LTA and LTB, and for TNFS14/LIGHT. TTFO0PM PD 4MXW; 1RF3 TTFO0PM SQ MLLPWATSAPGLAWGPLVLGLFGLLAASQPQAVPPYASENQTCRDQEKEYYEPQHRICCSRCPPGTYVSAKCSRIRDTVCATCAENSYNEHWNYLTICQLCRPCDPVMGLEEIAPCTSKRKTQCRCQPGMFCAAWALECTHCELLSDCPPGTEAELKDEVGKGNNHCVPCKAGHFQNTSSPSARCQPHTRCENQGLVEAAPGTAQSDTTCKNPLEPLPPEMSGTMLMLAVLLPLAFFLLLATVFSCIWKSHPSLCRKLGSLLKRRPQGEGPNPVAGSWEPPKAHPYFPDLVQPLLPISGDVSPVSTGLPAAPVLEAGVPQQQSPLDLTREPQLEPGEQSQVAHGTNGIHVTGGSMTITGNIYIYNGPVLGGPPGPGDLPATPEPPYPIPEEGDPGPPGLSTPHQEDGKAWHLAETEHCGATPSNRGPRNQFITHD TTFO0PM TT Clinical trial TTFO0PM FM Cytokine receptor TTFO0PM KE hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05166:HTLV-I infection; hsa05203:Viral carcinogenesis TTFO0PM RC R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway TTP73TM ID TTP73TM TTP73TM TN Lymphotoxin-alpha (LTA) TTP73TM UP P01374 TTP73TM UC TNFB_HUMAN TTP73TM BC Cytokine: tumor necrosis factor TTP73TM SN Tumor necrosis factor ligand superfamily member 1; TNFSF1; TNFB; TNF-beta; LT-alpha TTP73TM GN LTA TTP73TM FC In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo. Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM. TTP73TM PD 4MXW; 4MXV; 1TNR TTP73TM SQ MTPPERLFLPRVCGTTLHLLLLGLLLVLLPGAQGLPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL TTP73TM TT Clinical trial TTP73TM FM Cytokine: tumor necrosis factor TTP73TM KE hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04668:TNF signaling pathway; hsa04940:Type I diabetes mellitus; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection TTP73TM RC R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5669034:TNFs bind their physiological receptors; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway TT0IQER ID TT0IQER TT0IQER TN Macrophage colony-stimulating factor 1 (CSF1) TT0IQER UP P09603 TT0IQER UC CSF1_HUMAN TT0IQER SN Processed macrophagecolony-stimulating factor 1; MCSF; M-CSF; Lanimostim; CSF-1 TT0IQER GN CSF1 TT0IQER FC Promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance. Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. TT0IQER PD 5LXF; 4WRM; 4WRL; 4FA8; 4ADF TT0IQER SQ MTAPGAAGRCPPTTWLGSLLLLVCLLASRSITEEVSEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQELSLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQDVVTKPDCNCLYPKAIPSSDPASVSPHQPLAPSMAPVAGLTWEDSEGTEGSSLLPGEQPLHTVDPGSAKQRPPRSTCQSFEPPETPVVKDSTIGGSPQPRPSVGAFNPGMEDILDSAMGTNWVPEEASGEASEIPVPQGTELSPSRPGGGSMQTEPARPSNFLSASSPLPASAKGQQPADVTGTALPRVGPVRPTGQDWNHTPQKTDHPSALLRDPPEPGSPRISSLRPQGLSNPSTLSAQPQLSRSHSSGSVLPLGELEGRRSTRDRRSPAEPEGGPASEGAARPLPRFNSVPLTDTGHERQSEGSFSPQLQESVFHLLVPSVILVLLAVGGLLFYRWRRRSHQEPQRADSPLEQPEGSPLTQDDRQVELPV TT0IQER TT Clinical trial TT0IQER KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04380:Osteoclast differentiation; hsa04640:Hematopoietic cell lineage; hsa04668:TNF signaling pathway; hsa05323:Rheumatoid arthritis TT7MRDV ID TT7MRDV TT7MRDV TN Macrophage colony-stimulating factor 1 receptor (CSF1R) TT7MRDV UP P07333 TT7MRDV UC CSF1R_HUMAN TT7MRDV BC Kinase TT7MRDV SN Proto-oncogene c-Fms; M-CSF-R; FMS; CSF-1R; CSF-1-R; CSF-1 receptor; CD115 TT7MRDV GN CSF1R TT7MRDV FC Promotes the release of proinflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor. Tyrosine-protein kinase that acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. TT7MRDV EC EC 2.7.10.1 TT7MRDV PD 4WRM; 4WRL; 4R7I; 4R7H; 4LIQ TT7MRDV SQ MGPGVLLLLLVATAWHGQGIPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGAHTHPPDEFLFTPVVVACMSIMALLLLLLLLLLYKYKQKPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGVDYKNIHLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSNDSFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQAQEDRRERDYTNLPSSSRSGGSGSSSSELEEESSSEHLTCCEQGDIAQPLLQPNNYQFC TT7MRDV TT Successful TT7MRDV FM Protein kinase superfamily. Tyr protein kinase family TT7MRDV KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04061:Viral protein interaction with cytokine and cytokine receptor; hsa04151:PI3K-Akt signaling pathway; hsa04380:Osteoclast differentiation; hsa04640:Hematopoietic cell lineage; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05221:Acute myeloid leukemia TTRECN3 ID TTRECN3 TTRECN3 TN MAP kinase signal-integrating kinase 2 (MKNK2) TTRECN3 UP Q9HBH9 TTRECN3 UC MKNK2_HUMAN TTRECN3 BC Protein kinase superfamily. CAMK Ser/Thr protein kinase family TTRECN3 SN Mnk2; MAPK signal-integrating kinase 2 TTRECN3 GN MKNK2 TTRECN3 FC Serine/threonine-protein kinase that phosphorylates SFPQ/PSF, HNRNPA1 and EIF4E. May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. Required for mediating PP2A-inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from cytoplasm to nucleus. Isoform 1 displays a high basal kinase activity, but isoform 2 exhibits a very low kinase activity. Acts as a mediator of the suppressive effects of IFNgamma on hematopoiesis. Negative regulator for signals that control generation of arsenic trioxide As(2)O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal. TTRECN3 EC EC 2.7.11.1 TTRECN3 PD 6CKI; 6CK6; 6CK3; 6CJY; 6CJW TTRECN3 SQ MVQKKPAELQGFHRSFKGQNPFELAFSLDQPDHGDSDFGLQCSARPDMPASQPIDIPDAKKRGKKKKRGRATDSFSGRFEDVYQLQEDVLGEGAHARVQTCINLITSQEYAVKIIEKQPGHIRSRVFREVEMLYQCQGHRNVLELIEFFEEEDRFYLVFEKMRGGSILSHIHKRRHFNELEASVVVQDVASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDLGSGIKLNGDCSPISTPELLTPCGSAEYMAPEVVEAFSEEASIYDKRCDLWSLGVILYILLSGYPPFVGRCGSDCGWDRGEACPACQNMLFESIQEGKYEFPDKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWVQGCAPENTLPTPMVLQRNSCAKDLTSFAAEAIAMNRQLAQHDEDLAEEEAAGQGQPVLVRATSRCLQLSPPSQSKLAQRRQRASLSSAPVVLVGDHA TTRECN3 TT Clinical trial TTRECN3 KE hsa04010:MAPK signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04910:Insulin signaling pathway TTEZAUX ID TTEZAUX TTEZAUX TN MAPK signal-integrating kinase 1 (MKNK1) TTEZAUX UP Q9BUB5 TTEZAUX UC MKNK1_HUMAN TTEZAUX BC Protein kinase superfamily. CAMK Ser/Thr protein kinase family TTEZAUX SN Mnk1; MAP kinase signal-integrating kinase 1 TTEZAUX GN MKNK1 TTEZAUX FC May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. TTEZAUX EC EC 2.7.11.1 TTEZAUX PD 5WVD; 2Y9Q; 2HW6 TTEZAUX SQ MVSSQKLEKPIEMGSSEPLPIADGDRRRKKKRRGRATDSLPGKFEDMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKDKVSLCHLGWSAMAPSGLTAAPTSLGSSDPPTSASQVAGTTGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCTPITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGQAPEKGLPTPQVLQRNSSTMDLTLFAAEAIALNRQLSQHEENELAEEPEALADGLCSMKLSPPCKSRLARRRALAQAGRGEDRSPPTAL TTEZAUX TT Clinical trial TTEZAUX KE hsa04010:MAPK signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04910:Insulin signaling pathway TTQBCEJ ID TTQBCEJ TTQBCEJ TN MAPK/ERK kinase kinase 1 (MAP3K1) TTQBCEJ UP Q13233 TTQBCEJ UC M3K1_HUMAN TTQBCEJ BC Kinase TTQBCEJ SN Mitogenactivated protein kinase kinase kinase 1; Mitogen-activated protein kinase kinase kinase 1; MEKK1; MEKK 1; MEKK; MEK kinase 1; MAPKKK1 TTQBCEJ GN MAP3K1 TTQBCEJ FC Activates the ERK and JNK kinase pathways by phosphorylation of MAP2K1 and MAP2K4. May phosphorylate the MAPK8/JNK1 kinase. Activates CHUK and IKBKB, the central protein kinases of the NF-kappa-B pathway. Component of a protein kinase signal transduction cascade. TTQBCEJ EC EC 2.7.11.25 TTQBCEJ SQ MAAAAGNRASSSGFPGARATSPEAGGGGGALKASSAPAAAAGLLREAGSGGRERADWRRRQLRKVRSVELDQLPEQPLFLAASPPASSTSPSPEPADAAGSGTGFQPVAVPPPHGAASRGGAHLTESVAAPDSGASSPAAAEPGEKRAPAAEPSPAAAPAGREMENKETLKGLHKMDDRPEERMIREKLKATCMPAWKHEWLERRNRRGPVVVKPIPVKGDGSEMNHLAAESPGEVQASAASPASKGRRSPSPGNSPSGRTVKSESPGVRRKRVSPVPFQSGRITPPRRAPSPDGFSPYSPEETNRRVNKVMRARLYLLQQIGPNSFLIGGDSPDNKYRVFIGPQNCSCARGTFCIHLLFVMLRVFQLEPSDPMLWRKTLKNFEVESLFQKYHSRRSSRIKAPSRNTIQKFVSRMSNSHTLSSSSTSTSSSENSIKDEEEQMCPICLLGMLDEESLTVCEDGCRNKLHHHCMSIWAEECRRNREPLICPLCRSKWRSHDFYSHELSSPVDSPSSLRAAQQQTVQQQPLAGSRRNQESNFNLTHYGTQQIPPAYKDLAEPWIQVFGMELVGCLFSRNWNVREMALRRLSHDVSGALLLANGESTGNSGGSSGSSPSGGATSGSSQTSISGDVVEACCSVLSMVCADPVYKVYVAALKTLRAMLVYTPCHSLAERIKLQRLLQPVVDTILVKCADANSRTSQLSISTLLELCKGQAGELAVGREILKAGSIGIGGVDYVLNCILGNQTESNNWQELLGRLCLIDRLLLEFPAEFYPHIVSTDVSQAEPVEIRYKKLLSLLTFALQSIDNSHSMVGKLSRRIYLSSARMVTTVPHVFSKLLEMLSVSSSTHFTRMRRRLMAIADEVEIAEAIQLGVEDTLDGQQDSFLQASVPNNYLETTENSSPECTVHLEKTGKGLCATKLSASSEDISERLASISVGPSSSTTTTTTTTEQPKPMVQTKGRPHSQCLNSSPLSHHSQLMFPALSTPSSSTPSVPAGTATDVSKHRLQGFIPCRIPSASPQTQRKFSLQFHRNCPENKDSDKLSPVFTQSRPLPSSNIHRPKPSRPTPGNTSKQGDPSKNSMTLDLNSSSKCDDSFGCSSNSSNAVIPSDETVFTPVEEKCRLDVNTELNSSIEDLLEASMPSSDTTVTFKSEVAVLSPEKAENDDTYKDDVNHNQKCKEKMEAEEEEALAIAMAMSASQDALPIVPQLQVENGEDIIIIQQDTPETLPGHTKAKQPYREDTEWLKGQQIGLGAFSSCYQAQDVGTGTLMAVKQVTYVRNTSSEQEEVVEALREEIRMMSHLNHPNIIRMLGATCEKSNYNLFIEWMAGGSVAHLLSKYGAFKESVVINYTEQLLRGLSYLHENQIIHRDVKGANLLIDSTGQRLRIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVLRGQQYGRSCDVWSVGCAIIEMACAKPPWNAEKHSNHLALIFKIASATTAPSIPSHLSPGLRDVALRCLELQPQDRPPSRELLKHPVFRTTW TTQBCEJ TT Clinical trial TTQBCEJ FM Kinase TTQBCEJ KE hsa04010:MAPK signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa04622:RIG-I-like receptor signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04912:GnRH signaling pathway; hsa05161:Hepatitis B; hsa05166:HTLV-I infection TTQBCEJ RC R-HSA-166058:MyD88:Mal cascade initiated on plasma membrane; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-933542:TRAF6 mediated NF-kB activation; R-HSA-975138:TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation; R-HSA-975871:MyD88 cascade initiated on plasma membrane TTK1N5G ID TTK1N5G TTK1N5G TN MAPK/ERK kinase kinase 2 (MAP3K2) TTK1N5G UP Q9Y2U5 TTK1N5G UC M3K2_HUMAN TTK1N5G BC Kinase TTK1N5G SN Mitogen-activated protein kinase kinase kinase 2; MEKK2; MEKK 2; MEK kinase 2; MAPKKK2 TTK1N5G GN MAP3K2 TTK1N5G FC Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7. Plays a role in caveolae kiss-and-run dynamics. Component of a protein kinase signal transduction cascade. TTK1N5G EC EC 2.7.11.25 TTK1N5G PD 5HQ8; 5EX0; 2NPT; 2CU1 TTK1N5G SQ MDDQQALNSIMQDLAVLHKASRPALSLQETRKAKSSSPKKQNDVRVKFEHRGEKRILQFPRPVKLEDLRSKAKIAFGQSMDLHYTNNELVIPLTTQDDLDKAVELLDRSIHMKSLKILLVINGSTQATNLEPLPSLEDLDNTVFGAERKKRLSIIGPTSRDRSSPPPGYIPDELHQVARNGSFTSINSEGEFIPESMDQMLDPLSLSSPENSGSGSCPSLDSPLDGESYPKSRMPRAQSYPDNHQEFSDYDNPIFEKFGKGGTYPRRYHVSYHHQEYNDGRKTFPRARRTQGTSLRSPVSFSPTDHSLSTSSGSSIFTPEYDDSRIRRRGSDIDNPTLTVMDISPPSRSPRAPTNWRLGKLLGQGAFGRVYLCYDVDTGRELAVKQVQFDPDSPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQEKTLSIFMEYMPGGSIKDQLKAYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSTGNVKLGDFGASKRLQTICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVACTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPKLPPHVSDYTRDFLKRIFVEAKLRPSADELLRHMFVHYH TTK1N5G TT Clinical trial TTK1N5G FM Kinase TTK1N5G KE hsa04010:MAPK signaling pathway; hsa04540:Gap junction; hsa04912:GnRH signaling pathway TTMUG9D ID TTMUG9D TTMUG9D TN MAPK-activated protein kinase 2 (MAPKAPK2) TTMUG9D UP P49137 TTMUG9D UC MAPK2_HUMAN TTMUG9D BC Kinase TTMUG9D SN MK2; MK-2; MAPKactivated protein kinase 2; MAPKAPK-2; MAPKAP-K2; MAPKAP kinase 2; MAP kinaseactivated protein kinase 2; MAP kinase-activated protein kinase 2 TTMUG9D GN MAPKAPK2 TTMUG9D FC Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to the dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to the regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity, leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress induced by ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites. Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. TTMUG9D EC EC 2.7.11.1 TTMUG9D PD 4TYH; 3WI6; 3R30; 3R2Y; 3R2B TTMUG9D SQ MLSNSQGQSPPVPFPAPAPPPQPPTPALPHPPAQPPPPPPQQFPQFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATMRVDYEQIKIKKIEDASNPLLLKRRKKARALEAAALAH TTMUG9D TT Clinical trial TTMUG9D FM Kinase TTMUG9D KE hsa04010:MAPK signaling pathway; hsa04370:VEGF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa05203:Viral carcinogenesis TTMUG9D RC R-HSA-171007:p38MAPK events; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-3371453:Regulation of HSF1-mediated heat shock response; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-450302:activated TAK1 mediates p38 MAPK activation TTX4RTB ID TTX4RTB TTX4RTB TN Melanin-concentrating hormone receptor 1 (MCHR1) TTX4RTB UP Q99705 TTX4RTB UC MCHR1_HUMAN TTX4RTB BC GPCR rhodopsin TTX4RTB SN Somatostatinreceptor-like protein; Somatostatin receptor-like protein; SLC1; SLC-1; Melanin-concentrating hormone receptor subtype 1; MCHR-1; MCHR; MCH1R; MCH-R1; MCH-1R; MCH(1) receptor; MCH receptor1; MCH receptor 1; GPR24; G-protein coupled receptor 24; G protein coupled receptor 24 TTX4RTB GN MCHR1 TTX4RTB FC Receptor for melanin-concentrating hormone, coupled to both G proteins that inhibit adenylyl cyclase and G proteins that activate phosphoinositide hydrolysis. TTX4RTB SQ MSVGAMKKGVGRAVGLGGGSGCQATEEDPLPNCGACAPGQGGRRWRLPQPAWVEGSSARLWEQATGTGWMDLEASLLPTGPNASNTSDGPDNLTSAGSPPRTGSISYINIIMPSVFGTICLLGIIGNSTVIFAVVKKSKLHWCNNVPDIFIINLSVVDLLFLLGMPFMIHQLMGNGVWHFGETMCTLITAMDANSQFTSTYILTAMAIDRYLATVHPISSTKFRKPSVATLVICLLWALSFISITPVWLYARLIPFPGGAVGCGIRLPNPDTDLYWFTLYQFFLAFALPFVVITAAYVRILQRMTSSVAPASQRSIRLRTKRVTRTAIAICLVFFVCWAPYYVLQLTQLSISRPTLTFVYLYNAAISLGYANSCLNPFVYIVLCETFRKRLVLSVKPAAQGQLRAVSNAQTADEERTESKGT TTX4RTB TT Clinical trial TTX4RTB FM GPCR rhodopsin TTX4RTB KE hsa04080:Neuroactive ligand-receptor interaction TTX4RTB RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events TT0MV2T ID TT0MV2T TT0MV2T TN Melanocortin receptor 1 (MC1R) TT0MV2T UP Q01726 TT0MV2T UC MSHR_HUMAN TT0MV2T BC GPCR rhodopsin TT0MV2T SN Melanotropin receptor; Melanocyte-stimulating hormone receptor; Melanocortin-1 receptor; MSHR; MSH-R; MC1-R TT0MV2T GN MC1R TT0MV2T FC The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Receptor for MSH (alpha, beta and gamma) and ACTH. TT0MV2T SQ MAVQGSQRRLLGSLNSTPTAIPQLGLAANQTGARCLEVSISDGLFLSLGLVSLVENALVVATIAKNRNLHSPMYCFICCLALSDLLVSGSNVLETAVILLLEAGALVARAAVLQQLDNVIDVITCSSMLSSLCFLGAIAVDRYISIFYALRYHSIVTLPRARRAVAAIWVASVVFSTLFIAYYDHVAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIARLHKRQRPVHQGFGLKGAVTLTILLGIFFLCWGPFFLHLTLIVLCPEHPTCGCIFKNFNLFLALIICNAIIDPLIYAFHSQELRRTLKEVLTCSW TT0MV2T TT Successful TT0MV2T KE hsa04080:Neuroactive ligand-receptor interaction; hsa04916:Melanogenesis TT0MV2T RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events TT63M7Q ID TT63M7Q TT63M7Q TN Melanoma-associated antigen 1 (MAGEA1) TT63M7Q UP P43355 TT63M7Q UC MAGA1_HUMAN TT63M7Q BC Melanoma associated antigen TT63M7Q SN Melanomaassociated antigen 1; MAGE1A; MAGE1 antigen; MAGE1; MAGE-1 antigen; Cancer/testis antigen 1.1; CT1.1; Antigen MZ2E; Antigen MZ2-E TT63M7Q GN MAGEA1 TT63M7Q FC May inhibit notch intracellular domain (NICD) transactivation. May play a role in embryonal development and tumor transformation or aspects of tumor progression. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes. May be involved in transcriptional regulation through interaction with SNW1 and recruiting histone deactelyase HDAC1. TT63M7Q PD 3BO8; 1W72 TT63M7Q SQ MSLEQRSLHCKPEEALEAQQEALGLVCVQAATSSSSPLVLGTLEEVPTAGSTDPPQSPQGASAFPTTINFTRQRQPSEGSSSREEEGPSTSCILESLFRAVITKKVADLVGFLLLKYRAREPVTKAEMLESVIKNYKHCFPEIFGKASESLQLVFGIDVKEADPTGHSYVLVTCLGLSYDGLLGDNQIMPKTGFLIIVLVMIAMEGGHAPEEEIWEELSVMEVYDGREHSAYGEPRKLLTQDLVQEKYLEYRQVPDSDPARYEFLWGPRALAETSYVKVLEYVIKVSARVRFFFPSLREAALREEEEGV TT63M7Q TT Clinical trial TT63M7Q FM Melanoma associated protein TT9E64S ID TT9E64S TT9E64S TN Metalloreductase STEAP1 (STEAP1) TT9E64S UP Q9UHE8 TT9E64S UC STEA1_HUMAN TT9E64S BC Metal ion oxidoreductase TT9E64S SN Sixtransmembrane epithelial antigen of prostate 1; STEAP1 TT9E64S GN STEAP1 TT9E64S FC Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor. TT9E64S EC EC 1.16.1.- TT9E64S SQ MESRKDITNQEELWKMKPRRNLEEDDYLHKDTGETSMLKRPVLLHLHQTAHADEFDCPSELQHTQELFPQWHLPIKIAAIIASLTFLYTLLREVIHPLATSHQQYFYKIPILVINKVLPMVSITLLALVYLPGVIAAIVQLHNGTKYKKFPHWLDKWMLTRKQFGLLSFFFAVLHAIYSLSYPMRRSYRYKLLNWAYQQVQQNKEDAWIEHDVWRMEIYVSLGIVGLAILALLAVTSIPSVSDSLTWREFHYIQSKLGIVSLLLGTIHALIFAWNKWIDIKQFVWYTPPTFMIAVFLPIVVLIFKSILFLPCLRKKILKIRHGWEDVTKINKTEICSQL TT9E64S TT Clinical trial TT9E64S KE hsa04978:Mineral absorption TT4UXPE ID TT4UXPE TT4UXPE TN MHC class I NK cell receptor 2DL1 (CD158A) TT4UXPE UP P43626 TT4UXPE UC KI2L1_HUMAN TT4UXPE BC Immunoglobulin TT4UXPE SN p58.1 MHC class-I-specific NK receptor; p58 natural killer cell receptor clones CL-42/47.11; p58 NK receptor CL-42/47.11; Natural killer-associated transcript 1; NKAT1; NKAT-1; Killer cell immunoglobulin-like receptor 2DL1; CD158A; CD158 antigen-like family member A TT4UXPE GN KIR2DL1 TT4UXPE FC Receptor on natural killer (NK) cells for some HLA-C alleles such as w4 and w6. Inhibits the activity of NK cells thus preventing cell lysis. TT4UXPE PD 1NKR; 1IM9 TT4UXPE SQ MSLLVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGPLVKSEETVILQCWSDVMFEHFLLHREGMFNDTLRLIGEHHDGVSKANFSISRMTQDLAGTYRCYGSVTHSPYQVSAPSDPLDIVIIGLYEKPSLSAQPGPTVLAGENVTLSCSSRSSYDMYHLSREGEAHERRLPAGPKVNGTFQADFPLGPATHGGTYRCFGSFHDSPYEWSKSSDPLLVSVTGNPSNSWPSPTEPSSKTGNPRHLHILIGTSVVIILFILLFFLLHRWCSNKKNAAVMDQESAGNRTANSEDSDEQDPQEVTYTQLNHCVFTQRKITRPSQRPKTPPTDIIVYTELPNAESRSKVVSCP TT4UXPE TT Clinical trial TT4UXPE FM Immunoglobulin TT4UXPE KE hsa04612:Antigen processing and presentation; hsa04650:Natural killer cell mediated cytotoxicity; hsa05332:Graft-versus-host disease TT4UXPE RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell TTU0P73 ID TTU0P73 TTU0P73 TN MHC class I NK cell receptor 2DL2 (CD158b1) TTU0P73 UP P43627 TTU0P73 UC KI2L2_HUMAN TTU0P73 BC Immunoglobulin TTU0P73 SN p58 natural killer cell receptor clone CL-43; p58 NK receptor CL-43; Natural killer-associated transcript 6; NKAT6; NKAT-6; Killer cell immunoglobulin-like receptor 2DL2; CD158B1; CD158 antigen-like family member B1 TTU0P73 GN KIR2DL2 TTU0P73 FC Receptor on natural killer (NK) cells for HLA-Cw1, 3, 7, and 8 allotypes. Inhibits the activity of NK cells thus preventing cell lysis. TTU0P73 PD 2DLI; 2DL2; 1EFX TTU0P73 SQ MSLMVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGRLVKSEETVILQCWSDVRFEHFLLHREGKFKDTLHLIGEHHDGVSKANFSIGPMMQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVLAGESVTLSCSSRSSYDMYHLSREGEAHECRFSAGPKVNGTFQADFPLGPATHGGTYRCFGSFRDSPYEWSNSSDPLLVSVIGNPSNSWPSPTEPSSKTGNPRHLHILIGTSVVIILFILLFFLLHRWCSNKKNAAVMDQESAGNRTANSEDSDEQDPQEVTYTQLNHCVFTQRKITRPSQRPKTPPTDIIVYAELPNAESRSKVVSCP TTU0P73 TT Clinical trial TTU0P73 KE hsa04612:Antigen processing and presentation; hsa04650:Natural killer cell mediated cytotoxicity; hsa05332:Graft-versus-host disease TTU0P73 RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell TTEX3SI ID TTEX3SI TTEX3SI TN MHC class I NK cell receptor 2DL3 (CD158b2) TTEX3SI UP P43628 TTEX3SI UC KI2L3_HUMAN TTEX3SI BC Immunoglobulin TTEX3SI SN p58.2 MHC class-I-specific NK receptor; p58 natural killer cell receptor clone CL-6; p58 NK receptor CL-6; Natural killer-associated transcript 2; NKAT2b; NKAT2a; NKAT2; NKAT-2; Killer inhibitory receptor cl 2-3; Killer cell immunoglobulin-like receptor 2DL3; KIRCL23; KIR-023GB; CD158B2; CD158 antigen-like family member B2 TTEX3SI GN KIR2DL3 TTEX3SI FC Receptor on natural killer (NK) cells for HLA-C alleles (HLA-Cw1, HLA-Cw3 and HLA-Cw7). Inhibits the activity of NK cells thus preventing cell lysis. TTEX3SI PD 1B6U TTEX3SI SQ MSLMVVSMVCVGFFLLQGAWPHEGVHRKPSLLAHPGPLVKSEETVILQCWSDVRFQHFLLHREGKFKDTLHLIGEHHDGVSKANFSIGPMMQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVLAGESVTLSCSSRSSYDMYHLSREGEAHERRFSAGPKVNGTFQADFPLGPATHGGTYRCFGSFRDSPYEWSNSSDPLLVSVTGNPSNSWPSPTEPSSETGNPRHLHVLIGTSVVIILFILLLFFLLHRWCCNKKNAVVMDQEPAGNRTVNREDSDEQDPQEVTYAQLNHCVFTQRKITRPSQRPKTPPTDIIVYTELPNAEP TTEX3SI TT Clinical trial TTEX3SI KE hsa04612:Antigen processing and presentation; hsa04650:Natural killer cell mediated cytotoxicity; hsa05332:Graft-versus-host disease TTEX3SI RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell TT9HL5R ID TT9HL5R TT9HL5R TN Mitochondrial matrix protein P1 (HSPD1) TT9HL5R UP P10809 TT9HL5R UC CH60_HUMAN TT9HL5R BC Chaperonin ATPase TT9HL5R SN P60 lymphocyte protein; HuCHA60; Hsp60; Heat shock protein 60; HSP-60; Chaperonin 60; CPN60; 60 kDa heat shock protein, mitochondrial; 60 kDa chaperonin TT9HL5R GN HSPD1 TT9HL5R FC Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. Chaperonin implicated in mitochondrial protein import and macromolecular assembly. TT9HL5R EC EC 5.6.1.7 TT9HL5R PD 4PJ1 TT9HL5R SQ MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF TT9HL5R TT Clinical trial TT9HL5R FM Heat shock protein TT9HL5R KE hsa03018:RNA degradation; hsa04940:Type I diabetes mellitus; hsa05134:Legionellosis; hsa05152:Tuberculosis TT9HL5R RC R-HSA-1268020:Mitochondrial protein import TTZ963I ID TTZ963I TTZ963I TN Monoglyceride lipase (MAGL) TTZ963I UP Q99685 TTZ963I UC MGLL_HUMAN TTZ963I BC Carboxylic ester hydrolase TTZ963I SN Monoacylglycerol lipase; MGL; Lysophospholipaselike; Lysophospholipase-like; Lysophospholipase homolog; HUK5; HU-K5 TTZ963I GN MGLL TTZ963I FC Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain. Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth. Converts monoacylglycerides to free fatty acids and glycerol. TTZ963I EC EC 3.1.1.23 TTZ963I PD 6BQ0; 6AX1; 5ZUN; 4UUQ; 3PE6 TTZ963I SQ MPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTASPP TTZ963I TT Clinical trial TTZ963I FM Carboxylic ester hydrolase TTZ963I KE hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways; hsa04723:Retrograde endocannabinoid signaling TTZ963I RC R-HSA-1482883:Acyl chain remodeling of DAG and TAG; R-HSA-163560:Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis TT953CX ID TT953CX TT953CX TN Motilin receptor (MLNR) TT953CX UP O43193 TT953CX UC MTLR_HUMAN TT953CX BC GPCR rhodopsin TT953CX SN MLNR; Gprotein coupled receptor 38 TT953CX GN MLNR TT953CX FC Receptor for motilin. TT953CX SQ MGSPWNGSDGPEGAREPPWPALPPCDERRCSPFPLGALVPVTAVCLCLFVVGVSGNVVTVMLIGRYRDMRTTTNLYLGSMAVSDLLILLGLPFDLYRLWRSRPWVFGPLLCRLSLYVGEGCTYATLLHMTALSVERYLAICRPLRARVLVTRRRVRALIAVLWAVALLSAGPFLFLVGVEQDPGISVVPGLNGTARIASSPLASSPPLWLSRAPPPSPPSGPETAEAAALFSRECRPSPAQLGALRVMLWVTTAYFFLPFLCLSILYGLIGRELWSSRRPLRGPAASGRERGHRQTVRVLLVVVLAFIICWLPFHVGRIIYINTEDSRMMYFSQYFNIVALQLFYLSASINPILYNLISKKYRAAAFKLLLARKSRPRGFHRSRDTAGEVAGDTGGDTVGYTETSANVKTMG TT953CX TT Clinical trial TT953CX KE hsa04080:Neuroactive ligand-receptor interaction TT953CX RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTBD6I7 ID TTBD6I7 TTBD6I7 TN Mucosal addressin cell adhesion molecule 1 (MADCAM1) TTBD6I7 UP Q13477 TTBD6I7 UC MADCA_HUMAN TTBD6I7 SN hMAdCAM-1; MAdCAM-1; MADCAM1 TTBD6I7 GN MADCAM1 TTBD6I7 FC Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes. Isoform 2, lacking the mucin-like domain, may be specialized in supporting integrin alpha-4/beta-7-dependent adhesion strengthening, independent of L- selectin binding. TTBD6I7 PD 4HD9; 4HCR; 4HC1; 4HBQ; 1GSM TTBD6I7 SQ MDFGLALLLAGLLGLLLGQSLQVKPLQVEPPEPVVAVALGASRQLTCRLACADRGASVQWRGLDTSLGAVQSDTGRSVLTVRNASLSAAGTRVCVGSCGGRTFQHTVQLLVYAFPDQLTVSPAALVPGDPEVACTAHKVTPVDPNALSFSLLVGGQELEGAQALGPEVQEEEEEPQGDEDVLFRVTERWRLPPLGTPVPPALYCQATMRLPGLELSHRQAIPVLHSPTSPEPPDTTSPESPDTTSPESPDTTSQEPPDTTSPEPPDKTSPEPAPQQGSTHTPRSPGSTRTRRPEISQAGPTQGEVIPTGSSKPAGDQLPAALWTSSAVLGLLLLALPTYHLWKRCRHLAEDDTHPPASLRLLPQVSAWAGLRGTGQVGISPS TTBD6I7 TT Clinical trial TTBD6I7 KE hsa04514:Cell adhesion molecules (CAMs); hsa04672:Intestinal immune network for IgA production TT8V13P ID TT8V13P TT8V13P TN Myb messenger RNA (MYB mRNA) TT8V13P UP P10242 TT8V13P UC MYB_HUMAN TT8V13P BC mRNA target TT8V13P SN Transcriptional activator Myb (mRNA); Proto-oncogene c-Myb (mRNA) TT8V13P GN MYB TT8V13P FC Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells. Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. TT8V13P SQ MARRPRHSIYSSDEDDEDFEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQESSKASQPAVATSFQKNSHLMGFAQAPPTAQLPATGQPTVNNDYSYYHISEAQNVSSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELELLLMSTENELKGQQVLPTQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGEHHSTPSLPADPGSLPEESASPARCMIVHQGTILDNVKNLLEFAETLQFIDSFLNTSSNHENSDLEMPSLTSTPLIGHKLTVTTPFHRDQTVKTQKENTVFRTPAIKRSILESSPRTPTPFKHALAAQEIKYGPLKMLPQTPSHLVEDLQDVIKQESDESGIVAEFQENGPPLLKKIKQEVESPTDKSGNFFCSHHWEGDSLNTQLFTQTSPVADAPNILTSSVLMAPASEDEDNVLKAFTVPKNRSLASPLQPCSSTWEPASCGKMEEQMTSSSQARKYVNAFSARTLVM TT8V13P TT Clinical trial TT8V13P FM mRNA target TT8V13P KE hsa04151:PI3K-Akt signaling pathway; hsa05166:HTLV-I infection TT8V13P RC R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTNQ5ZP ID TTNQ5ZP TTNQ5ZP TN Myc messenger RNA (MYC mRNA) TTNQ5ZP UP P01106 TTNQ5ZP UC MYC_HUMAN TTNQ5ZP BC mRNA target TTNQ5ZP SN bHLHe39 (mRNA); Transcription factor p64 (mRNA); Proto-oncogene c-Myc (mRNA); Myc proto-oncogene protein (mRNA); Class E basic helix-loop-helix protein 39 (mRNA); C-myc oncogene (mRNA); C-myc (mRNA) TTNQ5ZP GN MYC TTNQ5ZP FC Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. TTNQ5ZP PD 6G6L; 6G6K; 6G6J; 6C4U; 5I50 TTNQ5ZP SQ MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA TTNQ5ZP TT Clinical trial TTNQ5ZP FM mRNA target TTNQ5ZP KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04110:Cell cycle; hsa04151:PI3K-Akt signaling pathway; hsa04310:Wnt signaling pathway; hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04630:Jak-STAT signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05213:Endometrial cancer; hsa05216:Thyroid cancer; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05230:Central carbon metabolism in cancer TTNQ5ZP RC R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2173796:SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-4411364:Binding of TCF/LEF:CTNNB1 to target gene promoters; R-HSA-5687128:MAPK6/MAPK4 signaling; R-HSA-69202:Cyclin E associated events during G1/S transition; R-HSA-69656:Cyclin A:Cdk2-associated events at S phase entry TT18ETS ID TT18ETS TT18ETS TN Myosin light kinase (MYLK) TT18ETS UP Q15746 TT18ETS UC MYLK_HUMAN TT18ETS BC Kinase TT18ETS SN smMLCK; Telokin; Myosin light chain kinase, smooth muscle; MYLK1; MLCK210; MLCK1; MLCK; Kinase-related protein; KRP; Endothelial cell (EC) MLCK isoform; EC mlck; 210,000 molecular weight myosin light chain kinase TT18ETS GN MYLK TT18ETS FC Regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e. g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp. -mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis. Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). TT18ETS EC EC 2.7.11.18 TT18ETS PD 6C6M; 5JTH; 5JQA; 2YR3; 2K0F TT18ETS SQ MGDVKLVASSHISKTSLSVDPSRVDSMPLTEAPAFILPPRNLCIKEGATAKFEGRVRGYPEPQVTWHRNGQPITSGGRFLLDCGIRGTFSLVIHAVHEEDRGKYTCEATNGSGARQVTVELTVEGSFAKQLGQPVVSKTLGDRFSAPAVETRPSIWGECPPKFATKLGRVVVKEGQMGRFSCKITGRPQPQVTWLKGNVPLQPSARVSVSEKNGMQVLEIHGVNQDDVGVYTCLVVNGSGKASMSAELSIQGLDSANRSFVRETKATNSDVRKEVTNVISKESKLDSLEAAAKSKNCSSPQRGGSPPWAANSQPQPPRESKLESCKDSPRTAPQTPVLQKTSSSITLQAARVQPEPRAPGLGVLSPSGEERKRPAPPRPATFPTRQPGLGSQDVVSKAANRRIPMEGQRDSAFPKFESKPQSQEVKENQTVKFRCEVSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVERLAVMEVAPSFSSVLKDCAVIEGQDFVLQCSVRGTPVPRITWLLNGQPIQYARSTCEAGVAELHIQDALPEDHGTYTCLAENALGQVSCSAWVTVHEKKSSRKSEYLLPVAPSKPTAPIFLQGLSDLKVMDGSQVTMTVQVSGNPPPEVIWLHNGNEIQESEDFHFEQRGTQHSLCIQEVFPEDTGTYTCEAWNSAGEVRTQAVLTVQEPHDGTQPWFISKPRSVTASLGQSVLISCAIAGDPFPTVHWLRDGKALCKDTGHFEVLQNEDVFTLVLKKVQPWHAGQYEILLKNRVGECSCQVSLMLQNSSARALPRGREPASCEDLCGGGVGADGGGSDRYGSLRPGWPARGQGWLEEEDGEDVRGVLKRRVETRQHTEEAIRQQEVEQLDFRDLLGKKVSTKTLSEDDLKEIPAEQMDFRANLQRQVKPKTVSEEERKVHSPQQVDFRSVLAKKGTSKTPVPEKVPPPKPATPDFRSVLGGKKKLPAENGSSSAETLNAKAVESSKPLSNAQPSGPLKPVGNAKPAETLKPMGNAKPAETLKPMGNAKPDENLKSASKEELKKDVKNDVNCKRGHAGTTDNEKRSESQGTAPAFKQKLQDVHVAEGKKLLLQCQVSSDPPATIIWTLNGKTLKTTKFIILSQEGSLCSVSIEKALPEDRGLYKCVAKNDAGQAECSCQVTVDDAPASENTKAPEMKSRRPKSSLPPVLGTESDATVKKKPAPKTPPKAAMPPQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLGSRQAQVNLTVVDKPDPPAGTPCASDIRSSSLTLSWYGSSYDGGSAVQSYSIEIWDSANKTWKELATCRSTSFNVQDLLPDHEYKFRVRAINVYGTSEPSQESELTTVGEKPEEPKDEVEVSDDDEKEPEVDYRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKYMARRKWQKTGNAVRAIGRLSSMAMISGLSGRKSSTGSPTSPLNAEKLESEEDVSQAFLEAVAEEKPHVKPYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEATCTAELIVETMEEGEGEGEEEEE TT18ETS TT Clinical trial TT18ETS FM Kinase TT18ETS KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04510:Focal adhesion; hsa04611:Platelet activation; hsa04810:Regulation of actin cytoskeleton; hsa04921:Oxytocin signaling pathway; hsa04971:Gastric acid secretion TT18ETS RC R-HSA-445355:Smooth Muscle Contraction TT4DP5S ID TT4DP5S TT4DP5S TN N-acetylmannosamine kinase (GNE) TT4DP5S UP Q9Y223 TT4DP5S UC GLCNE_HUMAN TT4DP5S BC Kinase TT4DP5S SN UDPGlcNAc2epimerase/ManAc kinase; GNE; Bifunctional UDPNacetylglucosamine 2epimerase/Nacetylmannosamine kinase TT4DP5S GN GNE TT4DP5S FC Regulates and initiates biosynthesis of N- acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays an essential role in early development. Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. {ECO:0000250, ECO:0000269|PubMed:10334995}. TT4DP5S PD 4ZHT; 3EO3; 2YI1; 2YHY; 2YHW TT4DP5S SQ MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRRIY TT4DP5S TT Clinical trial TT4DP5S KE hsa00520:Amino sugar and nucleotide sugar metabolism; hsa01100:Metabolic pathways TT4DP5S RC R-HSA-4085001:Sialic acid metabolism TTDN3LF ID TTDN3LF TTDN3LF TN Nerve growth factor (NGF) TTDN3LF UP P01138 TTDN3LF UC NGF_HUMAN TTDN3LF BC Growth factor TTDN3LF SN NGFB; Beta-nerve growth factor; Beta-NGF TTDN3LF GN NGF TTDN3LF FC Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (Probable). The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse. In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro) (By similarity). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI. Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer. The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form (By similarity). TTDN3LF PD 5JZ7; 4ZBN; 4EDX; 4EDW; 2IFG TTDN3LF SQ MSMLFYTLITAFLIGIQAEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNITVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRSSSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFETKCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTACVCVLSRKAVRRA TTDN3LF TT Clinical trial TTDN3LF FM Growth factor TTDN3LF KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04722:Neurotrophin signaling pathway; hsa04750:Inflammatory mediator regulation of TRP channels TTDN3LF RC R-HSA-170968:Frs2-mediated activation; R-HSA-170984:ARMS-mediated activation; R-HSA-193648:NRAGE signals death through JNK; R-HSA-193670:p75NTR negatively regulates cell cycle via SC1; R-HSA-198203:PI3K/AKT activation; R-HSA-205025:NADE modulates death signalling; R-HSA-205043:NRIF signals cell death from the nucleus; R-HSA-209543:p75NTR recruits signalling complexes; R-HSA-209560:NF-kB is activated and signals survival; R-HSA-209563:Axonal growth stimulation TTBPGLU ID TTBPGLU TTBPGLU TN Neuromedin-K receptor (TACR3) TTBPGLU UP P29371 TTBPGLU UC NK3R_HUMAN TTBPGLU BC GPCR rhodopsin TTBPGLU SN Tachykinin receptor 3; TACR3; Neuromedin K receptor; Neurokinin-3 receptor; Neurokinin B receptor; NKR; NK-3R; NK-3 receptor TTBPGLU GN TACR3 TTBPGLU FC This is a receptor for the tachykinin neuropeptide neuromedin-K (neurokinin B). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: neuromedin-K > substance K > substance P. TTBPGLU SQ MATLPAAETWIDGGGGVGADAVNLTASLAAGAATGAVETGWLQLLDQAGNLSSSPSALGLPVASPAPSQPWANLTNQFVQPSWRIALWSLAYGVVVAVAVLGNLIVIWIILAHKRMRTVTNYFLVNLAFSDASMAAFNTLVNFIYALHSEWYFGANYCRFQNFFPITAVFASIYSMTAIAVDRYMAIIDPLKPRLSATATKIVIGSIWILAFLLAFPQCLYSKTKVMPGRTLCFVQWPEGPKQHFTYHIIVIILVYCFPLLIMGITYTIVGITLWGGEIPGDTCDKYHEQLKAKRKVVKMMIIVVMTFAICWLPYHIYFILTAIYQQLNRWKYIQQVYLASFWLAMSSTMYNPIIYCCLNKRFRAGFKRAFRWCPFIKVSSYDELELKTTRFHPNRQSSMYTVTRMESMTVVFDPNDADTTRSSRKKRATPRDPSFNGCSRRNSKSASATSSFISSPYTSVDEYS TTBPGLU TT Clinical trial TTBPGLU KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTBPGLU RC R-HSA-416476:G alpha (q) signalling events TTRK9JT ID TTRK9JT TTRK9JT TN Neuropeptide Y receptor type 1 (NPY1R) TTRK9JT UP P25929 TTRK9JT UC NPY1R_HUMAN TTRK9JT BC GPCR rhodopsin TTRK9JT SN Neuropeptide Y-Y1 receptor; Neuropeptide Y receptor Y1; Neuropeptide Y Y(1) receptor; NPY1R; NPY1-R TTRK9JT GN NPY1R TTRK9JT FC Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is NPY > [Pro-34] PYY, PYY and [Leu-31, Pro-34] NPY > NPY (2-36) > [Ile-31, Gln-34] PP and PYY (3-36) > PP > NPY free acid. TTRK9JT PD 5ZBQ; 2IIL; 2F1U TTRK9JT SQ MNSTLFSQVENHSVHSNFSEKNAQLLAFENDDCHLPLAMIFTLALAYGAVIILGVSGNLALIIIILKQKEMRNVTNILIVNLSFSDLLVAIMCLPFTFVYTLMDHWVFGEAMCKLNPFVQCVSITVSIFSLVLIAVERHQLIINPRGWRPNNRHAYVGIAVIWVLAVASSLPFLIYQVMTDEPFQNVTLDAYKDKYVCFDQFPSDSHRLSYTTLLLVLQYFGPLCFIFICYFKIYIRLKRRNNMMDKMRDNKYRSSETKRINIMLLSIVVAFAVCWLPLTIFNTVFDWNHQIIATCNHNLLFLLCHLTAMISTCVNPIFYGFLNKNFQRDLQFFFNFCDFRSRDDDYETIAMSTMHTDVSKTSLKQASPVAFKKINNNDDNEKI TTRK9JT TT Clinical trial TTRK9JT KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTRK9JT RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTJ6WK9 ID TTJ6WK9 TTJ6WK9 TN Neuropeptide Y receptor type 2 (NPY2R) TTJ6WK9 UP P49146 TTJ6WK9 UC NPY2R_HUMAN TTJ6WK9 BC GPCR rhodopsin TTJ6WK9 SN Y2 receptor; NPY2R; NPY2-R; NPY-Y2 receptor TTJ6WK9 GN NPY2R TTJ6WK9 FC Receptor for neuropeptide Y andpeptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is PYY > NPY > PYY (3-36) > NPY (2-36) > [Ile-31, Gln-34] PP > [Leu- 31, Pro-34] NPY > PP, [Pro-34] PYY and NPY free acid. TTJ6WK9 PD 2IK3 TTJ6WK9 SQ MGPIGAEADENQTVEEMKVEQYGPQTTPRGELVPDPEPELIDSTKLIEVQVVLILAYCSIILLGVIGNSLVIHVVIKFKSMRTVTNFFIANLAVADLLVNTLCLPFTLTYTLMGEWKMGPVLCHLVPYAQGLAVQVSTITLTVIALDRHRCIVYHLESKISKRISFLIIGLAWGISALLASPLAIFREYSLIEIIPDFEIVACTEKWPGEEKSIYGTVYSLSSLLILYVLPLGIISFSYTRIWSKLKNHVSPGAANDHYHQRRQKTTKMLVCVVVVFAVSWLPLHAFQLAVDIDSQVLDLKEYKLIFTVFHIIAMCSTFANPLLYGWMNSNYRKAFLSAFRCEQRLDAIHSEVSVTFKAKKNLEVRKNSGPNDSFTEATNV TTJ6WK9 TT Clinical trial TTJ6WK9 KE hsa04080:Neuroactive ligand-receptor interaction TTJ6WK9 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTW4N16 ID TTW4N16 TTW4N16 TN Neuropeptide Y receptor type 4 (NPY4R) TTW4N16 UP P50391 TTW4N16 UC NPY4R_HUMAN TTW4N16 BC GPCR rhodopsin TTW4N16 SN Pancreatic polypeptide receptor 1; PPYR1; NPY4R; NPY4-R TTW4N16 GN NPY4R TTW4N16 FC Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is PP, PP (2-36) and [Ile-31, Gln-34] PP > [Pro-34] PYY > PYY and [Leu-31, Pro-34] NPY > NPY > PYY (3-36) and NPY (2-36) > PP (13- 36) > PP (31-36) > NPY free acid. TTW4N16 PD 2IK5 TTW4N16 SQ MNTSHLLALLLPKSPQGENRSKPLGTPYNFSEHCQDSVDVMVFIVTSYSIETVVGVLGNLCLMCVTVRQKEKANVTNLLIANLAFSDFLMCLLCQPLTAVYTIMDYWIFGETLCKMSAFIQCMSVTVSILSLVLVALERHQLIINPTGWKPSISQAYLGIVLIWVIACVLSLPFLANSILENVFHKNHSKALEFLADKVVCTESWPLAHHRTIYTTFLLLFQYCLPLGFILVCYARIYRRLQRQGRVFHKGTYSLRAGHMKQVNVVLVVMVVAFAVLWLPLHVFNSLEDWHHEAIPICHGNLIFLVCHLLAMASTCVNPFIYGFLNTNFKKEIKALVLTCQQSAPLEESEHLPLSTVHTEVSKGSLRLSGRSNPI TTW4N16 TT Clinical trial TTW4N16 KE hsa04080:Neuroactive ligand-receptor interaction TTW4N16 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTTUMEP ID TTTUMEP TTTUMEP TN Neurotensin receptor type 1 (NTSR1) TTTUMEP UP P30989 TTTUMEP UC NTR1_HUMAN TTTUMEP BC GPCR rhodopsin TTTUMEP SN NTSR1; NTRH; NTR1; NTR subtype 1; NT-R1; NT-R-1; High-affinity levocabastine-insensitive neurotensin receptor TTTUMEP GN NTSR1 TTTUMEP FC G-protein coupled receptor for the tridecapeptide neurotensin (NTS). Signaling is effected via G proteins that activate a phosphatidylinositol-calcium second messenger system. Signaling leads to the activation of downstream MAP kinases and protects cells against apoptosis. TTTUMEP PD 2LYW TTTUMEP SQ MRLNSSAPGTPGTPAADPFQRAQAGLEEALLAPGFGNASGNASERVLAAPSSELDVNTDIYSKVLVTAVYLALFVVGTVGNTVTAFTLARKKSLQSLQSTVHYHLGSLALSDLLTLLLAMPVELYNFIWVHHPWAFGDAGCRGYYFLRDACTYATALNVASLSVERYLAICHPFKAKTLMSRSRTKKFISAIWLASALLAVPMLFTMGEQNRSADGQHAGGLVCTPTIHTATVKVVIQVNTFMSFIFPMVVISVLNTIIANKLTVMVRQAAEQGQVCTVGGEHSTFSMAIEPGRVQALRHGVRVLRAVVIAFVVCWLPYHVRRLMFCYISDEQWTPFLYDFYHYFYMVTNALFYVSSTINPILYNLVSANFRHIFLATLACLCPVWRRRRKRPAFSRKADSVSSNHTLSSNATRETLY TTTUMEP TT Clinical trial TTTUMEP KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTTUMEP RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTUDPCI ID TTUDPCI TTUDPCI TN Neurotrophic tyrosine kinase ROR2 (ROR2) TTUDPCI UP Q01974 TTUDPCI UC ROR2_HUMAN TTUDPCI BC Kinase TTUDPCI SN receptor tyrosine kinase like orphan receptor 2; neurotrophic tyrosine kinase, receptor-related 2; Tyrosine-protein kinase transmembrane receptor ROR2; NTRKR2; BDB1; BDB TTUDPCI GN ROR2 TTUDPCI FC It seems to be required for cartilage and growth plate development. Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation. In contrast, has also been shown to have very little tyrosine kinase activity in vitro. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated signaling. Tyrosine-protein kinase receptor which may be involved in the early formation of the chondrocytes. TTUDPCI EC EC 2.7.10.1 TTUDPCI PD 4GT4; 3ZZW TTUDPCI SQ MARGSALPRRPLLCIPAVWAAAALLLSVSRTSGEVEVLDPNDPLGPLDGQDGPIPTLKGYFLNFLEPVNNITIVQGQTAILHCKVAGNPPPNVRWLKNDAPVVQEPRRIIIRKTEYGSRLRIQDLDTTDTGYYQCVATNGMKTITATGVLFVRLGPTHSPNHNFQDDYHEDGFCQPYRGIACARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTHLSDQCSQFAIPSFCHFVFPLCDARSRTPKPRELCRDECEVLESDLCRQEYTIARSNPLILMRLQLPKCEALPMPESPDAANCMRIGIPAERLGRYHQCYNGSGMDYRGTASTTKSGHQCQPWALQHPHSHHLSSTDFPELGGGHAYCRNPGGQMEGPWCFTQNKNVRMELCDVPSCSPRDSSKMGILYILVPSIAIPLVIACLFFLVCMCRNKQKASASTPQRRQLMASPSQDMEMPLINQHKQAKLKEISLSAVRFMEELGEDRFGKVYKGHLFGPAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRARLQHPNVVCLLGVVTKDQPLSMIFSYCSHGDLHEFLVMRSPHSDVGSTDDDRTVKSALEPPDFVHLVAQIAAGMEYLSSHHVVHKDLATRNVLVYDKLNVKISDLGLFREVYAADYYKLLGNSLLPIRWMAPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVVEMIRNRQVLPCPDDCPAWVYALMIECWNEFPSRRPRFKDIHSRLRAWGNLSNYNSSAQTSGASNTTQTSSLSTSPVSNVSNARYVGPKQKAPPFPQPQFIPMKGQIRPMVPPPQLYVPVNGYQPVPAYGAYLPNFYPVQIPMQMAPQQVPPQMVPKPSSHHSGSGSTSTGYVTTAPSNTSMADRAALLSEGADDTQNAPEDGAQSTVQEAEEEEEGSVPETELLGDCDTLQVDEAQVQLEA TTUDPCI TT Clinical trial TTUDPCI KE hsa04310:Wnt signaling pathway TTKLNRV ID TTKLNRV TTKLNRV TN NFKB messenger RNA (NFKB mRNA) TTKLNRV UP Q00653 TTKLNRV UC NFKB2_HUMAN TTKLNRV BC mRNA target TTKLNRV SN Oncogene Lyt-10 (mRNA); Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2 (mRNA); Nuclear factor NF-kappa-Bp52 subunit (mRNA); Nuclear factor NF-kappa-B p100 subunit (mRNA); Lyt10 (mRNA); Lymphocyte translocation chromosome 10 protein (mRNA); Lymphocyte translocation chromosome 10 (mRNA); H2TF1 (mRNA); DNA-binding factor KBF2 (mRNA) TTKLNRV GN NFKB2 TTKLNRV FC NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. TTKLNRV PD 5ZMC; 4OT9; 3DO7; 2D96; 1A3Q TTKLNRV SQ MESCYNPGLDGIIEYDDFKLNSSIVEPKEPAPETADGPYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSELGICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRPQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSKSPGASNLKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDENGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVFLQLKRKRGGDVSDSKQFTYYPLVEDKEEVQRKRRKALPTFSQPFGGGSHMGGGSGGAAGGYGGAGGGGSLGFFPSSLAYSPYQSGAGPMGCYPGGGGGAQMAATVPSRDSGEEAAEPSAPSRTPQCEPQAPEMLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIVYVIHHAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPAVPQLLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPLPSPPTSDSDSDSEGPEKDTRSSFRGHTPLDLTCSTKVKTLLLNAAQNTMEPPLTPPSPAGPGLSLGDTALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRGPETRDKLPSTAEVKEDSAYGSQSVEQEAEKLGPPPEPPGGLCHGHPQPQVH TTKLNRV TT Clinical trial TTKLNRV FM mRNA target TTKLNRV KE hsa04010:MAPK signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04380:Osteoclast differentiation; hsa05134:Legionellosis; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis TTKLNRV RC R-HSA-1810476:RIP-mediated NFkB activation via ZBP1; R-HSA-3134963:DEx/H-box helicases activate type I IFN and inflammatory cytokines production; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-448706:Interleukin-1 processing; R-HSA-5603027:IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR); R-HSA-5603029:IkBA variant leads to EDA-ID; R-HSA-5607761:Dectin-1 mediated noncanonical NF-kB signaling; R-HSA-5676590:NIK-->noncanonical NF-kB signaling; R-HSA-933542:TRAF6 mediated NF-kB activation TTPJ2SH ID TTPJ2SH TTPJ2SH TN N-sulphoglucosamine sulphohydrolase (SGSH) TTPJ2SH UP P51688 TTPJ2SH UC SPHM_HUMAN TTPJ2SH BC Sulfur-nitrogen hydrolase TTPJ2SH SN Sulphamidase; Sulfoglucosamine sulfamidase; HSS TTPJ2SH GN SGSH TTPJ2SH FC Catalyzes a step in lysosomal heparan sulfate degradation. TTPJ2SH EC EC 3.10.1.1 TTPJ2SH PD 4MIV; 4MHX TTPJ2SH SQ MSCPVPACCALLLVLGLCRARPRNALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFDKVRSLPLLLSQAGVRTGIIGKKHVGPETVYPFDFAYTEENGSVLQVGRNITRIKLLVRKFLQTQDDRPFFLYVAFHDPHRCGHSQPQYGTFCEKFGNGESGMGRIPDWTPQAYDPLDVLVPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPKRWGQVSEAYVSLLDLTPTILDWFSIPYPSYAIFGSKTIHLTGRSLLPALEAEPLWATVFGSQSHHEVTMSYPMRSVQHRHFRLVHNLNFKMPFPIDQDFYVSPTFQDLLNRTTAGQPTGWYKDLRHYYYRARWELYDRSRDPHETQNLATDPRFAQLLEMLRDQLAKWQWETHDPWVCAPDGVLEEKLSPQCQPLHNEL TTPJ2SH TT Clinical trial TTPJ2SH KE hsa00531:Glycosaminoglycan degradation; hsa01100:Metabolic pathways; hsa04142:Lysosome TTPJ2SH RC R-HSA-2024096:HS-GAG degradation TTA6ZN2 ID TTA6ZN2 TTA6ZN2 TN Nuclear factor erythroid 2-related factor 2 (Nrf2) TTA6ZN2 UP Q16236 TTA6ZN2 UC NF2L2_HUMAN TTA6ZN2 BC Basic leucine zipper bZIP TTA6ZN2 SN Nuclear factor, erythroid derived 2, like 2; NRF2; NFE2-related factor 2; NF-E2-related factor 2; HEBP1 TTA6ZN2 GN NFE2L2 TTA6ZN2 FC Important for the coordinated up-regulation of genes in response to oxidative stress and the regulation of cellular redox conditions. May be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region. Transcription activator that binds to antioxidant response (ARE) elements in the promoter regions of target genes. TTA6ZN2 PD 5WFV; 4IFL; 3ZGC; 2LZ1; 2FLU TTA6ZN2 SQ MMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN TTA6ZN2 TT Clinical trial TTA6ZN2 FM BZIP Maf transcription factor TTA6ZN2 KE hsa04141:Protein processing in endoplasmic reticulum TT60Q8D ID TT60Q8D TT60Q8D TN Orexin receptor type 1 (HCRTR1) TT60Q8D UP O43613 TT60Q8D UC OX1R_HUMAN TT60Q8D BC GPCR rhodopsin TT60Q8D SN Ox1r; Ox1-R; Ox-1-R; Orexin-1 receptor; Hypocretin receptor type 1; HFGAN72 receptor; 7-transmembrane G-protein coupledneuropeptide receptor TT60Q8D GN HCRTR1 TT60Q8D FC Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding. Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide. TT60Q8D PD 4ZJC; 4ZJ8 TT60Q8D SQ MEPSATPGAQMGVPPGSREPSPVPPDYEDEFLRYLWRDYLYPKQYEWVLIAAYVAVFVVALVGNTLVCLAVWRNHHMRTVTNYFIVNLSLADVLVTAICLPASLLVDITESWLFGHALCKVIPYLQAVSVSVAVLTLSFIALDRWYAICHPLLFKSTARRARGSILGIWAVSLAIMVPQAAVMECSSVLPELANRTRLFSVCDERWADDLYPKIYHSCFFIVTYLAPLGLMAMAYFQIFRKLWGRQIPGTTSALVRNWKRPSDQLGDLEQGLSGEPQPRARAFLAEVKQMRARRKTAKMLMVVLLVFALCYLPISVLNVLKRVFGMFRQASDREAVYACFTFSHWLVYANSAANPIIYNFLSGKFREQFKAAFSCCLPGLGPCGSLKAPSPRSSASHKSLSLQSRCSISKISEHVVLTSVTTVLP TT60Q8D TT Clinical trial TT60Q8D FM GPCR rhodopsin TT60Q8D KE hsa04080:Neuroactive ligand-receptor interaction TT60Q8D RC R-HSA-416476:G alpha (q) signalling events TTL31H0 ID TTL31H0 TTL31H0 TN OX40L receptor (CD134) TTL31H0 UP P43489 TTL31H0 UC TNR4_HUMAN TTL31H0 SN Tumor necrosis factor receptor superfamily member 4; TXGP1L; TAX transcriptionally-activated glycoprotein 1 receptor; CD134; ACT35 antigen TTL31H0 GN TNFRSF4 TTL31H0 FC Receptor for TNFSF4/OX40L/GP34. Is a costimulatory molecule implicated in long-term T-cell immunity. TTL31H0 PD 2HEY; 2HEV; 1D0A TTL31H0 SQ MCVGARRLGRGPCAALLLLGLGLSTVTGLHCVGDTYPSNDRCCHECRPGNGMVSRCSRSQNTVCRPCGPGFYNDVVSSKPCKPCTWCNLRSGSERKQLCTATQDTVCRCRAGTQPLDSYKPGVDCAPCPPGHFSPGDNQACKPWTNCTLAGKHTLQPASNSSDAICEDRDPPATQPQETQGPPARPITVQPTEAWPRTSQGPSTRPVEVPGGRAVAAILGLGLVLGLLGPLAILLALYLLRRDQRLPPDAHKPPGGGSFRTPIQEEQADAHSTLAKI TTL31H0 TT Clinical trial TTL31H0 FM Transmembrane protein TTL31H0 KE hsa04060:Cytokine-cytokine receptor interaction TTL31H0 RC R-HSA-5669034:TNFs bind their physiological receptors TTXA6PH ID TTXA6PH TTXA6PH TN Oxysterols receptor LXR-beta (NR1H2) TTXA6PH UP P55055 TTXA6PH UC NR1H2_HUMAN TTXA6PH BC Nuclear hormone receptor TTXA6PH SN Ubiquitously-expressed nuclear receptor; Nuclear receptor subfamily 1 group H member 2; Nuclear receptor NER; Nuclear orphan receptor LXR-beta; NER; Liver X receptor beta; LXRbeta; LXRB TTXA6PH GN NR1H2 TTXA6PH FC Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism. Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex. Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity. TTXA6PH PD 5KYJ; 5KYA; 5JY3; 5I4V; 5HJP TTXA6PH SQ MSSPTTSSLDTPLPGNGPPQPGAPSSSPTVKEEGPEPWPGGPDPDVPGTDEASSACSTDWVIPDPEEEPERKRKKGPAPKMLGHELCRVCGDKASGFHYNVLSCEGCKGFFRRSVVRGGARRYACRGGGTCQMDAFMRRKCQQCRLRKCKEAGMREQCVLSEEQIRKKKIRKQQQESQSQSQSPVGPQGSSSSASGPGASPGGSEAGSQGSGEGEGVQLTAAQELMIQQLVAAQLQCNKRSFSDQPKVTPWPLGADPQSRDARQQRFAHFTELAIISVQEIVDFAKQVPGFLQLGREDQIALLKASTIEIMLLETARRYNHETECITFLKDFTYSKDDFHRAGLQVEFINPIFEFSRAMRRLGLDDAEYALLIAINIFSADRPNVQEPGRVEALQQPYVEALLSYTRIKRPQDQLRFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE TTXA6PH TT Clinical trial TTXA6PH FM Nuclear hormone receptor family TTXA6PH RC R-HSA-383280:Nuclear Receptor transcription pathway TT2THBD ID TT2THBD TT2THBD TN P2X purinoceptor 3 (P2RX3) TT2THBD UP P56373 TT2THBD UC P2RX3_HUMAN TT2THBD BC ATP-gated P2X receptor cation channel TT2THBD SN P2X3 receptor; P2X3; P2RX3; ATP-gated ion channel P2X(3) TT2THBD GN P2RX3 TT2THBD FC Receptor for ATP that acts as a ligand-gated ionchannel. TT2THBD PD 5YVE; 5SVT; 5SVS; 5SVR; 5SVQ TT2THBD SQ MNCISDFFTYETTKSVVVKSWTIGIINRVVQLLIISYFVGWVFLHEKAYQVRDTAIESSVVTKVKGSGLYANRVMDVSDYVTPPQGTSVFVIITKMIVTENQMQGFCPESEEKYRCVSDSQCGPERLPGGGILTGRCVNYSSVLRTCEIQGWCPTEVDTVETPIMMEAENFTIFIKNSIRFPLFNFEKGNLLPNLTARDMKTCRFHPDKDPFCPILRVGDVVKFAGQDFAKLARTGGVLGIKIGWVCDLDKAWDQCIPKYSFTRLDSVSEKSSVSPGYNFRFAKYYKMENGSEYRTLLKAFGIRFDVLVYGNAGKFNIIPTIISSVAAFTSVGVGTVLCDIILLNFLKGADQYKAKKFEEVNETTLKIAALTNPVYPSDQTTAEKQSTDSGAFSIGH TT2THBD TT Clinical trial TT2THBD KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TT473XN ID TT473XN TT473XN TN P2X purinoceptor 7 (P2RX7) TT473XN UP Q99572 TT473XN UC P2RX7_HUMAN TT473XN BC ATP-gated P2X receptor cation channel TT473XN SN Purinergic receptor 7; P2Z receptor; P2X7; Adenosine P2X7 receptor; ATP receptor TT473XN GN P2RX7 TT473XN FC Responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Could function in both fast synaptic transmission and the ATP-mediated lysis of antigen-presenting cells. In the absence of its natural ligand, ATP, functions as a scavenger receptor in the recognition and engulfment of apoptotic cells. Receptor for ATP that acts as a ligand-gated ion channel. TT473XN SQ MPACCSCSDVFQYETNKVTRIQSMNYGTIKWFFHVIIFSYVCFALVSDKLYQRKEPVISSVHTKVKGIAEVKEEIVENGVKKLVHSVFDTADYTFPLQGNSFFVMTNFLKTEGQEQRLCPEYPTRRTLCSSDRGCKKGWMDPQSKGIQTGRCVVYEGNQKTCEVSAWCPIEAVEEAPRPALLNSAENFTVLIKNNIDFPGHNYTTRNILPGLNITCTFHKTQNPQCPIFRLGDIFRETGDNFSDVAIQGGIMGIEIYWDCNLDRWFHHCRPKYSFRRLDDKTTNVSLYPGYNFRYAKYYKENNVEKRTLIKVFGIRFDILVFGTGGKFDIIQLVVYIGSTLSYFGLAAVFIDFLIDTYSSNCCRSHIYPWCKCCQPCVVNEYYYRKKCESIVEPKPTLKYVSFVDESHIRMVNQQLLGRSLQDVKGQEVPRPAMDFTDLSRLPLALHDTPPIPGQPEEIQLLRKEATPRSRDSPVWCQCGSCLPSQLPESHRCLEELCCRKKPGACITTSELFRKLVLSRHVLQFLLLYQEPLLALDVDSTNSRLRHCAYRCYATWRFGSQDMADFAILPSCCRWRIRKEFPKSEGQYSGFKSPY TT473XN TT Clinical trial TT473XN FM ATP-gated P2X receptor cation channel TT473XN KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TT473XN RC R-HSA-844456:The NLRP3 inflammasome TTNVSKA ID TTNVSKA TTNVSKA TN P2Y purinoceptor 6 (P2RY6) TTNVSKA UP Q15077 TTNVSKA UC P2RY6_HUMAN TTNVSKA BC GPCR rhodopsin TTNVSKA SN P2Y6; P2RY6; Adenosine P2Y6 receptor TTNVSKA GN P2RY6 TTNVSKA FC Receptor for extracellular UDP > UTP > ATP. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. TTNVSKA PD 2B6R TTNVSKA SQ MEWDNGTGQALGLPPTTCVYRENFKQLLLPPVYSAVLAAGLPLNICVITQICTSRRALTRTAVYTLNLALADLLYACSLPLLIYNYAQGDHWPFGDFACRLVRFLFYANLHGSILFLTCISFQRYLGICHPLAPWHKRGGRRAAWLVCVAVWLAVTTQCLPTAIFAATGIQRNRTVCYDLSPPALATHYMPYGMALTVIGFLLPFAALLACYCLLACRLCRQDGPAEPVAQERRGKAARMAVVVAAAFAISFLPFHITKTAYLAVRSTPGVPCTVLEAFAAAYKGTRPFASANSVLDPILFYFTQKKFRRRPHELLQKLTAKWQRQGR TTNVSKA TT Clinical trial TTNVSKA KE hsa04080:Neuroactive ligand-receptor interaction TTNVSKA RC R-HSA-416476:G alpha (q) signalling events; R-HSA-417957:P2Y receptors TT12KOD ID TT12KOD TT12KOD TN P53 messenger RNA (TP53 mRNA) TT12KOD UP P04637 TT12KOD UC P53_HUMAN TT12KOD BC mRNA target TT12KOD SN Tumor suppressor p53 (mRNA); Phosphoprotein p53 (mRNA); P53 (mRNA); Antigen NY-CO-13 (mRNA) TT12KOD GN TP53 TT12KOD FC Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2. Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. TT12KOD PD 6GGF; 6GGE; 6GGD; 6GGC; 6GGB TT12KOD SQ MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD TT12KOD TT Clinical trial TT12KOD FM mRNA target TT12KOD KE hsa04010:MAPK signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04310:Wnt signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05016:Huntington's disease; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05217:Basal cell carcinoma; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer TT12KOD RC R-HSA-111448:Activation of NOXA and translocation to mitochondria; R-HSA-139915:Activation of PUMA and translocation to mitochondria; R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559584:Formation of Senescence-Associated Heterochromatin Foci (SAHF); R-HSA-2559585:Oncogene Induced Senescence; R-HSA-2559586:DNA Damage/Telomere Stress Induced Senescence; R-HSA-349425:Autodegradation of the E3 ubiquitin ligase COP1; R-HSA-5628897:TP53 Regulates Metabolic Genes; R-HSA-5693565:Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks; R-HSA-69541:Stabilization of p53; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TT7Y3BZ ID TT7Y3BZ TT7Y3BZ TN PAK-4 protein kinase (PAK4) TT7Y3BZ UP O96013 TT7Y3BZ UC PAK4_HUMAN TT7Y3BZ BC Kinase TT7Y3BZ SN p21-activated kinase 4; Serine/threonine-protein kinase PAK 4; PAK-4; KIAA1142 TT7Y3BZ GN PAK4 TT7Y3BZ FC Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN. Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. TT7Y3BZ EC EC 2.7.11.1 TT7Y3BZ PD 5ZJW; 5XVG; 5XVF; 5XVA; 5VEF TT7Y3BZ SQ MFGKRKKRVEISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESARRPKPLVDPACITSIQPGAPKTIVRGSKGAKDGALTLLLDEFENMSVTRSNSLRRDSPPPPARARQENGMPEEPATTARGGPGKAGSRGRFAGHSEAGGGSGDRRRAGPEKRPKSSREGSGGPQESSRDKRPLSGPDVGTPQPAGLASGAKLAAGRPFNTYPRADTDHPSRGAQGEPHDVAPNGPSAGGLAIPQSSSSSSRPPTRARGAPSPGVLGPHASEPQLAPPACTPAAPAVPGPPGPRSPQREPQRVSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR TT7Y3BZ TT Clinical trial TT7Y3BZ FM Kinase TT7Y3BZ KE hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04360:Axon guidance; hsa04510:Focal adhesion; hsa04660:T cell receptor signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma TTCUS9F ID TTCUS9F TTCUS9F TN Phosphatidylinositol-4-kinase alpha (PI4KA) TTCUS9F UP P42356 TTCUS9F UC PI4KA_HUMAN TTCUS9F BC PI3/PI4-kinase family. Type III PI4K subfamily TTCUS9F SN PtdIns-4-kinase alpha; PI4K-alpha; PI4-kinase alpha TTCUS9F GN PI4KA TTCUS9F FC Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate. TTCUS9F EC EC 2.7.1.67 TTCUS9F PD 6BQ1 TTCUS9F SQ MAAAPARGGGGGGGGGGGCSGSGSSASRGFYFNTVLSLARSLAVQRPASLEKVQKLLCMCPVDFHGIFQLDERRRDAVIALGIFLIESDLQHKDCVVPYLLRLLKGLPKVYWVEESTARKGRGALPVAESFSFCLVTLLSDVAYRDPSLRDEILEVLLQVLHVLLGMCQALEIQDKEYLCKYAIPCLIGISRAFGRYSNMEESLLSKLFPKIPPHSLRVLEELEGVRRRSFNDFRSILPSNLLTVCQEGTLKRKTSSVSSISQVSPERGMPPPSSPGGSAFHYFEASCLPDGTALEPEYYFSTISSSFSVSPLFNGVTYKEFNIPLEMLRELLNLVKKIVEEAVLKSLDAIVASVMEANPSADLYYTSFSDPLYLTMFKMLRDTLYYMKDLPTSFVKEIHDFVLEQFNTSQGELQKILHDADRIHNELSPLKLRCQANAACVDLMVWAVKDEQGAENLCIKLSEKLQSKTSSKVIIAHLPLLICCLQGLGRLCERFPVVVHSVTPSLRDFLVIPSPVLVKLYKYHSQYHTVAGNDIKISVTNEHSESTLNVMSGKKSQPSMYEQLRDIAIDNICRCLKAGLTVDPVIVEAFLASLSNRLYISQESDKDAHLIPDHTIRALGHIAVALRDTPKVMEPILQILQQKFCQPPSPLDVLIIDQLGCLVITGNQYIYQEVWNLFQQISVKASSVVYSATKDYKDHGYRHCSLAVINALANIAANIQDEHLVDELLMNLLELFVQLGLEGKRASERASEKGPALKASSSAGNLGVLIPVIAVLTRRLPPIKEAKPRLQKLFRDFWLYSVLMGFAVEGSGLWPEEWYEGVCEIATKSPLLTFPSKEPLRSVLQYNSAMKNDTVTPAELSELRSTIINLLDPPPEVSALINKLDFAMSTYLLSVYRLEYMRVLRSTDPDRFQVMFCYFEDKAIQKDKSGMMQCVIAVADKVFDAFLNMMADKAKTKENEEELERHAQFLLVNFNHIHKRIRRVADKYLSGLVDKFPHLLWSGTVLKTMLDILQTLSLSLSADIHKDQPYYDIPDAPYRITVPDTYEARESIVKDFAARCGMILQEAMKWAPTVTKSHLQEYLNKHQNWVSGLSQHTGLAMATESILHFAGYNKQNTTLGATQLSERPACVKKDYSNFMASLNLRNRYAGEVYGMIRFSGTTGQMSDLNKMMVQDLHSALDRSHPQHYTQAMFKLTAMLISSKDCDPQLLHHLCWGPLRMFNEHGMETALACWEWLLAGKDGVEVPFMREMAGAWHMTVEQKFGLFSAEIKEADPLAASEASQPKPCPPEVTPHYIWIDFLVQRFEIAKYCSSDQVEIFSSLLQRSMSLNIGGAKGSMNRHVAAIGPRFKLLTLGLSLLHADVVPNATIRNVLREKIYSTAFDYFSCPPKFPTQGEKRLREDISIMIKFWTAMFSDKKYLTASQLVPPDNQDTRSNLDITVGSRQQATQGWINTYPLSSGMSTISKKSGMSKKTNRGSQLHKYYMKRRTLLLSLLATEIERLITWYNPLSAPELELDQAGENSVANWRSKYISLSEKQWKDNVNLAWSISPYLAVQLPARFKNTEAIGNEVTRLVRLDPGAVSDVPEAIKFLVTWHTIDADAPELSHVLCWAPTDPPTGLSYFSSMYPPHPLTAQYGVKVLRSFPPDAILFYIPQIVQALRYDKMGYVREYILWAASKSQLLAHQFIWNMKTNIYLDEEGHQKDPDIGDLLDQLVEEITGSLSGPAKDFYQREFDFFNKITNVSAIIKPYPKGDERKKACLSALSEVKVQPGCYLPSNPEAIVLDIDYKSGTPMQSAAKAPYLAKFKVKRCGVSELEKEGLRCRSDSEDECSTQEADGQKISWQAAIFKVGDDCRQDMLALQIIDLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCTSRDQLGRQTDFGMYDYFTRQYGDESTLAFQQARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDKKGHIIHIDFGFMFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLVTLMLDTGLPCFRGQTIKLLKHRFSPNMTEREAANFIMKVIQSCFLSNRSRTYDMIQYYQNDIPY TTCUS9F TT Literature-reported TTCUS9F KE hsa00562:Inositol phosphate metabolism; hsa01100:Metabolic pathways; hsa04070:Phosphatidylinositol signaling system TT9QBI6 ID TT9QBI6 TT9QBI6 TN Phosphoinositide dependent protein kinase-1 (PDPK1) TT9QBI6 UP O15530 TT9QBI6 UC PDPK1_HUMAN TT9QBI6 BC Kinase TT9QBI6 SN PDK1; HPDK1; 3-phosphoinositide-dependent protein kinase 1; 3-Phosphoinositide-dependent kinase-1; 3'-phosphoinositide dependent kinase 1 TT9QBI6 GN PDPK1 TT9QBI6 FC Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. Isoform 3 is catalytically inactive. Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. TT9QBI6 EC EC 2.7.11.1 TT9QBI6 PD 5MRD; 5LVP; 5LVO; 5LVN; 5LVM TT9QBI6 SQ MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ TT9QBI6 TT Clinical trial TT9QBI6 FM Kinase TT9QBI6 KE hsa03320:PPAR signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04510:Focal adhesion; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04910:Insulin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04960:Aldosterone-regulated sodium reabsorption; hsa05145:Toxoplasmosis; hsa05160:Hepatitis C; hsa05205:Proteoglycans in cancer; hsa05213:Endometrial cancer; hsa05215:Prostate cancer; hsa05223:Non-small cell lung cancer; hsa05231:Choline metabolism in cancer TT9QBI6 RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-165158:Activation of AKT2; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-5218920:VEGFR2 mediated vascular permeability; R-HSA-5218921:VEGFR2 mediated cell proliferation; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-5625740:RHO GTPases activate PKNs; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer TTN0PCX ID TTN0PCX TTN0PCX TN Plasma kallikrein messenger RNA (KLKB1 mRNA) TTN0PCX UP P03952 TTN0PCX UC KLKB1_HUMAN TTN0PCX BC mRNA target TTN0PCX SN Plasma prekallikrein (mRNA); Plasma kallikrein light chain (mRNA); Plasma kallikrein heavy chain (mRNA); PKK (mRNA); Kininogenin (mRNA); KLK3 (mRNA); Fletcher factor (mRNA) TTN0PCX GN KLKB1 TTN0PCX FC It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin. The enzyme cleaves Lys-Arg and Arg-Ser bonds. TTN0PCX EC EC 3.4.21.34 TTN0PCX PD 6O1S; 6O1G; 6I44; 5TJX; 5F8Z TTN0PCX SQ MILFKQATYFISLFATVSCGCLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDMEKRFGCFLKDSVTGTLPKVHRTGAVSGHSLKQCGHQISACHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTNNIRCQFFSYATQTFHKAEYRNNCLLKYSPGGTPTAIKVLSNVESGFSLKPCALSEIGCHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKIESQRNVCLLKTSESGTPSSSTPQENTISGYSLLTCKRTLPEPCHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSLLPEDCKEEKCKCFLRLSMDGSPTRIAYGTQGSSGYSLRLCNTGDNSVCTTKTSTRIVGGTNSSWGEWPWQVSLQVKLTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDVWRIYSGILNLSDITKDTPFSQIKEIIIHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGEIQNILQKVNIPLVTNEECQKRYQDYKITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWILEKTQSSDGKAQMQSPA TTN0PCX TT Clinical trial TTN0PCX FM mRNA target TTN0PCX KE hsa04610:Complement and coagulation cascades TTN0PCX RC R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-1592389:Activation of Matrix Metalloproteinases TTH4IP0 ID TTH4IP0 TTH4IP0 TN PLK1 messenger RNA (PLK1 mRNA) TTH4IP0 UP P53350 TTH4IP0 UC PLK1_HUMAN TTH4IP0 BC mRNA target TTH4IP0 SN Serine/threonine-protein kinase PLK1 (mRNA); Serine/threonine-protein kinase 13 (mRNA); Serine-threonine protein kinase 13 (mRNA); STPK13 (mRNA); Plk1 (mRNA); PLK-1 (mRNA); PLK (mRNA); Mitoticserine-threonine kinase polo-like kinase 1 (mRNA) TTH4IP0 GN PLK1 TTH4IP0 FC Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning. Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage. Phosphorylates CEP68 and is required for its degradation. Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope. Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock. Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression. Regulates mitotic progression by phosphorylating RIOK2. Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. TTH4IP0 EC EC 2.7.11.21 TTH4IP0 PD 6AX4; 5TA8; 5TA6; 5NN2; 5NN1 TTH4IP0 SQ MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERPREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS TTH4IP0 TT Clinical trial TTH4IP0 FM mRNA target TTH4IP0 KE hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04114:Oocyte meiosis; hsa04914:Progesterone-mediated oocyte maturation TTH4IP0 RC R-HSA-156711:Polo-like kinase mediated events; R-HSA-162658:Golgi Cisternae Pericentriolar Stack Reorganization; R-HSA-174178:APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1; R-HSA-176412:Phosphorylation of the APC/C; R-HSA-176417:Phosphorylation of Emi1; R-HSA-2299718:Condensation of Prophase Chromosomes; R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-2565942:Regulation of PLK1 Activity at G2/M Transition; R-HSA-2980767:Activation of NIMA Kinases NEK9, NEK6, NEK7; R-HSA-380259:Loss of Nlp from mitotic centrosomes; R-HSA-380270:Recruitment of mitotic centrosome proteins and complexes; R-HSA-380284:Loss of proteins required for interphase microtubule organization?from the centrosome; R-HSA-5620912:Anchoring of the basal body to the plasma membrane; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-68877:Mitotic Prometaphase; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition TTT0HW3 ID TTT0HW3 TTT0HW3 TN Porphobilinogen deaminase (HMBS) TTT0HW3 UP P08397 TTT0HW3 UC HEM3_HUMAN TTT0HW3 BC Alkyl aryl transferase TTT0HW3 SN Preuroporphyrinogen synthase; PBGD; Hydroxymethylbilane synthase; HMBS TTT0HW3 GN HMBS TTT0HW3 FC Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. TTT0HW3 EC EC 2.5.1.61 TTT0HW3 PD 5M7F; 5M6R; 3EQ1; 3ECR TTT0HW3 SQ MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTGDKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHDPETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIHVPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDAH TTT0HW3 TT Clinical trial TTT0HW3 KE hsa00860:Porphyrin and chlorophyll metabolism; hsa01100:Metabolic pathways TTWN3F4 ID TTWN3F4 TTWN3F4 TN Presenilin 2 (PSEN2) TTWN3F4 UP P49810 TTWN3F4 UC PSN2_HUMAN TTWN3F4 BC Peptidase TTWN3F4 SN STM2; STM-2; Presenilin-2; PSNL2; PS-2; E5-1; AD5; AD4; AD3LP TTWN3F4 GN PSEN2 TTWN3F4 FC Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is involved in calcium homeostasis. Is a regulator of mitochondrion-endoplasmic reticulum membrane tethering and modulates calcium ions shuttling between ER and mitochondria. Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). TTWN3F4 EC EC 3.4.23.- TTWN3F4 SQ MLTFMASDSEEEVCDERTSLMSAESPTPRSCQEGRQGPEDGENTAQWRSQENEEDGEEDPDRYVCSGVPGRPPGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLLLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPEVFEPPLTGYPGEELEEEEERGVKLGLGDFIFYSVLVGKAAATGSGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI TTWN3F4 TT Clinical trial TTWN3F4 FM Peptidase TTWN3F4 KE hsa04330:Notch signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa05010:Alzheimer's disease TTWN3F4 RC R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-193692:Regulated proteolysis of p75NTR; R-HSA-205043:NRIF signals cell death from the nucleus; R-HSA-2122948:Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-2979096:NOTCH2 Activation and Transmission of Signal to the Nucleus; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TT9PB26 ID TT9PB26 TT9PB26 TN Presynaptic density protein 95 (DLG4) TT9PB26 UP P78352 TT9PB26 UC DLG4_HUMAN TT9PB26 BC Ezrin/radixin/moesin-binding phosphoprotein 50 TT9PB26 SN Synapse-associated protein 90; SAP90; SAP-90; Postsynaptic density-95; Postsynaptic density protein 95; PSD95; PSD-95; Disks large homolog 4; Discs, large homolog 4 TT9PB26 GN DLG4 TT9PB26 FC Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B. Also regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression. Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. TT9PB26 PD 6QJN; 6QJL; 6QJK; 6QJJ; 6QJI TT9PB26 SQ MDCLCIVTTKKYRYQDEDTPPLEHSPAHLPNQANSPPVIVNTDTLEAPGYELQVNGTEGEMEYEEITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFVNEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKVMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVYLKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAKDLLGEEDIPREPRRIVIHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDQILSVNGVDLRNASHEQAAIALKNAGQTVTIIAQYKPEEYSRFEAKIHDLREQLMNSSLGSGTASLRSNPKRGFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDASDEEWWQARRVHSDSETDDIGFIPSKRRVERREWSRLKAKDWGSSSGSQGREDSVLSYETVTQMEVHYARPIIILGPTKDRANDDLLSEFPDKFGSCVPHTTRPKREYEIDGRDYHFVSSREKMEKDIQAHKFIEAGQYNSHLYGTSVQSVREVAEQGKHCILDVSANAVRRLQAAHLHPIAIFIRPRSLENVLEINKRITEEQARKAFDRATKLEQEFTECFSAIVEGDSFEEIYHKVKRVIEDLSGPYIWVPARERL TT9PB26 TT Clinical trial TT9PB26 KE hsa04390:Hippo signaling pathway; hsa04724:Glutamatergic synapse; hsa05016:Huntington's disease; hsa05030:Cocaine addiction TT9PB26 RC R-HSA-399719:Trafficking of AMPA receptors; R-HSA-438066:Unblocking of NMDA receptor, glutamate binding and activation; R-HSA-442729:CREB phosphorylation through the activation of CaMKII; R-HSA-442982:Ras activation uopn Ca2+ infux through NMDA receptor; R-HSA-5625900:RHO GTPases activate CIT; R-HSA-5673001:RAF/MAP kinase cascade TT15SL0 ID TT15SL0 TT15SL0 TN Proheparin-binding EGF-like growth factor (HBEGF) TT15SL0 UP Q99075 TT15SL0 UC HBEGF_HUMAN TT15SL0 BC Growth factor TT15SL0 SN Proheparinbinding EGFlike growth factor; Heparinbinding EGFlike growth factor; Heparin-binding EGF-like growth factor; HEGFL; HB-EGF; Diphtheria toxin receptor; DTS; DTR; DT-R TT15SL0 GN HBEGF TT15SL0 FC Required for normal cardiac valve formation and normal heart function. Promotes smooth muscle cell proliferation. May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts, but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor. Growth factor that mediates its effects via EGFR, ERBB2 and ERBB4. TT15SL0 PD 2M8S; 1XDT TT15SL0 SQ MKLLPSVVLKLFLAAVLSALVTGESLERLRRGLAAGTSNPDPPTVSTDQLLPLGGGRDRKVRDLQEADLDLLRVTLSSKPQALATPNKEEHGKRKKKGKGLGKKRDPCLRKYKDFCIHGECKYVKELRAPSCICHPGYHGERCHGLSLPVENRLYTYDHTTILAVVAVVLSSVCLLVIVGLLMFRYHRRGGYDVENEEKVKLGMTNSH TT15SL0 TT Clinical trial TT15SL0 FM Growth factor TT15SL0 KE hsa04012:ErbB signaling pathway; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05205:Proteoglycans in cancer TT15SL0 RC R-HSA-1250196:SHC1 events in ERBB2 signaling; R-HSA-1250342:PI3K events in ERBB4 signaling; R-HSA-1250347:SHC1 events in ERBB4 signaling; R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1963640:GRB2 events in ERBB2 signaling; R-HSA-1963642:PI3K events in ERBB2 signaling; R-HSA-2179392:EGFR Transactivation by Gastrin; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5673001:RAF/MAP kinase cascade TTNVEIR ID TTNVEIR TTNVEIR TN Prostaglandin D2 receptor (PTGDR) TTNVEIR UP Q13258 TTNVEIR UC PD2R_HUMAN TTNVEIR BC GPCR rhodopsin TTNVEIR SN Prostanoid DP receptor; PGD2 receptor; PGD receptor TTNVEIR GN PTGDR TTNVEIR FC The activity of this receptor is mainly mediated by G(s) proteins that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP. A mobilization of calcium is also observed, but without formation of inositol 1,4,5-trisphosphate. Receptor for prostaglandin D2 (PGD2). TTNVEIR SQ MKSPFYRCQNTTSVEKGNSAVMGGVLFSTGLLGNLLALGLLARSGLGWCSRRPLRPLPSVFYMLVCGLTVTDLLGKCLLSPVVLAAYAQNRSLRVLAPALDNSLCQAFAFFMSFFGLSSTLQLLAMALECWLSLGHPFFYRRHITLRLGALVAPVVSAFSLAFCALPFMGFGKFVQYCPGTWCFIQMVHEEGSLSVLGYSVLYSSLMALLVLATVLCNLGAMRNLYAMHRRLQRHPRSCTRDCAEPRADGREASPQPLEELDHLLLLALMTVLFTMCSLPVIYRAYYGAFKDVKEKNRTSEEAEDLRALRFLSVISIVDPWIFIIFRSPVFRIFFHKIFIRPLRYRSRCSNSTNMESSL TTNVEIR TT Clinical trial TTNVEIR FM GPCR rhodopsin TTNVEIR KE hsa04080:Neuroactive ligand-receptor interaction TTNVEIR RC R-HSA-391908:Prostanoid ligand receptors; R-HSA-418555:G alpha (s) signalling events TTLA7IX ID TTLA7IX TTLA7IX TN Protein phosphatase 1A (PPM1A) TTLA7IX UP P35813 TTLA7IX UC PPM1A_HUMAN TTLA7IX BC PP2C family TTLA7IX SN Protein phosphatase IA; Protein phosphatase 2C isoform alpha; PP2C-alpha TTLA7IX GN PPM1A TTLA7IX FC Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. TTLA7IX EC EC 3.1.3.16 TTLA7IX PD 6B67; 4RAG; 4RAF; 4RA2; 3FXO TTLA7IX SQ MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLESWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSPEAVKKEAELDKYLECRVEEIIKKQGEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSTSTDDMW TTLA7IX TT Clinical trial TTLA7IX KE hsa04010:MAPK signaling pathway TTB18GJ ID TTB18GJ TTB18GJ TN Proto-oncogene c-RAF (c-RAF) TTB18GJ UP P04049 TTB18GJ UC RAF1_HUMAN TTB18GJ BC Kinase TTB18GJ SN cRaf; Raf-1; RAF proto-oncogene serine/threonine-protein kinase; RAF TTB18GJ GN RAF1 TTB18GJ FC RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. TTB18GJ EC EC 2.7.11.1 TTB18GJ PD 4IHL; 4IEA; 4G3X; 4G0N; 4FJ3 TTB18GJ SQ MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF TTB18GJ TT Clinical trial TTB18GJ FM Kinase TTE5VG0 ID TTE5VG0 TTE5VG0 TN P-selectin (SELP) TTE5VG0 UP P16109 TTE5VG0 UC LYAM3_HUMAN TTE5VG0 SN SELP; PADGEM; Leukocyte-endothelial cell adhesion molecule 3; LECAM3; Granule membrane protein 140; GMP-140; CD62P TTE5VG0 GN SELP TTE5VG0 FC Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1. TTE5VG0 PD 1KJD; 1HES; 1G1S; 1G1R; 1G1Q TTE5VG0 SQ MANCQIAILYQRFQRVVFGISQLLCFSALISELTNQKEVAAWTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGIRKNNKTWTWVGTKKALTNEAENWADNEPNNKRNNEDCVEIYIKSPSAPGKWNDEHCLKKKHALCYTASCQDMSCSKQGECLETIGNYTCSCYPGFYGPECEYVRECGELELPQHVLMNCSHPLGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQCLAAQCPPLKIPERGNMTCLHSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVCKAVQCQHLEAPSEGTMDCVHPLTAFAYGSSCKFECQPGYRVRGLDMLRCIDSGHWSAPLPTCEAISCEPLESPVHGSMDCSPSLRAFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVCQALQCQDLPVPNEARVNCSHPFGAFRYQSVCSFTCNEGLLLVGASVLQCLATGNWNSVPPECQAIPCTPLLSPQNGTMTCVQPLGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMCEAIKCPELFAPEQGSLDCSDTRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTCKGIASLPTPGLQCPALTTPGQGTMYCRHHPGTFGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPACRAVKCSELHVNKPIAMNCSNLWGNFSYGSICSFHCLEGQLLNGSAQTACQENGHWSTTVPTCQAGPLTIQEALTYFGGAVASTIGLIMGGTLLALLRKRFRQKDDGKCPLNPHSHLGTYGVFTNAAFDPSP TTE5VG0 TT Successful TTE5VG0 KE hsa04514:Cell adhesion molecules (CAMs); hsa05144:Malaria; hsa05150:Staphylococcus aureus infection TTE5VG0 RC R-HSA-114608:Platelet degranulation; R-HSA-202733:Cell surface interactions at the vascular wall TTAN5W2 ID TTAN5W2 TTAN5W2 TN Raf messenger RNA (Raf mRNA) TTAN5W2 UP P04049 TTAN5W2 UC RAF1_HUMAN TTAN5W2 BC mRNA target TTAN5W2 SN cRaf (mRNA); Raf-1 (mRNA); RAF proto-oncogene serine/threonine-protein kinase (mRNA); RAF (mRNA) TTAN5W2 GN RAF1 TTAN5W2 FC RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. TTAN5W2 EC EC 2.7.11.1 TTAN5W2 PD 4IHL; 4IEA; 4G3X; 4G0N; 4FJ3 TTAN5W2 SQ MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF TTAN5W2 TT Clinical trial TTAN5W2 FM mRNA target TTAN5W2 KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04370:VEGF signaling pathway; hsa04510:Focal adhesion; hsa04540:Gap junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05034:Alcoholism; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTAN5W2 RC R-HSA-2672351:Stimuli-sensing channels; R-HSA-430116:GP1b-IX-V activation signalling; R-HSA-442742:CREB phosphorylation through the activation of Ras; R-HSA-5621575:CD209 (DC-SIGN) signaling; R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5674499:Negative feedback regulation of MAPK pathway; R-HSA-5675221:Negative regulation of MAPK pathway TTAZF9M ID TTAZF9M TTAZF9M TN RAS-like protein KIR (GEM) TTAZF9M UP P55040 TTAZF9M UC GEM_HUMAN TTAZF9M BC Small GTPase superfamily TTAZF9M SN RASlike protein KIR; GTPbinding protein GEM; GTPbinding mitogeninduced Tcell protein TTAZF9M GN GEM TTAZF9M FC Could be a regulatory protein, possibly participating in receptor-mediated signal transduction at the plasma membrane. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity. TTAZF9M PD 2HT6; 2G3Y; 2CJW TTAZF9M SQ MTLNNVTMRQGTVGMQPQQQRWSIPADGRHLMVQKEPHQYSHRNRHSATPEDHCRRSWSSDSTDSVISSESGNTYYRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGEDTYERTLMVDGESATIILLDMWENKGENEWLHDHCMQVGDAYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIVRQVRLRRDSKEKNERRLAYQKRKESMPRKARRFWGKIVAKNNKNMAFKLKSKSCHDLSVL TTAZF9M TT Clinical trial TTKFVXR ID TTKFVXR TTKFVXR TN Renal carcinoma antigen NY-REN-64 (IRAK-4) TTKFVXR UP Q9NWZ3 TTKFVXR UC IRAK4_HUMAN TTKFVXR BC Kinase TTKFVXR SN Interleukin-1 receptor-associated kinase 4; IRAK-4 TTKFVXR GN IRAK4 TTKFVXR FC Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections. TTKFVXR EC EC 2.7.11.1 TTKFVXR PD 6O9D; 6O95; 6O94; 6O8U; 6N8G TTKFVXR SQ MNKPITPSTYVRCLNVGLIRKLSDFIDPQEGWKKLAVAIKKPSGDDRYNQFHIRRFEALLQTGKSPTSELLFDWGTTNCTVGDLVDLLIQNEFFAPASLLLPDAVPKTANTLPSKEAITVQQKQMPFCDKDRTLMTPVQNLEQSYMPPDSSSPENKSLEVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS TTKFVXR TT Clinical trial TTKFVXR FM Kinase TTKFVXR RC R-HSA-166058:MyD88:Mal cascade initiated on plasma membrane; R-HSA-446652:Interleukin-1 signaling; R-HSA-5602498:MyD88 deficiency (TLR2/4); R-HSA-5602680:MyD88 deficiency (TLR5); R-HSA-5603037:IRAK4 deficiency (TLR5); R-HSA-5603041:IRAK4 deficiency (TLR2/4); R-HSA-975110:TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling; R-HSA-975138:TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation; R-HSA-975155:MyD88 dependent cascade initiated on endosome; R-HSA-975871:MyD88 cascade initiated on plasma membrane TTVB0O3 ID TTVB0O3 TTVB0O3 TN Retinoic acid-inducible gene-1 (RIG-1) TTVB0O3 UP O95786 TTVB0O3 UC DDX58_HUMAN TTVB0O3 BC Acid anhydride hydrolase TTVB0O3 SN Retinoic acidinducible gene I protein; Retinoic acidinducible gene 1 protein; Retinoic acid-inducible gene I protein; Retinoic acid-inducible gene 1 protein; RLR1; RLR-1; RIGIlike receptor 1; RIGI; RIG1; RIG-I-like receptor 1; RIG-I; Probable ATPdependent RNA helicase DDX58; Probable ATP-dependent RNA helicase DDX58; DEAD box protein 58 TTVB0O3 GN DDX58 TTVB0O3 FC Its ligands include: 5'-triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotavirus and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration. Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. TTVB0O3 EC EC 3.6.4.13 TTVB0O3 PD 6GPG; 5F9H; 5F9F; 5F98; 5E3H TTVB0O3 SQ MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKERNKFSELWIVEKGIKDVETEDLEDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSPFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATVKHNLEELEQVVYKPQKFFRKVESRISDKFKYIIAQLMRDTESLAKRICKDLENLSQIQNREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFLYTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPKLSFLKPGILTGRGKTNQNTGMTLPAQKCILDAFKASGDHNILIATSVADEGIDIAQCNLVILYEYVGNVIKMIQTRGRGRARGSKCFLLTSNAGVIEKEQINMYKEKMMNDSILRLQTWDEAVFREKILHIQTHEKFIRDSQEKPKPVPDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPFDPAEMSK TTVB0O3 TT Clinical trial TTVB0O3 FM Acid anhydrides hydrolase TTVB0O3 KE hsa04064:NF-kappa B signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection TTVB0O3 RC R-HSA-1169408:ISG15 antiviral mechanism; R-HSA-918233:TRAF3-dependent IRF activation pathway; R-HSA-933541:TRAF6 mediated IRF7 activation; R-HSA-933542:TRAF6 mediated NF-kB activation; R-HSA-933543:NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10; R-HSA-936440:Negative regulators of RIG-I/MDA5 signaling TTVEOY6 ID TTVEOY6 TTVEOY6 TN RTP801 messenger RNA (RTP801 mRNA) TTVEOY6 UP Q9NX09 TTVEOY6 UC DDIT4_HUMAN TTVEOY6 BC mRNA target TTVEOY6 SN RTP801 (mRNA); REDD1 (mRNA); REDD-1 (mRNA); Protein regulated in development and DNA damage response 1 (mRNA); HIF-1 responsive protein RTP801 (mRNA); DNA damage-inducible transcript 4 protein (mRNA) TTVEOY6 GN DDIT4 TTVEOY6 FC Inhibition of mTORC1 is mediated by a pathway that involves DDIT4/REDD1, AKT1, the TSC1-TSC2 complex and the GTPase RHEB. Plays an important role in responses to cellular energy levels and cellular stress, including responses to hypoxia and DNA damage. Regulates p53/TP53-mediated apoptosis in response to DNA damage via its effect on mTORC1 activity. Its role in the response to hypoxia depends on the cell type; it mediates mTORC1 inhibition in fibroblasts and thymocytes, but not in hepatocytes. Required for mTORC1-mediated defense against viral protein synthesis and virus replication. Inhibits neuronal differentiation and neurite outgrowth mediated by NGF via its effect on mTORC1 activity. Required for normal neuron migration during embryonic brain development. Plays a role in neuronal cell death. Regulates cell growth, proliferation and survival via inhibition of the activity of the mammalian target of rapamycin complex 1 (mTORC1). TTVEOY6 PD 3LQ9 TTVEOY6 SQ MPSLWDRFSSSSTSSSPSSLPRTPTPDRPPRSAWGSATREEGFDRSTSLESSDCESLDSSNSGFGPEEDTAYLDGVSLPDFELLSDPEDEHLCANLMQLLQESLAQARLGSRRPARLLMPSQLVSQVGKELLRLAYSEPCGLRGALLDVCVEQGKSCHSVGQLALDPSLVPTFQLTLVLRLDSRLWPKIQGLFSSANSPFLPGFSQSLTLSTGFRVIKKKLYSSEQLLIEEC TTVEOY6 TT Clinical trial TTVEOY6 FM mRNA target TTVEOY6 KE hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa05206:MicroRNAs in cancer TTVEOY6 RC R-HSA-5628897:TP53 Regulates Metabolic Genes TTSMPXQ ID TTSMPXQ TTSMPXQ TN S-adenosylmethionine synthase type-2 (MAT2A) TTSMPXQ UP P31153 TTSMPXQ UC METK2_HUMAN TTSMPXQ BC AdoMet synthase family TTSMPXQ SN Methionine adenosyltransferase II; Methionine adenosyltransferase 2; MAT-II; MAT 2; AdoMet synthase 2 TTSMPXQ GN MAT2A TTSMPXQ FC Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. TTSMPXQ EC EC 2.5.1.6 TTSMPXQ PD 6G6R; 6FWB; 6FCD; 6FCB; 6FBP TTSMPXQ SQ MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY TTSMPXQ TT Clinical trial TTSMPXQ KE hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways; hsa01230:Biosynthesis of amino acids TTE6THL ID TTE6THL TTE6THL TN Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (ATP2A2) TTE6THL UP P16615 TTE6THL UC AT2A2_HUMAN TTE6THL BC Cation transporting ATPase TTE6THL SN SR Ca(2+)Sarcoplasmic/endoplasmic reticulum calcium ATPase 2-ATPase 2; SR Ca(2+)-ATPase 2; SR Ca(2+)-ATPase; SR Ca(2+) pump; SERCA2; Endoplasmic reticulum class 1/2 Ca(2+) ATPase; Cardiacsarcoplasmic reticulum calcium ATPase; CardiacCa2+ ATPase (SERCA2a); Calciumpump 2; Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform; Calcium pump 2; ATP2B TTE6THL GN ATP2A2 TTE6THL FC Isoform 2 is involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation. This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. TTE6THL EC EC 7.2.2.10 TTE6THL PD 6JJU; 5ZTF TTE6THL SQ MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDRVEGDTCSLNEFTITGSTYAPIGEVHKDDKPVNCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTSGVKQKIMSVIREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELNPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNVTQWLMVLKISLPVILMDETLKFVARNYLEPGKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS TTE6THL TT Clinical trial TTE6THL FM Acid anhydrides hydrolase TTE6THL KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04919:Thyroid hormone signaling pathway; hsa04972:Pancreatic secretion; hsa05010:Alzheimer's disease; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTE6THL RC R-HSA-1912420:Pre-NOTCH Processing in Golgi; R-HSA-936837:Ion transport by P-type ATPases TTLSW9V ID TTLSW9V TTLSW9V TN Scavenger decapping enzyme DcpS (DCPS) TTLSW9V UP Q96C86 TTLSW9V UC DCPS_HUMAN TTLSW9V BC Acid anhydrides hydrolase TTLSW9V SN Scavenger mRNA-decapping enzyme DcpS; Histidine triad protein member5; Hint-related 7meGMP-directed hydrolase; HINT-5; DCS-1; DCPS TTLSW9V GN DCPS TTLSW9V FC Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre- mRNAs. Inhibits activation-induced cell death. TTLSW9V EC EC 3.6.1.59 TTLSW9V PD 5OSY; 4QEB; 4QDV; 4QDE; 3BLA TTLSW9V SQ MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS TTLSW9V TT Clinical trial TTLSW9V KE hsa03018:RNA degradation TTHTKNY ID TTHTKNY TTHTKNY TN Serine/threonine PP2A-alpha (PPP2CA) TTHTKNY UP P67775 TTHTKNY UC PP2AA_HUMAN TTHTKNY BC Phosphoric monoester hydrolase TTHTKNY SN Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform; Replication protein C; RP-C; PP2A-alpha TTHTKNY GN PPP2CA TTHTKNY FC PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'. PP2A is the major phosphatase for microtubule-associated proteins (MAPs). TTHTKNY EC EC 3.1.3.16 TTHTKNY PD 5W0W; 4LAC; 4IYP; 4I5N; 4I5L TTHTKNY SQ MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL TTHTKNY TT Clinical trial TTHTKNY FM Phosphoric monoester hydrolases TTHTKNY KE hsa03015:mRNA surveillance pathway; hsa04071:Sphingolipid signaling pathway; hsa04114:Oocyte meiosis; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway; hsa04530:Tight junction; hsa04728:Dopaminergic synapse; hsa04730:Long-term depression; hsa05142:Chagas disease (American trypanosomiasis); hsa05160:Hepatitis C TTHTKNY RC R-HSA-1295596:Spry regulation of FGF signaling; R-HSA-180024:DARPP-32 events; R-HSA-195253:Degradation of beta-catenin by the destruction complex; R-HSA-198753:ERK/MAPK targets; R-HSA-2465910:MASTL Facilitates Mitotic Progression; R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-432142:Platelet sensitization by LDL; R-HSA-4641262:Disassembly of the destruction complex and recruitment of AXIN to the membrane; R-HSA-5358747:S33 mutants of beta-catenin aren't phosphorylated; R-HSA-5358749:S37 mutants of beta-catenin aren't phosphorylated; R-HSA-5358751:S45 mutants of beta-catenin aren't phosphorylated; R-HSA-5358752:T41 mutants of beta-catenin aren't phosphorylated; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-5673000:RAF activation; R-HSA-5675221:Negative regulation of MAPK pathway; R-HSA-68877:Mitotic Prometaphase; R-HSA-69231:Cyclin D associated events in G1; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition; R-HSA-70171:Glycolysis TT8ZYBQ ID TT8ZYBQ TT8ZYBQ TN Serine/threonine-protein kinase ATR (FRP1) TT8ZYBQ UP Q13535 TT8ZYBQ UC ATR_HUMAN TT8ZYBQ BC Kinase TT8ZYBQ SN FRAP-related protein 1; Ataxia telangiectasia and Rad3-related protein TT8ZYBQ GN ATR TT8ZYBQ FC Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates BRCA1, CHEK1, MCM2, RAD17, RPA2, SMC1 and p53/TP53, which collectively inhibit DNA replication and mitosis and promote DNA repair, recombination and apoptosis. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at sites of DNA damage, thereby regulating DNA damage response mechanism. Required for FANCD2 ubiquitination. Critical for maintenance of fragile site stability and efficient regulation of centrosome duplication. Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. TT8ZYBQ EC EC 2.7.11.1 TT8ZYBQ PD 5YZ0 TT8ZYBQ SQ MGEHGLELASMIPALRELGSATPEEYNTVVQKPRQILCQFIDRILTDVNVVAVELVKKTDSQPTSVMLLDFIQHIMKSSPLMFVNVSGSHEAKGSCIEFSNWIITRLLRIAATPSCHLLHKKICEVICSLLFLFKSKSPAIFGVLTKELLQLFEDLVYLHRRNVMGHAVEWPVVMSRFLSQLDEHMGYLQSAPLQLMSMQNLEFIEVTLLMVLTRIIAIVFFRRQELLLWQIGCVLLEYGSPKIKSLAISFLTELFQLGGLPAQPASTFFSSFLELLKHLVEMDTDQLKLYEEPLSKLIKTLFPFEAEAYRNIEPVYLNMLLEKLCVMFEDGVLMRLKSDLLKAALCHLLQYFLKFVPAGYESALQVRKVYVRNICKALLDVLGIEVDAEYLLGPLYAALKMESMEIIEEIQCQTQQENLSSNSDGISPKRRRLSSSLNPSKRAPKQTEEIKHVDMNQKSILWSALKQKAESLQISLEYSGLKNPVIEMLEGIAVVLQLTALCTVHCSHQNMNCRTFKDCQHKSKKKPSVVITWMSLDFYTKVLKSCRSLLESVQKLDLEATIDKVVKIYDALIYMQVNSSFEDHILEDLCGMLSLPWIYSHSDDGCLKLTTFAANLLTLSCRISDSYSPQAQSRCVFLLTLFPRRIFLEWRTAVYNWALQSSHEVIRASCVSGFFILLQQQNSCNRVPKILIDKVKDDSDIVKKEFASILGQLVCTLHGMFYLTSSLTEPFSEHGHVDLFCRNLKATSQHECSSSQLKASVCKPFLFLLKKKIPSPVKLAFIDNLHHLCKHLDFREDETDVKAVLGTLLNLMEDPDKDVRVAFSGNIKHILESLDSEDGFIKELFVLRMKEAYTHAQISRNNELKDTLILTTGDIGRAAKGDLVPFALLHLLHCLLSKSASVSGAAYTEIRALVAAKSVKLQSFFSQYKKPICQFLVESLHSSQMTALPNTPCQNADVRKQDVAHQREMALNTLSEIANVFDFPDLNRFLTRTLQVLLPDLAAKASPAASALIRTLGKQLNVNRREILINNFKYIFSHLVCSCSKDELERALHYLKNETEIELGSLLRQDFQGLHNELLLRIGEHYQQVFNGLSILASFASSDDPYQGPRDIISPELMADYLQPKLLGILAFFNMQLLSSSVGIEDKKMALNSLMSLMKLMGPKHVSSVRVKMMTTLRTGLRFKDDFPELCCRAWDCFVRCLDHACLGSLLSHVIVALLPLIHIQPKETAAIFHYLIIENRDAVQDFLHEIYFLPDHPELKKIKAVLQEYRKETSESTDLQTTLQLSMKAIQHENVDVRIHALTSLKETLYKNQEKLIKYATDSETVEPIISQLVTVLLKGCQDANSQARLLCGECLGELGAIDPGRLDFSTTETQGKDFTFVTGVEDSSFAYGLLMELTRAYLAYADNSRAQDSAAYAIQELLSIYDCREMETNGPGHQLWRRFPEHVREILEPHLNTRYKSSQKSTDWSGVKKPIYLSKLGSNFAEWSASWAGYLITKVRHDLASKIFTCCSIMMKHDFKVTIYLLPHILVYVLLGCNQEDQQEVYAEIMAVLKHDDQHTINTQDIASDLCQLSTQTVFSMLDHLTQWARHKFQALKAEKCPHSKSNRNKVDSMVSTVDYEDYQSVTRFLDLIPQDTLAVASFRSKAYTRAVMHFESFITEKKQNIQEHLGFLQKLYAAMHEPDGVAGVSAIRKAEPSLKEQILEHESLGLLRDATACYDRAIQLEPDQIIHYHGVVKSMLGLGQLSTVITQVNGVHANRSEWTDELNTYRVEAAWKLSQWDLVENYLAADGKSTTWSVRLGQLLLSAKKRDITAFYDSLKLVRAEQIVPLSAASFERGSYQRGYEYIVRLHMLCELEHSIKPLFQHSPGDSSQEDSLNWVARLEMTQNSYRAKEPILALRRALLSLNKRPDYNEMVGECWLQSARVARKAGHHQTAYNALLNAGESRLAELYVERAKWLWSKGDVHQALIVLQKGVELCFPENETPPEGKNMLIHGRAMLLVGRFMEETANFESNAIMKKYKDVTACLPEWEDGHFYLAKYYDKLMPMVTDNKMEKQGDLIRYIVLHFGRSLQYGNQFIYQSMPRMLTLWLDYGTKAYEWEKAGRSDRVQMRNDLGKINKVITEHTNYLAPYQFLTAFSQLISRICHSHDEVFVVLMEIIAKVFLAYPQQAMWMMTAVSKSSYPMRVNRCKEILNKAIHMKKSLEKFVGDATRLTDKLLELCNKPVDGSSSTLSMSTHFKMLKKLVEEATFSEILIPLQSVMIPTLPSILGTHANHASHEPFPGHWAYIAGFDDMVEILASLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKCLRKDAESRRRELHIRTYAVIPLNDECGIIEWVNNTAGLRPILTKLYKEKGVYMTGKELRQCMLPKSAALSEKLKVFREFLLPRHPPIFHEWFLRTFPDPTSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFDSLTGECVHVDFNCLFNKGETFEVPEIVPFRLTHNMVNGMGPMGTEGLFRRACEVTMRLMRDQREPLMSVLKTFLHDPLVEWSKPVKGHSKAPLNETGEVVNEKAKTHVLDIEQRLQGVIKTRNRVTGLPLSIEGHVHYLIQEATDENLLCQMYLGWTPYM TT8ZYBQ TT Clinical trial TT8ZYBQ FM Kinase TT8ZYBQ KE hsa03460:Fanconi anemia pathway; hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa05166:HTLV-I infection TT8ZYBQ RC R-HSA-1221632:Meiotic synapsis; R-HSA-176187:Activation of ATR in response to replication stress; R-HSA-3371453:Regulation of HSF1-mediated heat shock response; R-HSA-5685938:HDR through Single Strand Annealing (SSA); R-HSA-5693607:Processing of DNA double-strand break ends; R-HSA-5693616:Presynaptic phase of homologous DNA pairing and strand exchange; R-HSA-69473:G2/M DNA damage checkpoint TTB7VAT ID TTB7VAT TTB7VAT TN Serum amyloid P-component (APCS) TTB7VAT UP P02743 TTB7VAT UC SAMP_HUMAN TTB7VAT BC Pentraxin family TTB7VAT SN SAP; APCS; 9.5S alpha-1-glycoprotein TTB7VAT GN APCS TTB7VAT FC Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin. TTB7VAT PD 4AYU; 4AVV; 4AVT; 4AVS; 3KQR TTB7VAT SQ MNKPLLWISVLTSLLEAFAHTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV TTB7VAT TT Clinical trial TTB7VAT RC R-HSA-977225:Amyloid formation TTF8JAT ID TTF8JAT TTF8JAT TN SLC5A2 messenger RNA (SLC5A2 mRNA) TTF8JAT UP P31639 TTF8JAT UC SC5A2_HUMAN TTF8JAT BC mRNA target TTF8JAT SN Solute carrier family 5 member 2 (mRNA); Na(+)/glucose cotransporter 2 (mRNA); Low affinity sodium-glucose cotransporter (mRNA) TTF8JAT GN SLC5A2 TTF8JAT FC Has a Na(+) to glucose coupling ratio of 1:1. Sodium-dependent glucose transporter. TTF8JAT SQ MEEHTEAGSAPEMGAQKALIDNPADILVIAAYFLLVIGVGLWSMCRTNRGTVGGYFLAGRSMVWWPVGASLFASNIGSGHFVGLAGTGAASGLAVAGFEWNALFVVLLLGWLFAPVYLTAGVITMPQYLRKRFGGRRIRLYLSVLSLFLYIFTKISVDMFSGAVFIQQALGWNIYASVIALLGITMIYTVTGGLAALMYTDTVQTFVILGGACILMGYAFHEVGGYSGLFDKYLGAATSLTVSEDPAVGNISSFCYRPRPDSYHLLRHPVTGDLPWPALLLGLTIVSGWYWCSDQVIVQRCLAGKSLTHIKAGCILCGYLKLTPMFLMVMPGMISRILYPDEVACVVPEVCRRVCGTEVGCSNIAYPRLVVKLMPNGLRGLMLAVMLAALMSSLASIFNSSSTLFTMDIYTRLRPRAGDRELLLVGRLWVVFIVVVSVAWLPVVQAAQGGQLFDYIQAVSSYLAPPVSAVFVLALFVPRVNEQGAFWGLIGGLLMGLARLIPEFSFGSGSCVQPSACPAFLCGVHYLYFAIVLFFCSGLLTLTVSLCTAPIPRKHLHRLVFSLRHSKEEREDLDADEQQGSSLPVQNGCPESAMEMNEPQAPAPSLFRQCLLWFCGMSRGGVGSPPPLTQEEAAAAARRLEDISEDPSWARVVNLNALLMMAVAVFLWGFYA TTF8JAT TT Clinical trial TTF8JAT FM mRNA target TTF8JAT RC R-HSA-189200:Hexose transport; R-HSA-428808:Na+-dependent glucose transporters; R-HSA-429593:Inositol transporters TTVG0SN ID TTVG0SN TTVG0SN TN S-nitrosoglutathione reductase (CBR1) TTVG0SN UP P16152 TTVG0SN UC CBR1_HUMAN TTVG0SN BC Short-chain dehydrogenases reductase TTVG0SN SN ProstaglandinE(2) 9reductase; Prostaglandin 9ketoreductase; NADPHdependent carbonyl reductase 1; Carbonyl reductase [NADPH] 1; CBR1; 15hydroxyprostaglandin dehydrogenase [NADP(+)] TTVG0SN GN CBR1 TTVG0SN FC NADPH-dependent reductase with broad substratespecificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. TTVG0SN EC EC 1.1.1.184 TTVG0SN PD 4Z3D; 3BHM; 3BHJ; 3BHI; 2PFG TTVG0SN SQ MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW TTVG0SN TT Clinical trial TT2UE56 ID TT2UE56 TT2UE56 TN Sodium/glucose cotransporter 1 (SGLT1) TT2UE56 UP P13866 TT2UE56 UC SC5A1_HUMAN TT2UE56 BC Solute:sodium symporter TT2UE56 SN Solute carrier family 5 member 1; Na(+)/glucose cotransporter 1; NAGT; High affinity sodium-glucose cotransporter TT2UE56 GN SLC5A1 TT2UE56 FC Efficient substrate transport in mammalian kidney is provided by the concerted action of a low affinity high capacity and a high affinity low capacity Na(+)/glucose cotransporter arranged in series along kidney proximal tubules. Actively transports glucose into cells by Na(+) cotransport with a Na(+) to glucose coupling ratio of 2:1. TT2UE56 SQ MDSSTWSPKTTAVTRPVETHELIRNAADISIIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAASGIAIGGFEWNALVLVVVLGWLFVPIYIKAGVVTMPEYLRKRFGGQRIQVYLSLLSLLLYIFTKISADIFSGAIFINLALGLNLYLAIFLLLAITALYTITGGLAAVIYTDTLQTVIMLVGSLILTGFAFHEVGGYDAFMEKYMKAIPTIVSDGNTTFQEKCYTPRADSFHIFRDPLTGDLPWPGFIFGMSILTLWYWCTDQVIVQRCLSAKNMSHVKGGCILCGYLKLMPMFIMVMPGMISRILYTEKIACVVPSECEKYCGTKVGCTNIAYPTLVVELMPNGLRGLMLSVMLASLMSSLTSIFNSASTLFTMDIYAKVRKRASEKELMIAGRLFILVLIGISIAWVPIVQSAQSGQLFDYIQSITSYLGPPIAAVFLLAIFWKRVNEPGAFWGLILGLLIGISRMITEFAYGTGSCMEPSNCPTIICGVHYLYFAIILFAISFITIVVISLLTKPIPDVHLYRLCWSLRNSKEERIDLDAEEENIQEGPKETIEIETQVPEKKKGIFRRAYDLFCGLEQHGAPKMTEEEEKAMKMKMTDTSEKPLWRTVLNVNGIILVTVAVFCHAYFA TT2UE56 TT Clinical trial TT2UE56 FM Solute sodium symporter TT2UE56 KE hsa04973:Carbohydrate digestion and absorption; hsa04976:Bile secretion; hsa04978:Mineral absorption TT2UE56 RC R-HSA-189200:Hexose transport; R-HSA-428808:Na+-dependent glucose transporters; R-HSA-429593:Inositol transporters TTN7Y4P ID TTN7Y4P TTN7Y4P TN Sodium/glucose cotransporter 2 (SLC5A4) TTN7Y4P UP Q9NY91 TTN7Y4P UC SC5A4_HUMAN TTN7Y4P BC Solute:sodium symporter TTN7Y4P SN Sodium/glucose cotransporter 4; SLC5A4 TTN7Y4P GN SLC5A4 TTN7Y4P FC Sodium-dependent glucose transporter. TTN7Y4P SQ MASTVSPSTIAETPEPPPLSDHIRNAADISVIVIYFLVVMAVGLWAMLKTNRGTIGGFFLAGRDMAWWPMGASLFASNIGSNHYVGLAGTGAASGVATVTFEWTSSVMLLILGWIFVPIYIKSGVMTMPEYLKKRFGGERLQVYLSILSLFICVVLLISADIFAGAIFIKLALGLDLYLAIFILLAMTAVYTTTGGLASVIYTDTLQTIIMLIGSFILMGFAFNEVGGYESFTEKYVNATPSVVEGDNLTISASCYTPRADSFHIFRDAVTGDIPWPGIIFGMPITALWYWCTNQVIVQRCLCGKDMSHVKAACIMCAYLKLLPMFLMVMPGMISRILYTDMVACVVPSECVKHCGVDVGCTNYAYPTMVLELMPQGLRGLMLSVMLASLMSSLTSIFNSASTLFTIDLYTKMRKQASEKELLIAGRIFVLLLTVVSIVWVPLVQVSQNGQLIHYTESISSYLGPPIAAVFVLAIFCKRVNEQGAFWGLMVGLAMGLIRMITEFAYGTGSCLAPSNCPKIICGVHYLYFSIVLFFGSMLVTLGISLLTKPIPDVHLYRLCWVLRNSTEERIDIDAEEKSQEETDDGVEEDYPEKSRGCLKKAYDLFCGLQKGPKLTKEEEEALSKKLTDTSERPSWRTIVNINAILLLAVVVFIHGYYA TTN7Y4P TT Clinical trial TTN7Y4P RC R-HSA-189200:Hexose transport; R-HSA-428808:Na+-dependent glucose transporters; R-HSA-429593:Inositol transporters TTFZVPO ID TTFZVPO TTFZVPO TN Sodium/hydrogen exchanger 3 (SLC9A3) TTFZVPO UP P48764 TTFZVPO UC SL9A3_HUMAN TTFZVPO BC Monovalent cation:proton antiporter TTFZVPO SN SLC9A3; Na(+)/H(+) exchanger 3; NHE-3 TTFZVPO GN SLC9A3 TTFZVPO FC Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. TTFZVPO SQ MWGLGARGPDRGLLLALALGGLARAGGVEVEPGGAHGESGGFQVVTFEWAHVQDPYVIALWILVASLAKIGFHLSHKVTSVVPESALLIVLGLVLGGIVWAADHIASFTLTPTVFFFYLLPPIVLDAGYFMPNRLFFGNLGTILLYAVVGTVWNAATTGLSLYGVFLSGLMGDLQIGLLDFLLFGSLMAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFESFVALGGDNVTGVDCVKGIVSFFVVSLGGTLVGVVFAFLLSLVTRFTKHVRIIEPGFVFIISYLSYLTSEMLSLSAILAITFCGICCQKYVKANISEQSATTVRYTMKMLASSAETIIFMFLGISAVNPFIWTWNTAFVLLTLVFISVYRAIGVVLQTWLLNRYRMVQLEPIDQVVLSYGGLRGAVAFALVVLLDGDKVKEKNLFVSTTIIVVFFTVIFQGLTIKPLVQWLKVKRSEHREPRLNEKLHGRAFDHILSAIEDISGQIGHNYLRDKWSHFDRKFLSRVLMRRSAQKSRDRILNVFHELNLKDAISYVAEGERRGSLAFIRSPSTDNVVNVDFTPRSSTVEASVSYLLRENVSAVCLDMQSLEQRRRSIRDAEDMVTHHTLQQYLYKPRQEYKHLYSRHELTPTEDEKQDREIFHRTMRKRLESFKSTKLGLNQNKKAAKLYKRERAQKRRNSSIPNGKLPMESPAQNFTIKEKDLELSDTEEPPNYDEEMSGGIEFLASVTKDTASDSPAGIDNPVFSPDEALDRSLLARLPPWLSPGETVVPSQRARTQIPYSPGTFCRLMPFRLSSKSVDSFLQADGPEERPPAALPESTHM TTFZVPO TT Successful TTFZVPO KE hsa04964:Proximal tubule bicarbonate reclamation; hsa04974:Protein digestion and absorption; hsa04976:Bile secretion; hsa04978:Mineral absorption TT6Y1PG ID TT6Y1PG TT6Y1PG TN Solute carrier family 40 member 1 (SLC40A1) TT6Y1PG UP Q9NP59 TT6Y1PG UC S40A1_HUMAN TT6Y1PG BC Ferroportin protein TT6Y1PG SN SLC11A3; MSTP079; IREG1; Ferroportin-1; FPN1 TT6Y1PG GN SLC40A1 TT6Y1PG FC Mediates iron efflux in the presence of a ferroxidase (hephaestin and/or ceruloplasmin). May be involved in iron export from duodenal epithelial cell and also in transfer of iron between maternal and fetal circulation. TT6Y1PG SQ MTRAGDHNRQRGCCGSLADYLTSAKFLLYLGHSLSTWGDRMWHFAVSVFLVELYGNSLLLTAVYGLVVAGSVLVLGAIIGDWVDKNARLKVAQTSLVVQNVSVILCGIILMMVFLHKHELLTMYHGWVLTSCYILIITIANIANLASTATAITIQRDWIVVVAGEDRSKLANMNATIRRIDQLTNILAPMAVGQIMTFGSPVIGCGFISGWNLVSMCVEYVLLWKVYQKTPALAVKAGLKEEETELKQLNLHKDTEPKPLEGTHLMGVKDSNIHELEHEQEPTCASQMAEPFRTFRDGWVSYYNQPVFLAGMGLAFLYMTVLGFDCITTGYAYTQGLSGSILSILMGASAITGIMGTVAFTWLRRKCGLVRTGLISGLAQLSCLILCVISVFMPGSPLDLSVSPFEDIRSRFIQGESITPTKIPEITTEIYMSNGSNSANIVPETSPESVPIISVSLLFAGVIAARIGLWSFDLTVTQLLQENVIESERGIINGVQNSMNYLLDLLHFIMVILAPNPEAFGLLVLISVSFVAMGHIMYFRFAQNTLGNKLFACGPDAKEVRKENQANTSVV TT6Y1PG TT Clinical trial TT6Y1PG FM Ferroportin family TT6Y1PG KE hsa04978:Mineral absorption TT6Y1PG RC R-HSA-917937:Iron uptake and transport TTAE1BR ID TTAE1BR TTAE1BR TN Somatostatin receptor type 4 (SSTR4) TTAE1BR UP P31391 TTAE1BR UC SSR4_HUMAN TTAE1BR BC GPCR rhodopsin TTAE1BR SN SSTR4; SS4R TTAE1BR GN SSTR4 TTAE1BR FC Receptor for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. It is functionally coupled not only to inhibition of adenylate cyclase, but also to activation of both arachidonate release and mitogen-activated protein (MAP) kinase cascade. Mediates antiproliferative action of somatostatin in tumor cells. TTAE1BR SQ MSAPSTLPPGGEEGLGTAWPSAANASSAPAEAEEAVAGPGDARAAGMVAIQCIYALVCLVGLVGNALVIFVILRYAKMKTATNIYLLNLAVADELFMLSVPFVASSAALRHWPFGSVLCRAVLSVDGLNMFTSVFCLTVLSVDRYVAVVHPLRAATYRRPSVAKLINLGVWLASLLVTLPIAIFADTRPARGGQAVACNLQWPHPAWSAVFVVYTFLLGFLLPVLAIGLCYLLIVGKMRAVALRAGWQQRRRSEKKITRLVLMVVVVFVLCWMPFYVVQLLNLFVTSLDATVNHVSLILSYANSCANPILYGFLSDNFRRFFQRVLCLRCCLLEGAGGAEEEPLDYYATALKSKGGAGCMCPPLPCQQEALQPEPGRKRIPLTRTTTF TTAE1BR TT Clinical trial TTAE1BR KE hsa04080:Neuroactive ligand-receptor interaction TTAE1BR RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTCN0M9 ID TTCN0M9 TTCN0M9 TN Sphingosine kinase 2 (SPHK2) TTCN0M9 UP Q9NRA0 TTCN0M9 UC SPHK2_HUMAN TTCN0M9 BC Kinase TTCN0M9 SN SPK 2; SK 2 TTCN0M9 GN SPHK2 TTCN0M9 FC Acts on D-erythro-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides. Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. TTCN0M9 EC EC 2.7.1.91 TTCN0M9 SQ MNGHLEAEEQQDQRPDQELTGSWGHGPRSTLVRAKAMAPPPPPLAASTPLLHGEFGSYPARGPRFALTLTSQALHIQRLRPKPEARPRGGLVPLAEVSGCCTLRSRSPSDSAAYFCIYTYPRGRRGARRRATRTFRADGAATYEENRAEAQRWATALTCLLRGLPLPGDGEITPDLLPRPPRLLLLVNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPDWEEAVKMPVGILPCGSGNALAGAVNQHGGFEPALGLDLLLNCSLLLCRGGGHPLDLLSVTLASGSRCFSFLSVAWGFVSDVDIQSERFRALGSARFTLGTVLGLATLHTYRGRLSYLPATVEPASPTPAHSLPRAKSELTLTPDPAPPMAHSPLHRSVSDLPLPLPQPALASPGSPEPLPILSLNGGGPELAGDWGGAGDAPLSPDPLLSSPPGSPKAALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCGPPDHLLPPLGTPLPPDWVTLEGDFVLMLAISPSHLGADLVAAPHARFDDGLVHLCWVRSGISRAALLRLFLAMERGSHFSLGCPQLGYAAARAFRLEPLTPRGVLTVDGEQVEYGPLQAQMHPGIGTLLTGPPGCPGREP TTCN0M9 TT Clinical trial TTCN0M9 FM Kinase TTCN0M9 KE hsa00600:Sphingolipid metabolism; hsa01100:Metabolic pathways; hsa04020:Calcium signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04370:VEGF signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa05152:Tuberculosis TTCN0M9 RC R-HSA-1660661:Sphingolipid de novo biosynthesis TTTU72V ID TTTU72V TTTU72V TN Steroid 5-alpha-reductase 1 (SRD5A1) TTTU72V UP P18405 TTTU72V UC S5A1_HUMAN TTTU72V BC CH-CH donor oxidoreductase TTTU72V SN SRD5A1; SR type 1; 5-alpha reductase 1 TTTU72V GN SRD5A1 TTTU72V FC Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5- alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology. TTTU72V EC EC 1.3.1.22 TTTU72V SQ MATATGVAEERLLAALAYLQCAVGCAVFARNRQTNSVYGRHALPSHRLRVPARAAWVVQELPSLALPLYQYASESAPRLRSAPNCILLAMFLVHYGHRCLIYPFLMRGGKPMPLLACTMAIMFCTCNGYLQSRYLSHCAVYADDWVTDPRFLIGFGLWLTGMLINIHSDHILRNLRKPGDTGYKIPRGGLFEYVTAANYFGEIMEWCGYALASWSVQGAAFAFFTFCFLSGRAKEHHEWYLRKFEEYPKFRKIIIPFLF TTTU72V TT Clinical trial TTTU72V KE hsa00140:Steroid hormone biosynthesis TTTU72V RC R-HSA-193048:Androgen biosynthesis TT1WJCI ID TT1WJCI TT1WJCI TN Streptococcus Topoisomerase IV A (Stre-coc parC) TT1WJCI UP P72525 TT1WJCI UC PARC_STRPN TT1WJCI BC Topoisomerase GyrA ParC TT1WJCI SN parC of Streptococcus pneumoniae serotype 4; DNA topoisomerase IV of Streptococcus pneumoniae serotype 4 TT1WJCI GN Stre-coc parC TT1WJCI FC Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule. TT1WJCI EC EC 5.6.2.3 TT1WJCI PD 4Z53; 4Z4Q; 4Z3O; 4KPF; 4KPE TT1WJCI SQ MSNIQNMSLEDIMGERFGRYSKYIIQDRALPDIRDGLKPVQRRILYSMNKDSNTFDKSYRKSAKSVGNIMGNFHPHGDSSIYDAMVRMSQNWKNREILVEMHGNNGSMDGDPPAAMRYTEARLSEIAGYLLQDIEKKTVPFAWNFDDTEKEPTVLPAAFPNLLVNGSTGISAGYATDIPPHNLAEVIDAAVYMIDHPTAKIDKLMEFLPGPDFPTGAIIQGRDEIKKAYETGKGRVVVRSKTEIEKLKGGKEQIVIIEIPYEINKANLVKKIDDVRVNNKVAGIAEVRDESDRDGLRIAIELKKDANTELVLNYLFKYTDLQINYNFNMVAIDNFTPRQVGIVPILSSYIAHRREVILARSRFDKEKAEKRLHIVEGLIRVISILDEVIALIRASENKADAKENLKVSYDFTEEQAEAIVTLQLYRLTNTDVVVLQEEEAELREKIAMLAAIIGDERTMYNLMKKELREVKKKFATPRLSSLEDTAKAIEIDTASLIAEEDTYVSVTKAGYIKRTSPRSFAASTLEEIGKRDDDRLIFVQSAKTTQHLLMFTSLGNVIYRPIHELADIRWKDIGEHLSQTITNFETNEEILYVEVLDQFDDATTYFAVTRLGQIKRVERKEFTPWRTYRSKSVKYAKLKDDTDQIVAVAPIKLDDVVLVSQNGYALRFNIEEVPVVGAKAAGVKAMNLKEDDVLQSGFICNTSSFYLLTQRGSLKRVSIEEILATSRAKRGLQVLRELKNKPHRVFLAGAVAEQGFVGDFFSTEVDVNDQTLLVQSNKGTIYESRLQDLNLSERTSNGSFISDTISDEEVFDAYLQEVVTEDK TT1WJCI TT Clinical trial TTYO0A3 ID TTYO0A3 TTYO0A3 TN Substance-K receptor (TACR2) TTYO0A3 UP P21452 TTYO0A3 UC NK2R_HUMAN TTYO0A3 BC GPCR rhodopsin TTYO0A3 SN Tachykinin receptor 2; Tachykinin neurokinin 2 receptor; TACR2; SKR; Neurokinin A receptor; NK-2R; NK-2 receptor TTYO0A3 GN TACR2 TTYO0A3 FC This is a receptor for the tachykinin neuropeptide substance K (neurokinin A). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance K > neuromedin-K > substance P. TTYO0A3 SQ MGTCDIVTEANISSGPESNTTGITAFSMPSWQLALWATAYLALVLVAVTGNAIVIWIILAHRRMRTVTNYFIVNLALADLCMAAFNAAFNFVYASHNIWYFGRAFCYFQNLFPITAMFVSIYSMTAIAADRYMAIVHPFQPRLSAPSTKAVIAGIWLVALALASPQCFYSTVTMDQGATKCVVAWPEDSGGKTLLLYHLVVIALIYFLPLAVMFVAYSVIGLTLWRRAVPGHQAHGANLRHLQAMKKFVKTMVLVVLTFAICWLPYHLYFILGSFQEDIYCHKFIQQVYLALFWLAMSSTMYNPIIYCCLNHRFRSGFRLAFRCCPWVTPTKEDKLELTPTTSLSTRVNRCHTKETLFMAGDTAPSEATSGEAGRPQDGSGLWFGYGLLAPTKTHVEI TTYO0A3 TT Clinical trial TTYO0A3 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTYO0A3 RC R-HSA-416476:G alpha (q) signalling events TT9O4C5 ID TT9O4C5 TT9O4C5 TN Superoxide dismutase Mn (SOD Mn) TT9O4C5 UP P04179 TT9O4C5 UC SODM_HUMAN TT9O4C5 BC Superoxide dismutase/reductase TT9O4C5 SN Superoxide dismutase [Mn], mitochondrial TT9O4C5 GN SOD2 TT9O4C5 FC Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. TT9O4C5 EC EC 1.15.1.1 TT9O4C5 PD 5VF9; 5T30; 5GXO; 3C3T; 3C3S TT9O4C5 SQ MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK TT9O4C5 TT Clinical trial TT9O4C5 FM Oxidoreductases acting on superoxide as acceptor TT9O4C5 KE hsa04068:FoxO signaling pathway; hsa04146:Peroxisome; hsa05016:Huntington's disease TTYDSVG ID TTYDSVG TTYDSVG TN Syndecan-1 (SDC1) TTYDSVG UP P18827 TTYDSVG UC SDC1_HUMAN TTYDSVG BC Peptide translocating syndecan TTYDSVG SN SYND1; SDC; CD138 TTYDSVG GN SDC1 TTYDSVG FC Regulates exosome biogenesis in concert with SDCBP and PDCD6IP. Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix. TTYDSVG PD 6EJE; 4GVD; 4GVC TTYDSVG SQ MRRAALWLWLCALALSLQPALPQIVATNLPPEDQDGSGDDSDNFSGSGAGALQDITLSQQTPSTWKDTQLLTAIPTSPEPTGLEATAASTSTLPAGEGPKEGEAVVLPEVEPGLTAREQEATPRPRETTQLPTTHLASTTTATTAQEPATSHPHRDMQPGHHETSTPAGPSQADLHTPHTEDGGPSATERAAEDGASSQLPAAEGSGEQDFTFETSGENTAVVAVEPDRRNQSPVDQGATGASQGLLDRKEVLGGVIAGGLVGLIFAVCLVGFMLYRMKKKDEGSYSLEEPKQANGGAYQKPTKQEEFYA TTYDSVG TT Clinical trial TTYDSVG FM Syndecan proteoglycan TT08OSU ID TT08OSU TT08OSU TN Synuclein alpha (SNCA) TT08OSU UP P37840 TT08OSU UC SYUA_HUMAN TT08OSU BC Synuclein TT08OSU SN PARK1; Non-A4 component of amyloid precursor; Non-A beta component of AD amyloid; NACP; Alpha-synuclein TT08OSU GN SNCA TT08OSU FC Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores. Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis. Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5. This chaperone activity is important to sustain normal SNARE-complex assembly during aging. Plays also a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity. TT08OSU PD 6H6B; 6FLT; 6CU8; 6CU7; 6CT7 TT08OSU SQ MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA TT08OSU TT Clinical trial TT08OSU FM Synuclein family TT08OSU KE hsa05010:Alzheimer's disease; hsa05012:Parkinson's disease TT08OSU RC R-HSA-977225:Amyloid formation TTBW580 ID TTBW580 TTBW580 TN TAX transcriptionally-activated glycoprotein 1 (OX40) TTBW580 UP P23510 TTBW580 UC TNFL4_HUMAN TTBW580 BC Cytokine: tumor necrosis factor TTBW580 SN Tumor necrosis factor ligand superfamily member 4; TNFSF4; OX40L; Glycoprotein Gp34; CD252 TTBW580 GN TNFSF4 TTBW580 FC Cytokine that binds to TNFRSF4. Co-stimulates T-cell proliferation and cytokine production. TTBW580 PD 2HEV TTBW580 SQ MERVQPLEENVGNAARPRFERNKLLLVASVIQGLGLLLCFTYICLHFSALQVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVL TTBW580 TT Clinical trial TTBW580 KE hsa04060:Cytokine-cytokine receptor interaction TTBW580 RC R-HSA-5669034:TNFs bind their physiological receptors TT3C80U ID TT3C80U TT3C80U TN T-cell-specific kinase (ITK) TT3C80U UP Q08881 TT3C80U UC ITK_HUMAN TT3C80U BC Kinase TT3C80U SN Tyrosine kinase ITK; Inducible T cell kinase; EMT TT3C80U GN ITK TT3C80U FC Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Phosphorylates TBX21 at 'Tyr-530' and mediates its interaction with GATA3. Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. TT3C80U EC EC 2.7.10.2 TT3C80U PD 4RFM; 4QD6; 4PQN; 4PPC; 4PPB TT3C80U SQ MNNFILLEEQLIKKSQQKRRTSPSNFKVRFFVLTKASLAYFEDRHGKKRTLKGSIELSRIKCVEIVKSDISIPCHYKYPFQVVHDNYLLYVFAPDRESRQRWVLALKEETRNNNSLVPKYHPNFWMDGKWRCCSQLEKLATGCAQYDPTKNASKKPLPPTPEDNRRPLWEPEETVVIALYDYQTNDPQELALRRNEEYCLLDSSEIHWWRVQDRNGHEGYVPSSYLVEKSPNNLETYEWYNKSISRDKAEKLLLDTGKEGAFMVRDSRTAGTYTVSVFTKAVVSENNPCIKHYHIKETNDNPKRYYVAEKYVFDSIPLLINYHQHNGGGLVTRLRYPVCFGRQKAPVTAGLRYGKWVIDPSELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLFAAETLLGMCLDVCEGMAYLEEACVIHRDLAARNCLVGENQVIKVSDFGMTRFVLDDQYTSSTGTKFPVKWASPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCWKERPEDRPAFSRLLRQLAEIAESGL TT3C80U TT Clinical trial TT3C80U FM Kinase TT3C80U KE hsa04062:Chemokine signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04670:Leukocyte transendothelial migration TT3C80U RC R-HSA-202433:Generation of second messenger molecules; R-HSA-2871809:FCERI mediated Ca+2 mobilization TTI0KH6 ID TTI0KH6 TTI0KH6 TN TGF beta-2 messenger RNA (TGFB2 mRNA) TTI0KH6 UP P61812 TTI0KH6 UC TGFB2_HUMAN TTI0KH6 BC mRNA target TTI0KH6 SN Transforming growth factor beta-2 proprotein (mRNA); TGF-beta 2 (mRNA); Polyergin (mRNA); Glioblastoma-derived T-cell suppressor factor (mRNA); G-TSF (mRNA); Cetermin (mRNA); BSC-1 cell growth inhibitor (mRNA) TTI0KH6 GN TGFB2 TTI0KH6 FC Transforming growth factor beta-2 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively. TTI0KH6 PD 5TY4; 5TX4; 4KXZ; 2TGI; 1TFG TTI0KH6 SQ MHYCVLSAFLILHLVTVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPEEVPPEVISIYNSTRDLLQEKASRRAAACERERSDEEYYAKEVYKIDMPPFFPSENAIPPTFYRPYFRIVRFDVSAMEKNASNLVKAEFRVFRLQNPKARVPEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVHEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYTSGDQKTIKSTRKKNSGKTPHLLLMLLPSYRLESQQTNRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS TTI0KH6 TT Clinical trial TTI0KH6 FM mRNA target TTI0KH6 KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04144:Endocytosis; hsa04350:TGF-beta signaling pathway; hsa04380:Osteoclast differentiation; hsa04390:Hippo signaling pathway; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05220:Chronic myeloid leukemia; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05414:Dilated cardiomyopathy TTI0KH6 RC R-HSA-114608:Platelet degranulation; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-3000178:ECM proteoglycans TTZE3P7 ID TTZE3P7 TTZE3P7 TN TGF-beta receptor type II (TGFBR2) TTZE3P7 UP P37173 TTZE3P7 UC TGFR2_HUMAN TTZE3P7 BC Kinase TTZE3P7 SN Transforminggrowth factor-beta receptor type II; Transforming growth factor-beta receptor type II; TbetaR-II; TGFR-2; TGF-beta type II receptor; TGF-beta receptor type-2 TTZE3P7 GN TGFBR2 TTZE3P7 FC Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. TTZE3P7 EC EC 2.7.11.30 TTZE3P7 PD 5TY4; 5TX4; 5QIN; 5E8Y; 5E8V TTZE3P7 SQ MGRGLLRGLWPLHIVLWTRIASTIPPHVQKSVNNDMIVTDNNGAVKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPDLLLVIFQVTGISLLPPLGVAISVIIIFYCYRVNRQQKLSSTWETGKTRKLMEFSEHCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYASWKTEKDIFSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLESRMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVESMKDNVLRDRGRPEIPSFWLNHQGIQMVCETLTECWDHDPEARLTAQCVAERFSELEHLDRLSGRSCSEEKIPEDGSLNTTK TTZE3P7 TT Clinical trial TTZE3P7 FM Kinase TTZE3P7 KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04068:FoxO signaling pathway; hsa04144:Endocytosis; hsa04350:TGF-beta signaling pathway; hsa04380:Osteoclast differentiation; hsa04390:Hippo signaling pathway; hsa04520:Adherens junction; hsa05142:Chagas disease (American trypanosomiasis); hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05210:Colorectal cancer; hsa05212:Pancreatic cancer; hsa05220:Chronic myeloid leukemia TTZE3P7 RC R-HSA-2173789:TGF-beta receptor signaling activates SMADs; R-HSA-2173791:TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition); R-HSA-3304356:SMAD2/3 Phosphorylation Motif Mutants in Cancer; R-HSA-3315487:SMAD2/3 MH2 Domain Mutants in Cancer; R-HSA-3645790:TGFBR2 Kinase Domain Mutants in Cancer; R-HSA-3656532:TGFBR1 KD Mutants in Cancer; R-HSA-3656535:TGFBR1 LBD Mutants in Cancer TTIJP3Q ID TTIJP3Q TTIJP3Q TN TNF related activation protein (CD40LG) TTIJP3Q UP P29965 TTIJP3Q UC CD40L_HUMAN TTIJP3Q BC Cytokine: tumor necrosis factor TTIJP3Q SN Tumor necrosis factor ligand superfamily member 5; TRAP; TNFSF5; TNF-related activation protein; T-cell antigen Gp39; T cell antigen Gp39; CD40L; CD40-L; CD40 ligand; CD154 antigen; CD154 TTIJP3Q GN CD40LG TTIJP3Q FC Costimulates T-cell proliferation and cytokine production. Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation. Induces the activation of NF-kappa-B and kinases MAPK8 and PAK2 in T-cells. Induces tyrosine phosphorylation of isoform 3 of CD28. Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4. Involved in immunoglobulin class switching. Cytokine that binds to CD40/TNFRSF5. TTIJP3Q PD 6BRB; 3QD6; 3LKJ; 1I9R; 1ALY TTIJP3Q SQ MIETYNQTSPRSAATGLPISMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLHEDFVFMKTIQRCNTGERSLSLLNCEEIKSQFEGFVKDIMLNKEETKKENSFEMQKGDQNPQIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVNVTDPSQVSHGTGFTSFGLLKL TTIJP3Q TT Clinical trial TTIJP3Q FM Tumor necrosis factor TTIJP3Q KE hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04514:Cell adhesion molecules (CAMs); hsa04660:T cell receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05310:Asthma; hsa05320:Autoimmune thyroid disease; hsa05322:Systemic lupus erythematosus; hsa05330:Allograft rejection; hsa05340:Primary immunodeficiency; hsa05416:Viral myocarditis TTIJP3Q RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway TTA5MS9 ID TTA5MS9 TTA5MS9 TN TNF related apoptosis inducing ligand (TNFSF10) TTA5MS9 UP P50591 TTA5MS9 UC TNF10_HUMAN TTA5MS9 BC Cytokine: tumor necrosis factor TTA5MS9 SN Tumor necrosis factor ligand superfamily member 10; TRAIL; TNF-related apoptosis-inducing ligand; Protein TRAIL; CD253; Apo-2L; Apo-2 ligand; APO2L TTA5MS9 GN TNFSF10 TTA5MS9 FC Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis. Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. TTA5MS9 PD 5CIR; 4N90; 1DU3; 1DG6; 1D4V TTA5MS9 SQ MAMMEVQGGPSLGQTCVLIVIFTVLLQSLCVAVTYVYFTNELKQMQDKYSKSGIACFLKEDDSYWDPNDEESMNSPCWQVKWQLRQLVRKMILRTSEETISTVQEKQQNISPLVRERGPQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGELVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG TTA5MS9 TT Clinical trial TTA5MS9 FM Cytokine: tumor necrosis factor TTA5MS9 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04068:FoxO signaling pathway; hsa04210:Apoptosis; hsa04650:Natural killer cell mediated cytotoxicity; hsa05162:Measles; hsa05164:Influenza A TTA5MS9 RC R-HSA-140534:Ligand-dependent caspase activation; R-HSA-3371378:Regulation by c-FLIP; R-HSA-5213460:RIPK1-mediated regulated necrosis; R-HSA-5218900:CASP8 activity is inhibited; R-HSA-69416:Dimerization of procaspase-8; R-HSA-75158:TRAIL signaling TTKPS7V ID TTKPS7V TTKPS7V TN TNF superfamily receptor 12A (TNFRSF12A) TTKPS7V UP Q9NP84 TTKPS7V UC TNR12_HUMAN TTKPS7V BC Cytokine receptor TTKPS7V SN TweakR; Tweak-receptor; Tumor necrosis factor receptor superfamily member 12A; Fibroblast growth factor-inducible immediate-early response protein 14; FN14; FGF-inducible 14; CD266 TTKPS7V GN TNFRSF12A TTKPS7V FC Weak inducer of apoptosis in some cell types. Promotes angiogenesis and the proliferation of endothelial cells. May modulate cellular adhesion to matrix proteins. Receptor for TNFSF12/TWEAK. TTKPS7V PD 2RPJ; 2KMZ; 2EQP TTKPS7V SQ MARGSLRRLLRLLVLGLWLALLRSVAGEQAPGTAPCSRGSSWSADLDKCMDCASCRARPHSDFCLGCAAAPPAPFRLLWPILGGALSLTFVLGLLSGFLVWRRCRRREKFTTPIEETGGEGCPAVALIQ TTKPS7V TT Clinical trial TTKPS7V FM Cytokine receptor TTKPS7V KE hsa04060:Cytokine-cytokine receptor interaction TTKPS7V RC R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway TTY7ZHS ID TTY7ZHS TTY7ZHS TN Toll-like receptor 2 (TLR2) TTY7ZHS UP O60603 TTY7ZHS UC TLR2_HUMAN TTY7ZHS BC Toll-like receptor TTY7ZHS SN Toll/interleukin-1 receptor-like protein 4; TIL4; CD282 TTY7ZHS GN TLR2 TTY7ZHS FC Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also activate immune cells and promote apoptosis in response to the lipid moiety of lipoproteins. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B. burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6. Stimulation of monocytes in vitro with M. tuberculosis PstS1 induces p38 MAPK and ERK1/2 activation primarily via this receptor, but also partially via TLR4. MAPK activation in response to bacterial peptidoglycan also occurs via this receptor. Acts as a receptor for M. tuberculosis lipoproteins LprA, LprG, LpqH and PstS1, some lipoproteins are dependent on other coreceptors (TLR1, CD14 and/or CD36); the lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen. M. tuberculosis HSP70 (dnaK) but not HSP65 (groEL-2) acts via this protein to stimulate NF-kappa-B expression. Recognizes M. tuberculosis major T-antigen EsxA (ESAT-6) which inhibits downstream MYD88-dependent signaling (shown in mouse). Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides. Required for normal uptake of M. tuberculosis, a process that is inhibited by M. tuberculosis LppM. Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. TTY7ZHS PD 6NIG; 2Z80; 2Z7X; 1O77; 1FYX TTY7ZHS SQ MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLMVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNIDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS TTY7ZHS TT Clinical trial TTY7ZHS FM Toll like receptor TTY7ZHS KE hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05162:Measles; hsa05168:Herpes simplex infection; hsa05205:Proteoglycans in cancer; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis TTY7ZHS RC R-HSA-1461957:Beta defensins; R-HSA-166058:MyD88:Mal cascade initiated on plasma membrane; R-HSA-168188:Toll Like Receptor TLR6:TLR2 Cascade; R-HSA-5602498:MyD88 deficiency (TLR2/4); R-HSA-5603041:IRAK4 deficiency (TLR2/4) TT8CWFK ID TT8CWFK TT8CWFK TN Toll-like receptor 8 (TLR8) TT8CWFK UP Q9NR97 TT8CWFK UC TLR8_HUMAN TT8CWFK BC Toll-like receptor TT8CWFK SN UNQ249/PRO286; CD288 antigen; CD288 TT8CWFK GN TLR8 TT8CWFK FC Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. TT8CWFK PD 5Z15; 5Z14; 5WYZ; 5WYX; 5HDH TT8CWFK SQ MENMFLQSSMLTCIFLLISGSCELCAEENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGNPGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKVCEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFPCVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSFNYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLSENRISPLVKDTRQSYANSSSFQRHIRKRRSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPDIACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNLKVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASLTELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSNLLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDVTAVILFFFTFFITTMVMLAALAHHLFYWDVWFIYNVCLAKVKGYRSLSTSQTFYDAYISYDTKDASVTDWVINELRYHLEESRDKNVLLCLEERDWDPGLAIIDNLMQSINQSKKTVFVLTKKYAKSWNFKTAFYLALQRLMDENMDVIIFILLEPVLQHSQYLRLRQRICKSSILQWPDNPKAEGLFWQTLRNVVLTENDSRYNNMYVDSIKQY TT8CWFK TT Clinical trial TT8CWFK FM Toll-like receptor family TT8CWFK KE hsa04620:Toll-like receptor signaling pathway TT8CWFK RC R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-975110:TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling; R-HSA-975138:TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation; R-HSA-975155:MyD88 dependent cascade initiated on endosome TTSHG0T ID TTSHG0T TTSHG0T TN Toll-like receptor 9 (TLR9) TTSHG0T UP Q9NR96 TTSHG0T UC TLR9_HUMAN TTSHG0T BC Toll-like receptor TTSHG0T SN UNQ5798/PRO19605; TLR-9; CD289 TTSHG0T GN TLR9 TTSHG0T FC Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR9 is a nucleotide-sensing TLR which is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Controls lymphocyte response to Helicobacter infection. Upon CpG stimulation, induces B-cell proliferation, activation, survival and antibody production. TTSHG0T SQ MGFCRSALHPLSLLVQAIMLAMTLALGTLPAFLPCELQPHGLVNCNWLFLKSVPHFSMAAPRGNVTSLSLSSNRIHHLHDSDFAHLPSLRHLNLKWNCPPVGLSPMHFPCHMTIEPSTFLAVPTLEELNLSYNNIMTVPALPKSLISLSLSHTNILMLDSASLAGLHALRFLFMDGNCYYKNPCRQALEVAPGALLGLGNLTHLSLKYNNLTVVPRNLPSSLEYLLLSYNRIVKLAPEDLANLTALRVLDVGGNCRRCDHAPNPCMECPRHFPQLHPDTFSHLSRLEGLVLKDSSLSWLNASWFRGLGNLRVLDLSENFLYKCITKTKAFQGLTQLRKLNLSFNYQKRVSFAHLSLAPSFGSLVALKELDMHGIFFRSLDETTLRPLARLPMLQTLRLQMNFINQAQLGIFRAFPGLRYVDLSDNRISGASELTATMGEADGGEKVWLQPGDLAPAPVDTPSSEDFRPNCSTLNFTLDLSRNNLVTVQPEMFAQLSHLQCLRLSHNCISQAVNGSQFLPLTGLQVLDLSHNKLDLYHEHSFTELPRLEALDLSYNSQPFGMQGVGHNFSFVAHLRTLRHLSLAHNNIHSQVSQQLCSTSLRALDFSGNALGHMWAEGDLYLHFFQGLSGLIWLDLSQNRLHTLLPQTLRNLPKSLQVLRLRDNYLAFFKWWSLHFLPKLEVLDLAGNQLKALTNGSLPAGTRLRRLDVSCNSISFVAPGFFSKAKELRELNLSANALKTVDHSWFGPLASALQILDVSANPLHCACGAAFMDFLLEVQAAVPGLPSRVKCGSPGQLQGLSIFAQDLRLCLDEALSWDCFALSLLAVALGLGVPMLHHLCGWDLWYCFHLCLAWLPWRGRQSGRDEDALPYDAFVVFDKTQSAVADWVYNELRGQLEECRGRWALRLCLEERDWLPGKTLFENLWASVYGSRKTLFVLAHTDRVSGLLRASFLLAQQRLLEDRKDVVVLVILSPDGRRSRYVRLRQRLCRQSVLLWPHQPSGQRSFWAQLGMALTRDNHHFYNRNFCQGPTAE TTSHG0T TT Clinical trial TTSHG0T FM Toll like receptor TTSHG0T KE hsa04620:Toll-like receptor signaling pathway; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05152:Tuberculosis; hsa05162:Measles; hsa05168:Herpes simplex infection TTSHG0T RC R-HSA-109704:PI3K Cascade; R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-975110:TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling; R-HSA-975138:TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation; R-HSA-975155:MyD88 dependent cascade initiated on endosome TT946IA ID TT946IA TT946IA TN Transient receptor potential cation channel V3 (TRPV3) TT946IA UP Q8NET8 TT946IA UC TRPV3_HUMAN TT946IA BC Transient receptor potential catioin channel TT946IA SN Vanilloid receptor-like 3; VRL-3; TrpV3 TT946IA GN TRPV3 TT946IA FC Putative receptor-activated non-selective calcium permeant cation channel. It is activated by innocuous (warm) temperatures and shows an increased response at noxious temperatures greater than 39 degrees Celsius. Activation exhibits an outward rectification. May associate with TRPV1 and may modulate its activity. Is a negative regulator of hair growth and cycling: TRPV3-coupled signaling suppresses keratinocyte proliferation in hair follicles and induces apoptosis and premature hair follicle regression (catagen). TT946IA PD 6OT5; 6OT2; 6MHX; 6MHW; 6MHV TT946IA SQ MKAHPKEMVPLMGKRVAAPSGNPAILPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTSPPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRLKKRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNINPNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGADVNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNILHALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYILSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEMLTLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMGWLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLYLFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLGFGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGELCKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTDFNKIQDSSRNNSKTTLNAFEEVEEFPETSV TT946IA TT Clinical trial TT946IA KE hsa04750:Inflammatory mediator regulation of TRP channels TT946IA RC R-HSA-3295583:TRP channels TTKP2SU ID TTKP2SU TTKP2SU TN Transient receptor potential cation channel V4 (TRPV4) TTKP2SU UP Q9HBA0 TTKP2SU UC TRPV4_HUMAN TTKP2SU BC Transient receptor potential catioin channel TTKP2SU SN Vanilloid receptor-related osmotically-activated channel; Vanilloid receptor-like protein 2; Vanilloid receptor-like channel 2; VROAC; VRL2; VRL-2; VR-OAC; TrpV4; Transient receptor potential protein 12; Transient receptor potential cation channel subfamily V member 4; TRP12; Osm-9-like TRP channel 4; OTRPC4 TTKP2SU GN TRPV4 TTKP2SU FC Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification. Also activated by heat, low pH, citrate and phorbol esters. Increase of intracellular Ca(2+) potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism. Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers (By similarity). Acts as a regulator of intracellular Ca(2+) in synoviocytes. Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8. Together with PKD2, forms mechano- and thermosensitive channels in cilium. Negatively regulates expression of PPARGC1A, UCP1, oxidative metabolism and respiration in adipocytes (By similarity). Regulates expression of chemokines and cytokines related to proinflammatory pathway in adipocytes (By similarity). Together with AQP5, controls regulatory volume decrease in salivary epithelial cells (By similarity). Required for normal development and maintenance of bone and cartilage. TTKP2SU PD 4DX2; 4DX1 TTKP2SU SQ MADSSEGPRAGPGEVAELPGDESGTPGGEAFPLSSLANLFEGEDGSLSPSPADASRPAGPGDGRPNLRMKFQGAFRKGVPNPIDLLESTLYESSVVPGPKKAPMDSLFDYGTYRHHSSDNKRWRKKIIEKQPQSPKAPAPQPPPILKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRGQTALHIAIERRCKHYVELLVAQGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDLSSLDTCGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYPYRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCANMKVCNEDQTNCTVPTYPSCRDSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNETYQYYGFSHTVGRLRRDRWSSVVPRVVELNKNSNPDEVVVPLDSMGNPRCDGHQQGYPRKWRTDDAPL TTKP2SU TT Clinical trial TTKP2SU KE hsa04750:Inflammatory mediator regulation of TRP channels TTKP2SU RC R-HSA-3295583:TRP channels TTBK14N ID TTBK14N TTBK14N TN Transient receptor potential cation channel V6 (TRPV6) TTBK14N UP Q9H1D0 TTBK14N UC TRPV6_HUMAN TTBK14N BC Transient receptor potential catioin channel TTBK14N SN Transient receptor potential cation channel subfamily V, member 6; TRPV6; HTRP8; ECaC2; Calcium transport protein CaT1; Calcium channel CAT1 TTBK14N GN TRPV6 TTBK14N FC Calcium selective cation channel probably involved in Ca(2+) uptake in various tissues, including Ca(2+) reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin- dependent mechanism, the lattermay be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating. TTBK14N PD 6E2F; 6D7T; 6D7S; 6BOA; 6BO9 TTBK14N SQ MGPLQGDGGPALGGADVAPRLSPVRVWPRPQAPKEPALHPMGLSLPKEKGLILCLWSKFCRWFQRRESWAQSRDEQNLLQQKRIWESPLLLAAKDNDVQALNKLLKYEDCKVHQRGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTSELYEGQTALHIAVVNQNMNLVRALLARRASVSARATGTAFRRSPCNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDRHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHTQWTYGPLTSTLYDLTEIDSSGDEQSLLELIITTKKREARQILDQTPVKELVSLKWKRYGRPYFCMLGAIYLLYIICFTMCCIYRPLKPRTNNRTSPRDNTLLQQKLLQEAYMTPKDDIRLVGELVTVIGAIIILLVEVPDIFRMGVTRFFGQTILGGPFHVLIITYAFMVLVTMVMRLISASGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPEELGHFYDYPMALFSTFELFLTIIDGPANYNVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQIVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQDLNRQRIQRYAQAFHTRGSEDLDKDSVEKLELGCPFSPHLSLPMPSVSRSTSRSSANWERLRQGTLRRDLRGIINRGLEDGESWEYQI TTBK14N TT Clinical trial TTBK14N KE hsa04970:Salivary secretion; hsa04978:Mineral absorption TTBK14N RC R-HSA-3295583:TRP channels TTZSJHV ID TTZSJHV TTZSJHV TN Tryptophan 5-hydroxylase 1 (TPH1) TTZSJHV UP P17752 TTZSJHV UC TPH1_HUMAN TTZSJHV BC Paired donor oxygen oxidoreductase TTZSJHV SN Tryptophan 5-monooxygenase 1; TRPH; TPRH TTZSJHV GN TPH1 TTZSJHV FC Responsible for addition of the -HO group (hydroxylation) to the 5 position to form the amino acid 5-hydroxytryptophan (5-HTP), which is the initial and rate-limiting step in the synthesis of the neurotransmitter serotonin. TTZSJHV EC EC 1.14.16.4 TTZSJHV PD 5TPG; 5L01; 5J6D; 3HFB; 3HF8 TTZSJHV SQ MIEDNKENKDHSLERGRASLIFSLKNEVGGLIKALKIFQEKHVNLLHIESRKSKRRNSEFEIFVDCDINREQLNDIFHLLKSHTNVLSVNLPDNFTLKEDGMETVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQELNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTIKRPFGVKYNPYTRSIQILKDTKSITSAMNELQHDLDVVSDALAKVSRKPSI TTZSJHV TT Clinical trial TTZSJHV KE hsa00380:Tryptophan metabolism; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse TTG043C ID TTG043C TTG043C TN Tumor necrosis factor receptor type I (TNF-R1) TTG043C UP P19438 TTG043C UC TNR1A_HUMAN TTG043C BC Cytokine receptor TTG043C SN p60; p55; Tumor necrosis factor-binding protein 1; Tumor necrosis factor receptor superfamily member 1A; Tumor necrosis factor receptor 1; TNFR1; TNFR-I; TNFAR; TNF-RI; TBPI; CD120a TTG043C GN TNFRSF1A TTG043C FC The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. TTG043C PD 1TNR; 1NCF; 1ICH; 1FT4; 1EXT TTG043C SQ MGLSTVPDLLLPLVLLELLVGIYPSGVIGLVPHLGDREKRDSVCPQGKYIHPQNNSICCTKCHKGTYLYNDCPGPGQDTDCRECESGSFTASENHLRHCLSCSKCRKEMGQVEISSCTVDRDTVCGCRKNQYRHYWSENLFQCFNCSLCLNGTVHLSCQEKQNTVCTCHAGFFLRENECVSCSNCKKSLECTKLCLPQIENVKGTEDSGTTVLLPLVIFFGLCLLSLLFIGLMYRYQRWKSKLYSIVCGKSTPEKEGELEGTTTKPLAPNPSFSPTPGFTPTLGFSPVPSSTFTSSSTYTPGDCPNFAAPRREVAPPYQGADPILATALASDPIPNPLQKWEDSAHKPQSLDTDDPATLYAVVENVPPLRWKEFVRRLGLSDHEIDRLELQNGRCLREAQYSMLATWRRRTPRREATLELLGRVLRDMDLLGCLEDIEEALCGPAALPPAPSLLR TTG043C TT Clinical trial TTG043C FM Cytokine receptor TTG043C KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04210:Apoptosis; hsa04380:Osteoclast differentiation; hsa04668:TNF signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05010:Alzheimer's disease; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection TTG043C RC R-HSA-5357786:TNFR1-induced proapoptotic signaling; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5626978:TNFR1-mediated ceramide production; R-HSA-5669034:TNFs bind their physiological receptors; R-HSA-75893:TNF signaling TTBYWP2 ID TTBYWP2 TTBYWP2 TN TYK2 tyrosine kinase (TYK2) TTBYWP2 UP P29597 TTBYWP2 UC TYK2_HUMAN TTBYWP2 BC Kinase TTBYWP2 SN Non-receptor tyrosine-protein kinase TYK2 TTBYWP2 GN TYK2 TTBYWP2 FC Probably involved in intracellular signal transduction by being involved in the initiation of type I IFN signaling. Phosphorylates the interferon-alpha/beta receptor alpha chain. TTBYWP2 EC EC 2.7.10.2 TTBYWP2 PD 6DBM; 6DBK; 6AAM; 5WAL; 5TKD TTBYWP2 SQ MPLRHWGMARGSKPVGDGAQPMAAMGGLKVLLHWAGPGGGEPWVTFSESSLTAEEVCIHIAHKVGITPPCFNLFALFDAQAQVWLPPNHILEIPRDASLMLYFRIRFYFRNWHGMNPREPAVYRCGPPGTEASSDQTAQGMQLLDPASFEYLFEQGKHEFVNDVASLWELSTEEEIHHFKNESLGMAFLHLCHLALRHGIPLEEVAKKTSFKDCIPRSFRRHIRQHSALTRLRLRNVFRRFLRDFQPGRLSQQMVMVKYLATLERLAPRFGTERVPVCHLRLLAQAEGEPCYIRDSGVAPTDPGPESAAGPPTHEVLVTGTGGIQWWPVEEEVNKEEGSSGSSGRNPQASLFGKKAKAHKAVGQPADRPREPLWAYFCDFRDITHVVLKEHCVSIHRQDNKCLELSLPSRAAALSFVSLVDGYFRLTADSSHYLCHEVAPPRLVMSIRDGIHGPLLEPFVQAKLRPEDGLYLIHWSTSHPYRLILTVAQRSQAPDGMQSLRLRKFPIEQQDGAFVLEGWGRSFPSVRELGAALQGCLLRAGDDCFSLRRCCLPQPGETSNLIIMRGARASPRTLNLSQLSFHRVDQKEITQLSHLGQGTRTNVYEGRLRVEGSGDPEEGKMDDEDPLVPGRDRGQELRVVLKVLDPSHHDIALAFYETASLMSQVSHTHLAFVHGVCVRGPENIMVTEYVEHGPLDVWLRRERGHVPMAWKMVVAQQLASALSYLENKNLVHGNVCGRNILLARLGLAEGTSPFIKLSDPGVGLGALSREERVERIPWLAPECLPGGANSLSTAMDKWGFGATLLEICFDGEAPLQSRSPSEKEHFYQRQHRLPEPSCPQLATLTSQCLTYEPTQRPSFRTILRDLTRLQPHNLADVLTVNPDSPASDPTVFHKRYLKKIRDLGEGHFGKVSLYCYDPTNDGTGEMVAVKALKADCGPQHRSGWKQEIDILRTLYHEHIIKYKGCCEDQGEKSLQLVMEYVPLGSLRDYLPRHSIGLAQLLLFAQQICEGMAYLHAQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLELIGIAQGQMTVLRLTELLERGERLPRPDKCPCEVYHLMKNCWETEASFRPTFENLIPILKTVHEKYQGQAPSVFSVC TTBYWP2 TT Clinical trial TTBYWP2 FM Kinase TTBYWP2 KE hsa04380:Osteoclast differentiation; hsa04630:Jak-STAT signaling pathway; hsa05145:Toxoplasmosis; hsa05160:Hepatitis C; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection TTBYWP2 RC R-HSA-1059683:Interleukin-6 signaling; R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-112411:MAPK1 (ERK2) activation; R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912694:Regulation of IFNA signaling TT6TH8V ID TT6TH8V TT6TH8V TN Tyrosine-protein kinase BRK (PTK6) TT6TH8V UP Q13882 TT6TH8V UC PTK6_HUMAN TT6TH8V BC Kinase TT6TH8V SN Protein-tyrosine kinase 6; Breast tumor kinase; BRK TT6TH8V GN PTK6 TT6TH8V FC Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth. Function seems to be context dependent and differ depending on cell type, as well as its intracellular localization. A number of potential nuclear and cytoplasmic substrates have been identified. These include the RNA-binding proteins: KHDRBS1/SAM68, KHDRBS2/SLM1, KHDRBS3/SLM2 and SFPQ/PSF; transcription factors: STAT3 and STAT5A/B and a variety of signaling molecules: ARHGAP35/p190RhoGAP, PXN/paxillin, BTK/ATK, STAP2/BKS. Associates also with a variety of proteins that are likely upstream of PTK6 in various signaling pathways, or for which PTK6 may play an adapter-like role. These proteins include ADAM15, EGFR, ERBB2, ERBB3 and IRS4. In normal or non-tumorigenic tissues, PTK6 promotes cellular differentiation and apoptosis. In tumors PTK6 contributes to cancer progression by sensitizing cells to mitogenic signals and enhancing proliferation, anchorage-independent survival and migration/invasion. Association with EGFR, ERBB2, ERBB3 may contribute to mammary tumor development and growth through enhancement of EGF-induced signaling via BTK/AKT and PI3 kinase. Contributes to migration and proliferation by contributing to EGF-mediated phosphorylation of ARHGAP35/p190RhoGAP, which promotes association with RASA1/p120RasGAP, inactivating RhoA while activating RAS. EGF stimulation resulted in phosphorylation of PNX/Paxillin by PTK6 and activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. PTK6 activates STAT3 and STAT5B to promote proliferation. Nuclear PTK6 may be important for regulating growth in normal epithelia, while cytoplasmic PTK6 might activate oncogenic signaling pathways. TT6TH8V EC EC 2.7.10.2 TT6TH8V PD 6CZ4; 6CZ3; 6CZ2; 5H2U; 5DA3 TT6TH8V SQ MVSRDQAHLGPKYVGLWDFKSRTDEELSFRAGDVFHVARKEEQWWWATLLDEAGGAVAQGYVPHNYLAERETVESEPWFFGCISRSEAVRRLQAEGNATGAFLIRVSEKPSADYVLSVRDTQAVRHYKIWRRAGGRLHLNEAVSFLSLPELVNYHRAQSLSHGLRLAAPCRKHEPEPLPHWDDWERPREEFTLCRKLGSGYFGEVFEGLWKDRVQVAIKVISRDNLLHQQMLQSEIQAMKKLRHKHILALYAVVSVGDPVYIITELMAKGSLLELLRDSDEKVLPVSELLDIAWQVAEGMCYLESQNYIHRDLAARNILVGENTLCKVGDFGLARLIKEDVYLSHDHNIPYKWTAPEALSRGHYSTKSDVWSFGILLHEMFSRGQVPYPGMSNHEAFLRVDAGYRMPCPLECPPSVHKLMLTCWCRDPEQRPCFKALRERLSSFTSYENPT TT6TH8V TT Clinical trial TTW5UDX ID TTW5UDX TTW5UDX TN Urotensin II receptor (UTS2R) TTW5UDX UP Q9UKP6 TTW5UDX UC UR2R_HUMAN TTW5UDX BC GPCR rhodopsin TTW5UDX SN Urotensin-II receptor GPR14; UTS2R; UR-II-R; G protein coupled receptor 14 TTW5UDX GN UTS2R TTW5UDX FC High affinity receptor for urotensin-2 and urotensin-2B. The activity of this receptor is mediated by a G-protein that activate a phosphatidylinositol-calcium second messenger system. TTW5UDX SQ MALTPESPSSFPGLAATGSSVPEPPGGPNATLNSSWASPTEPSSLEDLVATGTIGTLLSAMGVVGVVGNAYTLVVTCRSLRAVASMYVYVVNLALADLLYLLSIPFIVATYVTKEWHFGDVGCRVLFGLDFLTMHASIFTLTVMSSERYAAVLRPLDTVQRPKGYRKLLALGTWLLALLLTLPVMLAMRLVRRGPKSLCLPAWGPRAHRAYLTLLFATSIAGPGLLIGLLYARLARAYRRSQRASFKRARRPGARALRLVLGIVLLFWACFLPFWLWQLLAQYHQAPLAPRTARIVNYLTTCLTYGNSCANPFLYTLLTRNYRDHLRGRVRGPGSGGGRGPVPSLQPRARFQRCSGRSLSSCSPQPTDSLVLAPAAPARPAPEGPRAPA TTW5UDX TT Clinical trial TTW5UDX KE hsa04080:Neuroactive ligand-receptor interaction TTW5UDX RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTNO1VA ID TTNO1VA TTNO1VA TN Utrophin (UTRN) TTNO1VA UP P46939 TTNO1VA UC UTRO_HUMAN TTNO1VA BC Zinc-finger TTNO1VA SN Dystrophin-related protein 1; DRP1; DRP-1; DMDL TTNO1VA GN UTRN TTNO1VA FC May play a role in anchoring the cytoskeleton to the plasma membrane. TTNO1VA PD 1QAG; 1BHD TTNO1VA SQ MAKYGEHEASPDNGQNEFSDIIKSRSDEHNDVQKKTFTKWINARFSKSGKPPINDMFTDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQVKDVMKDVMSDLQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPIERLEHAFSKAQTYLGIEKLLDPEDVAVQLPDKKSIIMYLTSLFEVLPQQVTIDAIREVETLPRKYKKECEEEAINIQSTAPEEEHESPRAETPSTVTEVDMDLDSYQIALEEVLTWLLSAEDTFQEQDDISDDVEEVKDQFATHEAFMMELTAHQSSVGSVLQAGNQLITQGTLSDEEEFEIQEQMTLLNARWEALRVESMDRQSRLHDVLMELQKKQLQQLSAWLTLTEERIQKMETCPLDDDVKSLQKLLEEHKSLQSDLEAEQVKVNSLTHMVVIVDENSGESATAILEDQLQKLGERWTAVCRWTEERWNRLQEINILWQELLEEQCLLKAWLTEKEEALNKVQTSNFKDQKELSVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQLLDNSKASKKINSDSEELTQRWDSLVQRLEDSSNQVTQAVAKLGMSQIPQKDLLETVRVREQAITKKSKQELPPPPPPKKRQIHVDIEAKKKFDAISAELLNWILKWKTAIQTTEIKEYMKMQDTSEMKKKLKALEKEQRERIPRADELNQTGQILVEQMGKEGLPTEEIKNVLEKVSSEWKNVSQHLEDLERKIQLQEDINAYFKQLDELEKVIKTKEEWVKHTSISESSRQSLPSLKDSCQRELTNLLGLHPKIEMARASCSALMSQPSAPDFVQRGFDSFLGRYQAVQEAVEDRQQHLENELKGQPGHAYLETLKTLKDVLNDSENKAQVSLNVLNDLAKVEKALQEKKTLDEILENQKPALHKLAEETKALEKNVHPDVEKLYKQEFDDVQGKWNKLKVLVSKDLHLLEEIALTLRAFEADSTVIEKWMDGVKDFLMKQQAAQGDDAGLQRQLDQCSAFVNEIETIESSLKNMKEIETNLRSGPVAGIKTWVQTRLGDYQTQLEKLSKEIATQKSRLSESQEKAANLKKDLAEMQEWMTQAEEEYLERDFEYKSPEELESAVEEMKRAKEDVLQKEVRVKILKDNIKLLAAKVPSGGQELTSELNVVLENYQLLCNRIRGKCHTLEEVWSCWIELLHYLDLETTWLNTLEERMKSTEVLPEKTDAVNEALESLESVLRHPADNRTQIRELGQTLIDGGILDDIISEKLEAFNSRYEDLSHLAESKQISLEKQLQVLRETDQMLQVLQESLGELDKQLTTYLTDRIDAFQVPQEAQKIQAEISAHELTLEELRRNMRSQPLTSPESRTARGGSQMDVLQRKLREVSTKFQLFQKPANFEQRMLDCKRVLDGVKAELHVLDVKDVDPDVIQTHLDKCMKLYKTLSEVKLEVETVIKTGRHIVQKQQTDNPKGMDEQLTSLKVLYNDLGAQVTEGKQDLERASQLARKMKKEAASLSEWLSATETELVQKSTSEGLLGDLDTEISWAKNVLKDLEKRKADLNTITESSAALQNLIEGSEPILEERLCVLNAGWSRVRTWTEDWCNTLMNHQNQLEIFDGNVAHISTWLYQAEALLDEIEKKPTSKQEEIVKRLVSELDDANLQVENVRDQALILMNARGSSSRELVEPKLAELNRNFEKVSQHIKSAKLLIAQEPLYQCLVTTETFETGVPFSDLEKLENDIENMLKFVEKHLESSDEDEKMDEESAQIEEVLQRGEEMLHQPMEDNKKEKIRLQLLLLHTRYNKIKAIPIQQRKMGQLASGIRSSLLPTDYLVEINKILLCMDDVELSLNVPELNTAIYEDFSFQEDSLKNIKDQLDKLGEQIAVIHEKQPDVILEASGPEAIQIRDTLTQLNAKWDRINRMYSDRKGCFDRAMEEWRQFHCDLNDLTQWITEAEELLVDTCAPGGSLDLEKARIHQQELEVGISSHQPSFAALNRTGDGIVQKLSQADGSFLKEKLAGLNQRWDAIVAEVKDRQPRLKGESKQVMKYRHQLDEIICWLTKAEHAMQKRSTTELGENLQELRDLTQEMEVHAEKLKWLNRTELEMLSDKSLSLPERDKISESLRTVNMTWNKICREVPTTLKECIQEPSSVSQTRIAAHPNVQKVVLVSSASDIPVQSHRTSEISIPADLDKTITELADWLVLIDQMLKSNIVTVGDVEEINKTVSRMKITKADLEQRHPQLDYVFTLAQNLKNKASSSDMRTAITEKLERVKNQWDGTQHGVELRQQQLEDMIIDSLQWDDHREETEELMRKYEARLYILQQARRDPLTKQISDNQILLQELGPGDGIVMAFDNVLQKLLEEYGSDDTRNVKETTEYLKTSWINLKQSIADRQNALEAEWRTVQASRRDLENFLKWIQEAETTVNVLVDASHRENALQDSILARELKQQMQDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLMSLEELIKWLNMKDEELKKQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNLQSKTELTPEERAQKIAKAMRKQSSEVKEKWESLNAVTSNWQKQVDKALEKLRDLQGAMDDLDADMKEAESVRNGWKPVGDLLIDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMSRQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQHFLSTSVQLPWQRSISHNKVPYYINHQTQTTCWDHPKMTELFQSLADLNNVRFSAYRTAIKIRRLQKALCLDLLELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWMHLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEYCIPTTSGEDVRDFTKVLKNKFRSKKYFAKHPRLGYLPVQTVLEGDNLETPITLISMWPEHYDPSQSPQLFHDDTHSRIEQYATRLAQMERTNGSFLTDSSSTTGSVEDEHALIQQYCQTLGGESPVSQPQSPAQILKSVEREERGELERIIADLEEEQRNLQVEYEQLKDQHLRRGLPVGSPPESIISPHHTSEDSELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPESDSRINGVSPWASPQHSALSYSLDPDASGPQFHQAAGEDLLAPPHDTSTDLTEVMEQIHSTFPSCCPNVPSRPQAM TTNO1VA TT Clinical trial TTNO1VA FM Zinc-finger TT7RGTM ID TT7RGTM TT7RGTM TN Voltage-gated calcium channel alpha Cav1.3 (CACNA1D) TT7RGTM UP Q01668 TT7RGTM UC CAC1D_HUMAN TT7RGTM BC Voltage-gated ion channel TT7RGTM SN Voltage-gated calcium channel alpha subunit Cav1.3; Voltage-gated L-type Ca2+ channel alpha1D; Calcium channel, L type, alpha-1 polypeptide, isoform 2; CACNA1D TT7RGTM GN CACNA1D TT7RGTM FC Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1D gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin- GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). TT7RGTM PD 3LV3 TT7RGTM SQ MMMMMMMKKMQHQRQQQADHANEANYARGTRLPLSGEGPTSQPNSSKQTVLSWQAAIDAARQAKAAQTMSTSAPPPVGSLSQRKRQQYAKSKKQGNSSNSRPARALFCLSLNNPIRRACISIVEWKPFDIFILLAIFANCVALAIYIPFPEDDSNSTNHNLEKVEYAFLIIFTVETFLKIIAYGLLLHPNAYVRNGWNLLDFVIVIVGLFSVILEQLTKETEGGNHSSGKSGGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFIGKMHKTCFFADSDIVAEEDPAPCAFSGNGRQCTANGTECRSGWVGPNGGITNFDNFAFAMLTVFQCITMEGWTDVLYWMNDAMGFELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEEEGGEEGKRNTSMPTSETESVNTENVSGEGENRGCCGSLCQAISKSKLSRRWRRWNRFNRRRCRAAVKSVTFYWLVIVLVFLNTLTISSEHYNQPDWLTQIQDIANKVLLALFTCEMLVKMYSLGLQAYFVSLFNRFDCFVVCGGITETILVELEIMSPLGISVFRCVRLLRIFKVTRHWTSLSNLVASLLNSMKSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDETQTKRSTFDNFPQALLTVFQILTGEDWNAVMYDGIMAYGGPSSSGMIVCIYFIILFICGNYILLNVFLAIAVDNLADAESLNTAQKEEAEEKERKKIARKESLENKKNNKPEVNQIANSDNKVTIDDYREEDEDKDPYPPCDVPVGEEEEEEEEDEPEVPAGPRPRRISELNMKEKIAPIPEGSAFFILSKTNPIRVGCHKLINHHIFTNLILVFIMLSSAALAAEDPIRSHSFRNTILGYFDYAFTAIFTVEILLKMTTFGAFLHKGAFCRNYFNLLDMLVVGVSLVSFGIQSSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIMIVTTLLQFMFACIGVQLFKGKFYRCTDEAKSNPEECRGLFILYKDGDVDSPVVRERIWQNSDFNFDNVLSAMMALFTVSTFEGWPALLYKAIDSNGENIGPIYNHRVEISIFFIIYIIIVAFFMMNIFVGFVIVTFQEQGEKEYKNCELDKNQRQCVEYALKARPLRRYIPKNPYQYKFWYVVNSSPFEYMMFVLIMLNTLCLAMQHYEQSKMFNDAMDILNMVFTGVFTVEMVLKVIAFKPKGYFSDAWNTFDSLIVIGSIIDVALSEADPTESENVPVPTATPGNSEESNRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIAMLFFIYAVIGMQMFGKVAMRDNNQINRNNNFQTFPQAVLLLFRCATGEAWQEIMLACLPGKLCDPESDYNPGEEYTCGSNFAIVYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWSEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVAMNMPLNSDGTVMFNATLFALVRTALKIKTEGNLEQANEELRAVIKKIWKKTSMKLLDQVVPPAGDDEVTVGKFYATFLIQDYFRKFKKRKEQGLVGKYPAKNTTIALQAGLRTLHDIGPEIRRAISCDLQDDEPEETKREEEDDVFKRNGALLGNHVNHVNSDRRDSLQQTNTTHRPLHVQRPSIPPASDTEKPLFPPAGNSVCHNHHNHNSIGKQVPTSTNANLNNANMSKAAHGKRPSIGNLEHVSENGHHSSHKHDREPQRRSSVKRTRYYETYIRSDSGDEQLPTICREDPEIHGYFRDPHCLGEQEYFSSEECYEDDSSPTWSRQNYGYYSRYPGRNIDSERPRGYHHPQGFLEDDDSPVCYDSRRSPRRRLLPPTPASHRRSSFNFECLRRQSSQEEVPSSPIFPHRTALPLHLMQQQIMAVAGLDSSKAQKYSPSHSTRSWATPPATPPYRDWTPCYTPLIQVEQSEALDQVNGSLPSLHRSSWYTDEPDISYRTFTPASLTVPSSFRNKNSDKQRSADSLVEAVLISEGLGRYARDPKFVSATKHEIADACDLTIDEMESAASTLLNGNVRPRANGDVGPLSHRQDYELQDFGPGYSDEEPDPGRDEEDLADEMICITTL TT7RGTM TT Clinical trial TT7RGTM KE hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04713:Circadian entrainment; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04727:GABAergic synapse; hsa04728:Dopaminergic synapse; hsa04911:Insulin secretion; hsa04912:GnRH signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04930:Type II diabetes mellitus; hsa04973:Carbohydrate digestion and absorption; hsa05010:Alzheimer's disease; hsa05031:Amphetamine addiction; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TT7RGTM RC R-HSA-400042:Adrenaline,noradrenaline inhibits insulin secretion; R-HSA-419037:NCAM1 interactions; R-HSA-422356:Regulation of insulin secretion TTY3UE6 ID TTY3UE6 TTY3UE6 TN Voltage-gated potassium channel Kv1.3 (KCNA3) TTY3UE6 UP P22001 TTY3UE6 UC KCNA3_HUMAN TTY3UE6 BC Voltage-gated ion channel TTY3UE6 SN Voltage-gated potassium channel subunit Kv1.3; Voltage-gated Kv1.3 K(+) channel; Voltage-gated K(+) channel Kv1.3; Potassium channel Kv1.3; KCNA3; HuKIII; HPCN3; HLK3; HGK5 TTY3UE6 GN KCNA3 TTY3UE6 FC Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. TTY3UE6 PD 4BGC TTY3UE6 SQ MDERLSLLRSPPPPSARHRAHPPQRPASSGGAHTLVNHGYAEPAAGRELPPDMTVVPGDHLLEPEVADGGGAPPQGGCGGGGCDRYEPLPPSLPAAGEQDCCGERVVINISGLRFETQLKTLCQFPETLLGDPKRRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRIRRPVNVPIDIFSEEIRFYQLGEEAMEKFREDEGFLREEERPLPRRDFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPEFRDEKDYPASTSQDSFEAAGNSTSGSRAGASSFSDPFFVVETLCIIWFSFELLVRFFACPSKATFSRNIMNLIDIVAIIPYFITLGTELAERQGNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEADDPTSGFSSIPDAFWWAVVTMTTVGYGDMHPVTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQSQYMHVGSCQHLSSSAEELRKARSNSTLSKSEYMVIEEGGMNHSAFPQTPFKTGNSTATCTTNNNPNSCVNIKKIFTDV TTY3UE6 TT Clinical trial TTY3UE6 RC R-HSA-1296072:Voltage gated Potassium channels TT3SZBT ID TT3SZBT TT3SZBT TN von Willebrand factor (VWF) TT3SZBT UP P04275 TT3SZBT UC VWF_HUMAN TT3SZBT SN vWF; F8VWF TT3SZBT GN VWF TT3SZBT FC Acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma. Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. TT3SZBT PD 6N29; 6FWN; 5BV8; 4NT5; 4DMU TT3SZBT SQ MIPARFAGVLLALALILPGTLCAEGTRGRSSTARCSLFGSDFVNTFDGSMYSFAGYCSYLLAGGCQKRSFSIIGDFQNGKRVSLSVYLGEFFDIHLFVNGTVTQGDQRVSMPYASKGLYLETEAGYYKLSGEAYGFVARIDGSGNFQVLLSDRYFNKTCGLCGNFNIFAEDDFMTQEGTLTSDPYDFANSWALSSGEQWCERASPPSSSCNISSGEMQKGLWEQCQLLKSTSVFARCHPLVDPEPFVALCEKTLCECAGGLECACPALLEYARTCAQEGMVLYGWTDHSACSPVCPAGMEYRQCVSPCARTCQSLHINEMCQERCVDGCSCPEGQLLDEGLCVESTECPCVHSGKRYPPGTSLSRDCNTCICRNSQWICSNEECPGECLVTGQSHFKSFDNRYFTFSGICQYLLARDCQDHSFSIVIETVQCADDRDAVCTRSVTVRLPGLHNSLVKLKHGAGVAMDGQDVQLPLLKGDLRIQHTVTASVRLSYGEDLQMDWDGRGRLLVKLSPVYAGKTCGLCGNYNGNQGDDFLTPSGLAEPRVEDFGNAWKLHGDCQDLQKQHSDPCALNPRMTRFSEEACAVLTSPTFEACHRAVSPLPYLRNCRYDVCSCSDGRECLCGALASYAAACAGRGVRVAWREPGRCELNCPKGQVYLQCGTPCNLTCRSLSYPDEECNEACLEGCFCPPGLYMDERGDCVPKAQCPCYYDGEIFQPEDIFSDHHTMCYCEDGFMHCTMSGVPGSLLPDAVLSSPLSHRSKRSLSCRPPMVKLVCPADNLRAEGLECTKTCQNYDLECMSMGCVSGCLCPPGMVRHENRCVALERCPCFHQGKEYAPGETVKIGCNTCVCQDRKWNCTDHVCDATCSTIGMAHYLTFDGLKYLFPGECQYVLVQDYCGSNPGTFRILVGNKGCSHPSVKCKKRVTILVEGGEIELFDGEVNVKRPMKDETHFEVVESGRYIILLLGKALSVVWDRHLSISVVLKQTYQEKVCGLCGNFDGIQNNDLTSSNLQVEEDPVDFGNSWKVSSQCADTRKVPLDSSPATCHNNIMKQTMVDSSCRILTSDVFQDCNKLVDPEPYLDVCIYDTCSCESIGDCACFCDTIAAYAHVCAQHGKVVTWRTATLCPQSCEERNLRENGYECEWRYNSCAPACQVTCQHPEPLACPVQCVEGCHAHCPPGKILDELLQTCVDPEDCPVCEVAGRRFASGKKVTLNPSDPEHCQICHCDVVNLTCEACQEPGGLVVPPTDAPVSPTTLYVEDISEPPLHDFYCSRLLDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVASTSEVLKYTLFQIFSKIDRPEASRITLLLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVGIGPHANLKQIRLIEKQAPENKAFVLSSVDELEQQRDEIVSYLCDLAPEAPPPTLPPDMAQVTVGPGLLGVSTLGPKRNSMVLDVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRTNTGLALRYLSDHSFLVSQGDREQAPNLVYMVTGNPASDEIKRLPGDIQVVPIGVGPNANVQELERIGWPNAPILIQDFETLPREAPDLVLQRCCSGEGLQIPTLSPAPDCSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTDVSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMVTLGNSFLHKLCSGFVRICMDEDGNEKRPGDVWTLPDQCHTVTCQPDGQTLLKSHRVNCDRGLRPSCPNSQSPVKVEETCGCRWTCPCVCTGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQDLEVILHNGACSPGARQGCMKSIEVKHSALSVELHSDMEVTVNGRLVSVPYVGGNMEVNVYGAIMHEVRFNHLGHIFTFTPQNNEFQLQLSPKTFASKTYGLCGICDENGANDFMLRDGTVTTDWKTLVQEWTVQRPGQTCQPILEEQCLVPDSSHCQVLLLPLFAECHKVLAPATFYAICQQDSCHQEQVCEVIASYAHLCRTNGVCVDWRTPDFCAMSCPPSLVYNHCEHGCPRHCDGNVSSCGDHPSEGCFCPPDKVMLEGSCVPEEACTQCIGEDGVQHQFLEAWVPDHQPCQICTCLSGRKVNCTTQPCPTAKAPTCGLCEVARLRQNADQCCPEYECVCDPVSCDLPPVPHCERGLQPTLTNPGECRPNFTCACRKEECKRVSPPSCPPHRLPTLRKTQCCDEYECACNCVNSTVSCPLGYLASTATNDCGCTTTTCLPDKVCVHRSTIYPVGQFWEEGCDVCTCTDMEDAVMGLRVAQCSQKPCEDSCRSGFTYVLHEGECCGRCLPSACEVVTGSPRGDSQSSWKSVGSQWASPENPCLINECVRVKEEVFIQQRNVSCPQLEVPVCPSGFQLSCKTSACCPSCRCERMEACMLNGTVIGPGKTVMIDVCTTCRCMVQVGVISGFKLECRKTTCNPCPLGYKEENNTGECCGRCLPTACTIQLRGGQIMTLKRDETLQDGCDTHFCKVNERGEYFWEKRVTGCPPFDEHKCLAEGGKIMKIPGTCCDTCEEPECNDITARLQYVKVGSCKSEVEVDIHYCQGKCASKAMYSIDINDVQDQCSCCSPTRTEPMQVALHCTNGSVVYHEVLNAMECKCSPRKCSK TT3SZBT TT Successful TT3SZBT KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04610:Complement and coagulation cascades; hsa04611:Platelet activation TT3SZBT RC R-HSA-114608:Platelet degranulation; R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-216083:Integrin cell surface interactions; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-354194:GRB2:SOS provides linkage to MAPK signaling for Integrins; R-HSA-372708:p130Cas linkage to MAPK signaling for integrins; R-HSA-430116:GP1b-IX-V activation signalling; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-75892:Platelet Adhesion to exposed collagen TTZ8UT4 ID TTZ8UT4 TTZ8UT4 TN Wilms tumor protein (WT1) TTZ8UT4 UP P19544 TTZ8UT4 UC WT1_HUMAN TTZ8UT4 BC EGR C2H2-type zinc-finger TTZ8UT4 SN Wilms' tumour 1 protein; WT33; WT1 protein TTZ8UT4 GN WT1 TTZ8UT4 FC Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'. Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors. Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing. Isoform 1 has lower affinity for DNA, and can bind RNA. Transcription factor that plays an important role in cellular development and cell survival. TTZ8UT4 PD 6BLW; 6B0R; 6B0Q; 6B0P; 6B0O TTZ8UT4 SQ MGSDVRDLNALLPAVPSLGGGGGCALPVSGAAQWAPVLDFAPPGASAYGSLGGPAPPPAPPPPPPPPPHSFIKQEPSWGGAEPHEEQCLSAFTVHFSGQFTGTAGACRYGPFGPPPPSQASSGQARMFPNAPYLPSCLESQPAIRNQGYSTVTFDGTPSYGHTPSHHAAQFPNHSFKHEDPMGQQGSLGEQQYSVPPPVYGCHTPTDSCTGSQALLLRTPYSSDNLYQMTSQLECMTWNQMNLGATLKGVAAGSSSSVKWTEGQSNHSTGYESDNHTTPILCGAQYRIHTHGVFRGIQDVRRVPGVAPTLVRSASETSEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMTKLQLAL TTZ8UT4 TT Clinical trial TTZ8UT4 FM Zinc finger TTZ8UT4 KE hsa05202:Transcriptional misregulation in cancer TTR7B60 ID TTR7B60 TTR7B60 TN X-linked inhibitor of apoptosis protein (XIAP) TTR7B60 UP P98170 TTR7B60 UC XIAP_HUMAN TTR7B60 BC Acyltransferase TTR7B60 SN hILP; hIAP3; hIAP-3; Xlinked IAP; X-linked IAP; RING-type E3 ubiquitin transferase XIAP; Inhibitor of apoptosis protein 3; ILP; IAPlike protein; IAP3; IAP-like protein; IAP-3; E3 ubiquitinprotein ligase XIAP; E3 ubiquitin-protein ligase XIAP; Baculoviral IAP repeatcontaining protein 4; Baculoviral IAP repeat-containing protein 4; BIRC4; API3 TTR7B60 GN XIAP TTR7B60 FC Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinationg COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program. Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. TTR7B60 EC EC 2.3.2.27 TTR7B60 PD 6QCI; 6EY2; 5OQW; 5O6T; 5M6M TTR7B60 SQ MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS TTR7B60 TT Clinical trial TTR7B60 FM Carbon-nitrogen ligase TTR7B60 KE hsa04064:NF-kappa B signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa04210:Apoptosis; hsa04510:Focal adhesion; hsa05145:Toxoplasmosis; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05222:Small cell lung cancer TTR7B60 RC R-HSA-111463:SMAC binds to IAPs; R-HSA-111464:SMAC-mediated dissociation of IAP:caspase complexes; R-HSA-3769402:Deactivation of the beta-catenin transactivating complex; R-HSA-5213460:RIPK1-mediated regulated necrosis; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5675482:Regulation of necroptotic cell death TTOI1RM ID TTOI1RM TTOI1RM TN A proliferation-inducing ligand (APRIL) TTOI1RM UP O75888 TTOI1RM UC TNF13_HUMAN TTOI1RM BC Cytokine: tumor necrosis factor TTOI1RM SN ZTNF2; UNQ383/PRO715; Tumor necrosis factor ligand superfamily member 13; TRDL-1; TNF-related death ligand 1; TNF- and APOL-related leukocyte expressed ligand 2; TALL2; TALL-2; CD256 TTOI1RM GN TNFSF13 TTOI1RM FC Plays a role in the regulation of tumor cell growth. May be involved in monocyte/macrophage-mediated immunological processes. Cytokine that binds to TNFRSF13B/TACI and to TNFRSF17/BCMA. TTOI1RM PD 4ZCH TTOI1RM SQ MPASSPFLLAPKGPPGNMGGPVREPALSVALWLSWGAALGAVACAMALLTQQTELQSLRREVSRLQGTGGPSQNGEGYPWQSLPEQSSDALEAWENGERSRKRRAVLTQKQKKQHSVLHLVPINATSKDDSDVTEVMWQPALRRGRGLQAQGYGVRIQDAGVYLLYSQVLFQDVTFTMGQVVSREGQGRQETLFRCIRSMPSHPDRAYNSCYSAGVFHLHQGDILSVIIPRARAKLNLSPHGTFLGFVKL TTOI1RM TT Clinical trial TTOI1RM FM Cytokine: tumor necrosis factor TTG6LA7 ID TTG6LA7 TTG6LA7 TN Activation-inducible TNFR family receptor (TNFRSF18) TTG6LA7 UP Q9Y5U5 TTG6LA7 UC TNR18_HUMAN TTG6LA7 BC Cytokine receptor TTG6LA7 SN UNQ319/PRO364; Tumor necrosis factor receptor superfamily member 18; Glucocorticoid-induced TNFR-related protein; GITR; CD357; AITR TTG6LA7 GN TNFRSF18 TTG6LA7 FC Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway. Receptor for TNFSF18. TTG6LA7 SQ MAQHGAMGAFRALCGLALLCALSLGQRPTGGPGCGPGRLLLGTGTDARCCRVHTTRCCRDYPGEECCSEWDCMCVQPEFHCGDPCCTTCRHHPCPPGQGVQSQGKFSFGFQCIDCASGTFSGGHEGHCKPWTDCTQFGFLTVFPGNKTHNAVCVPGSPPAEPLGWLTVVLLAVAACVLLLTSAQLGLHIWQLRSQCMWPRETQLLLEVPPSTEDARSCQFPEEERGERSAEEKGRLGDLWV TTG6LA7 TT Clinical trial TTG6LA7 FM Cytokine receptor TTG6LA7 KE hsa04060:Cytokine-cytokine receptor interaction TTG6LA7 RC R-HSA-5669034:TNFs bind their physiological receptors TTX2DRI ID TTX2DRI TTX2DRI TN Activin receptor type IIA (ACVR2A) TTX2DRI UP P27037 TTX2DRI UC AVR2A_HUMAN TTX2DRI BC Kinase TTX2DRI SN Activin receptor type2A; Activin receptor type-2A; ACVR2; ACTRIIA; ACTR-IIA TTX2DRI GN ACVR2A TTX2DRI FC Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. TTX2DRI EC EC 2.7.11.30 TTX2DRI PD 5NH3; 4ASX; 3SOC; 3Q4T TTX2DRI SQ MGAAAKLAFAVFLISCSSGAILGRSETQECLFFNANWEKDRTNQTGVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCVEKKDSPEVYFCCCEGNMCNEKFSYFPEMEVTQPTSNPVTPKPPYYNILLYSLVPLMLIAGIVICAFWVYRHHKMAYPPVLVPTQDPGPPPPSPLLGLKPLQLLEVKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEVYSLPGMKHENILQFIGAEKRGTSVDVDLWLITAFHEKGSLSDFLKANVVSWNELCHIAETMARGLAYLHEDIPGLKDGHKPAISHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELASRCTAADGPVDEYMLPFEEEIGQHPSLEDMQEVVVHKKKRPVLRDYWQKHAGMAMLCETIEECWDHDAEARLSAGCVGERITQMQRLTNIITTEDIVTVVTMVTNVDFPPKESSL TTX2DRI TT Clinical trial TTX2DRI FM Kinase TT0Z32T ID TT0Z32T TT0Z32T TN Adaptor-associated kinase 1 (AAK1) TT0Z32T UP Q2M2I8 TT0Z32T UC AAK1_HUMAN TT0Z32T BC Kinase TT0Z32T SN Adaptor-associated kinase 1 TT0Z32T GN AAK1 TT0Z32T FC Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity. TT0Z32T EC EC 2.7.11.1 TT0Z32T PD 5TE0; 5L4Q; 4WSQ TT0Z32T SQ MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKPQAPPSQPLPQTQAKQPQAPPTPQQTPSTQAQGLPAQAQATPQHQQQLFLKQQQQQQQPPPAQQQPAGTFYQQQQAQTQQFQAVHPATQKPAIAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQQQLATALHQQQLMTQQAALQQKPTMAAGQQPQPQPAAAPQPAPAQEPAIQAPVRQQPKVQTTPPPAVQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRTSQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQSTQGDAFATTSFSAGTAEKRKGGQTVDSGLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLLDCSLLSNPTTDLLEEFAPTAISAPVHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL TT0Z32T TT Clinical trial TT4DE1O ID TT4DE1O TT4DE1O TN Agouti-related protein (AGRP) TT4DE1O UP O00253 TT4DE1O UC AGRP_HUMAN TT4DE1O BC Agouti protein TT4DE1O SN Agouti-related peptide; Agouti related protein; AGRP TT4DE1O GN AGRP TT4DE1O FC Plays a role in weight homeostasis. Involved in the control of feeding behavior through the central melanocortin system. Acts as alpha melanocyte-stimulating hormone antagonist by inhibiting cAMP production mediated by stimulation of melanocortin receptors within the hypothalamus and adrenal gland. Has very low activity with MC5R. Is an inverse agonist for MC3R and MC4R being able to suppress their constitutive activity. It promotes MC3R and MC4R endocytosis in an arrestin-dependent manner. TT4DE1O PD 2IQV; 1MR0; 1HYK TT4DE1O SQ MLTAAVLSCALLLALPATRGAQMGLAPMEGIRRPDQALLPELPGLGLRAPLKKTTAEQAEEDLLQEAQALAEVLDLQDREPRSSRRCVRLHESCLGQQVPCCDPCATCYCRFFNAFCYCRKLGTAMNPCSRT TT4DE1O TT Clinical trial TT4DE1O KE hsa04920:Adipocytokine signaling pathway TTCFEA1 ID TTCFEA1 TTCFEA1 TN Alpha-fetoprotein (AFP) TTCFEA1 UP P02771 TTCFEA1 UC FETA_HUMAN TTCFEA1 BC Serum albumin family TTCFEA1 SN Alpha-fetoglobulin; Alpha-1-fetoprotein; AFP TTCFEA1 GN AFP TTCFEA1 FC Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. Only a small percentage (less than 2%) of the human AFP shows estrogen-binding properties. TTCFEA1 PD 3MRK TTCFEA1 SQ MKWVESIFLIFLLNFTESRTLHRNEYGIASILDSYQCTAEISLADLATIFFAQFVQEATYKEVSKMVKDALTAIEKPTGDEQSSGCLENQLPAFLEELCHEKEILEKYGHSDCCSQSEEGRHNCFLAHKKPTPASIPLFQVPEPVTSCEAYEEDRETFMNKFIYEIARRHPFLYAPTILLWAARYDKIIPSCCKAENAVECFQTKAATVTKELRESSLLNQHACAVMKNFGTRTFQAITVTKLSQKFTKVNFTEIQKLVLDVAHVHEHCCRGDVLDCLQDGEKIMSYICSQQDTLSNKITECCKLTTLERGQCIIHAENDEKPEGLSPNLNRFLGDRDFNQFSSGEKNIFLASFVHEYSRRHPQLAVSVILRVAKGYQELLEKCFQTENPLECQDKGEEELQKYIQESQALAKRSCGLFQKLGEYYLQNAFLVAYTKKAPQLTSSELMAITRKMAATAATCCQLSEDKLLACGEGAADIIIGHLCIRHEMTPVNPGVGQCCTSSYANRRPCFSSLVVDETYVPPAFSDDKFIFHKDLCQAQGVALQTMKQEFLINLVKQKPQITEEQLEAVIADFSGLLEKCCQGQEQEVCFAEEGQKLISKTRAALGV TTCFEA1 TT Clinical trial TTCFEA1 KE hsa04390:Hippo signaling pathway TTH8T6I ID TTH8T6I TTH8T6I TN Alpha-ketoglutarate dehydrogenase (OGDH) TTH8T6I UP Q02218 TTH8T6I UC ODO1_HUMAN TTH8T6I BC Aldehyde/oxo donor oxidoreductase TTH8T6I SN OGDC-E1; 2-oxoglutarate dehydrogenase, mitochondrial; 2-oxoglutarate dehydrogenase complex component E1 TTH8T6I GN OGDH TTH8T6I FC The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A. 2-oxoglutarate dehydrogenase (E1) component of the 2-oxoglutarate dehydrogenase complex, which mediates the decarboxylation of alpha-ketoglutarate. TTH8T6I EC EC 1.2.4.2 TTH8T6I PD 3ERY TTH8T6I SQ MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEEMYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNVDKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDESDLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFETPGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSENGVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINRVTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVMSILLHGDAAFAGQGIVYETFHLSDLPSYTTHGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNSDDPEAVMYVCKVAAEWRSTFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIRKQKPVLQKYAELLVSQGVVNQPEYEEEISKYDKICEEAFARSKDEKILHIKHWLDSPWPGFFTLDGQPRSMSCPSTGLTEDILTHIGNVASSVPVENFTIHGGLSRILKTRGEMVKNRTVDWALAEYMAFGSLLKEGIHIRLSGQDVERGTFSHRHHVLHDQNVDKRTCIPMNHLWPNQAPYTVCNSSLSEYGVLGFELGFAMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLPHGMEGMGPEHSSARPERFLQMCNDDPDVLPDLKEANFDINQLYDCNWVVVNCSTPGNFFHVLRRQILLPFRKPLIIFTPKSLLRHPEARSSFDEMLPGTHFQRVIPEDGPAAQNPENVKRLLFCTGKVYYDLTRERKARDMVGQVAITRIEQLSPFPFDLLLKEVQKYPNAELAWCQEEHKNQGYYDYVKPRLRTTISRAKPVWYAGRDPAAAPATGNKKTHLTELQRLLDTAFDLDVFKNFS TTH8T6I TT Clinical trial TTLAFZV ID TTLAFZV TTLAFZV TN AMP-activated protein kinase (AMPK) TTLAFZV UP Q13131; Q9Y478; P54619 TTLAFZV UC AAPK1_HUMAN; AAKB1_HUMAN; AAKG1_HUMAN TTLAFZV BC Kinase TTLAFZV SN AMPK; 5'-AMP-activated protein kinase TTLAFZV GN PRKAA1; PRKAB1; PRKAG1 TTLAFZV FC Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. TTLAFZV SQ MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ TTLAFZV TT Clinical trial TTLAFZV KE hsa04068:FoxO signaling pathway; hsa04140:Regulation of autophagy; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04710:Circadian rhythm; hsa04910:Insulin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04922:Glucagon signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05410:Hypertrophic cardiomyopathy (HCM) TTLAFZV RC R-HSA-1445148:Translocation of GLUT4 to the plasma membrane; R-HSA-1632852:Macroautophagy; R-HSA-2151209:Activation of PPARGC1A (PGC-1alpha) by phosphorylation; R-HSA-5628897:TP53 Regulates Metabolic Genes TT59GO7 ID TT59GO7 TT59GO7 TN ANGPTL3 messenger RNA (ANGPTL3 mRNA) TT59GO7 UP Q9Y5C1 TT59GO7 UC ANGL3_HUMAN TT59GO7 BC mRNA target TT59GO7 SN UNQ153/PRO179 (mRNA); Angiopoietin-related protein 3 (mRNA); Angiopoietin-like protein 3 (mRNA); Angiopoietin-5 (mRNA); ANGPT5 (mRNA); ANG-5 (mRNA) TT59GO7 GN ANGPTL3 TT59GO7 FC Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake. Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1. Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids. Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol. Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL)-TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT. Contributes to lower plasma levels of low density lipoprotein (LDL)-cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR. May stimulate hypothalamic LPL activity. Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. TT59GO7 PD 6EUA TT59GO7 SQ MFTIKLLLFIVPLVISSRIDQDNSSFDSLSPEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQPETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEISLSSKPRAPRTTPFLQLNEIRNVKHDGIPAECTTIYNRGEHTSGMYAIRPSNSQVFHVYCDVISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKIYSIVKQSNYVLRIELEDWKDNKHYIEYSFYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGHFNCPEGYSGGWWWHDECGENNLNGKYNKPRAKSKPERRRGLSWKSQNGRLYSIKSTKMLIHPTDSESFE TT59GO7 TT Clinical trial TT59GO7 FM mRNA target TT2Z83I ID TT2Z83I TT2Z83I TN Annexin A5 (ANXA5) TT2Z83I UP P08758 TT2Z83I UC ANXA5_HUMAN TT2Z83I BC Annexin protein TT2Z83I SN Vascular anticoagulantalpha; Vascular anticoagulant-alpha; VACalpha; VAC-alpha; Thromboplastin inhibitor; Placental anticoagulant protein I; Placental anticoagulant protein 4; PP4; PAPI; PAP-I; Lipocortin V; Endonexin II; ENX2; Calphobindin I; CBPI; CBP-I; Annexin5; Annexin-5; Annexin V; Anchorin CII; ANX5 TT2Z83I GN ANXA5 TT2Z83I FC This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. TT2Z83I PD 2XO3; 2XO2; 1SAV; 1HVG; 1HVF TT2Z83I SQ MAQVLRGTVTDFPGFDERADAETLRKAMKGLGTDEESILTLLTSRSNAQRQEISAAFKTLFGRDLLDDLKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTNEKVLTEIIASRTPEELRAIKQVYEEEYGSSLEDDVVGDTSGYYQRMLVVLLQANRDPDAGIDEAQVEQDAQALFQAGELKWGTDEEKFITIFGTRSVSHLRKVFDKYMTISGFQIEETIDRETSGNLEQLLLAVVKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVMVSRSEIDLFNIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLCGEDD TT2Z83I TT Clinical trial TT2Z83I FM Annexin family TT4L35O ID TT4L35O TT4L35O TN Apolipoprotein C-III (ApoCIII) TT4L35O UP P02656 TT4L35O UC APOC3_HUMAN TT4L35O BC Apolipoprotein TT4L35O SN Apolipoprotein CIII; Apolipoprotein C3; ApoC-III; Apo-CIII TT4L35O GN APOC3 TT4L35O FC Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners. Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. TT4L35O PD 2JQ3 TT4L35O SQ MQPRVLLVVALLALLASARASEAEDASLLSFMQGYMKHATKTAKDALSSVQESQVAQQARGWVTDGFSSLKDYWSTVKDKFSEFWDLDPEVRPTSAVAA TT4L35O TT Clinical trial TT4L35O FM Apolipoprotein TT4L35O KE hsa03320:PPAR signaling pathway TT4L35O RC R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-194223:HDL-mediated lipid transport; R-HSA-975634:Retinoid metabolism and transport TTKS9CB ID TTKS9CB TTKS9CB TN Apolipoprotein E (APOE) TTKS9CB UP P02649 TTKS9CB UC APOE_HUMAN TTKS9CB BC Apolipoprotein TTKS9CB SN ApoE; Apo-E TTKS9CB GN APOE TTKS9CB FC APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating to the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. APOE in also involved in innate and adaptive immune responses, controlling for instance the survival of myeloid-derived suppressor cells. APOE, may also play a role in transcription regulation through a receptor-dependent and cholesterol-independent mechanism, that activates MAP3K12 and a non-canonical MAPK signal transduction pathway that results in enhanced AP-1-mediated transcription of APP. APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. TTKS9CB PD 6NCO; 6NCN; 2L7B; 2KNY; 2KC3 TTKS9CB SQ MKVLWAALLVTFLAGCQAKVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRGEVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGLSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGTSAAPVPSDNH TTKS9CB TT Clinical trial TTKS9CB FM Apolipoprotein TTKS9CB KE hsa05010:Alzheimer's disease TTKS9CB RC R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-194223:HDL-mediated lipid transport; R-HSA-3000480:Scavenging by Class A Receptors; R-HSA-975634:Retinoid metabolism and transport TTGMFY7 ID TTGMFY7 TTGMFY7 TN Aspartyl aminopeptidase (DNPEP) TTGMFY7 UP Q9ULA0 TTGMFY7 UC DNPEP_HUMAN TTGMFY7 BC Peptidase TTGMFY7 SN DAP; ASPEP TTGMFY7 GN DNPEP TTGMFY7 FC Likely to play an important role in intracellular protein and peptide metabolism. Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. TTGMFY7 EC EC 3.4.11.21 TTGMFY7 PD 4DYO TTGMFY7 SQ MSGHSPTRGAMQVAMNGKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKWNIKPESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFGPNTEMHLVPILATAIQEELEKGTPEPGPLNAVDERHHSVLMSLLCAHLGLSPKDIVEMELCLADTQPAVLGGAYDEFIFAPRLDNLHSCFCALQALIDSCAGPGSLATEPHVRMVTLYDNEEVGSESAQGAQSLLTELVLRRISASCQHPTAFEEAIPKSFMISADMAHAVHPNYLDKHEENHRPLFHKGPVIKVNSKQRYASNAVSEALIREVANKVKVPLQDLMVRNDTPCGTTIGPILASRLGLRVLDLGSPQLAMHSIREMACTTGVLQTLTLFKGFFELFPSLSHNLLVD TTGMFY7 TT Clinical trial TTLB52K ID TTLB52K TTLB52K TN ATP-binding cassette transporter A4 (ABCA4) TTLB52K UP P78363 TTLB52K UC ABCA4_HUMAN TTLB52K BC ABC transporter TTLB52K SN Stargardt disease protein; RmP; Retinal-specific ATP-binding cassette transporter; RIM protein; RIM ABC transporter; ATP-binding cassette sub-family A member 4; ABCA4 TTLB52K GN ABCA4 TTLB52K FC In the visualcycle, acts as an inward-directed retinoid flipase, retinoid substrates imported by ABCA4 from the extracellular or intradiscal (rod) membrane surfaces to the cytoplasmic membrane surface are all-trans-retinaldehyde (ATR) and N-retinyl-phosphatidyl-ethanolamine (NR-PE). Once transported to the cytoplasmic surface, ATR is reduced to vitamin A by trans- retinol dehydrogenase (tRDH) and then transferred to the retinal pigment epithelium (RPE) where it is converted to 11-cis-retinal. May play a role in photoresponse, removing ATR/NR-PE from the extracellular photoreceptor surfaces during bleach recovery. TTLB52K EC EC 7.6.2.1 TTLB52K SQ MGFVRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSHHECHFPNKAMPSAGMLPWLQGIFCNVNNPCFQSPTPGESPGIVSNYNNSILARVYRDFQELLMNAPESQHLGRIWTELHILSQFMDTLRTHPERIAGRGIRIRDILKDEETLTLFLIKNIGLSDSVVYLLINSQVRPEQFAHGVPDLALKDIACSEALLERFIIFSQRRGAKTVRYALCSLSQGTLQWIEDTLYANVDFFKLFRVLPTLLDSRSQGINLRSWGGILSDMSPRIQEFIHRPSMQDLLWVTRPLMQNGGPETFTKLMGILSDLLCGYPEGGGSRVLSFNWYEDNNYKAFLGIDSTRKDPIYSYDRRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILYTPDSPAARRILKNANSTFEELEHVRKLVKAWEEVGPQIWYFFDNSTQMNMIRDTLGNPTVKDFLNRQLGEEGITAEAILNFLYKGPRESQADDMANFDWRDIFNITDRTLRLVNQYLECLVLDKFESYNDETQLTQRALSLLEENMFWAGVVFPDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQVQAEAPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMLCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTAELKKAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPTEGDEFSFLLSMQMMLLDAAVYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEETEDPEHPEGIHDSFFEREHPGWVPGVCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFLKNCFGTGLYLTLVRKMKNIQSQRKGSEGTCSCSSKGFSTTCPAHVDDLTPEQVLDGDVNELMDVVLHHVPEAKLVECIGQELIFLLPNKNFKHRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDSDSGPLFAGGAQQKRENVNPRHPCLGPREKAGQTPQDSNVCSPGAPAAHPEGQPPPEPECPGPQLNTGTQLVLQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIVIPPFGEYPALTLHPWIYGQQYTFFSMDEPGSEQFTVLADVLLNKPGFGNRCLKEGWLPEYPCGNSTPWKTPSVSPNITQLFQKQKWTQVNPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPVVPITGEALVGFLSDLGRIMNVSGGPITREASKEIPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRSPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFSMSFVPASFVLYLIQERVNKSKHLQFISGVSPTTYWVTNFLWDIMNYSVSAGLVVGIFIGFQKKAYTSPENLPALVALLLLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFILELFENNRTLLRFNAVLRKLLIVFPHFCLGRGLIDLALSQAVTDVYARFGEEHSANPFHWDLIGKNLFAMVVEGVVYFLLTLLVQRHFFLSQWIAEPTKEPIVDEDDDVAEERQRIITGGNKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGDGYIVTMKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFQLLLSHKDSLLIEEYSVTQTTLDQVFVNFAKQQTESHDLPLHPRAAGASRQAQD TTLB52K TT Clinical trial TTLB52K KE hsa02010:ABC transporters TTLB52K RC R-HSA-2453864:Retinoid cycle disease events; R-HSA-2453902:The canonical retinoid cycle in rods (twilight vision); R-HSA-382556:ABC-family proteins mediated transport TTNB7IF ID TTNB7IF TTNB7IF TN Atrial natriuretic peptide receptor B (NPR2) TTNB7IF UP P20594 TTNB7IF UC ANPRB_HUMAN TTNB7IF BC Phosphorus-oxygen lyase TTNB7IF SN NPR-B; Guanylate cyclase B; GC-B; Atrial natriuretic peptide receptor type B; Atrial natriuretic peptide receptor 2; ANPRB; ANPR-B; ANP-B TTNB7IF GN NPR2 TTNB7IF FC Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth. TTNB7IF EC EC 4.6.1.2 TTNB7IF SQ MALPSLLLLVAALAGGVRPPGARNLTLAVVLPEHNLSYAWAWPRVGPAVALAVEALGRALPVDLRFVSSELEGACSEYLAPLSAVDLKLYHDPDLLLGPGCVYPAASVARFASHWRLPLLTAGAVASGFSAKNDHYRTLVRTGPSAPKLGEFVVTLHGHFNWTARAALLYLDARTDDRPHYFTIEGVFEALQGSNLSVQHQVYAREPGGPEQATHFIRANGRIVYICGPLEMLHEILLQAQRENLTNGDYVFFYLDVFGESLRAGPTRATGRPWQDNRTREQAQALREAFQTVLVITYREPPNPEYQEFQNRLLIRAREDFGVELGPSLMNLIAGCFYDGILLYAEVLNETIQEGGTREDGLRIVEKMQGRRYHGVTGLVVMDKNNDRETDFVLWAMGDLDSGDFQPAAHYSGAEKQIWWTGRPIPWVKGAPPSDNPPCAFDLDDPSCDKTPLSTLAIVALGTGITFIMFGVSSFLIFRKLMLEKELASMLWRIRWEELQFGNSERYHKGAGSRLTLSLRGSSYGSLMTAHGKYQIFANTGHFKGNVVAIKHVNKKRIELTRQVLFELKHMRDVQFNHLTRFIGACIDPPNICIVTEYCPRGSLQDILENDSINLDWMFRYSLINDLVKGMAFLHNSIISSHGSLKSSNCVVDSRFVLKITDYGLASFRSTAEPDDSHALYAKKLWTAPELLSGNPLPTTGMQKADVYSFGIILQEIALRSGPFYLEGLDLSPKEIVQKVRNGQRPYFRPSIDRTQLNEELVLLMERCWAQDPAERPDFGQIKGFIRRFNKEGGTSILDNLLLRMEQYANNLEKLVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAIIDNFDVYKVETIGDAYMVVSGLPGRNGQRHAPEIARMALALLDAVSSFRIRHRPHDQLRLRIGVHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGQALKIHVSSTTKDALDELGCFQLELRGDVEMKGKGKMRTYWLLGERKGPPGLL TTNB7IF TT Clinical trial TT6CQUM ID TT6CQUM TT6CQUM TN B7 homolog 3 (CD276) TT6CQUM UP Q5ZPR3 TT6CQUM UC CD276_HUMAN TT6CQUM BC Immunoglobulin TT6CQUM SN UNQ309/PRO352; PSEC0249; Costimulatory molecule; CD276 antigen; B7H3; B7-H3; 4IgB7H3; 4Ig-B7-H3 TT6CQUM GN CD276 TT6CQUM FC May play a protective role in tumor cells by inhibiting natural-killer mediated cell lysis as well as a role of marker for detection of neuroblastoma cells. May be involved in the development of acute and chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. Could also play a key role in providing the placenta and fetus with a suitable immunological environment throughout pregnancy. Both isoform 1 and isoform 2 appear to be redundant in their ability to modulate CD4 T-cell responses. Isoform 2 is shown to enhance the induction of cytotoxic T-cells and selectively stimulates interferon gamma production in the presence of T-cell receptor signaling. May participate in the regulation of T-cell-mediated immune response. TT6CQUM SQ MLRRRGSPGMGVHVGAALGALWFCLTGALEVQVPEDPVVALVGTDATLCCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFAEGQDQGSAYANRTALFPDLLAQGNASLRLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPYSKPSMTLEPNKDLRPGDTVTITCSSYQGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSILRVVLGANGTYSCLVRNPVLQQDAHSSVTITPQRSPTGAVEVQVPEDPVVALVGTDATLRCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFTEGRDQGSAYANRTALFPDLLAQGNASLRLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPYSKPSMTLEPNKDLRPGDTVTITCSSYRGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSVLRVVLGANGTYSCLVRNPVLQQDAHGSVTITGQPMTFPPEALWVTVGLSVCLIALLVALAFVCWRKIKQSCEEENAGAEDQDGEGEGSKTALQPLKHSDSKEDDGQEIA TT6CQUM TT Clinical trial TT6CQUM FM Immunoglobulin superfamily TT6CQUM KE hsa04514:Cell adhesion molecules (CAMs) TTQ8J1V ID TTQ8J1V TTQ8J1V TN Bacterial Deoxy-manno-octulosonate cytidylyltransferase (Bact kdsB) TTQ8J1V UP P04951 TTQ8J1V UC KDSB_ECOLI TTQ8J1V BC Kinase TTQ8J1V SN kdsB; CMP-KDO synthetase; CMP-2-keto-3-deoxyoctulosonic acid synthetase; CKS; 3-deoxy-D-manno-octulosonate cytidylytransferase TTQ8J1V GN Bact kdsB TTQ8J1V FC Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. TTQ8J1V EC EC 2.7.7.38 TTQ8J1V PD 3K8E; 3K8D; 1VH1 TTQ8J1V SQ MSFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGAERIIVATDHEDVARAVEAAGGEVCMTRADHQSGTERLAEVVEKCAFSDDTVIVNVQGDEPMIPATIIRQVADNLAQRQVGMATLAVPIHNAEEAFNPNAVKVVLDAEGYALYFSRATIPWDRDRFAEGLETVGDNFLRHLGIYGYRAGFIRRYVNWQPSPLEHIEMLEQLRVLWYGEKIHVAVAQEVPGTGVDTPEDLERVRAEMR TTQ8J1V TT Clinical trial TTC67I0 ID TTC67I0 TTC67I0 TN Bacterial Glucosamine-6-phosphate synthase (Bact glmS) TTC67I0 UP P17169 TTC67I0 UC GLMS_ECOLI TTC67I0 BC Transaminase TTC67I0 SN glmS; L-glutamine-D-fructose-6-phosphate amidotransferase; Hexosephosphate aminotransferase; Glucosamine--fructose-6-phosphate aminotransferase; GFAT; D-fructose-6-phosphate amidotransferase TTC67I0 GN Bact glmS TTC67I0 FC Catalyzesthe first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. TTC67I0 EC EC 2.6.1.16 TTC67I0 PD 4AMV; 3OOJ; 2VF5; 2VF4; 2J6H TTC67I0 SQ MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE TTC67I0 TT Clinical trial TT7NJSE ID TT7NJSE TT7NJSE TN B-cell-activating factor receptor (TNFRSF13C) TT7NJSE UP Q96RJ3 TT7NJSE UC TR13C_HUMAN TT7NJSE BC Cytokine receptor TT7NJSE SN Tumor necrosis factor receptor superfamily member 13C; CD268; BR3; BLyS receptor 3; BAFFR; BAFF-R; BAFF receptor; B cell-activating factor receptor TT7NJSE GN TNFRSF13C TT7NJSE FC Promotes the survival of mature B-cells and the B-cell response. B-cell receptor specific for TNFSF13B/TALL1/BAFF/BLyS. TT7NJSE PD 4V46; 3V56; 2HFG; 1OSX; 1OQE TT7NJSE SQ MRRGPRSLRGRDAPAPTPCVPAECFDLLVRHCVACGLLRTPRPKPAGASSPAPRTALQPQESVGAGAGEAALPLPGLLFGAPALLGLALVLALVLVGLVSWRRRQRRLRGASSAEAPDGDKDAPEPLDKVIILSPGISDATAPAWPPPGEDPGTTPPGHSVPVPATELGSTELVTTKTAGPEQQ TT7NJSE TT Clinical trial TT7NJSE FM Cytokine receptor TT7NJSE RC R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway TTBN5I7 ID TTBN5I7 TTBN5I7 TN B-cell-specific glycoprotein B29 (CD79B) TTBN5I7 UP P40259 TTBN5I7 UC CD79B_HUMAN TTBN5I7 BC Immunoglobulin TTBN5I7 SN Immunoglobulinassociated B29 protein; Immunoglobulin-associated B29 protein; Igbeta; Ig-beta; IGB; CD79b; Bcellspecific glycoprotein B29; Bcell antigen receptor complexassociated protein beta chain; B29; B-cell antigen receptor complex-associated protein beta chain TTBN5I7 GN CD79B TTBN5I7 FC Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation. Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. TTBN5I7 PD 3KG5 TTBN5I7 SQ MARLALSPVPSHWMVALLLLLSAEPVPAARSEDRYRNPKGSACSRIWQSPRFIARKRGFTVKMHCYMNSASGNVSWLWKQEMDENPQQLKLEKGRMEESQNESLATLTIQGIRFEDNGIYFCQQKCNNTSEVYQGCGTELRVMGFSTLAQLKQRNTLKDGIIMIQTLLIILFIIVPIFLLLDKDDSKAGMEEDHTYEGLDIDQTATYEDIVTLRTGEVKWSVGEHPGQE TTBN5I7 TT Successful TTBN5I7 KE hsa04662:B cell receptor signaling pathway TTBN5I7 RC R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TT2I6UX ID TT2I6UX TT2I6UX TN Beta-N-acetylhexosaminidase (OGA) TT2I6UX UP O60502 TT2I6UX UC OGA_HUMAN TT2I6UX BC Glycosylase TT2I6UX SN OGA; Nuclear cytoplasmic OGlcNAcase and acetyltransferase; Meningiomaexpressed antigen 5; MGEA5; Histone acetyltransferase; Bifunctional protein NCOAT TT2I6UX GN MGEA5 TT2I6UX FC Isoform 3: Cleaves GlcNAc but not GalNAc from O- glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl- alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform1. {ECO:0000269|PubMed:20673219}. TT2I6UX EC EC 3.2.1.169 TT2I6UX PD 6HKI; 5VVX; 5VVV; 5VVU; 5VVT TT2I6UX SQ MVQKESQATLEERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKASVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPTTLTKEEEKKQPDEEPMDMVVEKQEETDHKNDNQILSEIVEAKMAEELKPMDTDKESIAESKSPEMSMQEDCISDIAPMQTDEQTNKEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCGLVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGLPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL TT2I6UX TT Clinical trial TTHYDUM ID TTHYDUM TTHYDUM TN Bombesin receptor (BS) TTHYDUM UP P28336; P30550; P32247 TTHYDUM UC NMBR_HUMAN; GRPR_HUMAN; BRS3_HUMAN TTHYDUM BC GPCR rhodopsin TTHYDUM SN BB TTHYDUM GN NMBR; GRPR; BRS3 TTHYDUM FC Bombesin receptor activity. G protein-coupled receptor activity. Receptor for neuromedin-B. G protein-coupled receptor signaling pathway. Phospholipase C-activating G protein-coupled receptor signaling pathway. TTHYDUM SQ MPSKSLSNLSVTTGANESGSVPEGWERDFLPASDGTTTELVIRCVIPSLYLLIITVGLLGNIMLVKIFITNSAMRSVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWMFGKVGCKLIPVIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGALLRTCVKAMGIWVVSVLLAVPEAVFSEVARISSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLAIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFIFCWFPNHILYMYRSFNYNEIDPSLGHMIVTLVARVLSFGNSCVNPFALYLLSESFRRHFNSQLCCGRKSYQERGTSYLLSSSAVRMTSLKSNAKNMVTNSVLLNGHSMKQEMAL TTHYDUM TT Clinical trial TTHYDUM KE hsa04080:Neuroactive ligand-receptor interaction TTHYDUM RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTP3IGX ID TTP3IGX TTP3IGX TN Bone morphogenetic protein 2 (BMP2) TTP3IGX UP P12643 TTP3IGX UC BMP2_HUMAN TTP3IGX BC Growth factor TTP3IGX SN Bone morphogenetic protein 2A; BMP2A; BMP-2A; BMP-2 TTP3IGX GN BMP2 TTP3IGX FC Stimulates the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A- ATF4 pathway. BMP2 activation of EIF2AK3 stimulates phosphorylation of EIF2A which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation. In addition stimulates TMEM119, which upregulates the expression of ATF4. Induces cartilage and bone formation. TTP3IGX PD 6OMN; 4UI2; 4UI1; 4UI0; 4UHZ TTP3IGX SQ MVAGTRCLLALLLPQVLLGGAAGLVPELGRRKFAAASSGRPSSQPSDEVLSEFELRLLSMFGLKQRPTPSRDAVVPPYMLDLYRRHSGQPGSPAPDHRLERAASRANTVRSFHHEESLEELPETSGKTTRRFFFNLSSIPTEEFITSAELQVFREQMQDALGNNSSFHHRINIYEIIKPATANSKFPVTRLLDTRLVNQNASRWESFDVTPAVMRWTAQGHANHGFVVEVAHLEEKQGVSKRHVRISRSLHQDEHSWSQIRPLLVTFGHDGKGHPLHKREKRQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR TTP3IGX TT Clinical trial TTP3IGX FM Transforming growth factor TTP3IGX KE hsa04060:Cytokine-cytokine receptor interaction; hsa04340:Hedgehog signaling pathway; hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa05200:Pathways in cancer; hsa05217:Basal cell carcinoma TTP3IGX RC R-HSA-2129379:Molecules associated with elastic fibres TTSMLOH ID TTSMLOH TTSMLOH TN Brain-derived neurotrophic factor (BDNF) TTSMLOH UP P23560 TTSMLOH UC BDNF_HUMAN TTSMLOH BC Growth factor TTSMLOH SN Brainderived neurotrophic factor; Abrineurin TTSMLOH GN BDNF TTSMLOH FC Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability. During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. TTSMLOH PD 1BND; 1B8M TTSMLOH SQ MTILFLTMVISYFGCMKAAPMKEANIRGQGGLAYPGVRTHGTLESVNGPKAGSRGLTSLADTFEHVIEELLDEDQKVRPNEENNKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR TTSMLOH TT Clinical trial TTSMLOH FM Growth factor TTSMLOH KE hsa04010:MAPK signaling pathway; hsa04024:cAMP signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa05016:Huntington's disease; hsa05030:Cocaine addiction; hsa05034:Alcoholism TT2T5M0 ID TT2T5M0 TT2T5M0 TN Calcium-activated potassium channel KCa2.2 (KCNN2) TT2T5M0 UP Q9H2S1 TT2T5M0 UC KCNN2_HUMAN TT2T5M0 BC Voltage-gated ion channel TT2T5M0 SN Small conductance calcium-activated potassium channel protein 2; SKCa2; SKCa 2; SK2; KCa2.2 TT2T5M0 GN KCNN2 TT2T5M0 FC Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin. TT2T5M0 PD 6ALE; 5WC5; 5WBX; 5V02 TT2T5M0 SQ MSSCRYNGGVMRPLSNLSASRRNLHEMDSEAQPLQPPASVGGGGGASSPSAAAAAAAAVSSSAPEIVVSKPEHNNSNNLALYGTGGGGSTGGGGGGGGSGHGSSSGTKSSKKKNQNIGYKLGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSWGAYDKASLYSLALKCLISLSTIILLGLIIVYHAREIQLFMVDNGADDWRIAMTYERIFFICLEILVCAIHPIPGNYTFTWTARLAFSYAPSTTTADVDIILSIPMFLRLYLIARVMLLHSKLFTDASSRSIGALNKINFNTRFVMKTLMTICPGTVLLVFSISLWIIAAWTVRACERYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPNTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQNIMYDMISDLNERSEDFEKRIVTLETKLETLIGSIHALPGLISQTIRQQQRDFIEAQMESYDKHVTYNAERSRSSSRRRRSSSTAPPTSSESS TT2T5M0 TT Clinical trial TTE76YK ID TTE76YK TTE76YK TN Calcium-release activated calcium channel (CRACM) TTE76YK UP Q96D31 TTE76YK UC CRCM1_HUMAN TTE76YK SN Transmembrane protein 142A; TMEM142A; Protein orai-1; Calcium release-activated calcium channel protein 1; CRACM1 TTE76YK GN ORAI1 TTE76YK FC CRAC channels are the main pathway for Ca(2+) influx in T-cells and promote the immune response to pathogens by activating the transcription factor NFAT. Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which mediates Ca(2+) influx following depletion of intracellular Ca(2+) stores and channel activation by the Ca(2+) sensor, STIM1. TTE76YK PD 4EHQ; 2MAK TTE76YK SQ MHPEPAPPPSRSSPELPPSGGSTTSGSRRSRRRSGDGEPPGAPPPPPSAVTYPDWIGQSYSEVMSLNEHSMQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLDADHDYPPGLLIAFSACTTVLVAVHLFALMISTCILPNIEAVSNVHNLNSVKESPHERMHRHIELAWAFSTVIGTLLFLAEVVLLCWVKFLPLKKQPGQPRPTSKPPASGAAANVSTSGITPGQAAAIASTTIMVPFGLIFIVFAVHFYRSLVSHKTDRQFQELNELAEFARLQDQLDHRGDHPLTPGSHYA TTE76YK TT Clinical trial TTE76YK KE hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04611:Platelet activation; hsa05340:Primary immunodeficiency TTE76YK RC R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTFYL58 ID TTFYL58 TTFYL58 TN CaM-kinase II (CAMK2) TTFYL58 UP Q9UQM7; Q13554; Q13557; Q13555 TTFYL58 UC KCC2A_HUMAN; KCC2B_HUMAN; KCC2D_HUMAN; KCC2G_HUMAN TTFYL58 BC Kinase TTFYL58 SN Calcium/calmodulin-dependent protein kinase type II; CaMK-II; CaM kinase II; CAMK TTFYL58 GN CAMK2A; CAMK2B; CAMK2D; CAMK2G TTFYL58 FC CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity. TTFYL58 SQ MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSGGKSGGNKKSDGVKESSESTNTTIEDEDTKVRKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAPSVLPH TTFYL58 TT Clinical trial TTFYL58 KE hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04114:Oocyte meiosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04310:Wnt signaling pathway; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04728:Dopaminergic synapse; hsa04740:Olfactory transduction; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04911:Insulin secretion; hsa04912:GnRH signaling pathway; hsa04916:Melanogenesis; hsa04921:Oxytocin signaling pathway; hsa04922:Glucagon signaling pathway; hsa04971:Gastric acid secretion; hsa05031:Amphetamine addiction; hsa05152:Tuberculosis; hsa05205:Proteoglycans in cancer; hsa05214:Glioma TTFYL58 RC R-HSA-3371571:HSF1-dependent transactivation; R-HSA-399719:Trafficking of AMPA receptors; R-HSA-4086398:Ca2+ pathway; R-HSA-438066:Unblocking of NMDA receptor, glutamate binding and activation; R-HSA-442729:CREB phosphorylation through the activation of CaMKII; R-HSA-442742:CREB phosphorylation through the activation of Ras; R-HSA-442982:Ras activation uopn Ca2+ infux through NMDA receptor; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-877300:Interferon gamma signaling TT9WOBN ID TT9WOBN TT9WOBN TN Cardiac myosin (MYBPC3) TT9WOBN UP Q14896 TT9WOBN UC MYPC3_HUMAN TT9WOBN BC Immunoglobulin TT9WOBN SN Myosinbinding protein C, cardiactype; Myosin-binding protein C, cardiac-type; Cprotein, cardiac muscle isoform; Cardiac MyBPC; Cardiac MyBP-C; C-protein, cardiac muscle isoform TT9WOBN GN MYBPC3 TT9WOBN FC In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role. Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. TT9WOBN PD 6G2T; 6CXJ; 6CXI; 5K6P; 3CX2 TT9WOBN SQ MPEPGKKPVSAFSKKPRSVEVAAGSPAVFEAETERAGVKVRWQRGGSDISASNKYGLATEGTRHTLTVREVGPADQGSYAVIAGSSKVKFDLKVIEAEKAEPMLAPAPAPAEATGAPGEAPAPAAELGESAPSPKGSSSAALNGPTPGAPDDPIGLFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFTGSYRCEVSTKDKFDCSNFNLTVHEAMGTGDLDLLSAFRRTSLAGGGRRISDSHEDTGILDFSSLLKKRDSFRTPRDSKLEAPAEEDVWEILRQAPPSEYERIAFQYGVTDLRGMLKRLKGMRRDEKKSTAFQKKLEPAYQVSKGHKIRLTVELADHDAEVKWLKNGQEIQMSGSKYIFESIGAKRTLTISQCSLADDAAYQCVVGGEKCSTELFVKEPPVLITRPLEDQLVMVGQRVEFECEVSEEGAQVKWLKDGVELTREETFKYRFKKDGQRHHLIINEAMLEDAGHYALCTSGGQALAELIVQEKKLEVYQSIADLMVGAKDQAVFKCEVSDENVRGVWLKNGKELVPDSRIKVSHIGRVHKLTIDDVTPADEADYSFVPEGFACNLSAKLHFMEVKIDFVPRQEPPKIHLDCPGRIPDTIVVVAGNKLRLDVPISGDPAPTVIWQKAITQGNKAPARPAPDAPEDTGDSDEWVFDKKLLCETEGRVRVETTKDRSIFTVEGAEKEDEGVYTVTVKNPVGEDQVNLTVKVIDVPDAPAAPKISNVGEDSCTVQWEPPAYDGGQPILGYILERKKKKSYRWMRLNFDLIQELSHEARRMIEGVVYEMRVYAVNAIGMSRPSPASQPFMPIGPPSEPTHLAVEDVSDTTVSLKWRPPERVGAGGLDGYSVEYCPEGCSEWVAALQGLTEHTSILVKDLPTGARLLFRVRAHNMAGPGAPVTTTEPVTVQEILQRPRLQLPRHLRQTIQKKVGEPVNLLIPFQGKPRPQVTWTKEGQPLAGEEVSIRNSPTDTILFIRAARRVHSGTYQVTVRIENMEDKATLVLQVVDKPSPPQDLRVTDAWGLNVALEWKPPQDVGNTELWGYTVQKADKKTMEWFTVLEHYRRTHCVVPELIIGNGYYFRVFSQNMVGFSDRAATTKEPVFIPRPGITYEPPNYKALDFSEAPSFTQPLVNRSVIAGYTAMLCCAVRGSPKPKISWFKNGLDLGEDARFRMFSKQGVLTLEIRKPCPFDGGIYVCRATNLQGEARCECRLEVRVPQ TT9WOBN TT Clinical trial TT9WOBN FM Immunoglobulin superfamily TT9WOBN KE hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05414:Dilated cardiomyopathy TT9WOBN RC R-HSA-390522:Striated Muscle Contraction TTXGTZU ID TTXGTZU TTXGTZU TN Cardiotrophin-1 (CTF1) TTXGTZU UP Q16619 TTXGTZU UC CTF1_HUMAN TTXGTZU BC Cytokine: interleukin TTXGTZU SN CTF1; CT-1 TTXGTZU GN CTF1 TTXGTZU FC Induces cardiac myocyte hypertrophy in vitro. Binds to and activates the ILST/gp130 receptor. TTXGTZU SQ MSRREGSLEDPQTDSSVSLLPHLEAKIRQTHSLAHLLTKYAEQLLQEYVQLQGDPFGLPSFSPPRLPVAGLSAPAPSHAGLPVHERLRLDAAALAALPPLLDAVCRRQAELNPRAPRLLRRLEDAARQARALGAAVEALLAALGAANRGPRAEPPAATASAASATGVFPAKVLGLRVCGLYREWLSRTEGDLGQLLPGGSA TTXGTZU TT Clinical trial TTXGTZU KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway TT12VNG ID TT12VNG TT12VNG TN Caspase 2 messenger RNA (CASP2 mRNA) TT12VNG UP P42575 TT12VNG UC CASP2_HUMAN TT12VNG BC mRNA target TT12VNG SN Protease ICH1 (mRNA); Protease ICH-1 (mRNA); Neural precursor cell expressed developmentally downregulated protein 2 (mRNA); Neural precursor cell expressed developmentally down-regulated protein 2 (mRNA); NEDD2 (mRNA); NEDD-2 (mRNA); ICH1 (mRNA); Caspase2 subunit p12 (mRNA); CASP-2 (mRNA) TT12VNG GN CASP2 TT12VNG FC Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival. Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress. Involved in the activation cascade of caspases responsible for apoptosis execution. TT12VNG EC EC 3.4.22.55 TT12VNG SQ MAAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT TT12VNG TT Clinical trial TT12VNG FM mRNA target TT12VNG RC R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-205025:NADE modulates death signalling TTM7Y45 ID TTM7Y45 TTM7Y45 TN Caspase-7 (CASP7) TTM7Y45 UP P55210 TTM7Y45 UC CASP7_HUMAN TTM7Y45 BC Peptidase TTM7Y45 SN MCH3; ICE-like apoptotic protease 3; ICE-LAP3; CMH-1; CASP-7; Apoptotic protease Mch-3 TTM7Y45 GN CASP7 TTM7Y45 FC Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death. Involved in the activation cascade of caspases responsible for apoptosis execution. TTM7Y45 EC EC 3.4.22.60 TTM7Y45 PD 5V6Z; 5V6U; 5K20; 5IC6; 4ZVU TTM7Y45 SQ MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ TTM7Y45 TT Clinical trial TTU3Y87 ID TTU3Y87 TTU3Y87 TN CCR3 messenger RNA (CCR3 mRNA) TTU3Y87 UP P51677 TTU3Y87 UC CCR3_HUMAN TTU3Y87 BC mRNA target TTU3Y87 SN Eosinophil eotaxin receptor (mRNA); Chemokine receptor CCR3 (mRNA); CMKBR3 (mRNA); CKR3 (mRNA); CD193 (mRNA); CCR-3 (mRNA); CC-CKR-3 (mRNA); C-C chemokine receptor type 3 (mRNA); C-C CKR-3 (mRNA) TTU3Y87 GN CCR3 TTU3Y87 FC Binds to eotaxin, eotaxin-3, MCP-3, MCP-4, RANTES and MIP-1 delta. Subsequently transduces a signal by increasing the intracellular calcium ions level. Alternative coreceptor with CD4 for HIV-1 infection. Receptor for a C-C type chemokine. TTU3Y87 SQ MTTSLDTVETFGTTSYYDDVGLLCEKADTRALMAQFVPPLYSLVFTVGLLGNVVVVMILIKYRRLRIMTNIYLLNLAISDLLFLVTLPFWIHYVRGHNWVFGHGMCKLLSGFYHTGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGVITSIVTWGLAVLAALPEFIFYETEELFEETLCSALYPEDTVYSWRHFHTLRMTIFCLVLPLLVMAICYTGIIKTLLRCPSKKKYKAIRLIFVIMAVFFIFWTPYNVAILLSSYQSILFGNDCERSKHLDLVMLVTEVIAYSHCCMNPVIYAFVGERFRKYLRHFFHRHLLMHLGRYIPFLPSEKLERTSSVSPSTAEPELSIVF TTU3Y87 TT Clinical trial TTU3Y87 FM mRNA target TTNCIE0 ID TTNCIE0 TTNCIE0 TN CD70 antigen (CD27-L) TTNCIE0 UP P32970 TTNCIE0 UC CD70_HUMAN TTNCIE0 BC Cytokine: tumor necrosis factor TTNCIE0 SN Tumor necrosis factor ligandsuperfamily member 7; Tumor necrosis factor ligand superfamily member 7; TNFSF7; CD27LG; CD27L; CD27 ligand TTNCIE0 GN CD70 TTNCIE0 FC Plays a role in T-cell activation. Induces the proliferation of costimulated T-cells and enhances the generation of cytolytic T-cells. Cytokine that binds to CD27. TTNCIE0 SQ MPEEGSGCSVRRRPYGCVLRAALVPLVAGLVICLVVCIQRFAQAQQQLPLESLGWDVAELQLNHTGPQQDPRLYWQGGPALGRSFLHGPELDKGQLRIHRDGIYMVHIQVTLAICSSTTASRHHPTTLAVGICSPASRSISLLRLSFHQGCTIASQRLTPLARGDTLCTNLTGTLLPSRNTDETFFGVQWVRP TTNCIE0 TT Clinical trial TTNCIE0 KE hsa04060:Cytokine-cytokine receptor interaction TTNCIE0 RC R-HSA-5669034:TNFs bind their physiological receptors TT1AQ50 ID TT1AQ50 TT1AQ50 TN Charybdotoxin receptor beta-4 (BKbeta4) TT1AQ50 UP Q86W47 TT1AQ50 UC KCMB4_HUMAN TT1AQ50 SN KCNMB4; Calcium activated potassium KCNMA1 (maxiK) channel TT1AQ50 GN KCNMB4 TT1AQ50 FC Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and alters its pharmacological properties. It slows down the activation and the deactivation kinetics of the channel. Acts as a negative regulator of smooth muscle contraction by enhancing the calcium sensitivity to KCNMA1. Its presence is also a requirement for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external binding of the agonist hormone 17-beta-estradiol (E2). Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1 peptide blocker by increasing the CTX association rate and decreasing the dissociation rate. TT1AQ50 PD 5Y7L TT1AQ50 SQ MAKLRVAYEYTEAEDKSIRLGLFLIISGVVSLFIFGFCWLSPALQDLQATEANCTVLSVQQIGEVFECTFTCGADCRGTSQYPCVQVYVNNSESNSRALLHSDEHQLLTNPKCSYIPPCKRENQKNLESVMNWQQYWKDEIGSQPFTCYFNQHQRPDDVLLHRTHDEIVLLHCFLWPLVTFVVGVLIVVLTICAKSLAVKAEAMKKRKFS TT1AQ50 TT Clinical trial TT1AQ50 KE hsa04022:cGMP-PKG signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04911:Insulin secretion; hsa04970:Salivary secretion; hsa04972:Pancreatic secretion TT1AQ50 RC R-HSA-418457:cGMP effects TT0NYDG ID TT0NYDG TT0NYDG TN Choline transporter-like protein 4 (SLC44A4) TT0NYDG UP Q53GD3 TT0NYDG UC CTL4_HUMAN TT0NYDG BC Choline transporter-like TT0NYDG SN hTPPT1; Thiamine pyrophosphate transporter 1; Solute carrier family 44 member 4; NG22; CTL4; C6orf29 TT0NYDG GN SLC44A4 TT0NYDG FC Choline transporter that plays a role in the choline-acetylcholine system and is required to the efferent innervation of hair cells in the olivocochlear bundle for the maintenance of physiological function of outer hair cells and the protection of hair cells from acoustic injury (By similarity). Also described as a thiamine pyrophosphate transporter in colon, may mediate the absorption of microbiota-generated thiamine pyrophosphate and contribute to host thiamine (vitamin B1) homeostasis. TT0NYDG SQ MGGKQRDEDDEAYGKPVKYDPSFRGPIKNRSCTDVICCVLFLLFILGYIVVGIVAWLYGDPRQVLYPRNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLQCPTPQVCVSSCPEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNMTVITSLQQELCPSFLLPSAPALGRCFPWTNVTPPALPGITNDTTIQQGISGLIDSLNARDISVKIFEDFAQSWYWILVALGVALVLSLLFILLLRLVAGPLVLVLILGVLGVLAYGIYYCWEEYRVLRDKGASISQLGFTTNLSAYQSVQETWLAALIVLAVLEAILLLMLIFLRQRIRIAIALLKEASKAVGQMMSTMFYPLVTFVLLLICIAYWAMTALYLATSGQPQYVLWASNISSPGCEKVPINTSCNPTAHLVNSSCPGLMCVFQGYSSKGLIQRSVFNLQIYGVLGLFWTLNWVLALGQCVLAGAFASFYWAFHKPQDIPTFPLISAFIRTLRYHTGSLAFGALILTLVQIARVILEYIDHKLRGVQNPVARCIMCCFKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAKNAFMLLMRNIVRVVVLDKVTDLLLFFGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPHLNYYWLPIMTSILGAYVIASGFFSVFGMCVDTLFLCFLEDLERNNGSLDRPYYMSKSLLKILGKKNEAPPDNKKRKK TT0NYDG TT Clinical trial TT0NYDG KE hsa05231:Choline metabolism in cancer TTUAIKM ID TTUAIKM TTUAIKM TN Cholinephosphate cytidylyltransferase (PCYT1B) TTUAIKM UP Q9Y5K3 TTUAIKM UC PCY1B_HUMAN TTUAIKM BC Nucleotidyltransferase TTUAIKM SN Phosphorylcholine transferase; PCYT1B; CTP:phosphocholine cytidylyltransferase; CT; CCT TTUAIKM GN PCYT1B TTUAIKM FC Controls phosphatidylcholine synthesis. TTUAIKM EC EC 2.7.7.15 TTUAIKM SQ MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADETNCQCQAPHEKLTIAQARLGTPADRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKRYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLELFGPDGAWKQMFQERSSRMLQALSPKQSPVSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISSMSEGDEDEK TTUAIKM TT Clinical trial TTUAIKM KE hsa00564:Glycerophospholipid metabolism; hsa01100:Metabolic pathways; hsa05231:Choline metabolism in cancer TTUH273 ID TTUH273 TTUH273 TN Choriogonadotropin beta (CG-beta) TTUH273 UP P0DN86 TTUH273 UC CGB3_HUMAN TTUH273 BC Hormone TTUH273 SN Chorionic gonadotropin beta subunit; Chorionic gonadotrophin beta subunit; CG-beta TTUH273 GN CGB3 TTUH273 FC Stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy. TTUH273 PD 1XUL; 1QFW; 1HRP; 1HCN TTUH273 SQ MEMFQGLLLLLLLSMGGTWASKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ TTUH273 TT Clinical trial TTPNE41 ID TTPNE41 TTPNE41 TN CI Man-6-P receptor (IGF2R) TTPNE41 UP P11717 TTPNE41 UC MPRI_HUMAN TTPNE41 BC Mannose 6-phosphate receptor TTPNE41 SN MPRI; MPR 300; M6PR; M6P/IGF2R; M6P/IGF2 receptor; Insulinlike growth factor II receptor; Insulinlike growth factor 2 receptor; Insulin-like growth factor II receptor; Insulin-like growth factor 2 receptor; IGFII receptor; IGF-II receptor; Cationindependent mannose6phosphate receptor; Cation-independent mannose-6-phosphate receptor; CIMPR; CI-MPR; CD222; 300 kDa mannose 6phosphate receptor; 300 kDa mannose 6-phosphate receptor TTPNE41 GN IGF2R TTPNE41 FC Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. TTPNE41 PD 5IEI; 2V5P; 2V5O; 2V5N; 2M6T TTPNE41 SQ MGAAAGRSPHLGPAPARRPQRSLLLLQLLLLVAAPGSTQAQAAPFPELCSYTWEAVDTKNNVLYKINICGSVDIVQCGPSSAVCMHDLKTRTYHSVGDSVLRSATRSLLEFNTTVSCDQQGTNHRVQSSIAFLCGKTLGTPEFVTATECVHYFEWRTTAACKKDIFKANKEVPCYVFDEELRKHDLNPLIKLSGAYLVDDSDPDTSLFINVCRDIDTLRDPGSQLRACPPGTAACLVRGHQAFDVGQPRDGLKLVRKDRLVLSYVREEAGKLDFCDGHSPAVTITFVCPSERREGTIPKLTAKSNCRYEIEWITEYACHRDYLESKTCSLSGEQQDVSIDLTPLAQSGGSSYISDGKEYLFYLNVCGETEIQFCNKKQAAVCQVKKSDTSQVKAAGRYHNQTLRYSDGDLTLIYFGGDECSSGFQRMSVINFECNKTAGNDGKGTPVFTGEVDCTYFFTWDTEYACVKEKEDLLCGATDGKKRYDLSALVRHAEPEQNWEAVDGSQTETEKKHFFINICHRVLQEGKARGCPEDAAVCAVDKNGSKNLGKFISSPMKEKGNIQLSYSDGDDCGHGKKIKTNITLVCKPGDLESAPVLRTSGEGGCFYEFEWHTAAACVLSKTEGENCTVFDSQAGFSFDLSPLTKKNGAYKVETKKYDFYINVCGPVSVSPCQPDSGACQVAKSDEKTWNLGLSNAKLSYYDGMIQLNYRGGTPYNNERHTPRATLITFLCDRDAGVGFPEYQEEDNSTYNFRWYTSYACPEEPLECVVTDPSTLEQYDLSSLAKSEGGLGGNWYAMDNSGEHVTWRKYYINVCRPLNPVPGCNRYASACQMKYEKDQGSFTEVVSISNLGMAKTGPVVEDSGSLLLEYVNGSACTTSDGRQTTYTTRIHLVCSRGRLNSHPIFSLNWECVVSFLWNTEAACPIQTTTDTDQACSIRDPNSGFVFNLNPLNSSQGYNVSGIGKIFMFNVCGTMPVCGTILGKPASGCEAETQTEELKNWKPARPVGIEKSLQLSTEGFITLTYKGPLSAKGTADAFIVRFVCNDDVYSGPLKFLHQDIDSGQGIRNTYFEFETALACVPSPVDCQVTDLAGNEYDLTGLSTVRKPWTAVDTSVDGRKRTFYLSVCNPLPYIPGCQGSAVGSCLVSEGNSWNLGVVQMSPQAAANGSLSIMYVNGDKCGNQRFSTRITFECAQISGSPAFQLQDGCEYVFIWRTVEACPVVRVEGDNCEVKDPRHGNLYDLKPLGLNDTIVSAGEYTYYFRVCGKLSSDVCPTSDKSKVVSSCQEKREPQGFHKVAGLLTQKLTYENGLLKMNFTGGDTCHKVYQRSTAIFFYCDRGTQRPVFLKETSDCSYLFEWRTQYACPPFDLTECSFKDGAGNSFDLSSLSRYSDNWEAITGTGDPEHYLINVCKSLAPQAGTEPCPPEAAACLLGGSKPVNLGRVRDGPQWRDGIIVLKYVDGDLCPDGIRKKSTTIRFTCSESQVNSRPMFISAVEDCEYTFAWPTATACPMKSNEHDDCQVTNPSTGHLFDLSSLSGRAGFTAAYSEKGLVYMSICGENENCPPGVGACFGQTRISVGKANKRLRYVDQVLQLVYKDGSPCPSKSGLSYKSVISFVCRPEARPTNRPMLISLDKQTCTLFFSWHTPLACEQATECSVRNGSSIVDLSPLIHRTGGYEAYDESEDDASDTNPDFYINICQPLNPMHGVPCPAGAAVCKVPIDGPPIDIGRVAGPPILNPIANEIYLNFESSTPCLADKHFNYTSLIAFHCKRGVSMGTPKLLRTSECDFVFEWETPVVCPDEVRMDGCTLTDEQLLYSFNLSSLSTSTFKVTRDSRTYSVGVCTFAVGPEQGGCKDGGVCLLSGTKGASFGRLQSMKLDYRHQDEAVVLSYVNGDRCPPETDDGVPCVFPFIFNGKSYEECIIESRAKLWCSTTADYDRDHEWGFCRHSNSYRTSSIIFKCDEDEDIGRPQVFSEVRGCDVTFEWKTKVVCPPKKLECKFVQKHKTYDLRLLSSLTGSWSLVHNGVSYYINLCQKIYKGPLGCSERASICRRTTTGDVQVLGLVHTQKLGVIGDKVVVTYSKGYPCGGNKTASSVIELTCTKTVGRPAFKRFDIDSCTYYFSWDSRAACAVKPQEVQMVNGTITNPINGKSFSLGDIYFKLFRASGDMRTNGDNYLYEIQLSSITSSRNPACSGANICQVKPNDQHFSRKVGTSDKTKYYLQDGDLDVVFASSSKCGKDKTKSVSSTIFFHCDPLVEDGIPEFSHETADCQYLFSWYTSAVCPLGVGFDSENPGDDGQMHKGLSERSQAVGAVLSLLLVALTCCLLALLLYKKERRETVISKLTTCCRRSSNVSYKYSKVNKEEETDENETEWLMEEIQLPPPRQGKEGQENGHITTKSVKALSSLHGDDQDSEDEVLTIPEVKVHSGRGAGAESSHPVRNAQSNALQEREDDRVGLVRGEKARKGKSSSAQQKTVSSTKLVSFHDDSDEDLLHI TTPNE41 TT Clinical trial TTPNE41 KE hsa04142:Lysosome TTPNE41 RC R-HSA-432722:Golgi Associated Vesicle Biogenesis TTJCPUT ID TTJCPUT TTJCPUT TN Coagulation factor XI (F11) TTJCPUT UP P03951 TTJCPUT UC FA11_HUMAN TTJCPUT BC Peptidase TTJCPUT SN Plasma thromboplastin antecedent; PTA; FXI TTJCPUT GN F11 TTJCPUT FC Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. TTJCPUT EC EC 3.4.21.27 TTJCPUT PD 6R8X; 6I58; 6C0S; 6AOD; 5WB6 TTJCPUT SQ MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV TTJCPUT TT Clinical trial TTUABC1 ID TTUABC1 TTUABC1 TN Collagen I (COL1A2) TTUABC1 UP P08123 TTUABC1 UC CO1A2_HUMAN TTUABC1 SN Collagen alpha-2(I) chain; Alpha-2 type I collagen TTUABC1 GN COL1A2 TTUABC1 FC Type I collagen is a member of group I collagen (fibrillar forming collagen). TTUABC1 PD 5CVA; 5CTI; 5CTD TTUABC1 SQ MLSFVDTRTLLLLAVTLCLATCQSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGAVGNAGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGSAGPQGPPGPSGEEGKRGPNGEAGSAGPPGPPGLRGSPGSRGLPGADGRAGVMGPPGSRGASGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPPGPPGFQGLPGPSGPAGEVGKPGERGLHGEFGLPGPAGPRGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAVGTAGPSGPSGLPGERGAAGIPGGKGEKGEPGLRGEIGNPGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGAKGPKGENGVVGPTGPVGAAGPAGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRTGEVGAVGPPGFAGEKGPSGEAGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNIGPVGAAGAPGPHGPVGPAGKHGNRGETGPSGPVGPAGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKGHNGLQGLPGIAGHHGDQGAPGSVGPAGPRGPAGPSGPAGKDGRTGHPGTVGPAGIRGPQGHQGPAGPPGPPGPPGPPGVSGGGYDFGYDGDFYRADQPRSAPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPENIPAKNWYRSSKDKKHVWLGETINAGSQFEYNVEGVTSKEMATQLAFMRLLANYASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFFVDIGPVCFK TTUABC1 TT Clinical trial TTUABC1 FM Fibrillar collagen family TTUABC1 KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04611:Platelet activation; hsa04974:Protein digestion and absorption; hsa05146:Amoebiasis TTUABC1 RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1442490:Collagen degradation; R-HSA-1650814:Collagen biosynthesis and modifying enzymes; R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-216083:Integrin cell surface interactions; R-HSA-2214320:Anchoring fibril formation; R-HSA-3000170:Syndecan interactions; R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-3000480:Scavenging by Class A Receptors; R-HSA-75892:Platelet Adhesion to exposed collagen TT5Z9WY ID TT5Z9WY TT5Z9WY TN Complement decay-accelerating factor (CD55) TT5Z9WY UP P08174 TT5Z9WY UC DAF_HUMAN TT5Z9WY SN DAF; Complement decayaccelerating factor; CR TT5Z9WY GN CD55 TT5Z9WY FC Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage. This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. TT5Z9WY PD 6ILK; 6ILJ; 5FOA; 3J24; 3IYP TT5Z9WY SQ MTVARPSVPAALPLLGELPRLLLLVLLCLPAVWGDCGLPPDVPNAQPALEGRTSFPEDTVITYKCEESFVKIPGEKDSVICLKGSQWSDIEEFCNRSCEVPTRLNSASLKQPYITQNYFPVGTVVEYECRPGYRREPSLSPKLTCLQNLKWSTAVEFCKKKSCPNPGEIRNGQIDVPGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQWSDPLPECREIYCPAPPQIDNGIIQGERDHYGYRQSVTYACNKGFTMIGEHSIYCTVNNDEGEWSGPPPECRGKSLTSKVPPTVQKPTTVNVPTTEVSPTSQKTTTKTTTPNAQATRSTPVSRTTKHFHETTPNKGSGTTSGTTRLLSGHTCFTLTGLLGTLVTMGLLT TT5Z9WY TT Clinical trial TT5Z9WY KE hsa04610:Complement and coagulation cascades; hsa04640:Hematopoietic cell lineage; hsa05416:Viral myocarditis TT5Z9WY RC R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-977606:Regulation of Complement cascade TTEA8OW ID TTEA8OW TTEA8OW TN Complement receptor type 1 (CR1) TTEA8OW UP P17927 TTEA8OW UC CR1_HUMAN TTEA8OW BC Receptor of complement activation TTEA8OW SN CR1; CD35 antigen; C3b/C4b receptor TTEA8OW GN CR1 TTEA8OW FC Mediates cellular binding of particles and immunecomplexes that have activated complement. TTEA8OW PD 5FO9; 2Q7Z; 2MCZ; 2MCY; 1PPQ TTEA8OW SQ MGASSPRSPEPVGPPAPGLPFCCGGSLLAVVVLLALPVAWGQCNAPEWLPFARPTNLTDEFEFPIGTYLNYECRPGYSGRPFSIICLKNSVWTGAKDRCRRKSCRNPPDPVNGMVHVIKGIQFGSQIKYSCTKGYRLIGSSSATCIISGDTVIWDNETPICDRIPCGLPPTITNGDFISTNRENFHYGSVVTYRCNPGSGGRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFVMKGPRRVKCQALNKWEPELPSCSRVCQPPPDVLHAERTQRDKDNFSPGQEVFYSCEPGYDLRGAASMRCTPQGDWSPAAPTCEVKSCDDFMGQLLNGRVLFPVNLQLGAKVDFVCDEGFQLKGSSASYCVLAGMESLWNSSVPVCEQIFCPSPPVIPNGRHTGKPLEVFPFGKTVNYTCDPHPDRGTSFDLIGESTIRCTSDPQGNGVWSSPAPRCGILGHCQAPDHFLFAKLKTQTNASDFPIGTSLKYECRPEYYGRPFSITCLDNLVWSSPKDVCKRKSCKTPPDPVNGMVHVITDIQVGSRINYSCTTGHRLIGHSSAECILSGNAAHWSTKPPICQRIPCGLPPTIANGDFISTNRENFHYGSVVTYRCNPGSGGRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFVMKGPRRVKCQALNKWEPELPSCSRVCQPPPDVLHAERTQRDKDNFSPGQEVFYSCEPGYDLRGAASMRCTPQGDWSPAAPTCEVKSCDDFMGQLLNGRVLFPVNLQLGAKVDFVCDEGFQLKGSSASYCVLAGMESLWNSSVPVCEQIFCPSPPVIPNGRHTGKPLEVFPFGKAVNYTCDPHPDRGTSFDLIGESTIRCTSDPQGNGVWSSPAPRCGILGHCQAPDHFLFAKLKTQTNASDFPIGTSLKYECRPEYYGRPFSITCLDNLVWSSPKDVCKRKSCKTPPDPVNGMVHVITDIQVGSRINYSCTTGHRLIGHSSAECILSGNTAHWSTKPPICQRIPCGLPPTIANGDFISTNRENFHYGSVVTYRCNLGSRGRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFVMKGPRRVKCQALNKWEPELPSCSRVCQPPPEILHGEHTPSHQDNFSPGQEVFYSCEPGYDLRGAASLHCTPQGDWSPEAPRCAVKSCDDFLGQLPHGRVLFPLNLQLGAKVSFVCDEGFRLKGSSVSHCVLVGMRSLWNNSVPVCEHIFCPNPPAILNGRHTGTPSGDIPYGKEISYTCDPHPDRGMTFNLIGESTIRCTSDPHGNGVWSSPAPRCELSVRAGHCKTPEQFPFASPTIPINDFEFPVGTSLNYECRPGYFGKMFSISCLENLVWSSVEDNCRRKSCGPPPEPFNGMVHINTDTQFGSTVNYSCNEGFRLIGSPSTTCLVSGNNVTWDKKAPICEIISCEPPPTISNGDFYSNNRTSFHNGTVVTYQCHTGPDGEQLFELVGERSIYCTSKDDQVGVWSSPPPRCISTNKCTAPEVENAIRVPGNRSFFSLTEIIRFRCQPGFVMVGSHTVQCQTNGRWGPKLPHCSRVCQPPPEILHGEHTLSHQDNFSPGQEVFYSCEPSYDLRGAASLHCTPQGDWSPEAPRCTVKSCDDFLGQLPHGRVLLPLNLQLGAKVSFVCDEGFRLKGRSASHCVLAGMKALWNSSVPVCEQIFCPNPPAILNGRHTGTPFGDIPYGKEISYACDTHPDRGMTFNLIGESSIRCTSDPQGNGVWSSPAPRCELSVPAACPHPPKIQNGHYIGGHVSLYLPGMTISYICDPGYLLVGKGFIFCTDQGIWSQLDHYCKEVNCSFPLFMNGISKELEMKKVYHYGDYVTLKCEDGYTLEGSPWSQCQADDRWDPPLAKCTSRTHDALIVGTLSGTIFFILLIIFLSWIILKHRKGNNAHENPKEVAIHLHSQGGSSVHPRTLQTNEENSRVLP TTEA8OW TT Clinical trial TTEA8OW KE hsa04610:Complement and coagulation cascades; hsa04640:Hematopoietic cell lineage; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05144:Malaria; hsa05152:Tuberculosis TTEA8OW RC R-HSA-977606:Regulation of Complement cascade TTSECX1 ID TTSECX1 TTSECX1 TN Connective tissue growth factor (CTGF) TTSECX1 UP P29279 TTSECX1 UC CTGF_HUMAN TTSECX1 SN Long; Insulin-like growth factor-binding protein 8; IGFBP8; IGFBP-8; IGF-binding protein 8; IBP-8; Hypertrophic chondrocyte-specific protein 24; HCS24; CCN2; CCN family member 2 TTSECX1 GN CTGF TTSECX1 FC Promotes proliferation and differentiation of chondrocytes. Mediates heparin- and divalent cation-dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells. Enhances fibroblast growth factor-induced DNA synthesis. Major connective tissue mitoattractant secreted by vascular endothelial cells. TTSECX1 SQ MTAASMGPVRVAFVVLLALCSRPAVGQNCSGPCRCPDEPAPRCPAGVSLVLDGCGCCRVCAKQLGELCTERDPCDPHKGLFCHFGSPANRKIGVCTAKDGAPCIFGGTVYRSGESFQSSCKYQCTCLDGAVGCMPLCSMDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKDQTVVGPALAAYRLEDTFGPDPTMIRANCLVQTTEWSACSKTCGMGISTRVTNDNASCRLEKQSRLCMVRPCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSMKTYRAKFCGVCTDGRCCTPHRTTTLPVEFKCPDGEVMKKNMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA TTSECX1 TT Clinical trial TTSECX1 FM CCN intercellular signaling protein TTSECX1 KE hsa04390:Hippo signaling pathway TTSECX1 RC R-HSA-1989781:PPARA activates gene expression; R-HSA-2032785:YAP1- and WWTR1 (TAZ)-stimulated gene expression TTPW9LJ ID TTPW9LJ TTPW9LJ TN Co-stimulatory molecule 4-1BB (CD137) TTPW9LJ UP Q07011 TTPW9LJ UC TNR9_HUMAN TTPW9LJ BC Cytokine receptor TTPW9LJ SN Tumor necrosis factor receptor superfamily member 9; T-cell antigen ILA; T-cell antigen 4-1BB homolog; ILA; CDw137; 4-1BB ligand receptor TTPW9LJ GN TNFRSF9 TTPW9LJ FC Possibly active during T cell activation. Receptor for TNFSF9/4-1BBL. TTPW9LJ PD 6MI2; 6MHR; 6MGP; 6CU0; 6CPR TTPW9LJ SQ MGNSCYNIVATLLLVLNFERTRSLQDPCSNCPAGTFCDNNRNQICSPCPPNSFSSAGGQRTCDICRQCKGVFRTRKECSSTSNAECDCTPGFHCLGAGCSMCEQDCKQGQELTKKGCKDCCFGTFNDQKRGICRPWTNCSLDGKSVLVNGTKERDVVCGPSPADLSPGASSVTPPAPAREPGHSPQIISFFLALTSTALLFLLFFLTLRFSVVKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCEL TTPW9LJ TT Clinical trial TTPW9LJ FM Cytokine receptor TTPW9LJ KE hsa04060:Cytokine-cytokine receptor interaction TTMYWL7 ID TTMYWL7 TTMYWL7 TN Cyclin-dependent kinase 3 (CDK3) TTMYWL7 UP Q00526 TTMYWL7 UC CDK3_HUMAN TTMYWL7 BC Kinase TTMYWL7 SN Cyclindependent kinase 3; Cell division protein kinase 3; CDKN3 TTMYWL7 GN CDK3 TTMYWL7 FC Interacts with CCNC/cyclin-C during interphase. Phosphorylates histone H1, ATF1, RB1 and CABLES1. ATF1 phosphorylation triggers ATF1 transactivation and transcriptional activities, and promotes cell proliferation and transformation. CDK3/cyclin-C mediated RB1 phosphorylation is required for G0-G1 transition. Promotes G1-S transition probably by contributing to the activation of E2F1, E2F2 and E2F3 in a RB1-independent manner. Serine/threonine-protein kinase that plays a critical role in the control of the eukaryotic cell cycle; involved in G0-G1 and G1-S cell cycle transitions. TTMYWL7 EC EC 2.7.11.22 TTMYWL7 PD 1LFN TTMYWL7 SQ MDMFQKVEKIGEGTYGVVYKAKNRETGQLVALKKIRLDLEMEGVPSTAIREISLLKELKHPNIVRLLDVVHNERKLYLVFEFLSQDLKKYMDSTPGSELPLHLIKSYLFQLLQGVSFCHSHRVIHRDLKPQNLLINELGAIKLADFGLARAFGVPLRTYTHEVVTLWYRAPEILLGSKFYTTAVDIWSIGCIFAEMVTRKALFPGDSEIDQLFRIFRMLGTPSEDTWPGVTQLPDYKGSFPKWTRKGLEEIVPNLEPEGRDLLMQLLQYDPSQRITAKTALAHPYFSSPEPSPAARQYVLQRFRH TTMYWL7 TT Clinical trial TTMYWL7 FM Kinase TT2B6PS ID TT2B6PS TT2B6PS TN Cytokine ML-1 (IL17F) TT2B6PS UP Q96PD4 TT2B6PS UC IL17F_HUMAN TT2B6PS BC Cytokine: interleukin TT2B6PS SN Interleukin-17F; IL-17F TT2B6PS GN IL17F TT2B6PS FC The heterodimer formed by IL17A and IL17F is a ligand for the heterodimeric complex formed by IL17RA and IL17RC. Involved in stimulating the production of other cytokines such as IL6, IL8 and CSF2, and in regulation of cartilage matrix turnover. Also involved in stimulating the proliferation of peripheral blood mononuclear cells and T-cells and in inhibition of angiogenesis. Plays a role in the induction of neutrophilia in the lungs and in the exacerbation of antigen-induced pulmonary allergic inflammation. Ligand for IL17RA and IL17RC. TT2B6PS PD 5NAN; 5N92; 3JVF; 1JPY TT2B6PS SQ MTVKTLHGPAMVKYLLLSILGLAFLSEAAARKIPKVGHTFFQKPESCPPVPGGSMKLDIGIINENQRVSMSRNIESRSTSPWNYTVTWDPNRYPSEVVQAQCRNLGCINAQGKEDISMNSVPIQQETLVVRRKHQGCSVSFQLEKVLVTVGCTCVTPVIHHVQ TT2B6PS TT Clinical trial TT2B6PS KE hsa04060:Cytokine-cytokine receptor interaction; hsa04657:IL-17 signaling pathway; hsa04659:Th17 cell differentiation; hsa05321:Inflammatory bowel disease (IBD) TTNDHVE ID TTNDHVE TTNDHVE TN Cytomegalovirus 65kDa phosphoprotein (HCV UL83) TTNDHVE UP P06725 TTNDHVE UC PP65_HCMVA TTNDHVE BC Herpesviridae pp65 TTNDHVE SN pp65; UL83; Tegument protein UL83; Phosphoprotein UL83; 65 kDa phosphoprotein; 65 kDa matrix phosphoprotein TTNDHVE GN HCV UL83 TTNDHVE FC Counteracts thehost antiviral immune response when activated and phosphorylated, by preventing IRF3 from entering the nucleus. Also participates in the transactivation of viral major immediate-early genes by the recruitment of host IFI16 to the promoters pf these genes. TTNDHVE PD 3GSO; 2X4T; 2X4R TTNDHVE SQ MESRGRRCPEMISVLGPISGHVLKAVFSRGDTPVLPHETRLLQTGIHVRVSQPSLILVSQYTPDSTPCHRGDNQLQVQHTYFTGSEVENVSVNVHNPTGRSICPSQEPMSIYVYALPLKMLNIPSINVHHYPSAAERKHRHLPVADAVIHASGKQMWQARLTVSGLAWTRQQNQWKEPDVYYTSAFVFPTKDVALRHVVCAHELVCSMENTRATKMQVIGDQYVKVYLESFCEDVPSGKLFMHVTLGSDVEEDLTMTRNPQPFMRPHERNGFTVLCPKNMIIKPGKISHIMLDVAFTSHEHFGLLCPKSIPGLSISGNLLMNGQQIFLEVQAIRETVELRQYDPVAALFFFDIDLLLQRGPQYSEHPTFTSQYRIQGKLEYRHTWDRHDEGAAQGDDDVWTSGSDSDEELVTTERKTPRVTGGGAMAGASTSAGRKRKSASSATACTSGVMTRGRLKAESTVAPEEDTDEDSDNEIHNPAVFTWPPWQAGILARNLVPMVATVQGQNLKYQEFFWDANDIYRIFAELEGVWQPAAQPKRRRHRQDALPGPCIASTPKKHRG TTNDHVE TT Clinical trial TTNDHVE RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell TTXQ04B ID TTXQ04B TTXQ04B TN Cytomegalovirus Ganciclovir kinase (CMV UL97) TTXQ04B UP P16788 TTXQ04B UC UL97_HCMVA TTXQ04B BC Kinase TTXQ04B SN UL97; Human cytomegalovirus UL97 protein kinase; HSRF3 protein TTXQ04B GN CMV UL97 TTXQ04B FC Phosphorylates the antiviral nucleoside analog ganciclovir. TTXQ04B EC EC 2.7.1.- TTXQ04B SQ MSSALRSRARSASLGTTTQGWDPPPLRRPSRARRRQWMREAAQAAAQAAVQAAQAAAAQVAQAHVDENEVVDLMADEAGGGVTTLTTLSSVSTTTVLGHATFSACVRSDVMRDGEKEDAASDKENLRRPVVPSTSSRGSAASGDGYHGLRCRETSAMWSFEYDRDGDVTSVRRALFTGGSDPSDSVSGVRGGRKRPLRPPLVSLARTPLCRRRVGGVDAVLEENDVELRAESQDSAVASGPGRIPQPLSGSSGEESATAVEADSTSHDDVHCTCSNDQIITTSIRGLTCDPRMFLRLTHPELCELSISYLLVYVPKEDDFCHKICYAVDMSDESYRLGQGSFGEVWPLDRYRVVKVARKHSETVLTVWMSGLIRTRAAGEQQQPPSLVGTGVHRGLLTATGCCLLHNVTVHRRFHTDMFHHDQWKLACIDSYRRAFCTLADAIKFLNHQCRVCHFDITPMNVLIDVNPHNPSEIVRAALCDYSLSEPYPDYNERCVAVFQETGTARRIPNCSHRLRECYHPAFRPMPLQKLLICDPHARFPVAGLRRYCMSELSALGNVLGFCLMRLLDRRGLDEVRMGTEALLFKHAGAACRALENGKLTHCSDACLLILAAQMSYGACLLGEHGAALVSHTLRFVEAKMSSCRVRAFRRFYHECSQTMLHEYVRKNVERLLATSDGLYLYNAFRRTTSIICEEDLDGDCRQLFPE TTXQ04B TT Clinical trial TTJGLZF ID TTJGLZF TTJGLZF TN Dipeptidyl peptidase 8 (DPP-8) TTJGLZF UP Q6V1X1 TTJGLZF UC DPP8_HUMAN TTJGLZF BC Peptidase TTJGLZF SN Prolyl dipeptidase DPP8; MSTP141; MSTP135; MSTP097; Dipeptidyl peptidase VIII; Dipeptidyl peptidase IV-related protein 1; DPRP1; DPRP-1; DPP VIII; DP8 TTJGLZF GN DPP8 TTJGLZF FC Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. TTJGLZF EC EC 3.4.14.5 TTJGLZF PD 6EOT; 6EOS; 6EOP; 6EOO TTJGLZF SQ MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIGTVGIASYDYHQGSGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHSNDIWISNIVTREERRLTYVHNELANMEEDARSAGVATFVLQEEFDRYSGYWWCPKAETTPSGGKILRILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIMIDAEGRIIDVIDKELIQPFEILFEGVEYIARAGWTPEGKYAWSILLDRSQTRLQIVLISPELFIPVEDDVMERQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQSHEEEIEFIFASECKTGFRHLYKITSILKESKYKRSSGGLPAPSDFKCPIKEEIAITSGEWEVLGRHGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSHSCCISQHCDFFISKYSNQKNPHCVSLYKLSSPEDDPTCKTKEFWATILDSAGPLPDYTPPEIFSFESTTGFTLYGMLYKPHDLQPGKKYPTVLFIYGGPQVQLVNNRFKGVKYFRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPSEPNRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSRIAALKVI TTJGLZF TT Clinical trial TTNDUL7 ID TTNDUL7 TTNDUL7 TN Dipeptidyl peptidase 9 (DPP-9) TTNDUL7 UP Q86TI2 TTNDUL7 UC DPP9_HUMAN TTNDUL7 BC Peptidase TTNDUL7 SN Dipeptidyl peptidase-like protein 9; Dipeptidyl peptidase IX; Dipeptidyl peptidase IV-related protein 2; DPRP2; DPRP-2; DPP IX; DPLP9; DP9 TTNDUL7 GN DPP9 TTNDUL7 FC Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. TTNDUL7 EC EC 3.4.14.5 TTNDUL7 PD 6EOR; 6EOQ TTNDUL7 SQ MATTGTPTADRGDAAATDDPAARFQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLLSWKQMLDHFQATPHHGVYSREEELLRERKRLGVFGITSYDFHSESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCSGPRMDPKICPADPAFFSFINNSDLWVANIETGEERRLTFCHQGLSNVLDDPKSAGVATFVIQEEFDRFTGYWWCPTASWEGSEGLKTLRILYEEVDESEVEVIHVPSPALEERKTDSYRYPRTGSKNPKIALKLAEFQTDSQGKIVSTQEKELVQPFSSLFPKVEYIARAGWTRDGKYAWAMFLDRPQQWLQLVLLPPALFIPSTENEEQRLASARAVPRNVQPYVVYEEVTNVWINVHDIFYPFPQSEGEDELCFLRANECKTGFCHLYKVTAVLKSQGYDWSEPFSPGEDEFKCPIKEEIALTSGEWEVLARHGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVRLTTPGFSHSCSMSQNFDMFVSHYSSVSTPPCVHVYKLSGPDDDPLHKQPRFWASMMEAASCPPDYVPPEIFHFHTRSDVRLYGMIYKPHALQPGKKHPTVLFVYGGPQVQLVNNSFKGIKYLRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTGYTERYMDVPENNQHGYEAGSVALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL TTNDUL7 TT Clinical trial TTZQTY2 ID TTZQTY2 TTZQTY2 TN DMPK messenger RNA (DMPK mRNA) TTZQTY2 UP Q09013 TTZQTY2 UC DMPK_HUMAN TTZQTY2 BC mRNA target TTZQTY2 SN Myotonin-protein kinase (mRNA); Myotonic dystrophy protein kinase (mRNA); MT-PK (mRNA); MDPK (mRNA); DMPK (mRNA); DMK (mRNA); DM1PK (mRNA); DM1 protein kinase (mRNA); DM-kinase (mRNA) TTZQTY2 GN DMPK TTZQTY2 FC May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity. Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. TTZQTY2 EC EC 2.7.11.1 TTZQTY2 PD 2VD5; 1WT6 TTZQTY2 SQ MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP TTZQTY2 TT Clinical trial TTZQTY2 FM mRNA target TTUIZKC ID TTUIZKC TTUIZKC TN DNA-binding factor KBF1 (p105) TTUIZKC UP P19838 TTUIZKC UC NFKB1_HUMAN TTUIZKC SN Nuclear factor of kappa light polypeptide gene enhancer in Bcells 1; Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1; Nuclear factor NFkappaB p50 subunit; Nuclear factor NFkappaB p105 subunit; Nuclear factor NF-kappa-B p105 subunit; EBP1; EBP-1; DNAbinding factor KBF1 TTUIZKC GN NFKB1 TTUIZKC FC NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. TTUIZKC PD 3GUT; 2O61; 2DBF; 1SVC; 1NFI TTUIZKC SQ MAEDDPYLGRPEQMFHLDPSLTHTIFNPEVFQPQMALPTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGGTGSTGPGYSFPHYGFPTYGGITFHPGTTKSNAGMKHGTMDTESKKDPEGCDKSDDKNTVNLFGKVIETTEQDQEPSEATVGNGEVTLTYATGTKEESAGVQDNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWENAGEDEGVVPGTTPLDMATSWQVFDILNGKPYEPEFTSDDLLAQGDMKQLAEDVKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQAASSPVKTTSQAHSLPLSPASTRQQIDELRDSDSVCDSGVETSFRKLSFTESLTSGASLLTLNKMPHDYGQEGPLEGKI TTUIZKC TT Clinical trial TTUIZKC KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04917:Prolactin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05030:Cocaine addiction; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05203:Viral carcinogenesis; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05215:Prostate cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05321:Inflammatory bowel disease (IBD) TTUIZKC RC R-HSA-1169091:Activation of NF-kappaB in B cells; R-HSA-1810476:RIP-mediated NFkB activation via ZBP1; R-HSA-193692:Regulated proteolysis of p75NTR; R-HSA-209560:NF-kB is activated and signals survival; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-3134963:DEx/H-box helicases activate type I IFN and inflammatory cytokines production; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-448706:Interleukin-1 processing; R-HSA-5603027:IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR); R-HSA-5603029:IkBA variant leads to EDA-ID; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-5621575:CD209 (DC-SIGN) signaling; R-HSA-5660668:CLEC7A/inflammasome pathway; R-HSA-5684264:MAP3K8 (TPL2)-dependent MAPK1/3 activation; R-HSA-933542:TRAF6 mediated NF-kB activation TTH6MBO ID TTH6MBO TTH6MBO TN dUTP pyrophosphatase (DUT) TTH6MBO UP P33316 TTH6MBO UC DUT_HUMAN TTH6MBO BC Acid anhydrides hydrolase TTH6MBO SN Deoxyuridine 5' triphosphate nucleotidohydrolase, mitochondrial; DUT TTH6MBO GN DUT TTH6MBO FC This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000269|PubMed:8805593}. TTH6MBO EC EC 3.6.1.23 TTH6MBO PD 5H4J; 4MZ6; 4MZ5; 3EHW; 3ARN TTH6MBO SQ MTPLCPRPALCYHFLTSLLRSAMQNARGARQRAEAAVLSGPGPPLGRAAQHGIPRPLSSAGRLSQGCRGASTVGAAGWKGELPKAGGSPAPGPETPAISPSKRARPAEVGGMQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN TTH6MBO TT Clinical trial TTNBTCW ID TTNBTCW TTNBTCW TN eIF4E-BP2 messenger RNA (eIF4E-BP2 mRNA) TTNBTCW UP Q13542 TTNBTCW UC 4EBP2_HUMAN TTNBTCW BC mRNA target TTNBTCW SN eIF4E-binding protein 2 (mRNA); Eukaryotic translation initiation factor 4E-binding protein 2 (mRNA); 4E-BP2 (mRNA) TTNBTCW GN EIF4EBP2 TTNBTCW FC Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. Repressor of translation initiation involved in synaptic plasticity, learning and memory formation. TTNBTCW PD 3AM7; 2MX4 TTNBTCW SQ MSSSAGSGHQPSQSRAIPTRTVAISDAAQLPHDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGTLIEDSKVEVNNLNNLNNHDRKHAVGDDAQFEMDI TTNBTCW TT Clinical trial TTNBTCW FM mRNA target TTNBTCW KE hsa03013:RNA transport TTZ6B2I ID TTZ6B2I TTZ6B2I TN Epidermal growth factor receptor variant III (EGFR vIII) TTZ6B2I UP P00533 TTZ6B2I UC EGFR_HUMAN TTZ6B2I BC Kinase TTZ6B2I SN ERBB1 variant III; ERBB variant III TTZ6B2I GN EGFR TTZ6B2I FC Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Plays a role in enhancing learning and memory performance (By similarity). TTZ6B2I EC EC 2.7.10.1 TTZ6B2I PD 6D8E; 6B3S; 6ARU; 5ZWJ; 5YU9 TTZ6B2I SQ MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA TTZ6B2I TT Clinical trial TT7WD0H ID TT7WD0H TT7WD0H TN Epidermal growth factor-like protein 7 (EGFL7) TT7WD0H UP Q9UHF1 TT7WD0H UC EGFL7_HUMAN TT7WD0H BC Growth factor TT7WD0H SN ZNEU1; Vascular endothelial statin; VE-statin; UNQ187/PRO1449; NOTCH4-like protein; Multiple epidermal growth factor-like domains protein 7; Multiple epidermal growth factor-like domain protein 7; Multiple EGF-like domains protein 7; Multiple EGF-like domain protein 7; MEGF7; EGF-like protein 7 TT7WD0H GN EGFL7 TT7WD0H FC Inhibits platelet-derived growth factor (PDGF)-BB-induced smooth muscle cell migration and promotes endothelial cell adhesion to the extracellular matrix and angiogenesis. Regulates vascular tubulogenesis in vivo. TT7WD0H SQ MRGSQEVLLMWLLVLAVGGTEHAYRPGRRVCAVRAHGDPVSESFVQRVYQPFLTTCDGHRACSTYRTIYRTAYRRSPGLAPARPRYACCPGWKRTSGLPGACGAAICQPPCRNGGSCVQPGRCRCPAGWRGDTCQSDVDECSARRGGCPQRCVNTAGSYWCQCWEGHSLSADGTLCVPKGGPPRVAPNPTGVDSAMKEEVQRLQSRVDLLEEKLQLVLAPLHSLASQALEHGLPDPGSLLVHSFQQLGRIDSLSEQISFLEEQLGSCSCKKDS TT7WD0H TT Clinical trial TT7WD0H FM Growth factor TTYSB89 ID TTYSB89 TTYSB89 TN Epiregulin (EREG) TTYSB89 UP O14944 TTYSB89 UC EREG_HUMAN TTYSB89 BC Growth factor TTYSB89 SN l=Epiregulin; Proepiregulin; EPR TTYSB89 GN EREG TTYSB89 FC Stimulates EGFR and ERBB4 tyrosine phosphorylation. Contributes to inflammation, wound healing, tissue repair, and oocyte maturation by regulating angiogenesis and vascular remodeling and by stimulating cell proliferation. Ligand of the EGF receptor/EGFR and ERBB4. TTYSB89 PD 5WB7; 5E8D; 1K37; 1K36 TTYSB89 SQ MTAGRRMEMLCAGRVPALLLCLGFHLLQAVLSTTVIPSCIPGESSDNCTALVQTEDNPRVAQVSITKCSSDMNGYCLHGQCIYLVDMSQNYCRCEVGYTGVRCEHFFLTVHQPLSKEYVALTVILIILFLITVVGSTYYFCRWYRNRKSKEPKKEYERVTSGDPELPQV TTYSB89 TT Clinical trial TTYSB89 FM Growth factor TTYSB89 KE hsa04012:ErbB signaling pathway TTYSB89 RC R-HSA-1250196:SHC1 events in ERBB2 signaling; R-HSA-1250342:PI3K events in ERBB4 signaling; R-HSA-1250347:SHC1 events in ERBB4 signaling; R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1963640:GRB2 events in ERBB2 signaling; R-HSA-1963642:PI3K events in ERBB2 signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5673001:RAF/MAP kinase cascade TTQG4NR ID TTQG4NR TTQG4NR TN Erythropoietin (EPO) TTQG4NR UP P01588 TTQG4NR UC EPO_HUMAN TTQG4NR SN Epoetin TTQG4NR GN EPO TTQG4NR FC Binds to EPOR leading to EPOR dimerization and JAK2 activation thereby activating specific downstream effectors, including STAT1 and STAT3. Hormone involved in the regulation of erythrocyte proliferation and differentiation and the maintenance of a physiological level of circulating erythrocyte mass. TTQG4NR PD 1EER; 1CN4; 1BUY TTQG4NR SQ MGVHECPAWLWLLLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR TTQG4NR TT Clinical trial TTQG4NR KE hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage TTQG4NR RC R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor TTYUMF5 ID TTYUMF5 TTYUMF5 TN Fast skeletal muscle troponin complex (TNNC2) TTYUMF5 UP P02585 TTYUMF5 UC TNNC2_HUMAN TTYUMF5 BC Troponin TTYUMF5 SN fTnT; Troponin T, fast skeletal muscle; Troponin I, fast-twitch isoform; Troponin I, fast skeletal muscle; Troponin C, skeletal muscle; TnTf; TNNT3; TNNI2; TNNC2; Fast skeletal muscle troponin T; Beta-TnTF TTYUMF5 GN TNNC2 TTYUMF5 FC Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. TTYUMF5 SQ MTDQQAEARSYLSEEMIAEFKAAFDMFDADGGGDISVKELGTVMRMLGQTPTKEELDAIIEEVDEDGSGTIDFEEFLVMMVRQMKEDAKGKSEEELAECFRIFDRNADGYIDPEELAEIFRASGEHVTDEEIESLMKDGDKNNDGRIDFDEFLKMMEGVQ TTYUMF5 TT Clinical trial TTYUMF5 RC R-HSA-390522:Striated Muscle Contraction TT6ICRA ID TT6ICRA TT6ICRA TN Fibroblast growth factor-18 (FGF18) TT6ICRA UP O76093 TT6ICRA UC FGF18_HUMAN TT6ICRA BC Growth factor TT6ICRA SN zFGF5; Fibroblast growth factor 18; FGF18 TT6ICRA GN FGF18 TT6ICRA FC Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation. TT6ICRA PD 4CJM TT6ICRA SQ MYSAPSACTCLCLHFLLLCFQVQVLVAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQPELQKPFKYTTVTKRSRRIRPTHPA TT6ICRA TT Clinical trial TT6ICRA KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer; hsa05218:Melanoma TT6ICRA RC R-HSA-109704:PI3K Cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-190322:FGFR4 ligand binding and activation; R-HSA-190372:FGFR3c ligand binding and activation; R-HSA-190375:FGFR2c ligand binding and activation; R-HSA-2033514:FGFR3 mutant receptor activation; R-HSA-2033519:Activated point mutants of FGFR2; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5654221:Phospholipase C-mediated cascade; R-HSA-5654227:Phospholipase C-mediated cascade; R-HSA-5654228:Phospholipase C-mediated cascade; R-HSA-5654695:PI-3K cascade:FGFR2; R-HSA-5654699:SHC-mediated cascade:FGFR2; R-HSA-5654700:FRS-mediated FGFR2 signaling; R-HSA-5654704:SHC-mediated cascade:FGFR3; R-HSA-5654706:FRS-mediated FGFR3 signaling; R-HSA-5654710:PI-3K cascade:FGFR3; R-HSA-5654712:FRS-mediated FGFR4 signaling; R-HSA-5654719:SHC-mediated cascade:FGFR4; R-HSA-5654720:PI-3K cascade:FGFR4; R-HSA-5654727:Negative regulation of FGFR2 signaling; R-HSA-5654732:Negative regulation of FGFR3 signaling; R-HSA-5654733:Negative regulation of FGFR4 signaling; R-HSA-5673001:RAF/MAP kinase cascade TT13GFV ID TT13GFV TT13GFV TN Follicle stimulating hormone (FSHB) TT13GFV UP P01225 TT13GFV UC FSHB_HUMAN TT13GFV BC Hormone TT13GFV SN Follitropin subunit beta; Follitropin beta chain; Follicle-stimulating hormone beta subunit; FSH-beta; FSH-B TT13GFV GN FSHB TT13GFV FC Together with the alpha chain CGA constitutes follitropin, the follicle-stimulating hormone, and provides its biological specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled receptor, on target cells to activate downstream signaling pathways. Follitropin is involved in follicle development and spermatogenesis in reproductive organs. TT13GFV PD 4MQW; 4AY9; 1XWD; 1FL7 TT13GFV SQ MKTLQFFFLFCCWKAICCNSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDPARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE TT13GFV TT Clinical trial TT13GFV KE hsa04080:Neuroactive ligand-receptor interaction; hsa04912:GnRH signaling pathway; hsa04913:Ovarian steroidogenesis; hsa04917:Prolactin signaling pathway; hsa04918:Thyroid hormone synthesis; hsa05320:Autoimmune thyroid disease TT13GFV RC R-HSA-209968:Thyroxine biosynthesis; R-HSA-375281:Hormone ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events TTUQMO5 ID TTUQMO5 TTUQMO5 TN Frizzled-7 receptor (FZD7) TTUQMO5 UP O75084 TTUQMO5 UC FZD7_HUMAN TTUQMO5 BC GPCR frizzled TTUQMO5 SN hFz7; FzE3; Fz7; Fz-7; Frizzled7; Frizzled-7 TTUQMO5 GN FZD7 TTUQMO5 FC Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Receptor for Wnt proteins. TTUQMO5 PD 6O3B; 6O3A; 6NE4; 6NE2; 5WBS TTUQMO5 SQ MRDPGAAAPLSSLGLCALVLALLGALSAGAGAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGPGGGPTAYPTAPYLPDLPFTALPPGASDGRGRPAFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFSDDGYRTVAQGTKKEGCTILFMVLYFFGMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDLLSGVCYVGLSSVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVLACYFYEQAFREHWERTWLLQTCKSYAVPCPPGHFPPMSPDFTVFMIKYLMTMIVGITTGFWIWSGKTLQSWRRFYHRLSHSSKGETAV TTUQMO5 TT Clinical trial TTUQMO5 FM GPCR frizzled TTUQMO5 KE hsa04310:Wnt signaling pathway; hsa04390:Hippo signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04916:Melanogenesis; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05217:Basal cell carcinoma TTUQMO5 RC R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-4086400:PCP/CE pathway TTWHDVK ID TTWHDVK TTWHDVK TN Fructose-1,6-bisphosphatase (FBP) TTWHDVK UP P09467; O00757 TTWHDVK UC F16P1_HUMAN; F16P2_HUMAN TTWHDVK BC Phosphoric monoester hydrolase TTWHDVK SN FBPase; D-fructose-1,6-bisphosphate 1-phosphohydrolase TTWHDVK GN FBP1; FBP2 TTWHDVK FC Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain. TTWHDVK SQ MADQAPFDTDVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHSAQ TTWHDVK TT Clinical trial TTWHDVK KE hsa00010:Glycolysis / Gluconeogenesis; hsa00030:Pentose phosphate pathway; hsa00051:Fructose and mannose metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa04152:AMPK signaling pathway; hsa04910:Insulin signaling pathway; hsa04922:Glucagon signaling pathway TTWHDVK RC R-HSA-70263:Gluconeogenesis TTBZHDM ID TTBZHDM TTBZHDM TN Fungal Isoleucyl t-RNA synthetase (Fung ILS1) TTBZHDM UP P09436 TTBZHDM UC SYIC_YEAST TTBZHDM BC Carbon-oxygen ligase TTBZHDM SN Fung Isoleucyl-tRNA synthetase; Fung Isoleucine--tRNA ligase, cytoplasmic; Fung IleRS TTBZHDM GN Fung ILS1 TTBZHDM FC Has aminoacyl-tRNA editing and isoleucine-tRNA ligase activity. TTBZHDM EC EC 6.1.1.5 TTBZHDM SQ MSESNAHFSFPKEEEKVLSLWDEIDAFHTSLELTKDKPEFSFFDGPPFATGTPHYGHILASTIKDIVPRYATMTGHHVERRFGWDTHGVPIEHIIDKKLGITGKDDVFKYGLENYNNECRSIVMTYASDWRKTIGRLGRWIDFDNDYKTMYPSFMESTWWAFKQLHEKGQVYRGFKVMPYSTGLTTPLSNFEAQQNYKDVNDPAVTIGFNVIGQEKTQLVAWTTTPWTLPSNLSLCVNADFEYVKIYDETRDRYFILLESLIKTLYKKPKNEKYKIVEKIKGSDLVGLKYEPLFPYFAEQFHETAFRVISDDYVTSDSGTGIVHNAPAFGEEDNAACLKNGVISEDSVLPNAIDDLGRFTKDVPDFEGVYVKDADKLIIKYLTNTGNLLLASQIRHSYPFCWRSDTPLLYRSVPAWFVRVKNIVPQMLDSVMKSHWVPNTIKEKRFANWIANARDWNVSRNRYWGTPIPLWVSDDFEEVVCVGSIKELEELTGVRNITDLHRDVIDKLTIPSKQGKGDLKRIEEVFDCWFESGSMPYASQHYPFENTEKFDERVPANFISEGLDQTRGWFYTLAVLGTHLFGSVPYKNVIVSGIVLAADGRKMSKSLKNYPDPSIVLNKYGADALRLYLINSPVLKAESLKFKEEGVKEVVSKVLLPWWNSFKFLDGQIALLKKMSNIDFQYDDSVKSDNVMDRWILASMQSLVQFIHEEMGQYKLYTVVPKLLNFIDELTNWYIRFNRRRLKGENGVEDCLKALNSLFDALFTFVRAMAPFTPFLSESIYLRLKEYIPEAVLAKYGKDGRSVHFLSYPVVKKEYFDEAIETAVSRMQSVIDLGRNIREKKTISLKTPLKTLVILHSDESYLKDVEALKNYIIEELNVRDVVITSDEAKYGVEYKAVADWPVLGKKLKKDAKKVKDALPSVTSEQVREYLESGKLEVAGIELVKGDLNAIRGLPESAVQAGQETRTDQDVLIIMDTNIYSELKSEGLARELVNRIQKLRKKCGLEATDDVLVEYELVKDTIDFEAIVKEHFDMLSKTCRSDIAKYDGSKTDPIGDEEQSINDTIFKLKVFKL TTBZHDM TT Clinical trial TTOPAY7 ID TTOPAY7 TTOPAY7 TN Galanin receptor (GAL-R) TTOPAY7 UP P47211; O43603; O60755 TTOPAY7 UC GALR1_HUMAN; GALR2_HUMAN; GALR3_HUMAN TTOPAY7 BC GPCR rhodopsin TTOPAY7 SN GALR; GALNR; GAL-R TTOPAY7 GN GALR1; GALR2; GALR3 TTOPAY7 FC Receptor for the hormone galanin. Receptor for the hormone spexin-1. TTOPAY7 SQ MELAVGNLSEGNASWPEPPAPEPGPLFGIGVENFVTLVVFGLIFALGVLGNSLVITVLARSKPGKPRSTTNLFILNLSIADLAYLLFCIPFQATVYALPTWVLGAFICKFIHYFFTVSMLVSIFTLAAMSVDRYVAIVHSRRSSSLRVSRNALLGVGCIWALSIAMASPVAYHQGLFHPRASNQTFCWEQWPDPRHKKAYVVCTFVFGYLLPLLLICFCYAKVLNHLHKKLKNMSKKSEASKKKTAQTVLVVVVVFGISWLPHHIIHLWAEFGVFPLTPASFLFRITAHCLAYSNSSVNPIIYAFLSENFRKAYKQVFKCHIRKDSHLSDTKESKSRIDTPPSTNCTHV TTOPAY7 TT Clinical trial TTOPAY7 KE hsa04080:Neuroactive ligand-receptor interaction TTOPAY7 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTFPQV7 ID TTFPQV7 TTFPQV7 TN Galectin-3 (LGALS3) TTFPQV7 UP P17931 TTFPQV7 UC LEG3_HUMAN TTFPQV7 SN Mac-2 antigen; MAC2; Lectin L-29; Laminin-binding protein; L-31; IgE-binding protein; Galactoside-binding protein; Galactose-specific lectin 3; Gal-3; GALBP; Carbohydrate-binding protein 35; Carbohydrate binding protein 35; CBP 35; Beta-galactoside-binding protein LGALS3; 35 kDa lectin TTFPQV7 GN LGALS3 TTFPQV7 FC May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis. In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes. Galactose-specific lectin which binds IgE. TTFPQV7 PD 6QGF; 6QGE; 6I78; 6I77; 6I76 TTFPQV7 SQ MADNFSLHDALSGSGNPNPQGWPGAWGNQPAGAGGYPGASYPGAYPGQAPPGAYPGQAPPGAYPGAPGAYPGAPAPGVYPGPPSGPGAYPSSGQPSATGAYPATGPYGAPAGPLIVPYNLPLPGGVVPRMLITILGTVKPNANRIALDFQRGNDVAFHFNPRFNENNRRVIVCNTKLDNNWGREERQSVFPFESGKPFKIQVLVEPDHFKVAVNDAHLLQYNHRVKKLNEISKLGISGDIDLTSASYTMI TTFPQV7 TT Clinical trial TTFPQV7 RC R-HSA-879415:Advanced glycosylation endproduct receptor signaling TT9W8GU ID TT9W8GU TT9W8GU TN Gamma-secretase (GS) TT9W8GU UP Q96BI3; Q8WW43; Q9NZ42; Q92542; P49768 TT9W8GU UC APH1A_HUMAN; APH1B_HUMAN; PEN2_HUMAN; NICA_HUMAN; PSN1_HUMAN TT9W8GU SN Presenilin-stabilization factor-like; PSFL; Aph-1beta TT9W8GU GN APH1A; APH1B; NCSTN; PSENEN; PSEN1 TT9W8GU FC Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (beta-amyloid precursor protein). It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. Probably present in a minority of gamma-secretase complexes compared to APH1A. TT9W8GU SQ MGAAVFFGCTFVAFGPAFALFLITVAGDPLRVIILVAGAFFWLVSLLLASVVWFILVHVTDRSDARLQYGLLIFGAAVSVLLQEVFRFAYYKLLKKADEGLASLSEDGRSPISIRQMAYVSGLSFGIISGVFSVINILADALGPGVVGIHGDSPYYFLTSAFLTAAIILLHTFWGVVFFDACERRRYWALGLVVGSHLLTSGLTFLNPWYEASLLPIYAVTVSMGLWAFITAGGSLRSIQRSLLCRRQEDSRVMVYSALRIPPED TT9W8GU TT Clinical trial TT9W8GU KE hsa04330:Notch signaling pathway; hsa05010:Alzheimer's disease TT9W8GU RC R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-193692:Regulated proteolysis of p75NTR; R-HSA-205043:NRIF signals cell death from the nucleus; R-HSA-2122948:Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-2979096:NOTCH2 Activation and Transmission of Signal to the Nucleus; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TTGOFW6 ID TTGOFW6 TTGOFW6 TN Ganglioside GM2 activator (GM2A) TTGOFW6 UP P17900 TTGOFW6 UC SAP3_HUMAN TTGOFW6 SN Sphingolipid activator protein 3; SAP3; Ganglioside GM2 activator isoform short; GM2AP; GM2A; Cerebroside sulfate activator protein TTGOFW6 GN GM2A TTGOFW6 FC The large binding pocket can accommodate severalsingle chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity. Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta- hexosaminidase A forcleavage of N-acetyl-D-galactosamine and conversion to GM3. TTGOFW6 PD 2AG9; 2AG4; 2AG2; 2AF9; 1TJJ TTGOFW6 SQ MQSLMQAPLLIALGLLLAAPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVMGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKRLGCIKIAASLKGI TTGOFW6 TT Clinical trial TT4F7SL ID TT4F7SL TT4F7SL TN Gap junction alpha-1 protein (GJA1) TT4F7SL UP P17302 TT4F7SL UC CXA1_HUMAN TT4F7SL BC Gap junction-forming connexin TT4F7SL SN Gap junction 43 kDa heart protein; GJAL; Cx43; Connexin-43; Connexin 43 TT4F7SL GN GJA1 TT4F7SL FC A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract. May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles. Gap junction protein that acts as a regulator of bladder capacity. TT4F7SL PD 2LL2 TT4F7SL SQ MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVDMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSIFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGKSDPYHATSGALSPAKDCGSQKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNSKKLAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI TT4F7SL TT Clinical trial TT4F7SL KE hsa04540:Gap junction; hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC) TT4F7SL RC R-HSA-190840:Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane; R-HSA-190861:Gap junction assembly TTHJWYD ID TTHJWYD TTHJWYD TN GHR messenger RNA (GHR mRNA) TTHJWYD UP P10912 TTHJWYD UC GHR_HUMAN TTHJWYD BC mRNA target TTHJWYD SN Somatotropin receptor (mRNA); Serum bindingprotein (mRNA); Growth hormone receptor (mRNA); GH receptor (mRNA) TTHJWYD GN GHR TTHJWYD FC On ligand binding, couples to the JAK2/STAT5 pathway. Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. TTHJWYD PD 5OHD; 5OEK; 3HHR; 2AEW; 1KF9 TTHJWYD SQ MDLWQLLLTLALAGSSDAFSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKTEESDTDRLLSSDHEKSHSNLGVKDGDSGRTSCCEPDILETDFNANDIHEGTSEVAQPQRLKGEADLLCLDQKNQNNSPYHDACPATQQPSVIQAEKNKPQPLPTEGAESTHQAAHIQLSNPSSLSNIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHPEMVSLCQENFLMDNAYFCEADAKKCIPVAPHIKVESHIQPSLNQEDIYITTESLTTAAGRPGTGEHVPGSEMPVPDYTSIHIVQSPQGLILNATALPLPDKEFLSSCGYVSTDQLNKIMP TTHJWYD TT Clinical trial TTHJWYD FM mRNA target TTHJWYD KE hsa04060:Cytokine-cytokine receptor interaction; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway TTHJWYD RC R-HSA-1170546:Prolactin receptor signaling; R-HSA-982772:Growth hormone receptor signaling TTF23ML ID TTF23ML TTF23ML TN Glial cell line-derived neurotrophic factor (GDNF) TTF23ML UP P39905 TTF23ML UC GDNF_HUMAN TTF23ML BC Growth factor TTF23ML SN hGDNF; Glial cell linederived neurotrophic factor; Astrocytederived trophic factor; Astrocyte-derived trophic factor; ATF TTF23ML GN GDNF TTF23ML FC Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. TTF23ML PD 4UX8; 3FUB; 2V5E TTF23ML SQ MKLWDVVAVCLVLLHTASAFPLPAGKRPPEAPAEDRSLGRRRAPFALSSDSNMPEDYPDQFDDVMDFIQATIKRLKRSPDKQMAVLPRRERNRQAAAANPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCDAAETTYDKILKNLSRNRRLVSDKVGQACCRPIAFDDDLSFLDDNLVYHILRKHSAKRCGCI TTF23ML TT Clinical trial TTF23ML FM Transforming growth factor TT0NUFM ID TT0NUFM TT0NUFM TN Glucagon (GCG) TT0NUFM UP P01275 TT0NUFM UC GLUC_HUMAN TT0NUFM BC Glucagon TT0NUFM SN GRPP; GLP2; GLP1; GLP-1 TT0NUFM GN GCG TT0NUFM FC Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes. TT0NUFM PD 6EDS; 5YQZ; 5VAI; 5OTX; 5OTW TT0NUFM SQ MKSIYFVAGLFVMLVQGSWQRSLQDTEEKSRSFSASQADPLSDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLAARDFINWLIQTKITDRK TT0NUFM TT Clinical trial TT0NUFM KE hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04714:Thermogenesis; hsa04911:Insulin secretion; hsa04922:Glucagon signaling pathway TTP6MT5 ID TTP6MT5 TTP6MT5 TN Glucose transporter type 4 (SLC2A4) TTP6MT5 UP P14672 TTP6MT5 UC GLUT4_HUMAN TTP6MT5 BC Major facilitator TTP6MT5 SN Solute carrier family 2, facilitated glucose transporter member 4; Glut4 protein; Glucose transporter type 4, insulin-responsive; GLUT4; GLUT-4 TTP6MT5 GN SLC2A4 TTP6MT5 FC Insulin-regulated facilitative glucose transporter. TTP6MT5 SQ MPSGFQQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPEGPSSIPPGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLVNNVLAVLGGSLMGLANAAASYEMLILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILIAQVLGLESLLGTASLWPLLLGLTVLPALLQLVLLPFCPESPRYLYIIQNLEGPARKSLKRLTGWADVSGVLAELKDEKRKLERERPLSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFETAGVGQPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFSNWTSNFIIGMGFQYVAEAMGPYVFLLFAVLLLGFFIFTFLRVPETRGRTFDQISAAFHRTPSLLEQEVKPSTELEYLGPDEND TTP6MT5 TT Clinical trial TTP6MT5 FM Major facilitator superfamily TTP6MT5 KE hsa04068:FoxO signaling pathway; hsa04152:AMPK signaling pathway; hsa04910:Insulin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04930:Type II diabetes mellitus TTP6MT5 RC R-HSA-1445148:Translocation of GLUT4 to the plasma membrane; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-428790:Facilitative Na+-independent glucose transporters; R-HSA-70153:Glucose transport TTB1RA4 ID TTB1RA4 TTB1RA4 TN GTPase KRas (KRAS) TTB1RA4 UP P01116 TTB1RA4 UC RASK_HUMAN TTB1RA4 BC Small GTPase TTB1RA4 SN c-Ki-ras; c-K-ras; RASK2; Ki-Ras; KRAS2; K-Ras 2 TTB1RA4 GN KRAS TTB1RA4 FC Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the regulation of cell proliferation. Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner. TTB1RA4 PD 6N2K; 6N2J; 6H47; 6H46; 6GQY TTB1RA4 SQ MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM TTB1RA4 TT Clinical trial TTB1RA4 KE hsa01521:EGFR tyrosine kinase inhibitor resistance; hsa01522:Endocrine resistance; hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04062:Chemokine signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04072:Phospholipase D signaling pathway; hsa04137:Mitophagy - animal; hsa04140:Autophagy - animal; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04211:Longevity regulating pathway; hsa04213:Longevity regulating pathway - multiple species; hsa04218:Cellular senescence; hsa04360:Axon guidance; hsa04370:VEGF signaling pathway; hsa04371:Apelin signaling pathway; hsa04540:Gap junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04625:C-type lectin receptor signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04714:Thermogenesis; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04926:Relaxin signaling pathway; hsa04933:AGE-RAGE signaling pathway in diabetic complications; hsa04960:Aldosterone-regulated sodium reabsorption; hsa05034:Alcoholism; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05163:Human cytomegalovirus infection; hsa05165:Human papillomavirus infection; hsa05166:Human T-cell leukemia virus 1 infection; hsa05167:Kaposi sarcoma-associated herpesvirus infection; hsa05170:Human immunodeficiency virus 1 infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer; hsa05224:Breast cancer; hsa05225:Hepatocellular carcinoma; hsa05226:Gastric cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer; hsa05235:PD-L1 expression and PD-1 checkpoint pathway in cancer TTE72ID ID TTE72ID TTE72ID TN Haemophilus influenzae DNA gyrase A (Hae-influ gyrA) TTE72ID UP P43700 TTE72ID UC GYRA_HAEIN TTE72ID BC ATP-hydrolyzing DNA topoisomerase TTE72ID SN GyrA; DNA gyrase subunit A of Haemophilus influenzae TTE72ID GN Hae-influ gyrA TTE72ID FC DNA gyrasenegatively supercoils closed circular double- stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. TTE72ID EC EC 5.6.2.3 TTE72ID SQ MTDSIQSSITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLFSMDREGNTANKKYVKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDAPAAMRYTEVRMQKITQALLTDLDKETVNFSPNYDGELMIPDVLPTRIPALLANGSSGIAVGMATNIPPHNLNEVLNGCLAYIDKNEITIDELMQHIPGPDFPTAALINGRKGIEEAYRTGRGKVYVRARATVETNEKGREQIIVSELPYQVNKAKLVEKIAELIREKKIEGISNITDLSNKEGIRIEIDIKRDAVGEVVLNHLYSLTQMQVTFGINMVALDHGQPRLFNLKEIIEAFVLHRREVVTRRSIFELRKARERTHILEGLAVARSNIDEMIAIIRNSKNREEAATSISSRSWTLHSDIINLLDASARPDELEENLGIQGEQYYLSPAQVNAILELRLHRLTGIAFEEVIKEYEELLVKIADLLHILSSAERLMEVIREELEEVKAQFGDDRLTEITAASGDIDLEDLIAQEDVVVTLSHEGYVKYQPLTDYEAQRRGGKGKSATKMKEEDFIEKLLVANTHDTILCFSSRGRLYWLKVYQLPQASRGARGRPIVNILPLQENERITAILPVSAYEEDKFVVMATAGGIVKKIALTEFSRPRSNGIIALNLRDEDELIGVDITDGSNEIMLFSSQGRVVRFAENAVRAMGRLATGVRGIKLALTNDISDDESAVEIEDISDDNAEASLDLNIDKVVSLVVPKGEGAILTATQNGYGKRTQLSEYPTKSRNTKGVISIKVSERNGKVVAATQVEETDQIMLITDAGTLVRTRVSEVSIVGRNTQGVRLIRTADDEHVVSLERVCDADEDDSLEESSSEE TTE72ID TT Clinical trial TTHYBIX ID TTHYBIX TTHYBIX TN Heat shock protein 70 (HSP70) TTHYBIX UP P0DMV8; P0DMV9 TTHYBIX UC HS71A_HUMAN; HS71B_HUMAN TTHYBIX BC Heat shock protein TTHYBIX SN Heat shock 70 kDa protein; HSP72; HSP70 TTHYBIX GN HSPA1A; HSPA1B TTHYBIX FC In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form. Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes. Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form. Binds to inverted 5'-NGAAN-3' pentamer DNA sequences. Binds to chromatin at heat shock gene promoters. Plays also several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells. Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner. Plays a role in nuclear export of stress-induced HSP70 mRNA. Plays a role in the regulation of mitotic progression. Plays also a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner. Involved in stress-induced cancer cell proliferation in a IER5-dependent manner. Function as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones heat shock proteins (HSPs) that protect cells from cellular insults' damage. TTHYBIX SQ MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD TTHYBIX TT Clinical trial TTH5YN2 ID TTH5YN2 TTH5YN2 TN Heat shock protein 90 beta (HSP90B) TTH5YN2 UP P08238 TTH5YN2 UC HS90B_HUMAN TTH5YN2 BC Heat shock protein TTH5YN2 SN Heat shock 84 kDa; HSP84; HSP 84 TTH5YN2 GN HSP90AB1 TTH5YN2 FC Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). TTH5YN2 PD 5UCJ; 5UCI; 5UCH; 5UC4; 5FWP TTH5YN2 SQ MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLEGDEDASRMEEVD TTH5YN2 TT Clinical trial TTH5YN2 KE hsa04141:Protein processing in endoplasmic reticulum; hsa04151:PI3K-Akt signaling pathway; hsa04217:Necroptosis; hsa04612:Antigen processing and presentation; hsa04621:NOD-like receptor signaling pathway; hsa04657:IL-17 signaling pathway; hsa04659:Th17 cell differentiation; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa05200:Pathways in cancer; hsa05215:Prostate cancer; hsa05418:Fluid shear stress and atherosclerosis TTM6HK1 ID TTM6HK1 TTM6HK1 TN Hemoglobin subunit beta (HBB) TTM6HK1 UP P68871 TTM6HK1 UC HBB_HUMAN TTM6HK1 BC Pore-forming globin TTM6HK1 SN LVVhemorphin7; Hemoglobin beta chain; Betaglobin; Beta-globin TTM6HK1 GN HBB TTM6HK1 FC Involved in oxygen transport from the lung to the various peripheral tissues. TTM6HK1 PD 6NBD; 6NBC; 6HBW; 6HAL; 6FQF TTM6HK1 SQ MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH TTM6HK1 TT Clinical trial TTM6HK1 KE hsa05143:African trypanosomiasis; hsa05144:Malaria TTM6HK1 RC R-HSA-1237044:Erythrocytes take up carbon dioxide and release oxygen; R-HSA-1247673:Erythrocytes take up oxygen and release carbon dioxide; R-HSA-2168880:Scavenging of heme from plasma; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TT01M3K ID TT01M3K TT01M3K TN Hepatocyte nuclear factor 1-alpha (HNF1A) TT01M3K UP P20823 TT01M3K UC HNF1A_HUMAN TT01M3K SN Transcription factor-1; Transcription factor 1; TCF1; TCF-1; Liver-specific transcription factor LF-B1; Liver specific transcription factor LF-B1; LFB1; HNF-1A; HNF-1-alpha; HNF-1 alpha TT01M3K GN HNF1A TT01M3K FC Binds to the inverted palindrome 5'-GTTAATNATTAAC-3'. Activates the transcription of CYP1A2, CYP2E1 and CYP3A11. Transcriptional activator that regulates the tissue specific expression of multiple genes, especially in pancreatic islet cells and in liver. TT01M3K PD 2GYP; 1IC8 TT01M3K SQ MVSKLSQLQTELLAALLESGLSKEALIQALGEPGPYLLAGEGPLDKGESCGGGRGELAELPNGLGETRGSEDETDDDGEDFTPPILKELENLSPEEAAHQKAVVETLLQEDPWRVAKMVKSYLQQHNIPQREVVDTTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREVAQQFTHAGQGGLIEEPTGDELPTKKGRRNRFKWGPASQQILFQAYERQKNPSKEERETLVEECNRAECIQRGVSPSQAQGLGSNLVTEVRVYNWFANRRKEEAFRHKLAMDTYSGPPPGPGPGPALPAHSSPGLPPPALSPSKVHGVRYGQPATSETAEVPSSSGGPLVTVSTPLHQVSPTGLEPSHSLLSTEAKLVSAAGGPLPPVSTLTALHSLEQTSPGLNQQPQNLIMASLPGVMTIGPGEPASLGPTFTNTGASTLVIGLASTQAQSVPVINSMGSSLTTLQPVQFSQPLHPSYQQPLMPPVQSHVTQSPFMATMAQLQSPHALYSHKPEVAQYTHTGLLPQTMLITDTTNLSALASLTPTKQVFTSDTEASSESGLHTPASQATTLHVPSQDPAGIQHLQPAHRLSASPTVSSSSLVLYQSSDSSNGQSHLLPSNHSVIETFISTQMASSSQ TT01M3K TT Clinical trial TT01M3K KE hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04950:Maturity onset diabetes of the young TT01M3K RC R-HSA-210745:Regulation of gene expression in beta cells TTWPA54 ID TTWPA54 TTWPA54 TN HIF2-alpha messenger RNA (EPAS1 mRNA) TTWPA54 UP Q99814 TTWPA54 UC EPAS1_HUMAN TTWPA54 BC mRNA target TTWPA54 SN PASD2 mRNA; PAS domain-containing protein 2 mRNA; Member of PAS protein 2 mRNA; MOP2 mRNA; Hypoxia-inducible factor 2-alpha mRNA; HLF mRNA; HIF2A mRNA; HIF2-alpha mRNA; HIF-2-alpha mRNA; HIF-1-alpha-like factor mRNA; Endothelial PAS domain-containing protein 1 mRNA; EPAS-1 mRNA; Class E basic helix-loop-helix protein 73 mRNA; Basic-helix-loop-helix-PAS protein MOP2 mRNA; BHLHE73 mRNA TTWPA54 GN EPAS1 TTWPA54 FC Transcription factor involved in the induction of oxygen regulated genes. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBBP and probably EP300. Interaction with redox regulatory protein APEX seems to activate CTAD (By similarity). TTWPA54 PD 6D0C; 6D0B; 6D09; 6CZW; 6BVB TTWPA54 SQ MTADKEKKRSSSERRKEKSRDAARCRRSKETEVFYELAHELPLPHSVSSHLDKASIMRLAISFLRTHKLLSSVCSENESEAEADQQMDNLYLKALEGFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENLSLKNGSGFGKKSKDMSTERDFFMRMKCTVTNRGRTVNLKSATWKVLHCTGQVKVYNNCPPHNSLCGYKEPLLSCLIIMCEPIQHPSHMDIPLDSKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVIYNPRNLQPQCIMCVNYVLSEIEKNDVVFSMDQTESLFKPHLMAMNSIFDSSGKGAVSEKSNFLFTKLKEEPEELAQLAPTPGDAIISLDFGNQNFEESSAYGKAILPPSQPWATELRSHSTQSEAGSLPAFTVPQAAAPGSTTPSATSSSSSCSTPNSPEDYYTSLDNDLKIEVIEKLFAMDTEAKDQCSTQTDFNELDLETLAPYIPMDGEDFQLSPICPEERLLAENPQSTPQHCFSAMTNIFQPLAPVAPHSPFLLDKFQQQLESKKTEPEHRPMSSIFFDAGSKASLPPCCGQASTPLSSMGGRSNTQWPPDPPLHFGPTKWAVGDQRTEFLGAAPLGPPVSPPHVSTFKTRSAKGFGARGPDVLSPAMVALSNKLKLKRQLEYEEQAFQDLSGGDPPGGSTSHLMWKRMKNLRGGSCPLMPDKPLSANVPNDKFTQNPMRGLGHPLRHLPLPQPPSAISPGENSKSRFPPQCYATQYQDYSLSSAHKVSGMASRLLGPSFESYLLPELTRYDCEVNVPVLGSSTLLQGGDLLRALDQAT TTWPA54 TT Clinical trial TTWPA54 FM mRNA target TTWPA54 KE hsa05200:Pathways in cancer; hsa05211:Renal cell carcinoma TTWPA54 RC R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-1234176:Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha; R-HSA-452723:Transcriptional regulation of pluripotent stem cells TTGS10J ID TTGS10J TTGS10J TN HLA class I antigen B-7 (HLA-B) TTGS10J UP P01889 TTGS10J UC 1B07_HUMAN TTGS10J BC MHC class I TTGS10J SN MHC class I antigen B*7; HLAB; HLA class I histocompatibility antigen, B7 alpha chain; HLA class I histocompatibility antigen, B-7 alpha chain TTGS10J GN HLA-B TTGS10J FC Involved in the presentation of foreign antigens to the immune system. TTGS10J PD 6AVG; 6AVF; 6AT5; 5WMP; 5WMO TTGS10J SQ MLVMAPRTVLLLLSAALALTETWAGSHSMRYFYTSVSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIYKAQAQTDRESLRNLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHDQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEQRRAYLEGECVEWLRRYLENGKDKLERADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSSQSTVPIVGIVAGLAVLAVVVIGAVVAAVMCRRKSSGGKGGSYSQAACSDSAQGSDVSLTA TTGS10J TT Clinical trial TTGS10J FM MHC class I family TT4NXYM ID TT4NXYM TT4NXYM TN Human immunodeficiency virus Negative factor (HIV nef) TT4NXYM UP P03407 TT4NXYM UC NEF_HV1A2 TT4NXYM BC Lentivirus primate group Nef TT4NXYM SN nef; Nef protein; F-protein; 3'ORF; 27 kDa protein TT4NXYM GN HIV nef TT4NXYM FC Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. TT4NXYM PD 6B72; 5XOV; 4U5W; 4U1N; 4U1M TT4NXYM SQ MGGKWSKRSMGGWSAIRERMRRAEPRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAALDISHFLKEKGGLEGLIWSQRRQEILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKVEEANEGENNSLLHPMSLHGMEDAEKEVLVWRFDSKLAFHHMARELHPEYYKDC TT4NXYM TT Clinical trial TTE2N95 ID TTE2N95 TTE2N95 TN Human papillomavirus protein E6 (HPV E6) TTE2N95 UP P03126 TTE2N95 UC VE6_HPV16 TTE2N95 BC Papillomaviridae E protein TTE2N95 SN Protein E6; E6 TTE2N95 GN HPV E6 TTE2N95 FC Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6P targets several other substrates to degradation via the proteasome including host NFX1- 91, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including Bak, Fas-associated death domain- containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway. TTE2N95 PD 6HKS; 4XR8; 4JOP; 4GIZ; 2LJZ TTE2N95 SQ MHQKRTAMFQDPQERPRKLPQLCTELQTTIHDIILECVYCKQQLLRREVYDFAFRDLCIVYRDGNPYAVCDKCLKFYSKISEYRHYCYSLYGTTLEQQYNKPLCDLLIRCINCQKPLCPEEKQRHLDKKQRFHNIRGRWTGRCMSCCRSSRTRRETQL TTE2N95 TT Clinical trial TTQHWNA ID TTQHWNA TTQHWNA TN Hypoxia-inducible factor 1 alpha (HIF-1A) TTQHWNA UP Q16665 TTQHWNA UC HIF1A_HUMAN TTQHWNA SN bHLHe78; Transcription factor HIF-1; PASD8; PAS domain-containing protein 8; Member of PAS protein 1; MOP1; Hypoxia-inducible transcription factor (HIF)-1; Hypoxia-inducible factor 1-alpha; Hypoxia-inducible factor 1 A; Hypoxia inducible factor 1; HIF1-alpha; HIF1 alpha; HIF-1alpha; HIF-1-alpha; HIF-1 alpha; Class E basic helix-loop-helix protein 78; Basic-helix-loop-helix-PAS protein MOP1; ARNT-interacting protein; ARNT interacting protein TTQHWNA GN HIF1A TTQHWNA FC Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia. Functions as a master transcriptional regulator of the adaptive response to hypoxia. TTQHWNA PD 6GMR; 6GFX; 5LAS; 5LA9; 5L9V TTQHWNA SQ MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN TTQHWNA TT Clinical trial TTQHWNA KE hsa04066:HIF-1 signaling pathway; hsa04150:mTOR signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05211:Renal cell carcinoma; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTQHWNA RC R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-1234176:Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha; R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-400253:Circadian Clock TT5RWKQ ID TT5RWKQ TT5RWKQ TN Immunoglobulin gamma Fc receptor IIB (FCGR2B) TT5RWKQ UP P31994 TT5RWKQ UC FCG2B_HUMAN TT5RWKQ BC Immunoglobulin TT5RWKQ SN Low affinity immunoglobulin gamma Fc region receptor II-b; IgG Fc receptor II-b; FcRII-b; Fc-gamma-RIIb; Fc-gamma RII-b; FCG2B; CDw32 B; CD32 B TT5RWKQ GN FCGR2B TT5RWKQ FC Receptor for the Fc region of complexed or aggregated immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells. Binding to this receptor results in down-modulation of previous state of cell activation triggered via antigen receptors on B-cells (BCR), T-cells (TCR) or via another Fc receptor. Isoform IIB1 fails to mediate endocytosis or phagocytosis. Isoform IIB2 does not trigger phagocytosis. TT5RWKQ PD 5OCC; 3WJJ; 2FCB TT5RWKQ SQ MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWINVLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPNFSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAAVVALIYCRKKRISALPGYPECREMGETLPEKPANPTNPDEADKVGAENTITYSLLMHPDALEEPDDQNRI TT5RWKQ TT Clinical trial TT5RWKQ KE hsa04145:Phagosome; hsa04380:Osteoclast differentiation; hsa04662:B cell receptor signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa05150:Staphylococcus aureus infection; hsa05152:Tuberculosis; hsa05162:Measles TT5RWKQ RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell TTMSB0A ID TTMSB0A TTMSB0A TN Integrin alpha-2/beta-1 (ITGA2/B1) TTMSB0A UP P17301-P05556 TTMSB0A UC ITA2_HUMAN-ITB1_HUMAN TTMSB0A BC Integrin TTMSB0A SN alpha(2)beta(1) integrin; Integrin alpha(2)beta(1); Alpha 2 beta 1 integrin TTMSB0A GN ITGA2-ITGB1 TTMSB0A FC Integrin alpha-2/beta-1 isa receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix. TTMSB0A SQ MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGKMGPERTGAAPLPLLLVLALSQGILNCCLAYNVGLPEAKIFSGPSSEQFGYAVQQFINPKGNWLLVGSPWSGFPENRMGDVYKCPVDLSTATCEKLNLQTSTSIPNVTEMKTNMSLGLILTRNMGTGGFLTCGPLWAQQCGNQYYTTGVCSDISPDFQLSASFSPATQPCPSLIDVVVVCDESNSIYPWDAVKNFLEKFVQGLDIGPTKTQVGLIQYANNPRVVFNLNTYKTKEEMIVATSQTSQYGGDLTNTFGAIQYARKYAYSAASGGRRSATKVMVVVTDGESHDGSMLKAVIDQCNHDNILRFGIAVLGYLNRNALDTKNLIKEIKAIASIPTERYFFNVSDEAALLEKAGTLGEQIFSIEGTVQGGDNFQMEMSQVGFSADYSSQNDILMLGAVGAFGWSGTIVQKTSHGHLIFPKQAFDQILQDRNHSSYLGYSVAAISTGESTHFVAGAPRANYTGQIVLYSVNENGNITVIQAHRGDQIGSYFGSVLCSVDVDKDTITDVLLVGAPMYMSDLKKEEGRVYLFTIKKGILGQHQFLEGPEGIENTRFGSAIAALSDINMDGFNDVIVGSPLENQNSGAVYIYNGHQGTIRTKYSQKILGSDGAFRSHLQYFGRSLDGYGDLNGDSITDVSIGAFGQVVQLWSQSIADVAIEASFTPEKITLVNKNAQIILKLCFSAKFRPTKQNNQVAIVYNITLDADGFSSRVTSRGLFKENNERCLQKNMVVNQAQSCPEHIIYIQEPSDVVNSLDLRVDISLENPGTSPALEAYSETAKVFSIPFHKDCGEDGLCISDLVLDVRQIPAAQEQPFIVSNQNKRLTFSVTLKNKRESAYNTGIVVDFSENLFFASFSLPVDGTEVTCQVAASQKSVACDVGYPALKREQQVTFTINFDFNLQNLQNQASLSFQALSESQEENKADNLVNLKIPLLYDAEIHLTRSTNINFYEISSDGNVPSIVHSFEDVGPKFIFSLKVTTGSVPVSMATVIIHIPQYTKEKNPLMYLTGVQTDKAGDISCNADINPLKIGQTSSSVSFKSENFRHTKELNCRTASCSNVTCWLKDVHMKGEYFVNVTTRIWNGTFASSTFQTVQLTAAAEINTYNPEIYVIEDNTVTIPLMIMKPDEKAEVPTGVIIGSIIAGILLLLALVAILWKLGFFKRKYEKMTKNPDEIDETTELSS TTMSB0A TT Clinical trial TTMSB0A RC R-HSA-1566948:Elastic fibre formation; R-HSA-1566977:Fibronectin matrix formation; R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-210991:Basigin interactions; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000157:Laminin interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-416700:Other semaphorin interactions; R-HSA-446343:Localization of the PINCH-ILK-PARVIN complex to focal adhesions; R-HSA-447041:CHL1 interactions; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-75892:Platelet Adhesion to exposed collagen TT6S84X ID TT6S84X TT6S84X TN Integrin alpha-4/beta-1 (ITGA4/B1) TT6S84X UP P13612-P05556 TT6S84X UC ITA4_HUMAN-ITB1_HUMAN TT6S84X BC Integrin TT6S84X SN alpha(4)beta(1) integrin; Alpha 4 beta 1 integrin TT6S84X GN ITGA4-ITGB1 TT6S84X FC Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha- 4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha- 4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. TT6S84X SQ MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGKMAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD TT6S84X TT Clinical trial TT6S84X KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04514:Cell adhesion molecules (CAMs); hsa04640:Hematopoietic cell lineage; hsa04670:Leukocyte transendothelial migration; hsa04672:Intestinal immune network for IgA production; hsa04810:Regulation of actin cytoskeleton; hsa05140:Leishmaniasis; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TT6S84X RC R-HSA-1566948:Elastic fibre formation; R-HSA-1566977:Fibronectin matrix formation; R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-210991:Basigin interactions; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000157:Laminin interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-416700:Other semaphorin interactions; R-HSA-446343:Localization of the PINCH-ILK-PARVIN complex to focal adhesions; R-HSA-447041:CHL1 interactions; R-HSA-5663220:RHO GTPases Activate Formins TTH4QIS ID TTH4QIS TTH4QIS TN Integrin alpha-5/beta-1 (ITGA5/B1) TTH4QIS UP P08648-P05556 TTH4QIS UC ITA5_HUMAN-ITB1_HUMAN TTH4QIS BC Integrin TTH4QIS SN alpha(5)beta(1) integrin; Alpha 5 beta 1 integrin TTH4QIS GN ITGA5-ITGB1 TTH4QIS FC binds to matrix macromolecules and proteinases and thereby stimulates angiogenesis. The interaction of VLA-5 with fibronectin plays an important role in regulating inflammatory cytokine production by human articular chondrocytes. TTH4QIS SQ MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGKMGSRTPESPLHAVQLRWGPRRRPPLLPLLLLLLPPPPRVGGFNLDAEAPAVLSGPPGSFFGFSVEFYRPGTDGVSVLVGAPKANTSQPGVLQGGAVYLCPWGASPTQCTPIEFDSKGSRLLESSLSSSEGEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKEPLSDPVGTCYLSTDNFTRILEYAPCRSDFSWAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQIAESYYPEYLINLVQGQLQTRQASSIYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTILNGSDIRSLYNFSGEQMASYFGYAVAATDVNGDGLDDLLVGAPLLMDRTPDGRPQEVGRVYVYLQHPAGIEPTPTLTLTGHDEFGRFGSSLTPLGDLDQDGYNDVAIGAPFGGETQQGVVFVFPGGPGGLGSKPSQVLQPLWAASHTPDFFGSALRGGRDLDGNGYPDLIVGSFGVDKAVVYRGRPIVSASASLTIFPAMFNPEERSCSLEGNPVACINLSFCLNASGKHVADSIGFTVELQLDWQKQKGGVRRALFLASRQATLTQTLLIQNGAREDCREMKIYLRNESEFRDKLSPIHIALNFSLDPQAPVDSHGLRPALHYQSKSRIEDKAQILLDCGEDNICVPDLQLEVFGEQNHVYLGDKNALNLTFHAQNVGEGGAYEAELRVTAPPEAEYSGLVRHPGNFSSLSCDYFAVNQSRLLVCDLGNPMKAGASLWGGLRFTVPHLRDTKKTIQFDFQILSKNLNNSQSDVVSFRLSVEAQAQVTLNGVSKPEAVLFPVSDWHPRDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQALEGQQLLYVTRVTGLNCTTNHPINPKGLELDPEGSLHHQQKREAPSRSSASSGPQILKCPEAECFRLRCELGPLHQQESQSLQLHFRVWAKTFLQREHQPFSLQCEAVYKALKMPYRILPRQLPQKERQVATAVQWTKAEGSYGVPLWIIILAILFGLLLLGLLIYILYKLGFFKRSLPYGTAMEKAQLKPPATSDA TTH4QIS TT Clinical trial TTH4QIS KE hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04640:Hematopoietic cell lineage; hsa04810:Regulation of actin cytoskeleton; hsa05100:Bacterial invasion of epithelial cells; hsa05131:Shigellosis; hsa05133:Pertussis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTH4QIS RC R-HSA-1566948:Elastic fibre formation; R-HSA-1566977:Fibronectin matrix formation; R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-210991:Basigin interactions; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000157:Laminin interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-416700:Other semaphorin interactions; R-HSA-446343:Localization of the PINCH-ILK-PARVIN complex to focal adhesions; R-HSA-447041:CHL1 interactions; R-HSA-5663220:RHO GTPases Activate Formins TT69TQN ID TT69TQN TT69TQN TN Integrin alpha-V/beta-3 (ITGAV/B3) TT69TQN UP P06756-P05106 TT69TQN UC ITAV_HUMAN-ITB3_HUMAN TT69TQN BC Integrin TT69TQN SN Integrin alphaVbeta3; Integrin alpha-v beta-3; Integrin alpha V beta 3; Alpha(v)beta(3) Integrin; Alpha v beta 3 integrin TT69TQN GN ITGAV-ITGB3 TT69TQN FC Receptor for phagocytosis on macrophages or dendritic cells. In cancer and other diseases, its role in angiogenesis is directly responsible to providing blood supply to problematic overgrowths. TT69TQN SQ MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGTMAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET TT69TQN TT Clinical trial TT69TQN FM Integrin TT69TQN KE hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04640:Hematopoietic cell lineage; hsa04810:Regulation of actin cytoskeleton; hsa05100:Bacterial invasion of epithelial cells; hsa05131:Shigellosis; hsa05133:Pertussis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TT69TQN RC R-HSA-114608:Platelet degranulation; R-HSA-1566948:Elastic fibre formation; R-HSA-1566977:Fibronectin matrix formation; R-HSA-210990:PECAM1 interactions; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-354194:GRB2:SOS provides linkage to MAPK signaling for Integrins; R-HSA-372708:p130Cas linkage to MAPK signaling for integrins; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5674135:MAP2K and MAPK activation TTSYFMA ID TTSYFMA TTSYFMA TN Interferon alpha/beta receptor 1 (IFNAR1) TTSYFMA UP P17181 TTSYFMA UC INAR1_HUMAN TTSYFMA BC Cytokine receptor TTSYFMA SN Type I interferon receptor 1; IFNalpha/beta receptor 1; IFNR1; IFNAR; IFN-alpha/beta receptor 1; IFN-R-1; Cytokine receptor family 2 member 1; Cytokine receptor classII member 1; Cytokine receptor class-II member 1; CRF21; CRF2-1 TTSYFMA GN IFNAR1 TTSYFMA FC Functions in general as heterodimer with IFNAR2. Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves. Can form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway. Component of the receptor for type I interferons, including interferons alpha, IFNB1 and IFNW1. TTSYFMA PD 4PO6; 3SE4; 3SE3; 3S98 TTSYFMA SQ MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSKIWLIVGICIALFALPFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDSGNYSNEDESESKTSEELQQDFV TTSYFMA TT Clinical trial TTSYFMA FM Type II cytokine receptor TTSYFMA KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection TTSYFMA RC R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912694:Regulation of IFNA signaling TTS2TGF ID TTS2TGF TTS2TGF TN Interferon-omega (IFNW1) TTS2TGF UP P05000 TTS2TGF UC IFNW1_HUMAN TTS2TGF BC Cytokine: interferon TTS2TGF SN Interferon omega1; Interferon omega-1; Interferon alphaII1; Interferon alpha-II-1 TTS2TGF GN IFNW1 TTS2TGF FC extracellular space, cytokine activity, cytokine receptor binding, type I interferon receptor binding, adaptive immune response, B cell differentiation, B cell proliferation, cell cycle arrest, cytokine-mediated signaling pathway, humoral immune response. TTS2TGF PD 3SE4 TTS2TGF SQ MALLFPLLAALVMTSYSPVGSLGCDLPQNHGLLSRNTLVLLHQMRRISPFLCLKDRRDFRFPQEMVKGSQLQKAHVMSVLHEMLQQIFSLFHTERSSAAWNMTLLDQLHTGLHQQLQHLETCLLQVVGEGESAGAISSPALTLRRYFQGIRVYLKEKKYSDCAWEVVRMEIMKSLFLSTNMQERLRSKDRDLGSS TTS2TGF TT Clinical trial TTS2TGF KE hsa04060:Cytokine-cytokine receptor interaction; hsa04622:RIG-I-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway TTGN89I ID TTGN89I TTGN89I TN Interleukin 15 receptor alpha (IL15RA) TTGN89I UP Q13261 TTGN89I UC I15RA_HUMAN TTGN89I BC Cytokine receptor TTGN89I SN sIL15Ralpha; sIL15RA; sIL15 receptor subunit alpha; Soluble interleukin15 receptor subunit alpha; Interleukin-15 receptor subunit alpha; IL15Ralpha; IL15 receptor subunit alpha; IL-15RA; IL-15R-alpha; IL-15 receptor subunit alpha; CD215 TTGN89I GN IL15RA TTGN89I FC Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. In neutrophils, binds and activates kinase SYK in response to IL15 stimulation. In neutrophils, required for IL15-induced phagocytosis in a SYK-dependent manner. Expression of different isoforms may alter or interfere with signal transduction. High-affinity receptor for interleukin-15. TTGN89I PD 4GS7; 2Z3R; 2Z3Q; 2ERS TTGN89I SQ MAPRRARGCRTLGLPALLLLLLLRPPATRGITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPAASSPSSNNTAATTAAIVPGSQLMPSKSPSTGTTEISSHESSHGTPSQTTAKNWELTASASHQPPGVYPQGHSDTTVAISTSTVLLCGLSAVSLLACYLKSRQTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL TTGN89I TT Clinical trial TTGN89I KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05166:HTLV-I infection TTZO9B0 ID TTZO9B0 TTZO9B0 TN Interleukin 21 receptor (IL21R) TTZO9B0 UP Q9HBE5 TTZO9B0 UC IL21R_HUMAN TTZO9B0 BC Cytokine receptor TTZO9B0 SN UNQ3121/PRO10273; Novel interleukin receptor; NILR; Interleukin-21 receptor; IL21 receptor; IL-21R; IL-21 receptor; CD360 TTZO9B0 GN IL21R TTZO9B0 FC This is a receptor for interleukin-21. TTZO9B0 PD 4NZD; 3TGX TTZO9B0 SQ MPRGWAAPLLLLLLQGGWGCPDLVCYTDYLQTVICILEMWNLHPSTLTLTWQDQYEELKDEATSCSLHRSAHNATHATYTCHMDVFHFMADDIFSVNITDQSGNYSQECGSFLLAESIKPAPPFNVTVTFSGQYNISWRSDYEDPAFYMLKGKLQYELQYRNRGDPWAVSPRRKLISVDSRSVSLLPLEFRKDSSYELQVRAGPMPGSSYQGTWSEWSDPVIFQTQSEELKEGWNPHLLLLLLLVIVFIPAFWSLKTHPLWRLWKKIWAVPSPERFFMPLYKGCSGDFKKWVGAPFTGSSLELGPWSPEVPSTLEVYSCHPPRSPAKRLQLTELQEPAELVESDGVPKPSFWPTAQNSGGSAYSEERDRPYGLVSIDTVTVLDAEGPCTWPCSCEDDGYPALDLDAGLEPSPGLEDPLLDAGTTVLSCGCVSAGSPGLGGPLGSLLDRLKPPLADGEDWAGGLPWGGRSPGGVSESEAGSPLAGLDMDTFDSGFVGSDCSSPVECDFTSPGDEGPPRSYLRQWVVIPPPLSSPGPQAS TTZO9B0 TT Clinical trial TTZO9B0 FM Cytokine receptor TTZO9B0 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa05321:Inflammatory bowel disease (IBD) TT6H4QR ID TT6H4QR TT6H4QR TN Interleukin 23 receptor (IL23R) TT6H4QR UP Q5VWK5 TT6H4QR UC IL23R_HUMAN TT6H4QR BC Cytokine receptor TT6H4QR SN Interleukin-23 receptor; IL23 receptor; IL-23R; IL-23 receptor TT6H4QR GN IL23R TT6H4QR FC Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response to infection in peripheral tissues. IL23 may be responsible for autoimmune inflammatory diseases and be important for tumorigenesis. Associates with IL12RB1 to form the interleukin-23 receptor. TT6H4QR PD 5MZV TT6H4QR SQ MNQVTIQWDAVIALYILFSWCHGGITNINCSGHIWVEPATIFKMGMNISIYCQAAIKNCQPRKLHFYKNGIKERFQITRINKTTARLWYKNFLEPHASMYCTAECPKHFQETLICGKDISSGYPPDIPDEVTCVIYEYSGNMTCTWNAGKLTYIDTKYVVHVKSLETEEEQQYLTSSYINISTDSLQGGKKYLVWVQAANALGMEESKQLQIHLDDIVIPSAAVISRAETINATVPKTIIYWDSQTTIEKVSCEMRYKATTNQTWNVKEFDTNFTYVQQSEFYLEPNIKYVFQVRCQETGKRYWQPWSSLFFHKTPETVPQVTSKAFQHDTWNSGLTVASISTGHLTSDNRGDIGLLLGMIVFAVMLSILSLIGIFNRSFRTGIKRRILLLIPKWLYEDIPNMKNSNVVKMLQENSELMNNNSSEQVLYVDPMITEIKEIFIPEHKPTDYKKENTGPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFLPEGSHLSNNNEITSLTLKPPVDSLDSGNNPRLQKHPNFAFSVSSVNSLSNTIFLGELSLILNQGECSSPDIQNSVEEETTMLLENDSPSETIPEQTLLPDEFVSCLGIVNEELPSINTYFPQNILESHFNRISLLEK TT6H4QR TT Clinical trial TT6H4QR FM Cytokine receptor TT6H4QR KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa05321:Inflammatory bowel disease (IBD) TTPYS82 ID TTPYS82 TTPYS82 TN Interleukin 3 receptor (CSF2RB) TTPYS82 UP P32927 TTPYS82 UC IL3RB_HUMAN TTPYS82 BC Cytokine receptor TTPYS82 SN IL5RB; IL3RB; IL-5R; GM-CSF/IL-3/IL-5 receptor common beta subunit; Cytokine receptor common subunit beta; CDw131; CD131 TTPYS82 GN CSF2RB TTPYS82 FC High affinity receptor for interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor. TTPYS82 PD 5DWU; 4NKQ; 2NA9; 2NA8; 2GYS TTPYS82 SQ MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYIVSVQPRRAEKHIKSSVNIQMAPPSLNVTKDGDSYSLRWETMKMRYEHIDHTFEIQYRKDTATWKDSKTETLQNAHSMALPALEPSTRYWARVRVRTSRTGYNGIWSEWSEARSWDTESVLPMWVLALIVIFLTIAVLLALRFCGIYGYRLRRKWEEKIPNPSKSHLFQNGSAELWPPGSMSAFTSGSPPHQGPWGSRFPELEGVFPVGFGDSEVSPLTIEDPKHVCDPPSGPDTTPAASDLPTEQPPSPQPGPPAASHTPEKQASSFDFNGPYLGPPHSRSLPDILGQPEPPQEGGSQKSPPPGSLEYLCLPAGGQVQLVPLAQAMGPGQAVEVERRPSQGAAGSPSLESGGGPAPPALGPRVGGQDQKDSPVAIPMSSGDTEDPGVASGYVSSADLVFTPNSGASSVSLVPSLGLPSDQTPSLCPGLASGPPGAPGPVKSGFEGYVELPPIEGRSPRSPRNNPVPPEAKSPVLNPGERPADVSPTSPQPEGLLVLQQVGDYCFLPGLGPGPLSLRSKPSSPGPGPEIKNLDQAFQVKKPPGQAVPQVPVIQLFKALKQQDYLSLPPWEVNKPGEVC TTPYS82 TT Clinical trial TTPYS82 FM Type I cytokine receptor TTPYS82 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage TTPYS82 RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-5683826:Surfactant metabolism; R-HSA-912526:Interleukin receptor SHC signaling TT1EPXZ ID TT1EPXZ TT1EPXZ TN Interleukin-24 (IL24) TT1EPXZ UP Q13007 TT1EPXZ UC IL24_HUMAN TT1EPXZ BC Cytokine: interleukin TT1EPXZ SN Suppression of tumorigenicity 16 protein; ST16; Melanoma differentiationassociated gene 7 protein; Melanoma differentiation-associated gene 7 protein; MDA7; MDA-7; Interleukin24; IL-24 TT1EPXZ GN IL24 TT1EPXZ FC Has antiproliferative properties on melanoma cells and may contribute to terminal cell differentiation. TT1EPXZ PD 6GG1; 6DF3 TT1EPXZ SQ MNFQQRLQSLWTLARPFCPPLLATASQMQMVVLPCLGFTLLLWSQVSGAQGQEFHFGPCQVKGVVPQKLWEAFWAVKDTMQAQDNITSARLLQQEVLQNVSDAESCYLVHTLLEFYLKTVFKNYHNRTVEVRTLKSFSTLANNFVLIVSQLQPSQENEMFSIRDSAHRRFLLFRRAFKQLDVEAALTKALGEVDILLTWMQKFYKL TT1EPXZ TT Clinical trial TT1EPXZ FM Cytokine: interleukin TT1EPXZ KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway TTLGTKB ID TTLGTKB TTLGTKB TN Interleukin-4 (IL4) TTLGTKB UP P05112 TTLGTKB UC IL4_HUMAN TTLGTKB BC Cytokine: interleukin TTLGTKB SN Pitrakinra; Lymphocyte stimulatory factor 1; IL-4; Binetrakin; BSF-1; B-cell stimulatory factor 1 TTLGTKB GN IL4 TTLGTKB FC It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4. Participates in at least several B-cell activation processes as well as of other cell types. TTLGTKB PD 5FHX; 4YDY; 3QB7; 3BPN; 3BPL TTLGTKB SQ MGLTSQLLPPLFFLLACAGNFVHGHKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSHHEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERLKTIMREKYSKCSS TTLGTKB TT Clinical trial TTLGTKB FM Growth factor TTLGTKB KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05140:Leishmaniasis; hsa05162:Measles; hsa05310:Asthma; hsa05320:Autoimmune thyroid disease; hsa05321:Inflammatory bowel disease (IBD); hsa05330:Allograft rejection TT2VIZQ ID TT2VIZQ TT2VIZQ TN ITGAV messenger RNA (ITGAV mRNA) TT2VIZQ UP P06756 TT2VIZQ UC ITAV_HUMAN TT2VIZQ BC mRNA target TT2VIZQ SN Vitronectin receptor subunit alpha (mRNA); Vitronectin receptor alpha subunit (mRNA); Vitronectin receptor (mRNA); VTNR (mRNA); VNRA (mRNA); MSK8 (mRNA); CD51 antigen (mRNA); CD51 (mRNA) TT2VIZQ GN ITGAV TT2VIZQ FC The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling. ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling. ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling. ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling. ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGAV:ITGB3 and ITGAV:ITGB6 act as a receptor for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1. Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6 or ITGAV:ITGB8) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation. TT2VIZQ PD 6DJP; 6AVU; 6AVR; 6AVQ; 5NEU TT2VIZQ SQ MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET TT2VIZQ TT Clinical trial TT2VIZQ FM mRNA target TT2FX8W ID TT2FX8W TT2FX8W TN Keratin 6A messenger RNA (KRT6A mRNA) TT2FX8W UP P02538 TT2FX8W UC K2C6A_HUMAN TT2FX8W BC mRNA target TT2FX8W SN Type-II keratin Kb6 (mRNA); Keratin-6A (mRNA); Keratin, type II cytoskeletal 6A (mRNA); KRT6D (mRNA); K6A (mRNA); Hom s 5 (mRNA); Cytokeratin-6D (mRNA); Cytokeratin-6A (mRNA); CK-6D (mRNA); CK-6A (mRNA) TT2FX8W GN KRT6A TT2FX8W FC Involved in the activation of follicular keratinocytes after wounding, while it does not play a major role in keratinocyte proliferation or migration. Participates in the regulation of epithelial migration by inhibiting the activity of SRC during wound repair. Epidermis-specific type I keratin involved in wound healing. TT2FX8W PD 5KI0 TT2FX8W SQ MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSVSVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVNISVVQSTVSSGYGGASGVGSGLGLGGGSSYSYGSGLGVGGGFSSSSGRAIGGGLSSVGGGSSTIKYTTTSSSSRKSYKH TT2FX8W TT Clinical trial TT2FX8W FM mRNA target TTK0FEA ID TTK0FEA TTK0FEA TN Leucine-rich repeat kinase 2 (LRRK2) TTK0FEA UP Q5S007 TTK0FEA UC LRRK2_HUMAN TTK0FEA BC Kinase TTK0FEA SN PARK8; Leucine-rich repeat serine/threonine-protein kinase 2; Dardarin TTK0FEA GN LRRK2 TTK0FEA FC Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). Plays a role in synaptic vesicle trafficking. Phosphorylates PRDX3. Has GTPase activity. May play a role in the phosphorylation of proteins central to Parkinson disease. Plays an important role in recuiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization. TTK0FEA EC EC 2.7.11.1 TTK0FEA PD 6DLP; 6DLO; 5MYC; 5MY9; 3D6T TTK0FEA SQ MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE TTK0FEA TT Clinical trial TTID542 ID TTID542 TTID542 TN Leukemia inhibitory factor receptor (LIFR) TTID542 UP P42702 TTID542 UC LIFR_HUMAN TTID542 BC Cytokine receptor TTID542 SN LIF-R; LIF receptor; CD118 TTID542 GN LIFR TTID542 FC May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells. Signal-transducing molecule. TTID542 PD 3E0G TTID542 SQ MMDIYVCLKRPSWMVDNKRMRTASNFQWLLSTFILLYLMNQVNSQKKGAPHDLKCVTNNLQVWNCSWKAPSGTGRGTDYEVCIENRSRSCYQLEKTSIKIPALSHGDYEITINSLHDFGSSTSKFTLNEQNVSLIPDTPEILNLSADFSTSTLYLKWNDRGSVFPHRSNVIWEIKVLRKESMELVKLVTHNTTLNGKDTLHHWSWASDMPLECAIHFVEIRCYIDNLHFSGLEEWSDWSPVKNISWIPDSQTKVFPQDKVILVGSDITFCCVSQEKVLSALIGHTNCPLIHLDGENVAIKIRNISVSASSGTNVVFTTEDNIFGTVIFAGYPPDTPQQLNCETHDLKEIICSWNPGRVTALVGPRATSYTLVESFSGKYVRLKRAEAPTNESYQLLFQMLPNQEIYNFTLNAHNPLGRSQSTILVNITEKVYPHTPTSFKVKDINSTAVKLSWHLPGNFAKINFLCEIEIKKSNSVQEQRNVTIKGVENSSYLVALDKLNPYTLYTFRIRCSTETFWKWSKWSNKKQHLTTEASPSKGPDTWREWSSDGKNLIIYWKPLPINEANGKILSYNVSCSSDEETQSLSEIPDPQHKAEIRLDKNDYIISVVAKNSVGSSPPSKIASMEIPNDDLKIEQVVGMGKGILLTWHYDPNMTCDYVIKWCNSSRSEPCLMDWRKVPSNSTETVIESDEFRPGIRYNFFLYGCRNQGYQLLRSMIGYIEELAPIVAPNFTVEDTSADSILVKWEDIPVEELRGFLRGYLFYFGKGERDTSKMRVLESGRSDIKVKNITDISQKTLRIADLQGKTSYHLVLRAYTDGGVGPEKSMYVVTKENSVGLIIAILIPVAVAVIVGVVTSILCYRKREWIKETFYPDIPNPENCKALQFQKSVCEGSSALKTLEMNPCTPNNVEVLETRSAFPKIEDTEIISPVAERPEDRSDAEPENHVVVSYCPPIIEEEIPNPAADEAGGTAQVIYIDVQSMYQPQAKPEEEQENDPVGGAGYKPQMHLPINSTVEDIAAEEDLDKTAGYRPQANVNTWNLVSPDSPRSIDSNSEIVSFGSPCSINSRQFLIPPKDEDSPKSNGGGWSFTNFFQNKPND TTID542 TT Clinical trial TTID542 FM Fibronectin TTID542 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04630:Jak-STAT signaling pathway TT0PZR5 ID TT0PZR5 TT0PZR5 TN Leukotriene CysLT2 receptor (CYSLTR2) TT0PZR5 UP Q9NS75 TT0PZR5 UC CLTR2_HUMAN TT0PZR5 BC GPCR rhodopsin TT0PZR5 SN hGPCR21; PSEC0146; HPN321; Gprotein coupled receptor HG57; Gprotein coupled receptor GPCR21; G-protein coupled receptor HG57; G-protein coupled receptor GPCR21; Cysteinyl leukotriene receptor 2; CysLTR2; CYSLT2R; CYSLT2 TT0PZR5 GN CYSLTR2 TT0PZR5 FC The response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Stimulation by BAY u9773, a partial agonist, induces specific contractions of pulmonary veins and might also have an indirect role in the relaxation of the pulmonary vascular endothelium. The rank order of affinities for the leukotrienes is LTC4 = LTD4 >> LTE4. Receptor for cysteinyl leukotrienes. TT0PZR5 SQ MERKFMSLQPSISVSEMEPNGTFSNNNSRNCTIENFKREFFPIVYLIIFFWGVLGNGLSIYVFLQPYKKSTSVNVFMLNLAISDLLFISTLPFRADYYLRGSNWIFGDLACRIMSYSLYVNMYSSIYFLTVLSVVRFLAMVHPFRLLHVTSIRSAWILCGIIWILIMASSIMLLDSGSEQNGSVTSCLELNLYKIAKLQTMNYIALVVGCLLPFFTLSICYLLIIRVLLKVEVPESGLRVSHRKALTTIIITLIIFFLCFLPYHTLRTVHLTTWKVGLCKDRLHKALVITLALAAANACFNPLLYYFAGENFKDRLKSALRKGHPQKAKTKCVFPVSVWLRKETRV TT0PZR5 TT Clinical trial TT0PZR5 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TT0PZR5 RC R-HSA-391906:Leukotriene receptors; R-HSA-416476:G alpha (q) signalling events TT5CZSM ID TT5CZSM TT5CZSM TN Lymphocyte activation antigen 4F2 (SLC3A2) TT5CZSM UP P08195 TT5CZSM UC 4F2_HUMAN TT5CZSM SN SLC3A2; Lymphocyte activation antigen 4F2 large subunit; CD98; 4F2hc; 4F2 heavy chain antigen; 4F2 cellsurface antigen heavy chain TT5CZSM GN SLC3A2 TT5CZSM FC Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L- nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. Whenassociated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier. TT5CZSM PD 6IRT; 6IRS; 2DH3; 2DH2 TT5CZSM SQ MELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLPSASQNAEMIETGSDCVTQAGLQLLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAGVDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLTSSYLSDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAALPGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQASDLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAA TT5CZSM TT Clinical trial TT5CZSM KE hsa04974:Protein digestion and absorption TT5CZSM RC R-HSA-210991:Basigin interactions; R-HSA-352230:Amino acid transport across the plasma membrane TTEKJP3 ID TTEKJP3 TTEKJP3 TN Lysyl hydroxylase 1 (PLOD1) TTEKJP3 UP Q02809 TTEKJP3 UC PLOD1_HUMAN TTEKJP3 BC Paired donor oxygen oxidoreductase TTEKJP3 SN Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1; Peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase; PLOD; Lysyl hydroxylase; LLH; LH1; LH TTEKJP3 GN PLOD1 TTEKJP3 FC Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. TTEKJP3 EC EC 1.14.11.4 TTEKJP3 SQ MRPLLLLALLGWLLLAEAKGDAKPEDNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGLGEDWNVEKGTSAGGGQKVRLLKKALEKHADKEDLVILFADSYDVLFASGPRELLKKFRQARSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQLFYTKIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLIHGNGPTKLQLNYLGNYIPRFWTFETGCTVCDEGLRSLKGIGDEALPTVLVGVFIEQPTPFVSLFFQRLLRLHYPQKHMRLFIHNHEQHHKAQVEEFLAQHGSEYQSVKLVGPEVRMANADARNMGADLCRQDRSCTYYFSVDADVALTEPNSLRLLIQQNKNVIAPLMTRHGRLWSNFWGALSADGYYARSEDYVDIVQGRRVGVWNVPYISNIYLIKGSALRGELQSSDLFHHSKLDPDMAFCANIRQQDVFMFLTNRHTLGHLLSLDSYRTTHLHNDLWEVFSNPEDWKEKYIHQNYTKALAGKLVETPCPDVYWFPIFTEVACDELVEEMEHFGQWSLGNNKDNRIQGGYENVPTIDIHMNQIGFEREWHKFLLEYIAPMTEKLYPGYYTRAQFDLAFVVRYKPDEQPSLMPHHDASTFTINIALNRVGVDYEGGGCRFLRYNCSIRAPRKGWTLMHPGRLTHYHEGLPTTRGTRYIAVSFVDP TTEKJP3 TT Clinical trial TTEKJP3 FM Oxidoreductases acting on paired donors TTEKJP3 KE hsa00310:Lysine degradation TTEKJP3 RC R-HSA-1650814:Collagen biosynthesis and modifying enzymes TT8I4WB ID TT8I4WB TT8I4WB TN Macrophage inflammatory protein 1-alpha (CCL3) TT8I4WB UP P10147 TT8I4WB UC CCL3_HUMAN TT8I4WB BC Cytokine: CC chemokine TT8I4WB SN Tonsillar lymphocyte LD78 alpha protein; Small-inducible cytokine A3; SIS-beta; SCYA3; PAT 464.1; Macrophage Inflammatory Protein-1alpha Nuclear Protein; MNP; MIP1A; MIP-1-alpha; G0S19-1 protein; G0S19-1; G0/G1 switch regulatory protein 19-1; C-C motif chemokine 3 TT8I4WB GN CCL3 TT8I4WB FC Binds to CCR1, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-alpha induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). Monokine with inflammatory and chemokinetic properties. TT8I4WB PD 5D65; 5COR; 4ZKB; 4RA8; 3KBX TT8I4WB SQ MQVSTAALAVLLCTMALCNQFSASLAADTPTACCFSYTSRQIPQNFIADYFETSSQCSKPGVIFLTKRSRQVCADPSEEWVQKYVSDLELSA TT8I4WB TT Clinical trial TT8I4WB FM Cytokine: CC chemokine TT8I4WB KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa05132:Salmonella infection; hsa05142:Chagas disease (American trypanosomiasis); hsa05323:Rheumatoid arthritis TT8I4WB RC R-HSA-380108:Chemokine receptors bind chemokines TTR01E9 ID TTR01E9 TTR01E9 TN Mannan-binding lectin serine protease-2 (MASP2) TTR01E9 UP O00187 TTR01E9 UC MASP2_HUMAN TTR01E9 BC Peptidase TTR01E9 SN Mannosebinding proteinassociated serine protease 2; Mannanbinding lectin serine protease 2 B chain; Mannanbinding lectin serine protease 2; MBLassociated serine protease 2; MASP2 TTR01E9 GN MASP2 TTR01E9 FC Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase. {ECO:0000269|PubMed:10946292}. TTR01E9 EC EC 3.4.21.104 TTR01E9 PD 5JPM; 4FXG; 3TVJ; 1ZJK; 1SZB TTR01E9 SQ MRLLTLLGLLCGSVATPLGPKWPEPVFGRLASPGFPGEYANDQERRWTLTAPPGYRLRLYFTHFDLELSHLCEYDFVKLSSGAKVLATLCGQESTDTERAPGKDTFYSLGSSLDITFRSDYSNEKPFTGFEAFYAAEDIDECQVAPGEAPTCDHHCHNHLGGFYCSCRAGYVLHRNKRTCSALCSGQVFTQRSGELSSPEYPRPYPKLSSCTYSISLEEGFSVILDFVESFDVETHPETLCPYDFLKIQTDREEHGPFCGKTLPHRIETKSNTVTITFVTDESGDHTGWKIHYTSTAQPCPYPMAPPNGHVSPVQAKYILKDSFSIFCETGYELLQGHLPLKSFTAVCQKDGSWDRPMPACSIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTMKVNDGKYVCEADGFWTSSKGEKSLPVCEPVCGLSARTTGGRIYGGQKAKPGDFPWQVLILGGTTAAGALLYDNWVLTAAHAVYEQKHDASALDIRMGTLKRLSPHYTQAWSEAVFIHEGYTHDAGFDNDIALIKLNNKVVINSNITPICLPRKEAESFMRTDDIGTASGWGLTQRGFLARNLMYVDIPIVDHQKCTAAYEKPPYPRGSVTANMLCAGLESGGKDSCRGDSGGALVFLDSETERWFVGGIVSWGSMNCGEAGQYGVYTKVINYIPWIENIISDF TTR01E9 TT Clinical trial TT5MN2U ID TT5MN2U TT5MN2U TN Maternal embryonic leucine zipper kinase (MELK) TT5MN2U UP Q14680 TT5MN2U UC MELK_HUMAN TT5MN2U BC Protein kinase superfamily. CAMK Ser/Thr protein kinase family TT5MN2U SN Protein kinase PK38; Protein kinase Eg3 TT5MN2U GN MELK TT5MN2U FC Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis. TT5MN2U EC EC 2.7.11.1 TT5MN2U PD 5TX3; 5TWZ; 5TWY; 5TWU; 5TWL TT5MN2U SQ MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV TT5MN2U TT Clinical trial TT4RXME ID TT4RXME TT4RXME TN Mesothelin (MSLN) TT4RXME UP Q13421 TT4RXME UC MSLN_HUMAN TT4RXME SN Prepromegakaryocytepotentiating factor; Pre-pro-megakaryocyte-potentiating factor; Mesothelin, cleaved form; MPF; CAK1 antigen TT4RXME GN MSLN TT4RXME FC Membrane-anchored forms may play a role in cellular adhesion. TT4RXME PD 4F3F TT4RXME SQ MALPTARPLLGSCGTPALGSLLFLLFSLGWVQPSRTLAGETGQEAAPLDGVLANPPNISSLSPRQLLGFPCAEVSGLSTERVRELAVALAQKNVKLSTEQLRCLAHRLSEPPEDLDALPLDLLLFLNPDAFSGPQACTRFFSRITKANVDLLPRGAPERQRLLPAALACWGVRGSLLSEADVRALGGLACDLPGRFVAESAEVLLPRLVSCPGPLDQDQQEAARAALQGGGPPYGPPSTWSVSTMDALRGLLPVLGQPIIRSIPQGIVAAWRQRSSRDPSWRQPERTILRPRFRREVEKTACPSGKKAREIDESLIFYKKWELEACVDAALLATQMDRVNAIPFTYEQLDVLKHKLDELYPQGYPESVIQHLGYLFLKMSPEDIRKWNVTSLETLKALLEVNKGHEMSPQAPRRPLPQVATLIDRFVKGRGQLDKDTLDTLTAFYPGYLCSLSPEELSSVPPSSIWAVRPQDLDTCDPRQLDVLYPKARLAFQNMNGSEYFVKIQSFLGGAPTEDLKALSQQNVSMDLATFMKLRTDAVLPLTVAEVQKLLGPHVEGLKAEERHRPVRDWILRQRQDDLDTLGLGLQGGIPNGYLVLDLSMQEALSGTPCLLGPGPVLTVLALLLASTLA TT4RXME TT Clinical trial TT4RXME FM Mesothelin TTS87KH ID TTS87KH TTS87KH TN Microtubule-associated protein tau (MAPT) TTS87KH UP P10636 TTS87KH UC TAU_HUMAN TTS87KH SN tau; Paired helical filamenttau; Paired helical filament-tau; Neurofibrillary tangle protein; MTBT1; MAPTL TTS87KH GN MAPT TTS87KH FC The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. TTS87KH PD 6QJQ; 6QJP; 6QJM; 6QJH; 6NWQ TTS87KH SQ MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPAQDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSSDPLIQPSSPAVCPEPPSSPKYVSSVTSRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL TTS87KH TT Clinical trial TTS87KH KE hsa04010:MAPK signaling pathway; hsa05010:Alzheimer's disease TTS87KH RC R-HSA-264870:Caspase-mediated cleavage of cytoskeletal proteins TTWYMFE ID TTWYMFE TTWYMFE TN Mitochondrial 10kDa heat shock protein (HSPE1) TTWYMFE UP P61604 TTWYMFE UC CH10_HUMAN TTWYMFE BC Heat shock protein TTWYMFE SN Hsp10; Earlypregnancy factor; Early-pregnancy factor; EPF; Chaperonin 10; CPN10; 10 kDa heat shock protein, mitochondrial; 10 kDa chaperonin TTWYMFE GN HSPE1 TTWYMFE FC Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. TTWYMFE PD 4PJ1 TTWYMFE SQ MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD TTWYMFE TT Clinical trial TTWYMFE FM Heat shock protein TT6I7DC ID TT6I7DC TT6I7DC TN Monocyte differentiation antigen CD14 (CD14) TT6I7DC UP P08571 TT6I7DC UC CD14_HUMAN TT6I7DC SN Myeloid cell-specific leucine-rich glycoprotein TT6I7DC GN CD14 TT6I7DC FC In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-). Coreceptor for bacterial lipopolysaccharide. TT6I7DC PD 4GLP TT6I7DC SQ MERASCLLLLLLPLVHVSATTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVDADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKITGTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAFSCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCAALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKLRVLDLSCNRLNRAPQPDELPEVDNLTLDGNPFLVPGTALPHEGSMNSGVVPACARSTLSVGVSGTLVLLQGARGFA TT6I7DC TT Clinical trial TT6I7DC FM Leucine rich repeat TT6I7DC KE hsa04010:MAPK signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04145:Phagosome; hsa04620:Toll-like receptor signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04810:Regulation of actin cytoskeleton; hsa05130:Pathogenic Escherichia coli infection; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05202:Transcriptional misregulation in cancer TT6I7DC RC R-HSA-140534:Ligand-dependent caspase activation; R-HSA-166016:Toll Like Receptor 4 (TLR4) Cascade; R-HSA-166058:MyD88:Mal cascade initiated on plasma membrane; R-HSA-166166:MyD88-independent TLR3/TLR4 cascade; R-HSA-168188:Toll Like Receptor TLR6:TLR2 Cascade; R-HSA-2562578:TRIF-mediated programmed cell death; R-HSA-5602498:MyD88 deficiency (TLR2/4); R-HSA-5603041:IRAK4 deficiency (TLR2/4); R-HSA-936964:Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon; R-HSA-937041:IKK complex recruitment mediated by RIP1; R-HSA-937072:TRAF6 mediated induction of TAK1 complex TTMTPG3 ID TTMTPG3 TTMTPG3 TN Mortalin (HSPA9) TTMTPG3 UP P38646 TTMTPG3 UC GRP75_HUMAN TTMTPG3 BC Heat shock protein TTMTPG3 SN mt-HSP70; Stress-70 protein, mitochondrial; Peptide-binding protein 74; PBP74; MOT; Heat shock 70 kDa protein 9; HSPA9B; GRP75; GRP-75; 75 kDa glucose-regulated protein TTMTPG3 GN HSPA9 TTMTPG3 FC Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging. Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. TTMTPG3 PD 6NHK; 4KBO; 3N8E TTMTPG3 SQ MISASRAAAARLVGAAASRGPTAARHQDSWNGLSHEAFRLVSRRDYASEAIKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDSSGPKHLNMKLTRAQFEGIVTDLIRRTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLKEEISKMRELLARKDSETGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSGTGEQKEDQKEEKQ TTMTPG3 TT Clinical trial TTMTPG3 FM Heat shock protein TTMTPG3 KE hsa03018:RNA degradation; hsa05152:Tuberculosis TTMTPG3 RC R-HSA-1268020:Mitochondrial protein import; R-HSA-3371453:Regulation of HSF1-mediated heat shock response TTW06P4 ID TTW06P4 TTW06P4 TN Mothers against decapentaplegic homolog 7 (SMAD7) TTW06P4 UP O15105 TTW06P4 UC SMAD7_HUMAN TTW06P4 BC Dwarfin/SMAD family TTW06P4 SN hSMAD7; Smad7; SMAD family member 7; SMAD 7; Mothers against decapentaplegic homolog 8; Mothers against DPP homolog 8; MAD homolog 8 TTW06P4 GN SMAD7 TTW06P4 FC Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. TTW06P4 PD 2LTZ; 2LTY; 2LTX; 2LTW; 2LTV TTW06P4 SQ MFRTKRSALVRRLWRSRAPGGEDEEEGAGGGGGGGELRGEGATDSRAHGAGGGGPGRAGCCLGKAVRGAKGHHHPHPPAAGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPAGAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR TTW06P4 TT Clinical trial TTW06P4 KE hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway TTBHFYQ ID TTBHFYQ TTBHFYQ TN Mucin-1 (MUC1) TTBHFYQ UP P15941 TTBHFYQ UC MUC1_HUMAN TTBHFYQ SN Tumour-associated antigen mucin 1; Tumor-associated mucin; Tumor-associated epithelial membraneantigen; Tumor-associated epithelial membrane antigen; Polymorphic epithelial mucin; Peanut-reactive urinary mucin; PUM; PEMT; PEM; MUC-1; Krebs von den Lungen-6; KL-6; H23AG; Episialin; EMA; Carcinoma-associated mucin; Cancer antigen 15-3; CD227 antigen; CD227; CA 15-3; Breast carcinoma-associated antigen DF3 TTBHFYQ GN MUC1 TTBHFYQ FC Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack. The alpha subunit has cell adhesive properties. TTBHFYQ PD 6FZR; 6FZQ; 5T78; 5T6P; 2FO4 TTBHFYQ SQ MTPGTQSPFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAHDVTSAPDNKPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDNRPALGSTAPPVHNVTSASGSASGSASTLVHNGTSARATTTPASKSTPFSIPSHHSDTPTTLASHSTKTDASSTHHSSVPPLTSSNHSTSPQLSTGVSFFFLSFHISNLQFNSSLEDPSTDYYQELQRDISEMFLQIYKQGGFLGLSNIKFRPGSVVVQLTLAFREGTINVHDVETQFNQYKTEAASRYNLTISDVSVSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPARDTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL TTBHFYQ TT Clinical trial TTBHFYQ FM Mucin family TTXDKHT ID TTXDKHT TTXDKHT TN Mutated oxalosuccinate decarboxylase (mIDH1) TTXDKHT UP O75874 (mutated) TTXDKHT UC IDHC_HUMAN TTXDKHT BC Short-chain dehydrogenases reductase TTXDKHT SN PICD (mutated); Oxalosuccinate decarboxylase (mutated); NADP(+)-specific ICDH (mutated); Isocitrate dehydrogenase [NADP] cytoplasmic (mutated); IDP (mutated); IDH (mutated); Cytosolic NADP-isocitrate dehydrogenase (mutated) TTXDKHT GN IDH1 TTXDKHT FC Catalyses the NADPH-dependent reduction of alpha-ketoglutarate to R(-)-2-hydroxyglutarate (2HG). TTXDKHT EC EC 1.1.1.42 TTXDKHT PD 6BL2; 6BL1; 6BL0; 6BKZ; 6BKY TTXDKHT SQ MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL TTXDKHT TT Clinical trial TT3IFEZ ID TT3IFEZ TT3IFEZ TN Mutated tyrosine-protein kinase Kit (mKIT) TT3IFEZ UP P10721 (mutated) TT3IFEZ UC KIT_HUMAN TT3IFEZ BC Kinase TT3IFEZ SN v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog (mutated); p145 c-kit (mutated); Tyrosine-protein kinase Kit (mutated); SCFR; Proto-oncogene c-Kit (mutated); Piebald trait protein (mutated); PBT (mutated); Mast/stem cell growth factor receptor Kit (mutated); CD117 (mutated) TT3IFEZ GN KIT TT3IFEZ FC Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1. TT3IFEZ EC EC 2.7.10.1 TT3IFEZ PD 6GQM; 6GQL; 6GQK; 6GQJ; 4U0I TT3IFEZ SQ MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWEDYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDSSAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSVGSTASSSQPLLVHDDV TT3IFEZ TT Literature-reported TTVW4XU ID TTVW4XU TTVW4XU TN MYCBP messenger RNA (MYCBP mRNA) TTVW4XU UP Q99417 TTVW4XU UC MYCBP_HUMAN TTVW4XU BC mRNA target TTVW4XU SN c-Myc-binding protein (mRNA); Associate of Myc 1 (mRNA); AMY1 (mRNA); AMY-1 (mRNA) TTVW4XU GN MYCBP TTVW4XU FC Stimulates the activation of E box-dependent transcription by MYC. May control the transcriptional activity of MYC. TTVW4XU PD 2YY0 TTVW4XU SQ MAHYKAADSKREQFRRYLEKSGVLDTLTKVLVALYEEPEKPNSALDFLKHHLGAATPENPEIELLRLELAEMKEKYEAIVEENKKLKAKLAQYEPPQEEKRAE TTVW4XU TT Clinical trial TTVW4XU FM mRNA target TTZYJ8U ID TTZYJ8U TTZYJ8U TN Mycobacterium Antigen complex 85A (MycB fbpA) TTZYJ8U UP P9WQP3 TTZYJ8U UC A85A_MYCTU TTZYJ8U BC Acyltransferase TTZYJ8U SN Fibronectinbinding protein A; Fbps A; Diacylglycerol acyltransferase/mycolyltransferase Ag85A; Antigen 85 complex A; Ag85A; AcylCoA:diacylglycerol acyltransferase; 85A TTZYJ8U GN MycB fbpA TTZYJ8U FC The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan, and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as the acyl acceptor. It has a preference for C26:0-CoAover C18:1-CoA. TTZYJ8U PD 1SFR TTZYJ8U SQ MQLVDRVRGAVTGMSRRLVVGAVGAALVSGLVGAVGGTATAGAFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGANSPALYLLDGLRAQDDFSGWDINTPAFEWYDQSGLSVVMPVGGQSSFYSDWYQPACGKAGCQTYKWETFLTSELPGWLQANRHVKPTGSAVVGLSMAASSALTLAIYHPQQFVYAGAMSGLLDPSQAMGPTLIGLAMGDAGGYKASDMWGPKEDPAWQRNDPLLNVGKLIANNTRVWVYCGNGKPSDLGGNNLPAKFLEGFVRTSNIKFQDAYNAGGGHNGVFDFPDSGTHSWEYWGAQLNAMKPDLQRALGATPNTGPAPQGA TTZYJ8U TT Clinical trial TTZYJ8U KE mtu00561:Glycerolipid metabolism; mtu01100:Metabolic pathways TTI0TCK ID TTI0TCK TTI0TCK TN Mycobacterium CDP-diacylglycerol-inositol phosphatidyltransferase (MycB pssA) TTI0TCK UP P9WPG1 TTI0TCK UC PSS_MYCTU TTI0TCK BC Kinase TTI0TCK SN pssA; PtdIns synthase; Phosphatidylinositol synthase; PI synthase TTI0TCK GN MycB pssA TTI0TCK FC Catalyzes the biosynthesis of phosphatidylinositol (ptdins) as well as ptdins:inositol exchange reaction. May thus act to reduce an excessive cellular ptdins content. The exchange activity is due to the reverse reaction of ptdins synthase. TTI0TCK EC EC 2.7.8.8 TTI0TCK SQ MIGKPRGRRGVNLQILPSAMTVLSICAGLTAIKFALEHQPKAAMALIAAAAILDGLDGRVARILDAQSRMGAEIDSLADAVNFGVTPALVLYVSMLSKWPVGWVVVLLYAVCVVLRLARYNALQDDGTQPAYAHEFFVGMPAPAGAVSMIGLLALKMQFGEGWWTSGWFLSFWVTGTSILLVSGIPMKKMHAVSVPPNYAAALLAVLAICAAAAVLAPYLLIWVIIIAYMCHIPFAVRSQRWLAQHPEVWDDKPKQRRAVRRASRRAHPYRPSMARLGLRKPGRRL TTI0TCK TT Clinical trial TT2RY5P ID TT2RY5P TT2RY5P TN Myelin basic protein (MBP) TT2RY5P UP P02686 TT2RY5P UC MBP_HUMAN TT2RY5P SN Myelin membrane encephalitogenic protein; Myelin A1 protein TT2RY5P GN MBP TT2RY5P FC The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation. TT2RY5P PD 1ZGL; 1YMM; 1QCL; 1K2D; 1HQR TT2RY5P SQ MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR TT2RY5P TT Clinical trial TT2RY5P FM Myelin basic protein TTNIMDP ID TTNIMDP TTNIMDP TN Myosin-7 (MYH7) TTNIMDP UP P12883 TTNIMDP UC MYH7_HUMAN TTNIMDP BC TRAFAC class myosin-kinesin ATPase TTNIMDP SN Myosin heavy chain, cardiac muscle beta isoform; Myosin heavy chain slow isoform; Myosin heavy chain 7; MyHCslow; MyHCbeta; MYH7 TTNIMDP GN MYH7 TTNIMDP FC Muscle contraction. TTNIMDP PD 5WME; 5WLZ; 5WLQ; 5WJB; 5WJ7 TTNIMDP SQ MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNEE TTNIMDP TT Clinical trial TTNIMDP KE hsa04022:cGMP-PKG signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04530:Tight junction; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05414:Dilated cardiomyopathy; hsa05416:Viral myocarditis TTNIMDP RC R-HSA-1445148:Translocation of GLUT4 to the plasma membrane TTQRBSJ ID TTQRBSJ TTQRBSJ TN NADPH oxidase 4 (NOX4) TTQRBSJ UP Q9NPH5 TTQRBSJ UC NOX4_HUMAN TTQRBSJ BC NADH/NADPH oxidoreductase TTQRBSJ SN Renal NAD(P)Hoxidase; Renal NAD(P)H-oxidase; RENOX; Kidney superoxideproducing NADPH oxidase; Kidney superoxide-producing NADPH oxidase; Kidney oxidase1; Kidney oxidase-1; KOX1; KOX-1 TTQRBSJ GN NOX4 TTQRBSJ FC Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB. May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation. Isoform 3 is not functional. Isoform 5 and isoform 6 display reduced activity. Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. TTQRBSJ EC EC 1.6.3.- TTQRBSJ SQ MAVSWRSWLANEGVKHLCLFIWLSMNVLLFWKTFLLYNQGPEYHYLHQMLGLGLCLSRASASVLNLNCSLILLPMCRTLLAYLRGSQKVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVNYSEDFVELNAARYRDEDPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSGGLLKYQTNLDTHPPGCISLNRTSSQNISLPEYFSEHFHEPFPEGFSKPAEFTQHKFVKICMEEPRFQANFPQTWLWISGPLCLYCAERLYRYIRSNKPVTIISVMSHPSDVMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQSRNYPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCMLHNKFWQENRPDYVNIQLYLSQTDGIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLSNQNNSYGTRFEYNKESFS TTQRBSJ TT Clinical trial TTQRBSJ FM Ferric reductase TT1WS0T ID TT1WS0T TT1WS0T TN Neural cadherin (CDH2) TT1WS0T UP P19022 TT1WS0T UC CADH2_HUMAN TT1WS0T BC Cadherin protein TT1WS0T SN NCAD; N-cadherin; Cadherin-2; CDw325; CDHN; CD325 TT1WS0T GN CDH2 TT1WS0T FC Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density. Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. TT1WS0T SQ MCRIAGALRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLSKDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPTLTEESVKESAEVEEIVFPRQFSKHSGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDREQIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRIVSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAVITVTDVNDNPPEFTAMTFYGEVPENRVDIIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIQTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTFTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPDPNSINITALDYDIDPNAGPFAFDLPLSPVTIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRMDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPRFKKLADMYGGGDD TT1WS0T TT Clinical trial TT1WS0T FM Cadherin TT1WS0T KE hsa04514:Cell adhesion molecules (CAMs); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC) TT1WS0T RC R-HSA-375170:CDO in myogenesis; R-HSA-418990:Adherens junctions interactions TTJ49OM ID TTJ49OM TTJ49OM TN Neuronal acetylcholine receptor alpha-10 (CHRNA10) TTJ49OM UP Q9GZZ6 TTJ49OM UC ACH10_HUMAN TTJ49OM BC Neurotransmitter receptor TTJ49OM SN Nicotinic acetylcholine receptor subunit alpha 10; NACHR alpha 10; CHRNA10 TTJ49OM GN CHRNA10 TTJ49OM FC Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding may induce an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes thecell membrane. In the ear, this may lead to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma. TTJ49OM SQ MGLRSHHLSLGLLLLFLLPAECLGAEGRLALKLFRDLFANYTSALRPVADTDQTLNVTLEVTLSQIIDMDERNQVLTLYLWIRQEWTDAYLRWDPNAYGGLDAIRIPSSLVWRPDIVLYNKADAQPPGSASTNVVLRHDGAVRWDAPAITRSSCRVDVAAFPFDAQHCGLTFGSWTHGGHQLDVRPRGAAASLADFVENVEWRVLGMPARRRVLTYGCCSEPYPDVTFTLLLRRRAAAYVCNLLLPCVLISLLAPLAFHLPADSGEKVSLGVTVLLALTVFQLLLAESMPPAESVPLIGKYYMATMTMVTFSTALTILIMNLHYCGPSVRPVPAWARALLLGHLARGLCVRERGEPCGQSRPPELSPSPQSPEGGAGPPAGPCHEPRCLCRQEALLHHVATIANTFRSHRAAQRCHEDWKRLARVMDRFFLAIFFSMALVMSLLVLVQAL TTJ49OM TT Clinical trial TTJ49OM KE hsa04080:Neuroactive ligand-receptor interaction TTDEJAU ID TTDEJAU TTDEJAU TN Neurotrophic tyrosine kinase ROR1 (ROR1) TTDEJAU UP Q01973 TTDEJAU UC ROR1_HUMAN TTDEJAU BC Kinase TTDEJAU SN receptor tyrosine kinase-like orphan receptor 1; receptor tyrosine kinase like orphan receptor 1; neurotrophic tyrosine kinase, receptor-related 1; dJ537F10.1; Tyrosine-protein kinase transmembrane receptor ROR1; NTRKR1; Inactive tyrosine-protein kinase transmembrane receptor ROR1 TTDEJAU GN ROR1 TTDEJAU FC Receptor for ligand WNT5A which activate downstream NFkB signaling pathway and may result in the inhibition of WNT3A-mediated signaling. In inner ear, crucial for spiral ganglion neurons to innervate auditory hair cells. Has very low kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo. TTDEJAU PD 6BAN; 6BA5; 5Z55 TTDEJAU SQ MHRPRRRGTRPPLLALLAALLLAARGAAAQETELSVSAELVPTSSWNISSELNKDSYLTLDEPMNNITTSLGQTAELHCKVSGNPPPTIRWFKNDAPVVQEPRRLSFRSTIYGSRLRIRNLDTTDTGYFQCVATNGKEVVSSTGVLFVKFGPPPTASPGYSDEYEEDGFCQPYRGIACARFIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSSVPKPRDLCRDECEILENVLCQTEYIFARSNPMILMRLKLPNCEDLPQPESPEAANCIRIGIPMADPINKNHKCYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHTFTALRFPELNGGHSYCRNPGNQKEAPWCFTLDENFKSDLCDIPACDSKDSKEKNKMEILYILVPSVAIPLAIALLFFFICVCRNNQKSSSAPVQRQPKHVRGQNVEMSMLNAYKPKSKAKELPLSAVRFMEELGECAFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYINQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSWEGLSSHTSSTTPSGGNATTQTTSLSASPVSNLSNPRYPNYMFPSQGITPQGQIAGFIGPPIPQNQRFIPINGYPIPPGYAAFPAAHYQPTGPPRVIQHCPPPKSRSPSSASGSTSTGHVTSLPSSGSNQEANIPLLPHMSIPNHPGGMGITVFGNKSQKPYKIDSKQASLLGDANIHGHTESMISAEL TTDEJAU TT Clinical trial TTDEJAU KE hsa04310:Wnt signaling pathway TT5Y4EM ID TT5Y4EM TT5Y4EM TN N-formyl peptide receptor (FPR1) TT5Y4EM UP P21462 TT5Y4EM UC FPR1_HUMAN TT5Y4EM BC GPCR rhodopsin TT5Y4EM SN N-formylpeptide chemoattractant receptor; FPR1; FPR TT5Y4EM GN FPR1 TT5Y4EM FC High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors (PubMed:2161213, PubMed:2176894, PubMed:10514456, PubMed:15153520). Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release (PubMed:2161213, PubMed:1712023, PubMed:15153520). This response is mediated via a G-protein that activates a phosphatidylinositol- calcium second messenger system(PubMed:1712023, PubMed:10514456). TT5Y4EM SQ METNSSLPTNISGGTPAVSAGYLFLDIITYLVFAVTFVLGVLGNGLVIWVAGFRMTHTVTTISYLNLAVADFCFTSTLPFFMVRKAMGGHWPFGWFLCKFVFTIVDINLFGSVFLIALIALDRCVCVLHPVWTQNHRTVSLAKKVIIGPWVMALLLTLPVIIRVTTVPGKTGTVACTFNFSPWTNDPKERINVAVAMLTVRGIIRFIIGFSAPMSIVAVSYGLIATKIHKQGLIKSSRPLRVLSFVAAAFFLCWSPYQVVALIATVRIRELLQGMYKEIGIAVDVTSALAFFNSCLNPMLYVFMGQDFRERLIHALPASLERALTEDSTQTSDTATNSTLPSAEVELQAK TT5Y4EM TT Clinical trial TT5Y4EM KE hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa05150:Staphylococcus aureus infection TT5Y4EM RC R-HSA-418594:G alpha (i) signalling events TTB1STW ID TTB1STW TTB1STW TN Notch-1 receptor (NOTCH1) TTB1STW UP P46531 TTB1STW UC NOTC1_HUMAN TTB1STW BC Notch protein TTB1STW SN hN1; Translocationassociated notch protein TAN1; Translocation-associated notch protein TAN-1; TAN1; Notch 1 intracellular domain; Notch 1; Neurogenic locus notch homolog protein 1; NICD TTB1STW GN NOTCH1 TTB1STW FC Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4(+) and CD8(+) cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. TTB1STW PD 6IDF; 5UB5; 5L0R; 5KZO; 5FMA TTB1STW SQ MPPLLAPLLCLALLPALAARGPRCSQPGETCLNGGKCEAANGTEACVCGGAFVGPRCQDPNPCLSTPCKNAGTCHVVDRRGVADYACSCALGFSGPLCLTPLDNACLTNPCRNGGTCDLLTLTEYKCRCPPGWSGKSCQQADPCASNPCANGGQCLPFEASYICHCPPSFHGPTCRQDVNECGQKPGLCRHGGTCHNEVGSYRCVCRATHTGPNCERPYVPCSPSPCQNGGTCRPTGDVTHECACLPGFTGQNCEENIDDCPGNNCKNGGACVDGVNTYNCRCPPEWTGQYCTEDVDECQLMPNACQNGGTCHNTHGGYNCVCVNGWTGEDCSENIDDCASAACFHGATCHDRVASFYCECPHGRTGLLCHLNDACISNPCNEGSNCDTNPVNGKAICTCPSGYTGPACSQDVDECSLGANPCEHAGKCINTLGSFECQCLQGYTGPRCEIDVNECVSNPCQNDATCLDQIGEFQCICMPGYEGVHCEVNTDECASSPCLHNGRCLDKINEFQCECPTGFTGHLCQYDVDECASTPCKNGAKCLDGPNTYTCVCTEGYTGTHCEVDIDECDPDPCHYGSCKDGVATFTCLCRPGYTGHHCETNINECSSQPCRHGGTCQDRDNAYLCFCLKGTTGPNCEINLDDCASSPCDSGTCLDKIDGYECACEPGYTGSMCNINIDECAGNPCHNGGTCEDGINGFTCRCPEGYHDPTCLSEVNECNSNPCVHGACRDSLNGYKCDCDPGWSGTNCDINNNECESNPCVNGGTCKDMTSGYVCTCREGFSGPNCQTNINECASNPCLNQGTCIDDVAGYKCNCLLPYTGATCEVVLAPCAPSPCRNGGECRQSEDYESFSCVCPTGWQGQTCEVDINECVLSPCRHGASCQNTHGGYRCHCQAGYSGRNCETDIDDCRPNPCHNGGSCTDGINTAFCDCLPGFRGTFCEEDINECASDPCRNGANCTDCVDSYTCTCPAGFSGIHCENNTPDCTESSCFNGGTCVDGINSFTCLCPPGFTGSYCQHDVNECDSQPCLHGGTCQDGCGSYRCTCPQGYTGPNCQNLVHWCDSSPCKNGGKCWQTHTQYRCECPSGWTGLYCDVPSVSCEVAAQRQGVDVARLCQHGGLCVDAGNTHHCRCQAGYTGSYCEDLVDECSPSPCQNGATCTDYLGGYSCKCVAGYHGVNCSEEIDECLSHPCQNGGTCLDLPNTYKCSCPRGTQGVHCEINVDDCNPPVDPVSRSPKCFNNGTCVDQVGGYSCTCPPGFVGERCEGDVNECLSNPCDARGTQNCVQRVNDFHCECRAGHTGRRCESVINGCKGKPCKNGGTCAVASNTARGFICKCPAGFEGATCENDARTCGSLRCLNGGTCISGPRSPTCLCLGPFTGPECQFPASSPCLGGNPCYNQGTCEPTSESPFYRCLCPAKFNGLLCHILDYSFGGGAGRDIPPPLIEEACELPECQEDAGNKVCSLQCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFSDGHCDSQCNSAGCLFDGFDCQRAEGQCNPLYDQYCKDHFSDGHCDQGCNSAECEWDGLDCAEHVPERLAAGTLVVVVLMPPEQLRNSSFHFLRELSRVLHTNVVFKRDAHGQQMIFPYYGREEELRKHPIKRAAEGWAAPDALLGQVKASLLPGGSEGGRRRRELDPMDVRGSIVYLEIDNRQCVQASSQCFQSATDVAAFLGALASLGSLNIPYKIEAVQSETVEPPPPAQLHFMYVAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKNASDGALMDDNQNEWGDEDLETKKFRFEEPVVLPDLDDQTDHRQWTQQHLDAADLRMSAMAPTPPQGEVDADCMDVNVRGPDGFTPLMIASCSGGGLETGNSEEEEDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPQLHGAPLGGTPTLSPPLCSPNGYLGSLKPGVQGKKVRKPSSKGLACGSKEAKDLKARRKKSQDGKGCLLDSSGMLSPVDSLESPHGYLSDVASPPLLPSPFQQSPSVPLNHLPGMPDTHLGIGHLNVAAKPEMAALGGGGRLAFETGPPRLSHLPVASGTSTVLGSSSGGALNFTVGGSTSLNGQCEWLSRLQSGMVPNQYNPLRGSVAPGPLSTQAPSLQHGMVGPLHSSLAASALSQMMSYQGLPSTRLATQPHLVQTQQVQPQNLQMQQQNLQPANIQQQQSLQPPPPPPQPHLGVSSAASGHLGRSFLSGEPSQADVQPLGPSSLAVHTILPQESPALPTSLPSSLVPPVTAAQFLTPPSQHSYSSPVDNTPSHQLQVPEHPFLTPSPESPDQWSSSSPHSNVSDWSEGVSSPPTSMQSQIARIPEAFK TTB1STW TT Clinical trial TTB1STW FM Notch family TTB1STW KE hsa04320:Dorso-ventral axis formation; hsa04330:Notch signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05020:Prion diseases; hsa05206:MicroRNAs in cancer TTB1STW RC R-HSA-1912399:Pre-NOTCH Processing in the Endoplasmic Reticulum; R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-1912420:Pre-NOTCH Processing in Golgi; R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2122948:Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2660826:Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant; R-HSA-2691232:Constitutive Signaling by NOTCH1 HD Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-350054:Notch-HLH transcription pathway TT82FVD ID TT82FVD TT82FVD TN Notch-2 receptor (NOTCH2) TT82FVD UP Q04721 TT82FVD UC NOTC2_HUMAN TT82FVD BC Notch protein TT82FVD SN hN2; Notch 2 intracellular domain; Notch 2; Neurogenic locus notch homolog protein 2 TT82FVD GN NOTCH2 TT82FVD FC Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in bone remodeling and homeostasis. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. Positively regulates self-renewal of liver cancer cells. Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. TT82FVD PD 5MWB; 2OO4 TT82FVD SQ MPALRPALLWALLALWLCCAAPAHALQCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGTCLNLPGSYQCQCPQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPGFEGSTCERNIDDCPNHRCQNGGVCVDGVNTYNCRCPPQWTGQFCTEDVDECLLQPNACQNGGTCANRNGGYGCVCVNGWSGDDCSENIDDCAFASCTPGSTCIDRVASFSCMCPEGKAGLLCHLDDACISNPCHKGALCDTNPLNGQYICTCPQGYKGADCTEDVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCEMDINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCELEINECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQIDIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGVLCEENIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICSDQIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGVNCEINFDDCASNPCIHGICMDGINRYSCVCSPGFTGQRCNIDIDECASNPCRKGATCINGVNGFRCICPEGPHHPSCYSQVNECLSNPCIHGNCTGGLSGYKCLCDAGWVGINCEVDKNECLSNPCQNGGTCDNLVNGYRCTCKKGFKGYNCQVNIDECASNPCLNQGTCFDDISGYTCHCVLPYTGKNCQTVLAPCSPNPCENAAVCKESPNFESYTCLCAPGWQGQRCTIDIDECISKPCMNHGLCHNTQGSYMCECPPGFSGMDCEEDIDDCLANPCQNGGSCMDGVNTFSCLCLPGFTGDKCQTDMNECLSEPCKNGGTCSDYVNSYTCKCQAGFDGVHCENNINECTESSCFNGGTCVDGINSFSCLCPVGFTGSFCLHEINECSSHPCLNEGTCVDGLGTYRCSCPLGYTGKNCQTLVNLCSRSPCKNKGTCVQKKAESQCLCPSGWAGAYCDVPNVSCDIAASRRGVLVEHLCQHSGVCINAGNTHYCQCPLGYTGSYCEEQLDECASNPCQHGATCSDFIGGYRCECVPGYQGVNCEYEVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCEENIDDCARGPHCLNGGQCMDRIGGYSCRCLPGFAGERCEGDINECLSNPCSSEGSLDCIQLTNDYLCVCRSAFTGRHCETFVDVCPQMPCLNGGTCAVASNMPDGFICRCPPGFSGARCQSSCGQVKCRKGEQCVHTASGPRCFCPSPRDCESGCASSPCQHGGSCHPQRQPPYYSCQCAPPFSGSRCELYTAPPSTPPATCLSQYCADKARDGVCDEACNSHACQWDGGDCSLTMENPWANCSSPLPCWDYINNQCDELCNTVECLFDNFECQGNSKTCKYDKYCADHFKDNHCDQGCNSEECGWDGLDCAADQPENLAEGTLVIVVLMPPEQLLQDARSFLRALGTLLHTNLRIKRDSQGELMVYPYYGEKSAAMKKQRMTRRSLPGEQEQEVAGSKVFLEIDNRQCVQDSDHCFKNTDAAAALLASHAIQGTLSYPLVSVVSESLTPERTQLLYLLAVAVVIILFIILLGVIMAKRKRKHGSLWLPEGFTLRRDASNHKRREPVGQDAVGLKNLSVQVSEANLIGTGTSEHWVDDEGPQPKKVKAEDEALLSEEDDPIDRRPWTQQHLEAADIRRTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVICGPNRSFLSLKHTPMGKKSRRPSAKSTMPTSLPNLAKEAKDAKGSRRKKSLSEKVQLSESSVTLSPVDSLESPHTYVSDTTSSPMITSPGILQASPNPMLATAAPPAPVHAQHALSFSNLHEMQPLAHGASTVLPSVSQLLSHHHIVSPGSGSAGSLSRLHPVPVPADWMNRMEVNETQYNEMFGMVLAPAEGTHPGIAPQSRPPEGKHITTPREPLPPIVTFQLIPKGSIAQPAGAPQPQSTCPPAVAGPLPTMYQIPEMARLPSVAFPTAMMPQQDGQVAQTILPAYHPFPASVGKYPTPPSQHSYASSNAAERTPSHSGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGAGGGQRGPGTHMSEPPHNNMQVYA TT82FVD TT Clinical trial TT82FVD FM Notch family TT82FVD KE hsa04320:Dorso-ventral axis formation; hsa04330:Notch signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05206:MicroRNAs in cancer TT82FVD RC R-HSA-1912399:Pre-NOTCH Processing in the Endoplasmic Reticulum; R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-1912420:Pre-NOTCH Processing in Golgi; R-HSA-2197563:NOTCH2 intracellular domain regulates transcription; R-HSA-2979096:NOTCH2 Activation and Transmission of Signal to the Nucleus; R-HSA-350054:Notch-HLH transcription pathway TTVX7IA ID TTVX7IA TTVX7IA TN Notch-3 receptor (NOTCH3) TTVX7IA UP Q9UM47 TTVX7IA UC NOTC3_HUMAN TTVX7IA BC Notch protein TTVX7IA SN Notch 3 intracellular domain; Notch 3; Neurogenic locus notch homolog protein 3 TTVX7IA GN NOTCH3 TTVX7IA FC Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. TTVX7IA PD 5CZX; 5CZV; 4ZLP TTVX7IA SQ MGPGARGRRRRRRPMSPPPPPPPVRALPLLLLLAGPGAAAPPCLDGSPCANGGRCTQLPSREAACLCPPGWVGERCQLEDPCHSGPCAGRGVCQSSVVAGTARFSCRCPRGFRGPDCSLPDPCLSSPCAHGARCSVGPDGRFLCSCPPGYQGRSCRSDVDECRVGEPCRHGGTCLNTPGSFRCQCPAGYTGPLCENPAVPCAPSPCRNGGTCRQSGDLTYDCACLPGFEGQNCEVNVDDCPGHRCLNGGTCVDGVNTYNCQCPPEWTGQFCTEDVDECQLQPNACHNGGTCFNTLGGHSCVCVNGWTGESCSQNIDDCATAVCFHGATCHDRVASFYCACPMGKTGLLCHLDDACVSNPCHEDAICDTNPVNGRAICTCPPGFTGGACDQDVDECSIGANPCEHLGRCVNTQGSFLCQCGRGYTGPRCETDVNECLSGPCRNQATCLDRIGQFTCICMAGFTGTYCEVDIDECQSSPCVNGGVCKDRVNGFSCTCPSGFSGSTCQLDVDECASTPCRNGAKCVDQPDGYECRCAEGFEGTLCDRNVDDCSPDPCHHGRCVDGIASFSCACAPGYTGTRCESQVDECRSQPCRHGGKCLDLVDKYLCRCPSGTTGVNCEVNIDDCASNPCTFGVCRDGINRYDCVCQPGFTGPLCNVEINECASSPCGEGGSCVDGENGFRCLCPPGSLPPLCLPPSHPCAHEPCSHGICYDAPGGFRCVCEPGWSGPRCSQSLARDACESQPCRAGGTCSSDGMGFHCTCPPGVQGRQCELLSPCTPNPCEHGGRCESAPGQLPVCSCPQGWQGPRCQQDVDECAGPAPCGPHGICTNLAGSFSCTCHGGYTGPSCDQDINDCDPNPCLNGGSCQDGVGSFSCSCLPGFAGPRCARDVDECLSNPCGPGTCTDHVASFTCTCPPGYGGFHCEQDLPDCSPSSCFNGGTCVDGVNSFSCLCRPGYTGAHCQHEADPCLSRPCLHGGVCSAAHPGFRCTCLESFTGPQCQTLVDWCSRQPCQNGGRCVQTGAYCLCPPGWSGRLCDIRSLPCREAAAQIGVRLEQLCQAGGQCVDEDSSHYCVCPEGRTGSHCEQEVDPCLAQPCQHGGTCRGYMGGYMCECLPGYNGDNCEDDVDECASQPCQHGGSCIDLVARYLCSCPPGTLGVLCEINEDDCGPGPPLDSGPRCLHNGTCVDLVGGFRCTCPPGYTGLRCEADINECRSGACHAAHTRDCLQDPGGGFRCLCHAGFSGPRCQTVLSPCESQPCQHGGQCRPSPGPGGGLTFTCHCAQPFWGPRCERVARSCRELQCPVGVPCQQTPRGPRCACPPGLSGPSCRSFPGSPPGASNASCAAAPCLHGGSCRPAPLAPFFRCACAQGWTGPRCEAPAAAPEVSEEPRCPRAACQAKRGDQRCDRECNSPGCGWDGGDCSLSVGDPWRQCEALQCWRLFNNSRCDPACSSPACLYDNFDCHAGGRERTCNPVYEKYCADHFADGRCDQGCNTEECGWDGLDCASEVPALLARGVLVLTVLLPPEELLRSSADFLQRLSAILRTSLRFRLDAHGQAMVFPYHRPSPGSEPRARRELAPEVIGSVVMLEIDNRLCLQSPENDHCFPDAQSAADYLGALSAVERLDFPYPLRDVRGEPLEPPEPSVPLLPLLVAGAVLLLVILVLGVMVARRKREHSTLWFPEGFSLHKDVASGHKGRREPVGQDALGMKNMAKGESLMGEVATDWMDTECPEAKRLKVEEPGMGAEEAVDCRQWTQHHLVAADIRVAPAMALTPPQGDADADGMDVNVRGPDGFTPLMLASFCGGALEPMPTEEDEADDTSASIISDLICQGAQLGARTDRTGETALHLAARYARADAAKRLLDAGADTNAQDHSGRTPLHTAVTADAQGVFQILIRNRSTDLDARMADGSTALILAARLAVEGMVEELIASHADVNAVDELGKSALHWAAAVNNVEATLALLKNGANKDMQDSKEETPLFLAAREGSYEAAKLLLDHFANREITDHLDRLPRDVAQERLHQDIVRLLDQPSGPRSPPGPHGLGPLLCPPGAFLPGLKAAQSGSKKSRRPPGKAGLGPQGPRGRGKKLTLACPGPLADSSVTLSPVDSLDSPRPFGGPPASPGGFPLEGPYAAATATAVSLAQLGGPGRAGLGRQPPGGCVLSLGLLNPVAVPLDWARLPPPAPPGPSFLLPLAPGPQLLNPGTPVSPQERPPPYLAVPGHGEEYPAAGAHSSPPKARFLRVPSEHPYLTPSPESPEHWASPSPPSLSDWSESTPSPATATGAMATTTGALPAQPLPLSVPSSLAQAQTQLGPQPEVTPKRQVLA TTVX7IA TT Clinical trial TTVX7IA FM Notch family TTVX7IA KE hsa04320:Dorso-ventral axis formation; hsa04330:Notch signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05206:MicroRNAs in cancer TTVX7IA RC R-HSA-1912399:Pre-NOTCH Processing in the Endoplasmic Reticulum; R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-1912420:Pre-NOTCH Processing in Golgi; R-HSA-350054:Notch-HLH transcription pathway TTCSZH7 ID TTCSZH7 TTCSZH7 TN Nucleolin (NCL) TTCSZH7 UP P19338 TTCSZH7 UC NUCL_HUMAN TTCSZH7 SN Protein C23 TTCSZH7 GN NCL TTCSZH7 FC It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Nucleolin is the major nucleolar protein of growing eukaryotic cells. TTCSZH7 PD 2KRR; 2FC9; 2FC8 TTCSZH7 SQ MVKLAKAGKNQGDPKKMAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDDDDDEEDDSEEEAMETTPAKGKKAAKVVPVKAKNVAEDEDEEEDDEDEDDDDDEDDEDDDDEDDEEEEEEEEEEPVKEAPGKRKKEMAKQKAAPEAKKQKVEGTEPTTAFNLFVGNLNFNKSAPELKTGISDVFAKNDLAVVDVRIGMTRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGKDSKKERDARTLLAKNLPYKVTQDELKEVFEDAAEIRLVSKDGKSKGIAYIEFKTEADAEKTFEEKQGTEIDGRSISLYYTGEKGQNQDYRGGKNSTWSGESKTLVLSNLSYSATEETLQEVFEKATFIKVPQNQNGKSKGYAFIEFASFEDAKEALNSCNKREIEGRAIRLELQGPRGSPNARSQPSKTLFVKGLSEDTTEETLKESFDGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDHKPQGKKTKFE TTCSZH7 TT Clinical trial TTCSZH7 FM RNA recognition motif TT1NLOA ID TT1NLOA TT1NLOA TN P2X purinoceptor 4 (P2RX4) TT1NLOA UP Q99571 TT1NLOA UC P2RX4_HUMAN TT1NLOA BC ATP-gated P2X receptor cation channel TT1NLOA SN P2X4; P2RX4 TT1NLOA GN P2RX4 TT1NLOA FC Receptor for ATP that acts as a ligand gated ion channel. This receptor is insensitive to the antagonists PPADS and suramin. TT1NLOA SQ MAGCCAALAAFLFEYDTPRIVLIRSRKVGLMNRAVQLLILAYVIGWVFVWEKGYQETDSVVSSVTTKVKGVAVTNTSKLGFRIWDVADYVIPAQEENSLFVMTNVILTMNQTQGLCPEIPDATTVCKSDASCTAGSAGTHSNGVSTGRCVAFNGSVKTCEVAAWCPVEDDTHVPQPAFLKAAENFTLLVKNNIWYPKFNFSKRNILPNITTTYLKSCIYDAKTDPFCPIFRLGKIVENAGHSFQDMAVEGGIMGIQVNWDCNLDRAASLCLPRYSFRRLDTRDVEHNVSPGYNFRFAKYYRDLAGNEQRTLIKAYGIRFDIIVFGKAGKFDIIPTMINIGSGLALLGMATVLCDIIVLYCMKKRLYYREKKYKYVEDYEQGLASELDQ TT1NLOA TT Clinical trial TT1NLOA KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TT9OUDQ ID TT9OUDQ TT9OUDQ TN p53-binding protein Mdm4 (MDM4) TT9OUDQ UP O15151 TT9OUDQ UC MDM4_HUMAN TT9OUDQ BC MDM2/MDM4 family TT9OUDQ SN Protein Mdmx; Mdm2-like p53-binding protein; Double minute 4 protein TT9OUDQ GN MDM4 TT9OUDQ FC Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. TT9OUDQ PD 6Q9Y; 6Q9W; 6Q9U; 6Q9S; 6Q9Q TT9OUDQ SQ MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLATATTDAAQTLALAQDHSMDIPSQDQLKQSAEESSTSRKRTTEDDIPTLPTSEHKCIHSREDEDLIENLAQDETSRLDLGFEEWDVAGLPWWFLGNLRSNYTPRSNGSTDLQTNQDVGTAIVSDTTDDLWFLNESVSEQLGVGIKVEAADTEQTSEEVGKVSDKKVIEVGKNDDLEDSKSLSDDTDVEVTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSDITAIPEKENEGNDVPDCRRTISAPVVRPKDAYIKKENSKLFDPCNSVEFLDLAHSSESQETISSMGEQLDNLSEQRTDTENMEDCQNLLKPCSLCEKRPRDGNIIHGRTGHLVTCFHCARRLKKAGASCPICKKEIQLVIKVFIA TT9OUDQ TT Clinical trial TT9OUDQ KE hsa04115:p53 signaling pathway; hsa05206:MicroRNAs in cancer TTSQC14 ID TTSQC14 TTSQC14 TN Palmitoyl-protein thioesterase 1 (PPT1) TTSQC14 UP P50897 TTSQC14 UC PPT1_HUMAN TTSQC14 BC Palmitoyl thioesterase TTSQC14 SN Palmitoyl-protein hydrolase 1; PPT-1; PPT; CLN1 TTSQC14 GN PPT1 TTSQC14 FC Prefers acyl chain lengths of 14 to 18 carbons. Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. TTSQC14 EC EC 3.1.2.22 TTSQC14 PD 3GRO TTSQC14 SQ MASPGCLWLLAVALLPWTCASRALQHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEKKIPGIYVLSLEIGKTLMEDVENSFFLNVNSQVTTVCQALAKDPKLQQGYNAMGFSQGGQFLRAVAQRCPSPPMINLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYSKVVQERLVQAEYWHDPIKEDVYRNHSIFLADINQERGINESYKKNLMALKKFVMVKFLNDSIVDPVDSEWFGFYRSGQAKETIPLQETSLYTQDRLGLKEMDNAGQLVFLATEGDHLQLSEEWFYAHIIPFLG TTSQC14 TT Clinical trial TTCGSZ4 ID TTCGSZ4 TTCGSZ4 TN Pancreatic alpha-amylase (AMY2A) TTCGSZ4 UP P04746 TTCGSZ4 UC AMYP_HUMAN TTCGSZ4 BC Glycosylase TTCGSZ4 SN PA; 1,4-alpha-D-glucan glucanohydrolase TTCGSZ4 GN AMY2A TTCGSZ4 FC Hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. TTCGSZ4 EC EC 3.2.1.1 TTCGSZ4 PD 5VA9; 5U3A; 5TD4; 5KEZ; 5EMY TTCGSZ4 SQ MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLTGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFVPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL TTCGSZ4 TT Clinical trial TTIB95A ID TTIB95A TTIB95A TN Pancreatic hormone (PH) TTIB95A UP P01298 (30-65) TTIB95A UC PAHO_HUMAN TTIB95A BC Neuropeptide Y TTIB95A SN Pancreatic prohormone; Pancreatic polypeptide; Pancreatic icosapeptide; PPY; PP; PI; PH; Obinepitide TTIB95A GN PPY TTIB95A FC The physiological role for the icosapeptide has notyet been elucidated. TTIB95A PD 1TZ5; 1TZ4 TTIB95A SQ APLEPVYPGDNATPEQMAQYAADLRRYINMLTRPRY TTIB95A TT Clinical trial TTIB95A RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTEPJL5 ID TTEPJL5 TTEPJL5 TN Parathyroid hormone receptor (PTH2R) TTEPJL5 UP P49190 TTEPJL5 UC PTH2R_HUMAN TTEPJL5 BC GPCR secretin TTEPJL5 SN PTHR2; PTH2R; PTH2 receptor TTEPJL5 GN PTH2R TTEPJL5 FC This is a specific receptor for parathyroid hormone. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. PTH2R may be responsible for PTH effects in a number of physiological systems. It may play asignificant role in pancreatic function. PTH2R presence in neurons indicates that it may function as a neurotransmitter receptor. TTEPJL5 SQ MAGLGASLHVWGWLMLGSCLLARAQLDSDGTITIEEQIVLVLKAKVQCELNITAQLQEGEGNCFPEWDGLICWPRGTVGKISAVPCPPYIYDFNHKGVAFRHCNPNGTWDFMHSLNKTWANYSDCLRFLQPDISIGKQEFFERLYVMYTVGYSISFGSLAVAILIIGYFRRLHCTRNYIHMHLFVSFMLRATSIFVKDRVVHAHIGVKELESLIMQDDPQNSIEATSVDKSQYIGCKIAVVMFIYFLATNYYWILVEGLYLHNLIFVAFFSDTKYLWGFILIGWGFPAAFVAAWAVARATLADARCWELSAGDIKWIYQAPILAAIGLNFILFLNTVRVLATKIWETNAVGHDTRKQYRKLAKSTLVLVLVFGVHYIVFVCLPHSFTGLGWEIRMHCELFFNSFQGFFVSIIYCYCNGEVQAEVKKMWSRWNLSVDWKRTPPCGSRRCGSVLTTVTHSTSSQSQVAASTRMVLISGKAAKIASRQPDSHITLPGYVWSNSEQDCLPHSFHEETKEDSGRQGDDILMEKPSRPMESNPDTEGCQGETEDVL TTEPJL5 TT Clinical trial TTEPJL5 KE hsa04080:Neuroactive ligand-receptor interaction TTEPJL5 RC R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-418555:G alpha (s) signalling events TTVFJLX ID TTVFJLX TTVFJLX TN Peptide tyrosine tyrosine PYY (PYY) TTVFJLX UP P10082 (31-64) TTVFJLX UC PYY_HUMAN TTVFJLX BC NPY family TTVFJLX SN PYY-II TTVFJLX GN PYY TTVFJLX FC This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility. TTVFJLX PD 2NA5; 2L60; 2DF0; 2DEZ TTVFJLX SQ IKPEAPREDASPEELNRYYASLRHYLNLVTRQRY TTVFJLX TT Clinical trial TTVFJLX RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTD4TKP ID TTD4TKP TTD4TKP TN Phosphodiesterase I beta (ENPP3) TTD4TKP UP O14638 TTD4TKP UC ENPP3_HUMAN TTD4TKP BC Phosphoric diester hydrolase TTD4TKP SN Phosphodiesterase I/nucleotide pyrophosphatase 3; PDNP3; PD-Ibeta; NPP3; Ectonucleotide pyrophosphatase/phosphodiesterase family member 3; E-NPP 3; CD203c TTD4TKP GN ENPP3 TTD4TKP FC Limits mast cell and basophil responses during inflammation and during the chronic phases of allergic responses by eliminating the extracellular ATP that functions as signaling molecule and activates basophils and mast cells and induces the release of inflammatory cytokines. Metabolizes extracellular ATP in the lumen of the small intestine, and thereby prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic cells. Has also alkaline phosphodiesterase activity. Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP. TTD4TKP PD 6C02; 6C01 TTD4TKP SQ MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFDASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCLQRKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTLMPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLSSKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERISTLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRNLHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNSEEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGGGNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLNHLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEITATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPTVPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEEFRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHYFVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVRDVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI TTD4TKP TT Clinical trial TTR59S1 ID TTR59S1 TTR59S1 TN Pigment epithelium-derived factor (SERPINF1) TTR59S1 UP P36955 TTR59S1 UC PEDF_HUMAN TTR59S1 BC Serpin protein TTR59S1 SN Serpin-F1; SERPINF1; PEDF; EPC-1 TTR59S1 GN SERPINF1 TTR59S1 FC Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformationaltransition characteristic of active serpins, it exhibits no serine protease inhibitory activity. TTR59S1 PD 1IMV TTR59S1 SQ MQALVLLLCIGALLGHSSCQNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYRVRSSTSPTTNVLLSPLSVATALSALSLGAEQRTESIIHRALYYDLISSPDIHGTYKELLDTVTAPQKNLKSASRIVFEKKLRIKSSFVAPLEKSYGTRPRVLTGNPRLDLQEINNWVQAQMKGKLARSTKEIPDEISILLLGVAHFKGQWVTKFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLTGSMSIIFFLPLKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKLSYEGEVTKSLQEMKLQSLFDSPDFSKITGKPIKLTQVEHRAGFEWNEDGAGTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLFIGKILDPRGP TTR59S1 TT Clinical trial TTW4LYC ID TTW4LYC TTW4LYC TN Pituitary adenylate cyclase-activating 38 (PACAP-38) TTW4LYC UP P18509 (132-169) TTW4LYC UC PACA_HUMAN TTW4LYC BC Glucagon TTW4LYC SN Pituitary adenylate cyclase-activating polypeptide; PACAP38; PACAP27; PACAP-38; PACAP-27; PACAP; ADCYAP1 TTW4LYC GN ADCYAP1 TTW4LYC FC Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells. Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway. TTW4LYC PD 2JOD; 2D2P; 1GEA TTW4LYC SQ HSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNK TTW4LYC TT Clinical trial TTW4LYC KE hsa04911:Insulin secretion TTW4LYC RC R-HSA-187024:NGF-independant TRKA activation; R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors TTARMD9 ID TTARMD9 TTARMD9 TN Placental cadherin (CDH3) TTARMD9 UP P22223 TTARMD9 UC CADH3_HUMAN TTARMD9 BC Cadherin protein TTARMD9 SN Pcadherin; P-cadherin; Cadherin-3; CDHP TTARMD9 GN CDH3 TTARMD9 FC Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. TTARMD9 PD 5JYM; 5JYL; 4ZMZ; 4ZMY; 4ZMX TTARMD9 SQ MGLPRGPLASLLLLQVCWLQCAASEPCRAVFREAEVTLEAGGAEQEPGQALGKVFMGCPGQEPALFSTDNDDFTVRNGETVQERRSLKERNPLKIFPSKRILRRHKRDWVVAPISVPENGKGPFPQRLNQLKSNKDRDTKIFYSITGPGADSPPEGVFAVEKETGWLLLNKPLDREEIAKYELFGHAVSENGASVEDPMNISIIVTDQNDHKPKFTQDTFRGSVLEGVLPGTSVMQVTATDEDDAIYTYNGVVAYSIHSQEPKDPHDLMFTIHRSTGTISVISSGLDREKVPEYTLTIQATDMDGDGSTTTAVAVVEILDANDNAPMFDPQKYEAHVPENAVGHEVQRLTVTDLDAPNSPAWRATYLIMGGDDGDHFTITTHPESNQGILTTRKGLDFEAKNQHTLYVEVTNEAPFVLKLPTSTATIVVHVEDVNEAPVFVPPSKVVEVQEGIPTGEPVCVYTAEDPDKENQKISYRILRDPAGWLAMDPDSGQVTAVGTLDREDEQFVRNNIYEVMVLAMDNGSPPTTGTGTLLLTLIDVNDHGPVPEPRQITICNQSPVRQVLNITDKDLSPHTSPFQAQLTDDSDIYWTAEVNEEGDTVVLSLKKFLKQDTYDVHLSLSDHGNKEQLTVIRATVCDCHGHVETCPGPWKGGFILPVLGAVLALLFLLLVLLLLVRKKRKIKEPLLLPEDDTRDNVFYYGEEGGGEEDQDYDITQLHRGLEARPEVVLRNDVAPTIIPTPMYRPRPANPDEIGNFIIENLKAANTDPTAPPYDTLLVFDYEGSGSDAASLSSLTSSASDQDQDYDYLNEWGSRFKKLADMYGGGEDD TTARMD9 TT Clinical trial TTARMD9 FM Cadherin TTARMD9 KE hsa04514:Cell adhesion molecules (CAMs) TTARMD9 RC R-HSA-418990:Adherens junctions interactions TTYQ4AE ID TTYQ4AE TTYQ4AE TN Plasmodium Adenylosuccinate synthetase (Malaria Adss) TTYQ4AE UP Q9U8D3 TTYQ4AE UC PURA_PLAFA TTYQ4AE BC Carbon-nitrogen ligase TTYQ4AE SN IMP--aspartate ligase; Adenylosuccinate synthase; AdSS; AMPSase TTYQ4AE GN Malaria Adss TTYQ4AE FC Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. TTYQ4AE EC EC 6.3.4.4 TTYQ4AE PD 1P9B TTYQ4AE SQ MNIFDHQIKNVDKGNVVAILGAQWGDEGKGKIIDMLSEYSDITCRFNGGANAGHTISVNDKKYALHLLPCGVLYDNNISVLGNGMVIHVKSLMEEIESVGGKLLDRLYLSNKAHILFDIHQIIDSIQETKKLKEGKQIGTTKRGIGPCYSTKASRIGIRLGTLKNFENFKNMYSKLIDHLMDLYNITEYDKEKELNLFYNYHIKLRDRIVDVISFMNTNLENNKKVLIEGANAAMLDIDFGTYPYVTSSCTTVGGVFSGLGIHHKKLNLVVGVVKSYLTRVGCGPFLTELNNDVGQYLREKGHEYGTTTKRPRRCGWLDIPMLLYVKCINSIDMINLTKLDVLSGLEEILLCVNFKNKKTGELLEKGCYPVEEEISEEYEPVYEKFSGWKEDISTCNEFDELPENAKKYILAIEKYLKTPIVWIGVGPNRKNMIVKKNFNLN TTYQ4AE TT Clinical trial TT68ZYJ ID TT68ZYJ TT68ZYJ TN Plasmodium Merozoite surface protein 1 (Malaria MSP-1) TT68ZYJ UP P04933 TT68ZYJ UC MSP1_PLAFW TT68ZYJ BC Merozoite surface protein TT68ZYJ SN p195; PMMSA; Merozoite surface protein 1; Merozoite surface antigens TT68ZYJ GN Malaria MSP-1 TT68ZYJ FC MSP-1 complex targets spectrin, a complex on the internal surface of the cell membrane of a red blood cell. The majority of the MSP-1 complex is shed upon entry into the red blood cell, but a small portion of the C-terminus, called MSP-119, is conserved. TT68ZYJ PD 2MUE; 2MU7; 2FLG; 1CEJ TT68ZYJ SQ MKIIFFLCSFLFFIINTQCVTHESYQELVKKLEALEDAVLTGYSLFQKEKMVLNEGTSGTAVTTSTPGSKGSVASGGSGGSVASGGSVASGGSVASGGSVASGGSGNSRRTNPSDNSSDSDAKSYADLKHRVRNYLLTIKELKYPQLFDLTNHMLTLCDNIHGFKYLIDGYEEINELLYKLNFYFDLLRAKLNDVCANDYCQIPFNLKIRANELDVLKKLVFGYRKPLDNIKDNVGKMEDYIKKNKKTIENINELIEESKKTIDKNKNATKEEEKKKLYQAQYDLSIYNKQLEEAHNLISVLEKRIDTLKKNENIKELLDKINEIKNPPPANSGNTPNTLLDKNKKIEEHEKEIKEIAKTIKFNIDSLFTDPLELEYYLREKNKNIDISAKVETKESTEPNEYPNGVTYPLSYNDINNALNELNSFGDLINPFDYTKEPSKNIYTDNERKKFINEIKEKIKIEKKKIESDKKSYEDRSKSLNDITKEYEKLLNEIYDSKFNNNIDLTNFEKMMGKRYSYKVEKLTHHNTFASYENSKHNLEKLTKALKYMEDYSLRNIVVEKELKYYKNLISKIENEIETLVENIKKDEEQLFEKKITKDENKPDEKILEVSDIVKVQVQKVLLMNKIDELKKTQLILKNVELKHNIHVPNSYKQENKQEPYYLIVLKKEIDKLKVFMPKVESLINEEKKNIKTEGQSDNSEPSTEGEITGQATTKPGQQAGSALEGDSVQAQAQEQKQAQPPVPVPVPEAKAQVPTPPAPVNNKTENVSKLDYLEKLYEFLNTSYICHKYILVSHSTMNEKILKQYKITKEEESKLSSCDPLDLLFNIQNNIPVMYSMFDSLNNSLSQLFMEIYEKEMVCNLYKLKDNDKIKNLLEEAKKVSTSVKTLSSSSMQPLSLTPQDKPEVSANDDTSHSTNLNNSLKLFENILSLGKNKNIYQELIGQKSSENFYEKILKDSDTFYNESFTNFVKSKADDINSLNDESKRKKLEEDINKLKKTLQLSFDLYNKYKLKLERLFDKKKTVGKYKMQIKKLTLLKEQLESKLNSLNNPKHVLQNFSVFFNKKKEAEIAETENTLENTKILLKHYKGLVKYYNGESSPLKTLSEESIQTEDNYASLENFKVLSKLEGKLKDNLNLEKKKLSYLSSGLHHLIAELKEVIKNKNYTGNSPSENNTDVNNALESYKKFLPEGTDVATVVSESGSDTLEQSQPKKPASTHVGAESNTITTSQNVDDEVDDVIIVPIFGESEEDYDDLGQVVTGEAVTPSVIDNILSKIENEYEVLYLKPLAGVYRSLKKQLENNVMTFNVNVKDILNSRFNKRENFKNVLESDLIPYKDLTSSNYVVKDPYKFLNKEKRDKFLSSYNYIKDSIDTDINFANDVLGYYKILSEKYKSDLDSIKKYINDKQGENEKYLPFLNNIETLYKTVNDKIDLFVIHLEAKVLNYTYEKSNVEVKIKELNYLKTIQDKLADFKKNNNFVGIADLSTDYNHNNLLTKFLSTGMVFENLAKTVLSNLLDGNLQGMLNISQHQCVKKQCPQNSGCFRHLDEREECKCLLNYKQEGDKCVENPNPTCNENNGGCDADAKCTEEDSGSNGKKITCECTKPDSYPLFDGIFCSSSNFLGISFLLILMLILYSFI TT68ZYJ TT Clinical trial TTBE4IR ID TTBE4IR TTBE4IR TN Plasmodium Oxoacyl-[acyl-carrier protein] reductase (Malaria fabG) TTBE4IR UP Q965D6 TTBE4IR UC Q965D6_PLAFA TTBE4IR BC Short-chain dehydrogenases reductase TTBE4IR SN 3-oxoacyl-acyl-carrier protein reductase TTBE4IR GN Malaria fabG TTBE4IR FC Participates in fatty acid biosynthesis and polyunsaturated fatty acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. TTBE4IR EC EC 1.1.1.100 TTBE4IR SQ MSVLHRFYLFFLFTKFFHCYKISYVLKNAKLAPNHAIKNINSLNLLSENKKENYYYCGENKVALVTGAGRGIGREIAKMLAKSVSHVICISRTQKSCDSVVDEIKSFGYESSGYAGDVSKKEEISEVINKILTEHKNVDILVSNAGITRDNLFLRMKNDEWEDVLRTNLNSLFYITQPISKRMINNRYGRIINISSIVGLTGNVGQANYSSSKAGVIGFTKSLAKELASRNITVNAIAPGFISSDMTDKISEQIKKNIISNIPAGRMGTPEEVANLACFLSSDKSGYINGRVFVIDGGLSP TTBE4IR TT Clinical trial TTTJUVZ ID TTTJUVZ TTTJUVZ TN Platelet glycoprotein VI (GP6) TTTJUVZ UP Q9HCN6 TTTJUVZ UC GPVI_HUMAN TTTJUVZ SN Glycoprotein 6; GPVI TTTJUVZ GN GP6 TTTJUVZ FC Collagen receptor involved in collagen-induced platelet adhesion and activation. Plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcR gamma-chain, the Src kinases (likely FYN or LYN) and SYK, the adapter protein LAT and leads to the activation of PLCG2. TTTJUVZ PD 5OU9; 5OU8; 5OU7; 2GI7 TTTJUVZ SQ MSPSPTALFCLGLCLGRVPAQSGPLPKPSLQALPSSLVPLEKPVTLRCQGPPGVDLYRLEKLSSSRYQDQAVLFIPAMKRSLAGRYRCSYQNGSLWSLPSDQLELVATGVFAKPSLSAQPGPAVSSGGDVTLQCQTRYGFDQFALYKEGDPAPYKNPERWYRASFPIITVTAAHSGTYRCYSFSSRDPYLWSAPSDPLELVVTGTSVTPSRLPTEPPSPVAEFSEATAELTVSFTNEVFTTETSRSITASPKESDSPAGPARQYYTKGNLVRICLGAVILIILAGFLAEDWHSRRKRLRHRGRAVQRPLPPLPPLPLTRKSNGGQDGGRQDVHSRGLCS TTTJUVZ TT Clinical trial TTTJUVZ KE hsa04512:ECM-receptor interaction; hsa04611:Platelet activation TTTJUVZ RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-75892:Platelet Adhesion to exposed collagen TTQA6SX ID TTQA6SX TTQA6SX TN Platelet-derived growth factor B (PDGFB) TTQA6SX UP P01127 TTQA6SX UC PDGFB_HUMAN TTQA6SX BC Growth factor TTQA6SX SN SIS; Protooncogene cSis; Proto-oncogene c-Sis; Plateletderived growth factor subunit B; Plateletderived growth factor beta polypeptide; Plateletderived growth factor B chain; Platelet-derived growth factor subunit B; Platelet-derived growth factor beta polypeptide; Platelet-derived growth factor B chain; PDGF2; PDGF-2; PDGF subunit B; Becaplermin TTQA6SX GN PDGFB TTQA6SX FC Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. TTQA6SX PD 4QCI; 4HQX; 4HQU; 3MJG; 1PDG TTQA6SX SQ MNRCWALFLSLCCYLRLVSAEGDPIPEELYEMLSDHSIRSFDDLQRLLHGDPGEEDGAELDLNMTRSHSGGELESLARGRRSLGSLTIAEPAMIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQLRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETVAAARPVTRSPGGSQEQRAKTPQTRVTIRTVRVRRPPKGKHRKFKHTHDKTALKETLGA TTQA6SX TT Clinical trial TTQA6SX FM Growth factor TTQA6SX KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04540:Gap junction; hsa04810:Regulation of actin cytoskeleton; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05231:Choline metabolism in cancer TTQA6SX RC R-HSA-114608:Platelet degranulation; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-5673001:RAF/MAP kinase cascade TTBPXMA ID TTBPXMA TTBPXMA TN Prolactin receptor (PRLR) TTBPXMA UP P16471 TTBPXMA UC PRLR_HUMAN TTBPXMA BC Cytokine receptor TTBPXMA SN PRL-R TTBPXMA GN PRLR TTBPXMA FC Acts as a prosurvival factor for spermatozoa by inhibiting sperm capacitation through suppression of SRC kinase activation and stimulation of AKT. Isoform 4 is unable to transduce prolactin signaling. Isoform 6 is unable to transduce prolactin signaling. This is a receptor for the anterior pituitary hormone prolactin (PRL). TTBPXMA PD 4I18; 3NCF; 3NCE; 3NCC; 3NCB TTBPXMA SQ MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGKQYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEWEIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIFPPVPGPKIKGFDAHLLEKGKSEELLSALGCQDFPPTSDYEDLLVEYLEVDDSEDQHLMSVHSKEHPSQGMKPTYLDPDTDSGRGSCDSPSLLSEKCEEPQANPSTFYDPEVIEKPENPETTHTWDPQCISMEGKIPYFHAGGSKCSTWPLPQPSQHNPRSSYHNITDVCELAVGPAGAPATLLNEAGKDALKSSQTIKSREEGKATQQREVESFHSETDQDTPWLLPQEKTPFGSAKPLDYVEIHKVNKDGALSLLPKQRENSGKPKKPGTPENNKEYAKVSGVMDNNILVLVPDPHAKNVACFEESAKEAPPSLEQNQAEKALANFTATSSKCRLQLGGLDYLDPACFTHSFH TTBPXMA TT Clinical trial TTBPXMA KE hsa04060:Cytokine-cytokine receptor interaction; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04917:Prolactin signaling pathway TTBPXMA RC R-HSA-1170546:Prolactin receptor signaling; R-HSA-982772:Growth hormone receptor signaling TTNH25W ID TTNH25W TTNH25W TN Prolyl 4-hydroxylasesubunit alpha-1 (P4HA1) TTNH25W UP P13674 TTNH25W UC P4HA1_HUMAN TTNH25W BC Paired donor oxygen oxidoreductase TTNH25W SN Prolyl 4-hydroxylase subunit alpha-1; Procollagenproline,2oxoglutarate4dioxygenase subunit alpha1; Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1; P4HA; 4PH alpha1; 4-PH alpha-1 TTNH25W GN P4HA1 TTNH25W FC Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. TTNH25W EC EC 1.14.11.2 TTNH25W PD 4BTB; 4BTA; 4BT9; 4BT8; 2YQ8 TTNH25W SQ MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE TTNH25W TT Clinical trial TTNH25W FM Oxidoreductases acting on paired donors TTG1QMU ID TTG1QMU TTG1QMU TN Prostaglandin E2 receptor EP1 (PTGER1) TTG1QMU UP P34995 TTG1QMU UC PE2R1_HUMAN TTG1QMU BC GPCR rhodopsin TTG1QMU SN Prostanoid EP1 receptor; Prostaglandin E2 receptor EP1 subtype; PGE2 receptor EP1 subtype; PGE receptor, EP1 subtype; PGE receptor EP1 subtype; EP1 receptor TTG1QMU GN PTGER1 TTG1QMU FC The activity of this receptor is mediated by G(q) proteins which activate a phosphatidylinositol-calcium second messenger system. May play a role as an important modulator of renal function. Implicated the smooth muscle contractile response to PGE2 in various tissues. Receptor for prostaglandin E2 (PGE2). TTG1QMU SQ MSPCGPLNLSLAGEATTCAAPWVPNTSAVPPSGASPALPIFSMTLGAVSNLLALALLAQAAGRLRRRRSAATFLLFVASLLATDLAGHVIPGALVLRLYTAGRAPAGGACHFLGGCMVFFGLCPLLLGCGMAVERCVGVTRPLLHAARVSVARARLALAAVAAVALAVALLPLARVGRYELQYPGTWCFIGLGPPGGWRQALLAGLFASLGLVALLAALVCNTLSGLALLRARWRRRSRRPPPASGPDSRRRWGAHGPRSASASSASSIASASTFFGGSRSSGSARRARAHDVEMVGQLVGIMVVSCICWSPMLVLVALAVGGWSSTSLQRPLFLAVRLASWNQILDPWVYILLRQAVLRQLLRLLPPRAGAKGGPAGLGLTPSAWEASSLRSSRHSGLSHF TTG1QMU TT Clinical trial TTG1QMU FM GPCR rhodopsin TTG1QMU KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa05200:Pathways in cancer TTG1QMU RC R-HSA-391908:Prostanoid ligand receptors; R-HSA-416476:G alpha (q) signalling events TTBRZQS ID TTBRZQS TTBRZQS TN Prostatic acid phosphatase (ACPP) TTBRZQS UP P15309 TTBRZQS UC PPAP_HUMAN TTBRZQS SN Thiamine monophosphatase; TMPase; PAP TTBRZQS GN ACPP TTBRZQS FC A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma. TTBRZQS EC EC 3.1.3.2 TTBRZQS PD 3PPD; 2MG0; 2L79; 2L77; 2L3H TTBRZQS SQ MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTTNSHQGTEDSTD TTBRZQS TT Clinical trial TTR1D7X ID TTR1D7X TTR1D7X TN Protein arginine methyltransferase 5 (PRMT5) TTR1D7X UP O14744 TTR1D7X UC ANM5_HUMAN TTR1D7X BC Methyltransferase TTR1D7X SN Shk1 kinase-binding protein 1 homolog; SKB1Hs; SKB1 homolog; SKB1; Protein arginine N-methyltransferase 5; Jak-binding protein 1; JBP1; IBP72; Histone-arginine N-methyltransferase PRMT5; HRMT1L5; 72 kDa ICln-binding protein TTR1D7X GN PRMT5 TTR1D7X FC Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation. Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter. Methylates GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner. Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression. Symmetrically methylates NCL. Methylates TP53; methylation might possibly affect TP53 target gene specificity. Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. TTR1D7X EC EC 2.1.1.320 TTR1D7X PD 6CKC; 5FA5; 5EMM; 5EML; 5EMK TTR1D7X SQ MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL TTR1D7X TT Clinical trial TT64I9Q ID TT64I9Q TT64I9Q TN Protein tyrosine phosphatase beta (PTPRB) TT64I9Q UP P23467 TT64I9Q UC PTPRB_HUMAN TT64I9Q BC Phosphoric monoester hydrolase TT64I9Q SN Vascular endothelial protein tyrosine phosphatase; VE-PTP; Receptor-type tyrosine-protein phosphatase beta; R-PTP-beta; PTPRB TT64I9Q GN PTPRB TT64I9Q FC Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin. TT64I9Q EC EC 3.1.3.48 TT64I9Q PD 2I5X; 2I4H; 2I4G; 2I4E; 2I3U TT64I9Q SQ MLSHGAGLALWITLSLLQTGLAEPERCNFTLAESKASSHSVSIQWRILGSPCNFSLIYSSDTLGAALCPTFRIDNTTYGCNLQDLQAGTIYNFRIISLDEERTVVLQTDPLPPARFGVSKEKTTSTSLHVWWTPSSGKVTSYEVQLFDENNQKIQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVSGGKRSFSVYTNGSTVPSPVKDIGISTKANSLLISWSHGSGNVERYRLMLMDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTVMTEAAGLQNYRWKLVRTAPMEVSNLKVTNDGSLTSLKVKWQRPPGNVDSYNITLSHKGTIKESRVLAPWITETHFKELVPGRLYQVTVSCVSGELSAQKMAVGRTFPDKVANLEANNNGRMRSLVVSWSPPAGDWEQYRILLFNDSVVLLNITVGKEETQYVMDDTGLVPGRQYEVEVIVESGNLKNSERCQGRTVPLAVLQLRVKHANETSLSIMWQTPVAEWEKYIISLADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGDLKNSSSVKGRTVPAQVTDLHVANQGMTSSLFTNWTQAQGDVEFYQVLLIHENVVIKNESISSETSRYSFHSLKSGSLYSVVVTTVSGGISSRQVVVEGRTVPSSVSGVTVNNSGRNDYLSVSWLLAPGDVDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGKYENHSFSQERTVPDKVQGVSVSNSARSDYLRVSWVHATGDFDHYEVTIKNKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSGQYEANEQGNGRTIPEPVKDLTLRNRSTEDLHVTWSGANGDVDQYEIQLLFNDMKVFPPFHLVNTATEYRFTSLTPGRQYKILVLTISGDVQQSAFIEGFTVPSAVKNIHISPNGATDSLTVNWTPGGGDVDSYTVSAFRHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSGSLKNQINVVGRTVPASVQGVIADNAYSSYSLIVSWQKAAGVAERYDILLLTENGILLRNTSEPATTKQHKFEDLTPGKKYKIQILTVSGGLFSKEAQTEGRTVPAAVTDLRITENSTRHLSFRWTASEGELSWYNIFLYNPDGNLQERAQVDPLVQSFSFQNLLQGRMYKMVIVTHSGELSNESFIFGRTVPASVSHLRGSNRNTTDSLWFNWSPASGDFDFYELILYNPNGTKKENWKDKDLTEWRFQGLVPGRKYVLWVVTHSGDLSNKVTAESRTAPSPPSLMSFADIANTSLAITWKGPPDWTDYNDFELQWLPRDALTVFNPYNNRKSEGRIVYGLRPGRSYQFNVKTVSGDSWKTYSKPIFGSVRTKPDKIQNLHCRPQNSTAIACSWIPPDSDFDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGMTSEVVEDSTITMIDRPPPPPPHIRVNEKDVLISKSSINFTVNCSWFSDTNGAVKYFTVVVREADGSDELKPEQQHPLPSYLEYRHNASIRVYQTNYFASKCAENPNSNSKSFNIKLGAEMESLGGKCDPTQQKFCDGPLKPHTAYRISIRAFTQLFDEDLKEFTKPLYSDTFFSLPITTESEPLFGAIEGVSAGLFLIGMLVAVVALLICRQKVSHGRERPSARLSIRRDRPLSVHLNLGQKGNRKTSCPIKINQFEGHFMKLQADSNYLLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLRARKLRSEQENPLFPIYENVNPEYHRDPVYSRH TT64I9Q TT Clinical trial TTOISYB ID TTOISYB TTOISYB TN Proto-oncogene Mas (MAS) TTOISYB UP P04201 TTOISYB UC MAS_HUMAN TTOISYB BC GPCR rhodopsin TTOISYB SN MGRA; MAS1 proto-oncogene, G protein-coupled receptor TTOISYB GN MAS1 TTOISYB FC Acts specifically as a functional antagonist of AGTR1 (angiotensin-2 type 1 receptor), although it up-regulates AGTR1 receptor levels. Positive regulation of AGTR1 levels occurs through activation of the G-proteins GNA11 and GNAQ, and stimulation of the protein kinase C signaling cascade. The antagonist effect on AGTR1 function is probably due to AGTR1 being physically altered by MAS1. Receptor for angiotensin 1-7. TTOISYB SQ MDGSNVTSFVVEEPTNISTGRNASVGNAHRQIPIVHWVIMSISPVGFVENGILLWFLCFRMRRNPFTVYITHLSIADISLLFCIFILSIDYALDYELSSGHYYTIVTLSVTFLFGYNTGLYLLTAISVERCLSVLYPIWYRCHRPKYQSALVCALLWALSCLVTTMEYVMCIDREEESHSRNDCRAVIIFIAILSFLVFTPLMLVSSTILVVKIRKNTWASHSSKLYIVIMVTIIIFLIFAMPMRLLYLLYYEYWSTFGNLHHISLLFSTINSSANPFIYFFVGSSKKKRFKESLKVVLTRAFKDEMQPRRQKDNCNTVTVETVV TTOISYB TT Clinical trial TTOISYB KE hsa04080:Neuroactive ligand-receptor interaction; hsa04614:Renin-angiotensin system TT4LOT8 ID TT4LOT8 TT4LOT8 TN Pyruvate kinase M2 (PKM) TT4LOT8 UP P14618 TT4LOT8 UC KPYM_HUMAN TT4LOT8 BC Kinase TT4LOT8 SN p58; Tumor M2-PK; Thyroid hormone-binding protein 1; THBP1; Pyruvate kinase muscle isozyme; Pyruvate kinase isozymes M1/M2; Pyruvate kinase PKM; Pyruvate kinase 2/3; PKM2; PK3; PK2; Opa-interacting protein 3; OIP3; OIP-3; Cytosolic thyroid hormone-binding protein; CTHBP TT4LOT8 GN PKM TT4LOT8 FC Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival. Promotes in a STAT1-dependent manner, the expression of the immune checkpoint protein CD274 in ARNTL/BMAL1-deficient macrophages. Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. TT4LOT8 EC EC 2.7.1.40 TT4LOT8 PD 6GG6; 6GG5; 6GG4; 6B6U; 5X1W TT4LOT8 SQ MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP TT4LOT8 TT Clinical trial TT4LOT8 FM Kinase TTAIQSN ID TTAIQSN TTAIQSN TN Receptor-interacting protein 1 (RIPK1) TTAIQSN UP Q13546 TTAIQSN UC RIPK1_HUMAN TTAIQSN BC Kinase TTAIQSN SN Receptor-interacting serine/threonine-protein kinase 1; RIP1; RIP-1; RIP; Cell death protein RIP TTAIQSN GN RIPK1 TTAIQSN FC Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necrosis-inducing complex. Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. TTAIQSN EC EC 2.7.11.1 TTAIQSN PD 6R5F; 6OCQ; 6NW2; 6HHO; 6C4D TTAIQSN SQ MQPDMSLNVIKMKSSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLEESVEEDVKSLKKEYSNENAVVKRMQSLQLDCVAVPSSRSNSATEQPGSLHSSQGLGMGPVEESWFAPSLEHPQEENEPSLQSKLQDEANYHLYGSRMDRQTKQQPRQNVAYNREEERRRRVSHDPFAQQRPYENFQNTEGKGTAYSSAASHGNAVHQPSGLTSQPQVLYQNNGLYSSHGFGTRPLDPGTAGPRVWYRPIPSHMPSLHNIPVPETNYLGNTPTMPFSSLPPTDESIKYTIYNSTGIQIGAYNYMEIGGTSSSLLDSTNTNFKEEPAAKYQAIFDNTTSLTDKHLDPIRENLGKHWKNCARKLGFTQSQIDEIDHDYERDGLKEKVYQMLQKWVMREGIKGATVGKLAQALHQCSRIDLLSSLIYVSQN TTAIQSN TT Clinical trial TTTHMQJ ID TTTHMQJ TTTHMQJ TN Renal carcinoma antigen NY-REN-56 (PFKFB3) TTTHMQJ UP Q16875 TTTHMQJ UC F263_HUMAN TTTHMQJ BC Kinase TTTHMQJ SN iPFK2; Renal carcinoma antigen NYREN56; PFKFB3; Fructose2,6bisphosphatase; 6phosphofructo2kinase/fructose2,6bisphosphatase 3; 6PF2K/Fru2,6P2ase brain/placentatype isozyme; 6PF2K/Fru2,6P2ase 3 TTTHMQJ GN PFKFB3 TTTHMQJ FC Synthesis and degradation of fructose 2,6-bisphosphate. TTTHMQJ PD 6IC0; 6IBZ; 6IBY; 6IBX; 6HVJ TTTHMQJ SQ MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH TTTHMQJ TT Clinical trial TTTHMQJ KE hsa00051:Fructose and mannose metabolism; hsa04066:HIF-1 signaling pathway; hsa04152:AMPK signaling pathway TTTHMQJ RC R-HSA-70171:Glycolysis TTURJV4 ID TTURJV4 TTURJV4 TN Repulsive guidance molecule A (RGMA) TTURJV4 UP Q96B86 TTURJV4 UC RGMA_HUMAN TTURJV4 BC Repulsive guidance molecule (RGM) family TTURJV4 SN RGM domain family member A TTURJV4 GN RGMA TTURJV4 FC Member of the repulsive guidance molecule (RGM) family that performs several functions in the developing and adult nervous system. Regulates cephalic neural tube closure, inhibits neurite outgrowth and cortical neuron branching, and the formation of mature synapses. Binding to its receptor NEO1/neogenin induces activation of RHOA-ROCK1/Rho-kinase signaling pathway through UNC5B-ARHGEF12/LARG-PTK2/FAK1 cascade, leading to collapse of the neuronal growth cone and neurite outgrowth inhibition. Furthermore, RGMA binding to NEO1/neogenin leads to HRAS inactivation by influencing HRAS-PTK2/FAK1-AKT1 pathway. It also functions as a bone morphogenetic protein (BMP) coreceptor that may signal through SMAD1, SMAD5, and SMAD8. TTURJV4 PD 4UHY TTURJV4 SQ MQPPRERLVVTGRAGWMGMGRGAGRSALGFWPTLAFLLCSFPAATSPCKILKCNSEFWSATSGSHAPASDDTPEFCAALRSYALCTRRTARTCRGDLAYHSAVHGIEDLMSQHNCSKDGPTSQPRLRTLPPAGDSQERSDSPEICHYEKSFHKHSATPNYTHCGLFGDPHLRTFTDRFQTCKVQGAWPLIDNNYLNVQVTNTPVLPGSAATATSKLTIIFKNFQECVDQKVYQAEMDELPAAFVDGSKNGGDKHGANSLKITEKVSGQHVEIQAKYIGTTIVVRQVGRYLTFAVRMPEEVVNAVEDWDSQGLYLCLRGCPLNQQIDFQAFHTNAEGTGARRLAAASPAPTAPETFPYETAVAKCKEKLPVEDLYYQACVFDLLTTGDVNFTLAAYYALEDVKMLHSNKDKLHLYDRTRDLPGRAAAGLPLAPRPLLGALVPLLALLPVFC TTURJV4 TT Clinical trial TTURJV4 KE hsa04350:TGF-beta signaling pathway; hsa04360:Axon guidance TTBOH16 ID TTBOH16 TTBOH16 TN Retinal pigment epithelium protein (RPE65) TTBOH16 UP Q16518 TTBOH16 UC RPE65_HUMAN TTBOH16 BC Carboxylic ester hydrolase TTBOH16 SN Retinol isomerase; Retinoid isomerohydrolase; Retinal pigment epithelium-specific 65 kDa protein; Meso-zeaxanthin isomerase; Lutein isomerase; All-trans-retinyl-palmitate hydrolase TTBOH16 GN RPE65 TTBOH16 FC Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore. Essential for the production of 11-cis retinal for both rod and cone photoreceptors. Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT (By similarity). TTBOH16 EC EC 3.1.1.64 TTBOH16 SQ MSIQVEHPAGGYKKLFETVEELSSPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEVTDNALVNVYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAHPHIENDGTVYNIGNCFGKNFSIAYNIVKIPPLQADKEDPISKSEIVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLFKFLSSWSLWGANYMDCFESNETMGVWLHIADKKRKKYLNNKYRTSPFNLFHHINTYEDNGFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKKNARKAPQPEVRRYVLPLNIDKADTGKNLVTLPNTTATAILCSDETIWLEPEVLFSGPRQAFEFPQINYQKYCGKPYTYAYGLGLNHFVPDRLCKLNVKTKETWVWQEPDSYPSEPIFVSHPDALEEDDGVVLSVVVSPGAGQKPAYLLILNAKDLSEVARAEVEINIPVTFHGLFKKS TTBOH16 TT Clinical trial TTBOH16 KE hsa00830:Retinol metabolism TTBOH16 RC R-HSA-2453902:The canonical retinoid cycle in rods (twilight vision) TTD91BL ID TTD91BL TTD91BL TN RING finger protein 43 (RNF43) TTD91BL UP Q68DV7 TTD91BL UC RNF43_HUMAN TTD91BL SN RING-type E3 ubiquitin transferase RNF43; E3 ubiquitin-protein ligase RNF43 TTD91BL GN RNF43 TTD91BL FC E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway. Along with RSPO2 and ZNRF3, constitutes a master switch that governs limb specification (By similarity). TTD91BL EC EC 2.3.2.27 TTD91BL PD 4KNG TTD91BL SQ MSGGHQLQLAALWPWLLMATLQAGFGRTGLVLAAAVESERSAEQKAIIRVIPLKMDPTGKLNLTLEGVFAGVAEITPAEGKLMQSHPLYLCNASDDDNLEPGFISIVKLESPRRAPRPCLSLASKARMAGERGASAVLFDITEDRAAAEQLQQPLGLTWPVVLIWGNDAEKLMEFVYKNQKAHVRIELKEPPAWPDYDVWILMTVVGTIFVIILASVLRIRCRPRHSRPDPLQQRTAWAISQLATRRYQASCRQARGEWPDSGSSCSSAPVCAICLEEFSEGQELRVISCLHEFHRNCVDPWLHQHRTCPLCMFNITEGDSFSQSLGPSRSYQEPGRRLHLIRQHPGHAHYHLPAAYLLGPSRSAVARPPRPGPFLPSQEPGMGPRHHRFPRAAHPRAPGEQQRLAGAQHPYAQGWGLSHLQSTSQHPAACPVPLRRARPPDSSGSGESYCTERSGYLADGPASDSSSGPCHGSSSDSVVNCTDISLQGVHGSSSTFCSSLSSDFDPLVYCSPKGDPQRVDMQPSVTSRPRSLDSVVPTGETQVSSHVHYHRHRHHHYKKRFQWHGRKPGPETGVPQSRPPIPRTQPQPEPPSPDQQVTRSNSAAPSGRLSNPQCPRALPEPAPGPVDASSICPSTSSLFNLQKSSLSARHPQRKRRGGPSEPTPGSRPQDATVHPACQIFPHYTPSVAYPWSPEAHPLICGPPGLDKRLLPETPGPCYSNSQPVWLCLTPRQPLEPHPPGEGPSEWSSDTAEGRPCPYPHCQVLSAQPGSEEELEELCEQAV TTD91BL TT Clinical trial TTI9HL4 ID TTI9HL4 TTI9HL4 TN Roof plate-specific spondin-1 (RSPO1) TTI9HL4 UP Q2MKA7 TTI9HL4 UC RSPO1_HUMAN TTI9HL4 SN hRspo1; R-spondin-1 TTI9HL4 GN RSPO1 TTI9HL4 FC Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Has a essential roles in ovary determination. Regulates Wnt signaling by antagonizing DKK1/KREM1-mediated internalization of LRP6 through an interaction with KREM1. Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. TTI9HL4 PD 4QXF; 4LI2; 4KT1; 4KNG; 4CDK TTI9HL4 SQ MRLGLCVVALVLSWTHLTISSRGIKGKRQRRISAEGSQACAKGCELCSEVNGCLKCSPKLFILLERNDIRQVGVCLPSCPPGYFDARNPDMNKCIKCKIEHCEACFSHNFCTKCKEGLYLHKGRCYPACPEGSSAANGTMECSSPAQCEMSEWSPWGPCSKKQQLCGFRRGSEERTRRVLHAPVGDHAACSDTKETRRCTVRRVPCPEGQKRRKGGQGRRENANRNLARKESKEAGAGSRRRKGQQQQQQQGTVGPLTSAGPA TTI9HL4 TT Clinical trial TTI9HL4 RC R-HSA-4641263:Regulation of FZD by ubiquitination TTYRO4F ID TTYRO4F TTYRO4F TN Sclerostin (SOST) TTYRO4F UP Q9BQB4 TTYRO4F UC SOST_HUMAN TTYRO4F SN UNQ2976/PRO7455/PRO7476 TTYRO4F GN SOST TTYRO4F FC Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation. TTYRO4F PD 3SOV; 2K8P TTYRO4F SQ MQLPLALCLVCLLVHTAFRVVEGQGWQAFKNDATEIIPELGEYPEPPPELENNKTMNRAENGGRPPHHPFETKDVSEYSCRELHFTRYVTDGPCRSAKPVTELVCSGQCGPARLLPNAIGRGKWWRPSGPDFRCIPDRYRAQRVQLLCPGGEAPRARKVRLVASCKCKRLTRFHNQSELKDFGTEAARPQKGRKPRPRARSAKANQAELENAY TTYRO4F TT Successful TTYRO4F KE hsa04310:Wnt signaling pathway TTYRO4F RC R-HSA-201681:TCF dependent signaling in response to WNT; R-HSA-3772470:Negative regulation of TCF-dependent signaling by WNT ligand antagonists TT5UT28 ID TT5UT28 TT5UT28 TN Semaphorin-4D (SEMA4D) TT5UT28 UP Q92854 TT5UT28 UC SEM4D_HUMAN TT5UT28 SN SEMAJ; GR3; CD100; C9orf164; BB18; A8 TT5UT28 GN SEMA4D TT5UT28 FC Regulates GABAergic synapse development. Promotes the development of inhibitory synapses in a PLXNB1-dependent manner. Modulates the complexity and arborization of developing neurites in hippocampal neurons by activating PLXNB1 and interaction with PLXNB1 mediates activation of RHOA. Promotes the migration of cerebellar granule cells. Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro). Induces endothelial cell migration through the activation of PTK2B/PYK2, SRC, and the phosphatidylinositol 3-kinase-AKT pathway. Cell surface receptor for PLXNB1 and PLXNB2 that plays an important role in cell-cell signaling. TT5UT28 PD 3OL2; 1OLZ TT5UT28 SQ MRMCTPIRGLLMALAVMFGTAMAFAPIPRITWEHREVHLVQFHEPDIYNYSALLLSEDKDTLYIGAREAVFAVNALNISEKQHEVYWKVSEDKKAKCAEKGKSKQTECLNYIRVLQPLSATSLYVCGTNAFQPACDHLNLTSFKFLGKNEDGKGRCPFDPAHSYTSVMVDGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSFVFADVIRKSPDSPDGEDDRVYFFFTEVSVEYEFVFRVLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSRPDSGLVFNVLRDVFVLRSPGLKVPVFYALFTPQLNNVGLSAVCAYNLSTAEEVFSHGKYMQSTTVEQSHTKWVRYNGPVPKPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIDNRPRLIKKDVNYTQIVVDRTQALDGTVYDVMFVSTDRGALHKAISLEHAVHIIEETQLFQDFEPVQTLLLSSKKGNRFVYAGSNSGVVQAPLAFCGKHGTCEDCVLARDPYCAWSPPTATCVALHQTESPSRGLIQEMSGDASVCPDKSKGSYRQHFFKHGGTAELKCSQKSNLARVFWKFQNGVLKAESPKYGLMGRKNLLIFNLSEGDSGVYQCLSEERVKNKTVFQVVAKHVLEVKVVPKPVVAPTLSVVQTEGSRIATKVLVASTQGSSPPTPAVQATSSGAITLPPKPAPTGTSCEPKIVINTVPQLHSEKTMYLKSSDNRLLMSLFLFFFVLFLCLFFYNCYKGYLPRQCLKFRSALLIGKKKPKSDFCDREQSLKETLVEPGSFSQQNGEHPKPALDTGYETEQDTITSKVPTDREDSQRIDDLSARDKPFDVKCELKFADSDADGD TT5UT28 TT Clinical trial TT5UT28 FM Semaphorin TT5UT28 KE hsa04360:Axon guidance TT5UT28 RC R-HSA-416550:Sema4D mediated inhibition of cell attachment and migration; R-HSA-416572:Sema4D induced cell migration and growth-cone collapse; R-HSA-416700:Other semaphorin interactions TT0J32Z ID TT0J32Z TT0J32Z TN Smad7 messenger RNA (Smad7 mRNA) TT0J32Z UP O15105 TT0J32Z UC SMAD7_HUMAN TT0J32Z BC mRNA target TT0J32Z SN hSMAD7 (mRNA); Smad7 (mRNA); SMAD family member 7 (mRNA); SMAD 7 (mRNA); Mothers against decapentaplegic homolog 8 (mRNA); Mothers against decapentaplegic homolog 7 (mRNA); Mothers against DPP homolog 8 (mRNA); Mothers against DPP homolog 7 (mRNA); MADH8 (mRNA); MADH7 (mRNA); MAD homolog 8 (mRNA); MAD homolog 7 (mRNA) TT0J32Z GN SMAD7 TT0J32Z FC Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. TT0J32Z PD 2LTZ; 2LTY; 2LTX; 2LTW; 2LTV TT0J32Z SQ MFRTKRSALVRRLWRSRAPGGEDEEEGAGGGGGGGELRGEGATDSRAHGAGGGGPGRAGCCLGKAVRGAKGHHHPHPPAAGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPAGAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR TT0J32Z TT Clinical trial TT0J32Z FM mRNA target TT0J32Z KE hsa04144:Endocytosis; hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway TT0J32Z RC R-HSA-2173796:SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription TTT3YKH ID TTT3YKH TTT3YKH TN Somatotropin (GH1) TTT3YKH UP P01241 TTT3YKH UC SOMA_HUMAN TTT3YKH BC Somatotropin/prolactin TTT3YKH SN Pituitary growth hormone; Growth hormone 1; Growth hormone; GH-N; GH TTT3YKH GN GH1 TTT3YKH FC Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. TTT3YKH PD 3HHR; 1KF9; 1HWH; 1HWG; 1HUW TTT3YKH SQ MATGSRTSLLLAFGLLCLPWLQEGSAFPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF TTT3YKH TT Clinical trial TTT3YKH FM Somatotropin hormone family TTT3YKH KE hsa04060:Cytokine-cytokine receptor interaction; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway TTT3YKH RC R-HSA-1170546:Prolactin receptor signaling; R-HSA-982772:Growth hormone receptor signaling TTDZCKV ID TTDZCKV TTDZCKV TN Sphingosine-1-phosphate receptor 5 (S1PR5) TTDZCKV UP Q9H228 TTDZCKV UC S1PR5_HUMAN TTDZCKV BC GPCR rhodopsin TTDZCKV SN Sphingosine 1-phosphate receptor Edg-8; S1PR5; S1P5; S1P receptor Edg-8; S1P receptor 5; Endothelial differentiation G-protein-coupled receptor 8 TTDZCKV GN S1PR5 TTDZCKV FC Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Is coupled to both the G(i/0)alpha and G(12) subclass of heteromeric G-proteins. May play a regulatory role in the transformation of radial glial cells into astrocytes and may affect proliferative activity of these cells. TTDZCKV SQ MESGLLRPAPVSEVIVLHYNYTGKLRGARYQPGAGLRADAVVCLAVCAFIVLENLAVLLVLGRHPRFHAPMFLLLGSLTLSDLLAGAAYAANILLSGPLTLKLSPALWFAREGGVFVALTASVLSLLAIALERSLTMARRGPAPVSSRGRTLAMAAAAWGVSLLLGLLPALGWNCLGRLDACSTVLPLYAKAYVLFCVLAFVGILAAICALYARIYCQVRANARRLPARPGTAGTTSTRARRKPRSLALLRTLSVVLLAFVACWGPLFLLLLLDVACPARTCPVLLQADPFLGLAMANSLLNPIIYTLTNRDLRHALLRLVCCGRHSCGRDPSGSQQSASAAEASGGLRRCLPPGLDGSFSGSERSSPQRDGLDTSGSTGSPGAPTAARTLVSEPAAD TTDZCKV TT Clinical trial TTDZCKV KE hsa04071:Sphingolipid signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTDZCKV RC R-HSA-418594:G alpha (i) signalling events; R-HSA-419408:Lysosphingolipid and LPA receptors TT5FLYB ID TT5FLYB TT5FLYB TN Staphylococcus Alpha-hemolysin (Stap-coc hly) TT5FLYB UP P09616 TT5FLYB UC HLA_STAAU TT5FLYB BC Alpha-hemolysin channel-forming toxin TT5FLYB SN hla; Alpha-toxin; Alpha-hemolysin; Alpha-HL TT5FLYB GN Stap-coc hly TT5FLYB FC Alpha-toxin binds to the membrane of eukaryotic cells (particularly red blood cells, RBC) forming pores, resulting in hemolysis, with the release of low-molecular weight molecules leading to eventual osmotic RBC lysis. Human RBCs bind much less alpha-toxin than do rabbit RBCs. Heptamer oligomerization and pore formation is required for lytic activity. TT5FLYB PD 7AHL; 4YHD; 4IDJ; 3M4E; 3M4D TT5FLYB SQ MKTRIVSSVTTTLLLGSILMNPVAGAADSDINIKTGTTDIGSNTTVKTGDLVTYDKENGMHKKVFYSFIDDKNHNKKLLVIRTKGTIAGQYRVYSEEGANKSGLAWPSAFKVQLQLPDNEVAQISDYYPRNSIDTKEYMSTLTYGFNGNVTGDDTGKIGGLIGANVSIGHTLKYVQPDFKTILESPTDKKVGWKVIFNNMVNQNWGPYDRDSWNPVYGNQLFMKTRNGSMKAADNFLDPNKASSLLSSGFSPDFATVITMDRKASKQQTNIDVIYERVRDDYQLHWTSTNWKGTNTKDKWTDRSSERYKIDWEKEEMTN TT5FLYB TT Clinical trial TT5FLYB RC R-HSA-844456:The NLRP3 inflammasome TTZBRVL ID TTZBRVL TTZBRVL TN Staphylococcus Enoyl ACP reductase (Stap-coc fabI) TTZBRVL UP Q2FZQ3 TTZBRVL UC FABI_STAA8 TTZBRVL BC Short-chain dehydrogenases reductase TTZBRVL SN NADPHdependent enoylACP reductase; Enoyl[acylcarrierprotein] reductase [NADPH] FabI TTZBRVL GN Stap-coc fabI TTZBRVL FC Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It has a preference for a long chain (C12) substrate compared to the shorter (C4) acyl group. Involved in the elongation cycle of fatty acid which are used in the lipid metabolism. TTZBRVL SQ MLNLENKTYVIMGIANKRSIAFGVAKVLDQLGAKLVFTYRKERSRKELEKLLEQLNQPEAHLYQIDVQSDEEVINGFEQIGKDVGNIDGVYHSIAFANMEDLRGRFSETSREGFLLAQDISSYSLTIVAHEAKKLMPEGGSIVATTYLGGEFAVQNYNVMGVAKASLEANVKYLALDLGPDNIRVNAISASPIRTLSAKGVGGFNTILKEIEERAPLKRNVDQVEVGKTAAYLLSDLSSGVTGENIHVDSGFHAIK TTZBRVL TT Clinical trial TTZBRVL KE sao00061:Fatty acid biosynthesis; sao00780:Biotin metabolism; sao01100:Metabolic pathways; sao01212:Fatty acid metabolism TTICO5G ID TTICO5G TTICO5G TN Staphylococcus Peptide deformylase (Stap-coc def) TTICO5G UP P68826 TTICO5G UC DEF_STAAU TTICO5G BC Carbon-nitrogen hydrolase TTICO5G SN def; Stap-coc Polypeptide deformylase TTICO5G GN Stap-coc def TTICO5G FC Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. TTICO5G PD 2AI9; 1Q1Y; 1LQW; 1LMH; 1LM4 TTICO5G SQ MLTMKDIIRDGHPTLRQKAAELELPLTKEEKETLIAMREFLVNSQDEEIAKRYGLRSGVGLAAPQINISKRMIAVLIPDDGSGKSYDYMLVNPKIVSHSVQEAYLPTGEGCLSVDDNVAGLVHRHNRITIKAKDIEGNDIQLRLKGYPAIVFQHEIDHLNGVMFYDHIDKNHPLQPHTDAVEV TTICO5G TT Clinical trial TTHJT3X ID TTHJT3X TTHJT3X TN STAT3 messenger RNA (STAT3 mRNA) TTHJT3X UP P40763 TTHJT3X UC STAT3_HUMAN TTHJT3X BC mRNA target TTHJT3X SN Transcription factor STAT3 (mRNA); Stat3 (mRNA); Signal transducer and activator of transcription 3 (mRNA); Acute-phase response factor (mRNA); APRF (mRNA) TTHJT3X GN STAT3 TTHJT3X FC Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity. Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1. Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation. May play an apoptotic role by transctivating BIRC5 expression under LEP activation. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion. Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. TTHJT3X PD 5U5S; 5AX3 TTHJT3X SQ MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMELTSECATSPM TTHJT3X TT Clinical trial TTHJT3X FM mRNA target TTHJT3X KE hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04630:Jak-STAT signaling pathway; hsa04917:Prolactin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa05145:Toxoplasmosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05221:Acute myeloid leukemia; hsa05321:Inflammatory bowel disease (IBD) TTHJT3X RC R-HSA-1059683:Interleukin-6 signaling; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-2892247:POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation; R-HSA-452723:Transcriptional regulation of pluripotent stem cells; R-HSA-982772:Growth hormone receptor signaling TTT402Y ID TTT402Y TTT402Y TN Stimulator of interferon genes protein (TMEM173) TTT402Y UP Q86WV6 TTT402Y UC STING_HUMAN TTT402Y BC TMEM173 family TTT402Y SN Mediator of IRF3 activation; Endoplasmic reticulum interferon stimulator; ERIS TTT402Y GN TMEM173 TTT402Y FC Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by recognizing and binding cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced in response to DNA virus in the cytosol: upon binding of c-di-GMP or cGAMP, autoinhibition is alleviated and TMEM173/STING is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons. May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II). Mediates death signaling via activation of the extracellular signal-regulated kinase (ERK) pathway. Essential for the induction of IFN-beta in response to human herpes simplex virus 1 (HHV-1) infection. Exhibits 2',3' phosphodiester linkage-specific ligand recognition. Can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:26300263). TTT402Y PD 6O8C; 6O8B; 6NT5; 6MXE; 6MX3 TTT402Y SQ MPHSSLHPSIPCPRGHGAQKAALVLLSACLVTLWGLGEPPEHTLRYLVLHLASLQLGLLLNGVCSLAEELRHIHSRYRGSYWRTVRACLGCPLRRGALLLLSIYFYYSLPNAVGPPFTWMLALLGLSQALNILLGLKGLAPAEISAVCEKGNFNVAHGLAWSYYIGYLRLILPELQARIRTYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLSMADPNIRFLDKLPQQTGDHAGIKDRVYSNSIYELLENGQRAGTCVLEYATPLQTLFAMSQYSQAGFSREDRLEQAKLFCRTLEDILADAPESQNNCRLIAYQEPADDSSFSLSQEVLRHLRQEEKEEVTVGSLKTSAVPSTSTMSQEPELLISGMEKPLPLRTDFS TTT402Y TT Clinical trial TTT402Y KE hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa05163:Human cytomegalovirus infection; hsa05168:Herpes simplex virus 1 infection; hsa05170:Human immunodeficiency virus 1 infection TTOJ46K ID TTOJ46K TTOJ46K TN Streptococcus Methionyl-tRNA synthetase (Stre-coc metG) TTOJ46K UP Q9A178 TTOJ46K UC SYM_STRP1 TTOJ46K BC Carbon-oxygen ligase TTOJ46K SN metG; Methionyl-transferribonucleic acid synthetase; Methionyl-transferribonucleate synthetase; Methionyl-transferRNA synthetase; Methionyl t-RNA synthetase; Methionine-tRNA ligase; Methionine--tRNA ligase; Methionine translase; MetRS; MRS TTOJ46K GN Stre-coc metG TTOJ46K FC Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. TTOJ46K EC EC 6.1.1.10 TTOJ46K SQ MKKPFYITTPIYYPSGKLHIGSAYTTIACDVLARYKRLMGHEVFYLTGLDEHGQKIQTKAKEAGITPQTYVDNMAKDVKALWQLLDISYDTFIRTTDDYHEEVVAAVFEKLLAQDDIYLGEYSGWYSVSDEEFFTESQLKEVFRDEDGQVIGGIAPSGHEVEWVSEESYFLRLSKYDDRLVAFFKERPDFIQPDGRMNEMVKNFIEPGLEDLAVSRTTFTWGVPVPSDPKHVVYVWIDALLNYATALGYRQANHANFDKFWNGTVFHMVGKDILRFHSIYWPILLMMLDLPMPDRLIAHGWFVMKDGKMSKSKGNVVYPEMLVERFGLDPLRYYLMRSLPVGSDGTFTPEDYVGRINYELANDLGNLLNRTVAMINKYFDGTVPAYVDNGTAFDADLSQLIDAQLADYHKHMEAVDYPRALEAVWTIIARTNKYIDETAPWVLAKEDGDKAQLASVMAHLAASLRLVAHVIQPFMMETSAAIMAQLGLEPVSDLSTLALADFPANTKVVAKGTPIFPRLDMEAEIDYIKAQMGDSSAISQEKEWVPEEVALKSEKDVITFETFDAVEIRVAEVKEVSKVEGSEKLLRFRVDAGDGQDRQILSGIAKFYPNEQELVGKKLQIVANLKPRKMMKKYISQGMILSAEHGDQLTVLTVDSSVPNGSIIG TTOJ46K TT Clinical trial TTOJ46K KE spy00450:Selenocompound metabolism; spy00970:Aminoacyl-tRNA biosynthesis TT4UGTF ID TT4UGTF TT4UGTF TN Stromal cell-derived factor 1 (CXCL12) TT4UGTF UP P48061 TT4UGTF UC SDF1_HUMAN TT4UGTF BC Cytokine: CXC chemokine TT4UGTF SN hSDF-1; SDF1B; SDF1A; SDF1; SDF-1; Pre-B cell growth-stimulating factor; Pre-B cell growth stimulating factor; PBSF; Intercrine reduced in hepatomas; IRH; HIRH; C-X-C motif chemokine 12 TT4UGTF GN CXCL12 TT4UGTF FC Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. Binds to the allosteric site (site 2) of integrins and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 in a CXCR4-independent manner. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation. Stimulates the proliferation of bone marrow-derived B-cell progenitors in the presence of IL7 as well as growth of stromal cell-dependent pre-B-cells. Chemoattractant active on T-lymphocytes and monocytes but not neutrophils. TT4UGTF PD 4UAI; 4LMQ; 3HP3; 3GV3; 2SDF TT4UGTF SQ MNAKVVVVLVLVLTALCLSDGKPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWIQEYLEKALNKRFKM TT4UGTF TT Clinical trial TT4UGTF FM Cytokine: CXC chemokine TT4UGTF KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04360:Axon guidance; hsa04670:Leukocyte transendothelial migration; hsa04672:Intestinal immune network for IgA production; hsa05200:Pathways in cancer; hsa05323:Rheumatoid arthritis TT4UGTF RC R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTDO1MV ID TTDO1MV TTDO1MV TN T-cell activation antigen CD27 (CD27) TTDO1MV UP P26842 TTDO1MV UC CD27_HUMAN TTDO1MV BC Cytokine receptor TTDO1MV SN Tumor necrosis factor receptor superfamily member 7; Tcell activation antigen CD27; TNFRSF7; T14; CD27L receptor; CD27 antigen TTDO1MV GN CD27 TTDO1MV FC May play a role in survival of activated T-cells. May play a role in apoptosis through association with SIVA1. Receptor for CD70/CD27L. TTDO1MV PD 5TLK; 5TLJ; 5TL5 TTDO1MV SQ MARPHPWWLCVLGTLVGLSATPAPKSCPERHYWAQGKLCCQMCEPGTFLVKDCDQHRKAAQCDPCIPGVSFSPDHHTRPHCESCRHCNSGLLVRNCTITANAECACRNGWQCRDKECTECDPLPNPSLTARSSQALSPHPQPTHLPYVSEMLEARTAGHMQTLADFRQLPARTLSTHWPPQRSLCSSDFIRILVIFSGMFLVFTLAGALFLHQRRKYRSNKGESPVEPAEPCHYSCPREEEGSTIPIQEDYRKPEPACSP TTDO1MV TT Clinical trial TTDO1MV FM Cytokine receptor TTDO1MV KE hsa04060:Cytokine-cytokine receptor interaction TTDO1MV RC R-HSA-5669034:TNFs bind their physiological receptors TT9DWLC ID TT9DWLC TT9DWLC TN T-cell-specific protein RANTES (CCL5) TT9DWLC UP P13501 TT9DWLC UC CCL5_HUMAN TT9DWLC BC Cytokine: CC chemokine TT9DWLC SN Tcellspecific protein RANTES; TCP228; T cellspecific protein P228; T cell-specific protein P228; Smallinducible cytokine A5; Small-inducible cytokine A5; SISdelta; SIS-delta; SCYA5; RANTES(468); Eosinophil chemotactic cytokine; EoCP; D17S136E; CC motif chemokine 5; C-C motif chemokine 5 TT9DWLC GN CCL5 TT9DWLC FC Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1-infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1-68) and RANTES(3-68) and is generated by an unidentified enzyme associated with monocytes and neutrophils. May also be an agonist of the G protein-coupled receptor GPR75, stimulating inositol trisphosphate production and calcium mobilization through its activation. Together with GPR75, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. By activating GPR75 may also play a role in insulin secretion by islet cells. Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. TT9DWLC PD 6FGP; 6C6D; 5UIW; 5L2U; 5DNF TT9DWLC SQ MKVSAAALAVILIATALCAPASASPYSSDTTPCCFAYIARPLPRAHIKEYFYTSGKCSNPAVVFVTRKNRQVCANPEKKWVREYINSLEMS TT9DWLC TT Clinical trial TT9DWLC FM Cytokine: CC chemokine TT9DWLC KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04668:TNF signaling pathway; hsa05020:Prion diseases; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05142:Chagas disease (American trypanosomiasis); hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05323:Rheumatoid arthritis TT9DWLC RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTUCPMY ID TTUCPMY TTUCPMY TN Tenascin (TNC) TTUCPMY UP P24821 TTUCPMY UC TENA_HUMAN TTUCPMY SN Tenascin-C; TN-C; TN; Neuronectin; Myotendinous antigen; Miotendinous antigen; JI; Hexabrachion; HXB; Glioma-associated-extracellular matrix antigen; GP 150-225; GMEM; Cytotactin TTUCPMY GN TNC TTUCPMY FC Promotes neurite outgrowth from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells. Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. TTUCPMY PD 6QNV; 6BRB; 2RBL; 2RB8; 1TEN TTUCPMY SQ MGAMTQLLAGVFLAFLALATEGGVLKKVIRHKRQSGVNATLPEENQPVVFNHVYNIKLPVGSQCSVDLESASGEKDLAPPSEPSESFQEHTVDGENQIVFTHRINIPRRACGCAAAPDVKELLSRLEELENLVSSLREQCTAGAGCCLQPATGRLDTRPFCSGRGNFSTEGCGCVCEPGWKGPNCSEPECPGNCHLRGRCIDGQCICDDGFTGEDCSQLACPSDCNDQGKCVNGVCICFEGYAGADCSREICPVPCSEEHGTCVDGLCVCHDGFAGDDCNKPLCLNNCYNRGRCVENECVCDEGFTGEDCSELICPNDCFDRGRCINGTCYCEEGFTGEDCGKPTCPHACHTQGRCEEGQCVCDEGFAGVDCSEKRCPADCHNRGRCVDGRCECDDGFTGADCGELKCPNGCSGHGRCVNGQCVCDEGYTGEDCSQLRCPNDCHSRGRCVEGKCVCEQGFKGYDCSDMSCPNDCHQHGRCVNGMCVCDDGYTGEDCRDRQCPRDCSNRGLCVDGQCVCEDGFTGPDCAELSCPNDCHGQGRCVNGQCVCHEGFMGKDCKEQRCPSDCHGQGRCVDGQCICHEGFTGLDCGQHSCPSDCNNLGQCVSGRCICNEGYSGEDCSEVSPPKDLVVTEVTEETVNLAWDNEMRVTEYLVVYTPTHEGGLEMQFRVPGDQTSTIIQELEPGVEYFIRVFAILENKKSIPVSARVATYLPAPEGLKFKSIKETSVEVEWDPLDIAFETWEIIFRNMNKEDEGEITKSLRRPETSYRQTGLAPGQEYEISLHIVKNNTRGPGLKRVTTTRLDAPSQIEVKDVTDTTALITWFKPLAEIDGIELTYGIKDVPGDRTTIDLTEDENQYSIGNLKPDTEYEVSLISRRGDMSSNPAKETFTTGLDAPRNLRRVSQTDNSITLEWRNGKAAIDSYRIKYAPISGGDHAEVDVPKSQQATTKTTLTGLRPGTEYGIGVSAVKEDKESNPATINAATELDTPKDLQVSETAETSLTLLWKTPLAKFDRYRLNYSLPTGQWVGVQLPRNTTSYVLRGLEPGQEYNVLLTAEKGRHKSKPARVKASTEQAPELENLTVTEVGWDGLRLNWTAADQAYEHFIIQVQEANKVEAARNLTVPGSLRAVDIPGLKAATPYTVSIYGVIQGYRTPVLSAEASTGETPNLGEVVVAEVGWDALKLNWTAPEGAYEYFFIQVQEADTVEAAQNLTVPGGLRSTDLPGLKAATHYTITIRGVTQDFSTTPLSVEVLTEEVPDMGNLTVTEVSWDALRLNWTTPDGTYDQFTIQVQEADQVEEAHNLTVPGSLRSMEIPGLRAGTPYTVTLHGEVRGHSTRPLAVEVVTEDLPQLGDLAVSEVGWDGLRLNWTAADNAYEHFVIQVQEVNKVEAAQNLTLPGSLRAVDIPGLEAATPYRVSIYGVIRGYRTPVLSAEASTAKEPEIGNLNVSDITPESFNLSWMATDGIFETFTIEIIDSNRLLETVEYNISGAERTAHISGLPPSTDFIVYLSGLAPSIRTKTISATATTEALPLLENLTISDINPYGFTVSWMASENAFDSFLVTVVDSGKLLDPQEFTLSGTQRKLELRGLITGIGYEVMVSGFTQGHQTKPLRAEIVTEAEPEVDNLLVSDATPDGFRLSWTADEGVFDNFVLKIRDTKKQSEPLEITLLAPERTRDITGLREATEYEIELYGISKGRRSQTVSAIATTAMGSPKEVIFSDITENSATVSWRAPTAQVESFRITYVPITGGTPSMVTVDGTKTQTRLVKLIPGVEYLVSIIAMKGFEESEPVSGSFTTALDGPSGLVTANITDSEALARWQPAIATVDSYVISYTGEKVPEITRTVSGNTVEYALTDLEPATEYTLRIFAEKGPQKSSTITAKFTTDLDSPRDLTATEVQSETALLTWRPPRASVTGYLLVYESVDGTVKEVIVGPDTTSYSLADLSPSTHYTAKIQALNGPLRSNMIQTIFTTIGLLYPFPKDCSQAMLNGDTTSGLYTIYLNGDKAEALEVFCDMTSDGGGWIVFLRRKNGRENFYQNWKAYAAGFGDRREEFWLGLDNLNKITAQGQYELRVDLRDHGETAFAVYDKFSVGDAKTRYKLKVEGYSGTAGDSMAYHNGRSFSTFDKDTDSAITNCALSYKGAFWYRNCHRVNLMGRYGDNNHSQGVNWFHWKGHEHSIQFAEMKLRPSNFRNLEGRRKRA TTUCPMY TT Clinical trial TTUCPMY KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa05206:MicroRNAs in cancer TTUCPMY RC R-HSA-216083:Integrin cell surface interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans TTZJ5U9 ID TTZJ5U9 TTZJ5U9 TN Thioredoxin (TXN) TTZJ5U9 UP P10599 TTZJ5U9 UC THIO_HUMAN TTZJ5U9 SN Trx; TRX1; TRDX; Surface-associated sulphydryl protein; Surface associated sulphydryl protein; SASP; ATL-derived factor; ADF TTZJ5U9 GN TXN TTZJ5U9 FC Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity. Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. TTZJ5U9 PD 5DQY; 4TRX; 4PUF; 4POM; 4POL TTZJ5U9 SQ MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV TTZJ5U9 TT Clinical trial TTZJ5U9 FM Thioredoxin TTZJ5U9 RC R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-3299685:Detoxification of Reactive Oxygen Species; R-HSA-5628897:TP53 Regulates Metabolic Genes; R-HSA-844456:The NLRP3 inflammasome TTCG5PE ID TTCG5PE TTCG5PE TN Thrombopoietin (THPO) TTCG5PE UP P40225 TTCG5PE UC TPO_HUMAN TTCG5PE BC EPO/TPO family TTCG5PE SN Myeloproliferative leukemia virus oncogene ligand; Megakaryocyte growth and development factor; Megakaryocyte colony-stimulating factor; ML; MGDF; C-mpl ligand TTCG5PE GN THPO TTCG5PE FC Lineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets. TTCG5PE PD 1V7N; 1V7M TTCG5PE SQ MELTELLLVVMLLLTARLTLSSPAPPACDLRVLSKLLRDSHVLHSRLSQCPEVHPLPTPVLLPAVDFSLGEWKTQMEETKAQDILGAVTLLLEGVMAARGQLGPTCLSSLLGQLSGQVRLLLGALQSLLGTQLPPQGRTTAHKDPNAIFLSFQHLLRGKVRFLMLVGGSTLCVRRAPPTTAVPSRTSLVLTLNELPNRTSGLLETNFTASARTTGSGLLKWQQGFRAKIPGLLNQTSRSLDQIPGYLNRIHELLNGTRGLFPGPSRRTLGAPDISSGTSDTGSLPPNLQPGYSPSPTHPPTGQYTLFPLPPTLPTPVVQLHPLLPDPSAPTPTPTSPLLNTSYTHSQNLSQEG TTCG5PE TT Clinical trial TTCG5PE KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage TTHMW3T ID TTHMW3T TTHMW3T TN Thymic stromal lymphopoietin (TSLP) TTHMW3T UP Q969D9 TTHMW3T UC TSLP_HUMAN TTHMW3T SN Thymic stromal lymphopoietin TTHMW3T GN TSLP TTHMW3T FC Isoform 1: Cytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c(+) dendritic cells. Can induce allergic inflammation by directly activating mast cells. TTHMW3T PD 5J13; 5J12; 5J11 TTHMW3T SQ MFPFALLYVLSVSFRKIFILQLVGLVLTYDFTNCDFEKIKAAYLSTISKDLITYMSGTKSTEFNNTVSCSNRPHCLTEIQSLTFNPTAGCASLAKEMFAMKTKAALAIWCPGYSETQINATQAMKKRRKRKVTTNKCLEQVSQLQGLWRRFNRPLLKQQ TTHMW3T TT Clinical trial TTHMW3T KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway TT38MDJ ID TT38MDJ TT38MDJ TN Tissue factor (F3) TT38MDJ UP P13726 TT38MDJ UC TF_HUMAN TT38MDJ SN Thromboplastin; TF; F3; Coagulation factor III; CD142 antigen TT38MDJ GN F3 TT38MDJ FC Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assemblyand propagation of the coagulation protease cascade. TT38MDJ PD 5W06; 4ZMA; 4Z6A; 4YLQ; 4M7L TT38MDJ SQ METPAWPRVPRPETAVARTLLLGWVFAQVAGASGTTNTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTGSAGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVECMGQEKGEFREIFYIIGAVVFVVIILVIILAISLHKCRKAGVGQSWKENSPLNVS TT38MDJ TT Clinical trial TT38MDJ KE hsa04610:Complement and coagulation cascades TT38MDJ RC R-HSA-140834:Extrinsic Pathway of Fibrin Clot Formation TT068JH ID TT068JH TT068JH TN Tissue factor pathway inhibitor (TFPI) TT068JH UP P10646 TT068JH UC TFPI1_HUMAN TT068JH SN TFPI1; Lipoprotein-associated coagulation inhibitor; LACI; Extrinsic pathway inhibitor; EPI TT068JH GN TFPI TT068JH FC It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma. Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. TT068JH PD 6BX8; 5NMV; 4DTG; 4BQD; 1TFX TT068JH SQ MIYTMKKVHALWASVCLLLNLAPAPLNADSEEDEEHTIITDTELPPLKLMHSFCAFKADDGPCKAIMKRFFFNIFTRQCEEFIYGGCEGNQNRFESLEECKKMCTRDNANRIIKTTLQQEKPDFCFLEEDPGICRGYITRYFYNNQTKQCERFKYGGCLGNMNNFETLEECKNICEDGPNGFQVDNYGTQLNAVNNSLTPQSTKVPSLFEFHGPSWCLTPADRGLCRANENRFYYNSVIGKCRPFKYSGCGGNENNFTSKQECLRACKKGFIQRISKGGLIKTKRKRKKQRVKIAYEEIFVKNM TT068JH TT Clinical trial TT068JH KE hsa04610:Complement and coagulation cascades TT068JH RC R-HSA-140834:Extrinsic Pathway of Fibrin Clot Formation TTCXP8J ID TTCXP8J TTCXP8J TN Toll-like receptor 5 (TLR5) TTCXP8J UP O60602 TTCXP8J UC TLR5_HUMAN TTCXP8J BC Toll-like receptor TTCXP8J SN Toll/interleukin-1 receptor-like protein 3; TIL3 TTCXP8J GN TLR5 TTCXP8J FC Recognizes small molecular motifs named pathogen-associated molecular pattern (PAMPs) expressed by pathogens and microbe-associated molecular patterns (MAMPs) usually expressed by resident microbiota. Upon ligand binding such as bacterial flagellins, recruits intracellular adapter proteins MYD88 and TRIF leading to NF-kappa-B activation, cytokine secretion and induction of the inflammatory response. Plays thereby an important role in the relationship between the intestinal epithelium and enteric microbes and contributes to the gut microbiota composition throughout life. Pattern recognition receptor (PRR) located on the cell surface that participates in the activation of innate immunity and inflammatory response. TTCXP8J PD 3J0A; 1P95 TTCXP8J SQ MGDHLDLLLGVVLMAGPVFGIPSCSFDGRIAFYRFCNLTQVPQVLNTTERLLLSFNYIRTVTASSFPFLEQLQLLELGSQYTPLTIDKEAFRNLPNLRILDLGSSKIYFLHPDAFQGLFHLFELRLYFCGLSDAVLKDGYFRNLKALTRLDLSKNQIRSLYLHPSFGKLNSLKSIDFSSNQIFLVCEHELEPLQGKTLSFFSLAANSLYSRVSVDWGKCMNPFRNMVLEILDVSGNGWTVDITGNFSNAISKSQAFSLILAHHIMGAGFGFHNIKDPDQNTFAGLARSSVRHLDLSHGFVFSLNSRVFETLKDLKVLNLAYNKINKIADEAFYGLDNLQVLNLSYNLLGELYSSNFYGLPKVAYIDLQKNHIAIIQDQTFKFLEKLQTLDLRDNALTTIHFIPSIPDIFLSGNKLVTLPKINLTANLIHLSENRLENLDILYFLLRVPHLQILILNQNRFSSCSGDQTPSENPSLEQLFLGENMLQLAWETELCWDVFEGLSHLQVLYLNHNYLNSLPPGVFSHLTALRGLSLNSNRLTVLSHNDLPANLEILDISRNQLLAPNPDVFVSLSVLDITHNKFICECELSTFINWLNHTNVTIAGPPADIYCVYPDSFSGVSLFSLSTEGCDEEEVLKSLKFSLFIVCTVTLTLFLMTILTVTKFRGFCFICYKTAQRLVFKDHPQGTEPDMYKYDAYLCFSSKDFTWVQNALLKHLDTQYSDQNRFNLCFEERDFVPGENRIANIQDAIWNSRKIVCLVSRHFLRDGWCLEAFSYAQGRCLSDLNSALIMVVVGSLSQYQLMKHQSIRGFVQKQQYLRWPEDFQDVGWFLHKLSQQILKKEKEKKKDNNIPLQTVATIS TTCXP8J TT Clinical trial TTCXP8J FM Toll-like receptor family TTCXP8J KE hsa04620:Toll-like receptor signaling pathway; hsa05130:Pathogenic Escherichia coli infection; hsa05132:Salmonella infection; hsa05134:Legionellosis; hsa05321:Inflammatory bowel disease (IBD) TTCXP8J RC R-HSA-5602680:MyD88 deficiency (TLR5); R-HSA-5603037:IRAK4 deficiency (TLR5); R-HSA-975871:MyD88 cascade initiated on plasma membrane TTWRI8V ID TTWRI8V TTWRI8V TN Toll-like receptor 6 (TLR6) TTWRI8V UP Q9Y2C9 TTWRI8V UC TLR6_HUMAN TTWRI8V BC Toll-like receptor TTWRI8V SN CD286 TTWRI8V GN TLR6 TTWRI8V FC Specifically recognizes diacylated and, to a lesser extent, triacylated lipopeptides. In response to diacylated lipopeptides, forms the activation cluster TLR2:TLR6:CD14:CD36, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B. burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR2. In complex with TLR4, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. Participates in the innate immune response to Gram-positive bacteria and fungi. TTWRI8V PD 4OM7 TTWRI8V SQ MTKDKEPIVKSFHFVCLMIIIVGTRIQFSDGNEFAVDKSKRGLIHVPKDLPLKTKVLDMSQNYIAELQVSDMSFLSELTVLRLSHNRIQLLDLSVFKFNQDLEYLDLSHNQLQKISCHPIVSFRHLDLSFNDFKALPICKEFGNLSQLNFLGLSAMKLQKLDLLPIAHLHLSYILLDLRNYYIKENETESLQILNAKTLHLVFHPTSLFAIQVNISVNTLGCLQLTNIKLNDDNCQVFIKFLSELTRGSTLLNFTLNHIETTWKCLVRVFQFLWPKPVEYLNIYNLTIIESIREEDFTYSKTTLKALTIEHITNQVFLFSQTALYTVFSEMNIMMLTISDTPFIHMLCPHAPSTFKFLNFTQNVFTDSIFEKCSTLVKLETLILQKNGLKDLFKVGLMTKDMPSLEILDVSWNSLESGRHKENCTWVESIVVLNLSSNMLTDSVFRCLPPRIKVLDLHSNKIKSVPKQVVKLEALQELNVAFNSLTDLPGCGSFSSLSVLIIDHNSVSHPSADFFQSCQKMRSIKAGDNPFQCTCELREFVKNIDQVSSEVLEGWPDSYKCDYPESYRGSPLKDFHMSELSCNITLLIVTIGATMLVLAVTVTSLCIYLDLPWYLRMVCQWTQTRRRARNIPLEELQRNLQFHAFISYSEHDSAWVKSELVPYLEKEDIQICLHERNFVPGKSIVENIINCIEKSYKSIFVLSPNFVQSEWCHYELYFAHHNLFHEGSNNLILILLEPIPQNSIPNKYHKLKALMTQRTYLQWPKEKSKRGLFWANIRAAFNMKLTLVTENNDVKS TTWRI8V TT Clinical trial TTWRI8V FM Toll-like receptor family TTWRI8V KE hsa04145:Phagosome; hsa04620:Toll-like receptor signaling pathway; hsa05142:Chagas disease (American trypanosomiasis); hsa05152:Tuberculosis TTWRI8V RC R-HSA-166058:MyD88:Mal cascade initiated on plasma membrane; R-HSA-168188:Toll Like Receptor TLR6:TLR2 Cascade; R-HSA-5602498:MyD88 deficiency (TLR2/4); R-HSA-5603041:IRAK4 deficiency (TLR2/4) TTV5YEH ID TTV5YEH TTV5YEH TN Transferrin (TF) TTV5YEH UP P02787 TTV5YEH UC TRFE_HUMAN TTV5YEH BC Transferrin TTV5YEH SN Siderophilin; Serotransferrin; PRO1400; Beta-1 metal-binding globulin TTV5YEH GN TF TTV5YEH FC It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. TTV5YEH PD 6D05; 6D04; 6D03; 6CTC; 5Y6K TTV5YEH SQ MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKSDNCEDTPEAGYFAIAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP TTV5YEH TT Clinical trial TTV5YEH FM Transferrin family TTV5YEH KE hsa04066:HIF-1 signaling pathway; hsa04978:Mineral absorption TTV5YEH RC R-HSA-114608:Platelet degranulation; R-HSA-917937:Iron uptake and transport; R-HSA-917977:Transferrin endocytosis and recycling TTTLQFR ID TTTLQFR TTTLQFR TN Transforming growth factor alpha (TGFA) TTTLQFR UP P01135 TTTLQFR UC TGFA_HUMAN TTTLQFR BC Growth factor TTTLQFR SN TGF-alpha (40-89); TGF type 1 (40-89); Protransforming growth factor alpha (40-89); ETGF (40-89); EGF-like TGF (40-89) TTTLQFR GN TGFA TTTLQFR FC TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar. TTTLQFR PD 5KN5; 4TGF; 3TGF; 3.00E+50; 2TGF TTTLQFR SQ MVPSAGQLALFALGIVLAACQALENSTSPLSADPPVAAAVVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLAVVAASQKKQAITALVVVSIVALAVLIITCVLIHCCQVRKHCEWCRALICRHEKPSALLKGRTACCHSETVV TTTLQFR TT Clinical trial TTTLQFR FM Growth factor TTTLQFR RC R-HSA-204005:COPII (Coat Protein 2) Mediated Vesicle Transport; R-HSA-5694530:Cargo concentration in the ER TTWOMY8 ID TTWOMY8 TTWOMY8 TN Transforming growth factor beta 3 (TGFB3) TTWOMY8 UP P10600 TTWOMY8 UC TGFB3_HUMAN TTWOMY8 BC Growth factor TTWOMY8 SN Transforming growth factor beta-3 proprotein; Transforming growth factor beta-3; TGF-beta-3; Latency-associated peptide TTWOMY8 GN TGFB3 TTWOMY8 FC Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively. TTWOMY8 PD 4UM9; 3EO1; 2PJY; 1TGK; 1TGJ TTWOMY8 SQ MKMHLQRALVVLALLNFATVSLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPTVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQENTESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNRTNLFRAEFRVLRVPNPSSKRNEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDNPGQGGQRKKRALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS TTWOMY8 TT Clinical trial TTWOMY8 FM Growth factor TTHU7JA ID TTHU7JA TTHU7JA TN Tumor susceptibility gene protein 101 (TSG101) TTHU7JA UP Q99816 TTHU7JA UC TS101_HUMAN TTHU7JA BC Ubiquitin-conjugating enzyme TTHU7JA SN Tumor susceptibility gene 101 protein; ESCRT-I complex subunit TSG101 TTHU7JA GN TSG101 TTHU7JA FC Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. Required for the exosomal release of SDCBP, CD63 and syndecan. It may also play a role in the extracellular release of microvesicles that differ from the exosomes. Component of the ESCRT-I complex, a regulator of vesicular trafficking process. TTHU7JA PD 5VKG; 4ZNY; 4YC1; 4EJE; 3P9H TTHU7JA SQ MAVSESQLKKMVSKYKYRDLTVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEPPVFSRPISASYPPYQATGPPNTSYMPGMPGGISPYPSGYPPNPSGYPGCPYPPGGPYPATTSSQYPSQPPVTTVGPSRDGTISEDTIRASLISAVSDKLRWRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKARKTAGLSDLY TTHU7JA TT Clinical trial TTHU7JA FM Ubiquitin family TTHU7JA KE hsa04144:Endocytosis TTHU7JA RC R-HSA-162588:Budding and maturation of HIV virion; R-HSA-174490:Membrane binding and targetting of GAG proteins TT0QUFV ID TT0QUFV TT0QUFV TN Vascular endothelial growth factor C (VEGFC) TT0QUFV UP P49767 TT0QUFV UC VEGFC_HUMAN TT0QUFV BC Growth factor TT0QUFV SN Vascular endothelial growth factor-related protein; VRP; VEGF-C; Flt4-L; Flt4 ligand TT0QUFV GN VEGFC TT0QUFV FC May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates KDR/VEGFR2 and FLT4/VEGFR3 receptors. Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. TT0QUFV PD 4BSK; 2X1X; 2X1W TT0QUFV SQ MHLLGFFSVACSLLAAALLPGPREAPAAAAAFESGLDLSDAEPDAGEATAYASKDLEEQLRSVSSVDELMTVLYPEYWKMYKCQLRKGGWQHNREQANLNSRTEETIKFAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGVATNTFFKPPCVSVYRCGGCCNSEGLQCMNTSTSYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRRSLPATLPQCQAANKTCPTNYMWNNHICRCLAQEDFMFSSDAGDDSTDGFHDICGPNKELDEETCQCVCRAGLRPASCGPHKELDRNSCQCVCKNKLFPSQCGANREFDENTCQCVCKRTCPRNQPLNPGKCACECTESPQKCLLKGKKFHHQTCSCYRRPCTNRQKACEPGFSYSEEVCRCVPSYWKRPQMS TT0QUFV TT Clinical trial TT0QUFV FM Growth factor TT0QUFV KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04668:TNF signaling pathway; hsa05200:Pathways in cancer TT0QUFV RC R-HSA-114608:Platelet degranulation; R-HSA-194313:VEGF ligand-receptor interactions; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization TTAMKGB ID TTAMKGB TTAMKGB TN Voltage-dependent anion-selective channel 1 (VDAC1) TTAMKGB UP P21796 TTAMKGB UC VDAC1_HUMAN TTAMKGB BC Eukaryotic mitochondrial porin TTAMKGB SN Porin 31HM; Porin 31HL; Plasmalemmal porin; Outer mitochondrial membrane protein porin 1 TTAMKGB GN VDAC1 TTAMKGB FC Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective (PubMed:11845315, PubMed:18755977, PubMed:20230784, PubMed:8420959). May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis (PubMed:15033708, PubMed:25296756). TTAMKGB PD 6G73; 6G6U; 5XDO; 5XDN; 5JDP TTAMKGB SQ MAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTETTKVTGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTGYKREHINLGCDMDFDIAGPSIRGALVLGYEGWLAGYQMNFETAKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQIDPDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA TTAMKGB TT Clinical trial TTAMKGB KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04217:Necroptosis; hsa04218:Cellular senescence; hsa04621:NOD-like receptor signaling pathway; hsa04979:Cholesterol metabolism; hsa05012:Parkinson disease; hsa05016:Huntington disease; hsa05164:Influenza A; hsa05166:Human T-cell leukemia virus 1 infection TTT48SQ ID TTT48SQ TTT48SQ TN Voltage-dependent anion-selective channel 3 (VDAC3) TTT48SQ UP Q9Y277 TTT48SQ UC VDAC3_HUMAN TTT48SQ BC Eukaryotic mitochondrial porin TTT48SQ SN hVDAC3; VDAC3; VDAC-3; Outer mitochondrial membrane protein porin 3 TTT48SQ GN VDAC3 TTT48SQ FC Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. TTT48SQ SQ MCNTPTYCDLGKAAKDVFNKGYGFGMVKIDLKTKSCSGVEFSTSGHAYTDTGKASGNLETKYKVCNYGLTFTQKWNTDNTLGTEISWENKLAEGLKLTLDTIFVPNTGKKSGKLKASYKRDCFSVGSNVDIDFSGPTIYGWAVLAFEGWLAGYQMSFDTAKSKLSQNNFALGYKAADFQLHTHVNDGTEFGGSIYQKVNEKIETSINLAWTAGSNNTRFGIAAKYMLDCRTSLSAKVNNASLIGLGYTQTLRPGVKLTLSALIDGKNFSAGGHKVGLGFELEA TTT48SQ TT Clinical trial TTT48SQ KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa05012:Parkinson's disease; hsa05016:Huntington's disease; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05203:Viral carcinogenesis TTUO98L ID TTUO98L TTUO98L TN Angiopoietin-related protein 3 (ANGPTL3) TTUO98L UP Q9Y5C1 TTUO98L UC ANGL3_HUMAN TTUO98L BC Fibrinogen protein TTUO98L SN UNQ153/PRO179; Angiopoietin-like protein 3; Angiopoietin-5; ANGPT5; ANG-5 TTUO98L GN ANGPTL3 TTUO98L FC Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake (By similarity). Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1. Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids. Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol. Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL)-TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT (By similarity). Contributes to lower plasma levels of low density lipoprotein (LDL)-cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR. May stimulate hypothalamic LPL activity (By similarity). TTUO98L PD 6EUA TTUO98L SQ MFTIKLLLFIVPLVISSRIDQDNSSFDSLSPEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQPETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEISLSSKPRAPRTTPFLQLNEIRNVKHDGIPAECTTIYNRGEHTSGMYAIRPSNSQVFHVYCDVISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKIYSIVKQSNYVLRIELEDWKDNKHYIEYSFYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGHFNCPEGYSGGWWWHDECGENNLNGKYNKPRAKSKPERRRGLSWKSQNGRLYSIKSTKMLIHPTDSESFE TTUO98L TT Successful TT2718H ID TT2718H TT2718H TN Apolipoprotein B-100 (APOB) TT2718H UP P04114 TT2718H UC APOB_HUMAN TT2718H BC Apolipoprotein TT2718H SN Apolipoprotein B48; Apo B48; Apo B100; Apo B-100 TT2718H GN APOB TT2718H FC Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor. Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). TT2718H SQ MDPPRPALLALLALPALLLLLLAGARAEEEMLENVSLVCPKDATRFKHLRKYTYNYEAESSSGVPGTADSRSATRINCKVELEVPQLCSFILKTSQCTLKEVYGFNPEGKALLKKTKNSEEFAAAMSRYELKLAIPEGKQVFLYPEKDEPTYILNIKRGIISALLVPPETEEAKQVLFLDTVYGNCSTHFTVKTRKGNVATEISTERDLGQCDRFKPIRTGISPLALIKGMTRPLSTLISSSQSCQYTLDAKRKHVAEAICKEQHLFLPFSYKNKYGMVAQVTQTLKLEDTPKINSRFFGEGTKKMGLAFESTKSTSPPKQAEAVLKTLQELKKLTISEQNIQRANLFNKLVTELRGLSDEAVTSLLPQLIEVSSPITLQALVQCGQPQCSTHILQWLKRVHANPLLIDVVTYLVALIPEPSAQQLREIFNMARDQRSRATLYALSHAVNNYHKTNPTGTQELLDIANYLMEQIQDDCTGDEDYTYLILRVIGNMGQTMEQLTPELKSSILKCVQSTKPSLMIQKAAIQALRKMEPKDKDQEVLLQTFLDDASPGDKRLAAYLMLMRSPSQADINKIVQILPWEQNEQVKNFVASHIANILNSEELDIQDLKKLVKEALKESQLPTVMDFRKFSRNYQLYKSVSLPSLDPASAKIEGNLIFDPNNYLPKESMLKTTLTAFGFASADLIEIGLEGKGFEPTLEALFGKQGFFPDSVNKALYWVNGQVPDGVSKVLVDHFGYTKDDKHEQDMVNGIMLSVEKLIKDLKSKEVPEARAYLRILGEELGFASLHDLQLLGKLLLMGARTLQGIPQMIGEVIRKGSKNDFFLHYIFMENAFELPTGAGLQLQISSSGVIAPGAKAGVKLEVANMQAELVAKPSVSVEFVTNMGIIIPDFARSGVQMNTNFFHESGLEAHVALKAGKLKFIIPSPKRPVKLLSGGNTLHLVSTTKTEVIPPLIENRQSWSVCKQVFPGLNYCTSGAYSNASSTDSASYYPLTGDTRLELELRPTGEIEQYSVSATYELQREDRALVDTLKFVTQAEGAKQTEATMTFKYNRQSMTLSSEVQIPDFDVDLGTILRVNDESTEGKTSYRLTLDIQNKKITEVALMGHLSCDTKEERKIKGVISIPRLQAEARSEILAHWSPAKLLLQMDSSATAYGSTVSKRVAWHYDEEKIEFEWNTGTNVDTKKMTSNFPVDLSDYPKSLHMYANRLLDHRVPQTDMTFRHVGSKLIVAMSSWLQKASGSLPYTQTLQDHLNSLKEFNLQNMGLPDFHIPENLFLKSDGRVKYTLNKNSLKIEIPLPFGGKSSRDLKMLETVRTPALHFKSVGFHLPSREFQVPTFTIPKLYQLQVPLLGVLDLSTNVYSNLYNWSASYSGGNTSTDHFSLRARYHMKADSVVDLLSYNVQGSGETTYDHKNTFTLSYDGSLRHKFLDSNIKFSHVEKLGNNPVSKGLLIFDASSSWGPQMSASVHLDSKKKQHLFVKEVKIDGQFRVSSFYAKGTYGLSCQRDPNTGRLNGESNLRFNSSYLQGTNQITGRYEDGTLSLTSTSDLQSGIIKNTASLKYENYELTLKSDTNGKYKNFATSNKMDMTFSKQNALLRSEYQADYESLRFFSLLSGSLNSHGLELNADILGTDKINSGAHKATLRIGQDGISTSATTNLKCSLLVLENELNAELGLSGASMKLTTNGRFREHNAKFSLDGKAALTELSLGSAYQAMILGVDSKNIFNFKVSQEGLKLSNDMMGSYAEMKFDHTNSLNIAGLSLDFSSKLDNIYSSDKFYKQTVNLQLQPYSLVTTLNSDLKYNALDLTNNGKLRLEPLKLHVAGNLKGAYQNNEIKHIYAISSAALSASYKADTVAKVQGVEFSHRLNTDIAGLASAIDMSTNYNSDSLHFSNVFRSVMAPFTMTIDAHTNGNGKLALWGEHTGQLYSKFLLKAEPLAFTFSHDYKGSTSHHLVSRKSISAALEHKVSALLTPAEQTGTWKLKTQFNNNEYSQDLDAYNTKDKIGVELTGRTLADLTLLDSPIKVPLLLSEPINIIDALEMRDAVEKPQEFTIVAFVKYDKNQDVHSINLPFFETLQEYFERNRQTIIVVLENVQRNLKHINIDQFVRKYRAALGKLPQQANDYLNSFNWERQVSHAKEKLTALTKKYRITENDIQIALDDAKINFNEKLSQLQTYMIQFDQYIKDSYDLHDLKIAIANIIDEIIEKLKSLDEHYHIRVNLVKTIHDLHLFIENIDFNKSGSSTASWIQNVDTKYQIRIQIQEKLQQLKRHIQNIDIQHLAGKLKQHIEAIDVRVLLDQLGTTISFERINDILEHVKHFVINLIGDFEVAEKINAFRAKVHELIERYEVDQQIQVLMDKLVELAHQYKLKETIQKLSNVLQQVKIKDYFEKLVGFIDDAVKKLNELSFKTFIEDVNKFLDMLIKKLKSFDYHQFVDETNDKIREVTQRLNGEIQALELPQKAEALKLFLEETKATVAVYLESLQDTKITLIINWLQEALSSASLAHMKAKFRETLEDTRDRMYQMDIQQELQRYLSLVGQVYSTLVTYISDWWTLAAKNLTDFAEQYSIQDWAKRMKALVEQGFTVPEIKTILGTMPAFEVSLQALQKATFQTPDFIVPLTDLRIPSVQINFKDLKNIKIPSRFSTPEFTILNTFHIPSFTIDFVEMKVKIIRTIDQMLNSELQWPVPDIYLRDLKVEDIPLARITLPDFRLPEIAIPEFIIPTLNLNDFQVPDLHIPEFQLPHISHTIEVPTFGKLYSILKIQSPLFTLDANADIGNGTTSANEAGIAASITAKGESKLEVLNFDFQANAQLSNPKINPLALKESVKFSSKYLRTEHGSEMLFFGNAIEGKSNTVASLHTEKNTLELSNGVIVKINNQLTLDSNTKYFHKLNIPKLDFSSQADLRNEIKTLLKAGHIAWTSSGKGSWKWACPRFSDEGTHESQISFTIEGPLTSFGLSNKINSKHLRVNQNLVYESGSLNFSKLEIQSQVDSQHVGHSVLTAKGMALFGEGKAEFTGRHDAHLNGKVIGTLKNSLFFSAQPFEITASTNNEGNLKVRFPLRLTGKIDFLNNYALFLSPSAQQASWQVSARFNQYKYNQNFSAGNNENIMEAHVGINGEANLDFLNIPLTIPEMRLPYTIITTPPLKDFSLWEKTGLKEFLKTTKQSFDLSVKAQYKKNKHRHSITNPLAVLCEFISQSIKSFDRHFEKNRNNALDFVTKSYNETKIKFDKYKAEKSHDELPRTFQIPGYTVPVVNVEVSPFTIEMSAFGYVFPKAVSMPSFSILGSDVRVPSYTLILPSLELPVLHVPRNLKLSLPDFKELCTISHIFIPAMGNITYDFSFKSSVITLNTNAELFNQSDIVAHLLSSSSSVIDALQYKLEGTTRLTRKRGLKLATALSLSNKFVEGSHNSTVSLTTKNMEVSVATTTKAQIPILRMNFKQELNGNTKSKPTVSSSMEFKYDFNSSMLYSTAKGAVDHKLSLESLTSYFSIESSTKGDVKGSVLSREYSGTIASEANTYLNSKSTRSSVKLQGTSKIDDIWNLEVKENFAGEATLQRIYSLWEHSTKNHLQLEGLFFTNGEHTSKATLELSPWQMSALVQVHASQPSSFHDFPDLGQEVALNANTKNQKIRWKNEVRIHSGSFQSQVELSNDQEKAHLDIAGSLEGHLRFLKNIILPVYDKSLWDFLKLDVTTSIGRRQHLRVSTAFVYTKNPNGYSFSIPVKVLADKFIIPGLKLNDLNSVLVMPTFHVPFTDLQVPSCKLDFREIQIYKKLRTSSFALNLPTLPEVKFPEVDVLTKYSQPEDSLIPFFEITVPESQLTVSQFTLPKSVSDGIAALDLNAVANKIADFELPTIIVPEQTIEIPSIKFSVPAGIVIPSFQALTARFEVDSPVYNATWSASLKNKADYVETVLDSTCSSTVQFLEYELNVLGTHKIEDGTLASKTKGTFAHRDFSAEYEEDGKYEGLQEWEGKAHLNIKSPAFTDLHLRYQKDKKGISTSAASPAVGTVGMDMDEDDDFSKWNFYYSPQSSPDKKLTIFKTELRVRESDEETQIKVNWEEEAASGLLTSLKDNVPKATGVLYDYVNKYHWEHTGLTLREVSSKLRRNLQNNAEWVYQGAIRQIDDIDVRFQKAASGTTGTYQEWKDKAQNLYQELLTQEGQASFQGLKDNVFDGLVRVTQEFHMKVKHLIDSLIDFLNFPRFQFPGKPGIYTREELCTMFIREVGTVLSQVYSKVHNGSEILFSYFQDLVITLPFELRKHKLIDVISMYRELLKDLSKEAQEVFKAIQSLKTTEVLRNLQDLLQFIFQLIEDNIKQLKEMKFTYLINYIQDEINTIFSDYIPYVFKLLKENLCLNLHKFNEFIQNELQEASQELQQIHQYIMALREEYFDPSIVGWTVKYYELEEKIVSLIKNLLVALKDFHSEYIVSASNFTSQLSSQVEQFLHRNIQEYLSILTDPDGKGKEKIAELSATAQEIIKSQAIATKKIISDYHQQFRYKLQDFSDQLSDYYEKFIAESKRLIDLSIQNYHTFLIYITELLKKLQSTTVMNPYMKLAPGELTIIL TT2718H TT Clinical trial TT2718H FM Apolipoprotein TT2718H KE hsa04975:Fat digestion and absorption; hsa04977:Vitamin digestion and absorption TT2718H RC R-HSA-171052:LDL-mediated lipid transport; R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-3000471:Scavenging by Class B Receptors; R-HSA-3000480:Scavenging by Class A Receptors; R-HSA-3000497:Scavenging by Class H Receptors; R-HSA-432142:Platelet sensitization by LDL; R-HSA-975634:Retinoid metabolism and transport TTYM94H ID TTYM94H TTYM94H TN Asialoglycoprotein receptor 1 (ASGR1) TTYM94H UP P07306 TTYM94H UC ASGR1_HUMAN TTYM94H SN Hepatic lectin H1; HL-1; C-type lectin domain family 4 member H1 TTYM94H GN ASGR1 TTYM94H FC Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. TTYM94H PD 5JQ1; 5JPV; 1DV8 TTYM94H SQ MTKEYQDLQHLDNEESDHHQLRKGPPPPQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIGSQNSQLQEELRGLRETFSNFTASTEAQVKGLSTQGGNVGRKMKSLESQLEKQQKDLSEDHSSLLLHVKQFVSDLRSLSCQMAALQGNGSERTCCPVNWVEHERSCYWFSRSGKAWADADNYCRLEDAHLVVVTSWEEQKFVQHHIGPVNTWMGLHDQNGPWKWVDGTDYETGFKNWRPEQPDDWYGHGLGGGEDCAHFTDDGRWNDDVCQRPYRWVCETELDKASQEPPLL TTYM94H TT Clinical trial TTYM94H KE hsa04918:Thyroid hormone synthesis TTOTSW1 ID TTOTSW1 TTOTSW1 TN ATP-dependent RNA helicase DDX5 (DDX5) TTOTSW1 UP P17844 TTOTSW1 UC DDX5_HUMAN TTOTSW1 SN RNA helicase p68; Probable ATP-dependent RNA helicase DDX5; HLR1; HELR; G17P1; DEAD box protein 5 TTOTSW1 GN DDX5 TTOTSW1 FC Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. TTOTSW1 EC EC 3.6.4.13 TTOTSW1 PD 4A4D; 3FE2 TTOTSW1 SQ MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ TTOTSW1 TT Clinical trial TTB9Z8R ID TTB9Z8R TTB9Z8R TN B7-related protein 1 (B7RP1) TTB9Z8R UP O75144 TTB9Z8R UC ICOSL_HUMAN TTB9Z8R BC Immunoglobulin TTB9Z8R SN KIAA0653; ICOSL; ICOS ligand; CD275; B7related protein 1; B7like protein Gl50; B7RP-1; B7H2; B7-like protein Gl50; B7-H2; B7 homolog 2 TTB9Z8R GN ICOSLG TTB9Z8R FC Acts as a costimulatory signal for T-cell proliferation and cytokine secretion; induces also B-cell proliferation and differentiation into plasma cells. Could play an important role in mediating local tissue responses to inflammatory conditions, as well as in modulating the secondary immune response by co-stimulating memory T-cell function. Ligand for the T-cell-specific cell surface receptor ICOS. TTB9Z8R SQ MRLGSPGLLFLLFSSLRADTQEKEVRAMVGSDVELSCACPEGSRFDLNDVYVYWQTSESKTVVTYHIPQNSSLENVDSRYRNRALMSPAGMLRGDFSLRLFNVTPQDEQKFHCLVLSQSLGFQEVLSVEVTLHVAANFSVPVVSAPHSPSQDELTFTCTSINGYPRPNVYWINKTDNSLLDQALQNDTVFLNMRGLYDVVSVLRIARTPSVNIGCCIENVLLQQNLTVGSQTGNDIGERDKITENPVSTGEKNAATWSILAVLCLLVVVAVAIGWVCRDRCLQHSYAGAWAVSPETELTGHV TTB9Z8R TT Clinical trial TTB9Z8R FM Immunoglobulin superfamily TTB9Z8R KE hsa04514:Cell adhesion molecules (CAMs); hsa04672:Intestinal immune network for IgA production TTB9Z8R RC R-HSA-388841:Costimulation by the CD28 family TTB52WU ID TTB52WU TTB52WU TN Bacterial Botulinum toxin A (Bact botA) TTB52WU UP P10845 TTB52WU UC BXA1_CLOBO TTB52WU BC Peptidase TTB52WU SN botA TTB52WU GN Bact botA TTB52WU FC Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-|-Arg- 198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure. TTB52WU PD 6MHJ; 6DKK; 5VGX; 5VGV; 5V8U TTB52WU SQ MPFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYNRQIERSSRTLGCSWEFIPVDDGWGERPL TTB52WU TT Clinical trial TTV8DM2 ID TTV8DM2 TTV8DM2 TN Bacterial Dihydrofolate reductase (Bact DHFR) TTV8DM2 UP P0ABQ4 TTV8DM2 UC DYR_ECOLI TTV8DM2 SN Bact Dihydrofolate reductase TTV8DM2 GN Bact DHFR TTV8DM2 FC Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. TTV8DM2 EC EC 1.5.1.3 TTV8DM2 PD 7DFR; 6MTH; 6MT8; 6MR9; 6DFR TTV8DM2 SQ MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR TTV8DM2 TT Clinical trial TTARBVH ID TTARBVH TTARBVH TN Beta-klotho (KLB) TTARBVH UP Q86Z14 TTARBVH UC KLOTB_HUMAN TTARBVH BC Glycosylase TTARBVH SN Klotho beta-like protein; BetaKlotho; BKL TTARBVH GN KLB TTARBVH FC Probably inactive as a glycosidase. Increases the ability of FGFR1 and FGFR4 to bind FGF21. Contributes to the transcriptional repression of cholesterol 7-alpha-hydroxylase (CYP7A1), the rate-limiting enzyme in bile acid synthesis. TTARBVH PD 6NFJ; 5WI9; 5VAQ; 5VAN; 5VAK TTARBVH SQ MKPGCAAGSPGNEWIFFSTDEITTRYRNTMSNGGLQRSVILSALILLRAVTGFSGDGRAIWSKNPNFTPVNESQLFLYDTFPKNFFWGIGTGALQVEGSWKKDGKGPSIWDHFIHTHLKNVSSTNGSSDSYIFLEKDLSALDFIGVSFYQFSISWPRLFPDGIVTVANAKGLQYYSTLLDALVLRNIEPIVTLYHWDLPLALQEKYGGWKNDTIIDIFNDYATYCFQMFGDRVKYWITIHNPYLVAWHGYGTGMHAPGEKGNLAAVYTVGHNLIKAHSKVWHNYNTHFRPHQKGWLSITLGSHWIEPNRSENTMDIFKCQQSMVSVLGWFANPIHGDGDYPEGMRKKLFSVLPIFSEAEKHEMRGTADFFAFSFGPNNFKPLNTMAKMGQNVSLNLREALNWIKLEYNNPRILIAENGWFTDSRVKTEDTTAIYMMKNFLSQVLQAIRLDEIRVFGYTAWSLLDGFEWQDAYTIRRGLFYVDFNSKQKERKPKSSAHYYKQIIRENGFSLKESTPDVQGQFPCDFSWGVTESVLKPESVASSPQFSDPHLYVWNATGNRLLHRVEGVRLKTRPAQCTDFVNIKKQLEMLARMKVTHYRFALDWASVLPTGNLSAVNRQALRYYRCVVSEGLKLGISAMVTLYYPTHAHLGLPEPLLHADGWLNPSTAEAFQAYAGLCFQELGDLVKLWITINEPNRLSDIYNRSGNDTYGAAHNLLVAHALAWRLYDRQFRPSQRGAVSLSLHADWAEPANPYADSHWRAAERFLQFEIAWFAEPLFKTGDYPAAMREYIASKHRRGLSSSALPRLTEAERRLLKGTVDFCALNHFTTRFVMHEQLAGSRYDSDRDIQFLQDITRLSSPTRLAVIPWGVRKLLRWVRRNYGDMDIYITASGIDDQALEDDRLRKYYLGKYLQEVLKAYLIDKVRIKGYYAFKLAEEKSKPRFGFFTSDFKAKSSIQFYNKVISSRGFPFENSSSRCSQTQENTECTVCLFLVQKKPLIFLGCCFFSTLVLLLSIAIFQRQKRRKFWKAKNLQHIPLKKGKRVVS TTARBVH TT Clinical trial TTARBVH FM Glycosyl hydrolase family TTYH1ZK ID TTYH1ZK TTYH1ZK TN Beta-microseminoprotein (MSMB) TTYH1ZK UP P08118 TTYH1ZK UC MSMB_HUMAN TTYH1ZK SN Seminal plasma beta-inhibin; Prostate secretory protein of 94 amino acids; Prostate secreted seminal plasma protein; PSP94; PSP-94; PRSP; PN44; Immunoglobulin-binding factor; IGBF TTYH1ZK GN MSMB TTYH1ZK FC A member of the immunoglobulin binding factor family. May have a role as an autocrine paracrine factor in uterine, breast and other female reproductive tissues. Inhibits growth of cancer cells in an experimental model of prostate cancer, though this property is cell line specific. TTYH1ZK PD 3IX0; 2IZ3 TTYH1ZK SQ MNVLLGSVVIFATFVTLCNASCYFIPNEGVPGDSTRKCMDLKGNKHPINSEWQTDNCETCTCYETEISCCTLVSTPVGYDKDNCQRIFKKEDCKYIVVEKKDPKKTCSVSEWII TTYH1ZK TT Clinical trial TT69DB8 ID TT69DB8 TT69DB8 TN Beta-site APP-cleaving enzyme 2 (BACE2) TT69DB8 UP Q9Y5Z0 TT69DB8 UC BACE2_HUMAN TT69DB8 SN Theta-secretase; Membrane-associated aspartic protease 1; Memapsin-1; Down region aspartic protease; DRAP; Beta-site amyloid precursor protein cleaving enzyme 2; Beta-site APP cleaving enzyme 2; Beta-secretase 2; Aspartyl protease 1; Aspartic-like protease 56 kDa; Asp 1; ASP21; ASP1; ALP56; AEPLC TT69DB8 GN BACE2 TT69DB8 FC Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. It has also been shown that it can cleave APP between residues 671 and 672. Responsible also for the proteolytic processing of CLTRN in pancreatic beta cells. TT69DB8 EC EC 3.4.23.45 TT69DB8 PD 4BFB; 4BEL; 3ZLQ; 3ZL7; 3ZKX TT69DB8 SQ MGALARALLLPLLAQWLLRAAPELAPAPFTLPLRVAAATNRVVAPTPGPGTPAERHADGLALALEPALASPAGAANFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLVNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARASLIPEFSDGFWTGSQLACWTNSETPWSYFPKISIYLRDENSSRSFRITILPQLYIQPMMGAGLNYECYRFGISPSTNALVIGATVMEGFYVIFDRAQKRVGFAASPCAEIAGAAVSEISGPFSTEDVASNCVPAQSLSEPILWIVSYALMSVCGAILLVLIVLLLLPFRCQRRPRDPEVVNDESSLVRHRWK TT69DB8 TT Clinical trial TTLCKI8 ID TTLCKI8 TTLCKI8 TN Blood group Rh(D) polypeptide (RHD) TTLCKI8 UP Q02161 TTLCKI8 UC RHD_HUMAN TTLCKI8 BC Ammonia transporter channel TTLCKI8 SN Rhesus D antigen; RhPII; Rh polypeptide 2; RHXIII; RHD; CD240D TTLCKI8 GN RHD TTLCKI8 FC May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. TTLCKI8 SQ MSSKYPRSVRRCLPLWALTLEAALILLFYFFTHYDASLEDQKGLVASYQVGQDLTVMAAIGLGFLTSSFRRHSWSSVAFNLFMLALGVQWAILLDGFLSQFPSGKVVITLFSIRLATMSALSVLISVDAVLGKVNLAQLVVMVLVEVTALGNLRMVISNIFNTDYHMNMMHIYVFAAYFGLSVAWCLPKPLPEGTEDKDQTATIPSLSAMLGALFLWMFWPSFNSALLRSPIERKNAVFNTYYAVAVSVVTAISGSSLAHPQGKISKTYVHSAVLAGGVAVGTSCHLIPSPWLAMVLGLVAGLISVGGAKYLPGCCNRVLGIPHSSIMGYNFSLLGLLGEIIYIVLLVLDTVGAGNGMIGFQVLLSIGELSLAIVIALMSGLLTGLLLNLKIWKAPHEAKYFDDQVFWKFPHLAVGF TTLCKI8 TT Clinical trial TT7M9I6 ID TT7M9I6 TT7M9I6 TN Calcium-activated potassium channel KCa3.1 (KCNN4) TT7M9I6 UP O15554 TT7M9I6 UC KCNN4_HUMAN TT7M9I6 BC Voltage-gated ion channel TT7M9I6 SN SKCa4; SKCa 4; SK4; Putative Gardos channel; KCa4; KCa3.1; Intermediate conductance calcium-activated potassium channel protein 4; IKCa1; IK1 TT7M9I6 GN KCNN4 TT7M9I6 FC Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells. Plays a role in the late stages of EGF-induced macropinocytosis. Forms a voltage-independent potassium channel that is activated by intracellular calcium. TT7M9I6 PD 6D42; 6CNO; 6CNN; 6CNM TT7M9I6 SQ MGGDLVLGLGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFLVKCTISISTFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPAPVRGPPCVQDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIQYTKEMKESAARVLQEAWMFYKHTRRKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMVDISKMHMILYDLQQNLSSSHRALEKQIDTLAGKLDALTELLSTALGPRQLPEPSQQSK TT7M9I6 TT Clinical trial TTQ4ESF ID TTQ4ESF TTQ4ESF TN Calgranulin D (S100A12) TTQ4ESF UP P80511 TTQ4ESF UC S10AC_HUMAN TTQ4ESF BC S100 calcium-binding protein TTQ4ESF SN S100 calcium-binding protein A12; Protein S100-A12; P6; Neutrophil S100 protein; Migration inhibitory factor-related protein 6; MRP-6; Extracellular newly identified RAGE-binding protein; EN-RAGE; Calgranulin-C; Calcium-binding protein in amniotic fluid 1; CGRP; CAGC; CAAF1 TTQ4ESF GN S100A12 TTQ4ESF FC Its proinflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of proinflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites. Possesses filariacidal and filariastatic activity. Calcitermin possesses antifungal activity against C. albicans and is also active against E. coli and P. aeruginosa but not L. monocytogenes and S. aureus. S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. TTQ4ESF PD 2WCF; 2WCE; 2WCB; 2WC8; 2M9G TTQ4ESF SQ MTKLEEHLEGIVNIFHQYSVRKGHFDTLSKGELKQLLTKELANTIKNIKDKAVIDEIFQGLDANQDEQVDFQEFISLVAIALKAAHYHTHKE TTQ4ESF TT Clinical trial TT9M6NA ID TT9M6NA TT9M6NA TN Cancer/testis antigen MAGE-C1/CT7 (MAGEC1) TT9M6NA UP O60732 TT9M6NA UC MAGC1_HUMAN TT9M6NA BC Melanoma associated antigen family TT9M6NA SN Melanoma-associated antigen C1; MAGE-C1 antigen; Cancer/testis antigen 7.1; CT7.1 TT9M6NA GN MAGEC1 TT9M6NA FC Tumor antigen. TT9M6NA SQ MGDKDMPTAGMPSLLQSSSESPQSCPEGEDSQSPLQIPQSSPESDDTLYPLQSPQSRSEGEDSSDPLQRPPEGKDSQSPLQIPQSSPEGDDTQSPLQNSQSSPEGKDSLSPLEISQSPPEGEDVQSPLQNPASSFFSSALLSIFQSSPESTQSPFEGFPQSVLQIPVSAASSSTLVSIFQSSPESTQSPFEGFPQSPLQIPVSRSFSSTLLSIFQSSPERTQSTFEGFAQSPLQIPVSPSSSSTLLSLFQSFSERTQSTFEGFAQSSLQIPVSPSFSSTLVSLFQSSPERTQSTFEGFPQSPLQIPVSSSSSSTLLSLFQSSPERTHSTFEGFPQSLLQIPMTSSFSSTLLSIFQSSPESAQSTFEGFPQSPLQIPGSPSFSSTLLSLFQSSPERTHSTFEGFPQSPLQIPMTSSFSSTLLSILQSSPESAQSAFEGFPQSPLQIPVSSSFSYTLLSLFQSSPERTHSTFEGFPQSPLQIPVSSSSSSSTLLSLFQSSPECTQSTFEGFPQSPLQIPQSPPEGENTHSPLQIVPSLPEWEDSLSPHYFPQSPPQGEDSLSPHYFPQSPPQGEDSLSPHYFPQSPQGEDSLSPHYFPQSPPQGEDSMSPLYFPQSPLQGEEFQSSLQSPVSICSSSTPSSLPQSFPESSQSPPEGPVQSPLHSPQSPPEGMHSQSPLQSPESAPEGEDSLSPLQIPQSPLEGEDSLSSLHFPQSPPEWEDSLSPLHFPQFPPQGEDFQSSLQSPVSICSSSTSLSLPQSFPESPQSPPEGPAQSPLQRPVSSFFSYTLASLLQSSHESPQSPPEGPAQSPLQSPVSSFPSSTSSSLSQSSPVSSFPSSTSSSLSKSSPESPLQSPVISFSSSTSLSPFSEESSSPVDEYTSSSDTLLESDSLTDSESLIESEPLFTYTLDEKVDELARFLLLKYQVKQPITKAEMLTNVISRYTGYFPVIFRKAREFIEILFGISLREVDPDDSYVFVNTLDLTSEGCLSDEQGMSQNRLLILILSIIFIKGTYASEEVIWDVLSGIGVRAGREHFAFGEPRELLTKVWVQEHYLEYREVPNSSPPRYEFLWGPRAHSEVIKRKVVEFLAMLKNTVPITFPSSYKDALKDVEERAQAIIDTTDDSTATESASSSVMSPSFSSE TT9M6NA TT Clinical trial TTBGVF1 ID TTBGVF1 TTBGVF1 TN Candida Chitin synthase 3 (Candi CHS3) TTBGVF1 UP P30573 TTBGVF1 UC CHS3_CANAX TTBGVF1 BC Hexosyltransferase TTBGVF1 SN ClassIV chitin synthase3; ChitinUDP acetylglucosaminyl transferase 3; Chitin synthase 3; CHS3 TTBGVF1 GN Candi CHS3 TTBGVF1 FC Formation and repair ofthe disk-shaped septum in yeast and the cross walls of the hyphal phase. TTBGVF1 EC EC 2.4.1.16 TTBGVF1 SQ MSNFRDSSSPRRGYSEFDPESGEGLGRKKSLIRPERSRMDESHPRFHYTQVANQESNHIKVQPSSTGVDPRKSNELSTSRSHLSNYATPPHQEEEEDEGIPLMDIHNASPNVSSDQNNDLKGGREVYGLNDEINDYGSSPKKNQVISSSRPMNNEKPAKPKHDIYFWKVYCYAITFWAPAPLLKLFGLPTKDRQFAWREKIGLISCILYVGAFVAYLTFGFTKTVCSSQVVRTQINHVNGGYLIINGRAYDLTSSQHPKAAGIQAGSNVLYPPMNAGGKDASFLFQNVNGNCKGLIKPRDNCSIPYDGDELAWYMPCRLFNQDGSTKPNNTFAYYKGWACHTSETARDAYYKLKVNGDVYFTWDDVKNSSRNLVVYSGNVLDLDLINWIETDDVTYPELFDKLRDDETYRGLDISLVLTNSEERQAARCLTEIIKVGSIDTDTIGCIASKVVLYMSLVFILSVVVVKFIMACWFKWVTSRKQGATMYDSKAWAKRNREIEDWVDHDHGIGAEVKTVPVKARANYKAAKTNRQSVFHRAQKLSLGPNADLSQYYDNPNALSKTFKYTTMSTQAALLGRNGYGKRGNNANKSVSGGFNGRQSNLYLTDQGSSTDLLNRPVSSYNPFDSMGDDSIVINGLSPDIIHPDVVPQPPVEYQPFGYPLAHTINLVTCYSEDEEGIRITLDSIATTDYPNSHKLILVICDGIIKGSGNDETTPDIVLDMMSDLTVPRDEVEAYSYVAVAQGSKRHNMAKVYAGFYKYNDETVPPEKQQRIPMITIVKCGTPEEASAPKPGNRGKRDSQIILMSFLQKVVFDERMTSLEYEMLQSIWRITGLMAEFYEIVLMVDADTKVFPDSLTHMVAEMVKDPTIMGLCGETKISNKAQTWVTAIQVFEYYISHHQAKAFESIFGGVTCLPGCFCMYRIKAPKGSDGYWVPILANPDIVERYSDNVVDTLHRKNLLLLGEDRYLSSLMLRTFPTRKQVFVPKAACKTVVPDKFKVLLSQRRRWINSTVHNLFELVLVKDLCGTFCFSMQFVIFIELIGTLVLPAAITFTIYVIIVAIVSKPTPVMSLVLLAVIFGLPGCLIVITVSSLSYLVYFVIYLFALPIWNFVLPSYAYWKFDDFSWGETRTVAGGDKGDHSAVEGKFDSSKIAMKRWREWERERRSTENRKQQQQQQLTNNSSNNLAVPGAAWDPSNTGGNLIDDLSQGSSSGSS TTBGVF1 TT Clinical trial TT96HUR ID TT96HUR TT96HUR TN Cell surface A33 antigen (GPA33) TT96HUR UP Q99795 TT96HUR UC GPA33_HUMAN TT96HUR BC Immunoglobulin TT96HUR SN GPA33; A33 cognate antigen; A33 antigen TT96HUR GN GPA33 TT96HUR FC May play a role in cell-cell recognition and signaling. TT96HUR SQ MVGKMWPVLWTLCAVRVTVDAISVETPQDVLRASQGKSVTLPCTYHTSTSSREGLIQWDKLLLTHTERVVIWPFSNKNYIHGELYKNRVSISNNAEQSDASITIDQLTMADNGTYECSVSLMSDLEGNTKSRVRLLVLVPPSKPECGIEGETIIGNNIQLTCQSKEGSPTPQYSWKRYNILNQEQPLAQPASGQPVSLKNISTDTSGYYICTSSNEEGTQFCNITVAVRSPSMNVALYVGIAVGVVAALIIIGIIIYCCCCRGKDDNTEDKEDARPNREAYEEPPEQLRELSREREEEDDYRQEEQRSTGRESPDHLDQ TT96HUR TT Clinical trial TT6PKBX ID TT6PKBX TT6PKBX TN Claudin-18 (CLDN18) TT6PKBX UP P56856 TT6PKBX UC CLD18_HUMAN TT6PKBX SN UNQ778/PRO1572; Claudin18 TT6PKBX GN CLDN18 TT6PKBX FC Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. TT6PKBX SQ MSTTTCQVVAFLLSILGLAGCIAATGMDMWSTQDLYDNPVTSVFQYEGLWRSCVRQSSGFTECRPYFTILGLPAMLQAVRALMIVGIVLGAIGLLVSIFALKCIRIGSMEDSAKANMTLTSGIMFIVSGLCAIAGVSVFANMLVTNFWMSTANMYTGMGGMVQTVQTRYTFGAALFVGWVAGGLTLIGGVMMCIACRGLAPEETNYKAVSYHASGHSVAYKPGGFKASTGFGSNTKNKKIYDGGARTEDEVQSYPSKHDYV TT6PKBX TT Clinical trial TT6PKBX KE hsa04514:Cell adhesion molecules (CAMs); hsa04530:Tight junction; hsa04670:Leukocyte transendothelial migration; hsa05160:Hepatitis C TT6PKBX RC R-HSA-420029:Tight junction interactions TT64H8L ID TT64H8L TT64H8L TN Clostridium difficile Toxin A (CD toxA) TT64H8L UP P16154 TT64H8L UC TOXA_CLODI TT64H8L SN Toxin A TT64H8L GN CD toxA TT64H8L FC Only after the enteral delivery of the enterotoxin A may the characteristic disease called pseudomembranous colitis be induced. TT64H8L EC EC 3.4.22.- TT64H8L PD 5UQL; 5UQK; 5UMI; 4R04; 4DMW TT64H8L SQ MSLISKEELIKLAYSIRPRENEYKTILTNLDEYNKLTTNNNENKYLQLKKLNESIDVFMNKYKTSSRNRALSNLKKDILKEVILIKNSNTSPVEKNLHFVWIGGEVSDIALEYIKQWADINAEYNIKLWYDSEAFLVNTLKKAIVESSTTEALQLLEEEIQNPQFDNMKFYKKRMEFIYDRQKRFINYYKSQINKPTVPTIDDIIKSHLVSEYNRDETVLESYRTNSLRKINSNHGIDIRANSLFTEQELLNIYSQELLNRGNLAAASDIVRLLALKNFGGVYLDVDMLPGIHSDLFKTISRPSSIGLDRWEMIKLEAIMKYKKYINNYTSENFDKLDQQLKDNFKLIIESKSEKSEIFSKLENLNVSDLEIKIAFALGSVINQALISKQGSYLTNLVIEQVKNRYQFLNQHLNPAIESDNNFTDTTKIFHDSLFNSATAENSMFLTKIAPYLQVGFMPEARSTISLSGPGAYASAYYDFINLQENTIEKTLKASDLIEFKFPENNLSQLTEQEINSLWSFDQASAKYQFEKYVRDYTGGSLSEDNGVDFNKNTALDKNYLLNNKIPSNNVEEAGSKNYVHYIIQLQGDDISYEATCNLFSKNPKNSIIIQRNMNESAKSYFLSDDGESILELNKYRIPERLKNKEKVKVTFIGHGKDEFNTSEFARLSVDSLSNEISSFLDTIKLDISPKNVEVNLLGCNMFSYDFNVEETYPGKLLLSIMDKITSTLPDVNKNSITIGANQYEVRINSEGRKELLAHSGKWINKEEAIMSDLSSKEYIFFDSIDNKLKAKSKNIPGLASISEDIKTLLLDASVSPDTKFILNNLKLNIESSIGDYIYYEKLEPVKNIIHNSIDDLIDEFNLLENVSDELYELKKLNNLDEKYLISFEDISKNNSTYSVRFINKSNGESVYVETEKEIFSKYSEHITKEISTIKNSIITDVNGNLLDNIQLDHTSQVNTLNAAFFIQSLIDYSSNKDVLNDLSTSVKVQLYAQLFSTGLNTIYDSIQLVNLISNAVNDTINVLPTITEGIPIVSTILDGINLGAAIKELLDEHDPLLKKELEAKVGVLAINMSLSIAATVASIVGIGAEVTIFLLPIAGISAGIPSLVNNELILHDKATSVVNYFNHLSESKKYGPLKTEDDKILVPIDDLVISEIDFNNNSIKLGTCNILAMEGGSGHTVTGNIDHFFSSPSISSHIPSLSIYSAIGIETENLDFSKKIMMLPNAPSRVFWWETGAVPGLRSLENDGTRLLDSIRDLYPGKFYWRFYAFFDYAITTLKPVYEDTNIKIKLDKDTRNFIMPTITTNEIRNKLSYSFDGAGGTYSLLLSSYPISTNINLSKDDLWIFNIDNEVREISIENGTIKKGKLIKDVLSKIDINKNKLIIGNQTIDFSGDIDNKDRYIFLTCELDDKISLIIEINLVAKSYSLLLSGDKNYLISNLSNTIEKINTLGLDSKNIAYNYTDESNNKYFGAISKTSQKSIIHYKKDSKNILEFYNDSTLEFNSKDFIAEDINVFMKDDINTITGKYYVDNNTDKSIDFSISLVSKNQVKVNGLYLNESVYSSYLDFVKNSDGHHNTSNFMNLFLDNISFWKLFGFENINFVIDKYFTLVGKTNLGYVEFICDNNKNIDIYFGEWKTSSSKSTIFSGNGRNVVVEPIYNPDTGEDISTSLDFSYEPLYGIDRYINKVLIAPDLYTSLININTNYYSNEYYPEIIVLNPNTFHKKVNINLDSSSFEYKWSTEGSDFILVRYLEESNKKILQKIRIKGILSNTQSFNKMSIDFKDIKKLSLGYIMSNFKSFNSENELDRDHLGFKIIDNKTYYYDEDSKLVKGLININNSLFYFDPIEFNLVTGWQTINGKKYYFDINTGAALTSYKIINGKHFYFNNDGVMQLGVFKGPDGFEYFAPANTQNNNIEGQAIVYQSKFLTLNGKKYYFDNNSKAVTGWRIINNEKYYFNPNNAIAAVGLQVIDNNKYYFNPDTAIISKGWQTVNGSRYYFDTDTAIAFNGYKTIDGKHFYFDSDCVVKIGVFSTSNGFEYFAPANTYNNNIEGQAIVYQSKFLTLNGKKYYFDNNSKAVTGLQTIDSKKYYFNTNTAEAATGWQTIDGKKYYFNTNTAEAATGWQTIDGKKYYFNTNTAIASTGYTIINGKHFYFNTDGIMQIGVFKGPNGFEYFAPANTDANNIEGQAILYQNEFLTLNGKKYYFGSDSKAVTGWRIINNKKYYFNPNNAIAAIHLCTINNDKYYFSYDGILQNGYITIERNNFYFDANNESKMVTGVFKGPNGFEYFAPANTHNNNIEGQAIVYQNKFLTLNGKKYYFDNDSKAVTGWQTIDGKKYYFNLNTAEAATGWQTIDGKKYYFNLNTAEAATGWQTIDGKKYYFNTNTFIASTGYTSINGKHFYFNTDGIMQIGVFKGPNGFEYFAPANTDANNIEGQAILYQNKFLTLNGKKYYFGSDSKAVTGLRTIDGKKYYFNTNTAVAVTGWQTINGKKYYFNTNTSIASTGYTIISGKHFYFNTDGIMQIGVFKGPDGFEYFAPANTDANNIEGQAIRYQNRFLYLHDNIYYFGNNSKAATGWVTIDGNRYYFEPNTAMGANGYKTIDNKNFYFRNGLPQIGVFKGSNGFEYFAPANTDANNIEGQAIRYQNRFLHLLGKIYYFGNNSKAVTGWQTINGKVYYFMPDTAMAAAGGLFEIDGVIYFFGVDGVKAPGIYG TT64H8L TT Clinical trial TTAXGIP ID TTAXGIP TTAXGIP TN Coagulation factor XIII (F13B) TTAXGIP UP P05160 TTAXGIP UC F13B_HUMAN TTAXGIP BC Acyltransferase TTAXGIP SN F13B TTAXGIP GN F13B TTAXGIP FC Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl- epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. TTAXGIP SQ MRLKNLTFIIILIISGELYAEEKPCGFPHVENGRIAQYYYTFKSFYFPMSIDKKLSFFCLAGYTTESGRQEEQTTCTTEGWSPEPRCFKKCTKPDLSNGYISDVKLLYKIQENMRYGCASGYKTTGGKDEEVVQCLSDGWSSQPTCRKEHETCLAPELYNGNYSTTQKTFKVKDKVQYECATGYYTAGGKKTEEVECLTYGWSLTPKCTKLKCSSLRLIENGYFHPVKQTYEEGDVVQFFCHENYYLSGSDLIQCYNFGWYPESPVCEGRRNRCPPPPLPINSKIQTHSTTYRHGEIVHIECELNFEIHGSAEIRCEDGKWTEPPKCIEGQEKVACEEPPFIENGAANLHSKIYYNGDKVTYACKSGYLLHGSNEITCNRGKWTLPPECVENNENCKHPPVVMNGAVADGILASYATGSSVEYRCNEYYLLRGSKISRCEQGKWSSPPVCLEPCTVNVDYMNRNNIEMKWKYEGKVLHGDLIDFVCKQGYDLSPLTPLSELSVQCNRGEVKYPLCTRKESKGMCTSPPLIKHGVIISSTVDTYENGSSVEYRCFDHHFLEGSREAYCLDGMWTTPPLCLEPCTLSFTEMEKNNLLLKWDFDNRPHILHGEYIEFICRGDTYPAELYITGSILRMQCDRGQLKYPRCIPRQSTLSYQEPLRT TTAXGIP TT Clinical trial TTAXGIP KE hsa04610:Complement and coagulation cascades TTAXGIP RC R-HSA-140875:Common Pathway of Fibrin Clot Formation TTUW6OP ID TTUW6OP TTUW6OP TN Complement factor H (CFH) TTUW6OP UP P08603 TTUW6OP UC CFAH_HUMAN TTUW6OP SN HF2; HF1; HF; H factor 1 TTUW6OP GN CFH TTUW6OP FC Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces. Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop. As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited C3b. In addition, mediates several cellular responses through interaction with specific receptors. For example, interacts with CR3/ITGAM receptor and thereby mediates the adhesion of human neutrophils to different pathogens. In turn, these pathogens are phagocytosed and destroyed. TTUW6OP PD 6ATG; 5WTB; 5O35; 5O32; 5NBQ TTUW6OP SQ MRLLAKIICLMLWAICVAEDCNELPPRRNTEILTGSWSDQTYPEGTQAIYKCRPGYRSLGNVIMVCRKGEWVALNPLRKCQKRPCGHPGDTPFGTFTLTGGNVFEYGVKAVYTCNEGYQLLGEINYRECDTDGWTNDIPICEVVKCLPVTAPENGKIVSSAMEPDREYHFGQAVRFVCNSGYKIEGDEEMHCSDDGFWSKEKPKCVEISCKSPDVINGSPISQKIIYKENERFQYKCNMGYEYSERGDAVCTESGWRPLPSCEEKSCDNPYIPNGDYSPLRIKHRTGDEITYQCRNGFYPATRGNTAKCTSTGWIPAPRCTLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDGWSPAVPCLRKCYFPYLENGYNQNYGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSPTPRCIRVKTCSKSSIDIENGFISESQYTYALKEKAKYQCKLGYVTADGETSGSITCGKDGWSAQPTCIKSCDIPVFMNARTKNDFTWFKLNDTLDYECHDGYESNTGSTTGSIVCGYNGWSDLPICYERECELPKIDVHLVPDRKKDQYKVGEVLKFSCKPGFTIVGPNSVQCYHFGLSPDLPICKEQVQSCGPPPELLNGNVKEKTKEEYGHSEVVEYYCNPRFLMKGPNKIQCVDGEWTTLPVCIVEESTCGDIPELEHGWAQLSSPPYYYGDSVEFNCSESFTMIGHRSITCIHGVWTQLPQCVAIDKLKKCKSSNLIILEEHLKNKKEFDHNSNIRYRCRGKEGWIHTVCINGRWDPEVNCSMAQIQLCPPPPQIPNSHNMTTTLNYRDGEKVSVLCQENYLIQEGEEITCKDGRWQSIPLCVEKIPCSQPPQIEHGTINSSRSSQESYAHGTKLSYTCEGGFRISEENETTCYMGKWSSPPQCEGLPCKSPPEISHGVVAHMSDSYQYGEEVTYKCFEGFGIDGPAIAKCLGEKWSHPPSCIKTDCLSLPSFENAIPMGEKKDVYKAGEQVTYTCATYYKMDGASNVTCINSRWTGRPTCRDTSCVNPPTVQNAYIVSRQMSKYPSGERVRYQCRSPYEMFGDEEVMCLNGNWTEPPQCKDSTGKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKCLHPCVISREIMENYNIALRWTAKQKLYSRTGESVEFVCKRGYRLSSRSHTLRTTCWDGKLEYPTCAKR TTUW6OP TT Clinical trial TTUW6OP FM Complement system TTUW6OP KE hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection TTUW6OP RC R-HSA-977606:Regulation of Complement cascade TT0HUN7 ID TT0HUN7 TT0HUN7 TN Complement receptor type 2 (CD21) TT0HUN7 UP P20023 TT0HUN7 UC CR2_HUMAN TT0HUN7 SN EpsteinBarr virus receptor; Epstein-Barr virus receptor; EBV receptor; Cr2; Complement C3d receptor; C3DR TT0HUN7 GN CR2 TT0HUN7 FC Participates in B lymphocytes activation. Receptor for complement C3, for the Epstein-Barr virus on human B-cells and T-cells and for HNRNPU. TT0HUN7 PD 3OED; 2GSX; 2ATY; 1W2S; 1W2R TT0HUN7 SQ MGAAGLLGVFLALVAPGVLGISCGSPPPILNGRISYYSTPIAVGTVIRYSCSGTFRLIGEKSLLCITKDKVDGTWDKPAPKCEYFNKYSSCPEPIVPGGYKIRGSTPYRHGDSVTFACKTNFSMNGNKSVWCQANNMWGPTRLPTCVSVFPLECPALPMIHNGHHTSENVGSIAPGLSVTYSCESGYLLVGEKIINCLSSGKWSAVPPTCEEARCKSLGRFPNGKVKEPPILRVGVTANFFCDEGYRLQGPPSSRCVIAGQGVAWTKMPVCEEIFCPSPPPILNGRHIGNSLANVSYGSIVTYTCDPDPEEGVNFILIGESTLRCTVDSQKTGTWSGPAPRCELSTSAVQCPHPQILRGRMVSGQKDRYTYNDTVIFACMFGFTLKGSKQIRCNAQGTWEPSAPVCEKECQAPPNILNGQKEDRHMVRFDPGTSIKYSCNPGYVLVGEESIQCTSEGVWTPPVPQCKVAACEATGRQLLTKPQHQFVRPDVNSSCGEGYKLSGSVYQECQGTIPWFMEIRLCKEITCPPPPVIYNGAHTGSSLEDFPYGTTVTYTCNPGPERGVEFSLIGESTIRCTSNDQERGTWSGPAPLCKLSLLAVQCSHVHIANGYKISGKEAPYFYNDTVTFKCYSGFTLKGSSQIRCKADNTWDPEIPVCEKETCQHVRQSLQELPAGSRVELVNTSCQDGYQLTGHAYQMCQDAENGIWFKKIPLCKVIHCHPPPVIVNGKHTGMMAENFLYGNEVSYECDQGFYLLGEKKLQCRSDSKGHGSWSGPSPQCLRSPPVTRCPNPEVKHGYKLNKTHSAYSHNDIVYVDCNPGFIMNGSRVIRCHTDNTWVPGVPTCIKKAFIGCPPPPKTPNGNHTGGNIARFSPGMSILYSCDQGYLLVGEALLLCTHEGTWSQPAPHCKEVNCSSPADMDGIQKGLEPRKMYQYGAVVTLECEDGYMLEGSPQSQCQSDHQWNPPLAVCRSRSLAPVLCGIAAGLILLTFLIVITLYVISKHRARNYYTDTSQKEAFHLEAREVYSVDPYNPAS TT0HUN7 TT Clinical trial TT0HUN7 KE hsa04610:Complement and coagulation cascades; hsa04640:Hematopoietic cell lineage; hsa04662:B cell receptor signaling pathway; hsa05169:Epstein-Barr virus infection TTCJVNE ID TTCJVNE TTCJVNE TN CTGF messenger RNA (CTGF mRNA) TTCJVNE UP P29279 TTCJVNE UC CTGF_HUMAN TTCJVNE BC mRNA target TTCJVNE SN Long (mRNA); Insulin-like growth factor-binding protein 8 (mRNA); IGFBP8 (mRNA); IGFBP-8 (mRNA); IGF-binding protein 8 (mRNA); IBP-8 (mRNA); Hypertrophic chondrocyte-specific protein 24 (mRNA); HCS24 (mRNA); Connective tissue growth factor (mRNA); CCN2 (mRNA); CCN family member 2 (mRNA) TTCJVNE GN CTGF TTCJVNE FC Promotes proliferation and differentiation of chondrocytes. Mediates heparin- and divalent cation-dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells. Enhances fibroblast growth factor-induced DNA synthesis. Major connective tissue mitoattractant secreted by vascular endothelial cells. TTCJVNE SQ MTAASMGPVRVAFVVLLALCSRPAVGQNCSGPCRCPDEPAPRCPAGVSLVLDGCGCCRVCAKQLGELCTERDPCDPHKGLFCHFGSPANRKIGVCTAKDGAPCIFGGTVYRSGESFQSSCKYQCTCLDGAVGCMPLCSMDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKDQTVVGPALAAYRLEDTFGPDPTMIRANCLVQTTEWSACSKTCGMGISTRVTNDNASCRLEKQSRLCMVRPCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSMKTYRAKFCGVCTDGRCCTPHRTTTLPVEFKCPDGEVMKKNMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA TTCJVNE TT Clinical trial TTCJVNE FM mRNA target TTCJVNE KE hsa04390:Hippo signaling pathway TTCJVNE RC R-HSA-1989781:PPARA activates gene expression; R-HSA-2032785:YAP1- and WWTR1 (TAZ)-stimulated gene expression TTRK0B9 ID TTRK0B9 TTRK0B9 TN C-type natriuretic peptide (NPPC) TTRK0B9 UP P23582 TTRK0B9 UC ANFC_HUMAN TTRK0B9 BC C-type natriuretic peptide TTRK0B9 SN NPPC; Ctype natriuretic peptide; CNP53 TTRK0B9 GN NPPC TTRK0B9 FC Hormone which plays a role in endochondral ossification through regulation of cartilaginous growth plate chondrocytes proliferation and differentiation. May also be vasoactive and natriuretic. Specifically binds and stimulates the cGMP production of the NPR2 receptor. Binds the clearance receptor NPR3. TTRK0B9 PD 1JDP TTRK0B9 SQ MHLSQLLACALLLTLLSLRPSEAKPGAPPKVPRTPPAEELAEPQAAGGGQKKGDKAPGGGGANLKGDRSRLLRDLRVDTKSRAAWARLLQEHPNARKYKGANKKGLSKGCFGLKLDRIGSMSGLGC TTRK0B9 TT Clinical trial TTUR18Y ID TTUR18Y TTUR18Y TN Cytomegalovirus Glycoprotein B (CMV gB) TTUR18Y UP P06473 TTUR18Y UC GB_HCMVA TTUR18Y BC Hepacivirus polyprotein TTUR18Y SN gB; Envelope glycoprotein B TTUR18Y GN CMV gB TTUR18Y FC Viral ligand for CD209/DC-SIGN. This interaction allows capture of viral particles by dendritic (DCs) cells and subsequent virus transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they entrap pathogens and convey them to local lymphoid tissue or lymph node for establishment of immunity. CMV subverts the migration properties of dendritic cells to gain access to target organs or susceptible cells. TTUR18Y PD 5CXF TTUR18Y SQ MESRIWCLVVCVNLCIVCLGAAVSSSSTSHATSSTHNGSHTSRTTSAQTRSVYSQHVTSSEAVSHRANETIYNTTLKYGDVVGVNTTKYPYRVCSMAQGTDLIRFERNIICTSMKPINEDLDEGIMVVYKRNIVAHTFKVRVYQKVLTFRRSYAYIYTTYLLGSNTEYVAPPMWEIHHINKFAQCYSSYSRVIGGTVFVAYHRDSYENKTMQLIPDDYSNTHSTRYVTVKDQWHSRGSTWLYRETCNLNCMLTITTARSKYPYHFFATSTGDVVYISPFYNGTNRNASYFGENADKFFIFPNYTIVSDFGRPNAAPETHRLVAFLERADSVISWDIQDEKNVTCQLTFWEASERTIRSEAEDSYHFSSAKMTATFLSKKQEVNMSDSALDCVRDEAINKLQQIFNTSYNQTYEKYGNVSVFETSGGLVVFWQGIKQKSLVELERLANRSSLNITHRTRRSTSDNNTTHLSSMESVHNLVYAQLQFTYDTLRGYINRALAQIAEAWCVDQRRTLEVFKELSKINPSAILSAIYNKPIAARFMGDVLGLASCVTINQTSVKVLRDMNVKESPGRCYSRPVVIFNFANSSYVQYGQLGEDNEILLGNHRTEECQLPSLKIFIAGNSAYEYVDYLFKRMIDLSSISTVDSMIALDIDPLENTDFRVLELYSQKELRSSNVFDLEEIMREFNSYKQRVKYVEDKVVDPLPPYLKGLDDLMSGLGAAGKAVGVAIGAVGGAVASVVEGVATFLKNPFGAFTIILVAIAVVIITYLIYTRQRRLCTQPLQNLFPYLVSADGTTVTSGSTKDTSLQAPPSYEESVYNSGRKGPGPPSSDASTAAPPYTNEQAYQMLLALARLDAEQRAQQNGTDSLDGQTGTQDKGQKPNLLDRLRHRKNGYRHLKDSDEEENV TTUR18Y TT Clinical trial TTV23LH ID TTV23LH TTV23LH TN Delta-like protein 4 (DLL4) TTV23LH UP Q9NR61 TTV23LH UC DLL4_HUMAN TTV23LH SN UNQ1895/PRO4341; Drosophila Delta homolog 4; Deltalike protein 4; Delta4 TTV23LH GN DLL4 TTV23LH FC Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Essential for retinal progenitor proliferation. Required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types. During spinal cord neurogenesis, inhibits V2a interneuron fate. Involved in the Notch signaling pathway as Notch ligand. TTV23LH PD 5MVX TTV23LH SQ MAAASRSASGWALLLLVALWQQRAAGSGVFQLQLQEFINERGVLASGRPCEPGCRTFFRVCLKHFQAVVSPGPCTFGTVSTPVLGTNSFAVRDDSSGGGRNPLQLPFNFTWPGTFSLIIEAWHAPGDDLRPEALPPDALISKIAIQGSLAVGQNWLLDEQTSTLTRLRYSYRVICSDNYYGDNCSRLCKKRNDHFGHYVCQPDGNLSCLPGWTGEYCQQPICLSGCHEQNGYCSKPAECLCRPGWQGRLCNECIPHNGCRHGTCSTPWQCTCDEGWGGLFCDQDLNYCTHHSPCKNGATCSNSGQRSYTCTCRPGYTGVDCELELSECDSNPCRNGGSCKDQEDGYHCLCPPGYYGLHCEHSTLSCADSPCFNGGSCRERNQGANYACECPPNFTGSNCEKKVDRCTSNPCANGGQCLNRGPSRMCRCRPGFTGTYCELHVSDCARNPCAHGGTCHDLENGLMCTCPAGFSGRRCEVRTSIDACASSPCFNRATCYTDLSTDTFVCNCPYGFVGSRCEFPVGLPPSFPWVAVSLGVGLAVLLVLLGMVAVAVRQLRLRRPDDGSREAMNNLSDFQKDNLIPAAQLKNTNQKKELEVDCGLDKSNCGKQQNHTLDYNLAPGPLGRGTMPGKFPHSDKSLGEKAPLRLHSEKPECRISAICSPRDSMYQSVCLISEERNECVIATEV TTV23LH TT Clinical trial TTV23LH FM Delta serrate TTV23LH KE hsa04330:Notch signaling pathway TTV23LH RC R-HSA-2122948:Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2660826:Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant; R-HSA-2691232:Constitutive Signaling by NOTCH1 HD Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-2979096:NOTCH2 Activation and Transmission of Signal to the Nucleus TTY2ZV6 ID TTY2ZV6 TTY2ZV6 TN Dickkopf-related protein 3 (DKK3) TTY2ZV6 UP Q9UBP4 TTY2ZV6 UC DKK3_HUMAN TTY2ZV6 BC Dickkopf protein TTY2ZV6 SN hDkk-3; UNQ258/PRO295; REIC; Dkk-3; Dickkopf-3 TTY2ZV6 GN DKK3 TTY2ZV6 FC DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. TTY2ZV6 SQ MQRLGATLLCLLLAAAVPTAPAPAPTATSAPVKPGPALSYPQEEATLNEMFREVEELMEDTQHKLRSAVEEMEAEEAAAKASSEVNLANLPPSYHNETNTDTKVGNNTIHVHREIHKITNNQTGQMVFSETVITSVGDEEGRRSHECIIDEDCGPSMYCQFASFQYTCQPCRGQRMLCTRDSECCGDQLCVWGHCTKMATRGSNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPASRLLDLITWELEPDGALDRCPCASGLLCQPHSHSLVYVCKPTFVGSRDQDGEILLPREVPDEYEVGSFMEEVRQELEDLERSLTEEMALREPAAAAAALLGGEEI TTY2ZV6 TT Clinical trial TTVJDNB ID TTVJDNB TTVJDNB TN E2F transcription factor 1 (E2F1) TTVJDNB UP Q01094 TTVJDNB UC E2F1_HUMAN TTVJDNB SN pRB-binding protein E2F-1; Transcription factor E2F1; Retinoblastoma-binding protein 3; Retinoblastoma-associated protein 1; RBBP3; RBBP-3; RBAP-1; PBR3; E2F-1 TTVJDNB GN E2F1 TTVJDNB FC The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters. Positively regulates transcription of RRP1B. Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. TTVJDNB PD 6G0P; 5M9O; 5M9N; 2AZE; 1O9K TTVJDNB SQ MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF TTVJDNB TT Clinical trial TTVJDNB KE hsa04110:Cell cycle; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer TTVJDNB RC R-HSA-111448:Activation of NOXA and translocation to mitochondria; R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-139915:Activation of PUMA and translocation to mitochondria; R-HSA-1538133:G0 and Early G1; R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559585:Oncogene Induced Senescence; R-HSA-68689:CDC6 association with the ORC:origin complex; R-HSA-68911:G2 Phase; R-HSA-69205:G1/S-Specific Transcription; R-HSA-69231:Cyclin D associated events in G1; R-HSA-69298:Association of licensing factors with the pre-replicative complex TTUQREN ID TTUQREN TTUQREN TN Early growth response protein 1 (EGR-1) TTUQREN UP P18146 TTUQREN UC EGR1_HUMAN TTUQREN BC EGR C2H2-type zinc-finger TTUQREN SN Zinc finger protein Krox24; Zinc finger protein Krox-24; Zinc finger protein 225; ZNF225; Transcription factor Zif268; Transcription factor ETR103; Nerve growth factorinduced protein A; Nerve growth factor-induced protein A; NGFIA; NGFI-A; KROX24; AT225 TTUQREN GN EGR1 TTUQREN FC Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes. Binds double-stranded target DNA, irrespective of the cytosine methylation status. Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia. Plays a role in the regulation of cell survival, proliferation and cell death. Activates expression of p53/TP53 and TGFB1, and thereby helps prevent tumor formation. Required for normal progress through mitosis and normal proliferation of hepatocytes after partial hepatectomy. Mediates responses to ischemia and hypoxia; regulates the expression of proteins such as IL1B and CXCL2 that are involved in inflammatory processes and development of tissue damage after ischemia. Regulates biosynthesis of luteinizing hormone (LHB) in the pituitary. Regulates the amplitude of the expression rhythms of clock genes: ARNTL/BMAL1, PER2 and NR1D1 in the liver via the activation of PER1 (clock repressor) transcription. Regulates the rhythmic expression of core-clock gene ARNTL/BMAL1 in the suprachiasmatic nucleus (SCN). Transcriptional regulator. TTUQREN PD 5N14; 4X9J; 4R2D; 4R2C; 4R2A TTUQREN SQ MAAAKAEMQLMSPLQISDPFGSFPHSPTMDNYPKLEEMMLLSNGAPQFLGAAGAPEGSGSNSSSSSSGGGGGGGGGSNSSSSSSTFNPQADTGEQPYEHLTAESFPDISLNNEKVLVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPASSSSAPSPAASSASASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPAAKGGFQVPMIPDYLFPQQQGDLGLGTPDQKPFQGLESRTQQPSLTPLSTIKAFATQSGSQDLKALNTSYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKADKSVVASSATSSLSSYPSPVATSYPSPVTTSYPSPATTSYPSPVPTSFSSPGSSTYPSPVHSGFPSPSVATTYSSVPPAFPAQVSSFPSSAVTNSFSASTGLSDMTATFSPRTIEIC TTUQREN TT Clinical trial TTUQREN FM EGR C2H2-type zinc-finger TTDJLWQ ID TTDJLWQ TTDJLWQ TN Ebola virus VP24 messenger RNA (EV VP24 mRNA) TTDJLWQ UP Q5XX02 TTDJLWQ UC VP24_EBOSU TTDJLWQ BC mRNA target TTDJLWQ SN rVP24 (mRNA); VP24 (mRNA); Reston VP24 (mRNA); Membrane-associated protein VP24 (mRNA) TTDJLWQ GN EV VP24 mRNA TTDJLWQ FC Blocks the IFN-induced nuclear accumulation of host phosphorylated STAT1, by interacting with the STAT1-binding region of host importin alpha-1/KPNA1 protein, thereby inhibiting the latter. Without the activity of this protein, activated STAT1 would not enter the nucleus and be unable to activate IFN-induced genes. Plays a role in assembly of viral nucleocapsid and virion budding. May act as a minor matrix protein that plays a role in assembly of viral nucleocapsid and virion budding. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways. TTDJLWQ PD 3VNF; 3VNE TTDJLWQ SQ MAKATGRYNLVTPKRELEQGVVFSDLCNFLVTPTVQGWKVYWAGLEFDVNQKGITLLNRLKVNDFAPAWAMTRNLFPHLFKNQQSEVQTPIWALRVILAAGILDQLMDHSLIEPLSGALNLIADWLLTTSTNHFNMRTQRVKDQLSMRMLSLIRSNIINFINKLETLHVVNYKGLLSSVEIGTPSYAIIITRTNMGYLVEVQEPDKSAMDIRHPGPVKFSLLHESTLKPVATPKPSSITSLIMEFNSSLAI TTDJLWQ TT Clinical trial TTDJLWQ FM mRNA target TTB30LE ID TTB30LE TTB30LE TN Endoglin CD105 (ENG) TTB30LE UP P17813 TTB30LE UC EGLN_HUMAN TTB30LE SN Endoglin; END; CD105 TTB30LE GN ENG TTB30LE FC Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis. Required for normal structure and integrity of adult vasculature. Regulates the migration of vascular endothelial cells. Required for normal extraembryonic angiogenesis and for embryonic heart development (By similarity). May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (By similarity). May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors. Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors. Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3. TTB30LE PD 5I04; 5HZW; 5HZV TTB30LE SQ MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTYTTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVLSVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPITSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLEGVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLIDANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPLASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKELVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNILSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSEFLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPIPKTGTLSCTVALRPKTGSQDQEVHRTVFMRLNIISPDLSGCTSKGLVLPAVLGITFGAFLIGALLTAALWYIYSHTRSPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA TTB30LE TT Clinical trial TT63DI9 ID TT63DI9 TT63DI9 TN Endostatin (COL18A1) TT63DI9 UP P39060 TT63DI9 UC COIA1_HUMAN TT63DI9 SN Collagen alpha1(XVIII) chain; Collagen alpha-1(XVIII) chain TT63DI9 GN COL18A1 TT63DI9 FC Probably plays a major role in determining the retinal structure as well as in the closure of the neural tube. TT63DI9 PD 3HSH; 3HON; 1BNL TT63DI9 SQ MAPYPCGCHILLLLFCCLAAARANLLNLNWLWFNNEDTSHAATTIPEPQGPLPVQPTADTTTHVTPRNGSTEPATAPGSPEPPSELLEDGQDTPTSAESPDAPEENIAGVGAEILNVAKGIRSFVQLWNDTVPTESLARAETLVLETPVGPLALAGPSSTPQENGTTLWPSRGIPSSPGAHTTEAGTLPAPTPSPPSLGRPWAPLTGPSVPPPSSGRASLSSLLGGAPPWGSLQDPDSQGLSPAAAAPSQQLQRPDVRLRTPLLHPLVMGSLGKHAAPSAFSSGLPGALSQVAVTTLTRDSGAWVSHVANSVGPGLANNSALLGADPEAPAGRCLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQFCEALQDACWSRLGGGRLPVACASLPTQEDGYCVLIGPAAERISEEVGLLQLLGDPPPQQVTQTDDPDVGLAYVFGPDANSGQVARYHFPSLFFRDFSLLFHIRPATEGPGVLFAITDSAQAMVLLGVKLSGVQDGHQDISLLYTEPGAGQTHTAASFRLPAFVGQWTHLALSVAGGFVALYVDCEEFQRMPLARSSRGLELEPGAGLFVAQAGGADPDKFQGVIAELKVRRDPQVSPMHCLDEEGDDSDGASGDSGSGLGDARELLREETGAALKPRLPAPPPVTTPPLAGGSSTEDSRSEEVEEQTTVASLGAQTLPGSDSVSTWDGSVRTPGGRVKEGGLKGQKGEPGVPGPPGRAGPPGSPCLPGPPGLPCPVSPLGPAGPALQTVPGPQGPPGPPGRDGTPGRDGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPGVGERGPPGPQGPPGPPGPSFRHDKLTFIDMEGSGFGGDLEALRGPRGFPGPPGPPGVPGLPGEPGRFGVNSSDVPGPAGLPGVPGREGPPGFPGLPGPPGPPGREGPPGRTGQKGSLGEAGAPGHKGSKGAPGPAGARGESGLAGAPGPAGPPGPPGPPGPPGPGLPAGFDDMEGSGGPFWSTARSADGPQGPPGLPGLKGDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDPGKDGVGQPGLPGPPGPPGPVVYVSEQDGSVLSVPGPEGRPGFAGFPGPAGPKGNLGSKGERGSPGPKGEKGEPGSIFSPDGGALGPAQKGAKGEPGFRGPPGPYGRPGYKGEIGFPGRPGRPGMNGLKGEKGEPGDASLGFGMRGMPGPPGPPGPPGPPGTPVYDSNVFAESSRPGPPGLPGNQGPPGPKGAKGEVGPPGPPGQFPFDFLQLEAEMKGEKGDRGDAGQKGERGEPGGGGFFGSSLPGPPGPPGPPGPRGYPGIPGPKGESIRGQPGPPGPQGPPGIGYEGRQGPPGPPGPPGPPSFPGPHRQTISVPGPPGPPGPPGPPGTMGASSGVRLWATRQAMLGQVHEVPEGWLIFVAEQEELYVRVQNGFRKVQLEARTPLPRGTDNEVAALQPPVVQLHDSNPYPRREHPHPTARPWRADDILASPPRLPEPQPYPGAPHHSSYVHLRPARPTSPPAHSHRDFQPVLHLVALNSPLSGGMRGIRGADFQCFQQARAVGLAGTFRAFLSSRLQDLYSIVRRADRAAVPIVNLKDELLFPSWEALFSGSEGPLKPGARIFSFDGKDVLRHPTWPQKSVWHGSDPNGRRLTESYCETWRTEAPSATGQASSLLGGRLLGQSAASCHHAYIVLCIENSFMTASK TT63DI9 TT Clinical trial TT63DI9 KE hsa04974:Protein digestion and absorption TT63DI9 RC R-HSA-1442490:Collagen degradation; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-1650814:Collagen biosynthesis and modifying enzymes; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000157:Laminin interactions TTNJA0C ID TTNJA0C TTNJA0C TN Enhancer of zeste homolog 1 (EZH1) TTNJA0C UP Q92800 TTNJA0C UC EZH1_HUMAN TTNJA0C BC Methyltransferase TTNJA0C SN KIAA0388; Histone-lysine N-methyltransferase EZH1; ENX-2 TTNJA0C GN EZH1 TTNJA0C FC Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH2-containing complexes, it is less abundant in embryonic stem cells, has weak methyltransferase activity and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. Polycomb group (PcG) protein. TTNJA0C EC EC 2.1.1.43 TTNJA0C SQ MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELVDALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAIASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGRRRRRHHIVSASCSNASASAVAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPPQLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILKLPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNSSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEKFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVL TTNJA0C TT Clinical trial TTBK351 ID TTBK351 TTBK351 TN Epstein-Barr virus Latent membrane protein 2 (EBV LMP2) TTBK351 UP P13285 TTBK351 UC LMP2_EBVB9 TTBK351 BC Herpesviridae LMP-2 TTBK351 SN Terminal protein; Latent membrane protein 2 TTBK351 GN EBV LMP2 TTBK351 FC Isoform LMP2B may be a negative regulator of isoform LMP2A. TTBK351 PD 5GSD; 5GRD; 3REW; 3BVN; 2JO9 TTBK351 SQ MGSLEMVPMGAGPPSPGGDPDGYDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQDQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALSLLLLAAVASSYAAAQRKLLTPVTVLTAVVTFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWRRLTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAALLTLAAALALLASLILGTLNLTTMFLLMLLWTLVVLLICSSCSSCPLSKILLARLFLYALALLLLASALIAGGSILQTNFKSLSSTEFIPNLFCMLLLIVAGILFILAILTEWGSGNRTYGPVFMCLGGLLTMVAGAVWLTVMSNTLLSAWILTAGFLIFLIGFALFGVIRCCRYCCYYCLTLESEERPPTPYRNTV TTBK351 TT Clinical trial TTWFBT7 ID TTWFBT7 TTWFBT7 TN Extracellular matrix receptor III (CD44) TTWFBT7 UP P16070 TTWFBT7 UC CD44_HUMAN TTWFBT7 SN Phagocytic glycoprotein I; Phagocytic glycoprotein 1; PGP-I; PGP-1; MIC4; MDU3; MDU2; LHR; Hyaluronate receptor; Hermes antigen; Heparan sulfate proteoglycan; HUTCH-I; GP90 lymphocyte homing/adhesion receptor; Extracellular matrix receptor-III; Epican; ECMR-III; CDw44; CD44 antigen TTWFBT7 GN CD44 TTWFBT7 FC Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion. Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. TTWFBT7 PD 4PZ4; 4PZ3; 2I83; 1UUH; 1POZ TTWFBT7 SQ MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSSGSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSNTISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEASKSQEMVHLVNKESSETPDQFMTADETRNLQNVDMKIGV TTWFBT7 TT Clinical trial TTWFBT7 FM Transmembrane protein TTWFBT7 KE hsa04512:ECM-receptor interaction; hsa04640:Hematopoietic cell lineage; hsa05131:Shigellosis; hsa05169:Epstein-Barr virus infection; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer TTWFBT7 RC R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-216083:Integrin cell surface interactions; R-HSA-2160916:Hyaluronan uptake and degradation; R-HSA-877300:Interferon gamma signaling TTETDKQ ID TTETDKQ TTETDKQ TN Facilitates chromatin transcription complex (FACT) TTETDKQ UP Q08945 TTETDKQ UC SSRP1_HUMAN TTETDKQ SN hSSRP1; T160; Structure-specific recognition protein 1; Recombination signal sequence recognition protein 1; Facilitates chromatin transcription complex subunit SSRP1; Facilitates chromatin transcription complex 80 kDa subunit; FACTp80; FACT80; FACT complex subunit SSRP1; FACT 80 kDa subunit; Chromatin-specific transcription elongation factor 80 kDa subunit TTETDKQ GN SSRP1 TTETDKQ FC The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63. Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. TTETDKQ PD 5VWE; 5UMS; 5UMR; 4IFS TTETDKQ SQ MAETLEFNDVYQEVKGSMNDGRLRLSRQGIIFKNSKTGKVDNIQAGELTEGIWRRVALGHGLKLLTKNGHVYKYDGFRESEFEKLSDFFKTHYRLELMEKDLCVKGWNWGTVKFGGQLLSFDIGDQPVFEIPLSNVSQCTTGKNEVTLEFHQNDDAEVSLMEVRFYVPPTQEDGVDPVEAFAQNVLSKADVIQATGDAICIFRELQCLTPRGRYDIRIYPTFLHLHGKTFDYKIPYTTVLRLFLLPHKDQRQMFFVISLDPPIKQGQTRYHFLILLFSKDEDISLTLNMNEEEVEKRFEGRLTKNMSGSLYEMVSRVMKALVNRKITVPGNFQGHSGAQCITCSYKASSGLLYPLERGFIYVHKPPVHIRFDEISFVNFARGTTTTRSFDFEIETKQGTQYTFSSIEREEYGKLFDFVNAKKLNIKNRGLKEGMNPSYDEYADSDEDQHDAYLERMKEEGKIREENANDSSDDSGEETDESFNPGEEEEDVAEEFDSNASASSSSNEGDSDRDEKKRKQLKKAKMAKDRKSRKKPVEVKKGKDPNAPKRPMSAYMLWLNASREKIKSDHPGISITDLSKKAGEIWKGMSKEKKEEWDRKAEDARRDYEKAMKEYEGGRGESSKRDKSKKKKKVKVKMEKKSTPSRGSSSKSSSRQLSESFKSKEFVSSDESSSGENKSKKKRRRSEDSEEEELASTPPSSEDSASGSDE TTETDKQ TT Clinical trial TTETDKQ FM Metallopeptidase family M24 TTSTRZY ID TTSTRZY TTSTRZY TN Filamin A (FLNA) TTSTRZY UP P21333 TTSTRZY UC FLNA_HUMAN TTSTRZY BC Dystrophin protein TTSTRZY SN Nonmuscle filamin; Non-muscle filamin; Filamin-A; Filamin-1; Filamin 1; FLN1; FLN-A; FLN; Endothelial actin-binding protein; Endothelial actin cytoskeleton; Alpha-filamin; Actin-binding protein 280; ABP-280 TTSTRZY GN FLNA TTSTRZY FC Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking. Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance. Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. TTSTRZY PD 6EW1; 6D8C; 5XR1; 4P3W; 4M9P TTSTRZY SQ MSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLFAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSPFSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKVEPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQCYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKVPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTALAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHCDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPRLVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGSPYRVVVP TTSTRZY TT Clinical trial TTSTRZY FM Filamin family TT0FYAN ID TT0FYAN TT0FYAN TN Free fatty acid receptor 2 (FFAR2) TT0FYAN UP O15552 TT0FYAN UC FFAR2_HUMAN TT0FYAN BC GPCR rhodopsin TT0FYAN SN Gprotein coupled receptor 43; FFAR2 TT0FYAN GN FFAR2 TT0FYAN FC G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins but also to the Gq family (PubMed:12496283, PubMed:12711604, PubMed:23589301). Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. May play a role in glucose homeostasis by regulating the secretion of GLP-1, in response to short-chain fatty acids accumulating in the intestine. May also regulate the production of LEP/Leptin, a hormone acting on the central nervous system to inhibit food intake. Finally, may also regulate whole-body energy homeostasis through adipogenesis regulating both differentiation and lipid storage of adipocytes. In parallel to its role in energy homeostasis, may also mediate the activation of the inflammatory and immune responses by SCFA in the intestine, regulating the rapid production of chemokines and cytokines. May also play a role in the resolution of the inflammatory response and control chemotaxis in neutrophils. In addition to SCFAs, may also be activated by the extracellular lectin FCN1 in a process leading to activation of monocytes and inducing the secretion of interleukin- 8/IL-8 in response to the presence of microbes (PubMed:21037097). Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably acetate, propionate and butyrate (PubMed:12496283, PubMed:12711604). Exhibits a SCFA- independent constitutive G protein-coupled receptor activity (PubMed:23066016). TT0FYAN SQ MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKVVCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGNEITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQPLVGAQRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQVLRNQGSSLLGRRGKDTAEGTNEDRGVGQGEGMPSSDFTTE TT0FYAN TT Clinical trial TT0FYAN KE hsa04024:cAMP signaling pathway TT0FYAN RC R-HSA-416476:G alpha (q) signalling events TTUPAD7 ID TTUPAD7 TTUPAD7 TN Galactoside 3(4)-L-fucosyltransferase (FUT3) TTUPAD7 UP P21217 TTUPAD7 UC FUT3_HUMAN TTUPAD7 BC Hexosyltransferase TTUPAD7 SN Lewis FT; Fucosyltransferase III; Fucosyltransferase 3; FucTIII; FUT3; Blood group Lewis alpha4fucosyltransferase TTUPAD7 GN FUT3 TTUPAD7 FC May catalyze alpha-1,3and alpha-1,4 glycosidic linkages involved in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. May be involved in blood group Lewis determination; Lewis-positive(Le(+)) individuals have an active enzyme while Lewis-negative (Le(-)) individuals have an inactive enzyme. Also acts on the corresponding 1,4-galactosyl derivative, forming 1,3-L-fucosyl links. TTUPAD7 EC EC 2.4.1.65 TTUPAD7 SQ MDPLGAAKPQWPWRRCLAALLFQLLVAVCFFSYLRVSRDDATGSPRAPSGSSRQDTTPTRPTLLILLWTWPFHIPVALSRCSEMVPGTADCHITADRKVYPQADTVIVHHWDIMSNPKSRLPPSPRPQGQRWIWFNLEPPPNCQHLEALDRYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKPDSARVRYYQSLQAHLKVDVYGRSHKPLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALDFCKACWKLQQESRYQTVRSIAAWFT TTUPAD7 TT Clinical trial TTCSJBZ ID TTCSJBZ TTCSJBZ TN GAR transformylase (GART) TTCSJBZ UP P22102 (810-1010) TTCSJBZ UC PUR2_HUMAN TTCSJBZ SN Phosphoribosylglycinamide formyltransferase; 5'-phosphoribosylglycinamide transformylase; GART TTCSJBZ GN GART TTCSJBZ FC A folate-dependent enzyme, essential for the de novo purine synthesis pathway. TTCSJBZ EC EC 2.1.2.2 TTCSJBZ PD 5J9F; 4ZZ3; 4ZZ2; 4ZZ1; 4ZZ0 TTCSJBZ SQ VAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE TTCSJBZ TT Clinical trial TTX20QP ID TTX20QP TTX20QP TN Geranylgeranyl transferase I (GGTase-I) TTX20QP UP P53609 TTX20QP UC PGTB1_HUMAN TTX20QP BC Alkyl aryl transferase TTX20QP SN Type I protein geranyl-geranyltransferase subunit beta; Type I protein geranyl-geranyltransferase beta subunit of Saccharomyces cerevisiae; RAS proteins geranylgeranyltransferase beta subunit; PGGT; Geranylgeranyl transferase type-1 subunit beta; Geranylgeranyl transferase type I subunit beta; GGTase-I-beta of Saccharomyces cerevisiae; GGTase-I-beta; CDC43 TTX20QP GN PGGT1B TTX20QP FC Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and RAP1B. TTX20QP EC EC 2.5.1.59 TTX20QP SQ MAATEDERLAGSGEGERLDFLRDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQVLPTEDRSNLNRCGFRGSSYLGIPFNPSKAPGTAHPYDSGHIAMTYTGLSCLVILGDDLSRVNKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCASCICYMLNNWSGMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFSEKELNRIKRWCIMRQQNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLMEESGICKVHPALNVSTRTSERLLDLHQSWKTKDSKQCSENVHIST TTX20QP TT Clinical trial TT1OCL0 ID TT1OCL0 TT1OCL0 TN Ghrelin (GHRL) TT1OCL0 UP Q9UBU3 TT1OCL0 UC GHRL_HUMAN TT1OCL0 SN UNQ524/PRO1066; Motilin-related peptide; M46 protein; Growth hormone secretagogue; Growth hormone releasing peptide; Gastric peptide ghrelin; GHRL TT1OCL0 GN GHRL TT1OCL0 FC Specific ligand for the growth hormone secretagogue receptor type 1 (ghsr) inducing the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion.Involved in growth regulation. TT1OCL0 PD 1P7X TT1OCL0 SQ MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQQRKESKKPPAKLQPRALAGWLRPEDGGQAEGAEDELEVRFNAPFDVGIKLSGVQYQQHSQALGKFLQDILWEEAKEAPADK TT1OCL0 TT Clinical trial TT1OCL0 KE hsa04024:cAMP signaling pathway TTCW0KX ID TTCW0KX TTCW0KX TN Glutaminase (GLS) TTCW0KX UP O94925; Q9UI32 TTCW0KX UC GLSK_HUMAN; GLSL_HUMAN TTCW0KX BC Carbon-nitrogen hydrolase TTCW0KX SN L-glutamine amidohydrolase; Glutaminase, mitochondrial; GLS TTCW0KX GN GLS; GLS2 TTCW0KX FC Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity. Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. TTCW0KX SQ MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGGGGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEGKELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTVHKNLDGLL TTCW0KX TT Clinical trial TTCW0KX KE hsa00220:Arginine biosynthesis; hsa00250:Alanine, aspartate and glutamate metabolism; hsa00471:D-Glutamine and D-glutamate metabolism; hsa01100:Metabolic pathways; hsa04724:Glutamatergic synapse; hsa04727:GABAergic synapse; hsa04964:Proximal tubule bicarbonate reclamation; hsa05206:MicroRNAs in cancer; hsa05230:Central carbon metabolism in cancer TTJTSX4 ID TTJTSX4 TTJTSX4 TN Glypican-3 (GPC3) TTJTSX4 UP P51654 TTJTSX4 UC GPC3_HUMAN TTJTSX4 SN Secreted glypican3; OCI5; MXR7; Intestinal protein OCI5; Intestinal protein OCI-5; GTR22; GTR2-2 TTJTSX4 GN GPC3 TTJTSX4 FC Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins. Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation. Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligands. Positively regulates the non-canonical Wnt signaling pathway. Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression. Inhibits the dipeptidyl peptidase activity of DPP4. Plays a role in limb patterning and skeletal development by controlling the cellular response to BMP4. Modulates the effects of growth factors BMP2, BMP7 and FGF7 on renal branching morphogenesis. Required for coronary vascular development. Plays a role in regulating cell movements during gastrulation. Cell surface proteoglycan that bears heparan sulfate. TTJTSX4 SQ MAGTVRTACLVVAMLLSLDFPGQAQPPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASMELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQLMNPGLPDSALDINECLRGARRDLKVFGNFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVLLGLFSTIHDSIQYVQKNAGKLTTTIGKLCAHSQQRQYRSAYYPEDLFIDKKVLKVAHVEHEETLSSRRRELIQKLKSFISFYSALPGYICSHSPVAENDTLCWNGQELVERYSQKAARNGMKNQFNLHELKMKGPEPVVSQIIDKLKHINQLLRTMSMPKGRVLDKNLDEEGFESGDCGDDEDECIGGSGDGMIKVKNQLRFLAELAYDLDVDDAPGNSQQATPKDNEISTFHNLGNVHSPLKLLTSMAISVVCFFFLVH TTJTSX4 TT Clinical trial TTJTSX4 KE hsa05205:Proteoglycans in cancer TTJTSX4 RC R-HSA-1971475:A tetrasaccharide linker sequence is required for GAG synthesis; R-HSA-2024096:HS-GAG degradation; R-HSA-975634:Retinoid metabolism and transport TTAP4T1 ID TTAP4T1 TTAP4T1 TN Growth/differentiation factor 2 (GDF2) TTAP4T1 UP Q9UK05 TTAP4T1 UC GDF2_HUMAN TTAP4T1 BC Growth factor TTAP4T1 SN GDF2; Bone morphogenetic protein 9; BMP9 TTAP4T1 GN GDF2 TTAP4T1 FC Potent circulating inhibitor of angiogenesis. Couldbe involved in bone formation. Signals through the type I activin receptor ACVRL1 but not other Alks. Signaling through SMAD1 in endothelial cells requires TGF-beta coreceptor endoglin/ENG. TTAP4T1 PD 5I05; 5HZW; 4YCI; 4YCG; 4MPL TTAP4T1 SQ MCPGALWVALPLLSLLAGSLQGKPLQSWGRGSAGGNAHSPLGVPGGGLPEHTFNLKMFLENVKVDFLRSLNLSGVPSQDKTRVEPPQYMIDLYNRYTSDKSTTPASNIVRSFSMEDAISITATEDFPFQKHILLFNISIPRHEQITRAELRLYVSCQNHVDPSHDLKGSVVIYDVLDGTDAWDSATETKTFLVSQDIQDEGWETLEVSSAVKRWVRSDSTKSKNKLEVTVESHRKGCDTLDISVPPGSRNLPFFVVFSNDHSSGTKETRLELREMISHEQESVLKKLSKDGSTEAGESSHEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR TTAP4T1 TT Clinical trial TTLC8E1 ID TTLC8E1 TTLC8E1 TN Haptoglobin (HP) TTLC8E1 UP P00738 TTLC8E1 UC HPT_HUMAN TTLC8E1 BC Peptidase TTLC8E1 SN Haptoglobin beta chain; HP TTLC8E1 GN HP TTLC8E1 FC Uncleaved haptoglogin, also known as zonulin, plays a role in intestinal permeability, allowing intercellular tight junction disassembly, and controlling the equilibrium between tolerance and immunity to non-self antigens. {ECO:0000269|PubMed:21248165}. TTLC8E1 PD 5HU6; 4X0L; 4WJG TTLC8E1 SQ MSALGAVIALLLWGQLFAVDSGNDVTDIADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNDKKQWINKAVGDKLPECEADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNNEKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYSQVDIGLIKLKQKVSVNERVMPICLPSKDYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEGSTVPEKKTPKSPVGVQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDLEEDTWYATGILSFDKSCAVAEYGVYVKVTSIQDWVQKTIAEN TTLC8E1 TT Clinical trial TT5IP87 ID TT5IP87 TT5IP87 TN Heat shock protein 20 (HSP20) TT5IP87 UP P04792 TT5IP87 UC HSPB1_HUMAN TT5IP87 BC Heat shock protein TT5IP87 SN Stress-responsive protein 27; SRP27; HspB1; Heat shock protein beta-1; Heat shock 27 kDa protein; HSP28; HSP27; HSP 27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein TT5IP87 GN HSPB1 TT5IP87 FC Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins. TT5IP87 PD 4MJH; 3Q9Q; 3Q9P; 2N3J TT5IP87 SQ MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK TT5IP87 TT Clinical trial TTMG98T ID TTMG98T TTMG98T TN Heat shock protein 27 (HSP27) TTMG98T UP Q12988 TTMG98T UC HSPB3_HUMAN TTMG98T BC Heat shock protein TTMG98T SN Protein 3; HspB3; Heat shock protein beta3; Heat shock 17 kDa protein; HSP 17 TTMG98T GN HSPB3 TTMG98T FC Inhibitor of actin polymerization. TTMG98T PD 6F2R TTMG98T SQ MAKIILRHLIEIPVRYQEEFEARGLEDCRLDHALYALPGPTIVDLRKTRAAQSPPVDSAAETPPREGKSHFQILLDVVQFLPEDIIIQTFEGWLLIKAQHGTRMDEHGFISRSFTRQYKLPDGVEIKDLSAVLCHDGILVVEVKDPVGTK TTMG98T TT Clinical trial TT1RWL7 ID TT1RWL7 TT1RWL7 TN Hepatitis A virus cellular receptor 2 (TIM3) TT1RWL7 UP Q8TDQ0 TT1RWL7 UC HAVR2_HUMAN TT1RWL7 BC Immunoglobulin TT1RWL7 SN TIMD3; TIMD-3; TIM3; TIM-3; T-cell membrane protein 3; T-cell immunoglobulin mucin receptor 3; T-cell immunoglobulin and mucin domain-containing protein 3; HAVcr-2; HAVCR2; CD366 TT1RWL7 GN Hepatitis A virus HAVCR2 TT1RWL7 FC Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand. Regulates macrophage activation. Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. In CD8+ cells attenuates TCR-induced signaling, specifically by blocking NF-kappaB and NFAT promoter activities resulting in the loss of IL-2 secretion. The function may implicate its association with LCK proposed to impair phosphorylation of TCR subunits, and/or LGALS9-dependent recruitment of PTPRC to the immunological synapse. In contrast, shown to activate TCR-induced signaling in T-cells probably implicating ZAP70, LCP2, LCK and FYN. Expressed on Treg cells can inhibit Th17 cell responses. Receptor for LGALS9. Binding to LGALS9 is believed to result in suppression of T-cell responses; the resulting apoptosis of antigen-specific cells may implicate HAVCR2 phosphorylation and disruption of its association with BAG6. Binding to LGALS9 is proposed to be involved in innate immune response to intracellular pathogens. Expressed on Th1 cells interacts with LGALS9 expressed on Mycobacterium tuberculosis-infected macrophages to stimulate antibactericidal activity including IL-1 beta secretion and to restrict intracellular bacterial growth. However, the function as receptor for LGALS9 has been challenged. Also reported to enhance CD8+ T-cell responses to an acute infection such as by Listeria monocytogenes. Receptor for phosphatidylserine (PtSer); PtSer-binding is calcium-dependent. May recognize PtSer on apoptotic cells leading to their phagocytosis. Mediates the engulfment of apoptotic cells by dendritic cells. Expressed on T-cells, promotes conjugation but not engulfment of apoptotic cells. Expressed on dendritic cells (DCs) positively regulates innate immune response and in synergy with Toll-like receptors promotes secretion of TNF-alpha. In tumor-imfiltrating DCs suppresses nucleic acid-mediated innate immune repsonse by interaction with HMGB1 and interfering with nucleic acid-sensing and trafficking of nucleid acids to endosomes. Expressed on natural killer (NK) cells acts as a coreceptor to enhance IFN-gamma production in response to LGALS9. In contrast, shown to suppress NK cell-mediated cytotoxicity. Negatively regulates NK cell function in LPS-induced endotoxic shock. Cell surface receptor implicated in modulating innate and adaptive immune responses. TT1RWL7 PD 6DHB; 5F71; 5DZL TT1RWL7 SQ MFSHLPFDCVLLLLLLLLTRSSEVEYRAEVGQNAYLPCFYTPAAPGNLVPVCWGKGACPVFECGNVVLRTDERDVNYWTSRYWLNGDFRKGDVSLTIENVTLADSGIYCCRIQIPGIMNDEKFNLKLVIKPAKVTPAPTRQRDFTAAFPRMLTTRGHGPAETQTLGSLPDINLTQISTLANELRDSRLANDLRDSGATIRIGIYIGAGICAGLALALIFGALIFKWYSHSKEKIQNLSLISLANLPPSGLANAVAEGIRSEENIYTIEENVYEVEEPNEYYCYVSSRQQPSQPLGCRFAMP TT1RWL7 TT Clinical trial TT1RWL7 FM Immunoglobulin superfamily TT6KSF7 ID TT6KSF7 TT6KSF7 TN Hepatitis B virus Large envelope protein (HBV S) TT6KSF7 UP P03141 TT6KSF7 UC HBSAG_HBVA3 TT6KSF7 BC Orthohepadnavirus major surface antigen TT6KSF7 SN Major surface antigen; Large surface protein; Large envelope protein; Large S protein; LHB; L-HBsAg; L glycoprotein TT6KSF7 GN HBV S TT6KSF7 FC The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. TT6KSF7 SQ MGGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPVKDDWPAANQVGVGAFGPRLTPPHGGILGWSPQAQGILTTVSTIPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTAFHQTLQDPRVRGLYLPAGGSSSGTVNPAPNIASHISSISARTGDPVTNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSTTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSAIWMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI TT6KSF7 TT Clinical trial TTALKDS ID TTALKDS TTALKDS TN Hepatitis C virus Non-structural 4B (HCV NS4B) TTALKDS UP P26664 (1712-1972) TTALKDS UC POLG_HCV1 TTALKDS BC Hepacivirus polyprotein TTALKDS SN HCV p27 TTALKDS GN HCV NS4B TTALKDS FC Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). TTALKDS PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TTALKDS SQ SQHLPYIEQGMMLAEQFKQKALGLLQTASRQAEVIAPAVQTNWQKLETFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTSQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAAIGSVGLGKVLIDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPC TTALKDS TT Clinical trial TTKCVJR ID TTKCVJR TTKCVJR TN Herpes simplex virus Helicase-primase (HSV UL8) TTKCVJR UP P10192 TTKCVJR UC HEPA_HHV11 TTKCVJR BC Acid anhydrides hydrolase TTKCVJR SN Primase-associated factor; HEPA; DNA helicase/primase complex-associated protein TTKCVJR GN HSV UL8 TTKCVJR FC Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase presumably elongates using dNTPs. The primase-associated factor has no known catalytic activity in the complex and may serve to facilitate the formation of the replisome by directly interacting with the origin-binding protein and the polymerase. TTKCVJR SQ MDTADIVWVEESVSAITLYAVWLPPRAREYFHALVYFVCRNAAGEGRARFAEVSVTATELRDFYGSADVSVQAVVAAARAATTPAASPLEPLENPTLWRALYACVLAALERQTGPVALFAPLRIGSDPRTGLVVKVERASWGPPAAPRAALLVAEANIDIDPMALAARVAEHPDARLAWARLAAIRDTPQCASAASLTVNITTGTALFAREYQTLAFPPIKKEGAFGDLVEVCEVGLRPRGHPQRVTARVLLPRDYDYFVSAGEKFSAPALVALFRQWHTTVHAAPGALAPVFAFLGPEFEVRGGPVPYFAVLGFPGWPTFTVPATAESARDLVRGAAAAYAALLGAWPAVGARVVLPPRAWPGVASAAAGCLLPAVREAVARWHPATKIIQLLDPPAAVGPVWTARFCFPGLRAQLLAALADLGGSGLADPHGRTGLARLDALVVAAPSEPWAGAVLERLVPDTCNACPALRQLLGGVMAAVCLQIEETASSVKFAVCGGDGGAFWGVFNVDPQDADAASGVIEDARRAIETAVGAVLRANAVRLRHPLCLALEGVYTHAVAWSQAGVWFWNSRDNTDHLGGFPLRGPAYTTAAGVVRDTLRRVLGLTTACVPEEDALTARGLMEDACDRLILDAFNKRLDAEYWSVRVSPFEASDPLPPTAFRGGALLDAEHYWRRVVRVCPGGGESVGVPVDLYPRPLVLPPVDCAHHLREILREIELVFTGVLAGVWGEGGKFVYPFDDKMSFLFA TTKCVJR TT Clinical trial TTUXSTW ID TTUXSTW TTUXSTW TN HLA class II antigen DR10 (HLA-DRB1) TTUXSTW UP Q30167 TTUXSTW UC 2B1A_HUMAN TTUXSTW BC MHC class II TTUXSTW SN MHC class II antigen DRB1*10; HLADRB1; HLA class II histocompatibility antigen, DRB110 beta chain; DRw10 TTUXSTW GN HLA-DRB1 TTUXSTW FC Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route; where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules; and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments; exogenous antigens must compete withthose derived from endogenous components. Autophagy is also a source of endogenous peptides; autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs; other cells of the gastrointestinal tract; such as epithelial cells; express MHC class II molecules and CD74 and act as APCs; which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen; three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs; CD74 undergoes a sequential degradation by various proteases; including CTSS and CTSL; leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells; the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules; increased acidification produces increased proteolysis and efficient peptide loading. TTUXSTW SQ MVCLKLPGGSCMTALTVTLMVLSSPLALSGDTRPRFLWQPKRECHFFNGTERVRFLDRYFYNQEESVRFDSDVGEFRAVTELGRPDAEYWNSQKDILEQARAAVDTYCRHNYGVVESFTVQRRVQPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFLNGQEEKAGMVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRARSESAQSKMLSGVGGFVLGLLFLGAGLFIYFRNQKGHSGLQPTGFLS TTUXSTW TT Clinical trial TTUXSTW RC R-HSA-202427:Phosphorylation of CD3 and TCR zeta chains; R-HSA-202430:Translocation of ZAP-70 to Immunological synapse; R-HSA-202433:Generation of second messenger molecules; R-HSA-2132295:MHC class II antigen presentation; R-HSA-389948:PD-1 signaling; R-HSA-877300:Interferon gamma signaling TTCMYP9 ID TTCMYP9 TTCMYP9 TN HLA-DR antigens-associated invariant (CD74) TTCMYP9 UP P04233 TTCMYP9 UC HG2A_HUMAN TTCMYP9 SN Ii; Ia antigenassociated invariant chain; Ia antigen-associated invariant chain; HLADR antigensassociated invariant chain; HLA-DR antigens-associated invariant chain; HLA class II histocompatibility antigen gamma chain; DHLAG TTCMYP9 GN CD74 TTCMYP9 FC Serves as cell surface receptor for the cytokine MIF. Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to the endosomal/lysosomal system where the antigen processing and binding of antigenic peptides to MHC class II takes place. TTCMYP9 PD 5KSV; 5KSU; 4X5W; 4AH2; 4AEN TTCMYP9 SQ MHRRRSRSCREDQKPVMDDQRDLISNNEQLPMLGRRPGAPESKCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKPPKPVSKMRMATPLLMQALPMGALPQGPMQNATKYGNMTEDHVMHLLQNADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPTDAPPKVLTKCQEEVSHIPAVHPGSFRPKCDENGNYLPLQCYGSIGYCWCVFPNGTEVPNTRSRGHHNCSESLELEDPSSGLGVTKQDLGPVPM TTCMYP9 TT Clinical trial TTCMYP9 KE hsa04612:Antigen processing and presentation; hsa05152:Tuberculosis; hsa05168:Herpes simplex infection TTCMYP9 RC R-HSA-2132295:MHC class II antigen presentation TTFGZB6 ID TTFGZB6 TTFGZB6 TN Human immunodeficiency virus GAG protein (HIV gag) TTFGZB6 UP P04591 TTFGZB6 UC GAG_HV1H2 TTFGZB6 SN Pr55Gag; Gag polyprotein TTFGZB6 GN HIV gag TTFGZB6 FC Gag polyprotein: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). TTFGZB6 PD 6CQR; 6CQQ; 6CQN; 6CQL; 6CQJ TTFGZB6 SQ MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNFLQSRPEPTAPPEESFRSGVETTTPPQKQEPIDKELYPLTSLRSLFGNDPSSQ TTFGZB6 TT Clinical trial TTFGZB6 RC R-HSA-162585:Uncoating of the HIV Virion; R-HSA-162588:Budding and maturation of HIV virion; R-HSA-162592:Integration of provirus; R-HSA-162594:Early Phase of HIV Life Cycle; R-HSA-164516:Minus-strand DNA synthesis; R-HSA-164525:Plus-strand DNA synthesis; R-HSA-164843:2-LTR circle formation; R-HSA-173107:Binding and entry of HIV virion; R-HSA-174490:Membrane binding and targetting of GAG proteins; R-HSA-175474:Assembly Of The HIV Virion; R-HSA-175567:Integration of viral DNA into host genomic DNA; R-HSA-177539:Autointegration results in viral DNA circles; R-HSA-180689:APOBEC3G mediated resistance to HIV-1 infection; R-HSA-180910:Vpr-mediated nuclear import of PICs TTI3NXG ID TTI3NXG TTI3NXG TN Human immunodeficiency virus Matrix p17 (HIV MA) TTI3NXG UP P03366 (2-132) TTI3NXG UC POL_HV1B1 TTI3NXG SN gag TTI3NXG GN HIV MA TTI3NXG FC p6-gag: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. TTI3NXG PD 6OE3; 6HAK; 6ELI; 6DUH; 6DUG TTI3NXG SQ GARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNY TTI3NXG TT Clinical trial TTI3NXG RC R-HSA-162585:Uncoating of the HIV Virion; R-HSA-162588:Budding and maturation of HIV virion; R-HSA-162592:Integration of provirus; R-HSA-162594:Early Phase of HIV Life Cycle; R-HSA-164516:Minus-strand DNA synthesis; R-HSA-164525:Plus-strand DNA synthesis; R-HSA-164843:2-LTR circle formation; R-HSA-173107:Binding and entry of HIV virion; R-HSA-174490:Membrane binding and targetting of GAG proteins; R-HSA-175474:Assembly Of The HIV Virion; R-HSA-175567:Integration of viral DNA into host genomic DNA; R-HSA-177539:Autointegration results in viral DNA circles; R-HSA-180689:APOBEC3G mediated resistance to HIV-1 infection; R-HSA-180910:Vpr-mediated nuclear import of PICs TTFP96H ID TTFP96H TTFP96H TN Human immunodeficiency virus Tat messenger RNA (HIV tat mRNA) TTFP96H UP P04608 TTFP96H UC TAT_HV1H2 TTFP96H BC mRNA target TTFP96H SN tat (mRNA); Transactivating regulatory protein (mRNA); Protein Tat (mRNA) TTFP96H GN HIV tat mRNA TTFP96H FC Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. TTFP96H PD 6MCF; 6MCE; 5V61; 4OR5; 3MIA TTFP96H SQ MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAHQNSQTHQASLSKQPTSQPRGDPTGPKE TTFP96H TT Clinical trial TTFP96H FM mRNA target TT3CPZW ID TT3CPZW TT3CPZW TN Human papillomavirus protein E7 (HPV E7) TT3CPZW UP P03129 TT3CPZW UC VE7_HPV16 TT3CPZW BC Papillomaviridae E protein TT3CPZW SN Protein E7; E7 TT3CPZW GN HPV E7 TT3CPZW FC E7 protein has both transforming and trans-activating activities. Disrupts the function of host retinoblastoma protein RB1/pRb, which is a key regulator of the cell cycle. Induces the disassembly of the E2F1 transcription factors from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. Interferes with histone deacetylation mediated by HDAC1 and HDAC2, leading to activation of transcription. TT3CPZW PD 6APN; 4YOZ TT3CPZW SQ MHGDTPTLHEYMLDLQPETTDLYCYEQLNDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP TT3CPZW TT Clinical trial TTDMLNT ID TTDMLNT TTDMLNT TN Hypoxia-inducible factor 2 alpha (HIF-2A) TTDMLNT UP Q99814 TTDMLNT UC EPAS1_HUMAN TTDMLNT SN bHLHe73; PASD2; PAS domain-containing protein 2; Member of PAS protein 2; MOP2; Hypoxia-inducible factor 2-alpha; HLF; HIF2A; HIF2-alpha; HIF-2-alpha; HIF-1-alpha-like factor; Endothelial PAS domain-containing protein 1; EPAS-1; Class E basic helix-loop-helix protein 73; Basic-helix-loop-helix-PAS protein MOP2 TTDMLNT GN EPAS1 TTDMLNT FC Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters. Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBBP and probably EP300. Interaction with redox regulatory protein APEX seems to activate CTAD. Transcription factor involved in the induction of oxygen regulated genes. TTDMLNT PD 6D0C; 6D0B; 6D09; 6CZW; 6BVB TTDMLNT SQ MTADKEKKRSSSERRKEKSRDAARCRRSKETEVFYELAHELPLPHSVSSHLDKASIMRLAISFLRTHKLLSSVCSENESEAEADQQMDNLYLKALEGFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENLSLKNGSGFGKKSKDMSTERDFFMRMKCTVTNRGRTVNLKSATWKVLHCTGQVKVYNNCPPHNSLCGYKEPLLSCLIIMCEPIQHPSHMDIPLDSKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVIYNPRNLQPQCIMCVNYVLSEIEKNDVVFSMDQTESLFKPHLMAMNSIFDSSGKGAVSEKSNFLFTKLKEEPEELAQLAPTPGDAIISLDFGNQNFEESSAYGKAILPPSQPWATELRSHSTQSEAGSLPAFTVPQAAAPGSTTPSATSSSSSCSTPNSPEDYYTSLDNDLKIEVIEKLFAMDTEAKDQCSTQTDFNELDLETLAPYIPMDGEDFQLSPICPEERLLAENPQSTPQHCFSAMTNIFQPLAPVAPHSPFLLDKFQQQLESKKTEPEHRPMSSIFFDAGSKASLPPCCGQASTPLSSMGGRSNTQWPPDPPLHFGPTKWAVGDQRTEFLGAAPLGPPVSPPHVSTFKTRSAKGFGARGPDVLSPAMVALSNKLKLKRQLEYEEQAFQDLSGGDPPGGSTSHLMWKRMKNLRGGSCPLMPDKPLSANVPNDKFTQNPMRGLGHPLRHLPLPQPPSAISPGENSKSRFPPQCYATQYQDYSLSSAHKVSGMASRLLGPSFESYLLPELTRYDCEVNVPVLGSSTLLQGGDLLRALDQAT TTDMLNT TT Clinical trial TTDMLNT KE hsa05200:Pathways in cancer; hsa05211:Renal cell carcinoma TTUS18T ID TTUS18T TTUS18T TN IL-1 receptor-like 2 (IL1RL2) TTUS18T UP Q9HB29 TTUS18T UC ILRL2_HUMAN TTUS18T BC Cytokine receptor TTUS18T SN Interleukin-1 receptor-related protein 2; Interleukin-1 receptor-like 2; IL1RRP2; IL1R-rp2; IL-36R; IL-36 receptor; IL-1Rrp2 TTUS18T GN IL1RL2 TTUS18T FC After binding to interleukin-36 associates with the coreceptor IL1RAP to form the interleukin-36 receptor complex which mediates interleukin-36-dependent activation of NF-kappa-B, MAPK and other pathways. The IL-36 signaling system is thought to be present in epithelial barriers and to take part in local inflammatory response; it is similar to the IL-1 system. Seems to be involved in skin inflammatory response by induction of the IL-23/IL-17/IL-22 pathway. Receptor for interleukin-36 (IL36A, IL36B and IL36G). TTUS18T SQ MWSLLLCGLSIALPLSVTADGCKDIFMKNEILSASQPFAFNCTFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGRDSCHRIHVNLTVFEKHWCDTSIGGLPNLSDEYKQILHLGKDDSLTCHLHFPKSCVLGPIKWYKDCNEIKGERFTVLETRLLVSNVSAEDRGNYACQAILTHSGKQYEVLNGITVSITERAGYGGSVPKIIYPKNHSIEVQLGTTLIVDCNVTDTKDNTNLRCWRVNNTLVDDYYDESKRIREGVETHVSFREHNLYTVNITFLEVKMEDYGLPFMCHAGVSTAYIILQLPAPDFRAYLIGGLIALVAVAVSVVYIYNIFKIDIVLWYRSAFHSTETIVDGKLYDAYVLYPKPHKESQRHAVDALVLNILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLLKNLSEEQIAVYSALIQDGMKVILIELEKIEDYTVMPESIQYIKQKHGAIRWHGDFTEQSQCMKTKFWKTVRYHMPPRRCRPFPPVQLLQHTPCYRTAGPELGSRRKKCTLTTG TTUS18T TT Clinical trial TTUS18T KE hsa04060:Cytokine-cytokine receptor interaction TTPI1M5 ID TTPI1M5 TTPI1M5 TN Ileal sodium/bile acid cotransporter (SLC10A2) TTPI1M5 UP Q12908 TTPI1M5 UC NTCP2_HUMAN TTPI1M5 SN Solute carrier family 10 member 2; Sodium/taurocholate cotransporting polypeptide, ileal; SLC10A2; Na(+)dependent ileal bile acid transporter; Ileal sodiumdependent bile acid transporter; Ileal Na(+)/bile acid cotransporter; ISBT; IBAT; Apical sodiumdependent bile acid transporter; ASBT TTPI1M5 GN SLC10A2 TTPI1M5 FC Plays a critical role in the sodium-dependent reabsorption of bile acids from the lumen of the small intestine. Plays a key role in cholesterol metabolism. TTPI1M5 SQ MNDPNSCVDNATVCSGASCVVPESNFNNILSVVLSTVLTILLALVMFSMGCNVEIKKFLGHIKRPWGICVGFLCQFGIMPLTGFILSVAFDILPLQAVVVLIIGCCPGGTASNILAYWVDGDMDLSVSMTTCSTLLALGMMPLCLLIYTKMWVDSGSIVIPYDNIGTSLVSLVVPVSIGMFVNHKWPQKAKIILKIGSIAGAILIVLIAVVGGILYQSAWIIAPKLWIIGTIFPVAGYSLGFLLARIAGLPWYRCRTVAFETGMQNTQLCSTIVQLSFTPEELNVVFTFPLIYSIFQLAFAAIFLGFYVAYKKCHGKNKAEIPESKENGTEPESSFYKANGGFQPDEK TTPI1M5 TT Clinical trial TTPI1M5 KE hsa04976:Bile secretion TTPI1M5 RC R-HSA-159418:Recycling of bile acids and salts TTIFOC0 ID TTIFOC0 TTIFOC0 TN Immunoglobulin gamma Fc receptor IIIA (FCGR3A) TTIFOC0 UP P08637 TTIFOC0 UC FCG3A_HUMAN TTIFOC0 BC Immunoglobulin TTIFOC0 SN FCGR3A TTIFOC0 GN FCGR3A TTIFOC0 FC Receptor for the Fc region of IgG. Binds complexed or aggregated IgG and also monomeric IgG. Mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis. TTIFOC0 PD 5YC5; 5XJF; 5XJE; 5VU0; 5MN2 TTIFOC0 SQ MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQWFHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKNVSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDWKDHKFKWRKDPQDK TTIFOC0 TT Clinical trial TTE5VP6 ID TTE5VP6 TTE5VP6 TN Inducible T-cell costimulator (ICOS) TTE5VP6 UP Q9Y6W8 TTE5VP6 UC ICOS_HUMAN TTE5VP6 BC Immunoglobulin TTE5VP6 SN Inducible costimulator; Inducible T-cell co-stimulator; Inducible COSTIMULATOR precursor; CD278; Activation-inducible lymphocyte immunomediatory molecule; AILIM TTE5VP6 GN ICOS TTE5VP6 FC Essential both for efficient interaction between T and B-cells and for normal antibody responses to T-cell dependent antigens. Does not up-regulate the production of interleukin-2, but superinduces the synthesis of interleukin-10. Prevents the apoptosis of pre-activated T-cells. Plays a critical role in CD40-mediated class switching of immunoglobin isotypes. Enhances all basic T-cell responses to a foreign antigen, namely proliferation, secretion of lymphokines, up-regulation of molecules that mediate cell-cell interaction, and effective help for antibody secretion by B-cells. TTE5VP6 SQ MKSGLWYFFLFCLRIKVLTGEINGSANYEMFIFHNGGVQILCKYPDIVQQFKMQLLKGGQILCDLTKTKGSGNTVSIKSLKFCHSQLSNNSVSFFLYNLDHSHANYYFCNLSIFDPPPFKVTLTGGYLHIYESQLCCQLKFWLPIGCAAFVVVCILGCILICWLTKKKYSSSVHDPNGEYMFMRAVNTAKKSRLTDVTL TTE5VP6 TT Clinical trial TTE5VP6 FM Immunoglobulin superfamily TTE5VP6 KE hsa04514:Cell adhesion molecules (CAMs); hsa04660:T cell receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05340:Primary immunodeficiency TTPERWV ID TTPERWV TTPERWV TN Integrin alpha-1 (VLA-1) TTPERWV UP P56199 TTPERWV UC ITA1_HUMAN TTPERWV BC Integrin TTPERWV SN Laminin and collagen receptor; Integrin alpha1; ITGA1; CD49a; CD49 antigenlike family member A TTPERWV GN ITGA1 TTPERWV FC Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G- E-R in collagen. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. TTPERWV PD 5HGJ; 4A0Q; 2M32; 2L8S; 1QCY TTPERWV SQ MAPRPRARPGVAVACCWLLTVVLRCCVSFNVDVKNSMTFSGPVEDMFGYTVQQYENEEGKWVLIGSPLVGQPKNRTGDVYKCPVGRGESLPCVKLDLPVNTSIPNVTEVKENMTFGSTLVTNPNGGFLACGPLYAYRCGHLHYTTGICSDVSPTFQVVNSIAPVQECSTQLDIVIVLDGSNSIYPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTMTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRGNLSTEKFVEEIKSIASEPTEKHFFNVSDELALVTIVKTLGERIFALEATADQSAASFEMEMSQTGFSAHYSQDWVMLGAVGAYDWNGTVVMQKASQIIIPRNTTFNVESTKKNEPLASYLGYTVNSATASSGDVLYIAGQPRYNHTGQVIIYRMEDGNIKILQTLSGEQIGSYFGSILTTTDIDKDSNTDILLVGAPMYMGTEKEEQGKVYVYALNQTRFEYQMSLEPIKQTCCSSRQHNSCTTENKNEPCGARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHGGAVYIYHGSGKTIRKEYAQRIPSGGDGKTLKFFGQSIHGEMDLNGDGLTDVTIGGLGGAALFWSRDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSKEDTIYEADLQYRVTLDSLRQISRSFFSGTQERKVQRNITVRKSECTKHSFYMLDKHDFQDSVRITLDFNLTDPENGPVLDDSLPNSVHEYIPFAKDCGNKEKCISDLSLHVATTEKDLLIVRSQNDKFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKDSCESNHNITCKVGYPFLRRGEMVTFKILFQFNTSYLMENVTIYLSATSDSEEPPETLSDNVVNISIPVKYEVGLQFYSSASEYHISIAANETVPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSENANCRPHIFEDPFSINSGKKMTTSTDHLKRGTILDCNTCKFATITCNLTSSDISQVNVSLILWKPTFIKSYFSSLNLTIRGELRSENASLVLSSSNQKRELAIQISKDGLPGRVPLWVILLSAFAGLLLLMLLILALWKIGFFKRPLKKKMEK TTPERWV TT Clinical trial TTLHGSF ID TTLHGSF TTLHGSF TN Interferon-alpha 5 (IFNA5) TTLHGSF UP P01569 TTLHGSF UC IFNA5_HUMAN TTLHGSF BC Cytokine: interferon TTLHGSF SN LeIF G; Interferon alphaG; Interferon alpha61; Interferon alpha5; Interferon alpha-G; Interferon alpha-61; Interferon alpha-5; IFNalpha5; IFN-alpha-5 TTLHGSF GN IFNA5 TTLHGSF FC Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. Produced by macrophages, IFN-alpha have antiviral activities. TTLHGSF SQ MALPFVLLMALVVLNCKSICSLGCDLPQTHSLSNRRTLMIMAQMGRISPFSCLKDRHDFGFPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTKDSSATWDETLLDKFYTELYQQLNDLEACMMQEVGVEDTPLMNVDSILTVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSLSANLQERLRRKE TTLHGSF TT Clinical trial TTLHGSF KE hsa04060:Cytokine-cytokine receptor interaction; hsa04140:Regulation of autophagy; hsa04151:PI3K-Akt signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05320:Autoimmune thyroid disease TTLHGSF RC R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912694:Regulation of IFNA signaling; R-HSA-933541:TRAF6 mediated IRF7 activation; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTVMO5W ID TTVMO5W TTVMO5W TN Interleukin-25 (IL25) TTVMO5W UP Q9H293 TTVMO5W UC IL25_HUMAN TTVMO5W BC Cytokine: interleukin TTVMO5W SN UNQ3120/PRO10272; Interleukin-17E; IL17E; IL-25; IL-17E TTVMO5W GN IL25 TTVMO5W FC Proinflammatory cytokine favoring Th2-type immune responses. Induces activation of NF-kappa-B and stimulates production of the proinflammatory chemokine IL-8. TTVMO5W SQ MRERPRLGEDSSLISLFLQVVAFLAMVMGTHTYSHWPSCCPSKGQDTSEELLRWSTVPVPPLEPARPNRHPESCRASEDGPLNSRAISPWRYELDRDLNRLPQDLYHARCLCPHCVSLQTGSHMDPRGNSELLYHNQTVFYRRPCHGEKGTHKGYCLERRLYRVSLACVCVRPRVMG TTVMO5W TT Clinical trial TTVMO5W FM Cytokine: interleukin TTVMO5W KE hsa04060:Cytokine-cytokine receptor interaction; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis TTDJ4MY ID TTDJ4MY TTDJ4MY TN Kininogen (KNG1) TTDJ4MY UP P01042 TTDJ4MY UC KNG1_HUMAN TTDJ4MY SN KNG1; Bradykinin TTDJ4MY GN KNG1 TTDJ4MY FC Kininogens are inhibitors of thiol proteases; hmw-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor xi next to factor xii; hmw-kininogen inhibits the thrombin-and plasmin- induced process. TTDJ4MY PD 6F3Y; 6F3X; 6F3W; 6F3V; 6F27 TTDJ4MY SQ MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRITEATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFSVATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLNEVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLRIASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFKIDNVKKARVQVVAGKKYFIDFVARETTCSKESNEELTESCETKKLGQSLDCNAEVYVVPWEKKIYPTVNCQPLGMISLMKRPPGFSPFRSSRIGEIKEETTVSPPHTSMAPAQDEERDSGKEQGHTRRHDWGHEKQRKHNLGHGHKHERDQGHGHQRGHGLGHGHEQQHGLGHGHKFKLDDDLEHQGGHVLDHGHKHKHGHGHGKHKNKGKKNGKHNGWKTEHLASSSEDSTTPSAQTQEKTEGPTPIPSLAKPGVTVTFSDFQDSDLIATMMPPISPAPIQSDDDWIPDIQIDPNGLSFNPISDFPDTTSPKCPGRPWKSVSEINPTTQMKESYYFDLTDGLS TTDJ4MY TT Clinical trial TTDJ4MY KE hsa04610:Complement and coagulation cascades TTDJ4MY RC R-HSA-114608:Platelet degranulation; R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events TTFCW29 ID TTFCW29 TTFCW29 TN Leukocyte antigen CD37 (CD37) TTFCW29 UP P11049 TTFCW29 UC CD37_HUMAN TTFCW29 BC Tetraspanin TTFCW29 SN Tspan26; Tspan-26; Tetraspanin26; Tetraspanin-26 TTFCW29 GN CD37 TTFCW29 FC extracellular exosome, immunological synapse, integral component of plasma membrane, membrane, cell surface receptor signaling pathway. TTFCW29 SQ MSAQESCLSLIKYFLFVFNLFFFVLGSLIFCFGIWILIDKTSFVSFVGLAFVPLQIWSKVLAISGIFTMGIALLGCVGALKELRCLLGLYFGMLLLLFATQITLGILISTQRAQLERSLRDVVEKTIQKYGTNPEETAAEESWDYVQFQLRCCGWHYPQDWFQVLILRGNGSEAHRVPCSCYNLSATNDSTILDKVILPQLSRLGHLARSRHSADICAVPAESHIYREGCAQGLQKWLHNNLISIVGICLGVGLLELGFMTLSIFLCRNLDHVYNRLARYR TTFCW29 TT Clinical trial TTFCW29 KE hsa04640:Hematopoietic cell lineage TT28S46 ID TT28S46 TT28S46 TN Leukocyte surface antigen CD47 (CD47) TT28S46 UP Q08722 TT28S46 UC CD47_HUMAN TT28S46 BC Osteoclast fusion complex TT28S46 SN Protein MER6; MER6; Integrinassociated protein; Integrin-associated protein; IAP; Antigenic surface determinant protein OA3 TT28S46 GN CD47 TT28S46 FC Plays an important role in memory formation and synaptic plasticity in the hippocampus. Receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation. May play a role in membrane transport and/or integrin dependent signal transduction. May prevent premature elimination of red blood cells. May be involved in membrane permeability changes induced following virus infection. Has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins. TT28S46 PD 5TZU; 5TZT; 5TZ2; 5IWL; 4KJY TT28S46 SQ MWPLVAALLLGSACCGSAQLLFNKTKSVEFTFCNDTVVIPCFVTNMEAQNTTEVYVKWKFKGRDIYTFDGALNKSTVPTDFSSAKIEVSQLLKGDASLKMDKSDAVSHTGNYTCEVTELTREGETIIELKYRVVSWFSPNENILIVIFPIFAILLFWGQFGIKTLKYRSGGMDEKTIALLVAGLVITVIVIVGAILFVPGEYSLKNATGLGLIVTSTGILILLHYYVFSTAIGLTSFVIAILVIQVIAYILAVVGLSLCIAACIPMHGPLLISGLSILALAQLLGLVYMKFVASNQKTIQPPRKAVEEPLNAFKESKGMMNDE TT28S46 TT Clinical trial TT28S46 FM Transmembrane protein TT2XAZY ID TT2XAZY TT2XAZY TN Liver and activation-regulated chemokine (CCL20) TT2XAZY UP P78556 TT2XAZY UC CCL20_HUMAN TT2XAZY BC Cytokine: CC chemokine TT2XAZY SN Smallinducible cytokine A20; Small-inducible cytokine A20; SCYA20; Macrophage inflammatory protein 3 alpha; MIP3alpha; MIP3A; MIP-3-alpha; Liver and activationregulated chemokine; LARC; CCL20(270); CC motif chemokine 20; CC chemokine LARC; C-C motif chemokine 20; Betachemokine exodus1; Beta-chemokine exodus-1 TT2XAZY GN CCL20 TT2XAZY FC Signals through binding and activation of CCR6 and induces a strong chemotactic response and mobilization of intracellular calcium ions. The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/memory T-cells and B-cells and plays an important role at skin and mucosal surfaces under homeostatic and inflammatory conditions, as well as in pathology, including cancer and various autoimmune diseases. CCL20 acts as a chemotactic factor that attracts lymphocytes and, slightly, neutrophils, but not monocytes. Involved in the recruitment of both the proinflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation. Required for optimal migration of thymic natural regulatory T cells (nTregs) and DN1 early thymocyte progenitor cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. Positively regulates sperm motility and chemotaxis via its binding to CCR6 which triggers Ca2+ mobilization in the sperm which is important for its motility. Inhibits proliferation of myeloid progenitors in colony formation assays. May be involved in formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. Possesses antibacterial activity towards E. coli ATCC 25922 and S. aureus ATCC 29213. Acts as a ligand for C-C chemokine receptor CCR6. TT2XAZY PD 5UR7; 2JYO; 2HCI; 1M8A TT2XAZY SQ MCCTKSLLLAALMSVLLLHLCGESEAASNFDCCLGYTDRILHPKFIVGFTRQLANEGCDINAIIFHTKKKLSVCANPKQTWVKYIVRLLSKKVKNM TT2XAZY TT Clinical trial TT2XAZY FM Cytokine: intecrine/chemokine TTJ2HKA ID TTJ2HKA TTJ2HKA TN Long transient receptor potential channel 4 (TRPM4) TTJ2HKA UP Q8TD43 TTJ2HKA UC TRPM4_HUMAN TTJ2HKA BC Transient receptor potential catioin channel TTJ2HKA SN hTRPM4; Transient receptor potential cation channel subfamily M member 4; Melastatin-4; LTrpC4; LTrpC-4; Calcium-activated non-selective cation channel 1 TTJ2HKA GN TRPM4 TTJ2HKA FC Calcium-activated non selective (CAN) cation channel that mediates membrane depolarization. While it is activated by increase in intracellular Ca(2+), it is impermeable to it. Mediates transport of monovalent cations (Na(+) > K(+) > Cs(+) > Li(+)), leading to depolarize the membrane. It thereby plays a central role in cadiomyocytes, neurons from entorhinal cortex, dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells, cochlea hair cells etc. Participates in T-cell activation by modulating Ca(2+) oscillations after T lymphocyte activation, which is required for NFAT-dependent IL2 production. Involved in myogenic constriction of cerebral arteries. Controls insulin secretion in pancreatic beta-cells. May also be involved in pacemaking or could cause irregular electrical activity under conditions of Ca(2+) overload. Affects T-helper 1 (Th1) and T-helper 2 (Th2) cell motility and cytokine production through differential regulation of calcium signaling and NFATC1 localization. Enhances cell proliferation through up-regulation of the beta-catenin signaling pathway. TTJ2HKA PD 6BWI; 6BQV; 6BQR; 5WP6 TTJ2HKA SQ MVVPEKEQSWIPKIFKKKTCTTFIVDSTDPGGTLCQCGRPRTAHPAVAMEDAFGAAVVTVWDSDAHTTEKPTDAYGELDFTGAGRKHSNFLRLSDRTDPAAVYSLVTRTWGFRAPNLVVSVLGGSGGPVLQTWLQDLLRRGLVRAAQSTGAWIVTGGLHTGIGRHVGVAVRDHQMASTGGTKVVAMGVAPWGVVRNRDTLINPKGSFPARYRWRGDPEDGVQFPLDYNYSAFFLVDDGTHGCLGGENRFRLRLESYISQQKTGVGGTGIDIPVLLLLIDGDEKMLTRIENATQAQLPCLLVAGSGGAADCLAETLEDTLAPGSGGARQGEARDRIRRFFPKGDLEVLQAQVERIMTRKELLTVYSSEDGSEEFETIVLKALVKACGSSEASAYLDELRLAVAWNRVDIAQSELFRGDIQWRSFHLEASLMDALLNDRPEFVRLLISHGLSLGHFLTPMRLAQLYSAAPSNSLIRNLLDQASHSAGTKAPALKGGAAELRPPDVGHVLRMLLGKMCAPRYPSGGAWDPHPGQGFGESMYLLSDKATSPLSLDAGLGQAPWSDLLLWALLLNRAQMAMYFWEMGSNAVSSALGACLLLRVMARLEPDAEEAARRKDLAFKFEGMGVDLFGECYRSSEVRAARLLLRRCPLWGDATCLQLAMQADARAFFAQDGVQSLLTQKWWGDMASTTPIWALVLAFFCPPLIYTRLITFRKSEEEPTREELEFDMDSVINGEGPVGTADPAEKTPLGVPRQSGRPGCCGGRCGGRRCLRRWFHFWGAPVTIFMGNVVSYLLFLLLFSRVLLVDFQPAPPGSLELLLYFWAFTLLCEELRQGLSGGGGSLASGGPGPGHASLSQRLRLYLADSWNQCDLVALTCFLLGVGCRLTPGLYHLGRTVLCIDFMVFTVRLLHIFTVNKQLGPKIVIVSKMMKDVFFFLFFLGVWLVAYGVATEGLLRPRDSDFPSILRRVFYRPYLQIFGQIPQEDMDVALMEHSNCSSEPGFWAHPPGAQAGTCVSQYANWLVVLLLVIFLLVANILLVNLLIAMFSYTFGKVQGNSDLYWKAQRYRLIREFHSRPALAPPFIVISHLRLLLRQLCRRPRSPQPSSPALEHFRVYLSKEAERKLLTWESVHKENFLLARARDKRESDSERLKRTSQKVDLALKQLGHIREYEQRLKVLEREVQQCSRVLGWVAEALSRSALLPPGGPPPPDLPGSKD TTJ2HKA TT Clinical trial TTE2YJR ID TTE2YJR TTE2YJR TN Lysophosphatidate-3 receptor (LPAR3) TTE2YJR UP Q9UBY5 TTE2YJR UC LPAR3_HUMAN TTE2YJR BC GPCR rhodopsin TTE2YJR SN Lysophosphatidic acid receptor Edg7; Lysophosphatidic acid receptor 3; LPAR3; LPA3; LPA receptor 3 TTE2YJR GN LPAR3 TTE2YJR FC Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. May play a role in the development of ovarian cancer. Seems to be coupled to the G(i)/G(o) and G(q) families of heteromeric G proteins. TTE2YJR SQ MNECHYDKHMDFFYNRSNTDTVDDWTGTKLVIVLCVGTFFCLFIFFSNSLVIAAVIKNRKFHFPFYYLLANLAAADFFAGIAYVFLMFNTGPVSKTLTVNRWFLRQGLLDSSLTASLTNLLVIAVERHMSIMRMRVHSNLTKKRVTLLILLVWAIAIFMGAVPTLGWNCLCNISACSSLAPIYSRSYLVFWTVSNLMAFLIMVVVYLRIYVYVKRKTNVLSPHTSGSISRRRTPMKLMKTVMTVLGAFVVCWTPGLVVLLLDGLNCRQCGVQHVKRWFLLLALLNSVVNPIIYSYKDEDMYGTMKKMICCFSQENPERRPSRIPSTVLSRSDTGSQYIEDSISQGAVCNKSTS TTE2YJR TT Clinical trial TTE2YJR KE hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa05200:Pathways in cancer TTE2YJR RC R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events; R-HSA-419408:Lysosphingolipid and LPA receptors TTFSUHX ID TTFSUHX TTFSUHX TN Lysyl oxidase homolog 2 (LOXL2) TTFSUHX UP Q9Y4K0 TTFSUHX UC LOXL2_HUMAN TTFSUHX SN Lysyl oxidaserelated protein WS914; Lysyl oxidaserelated protein 2; Lysyl oxidaselike protein 2; LOXL2 TTFSUHX GN LOXL2 TTFSUHX FC Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). When secreted in extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. When nuclear, acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E- cadherin, probably by mediating deamination of histone H3. Also involved in E-cadherin repression following hypoxia, a hallmark of epithelial to mesenchymal transition believed to amplify tumor aggressiveness, suggesting that it may play a role in tumor progression. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation. TTFSUHX EC EC 1.4.3.13 TTFSUHX PD 5ZE3 TTFSUHX SQ MERPLCSHLCSCLAMLALLSPLSLAQYDSWPHYPEYFQQPAPEYHQPQAPANVAKIQLRLAGQKRKHSEGRVEVYYDGQWGTVCDDDFSIHAAHVVCRELGYVEAKSWTASSSYGKGEGPIWLDNLHCTGNEATLAACTSNGWGVTDCKHTEDVGVVCSDKRIPGFKFDNSLINQIENLNIQVEDIRIRAILSTYRKRTPVMEGYVEVKEGKTWKQICDKHWTAKNSRVVCGMFGFPGERTYNTKVYKMFASRRKQRYWPFSMDCTGTEAHISSCKLGPQVSLDPMKNVTCENGLPAVVSCVPGQVFSPDGPSRFRKAYKPEQPLVRLRGGAYIGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGSAKEAVTGSRLGQGIGPIHLNEIQCTGNEKSIIDCKFNAESQGCNHEEDAGVRCNTPAMGLQKKLRLNGGRNPYEGRVEVLVERNGSLVWGMVCGQNWGIVEAMVVCRQLGLGFASNAFQETWYWHGDVNSNKVVMSGVKCSGTELSLAHCRHDGEDVACPQGGVQYGAGVACSETAPDLVLNAEMVQQTTYLEDRPMFMLQCAMEENCLSASAAQTDPTTGYRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEGDIQKNYECANFGDQGITMGCWDMYRHDIDCQWVDITDVPPGDYLFQVVINPNFEVAESDYSNNIMKCRSRYDGHRIWMYNCHIGGSFSEETEKKFEHFSGLLNNQLSPQ TTFSUHX TT Clinical trial TT1E5A4 ID TT1E5A4 TT1E5A4 TN Marburg virus NP messenger RNA (MV NP mRNA) TT1E5A4 UP P27588 TT1E5A4 UC NCAP_MABVM TT1E5A4 BC mRNA target TT1E5A4 SN Protein N (mRNA); Nucleoprotein (mRNA); Nucleocapsid protein (mRNA) TT1E5A4 GN MV NP mRNA TT1E5A4 FC The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. During replication, encapsidation by NP is coupled to RNA synthesis and all replicative products are resistant to nucleases. Encapsidates the genome, protecting it from nucleases. TT1E5A4 PD 6APP; 5T3W; 4W2Q; 4W2O TT1E5A4 SQ MDLHSLLELGTKPTAPHVRNKKVILFDTNHQVSICNQIIDAINSGIDLGDLLEGGLLTLCVEHYYNSDKDKFNTSPVAKYLRDAGYEFDVIKNADATRFLDVSPNEPHYSPLILALKTLESTESQRGRIGLFLSFCSLFLPKLVVGDRASIEKALRQVTVHQEQGIVTYPNHWLTTGHMKVIFGILRSSFILKFVLIHQGVNLVTGHDAYDSIISNSVGQTRFSGLLIVKTVLEFILQKTDSGVTLHPLVRTSKVKNEVASFKQALSNLARHGEYAPFARVLNLSGINNLEHGLYPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAAHDAEVKLQRRHEHQEIQAIAEDDEERKILEQFHLQKTEITHSQTLAVLSQKREKLARLAAEIENNIVEDQGFKQSQNRVSQSFLNDPTPVEVTVQARPMNRPTALPPPVDDKIEHESTEDSSSSSSFVDLNDPFALLNEDEDTLDDSVMIPGTTSREFQGIPEPPRQSQDLNNSQGKQEDESTNRIKKQFLRYQELPPVQEDDESEYTTDSQESIDQPGSDNEQGVDLPPPPLYAQEKRQDPIQHPAANPQDPFGSIGDVNGDILEPIRSPSSPSAPQEDTRMREAYELSPDFTNDEDNQQNWPQRVVTKKGRTFLYPNDLLQTNPPESLITALVEEYQNPVSAKELQADWPDMSFDERRHVAMNL TT1E5A4 TT Clinical trial TT1E5A4 FM mRNA target TT362RB ID TT362RB TT362RB TN MART-1 melanoma antigen (MLANA) TT362RB UP Q16655 TT362RB UC MAR1_HUMAN TT362RB SN Protein MelanA; Melanoma antigen recognized by Tcells 1; MLANA; MART1; Antigen SK29AA; Antigen LB39AA TT362RB GN MLANA TT362RB FC Involved in melanosome biogenesis by ensuring the stability of GPR143. Plays a vital role in the expression, stability, trafficking, and processing of melanocyte protein PMEL, which is critical to the formation of stage II melanosomes. TT362RB PD 6DKP; 6D78; 5NQK; 5NHT; 5E9D TT362RB SQ MPREDAHFIYGYPKKGHGHSYTTAEEAAGIGILTVILGVLLLIGCWYCRRRNGYRALMDKSLHVGTQCALTRRCPQEGFDHRDSKVSLQEKNCEPVVPNAPPAYEKLSAEQSPPPYSP TT362RB TT Clinical trial TTUPB12 ID TTUPB12 TTUPB12 TN Measles virus Fusion glycoprotein (MeV F) TTUPB12 UP Q786F3 TTUPB12 UC FUS_MEASC TTUPB12 BC Paramyxoviruses fusion glycoprotein TTUPB12 SN Measles virus fusion protein; MV fusion protein; Fusion protein TTUPB12 GN MeV F TTUPB12 FC Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion,the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C- terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. TTUPB12 PD 5YZD; 5YZC; 5YXW TTUPB12 SQ MGLKVNVSAIFMAVLLTLQTPTGQIHWGNLSKIGVVGIGSASYKVMTRSSHQSLVIKLMPNITLLNNCTRVEIAEYRRLLRTVLEPIRDALNAMTQNIRPVQSVASSRRHKRFAGVVLAGAALGVATAAQITAGIALHQSMLNSQAIDNLRASLETTNQAIEAIRQAGQEMILAVQGVQDYINNELIPSMNQLSCDLIGQKLGLKLLRYYTEILSLFGPSLRDPISAEISIQALSYALGGDINKVLEKLGYSGGDLLGILESRGIKARITHVDTESYFIVLSIAYPTLSEIKGVIVHRLEGVSYNIGSQEWYTTVPKYVATQGYLISNFDESSCTFMPEGTVCSQNALYPMSPLLQECLRGSTKSCARTLVSGSFGNRFILSQGNLIANCASILCKCYTTGTIINQDPDKILTYIAADHCPVVEVNGVTIQVGSRRYPDAVYLHRIDLGPPISLERLDVGTNLGNAIAKLEDAKELLESSDQILRSMKGLSSTSIVYILIAVCLGGLIGIPALICCCRGRCNKKGEQVGMSRPGLKPDLTGTSKSYVRSL TTUPB12 TT Clinical trial TT6QAJ3 ID TT6QAJ3 TT6QAJ3 TN Melanocortin receptor 5 (MC5R) TT6QAJ3 UP P33032 TT6QAJ3 UC MC5R_HUMAN TT6QAJ3 BC GPCR rhodopsin TT6QAJ3 SN MC5-R; MC2; MC-2 TT6QAJ3 GN MC5R TT6QAJ3 FC The activity of this receptor is mediated by G proteins which activate adenylate cyclase. This receptor is a possible mediator of the immunomodulation properties of melanocortins. Receptor for MSH (alpha, beta and gamma) and ACTH. TT6QAJ3 SQ MNSSFHLHFLDLNLNATEGNLSGPNVKNKSSPCEDMGIAVEVFLTLGVISLLENILVIGAIVKNKNLHSPMYFFVCSLAVADMLVSMSSAWETITIYLLNNKHLVIADAFVRHIDNVFDSMICISVVASMCSLLAIAVDRYVTIFYALRYHHIMTARRSGAIIAGIWAFCTGCGIVFILYSESTYVILCLISMFFAMLFLLVSLYIHMFLLARTHVKRIAALPGASSARQRTSMQGAVTVTMLLGVFTVCWAPFFLHLTLMLSCPQNLYCSRFMSHFNMYLILIMCNSVMDPLIYAFRSQEMRKTFKEIICCRGFRIACSFPRRD TT6QAJ3 TT Clinical trial TT6QAJ3 KE hsa04080:Neuroactive ligand-receptor interaction TT6QAJ3 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events TT8MK59 ID TT8MK59 TT8MK59 TN Melanocytes lineage-specific antigen GP100 (PMEL) TT8MK59 UP P40967 TT8MK59 UC PMEL_HUMAN TT8MK59 SN Silver locus protein homolog; SILV; Premelanosome protein; PMEL17; P100; P1; Melanomaassociated ME20 antigen; Melanoma-associated ME20 antigen; Melanocyte protein Pmel 17; Melanocyte protein PMEL; Mbeta; ME20S; ME20M; ME20-M; D12S53E TT8MK59 GN PMEL TT8MK59 FC Involved in the maturation of melanosomes from stage I to II. The transition from stage I melanosomes to stage II melanosomes involves an elongation of the vesicle, and the appearance within of distinct fibrillar structures. Release of the soluble form, ME20-S, could protect tumor cells from antibody mediated immunity. Plays a central role in the biogenesis of melanosomes. TT8MK59 PD 5EU6; 5EU5; 5EU4; 5EU3; 4IS6 TT8MK59 SQ MDLVLKRCLLHLAVIGALLAVGATKVPRNQDWLGVSRQLRTKAWNRQLYPEWTEAQRLDCWRGGQVSLKVSNDGPTLIGANASFSIALNFPGSQKVLPDGQVIWVNNTIINGSQVWGGQPVYPQETDDACIFPDGGPCPSGSWSQKRSFVYVWKTWGQYWQVLGGPVSGLSIGTGRAMLGTHTMEVTVYHRRGSRSYVPLAHSSSAFTITDQVPFSVSVSQLRALDGGNKHFLRNQPLTFALQLHDPSGYLAEADLSYTWDFGDSSGTLISRALVVTHTYLEPGPVTAQVVLQAAIPLTSCGSSPVPGTTDGHRPTAEAPNTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEVISTAPVQMPTAESTGMTPEKVPVSEVMGTTLAEMSTPEATGMTPAEVSIVVLSGTTAAQVTTTEWVETTARELPIPEPEGPDASSIMSTESITGSLGPLLDGTATLRLVKRQVPLDCVLYRYGSFSVTLDIVQGIESAEILQAVPSGEGDAFELTVSCQGGLPKEACMEISSPGCQPPAQRLCQPVLPSPACQLVLHQILKGGSGTYCLNVSLADTNSLAVVSTQLIMPGQEAGLGQVPLIVGILLVLMAVVLASLIYRRRLMKQDFSVPQLPHSSSHWLRLPRIFCSCPIGENSPLLSGQQV TT8MK59 TT Clinical trial TTWSKHD ID TTWSKHD TTWSKHD TN Melanoma-associated antigen 3 (MAGEA3) TTWSKHD UP P43357 TTWSKHD UC MAGA3_HUMAN TTWSKHD BC Melanoma associated antigen TTWSKHD SN Melanoma associated antigen-A3; Melanoma antigen 3; MAGE3; MAGE-A3 antigen; MAGE-A3; MAGE-3 antigen; Cancer/testis antigen 1.3; CT1.3; Antigen MZ2-D TTWSKHD GN MAGEA3 TTWSKHD FC May enhance ubiquitin ligase activity of TRIM28 and stimulate p53/TP53 ubiquitination by TRIM28. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in embryonal development and tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes. Proposed to enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. TTWSKHD PD 5BRZ; 4V0P; 1QEW TTWSKHD SQ MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQEAASSSSTLVEVTLGEVPAAESPDPPQSPQGASSLPTTMNYPLWSQSYEDSSNQEEEGPSTFPDLESEFQAALSRKVAELVHFLLLKYRAREPVTKAEMLGSVVGNWQYFFPVIFSKASSSLQLVFGIELMEVDPIGHLYIFATCLGLSYDGLLGDNQIMPKAGLLIIVLAIIAREGDCAPEEKIWEELSVLEVFEGREDSILGDPKKLLTQHFVQENYLEYRQVPGSDPACYEFLWGPRALVETSYVKVLHHMVKISGGPHISYPPLHEWVLREGEE TTWSKHD TT Clinical trial TTWSKHD FM Melanoma associated antigen family TT9EQUY ID TT9EQUY TT9EQUY TN Melanoma-associated antigen 4 (MAGEA4) TT9EQUY UP P43358 TT9EQUY UC MAGA4_HUMAN TT9EQUY BC Melanoma associated antigen TT9EQUY SN MAGE4; MAGE-X2 antigen; MAGE-X2; MAGE-41 antigen; MAGE-41; MAGE-4 protein; MAGE-4 antigen; Cancer/testis antigen 1.4; CT1.4 TT9EQUY GN MAGEA4 TT9EQUY FC Not known, though may play a role in embryonal development and tumor transformation or aspects of tumor progression. TT9EQUY PD 2WA0; 1I4F TT9EQUY SQ MSSEQKSQHCKPEEGVEAQEEALGLVGAQAPTTEEQEAAVSSSSPLVPGTLEEVPAAESAGPPQSPQGASALPTTISFTCWRQPNEGSSSQEEEGPSTSPDAESLFREALSNKVDELAHFLLRKYRAKELVTKAEMLERVIKNYKRCFPVIFGKASESLKMIFGIDVKEVDPASNTYTLVTCLGLSYDGLLGNNQIFPKTGLLIIVLGTIAMEGDSASEEEIWEELGVMGVYDGREHTVYGEPRKLLTQDWVQENYLEYRQVPGSNPARYEFLWGPRALAETSYVKVLEHVVRVNARVRIAYPSLREAALLEEEEGV TT9EQUY TT Clinical trial TT9EQUY FM Melanoma associated antigen family TTKGUEB ID TTKGUEB TTKGUEB TN Melanoma-associated antigen C2 (MAGEC2) TTKGUEB UP Q9UBF1 TTKGUEB UC MAGC2_HUMAN TTKGUEB BC Melanoma associated antigen TTKGUEB SN MAGEE1 antigen; MAGEE1; MAGEC2 antigen; MAGE-E1 antigen; MAGE-C2 antigen; Hepatocellular carcinomaassociated antigen 587; Hepatocellular carcinoma-associated antigen 587; HCA587; Cancer/testis antigen 10; CT10 TTKGUEB GN MAGEC2 TTKGUEB FC In vitro enhances ubiquitin ligase activity of TRIM28 and stimulates p53/TP53 ubiquitination in presence of Ubl-conjugating enzyme UBE2H leading to p53/TP53 degradation. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzymes (E2) at the E3:substrate complex. Proposed to enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. TTKGUEB SQ MPPVPGVPFRNVDNDSPTSVELEDWVDAQHPTDEEEEEASSASSTLYLVFSPSSFSTSSSLILGGPEEEEVPSGVIPNLTESIPSSPPQGPPQGPSQSPLSSCCSSFSWSSFSEESSSQKGEDTGTCQGLPDSESSFTYTLDEKVAELVEFLLLKYEAEEPVTEAEMLMIVIKYKDYFPVILKRAREFMELLFGLALIEVGPDHFCVFANTVGLTDEGSDDEGMPENSLLIIILSVIFIKGNCASEEVIWEVLNAVGVYAGREHFVYGEPRELLTKVWVQGHYLEYREVPHSSPPYYEFLWGPRAHSESIKKKVLEFLAKLNNTVPSSFPSWYKDALKDVEERVQATIDTADDATVMASESLSVMSSNVSFSE TTKGUEB TT Clinical trial TTKGUEB FM Melanoma associated protein TT0BE68 ID TT0BE68 TT0BE68 TN Membrane glycoprotein OX2 (CD200) TT0BE68 UP P41217 TT0BE68 UC OX2G_HUMAN TT0BE68 BC Immunoglobulin TT0BE68 SN OX2 membrane glycoprotein; OX-2 membrane glycoprotein; My033; MOX2; MOX1 TT0BE68 GN CD200 TT0BE68 FC May regulate myeloid cell activity in a variety of tissues. Costimulates T-cell proliferation. TT0BE68 SQ MERLVIRMPFSHLSTYSLVWVMAAVVLCTAQVQVVTQDEREQLYTPASLKCSLQNAQEALIVTWQKKKAVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNSTITFWNITLEDEGCYMCLFNTFGFGKISGTACLTVYVQPIVSLHYKFSEDHLNITCSATARPAPMVFWKVPRSGIENSTVTLSHPNGTTSVTSILHIKDPKNQVGKEVICQVLHLGTVTDFKQTVNKGYWFSVPLLLSIVSLVILLVLISILLYWKRHRNQDRGELSQGVQKMT TT0BE68 TT Clinical trial TT0BE68 FM Immunoglobulin superfamily TT0BE68 RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell TTV3CFI ID TTV3CFI TTV3CFI TN MHC class I NK cell receptor 2DS2 (CD158j) TTV3CFI UP P43631 TTV3CFI UC KI2S2_HUMAN TTV3CFI BC Immunoglobulin TTV3CFI SN p58 natural killer cell receptor clone CL-49; p58 NK receptor CL-49; Natural killer-associated transcript 5; NKAT5; NKAT-5; NK receptor 183 ActI; MHC class I NK cell receptor; Killer cell immunoglobulin-like receptor 2DS2; CD158J; CD158 antigen-like family member J TTV3CFI GN KIR2DS2 TTV3CFI FC Receptor on natural killer (NK) cells for HLA-C alleles. Does not inhibit the activity of NK cells. TTV3CFI PD 4N8V; 1M4K TTV3CFI SQ MSLMVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGPLVKSEETVILQCWSDVRFEHFLLHREGKYKDTLHLIGEHHDGVSKANFSIGPMMQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVLAGESVTLSCSSRSSYDMYHLSREGEAHERRFSAGPKVNGTFQADFPLGPATHGGTYRCFGSFRDSPYEWSNSSDPLLVSVTGNPSNSWPSPTEPSSKTGNPRHLHVLIGTSVVKIPFTILLFFLLHRWCSNKKNAAVMDQEPAGNRTVNSEDSDEQDHQEVSYA TTV3CFI TT Clinical trial TTYA75N ID TTYA75N TTYA75N TN MHC class II antigen DR (HLA-DR) TTYA75N UP P01903; P01911; P79483; P13762; Q30154 TTYA75N UC DRA_HUMAN; 2B1F_HUMAN; DRB3_HUMAN; DRB4_HUMAN; DRB5_HUMAN TTYA75N BC MHC class II TTYA75N SN HLA class II histocompatibility antigen TTYA75N GN HLA-DRA; HLA-DRB1; HLA-DRB3; HLA-DRB4; HLA-DRB5 TTYA75N FC Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of thiscomplex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class IImolecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DMand MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. TTYA75N SQ MAISGVPVLGFFIIAVLMSAQESWAIKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEFDAPSPLPETTENVVCALGLTVGLVGIIIGTIFIIKGVRKSNAAERRGPL TTYA75N TT Clinical trial TTYA75N KE hsa04145:Phagosome; hsa04514:Cell adhesion molecules (CAMs); hsa04612:Antigen processing and presentation; hsa04640:Hematopoietic cell lineage; hsa04672:Intestinal immune network for IgA production; hsa04940:Type I diabetes mellitus; hsa05140:Leishmaniasis; hsa05145:Toxoplasmosis; hsa05150:Staphylococcus aureus infection; hsa05152:Tuberculosis; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05310:Asthma; hsa05320:Autoimmune thyroid disease; hsa05321:Inflammatory bowel disease (IBD); hsa05322:Systemic lupus erythematosus; hsa05323:Rheumatoid arthritis; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease; hsa05416:Viral myocarditis TTYA75N RC R-HSA-202427:Phosphorylation of CD3 and TCR zeta chains; R-HSA-202430:Translocation of ZAP-70 to Immunological synapse; R-HSA-202433:Generation of second messenger molecules; R-HSA-2132295:MHC class II antigen presentation; R-HSA-389948:PD-1 signaling; R-HSA-877300:Interferon gamma signaling TTI12YJ ID TTI12YJ TTI12YJ TN Mitochondrial uncoupling protein 1 (UCP1) TTI12YJ UP P25874 TTI12YJ UC UCP1_HUMAN TTI12YJ BC Mitochondrial carrier TTI12YJ SN UCP 1; UCP; Thermogenin; Solute carrier family 25 member 7; SLC25A7; Mitochondrial brown fat uncoupling protein 1 TTI12YJ GN UCP1 TTI12YJ FC Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane. However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP. Regulates the production of reactive oxygen species/ROS by mitochondria. Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates to non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance. TTI12YJ SQ MGGLTASDVHPTLGVQLFSAGIAACLADVITFPLDTAKVRLQVQGECPTSSVIRYKGVLGTITAVVKTEGRMKLYSGLPAGLQRQISSASLRIGLYDTVQEFLTAGKETAPSLGSKILAGLTTGGVAVFIGQPTEVVKVRLQAQSHLHGIKPRYTGTYNAYRIIATTEGLTGLWKGTTPNLMRSVIINCTELVTYDLMKEAFVKNNILADDVPCHLVSALIAGFCATAMSSPVDVVKTRFINSPPGQYKSVPNCAMKVFTNEGPTAFFKGLVPSFLRLGSWNVIMFVCFEQLKRELSKSRQTMDCAT TTI12YJ TT Clinical trial TTI12YJ FM Mitochondrial carrier TTI12YJ KE hsa03320:PPAR signaling pathway; hsa05016:Huntington's disease TTSC2YM ID TTSC2YM TTSC2YM TN Mitochondrial uncoupling protein 2 (UCP2) TTSC2YM UP P55851 TTSC2YM UC UCP2_HUMAN TTSC2YM BC Mitochondrial carrier TTSC2YM SN UCPH; UCP 2; Solute carrier family 25 member 8; SLC25A8 TTSC2YM GN UCP2 TTSC2YM FC UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation from ATP synthesis. As a result, energy is dissipated in the form of heat. TTSC2YM SQ MVGFKATDVPPTATVKFLGAGTAACIADLITFPLDTAKVRLQIQGESQGPVRATASAQYRGVMGTILTMVRTEGPRSLYNGLVAGLQRQMSFASVRIGLYDSVKQFYTKGSEHASIGSRLLAGSTTGALAVAVAQPTDVVKVRFQAQARAGGGRRYQSTVNAYKTIAREEGFRGLWKGTSPNVARNAIVNCAELVTYDLIKDALLKANLMTDDLPCHFTSAFGAGFCTTVIASPVDVVKTRYMNSALGQYSSAGHCALTMLQKEGPRAFYKGFMPSFLRLGSWNVVMFVTYEQLKRALMAACTSREAPF TTSC2YM TT Clinical trial TTSC2YM FM Mitochondrial carrier TT12RJK ID TT12RJK TT12RJK TN Mitochondrial uncoupling protein 3 (UCP3) TT12RJK UP P55916 TT12RJK UC UCP3_HUMAN TT12RJK BC Mitochondrial carrier TT12RJK SN UCP 3; Solute carrier family 25 member 9; SLC25A9 TT12RJK GN UCP3 TT12RJK FC UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. As a result, energy is dissipated in the form of heat. May play a role in the modulation of tissue respiratory control. Participates in thermogenesis and energy balance. TT12RJK SQ MVGLKPSDVPPTMAVKFLGAGTAACFADLVTFPLDTAKVRLQIQGENQAVQTARLVQYRGVLGTILTMVRTEGPCSPYNGLVAGLQRQMSFASIRIGLYDSVKQVYTPKGADNSSLTTRILAGCTTGAMAVTCAQPTDVVKVRFQASIHLGPSRSDRKYSGTMDAYRTIAREEGVRGLWKGTLPNIMRNAIVNCAEVVTYDILKEKLLDYHLLTDNFPCHFVSAFGAGFCATVVASPVDVVKTRYMNSPPGQYFSPLDCMIKMVAQEGPTAFYKGFTPSFLRLGSWNVVMFVTYEQLKRALMKVQMLRESPF TT12RJK TT Clinical trial TT12RJK FM Mitochondrial carrier TT9XFON ID TT9XFON TT9XFON TN Myelin-associated glycoprotein (MAG) TT9XFON UP P20916 TT9XFON UC MAG_HUMAN TT9XFON BC Immunoglobulin TT9XFON SN MAG TT9XFON GN MAG TT9XFON FC Adhesion molecule in postnatal neural development that mediates sialic-acid dependent cell-cell interactions between neuronal and myelinating cells. Preferentially binds to alpha-2,3- linked sialic acid. TT9XFON SQ MIFLTALPLFWIMISASRGGHWGAWMPSSISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSNVSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPAVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQASFPNTTLQFEGYASMDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGTVLREAVAESLLLELEEVTPAEDGVYACLAENAYGQDNRTVGLSVMYAPWKPTVNGTMVAVEGETVSILCSTQSNPDPILTIFKEKQILSTVIYESELQLELPAVSPEDDGEYWCVAENQYGQRATAFNLSVEFAPVLLLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNESEREFVYSERSGLVLTSILTLRGQAQAPPRVICTARNLYGAKSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKKNVTESPSFSAGDNPPVLFSSDFRISGAPEKYESERRLGSERRLLGLRGEPPELDLSYSHSDLGKRPTKDSYTLTEELAEYAEIRVK TT9XFON TT Clinical trial TTWVLS6 ID TTWVLS6 TTWVLS6 TN Natriuretic peptide receptor (NPR3) TTWVLS6 UP P17342 TTWVLS6 UC ANPRC_HUMAN TTWVLS6 BC Phosphorus-oxygen lyase TTWVLS6 SN NPR3 TTWVLS6 GN NPR3 TTWVLS6 FC Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand. TTWVLS6 PD 1YK1; 1YK0; 1JDP; 1JDN TTWVLS6 SQ MPSLLVLTFSPCVLLGWALLAGGTGGGGVGGGGGGAGIGGGRQEREALPPQKIEVLVLLPQDDSYLFSLTRVRPAIEYALRSVEGNGTGRRLLPPGTRFQVAYEDSDCGNRALFSLVDRVAAARGAKPDLILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDSEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNCYFTLEGVHEVFQEEGLHTSIYSFDETKDLDLEDIVRNIQASERVVIMCASSDTIRSIMLVAHRHGMTSGDYAFFNIELFNSSSYGDGSWKRGDKHDFEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQGLNMEDYVNMFVEGFHDAILLYVLALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVIAMTDVEAGTQEVIGDYFGKEGRFEMRPNVKYPWGPLKLRIDENRIVEHTNSSPCKSSGGLEESAVTGIVVGALLGAGLLMAFYFFRKKYRITIERRTQQEESNLGKHRELREDSIRSHFSVA TTWVLS6 TT Clinical trial TTPO9EG ID TTPO9EG TTPO9EG TN Nectin cell adhesion molecule 4 (NECTIN4) TTPO9EG UP Q96NY8 TTPO9EG UC NECT4_HUMAN TTPO9EG SN Poliovirus receptor-related protein 4; PVRL4; PRR4; Nectin-4; LNIR; Ig superfamily receptor LNIR TTPO9EG GN NECTIN4 TTPO9EG FC Does not act as receptor for alpha-herpesvirus entry into cells. Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. TTPO9EG PD 4JJH; 4GJT; 4FRW TTPO9EG SQ MPLSLGAEMWGPEAWLLLLLLLASFTGRCPAGELETSDVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELALLHSKYGLHVSPAYEGRVEQPPPPRNPLDGSVLLRNAVQADEGEYECRVSTFPAGSFQARLRLRVLVPPLPSLNPGPALEEGQGLTLAASCTAEGSPAPSVTWDTEVKGTTSSRSFKHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGLLQDQRITHILHVSFLAEASVRGLEDQNLWHIGREGAMLKCLSEGQPPPSYNWTRLDGPLPSGVRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQVTVDVLDPQEDSGKQVDLVSASVVVVGVIAALLFCLLVVVVVLMSRYHRRKAQQMTQKYEEELTLTRENSIRRLHSHHTDPRSQPEESVGLRAEGHPDSLKDNSSCSVMSEEPEGRSYSTLTTVREIETQTELLSPGSGRAEEEEDQDEGIKQAMNHFVQENGTLRAKPTGNGIYINGRGHLV TTPO9EG TT Successful TTPO9EG KE hsa04520:Adherens junction TTPO9EG RC R-HSA-418990:Adherens junctions interactions TTVXPHT ID TTVXPHT TTVXPHT TN Neural cell adhesion molecule 1 (NCAM1) TTVXPHT UP P13591 TTVXPHT UC NCAM1_HUMAN TTVXPHT SN NCAM-1; NCAM; N-CAM-1; MSK39; CD56 TTVXPHT GN NCAM1 TTVXPHT FC This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. TTVXPHT PD 5LKN; 5AEA; 3MTR; 2VKX; 2VKW TTVXPHT SQ MLQTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQKLMFKNAPTPQEFREGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPTIQARQNIVNATANLGQSVTLVCDAEGFPEPTMSWTKDGEQIEQEEDDEKYIFSDDSSQLTIKKVDKNDEAEYICIAENKAGEQDATIHLKVFAKPKITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTRPEKQETLDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEVQYAPKLQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQESLEFILVQADTPSSPSIDQVEPYSSTAQVQFDEPEATGGVPILKYKAEWRAVGEEVWHSKWYDAKEASMEGIVTIVGLKPETTYAVRLAALNGKGLGEISAASEFKTQPVQGEPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVRYRALSSEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSAQPTAIPANGSPTSGLSTGAIVGILIVIFVLLLVVVDITCYFLNKCGLFMCIAVNLCGKAGPGAKGKDMEEGKAAFSKDESKEPIVEVRTEEERTPNHDGGKHTEPNETTPLTEPEKGPVEAKPECQETETKPAPAEVKTVPNDATQTKENESKA TTVXPHT TT Clinical trial TTVXPHT KE hsa04514:Cell adhesion molecules (CAMs); hsa05020:Prion diseases TTC9D3K ID TTC9D3K TTC9D3K TN Neural cell adhesion molecule L1 (L1CAM) TTC9D3K UP P32004 TTC9D3K UC L1CAM_HUMAN TTC9D3K BC Immunoglobulin TTC9D3K SN SPG1; S10; NCAM-L1; N-CAML1; N-CAM-L1; MIC5; MASA; L1 cell adhesion molecule; HSAS1; HSAS; CD171; CAML1 TTC9D3K GN L1CAM TTC9D3K FC During brain development, critical in multiple processes, including neuronal migration, axonal growth and fasciculation, and synaptogenesis. In the mature brain, plays a role in the dynamics of neuronal structure and function, including synaptic plasticity. Neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. TTC9D3K SQ MVVALRYVWPLLLCSPCLLIQIPEEYEGHHVMEPPVITEQSPRRLVVFPTDDISLKCEASGKPEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASNKLGTAMSHEIRLMAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAEPLRIYWMNSKILHIKQDERVTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEPIDLRVKATNSMIDRKPRLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLKVGEEDDGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYVVQLPAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGIRDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDPSLQPSITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDVVESRAQLLVVGSPGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVKGEGNETTNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLVVSNTSTFVPYEIKVQAVNSQGKGPEPQVTIGYSGEDYPQAIPELEGIEILNSSAVLVKWRPVDLAQVKGHLRGYNVTYWREGSQRKHSKRHIHKDHVVVPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTFSTPEGVPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRDPELRTHNLTDLSPHLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNISATAGENYSVVSWVPKEGQCNFRFHILFKALGEEKGGASLSPQYVSYNQSSYTQWDLQPDTDYEIHLFKERMFRHQMAVKTNGTGRVRLPPAGFATEGWFIGFVSAIILLLLVLLILCFIKRSKGGKYSVKDKEDTQVDSEARPMKDETFGEYRSLESDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVDVQFNEDGSFIGQYSGKKEKEAAGGNDSSGATSPINPAVALE TTC9D3K TT Clinical trial TTC9D3K KE hsa04360:Axon guidance; hsa04514:Cell adhesion molecules (CAMs) TTNJ5A6 ID TTNJ5A6 TTNJ5A6 TN Neuronal pentraxin-2 (NPTX2) TTNJ5A6 UP P47972 TTNJ5A6 UC NPTX2_HUMAN TTNJ5A6 BC Pentaxin family TTNJ5A6 SN Neuronal pentraxin II; NPTX2; NPII; NP2 TTNJ5A6 GN NPTX2 TTNJ5A6 FC Likely to play role in the modification of cellular properties that underlie long-term plasticity. Binds to agar matrix in a calcium-dependent manner. TTNJ5A6 SQ MLALLAASVALAVAAGAQDSPAPGSRFVCTALPPEAVHAGCPLPAMPMQGGAQSPEEELRAAVLQLRETVVQQKETLGAQREAIRELTGKLARCEGLAGGKARGAGATGKDTMGDLPRDPGHVVEQLSRSLQTLKDRLESLEHQLRANVSNAGLPGDFREVLQQRLGELERQLLRKVAELEDEKSLLHNETSAHRQKTESTLNALLQRVTELERGNSAFKSPDAFKVSLPLRTNYLYGKIKKTLPELYAFTICLWLRSSASPGIGTPFSYAVPGQANEIVLIEWGNNPIELLINDKVAQLPLFVSDGKWHHICVTWTTRDGMWEAFQDGEKLGTGENLAPWHPIKPGGVLILGQEQDTVGGRFDATQAFVGELSQFNIWDRVLRAQEIVNIANCSTNMPGNIIPWVDNNVDVFGGASKWPVETCEERLLDL TTNJ5A6 TT Clinical trial TTC4IMS ID TTC4IMS TTC4IMS TN NKG2-A/B-activating NK receptor (NKG2A) TTC4IMS UP P26715 TTC4IMS UC NKG2A_HUMAN TTC4IMS SN NKG2A/NKG2B type II integral membrane protein; NKG2A/Bactivating NK receptor; NK cell receptor A; KLRC1; CD159a; CD159 antigenlike family member A TTC4IMS GN KLRC1 TTC4IMS FC Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. TTC4IMS PD 3CII; 3CDG; 3BDW; 2YU7; 2RMX TTC4IMS SQ MDNQGVIYSDLNLPPNPKRQQRKPKGNKNSILATEQEITYAELNLQKASQDFQGNDKTYHCKDLPSAPEKLIVGILGIICLILMASVVTIVVIPSTLIQRHNNSSLNTRTQKARHCGHCPEEWITYSNSCYYIGKERRTWEESLLACTSKNSSLLSIDNEEEMKFLSIISPSSWIGVFRNSSHHPWVTMNGLAFKHEIKDSDNAELNCAVLQVNRLKSAQCGSSIIYHCKHKL TTC4IMS TT Clinical trial TTC4IMS KE hsa04612:Antigen processing and presentation; hsa04650:Natural killer cell mediated cytotoxicity; hsa05332:Graft-versus-host disease TTC4IMS RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell TTXDIK2 ID TTXDIK2 TTXDIK2 TN Notch-4 receptor (NOTCH4) TTXDIK2 UP Q99466 TTXDIK2 UC NOTC4_HUMAN TTXDIK2 BC Notch protein TTXDIK2 SN hNotch4; Notch 4; Neurogenic locus notch homolog protein 4; INT3 TTXDIK2 GN NOTCH4 TTXDIK2 FC Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. May regulate branching morphogenesis in the developing vascular system. Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. TTXDIK2 SQ MQPPSLLLLLLLLLLLCVSVVRPRGLLCGSFPEPCANGGTCLSLSLGQGTCQCAPGFLGETCQFPDPCQNAQLCQNGGSCQALLPAPLGLPSSPSPLTPSFLCTCLPGFTGERCQAKLEDPCPPSFCSKRGRCHIQASGRPQCSCMPGWTGEQCQLRDFCSANPCVNGGVCLATYPQIQCHCPPGFEGHACERDVNECFQDPGPCPKGTSCHNTLGSFQCLCPVGQEGPRCELRAGPCPPRGCSNGGTCQLMPEKDSTFHLCLCPPGFIGPDCEVNPDNCVSHQCQNGGTCQDGLDTYTCLCPETWTGWDCSEDVDECETQGPPHCRNGGTCQNSAGSFHCVCVSGWGGTSCEENLDDCIAATCAPGSTCIDRVGSFSCLCPPGRTGLLCHLEDMCLSQPCHGDAQCSTNPLTGSTLCLCQPGYSGPTCHQDLDECLMAQQGPSPCEHGGSCLNTPGSFNCLCPPGYTGSRCEADHNECLSQPCHPGSTCLDLLATFHCLCPPGLEGQLCEVETNECASAPCLNHADCHDLLNGFQCICLPGFSGTRCEEDIDECRSSPCANGGQCQDQPGAFHCKCLPGFEGPRCQTEVDECLSDPCPVGASCLDLPGAFFCLCPSGFTGQLCEVPLCAPNLCQPKQICKDQKDKANCLCPDGSPGCAPPEDNCTCHHGHCQRSSCVCDVGWTGPECEAELGGCISAPCAHGGTCYPQPSGYNCTCPTGYTGPTCSEEMTACHSGPCLNGGSCNPSPGGYYCTCPPSHTGPQCQTSTDYCVSAPCFNGGTCVNRPGTFSCLCAMGFQGPRCEGKLRPSCADSPCRNRATCQDSPQGPRCLCPTGYTGGSCQTLMDLCAQKPCPRNSHCLQTGPSFHCLCLQGWTGPLCNLPLSSCQKAALSQGIDVSSLCHNGGLCVDSGPSYFCHCPPGFQGSLCQDHVNPCESRPCQNGATCMAQPSGYLCQCAPGYDGQNCSKELDACQSQPCHNHGTCTPKPGGFHCACPPGFVGLRCEGDVDECLDQPCHPTGTAACHSLANAFYCQCLPGHTGQWCEVEIDPCHSQPCFHGGTCEATAGSPLGFICHCPKGFEGPTCSHRAPSCGFHHCHHGGLCLPSPKPGFPPRCACLSGYGGPDCLTPPAPKGCGPPSPCLYNGSCSETTGLGGPGFRCSCPHSSPGPRCQKPGAKGCEGRSGDGACDAGCSGPGGNWDGGDCSLGVPDPWKGCPSHSRCWLLFRDGQCHPQCDSEECLFDGYDCETPPACTPAYDQYCHDHFHNGHCEKGCNTAECGWDGGDCRPEDGDPEWGPSLALLVVLSPPALDQQLFALARVLSLTLRVGLWVRKDRDGRDMVYPYPGARAEEKLGGTRDPTYQERAAPQTQPLGKETDSLSAGFVVVMGVDLSRCGPDHPASRCPWDPGLLLRFLAAMAAVGALEPLLPGPLLAVHPHAGTAPPANQLPWPVLCSPVAGVILLALGALLVLQLIRRRRREHGALWLPPGFTRRPRTQSAPHRRRPPLGEDSIGLKALKPKAEVDEDGVVMCSGPEEGEEVGQAEETGPPSTCQLWSLSGGCGALPQAAMLTPPQESEMEAPDLDTRGPDGVTPLMSAVCCGEVQSGTFQGAWLGCPEPWEPLLDGGACPQAHTVGTGETPLHLAARFSRPTAARRLLEAGANPNQPDRAGRTPLHAAVAADAREVCQLLLRSRQTAVDARTEDGTTPLMLAARLAVEDLVEELIAAQADVGARDKWGKTALHWAAAVNNARAARSLLQAGADKDAQDNREQTPLFLAAREGAVEVAQLLLGLGAARELRDQAGLAPADVAHQRNHWDLLTLLEGAGPPEARHKATPGREAGPFPRARTVSVSVPPHGGGALPRCRTLSAGAGPRGGGACLQARTWSVDLAARGGGAYSHCRSLSGVGAGGGPTPRGRRFSAGMRGPRPNPAIMRGRYGVAAGRGGRVSTDDWPCDWVALGACGSASNIPIPPPCLTPSPERGSPQLDCGPPALQEMPINQGGEGKK TTXDIK2 TT Clinical trial TTXDIK2 KE hsa04320:Dorso-ventral axis formation; hsa04330:Notch signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05020:Prion diseases; hsa05206:MicroRNAs in cancer TTXDIK2 RC R-HSA-1912399:Pre-NOTCH Processing in the Endoplasmic Reticulum; R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-1912420:Pre-NOTCH Processing in Golgi; R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2122948:Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2197563:NOTCH2 intracellular domain regulates transcription; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2660826:Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant; R-HSA-2691232:Constitutive Signaling by NOTCH1 HD Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-350054:Notch-HLH transcription pathway TTGV6LY ID TTGV6LY TTGV6LY TN Nuclear receptor ROR-gamma (RORG) TTGV6LY UP P51449 TTGV6LY UC RORG_HUMAN TTGV6LY BC Nuclear hormone receptor TTGV6LY SN Retinoid-related orphan receptor-gamma; RZRG; RORG; RAR-related orphan receptor C; Nuclear receptor subfamily 1 group F member 3; Nuclear receptor RZR-gamma; NR1F3 TTGV6LY GN RORC TTGV6LY FC Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of cellular differentiation, immunity, peripheral circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively. Recruits distinct combinations of cofactors to target gene regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates the circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-selective manner. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as ARNTL/BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORC-mediated activation of the expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism, including PLIN2 and AVPR1A. Negative regulator of adipocyte differentiation through the regulation of early phase genes expression, such as MMP3. Controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. In liver, has specific and redundant functions with RORA as positive or negative modulator of expression of genes encoding phase I and Phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as SULT1E1. Also plays also a role in the regulation of hepatocyte glucose metabolism through the regulation of G6PC and PCK1. Regulates the rhythmic expression of PROX1 and promotes its nuclear localization. Plays an indispensable role in the induction of IFN-gamma dependent anti-mycobacterial systemic immunity. TTGV6LY PD 6O98; 6NAD; 6J1L; 6IVX; 6G07 TTGV6LY SQ MDRAPQRQHRASRELLAAKKTHTSQIEVIPCKICGDKSSGIHYGVITCEGCKGFFRRSQRCNAAYSCTRQQNCPIDRTSRNRCQHCRLQKCLALGMSRDAVKFGRMSKKQRDSLHAEVQKQLQQRQQQQQEPVVKTPPAGAQGADTLTYTLGLPDGQLPLGSSPDLPEASACPPGLLKASGSGPSYSNNLAKAGLNGASCHLEYSPERGKAEGRESFYSTGSQLTPDRCGLRFEEHRHPGLGELGQGPDSYGSPSFRSTPEAPYASLTEIEHLVQSVCKSYRETCQLRLEDLLRQRSNIFSREEVTGYQRKSMWEMWERCAHHLTEAIQYVVEFAKRLSGFMELCQNDQIVLLKAGAMEVVLVRMCRAYNADNRTVFFEGKYGGMELFRALGCSELISSIFDFSHSLSALHFSEDEIALYTALVLINAHRPGLQEKRKVEQLQYNLELAFHHHLCKTHRQSILAKLPPKGKLRSLCSQHVERLQIFQHLHPIVVQAAFPPLYKELFSTETESPVGLSK TTGV6LY TT Clinical trial TTHBS98 ID TTHBS98 TTHBS98 TN Nucleophosmin (NPM1) TTHBS98 UP P06748 TTHBS98 UC NPM_HUMAN TTHBS98 SN Numatrin; Nucleolar protein NO38; Nucleolar phosphoprotein B23; NPM TTHBS98 GN NPM1 TTHBS98 FC Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade. In complex with MYC enhances the transcription of MYC target genes. Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. TTHBS98 PD 5EHD; 2VXD; 2P1B; 2LLH TTHBS98 SQ MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL TTHBS98 TT Clinical trial TTHBS98 FM Nucleoplasmin TTIVXSE ID TTIVXSE TTIVXSE TN Oncostatin-M (OSM) TTIVXSE UP P13725 TTIVXSE UC ONCM_HUMAN TTIVXSE SN OSM TTIVXSE GN OSM TTIVXSE FC Growth regulator. Inhibits the proliferation of a number of tumor cell lines. Stimulates proliferation of AIDS-KS cells. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. Uses both type I OSM receptor (heterodimers composed of LIPR and IL6ST) and type II OSM receptor (heterodimers composed of OSMR and IL6ST). Involved in the maturation of fetal hepatocytes, thereby promoting liver development and regeneration. TTIVXSE PD 1EVS TTIVXSE SQ MGVLLTQRTLLSLVLALLFPSMASMAAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPGAFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDLEKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQRKLEGCRFLHGYHRFMHSVGRVFSKWGESPNRSRRHSPHQALRKGVRRTRPSRKGKRLMTRGQLPR TTIVXSE TT Clinical trial TTIVXSE KE hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway TT70MLA ID TT70MLA TT70MLA TN Oncotrophoblast glycoprotein 5T4 (TPBG) TT70MLA UP Q13641 TT70MLA UC TPBG_HUMAN TT70MLA SN Trophoblast glycoprotein; TPBG TT70MLA GN TPBG TT70MLA FC May function as an inhibitor of Wnt/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a- dependent LRP6 internalization. TT70MLA PD 4CNM; 4CNC TT70MLA SQ MPGGCSRGPAAGDGRLRLARLALVLLGWVSSSSPTSSASSFSSSAPFLASAVSAQPPLPDQCPALCECSEAARTVKCVNRNLTEVPTDLPAYVRNLFLTGNQLAVLPAGAFARRPPLAELAALNLSGSRLDEVRAGAFEHLPSLRQLDLSHNPLADLSPFAFSGSNASVSAPSPLVELILNHIVPPEDERQNRSFEGMVVAALLAGRALQGLRRLELASNHFLYLPRDVLAQLPSLRHLDLSNNSLVSLTYVSFRNLTHLESLHLEDNALKVLHNGTLAELQGLPHIRVFLDNNPWVCDCHMADMVTWLKETEVVQGKDRLTCAYPEKMRNRVLLELNSADLDCDPILPPSLQTSYVFLGIVLALIGAIFLLVLYLNRKGIKKWMHNIRDACRDHMEGYHYRYEINADPRLTNLSSNSDV TT70MLA TT Clinical trial TTC1PS3 ID TTC1PS3 TTC1PS3 TN Ovarian carcinoma antigen CA125 (MUC16) TTC1PS3 UP Q8WXI7 TTC1PS3 UC MUC16_HUMAN TTC1PS3 BC Mucin TTC1PS3 SN Ovarian cancerrelated tumor marker CA125; Mucin16; MUC16; CA125 TTC1PS3 GN MUC16 TTC1PS3 FC Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. TTC1PS3 SQ MLKPSGLPGSSSPTRSLMTGSRSTKATPEMDSGLTGATLSPKTSTGAIVVTEHTLPFTSPDKTLASPTSSVVGRTTQSLGVMSSALPESTSRGMTHSEQRTSPSLSPQVNGTPSRNYPATSMVSGLSSPRTRTSSTEGNFTKEASTYTLTVETTSGPVTEKYTVPTETSTTEGDSTETPWDTRYIPVKITSPMKTFADSTASKENAPVSMTPAETTVTDSHTPGRTNPSFGTLYSSFLDLSPKGTPNSRGETSLELILSTTGYPFSSPEPGSAGHSRISTSAPLSSSASVLDNKISETSIFSGQSLTSPLSPGVPEARASTMPNSAIPFSMTLSNAETSAERVRSTISSLGTPSISTKQTAETILTFHAFAETMDIPSTHIAKTLASEWLGSPGTLGGTSTSALTTTSPSTTLVSEETNTHHSTSGKETEGTLNTSMTPLETSAPGEESEMTATLVPTLGFTTLDSKIRSPSQVSSSHPTRELRTTGSTSGRQSSSTAAHGSSDILRATTSSTSKASSWTSESTAQQFSEPQHTQWVETSPSMKTERPPASTSVAAPITTSVPSVVSGFTTLKTSSTKGIWLEETSADTLIGESTAGPTTHQFAVPTGISMTGGSSTRGSQGTTHLLTRATASSETSADLTLATNGVPVSVSPAVSKTAAGSSPPGGTKPSYTMVSSVIPETSSLQSSAFREGTSLGLTPLNTRHPFSSPEPDSAGHTKISTSIPLLSSASVLEDKVSATSTFSHHKATSSITTGTPEISTKTKPSSAVLSSMTLSNAATSPERVRNATSPLTHPSPSGEETAGSVLTLSTSAETTDSPNIHPTGTLTSESSESPSTLSLPSVSGVKTTFSSSTPSTHLFTSGEETEETSNPSVSQPETSVSRVRTTLASTSVPTPVFPTMDTWPTRSAQFSSSHLVSELRATSSTSVTNSTGSALPKISHLTGTATMSQTNRDTFNDSAAPQSTTWPETSPRFKTGLPSATTTVSTSATSLSATVMVSKFTSPATSSMEATSIREPSTTILTTETTNGPGSMAVASTNIPIGKGYITEGRLDTSHLPIGTTASSETSMDFTMAKESVSMSVSPSQSMDAAGSSTPGRTSQFVDTFSDDVYHLTSREITIPRDGTSSALTPQMTATHPPSPDPGSARSTWLGILSSSPSSPTPKVTMSSTFSTQRVTTSMIMDTVETSRWNMPNLPSTTSLTPSNIPTSGAIGKSTLVPLDTPSPATSLEASEGGLPTLSTYPESTNTPSIHLGAHASSESPSTIKLTMASVVKPGSYTPLTFPSIETHIHVSTARMAYSSGSSPEMTAPGETNTGSTWDPTTYITTTDPKDTSSAQVSTPHSVRTLRTTENHPKTESATPAAYSGSPKISSSPNLTSPATKAWTITDTTEHSTQLHYTKLAEKSSGFETQSAPGPVSVVIPTSPTIGSSTLELTSDVPGEPLVLAPSEQTTITLPMATWLSTSLTEEMASTDLDISSPSSPMSTFAIFPPMSTPSHELSKSEADTSAIRNTDSTTLDQHLGIRSLGRTGDLTTVPITPLTTTWTSVIEHSTQAQDTLSATMSPTHVTQSLKDQTSIPASASPSHLTEVYPELGTQGRSSSEATTFWKPSTDTLSREIETGPTNIQSTPPMDNTTTGSSSSGVTLGIAHLPIGTSSPAETSTNMALERRSSTATVSMAGTMGLLVTSAPGRSISQSLGRVSSVLSESTTEGVTDSSKGSSPRLNTQGNTALSSSLEPSYAEGSQMSTSIPLTSSPTTPDVEFIGGSTFWTKEVTTVMTSDISKSSARTESSSATLMSTALGSTENTGKEKLRTASMDLPSPTPSMEVTPWISLTLSNAPNTTDSLDLSHGVHTSSAGTLATDRSLNTGVTRASRLENGSDTSSKSLSMGNSTHTSMTYTEKSEVSSSIHPRPETSAPGAETTLTSTPGNRAISLTLPFSSIPVEEVISTGITSGPDINSAPMTHSPITPPTIVWTSTGTIEQSTQPLHAVSSEKVSVQTQSTPYVNSVAVSASPTHENSVSSGSSTSSPYSSASLESLDSTISRRNAITSWLWDLTTSLPTTTWPSTSLSEALSSGHSGVSNPSSTTTEFPLFSAASTSAAKQRNPETETHGPQNTAASTLNTDASSVTGLSETPVGASISSEVPLPMAITSRSDVSGLTSESTANPSLGTASSAGTKLTRTISLPTSESLVSFRMNKDPWTVSIPLGSHPTTNTETSIPVNSAGPPGLSTVASDVIDTPSDGAESIPTVSFSPSPDTEVTTISHFPEKTTHSFRTISSLTHELTSRVTPIPGDWMSSAMSTKPTGASPSITLGERRTITSAAPTTSPIVLTASFTETSTVSLDNETTVKTSDILDARKTNELPSDSSSSSDLINTSIASSTMDVTKTASISPTSISGMTASSSPSLFSSDRPQVPTSTTETNTATSPSVSSNTYSLDGGSNVGGTPSTLPPFTITHPVETSSALLAWSRPVRTFSTMVSTDTASGENPTSSNSVVTSVPAPGTWTSVGSTTDLPAMGFLKTSPAGEAHSLLASTIEPATAFTPHLSAAVVTGSSATSEASLLTTSESKAIHSSPQTPTTPTSGANWETSATPESLLVVTETSDTTLTSKILVTDTILFSTVSTPPSKFPSTGTLSGASFPTLLPDTPAIPLTATEPTSSLATSFDSTPLVTIASDSLGTVPETTLTMSETSNGDALVLKTVSNPDRSIPGITIQGVTESPLHPSSTSPSKIVAPRNTTYEGSITVALSTLPAGTTGSLVFSQSSENSETTALVDSSAGLERASVMPLTTGSQGMASSGGIRSGSTHSTGTKTFSSLPLTMNPGEVTAMSEITTNRLTATQSTAPKGIPVKPTSAESGLLTPVSASSSPSKAFASLTTAPPTWGIPQSTLTFEFSEVPSLDTKSASLPTPGQSLNTIPDSDASTASSSLSKSPEKNPRARMMTSTKAISASSFQSTGFTETPEGSASPSMAGHEPRVPTSGTGDPRYASESMSYPDPSKASSAMTSTSLASKLTTLFSTGQAARSGSSSSPISLSTEKETSFLSPTASTSRKTSLFLGPSMARQPNILVHLQTSALTLSPTSTLNMSQEEPPELTSSQTIAEEEGTTAETQTLTFTPSETPTSLLPVSSPTEPTARRKSSPETWASSISVPAKTSLVETTDGTLVTTIKMSSQAAQGNSTWPAPAEETGSSPAGTSPGSPEMSTTLKIMSSKEPSISPEIRSTVRNSPWKTPETTVPMETTVEPVTLQSTALGSGSTSISHLPTGTTSPTKSPTENMLATERVSLSPSPPEAWTNLYSGTPGGTRQSLATMSSVSLESPTARSITGTGQQSSPELVSKTTGMEFSMWHGSTGGTTGDTHVSLSTSSNILEDPVTSPNSVSSLTDKSKHKTETWVSTTAIPSTVLNNKIMAAEQQTSRSVDEAYSSTSSWSDQTSGSDITLGASPDVTNTLYITSTAQTTSLVSLPSGDQGITSLTNPSGGKTSSASSVTSPSIGLETLRANVSAVKSDIAPTAGHLSQTSSPAEVSILDVTTAPTPGISTTITTMGTNSISTTTPNPEVGMSTMDSTPATERRTTSTEHPSTWSSTAASDSWTVTDMTSNLKVARSPGTISTMHTTSFLASSTELDSMSTPHGRITVIGTSLVTPSSDASAVKTETSTSERTLSPSDTTASTPISTFSRVQRMSISVPDILSTSWTPSSTEAEDVPVSMVSTDHASTKTDPNTPLSTFLFDSLSTLDWDTGRSLSSATATTSAPQGATTPQELTLETMISPATSQLPFSIGHITSAVTPAAMARSSGVTFSRPDPTSKKAEQTSTQLPTTTSAHPGQVPRSAATTLDVIPHTAKTPDATFQRQGQTALTTEARATSDSWNEKEKSTPSAPWITEMMNSVSEDTIKEVTSSSSVLRTLNTLDINLESGTTSSPSWKSSPYERIAPSESTTDKEAIHPSTNTVETTGWVTSSEHASHSTIPAHSASSKLTSPVVTTSTREQAIVSMSTTTWPESTRARTEPNSFLTIELRDVSPYMDTSSTTQTSIISSPGSTAITKGPRTEITSSKRISSSFLAQSMRSSDSPSEAITRLSNFPAMTESGGMILAMQTSPPGATSLSAPTLDTSATASWTGTPLATTQRFTYSEKTTLFSKGPEDTSQPSPPSVEETSSSSSLVPIHATTSPSNILLTSQGHSPSSTPPVTSVFLSETSGLGKTTDMSRISLEPGTSLPPNLSSTAGEALSTYEASRDTKAIHHSADTAVTNMEATSSEYSPIPGHTKPSKATSPLVTSHIMGDITSSTSVFGSSETTEIETVSSVNQGLQERSTSQVASSATETSTVITHVSSGDATTHVTKTQATFSSGTSISSPHQFITSTNTFTDVSTNPSTSLIMTESSGVTITTQTGPTGAATQGPYLLDTSTMPYLTETPLAVTPDFMQSEKTTLISKGPKDVSWTSPPSVAETSYPSSLTPFLVTTIPPATSTLQGQHTSSPVSATSVLTSGLVKTTDMLNTSMEPVTNSPQNLNNPSNEILATLAATTDIETIHPSINKAVTNMGTASSAHVLHSTLPVSSEPSTATSPMVPASSMGDALASISIPGSETTDIEGEPTSSLTAGRKENSTLQEMNSTTESNIILSNVSVGAITEATKMEVPSFDATFIPTPAQSTKFPDIFSVASSRLSNSPPMTISTHMTTTQTGSSGATSKIPLALDTSTLETSAGTPSVVTEGFAHSKITTAMNNDVKDVSQTNPPFQDEASSPSSQAPVLVTTLPSSVAFTPQWHSTSSPVSMSSVLTSSLVKTAGKVDTSLETVTSSPQSMSNTLDDISVTSAATTDIETTHPSINTVVTNVGTTGSAFESHSTVSAYPEPSKVTSPNVTTSTMEDTTISRSIPKSSKTTRTETETTSSLTPKLRETSISQEITSSTETSTVPYKELTGATTEVSRTDVTSSSSTSFPGPDQSTVSLDISTETNTRLSTSPIMTESAEITITTQTGPHGATSQDTFTMDPSNTTPQAGIHSAMTHGFSQLDVTTLMSRIPQDVSWTSPPSVDKTSSPSSFLSSPAMTTPSLISSTLPEDKLSSPMTSLLTSGLVKITDILRTRLEPVTSSLPNFSSTSDKILATSKDSKDTKEIFPSINTEETNVKANNSGHESHSPALADSETPKATTQMVITTTVGDPAPSTSMPVHGSSETTNIKREPTYFLTPRLRETSTSQESSFPTDTSFLLSKVPTGTITEVSSTGVNSSSKISTPDHDKSTVPPDTFTGEIPRVFTSSIKTKSAEMTITTQASPPESASHSTLPLDTSTTLSQGGTHSTVTQGFPYSEVTTLMGMGPGNVSWMTTPPVEETSSVSSLMSSPAMTSPSPVSSTSPQSIPSSPLPVTALPTSVLVTTTDVLGTTSPESVTSSPPNLSSITHERPATYKDTAHTEAAMHHSTNTAVTNVGTSGSGHKSQSSVLADSETSKATPLMSTTSTLGDTSVSTSTPNISQTNQIQTEPTASLSPRLRESSTSEKTSSTTETNTAFSYVPTGAITQASRTEISSSRTSISDLDRPTIAPDISTGMITRLFTSPIMTKSAEMTVTTQTTTPGATSQGILPWDTSTTLFQGGTHSTVSQGFPHSEITTLRSRTPGDVSWMTTPPVEETSSGFSLMSPSMTSPSPVSSTSPESIPSSPLPVTALLTSVLVTTTNVLGTTSPEPVTSSPPNLSSPTQERLTTYKDTAHTEAMHASMHTNTAVANVGTSISGHESQSSVPADSHTSKATSPMGITFAMGDTSVSTSTPAFFETRIQTESTSSLIPGLRDTRTSEEINTVTETSTVLSEVPTTTTTEVSRTEVITSSRTTISGPDHSKMSPYISTETITRLSTFPFVTGSTEMAITNQTGPIGTISQATLTLDTSSTASWEGTHSPVTQRFPHSEETTTMSRSTKGVSWQSPPSVEETSSPSSPVPLPAITSHSSLYSAVSGSSPTSALPVTSLLTSGRRKTIDMLDTHSELVTSSLPSASSFSGEILTSEASTNTETIHFSENTAETNMGTTNSMHKLHSSVSIHSQPSGHTPPKVTGSMMEDAIVSTSTPGSPETKNVDRDSTSPLTPELKEDSTALVMNSTTESNTVFSSVSLDAATEVSRAEVTYYDPTFMPASAQSTKSPDISPEASSSHSNSPPLTISTHKTIATQTGPSGVTSLGQLTLDTSTIATSAGTPSARTQDFVDSETTSVMNNDLNDVLKTSPFSAEEANSLSSQAPLLVTTSPSPVTSTLQEHSTSSLVSVTSVPTPTLAKITDMDTNLEPVTRSPQNLRNTLATSEATTDTHTMHPSINTAVANVGTTSSPNEFYFTVSPDSDPYKATSAVVITSTSGDSIVSTSMPRSSAMKKIESETTFSLIFRLRETSTSQKIGSSSDTSTVFDKAFTAATTEVSRTELTSSSRTSIQGTEKPTMSPDTSTRSVTMLSTFAGLTKSEERTIATQTGPHRATSQGTLTWDTSITTSQAGTHSAMTHGFSQLDLSTLTSRVPEYISGTSPPSVEKTSSSSSLLSLPAITSPSPVPTTLPESRPSSPVHLTSLPTSGLVKTTDMLASVASLPPNLGSTSHKIPTTSEDIKDTEKMYPSTNIAVTNVGTTTSEKESYSSVPAYSEPPKVTSPMVTSFNIRDTIVSTSMPGSSEITRIEMESTFSLAHGLKGTSTSQDPIVSTEKSAVLHKLTTGATETSRTEVASSRRTSIPGPDHSTESPDISTEVIPSLPISLGITESSNMTIITRTGPPLGSTSQGTFTLDTPTTSSRAGTHSMATQEFPHSEMTTVMNKDPEILSWTIPPSIEKTSFSSSLMPSPAMTSPPVSSTLPKTIHTTPSPMTSLLTPSLVMTTDTLGTSPEPTTSSPPNLSSTSHEILTTDEDTTAIEAMHPSTSTAATNVETTSSGHGSQSSVLADSEKTKATAPMDTTSTMGHTTVSTSMSVSSETTKIKRESTYSLTPGLRETSISQNASFSTDTSIVLSEVPTGTTAEVSRTEVTSSGRTSIPGPSQSTVLPEISTRTMTRLFASPTMTESAEMTIPTQTGPSGSTSQDTLTLDTSTTKSQAKTHSTLTQRFPHSEMTTLMSRGPGDMSWQSSPSLENPSSLPSLLSLPATTSPPPISSTLPVTISSSPLPVTSLLTSSPVTTTDMLHTSPELVTSSPPKLSHTSDERLTTGKDTTNTEAVHPSTNTAASNVEIPSSGHESPSSALADSETSKATSPMFITSTQEDTTVAISTPHFLETSRIQKESISSLSPKLRETGSSVETSSAIETSAVLSEVSIGATTEISRTEVTSSSRTSISGSAESTMLPEISTTRKIIKFPTSPILAESSEMTIKTQTSPPGSTSESTFTLDTSTTPSLVITHSTMTQRLPHSEITTLVSRGAGDVPRPSSLPVEETSPPSSQLSLSAMISPSPVSSTLPASSHSSSASVTSLLTPGQVKTTEVLDASAEPETSSPPSLSSTSVEILATSEVTTDTEKIHPFSNTAVTKVGTSSSGHESPSSVLPDSETTKATSAMGTISIMGDTSVSTLTPALSNTRKIQSEPASSLTTRLRETSTSEETSLATEANTVLSKVSTGATTEVSRTEAISFSRTSMSGPEQSTMSQDISIGTIPRISASSVLTESAKMTITTQTGPSESTLESTLNLNTATTPSWVETHSIVIQGFPHPEMTTSMGRGPGGVSWPSPPFVKETSPPSSPLSLPAVTSPHPVSTTFLAHIPPSPLPVTSLLTSGPATTTDILGTSTEPGTSSSSSLSTTSHERLTTYKDTAHTEAVHPSTNTGGTNVATTSSGYKSQSSVLADSSPMCTTSTMGDTSVLTSTPAFLETRRIQTELASSLTPGLRESSGSEGTSSGTKMSTVLSKVPTGATTEISKEDVTSIPGPAQSTISPDISTRTVSWFSTSPVMTESAEITMNTHTSPLGATTQGTSTLDTSSTTSLTMTHSTISQGFSHSQMSTLMRRGPEDVSWMSPPLLEKTRPSFSLMSSPATTSPSPVSSTLPESISSSPLPVTSLLTSGLAKTTDMLHKSSEPVTNSPANLSSTSVEILATSEVTTDTEKTHPSSNRTVTDVGTSSSGHESTSFVLADSQTSKVTSPMVITSTMEDTSVSTSTPGFFETSRIQTEPTSSLTLGLRKTSSSEGTSLATEMSTVLSGVPTGATAEVSRTEVTSSSRTSISGFAQLTVSPETSTETITRLPTSSIMTESAEMMIKTQTDPPGSTPESTHTVDISTTPNWVETHSTVTQRFSHSEMTTLVSRSPGDMLWPSQSSVEETSSASSLLSLPATTSPSPVSSTLVEDFPSASLPVTSLLNPGLVITTDRMGISREPGTSSTSNLSSTSHERLTTLEDTVDTEDMQPSTHTAVTNVRTSISGHESQSSVLSDSETPKATSPMGTTYTMGETSVSISTSDFFETSRIQIEPTSSLTSGLRETSSSERISSATEGSTVLSEVPSGATTEVSRTEVISSRGTSMSGPDQFTISPDISTEAITRLSTSPIMTESAESAITIETGSPGATSEGTLTLDTSTTTFWSGTHSTASPGFSHSEMTTLMSRTPGDVPWPSLPSVEEASSVSSSLSSPAMTSTSFFSTLPESISSSPHPVTALLTLGPVKTTDMLRTSSEPETSSPPNLSSTSAEILATSEVTKDREKIHPSSNTPVVNVGTVIYKHLSPSSVLADLVTTKPTSPMATTSTLGNTSVSTSTPAFPETMMTQPTSSLTSGLREISTSQETSSATERSASLSGMPTGATTKVSRTEALSLGRTSTPGPAQSTISPEISTETITRISTPLTTTGSAEMTITPKTGHSGASSQGTFTLDTSSRASWPGTHSAATHRSPHSGMTTPMSRGPEDVSWPSRPSVEKTSPPSSLVSLSAVTSPSPLYSTPSESSHSSPLRVTSLFTPVMMKTTDMLDTSLEPVTTSPPSMNITSDESLATSKATMETEAIQLSENTAVTQMGTISARQEFYSSYPGLPEPSKVTSPVVTSSTIKDIVSTTIPASSEITRIEMESTSTLTPTPRETSTSQEIHSATKPSTVPYKALTSATIEDSMTQVMSSSRGPSPDQSTMSQDISTEVITRLSTSPIKTESTEMTITTQTGSPGATSRGTLTLDTSTTFMSGTHSTASQGFSHSQMTALMSRTPGDVPWLSHPSVEEASSASFSLSSPVMTSSSPVSSTLPDSIHSSSLPVTSLLTSGLVKTTELLGTSSEPETSSPPNLSSTSAEILAITEVTTDTEKLEMTNVVTSGYTHESPSSVLADSVTTKATSSMGITYPTGDTNVLTSTPAFSDTSRIQTKSKLSLTPGLMETSISEETSSATEKSTVLSSVPTGATTEVSRTEAISSSRTSIPGPAQSTMSSDTSMETITRISTPLTRKESTDMAITPKTGPSGATSQGTFTLDSSSTASWPGTHSATTQRFPQSVVTTPMSRGPEDVSWPSPLSVEKNSPPSSLVSSSSVTSPSPLYSTPSGSSHSSPVPVTSLFTSIMMKATDMLDASLEPETTSAPNMNITSDESLAASKATTETEAIHVFENTAASHVETTSATEELYSSSPGFSEPTKVISPVVTSSSIRDNMVSTTMPGSSGITRIEIESMSSLTPGLRETRTSQDITSSTETSTVLYKMPSGATPEVSRTEVMPSSRTSIPGPAQSTMSLDISDEVVTRLSTSPIMTESAEITITTQTGYSLATSQVTLPLGTSMTFLSGTHSTMSQGLSHSEMTNLMSRGPESLSWTSPRFVETTRSSSSLTSLPLTTSLSPVSSTLLDSSPSSPLPVTSLILPGLVKTTEVLDTSSEPKTSSSPNLSSTSVEIPATSEIMTDTEKIHPSSNTAVAKVRTSSSVHESHSSVLADSETTITIPSMGITSAVDDTTVFTSNPAFSETRRIPTEPTFSLTPGFRETSTSEETTSITETSAVLYGVPTSATTEVSMTEIMSSNRIHIPDSDQSTMSPDIITEVITRLSSSSMMSESTQMTITTQKSSPGATAQSTLTLATTTAPLARTHSTVPPRFLHSEMTTLMSRSPENPSWKSSLFVEKTSSSSSLLSLPVTTSPSVSSTLPQSIPSSSFSVTSLLTPGMVKTTDTSTEPGTSLSPNLSGTSVEILAASEVTTDTEKIHPSSSMAVTNVGTTSSGHELYSSVSIHSEPSKATYPVGTPSSMAETSISTSMPANFETTGFEAEPFSHLTSGFRKTNMSLDTSSVTPTNTPSSPGSTHLLQSSKTDFTSSAKTSSPDWPPASQYTEIPVDIITPFNASPSITESTGITSFPESRFTMSVTESTHHLSTDLLPSAETISTGTVMPSLSEAMTSFATTGVPRAISGSGSPFSRTESGPGDATLSTIAESLPSSTPVPFSSSTFTTTDSSTIPALHEITSSSATPYRVDTSLGTESSTTEGRLVMVSTLDTSSQPGRTSSSPILDTRMTESVELGTVTSAYQVPSLSTRLTRTDGIMEHITKIPNEAAHRGTIRPVKGPQTSTSPASPKGLHTGGTKRMETTTTALKTTTTALKTTSRATLTTSVYTPTLGTLTPLNASMQMASTIPTEMMITTPYVFPDVPETTSSLATSLGAETSTALPRTTPSVFNRESETTASLVSRSGAERSPVIQTLDVSSSEPDTTASWVIHPAETIPTVSKTTPNFFHSELDTVSSTATSHGADVSSAIPTNISPSELDALTPLVTISGTDTSTTFPTLTKSPHETETRTTWLTHPAETSSTIPRTIPNFSHHESDATPSIATSPGAETSSAIPIMTVSPGAEDLVTSQVTSSGTDRNMTIPTLTLSPGEPKTIASLVTHPEAQTSSAIPTSTISPAVSRLVTSMVTSLAAKTSTTNRALTNSPGEPATTVSLVTHPAQTSPTVPWTTSIFFHSKSDTTPSMTTSHGAESSSAVPTPTVSTEVPGVVTPLVTSSRAVISTTIPILTLSPGEPETTPSMATSHGEEASSAIPTPTVSPGVPGVVTSLVTSSRAVTSTTIPILTFSLGEPETTPSMATSHGTEAGSAVPTVLPEVPGMVTSLVASSRAVTSTTLPTLTLSPGEPETTPSMATSHGAEASSTVPTVSPEVPGVVTSLVTSSSGVNSTSIPTLILSPGELETTPSMATSHGAEASSAVPTPTVSPGVSGVVTPLVTSSRAVTSTTIPILTLSSSEPETTPSMATSHGVEASSAVLTVSPEVPGMVTSLVTSSRAVTSTTIPTLTISSDEPETTTSLVTHSEAKMISAIPTLAVSPTVQGLVTSLVTSSGSETSAFSNLTVASSQPETIDSWVAHPGTEASSVVPTLTVSTGEPFTNISLVTHPAESSSTLPRTTSRFSHSELDTMPSTVTSPEAESSSAISTTISPGIPGVLTSLVTSSGRDISATFPTVPESPHESEATASWVTHPAVTSTTVPRTTPNYSHSEPDTTPSIATSPGAEATSDFPTITVSPDVPDMVTSQVTSSGTDTSITIPTLTLSSGEPETTTSFITYSETHTSSAIPTLPVSPGASKMLTSLVISSGTDSTTTFPTLTETPYEPETTAIQLIHPAETNTMVPRTTPKFSHSKSDTTLPVAITSPGPEASSAVSTTTISPDMSDLVTSLVPSSGTDTSTTFPTLSETPYEPETTATWLTHPAETSTTVSGTIPNFSHRGSDTAPSMVTSPGVDTRSGVPTTTIPPSIPGVVTSQVTSSATDTSTAIPTLTPSPGEPETTASSATHPGTQTGFTVPIRTVPSSEPDTMASWVTHPPQTSTPVSRTTSSFSHSSPDATPVMATSPRTEASSAVLTTISPGAPEMVTSQITSSGAATSTTVPTLTHSPGMPETTALLSTHPRTETSKTFPASTVFPQVSETTASLTIRPGAETSTALPTQTTSSLFTLLVTGTSRVDLSPTASPGVSAKTAPLSTHPGTETSTMIPTSTLSLGLLETTGLLATSSSAETSTSTLTLTVSPAVSGLSSASITTDKPQTVTSWNTETSPSVTSVGPPEFSRTVTGTTMTLIPSEMPTPPKTSHGEGVSPTTILRTTMVEATNLATTGSSPTVAKTTTTFNTLAGSLFTPLTTPGMSTLASESVTSRTSYNHRSWISTTSSYNRRYWTPATSTPVTSTFSPGISTSSIPSSTAATVPFMVPFTLNFTITNLQYEEDMRHPGSRKFNATERELQGLLKPLFRNSSLEYLYSGCRLASLRPEKDSSATAVDAICTHRPDPEDLGLDRERLYWELSNLTNGIQELGPYTLDRNSLYVNGFTHRSSMPTTSTPGTSTVDVGTSGTPSSSPSPTTAGPLLMPFTLNFTITNLQYEEDMRRTGSRKFNTMESVLQGLLKPLFKNTSVGPLYSGCRLTLLRPEKDGAATGVDAICTHRLDPKSPGLNREQLYWELSKLTNDIEELGPYTLDRNSLYVNGFTHQSSVSTTSTPGTSTVDLRTSGTPSSLSSPTIMAAGPLLVPFTLNFTITNLQYGEDMGHPGSRKFNTTERVLQGLLGPIFKNTSVGPLYSGCRLTSLRSEKDGAATGVDAICIHHLDPKSPGLNRERLYWELSQLTNGIKELGPYTLDRNSLYVNGFTHRTSVPTSSTPGTSTVDLGTSGTPFSLPSPATAGPLLVLFTLNFTITNLKYEEDMHRPGSRKFNTTERVLQTLLGPMFKNTSVGLLYSGCRLTLLRSEKDGAATGVDAICTHRLDPKSPGVDREQLYWELSQLTNGIKELGPYTLDRNSLYVNGFTHWIPVPTSSTPGTSTVDLGSGTPSSLPSPTTAGPLLVPFTLNFTITNLKYEEDMHCPGSRKFNTTERVLQSLLGPMFKNTSVGPLYSGCRLTLLRSEKDGAATGVDAICTHRLDPKSPGVDREQLYWELSQLTNGIKELGPYTLDRNSLYVNGFTHQTSAPNTSTPGTSTVDLGTSGTPSSLPSPTSAGPLLVPFTLNFTITNLQYEEDMHHPGSRKFNTTERVLQGLLGPMFKNTSVGLLYSGCRLTLLRPEKNGAATGMDAICSHRLDPKSPGLNREQLYWELSQLTHGIKELGPYTLDRNSLYVNGFTHRSSVAPTSTPGTSTVDLGTSGTPSSLPSPTTAVPLLVPFTLNFTITNLQYGEDMRHPGSRKFNTTERVLQGLLGPLFKNSSVGPLYSGCRLISLRSEKDGAATGVDAICTHHLNPQSPGLDREQLYWQLSQMTNGIKELGPYTLDRNSLYVNGFTHRSSGLTTSTPWTSTVDLGTSGTPSPVPSPTTTGPLLVPFTLNFTITNLQYEENMGHPGSRKFNITESVLQGLLKPLFKSTSVGPLYSGCRLTLLRPEKDGVATRVDAICTHRPDPKIPGLDRQQLYWELSQLTHSITELGPYTLDRDSLYVNGFTQRSSVPTTSTPGTFTVQPETSETPSSLPGPTATGPVLLPFTLNFTITNLQYEEDMRRPGSRKFNTTERVLQGLLMPLFKNTSVSSLYSGCRLTLLRPEKDGAATRVDAVCTHRPDPKSPGLDRERLYWKLSQLTHGITELGPYTLDRHSLYVNGFTHQSSMTTTRTPDTSTMHLATSRTPASLSGPMTASPLLVLFTINFTITNLRYEENMHHPGSRKFNTTERVLQGLLRPVFKNTSVGPLYSGCRLTLLRPKKDGAATKVDAICTYRPDPKSPGLDREQLYWELSQLTHSITELGPYTLDRDSLYVNGFTQRSSVPTTSIPGTPTVDLGTSGTPVSKPGPSAASPLLVLFTLNFTITNLRYEENMQHPGSRKFNTTERVLQGLLRSLFKSTSVGPLYSGCRLTLLRPEKDGTATGVDAICTHHPDPKSPRLDREQLYWELSQLTHNITELGPYALDNDSLFVNGFTHRSSVSTTSTPGTPTVYLGASKTPASIFGPSAASHLLILFTLNFTITNLRYEENMWPGSRKFNTTERVLQGLLRPLFKNTSVGPLYSGCRLTLLRPEKDGEATGVDAICTHRPDPTGPGLDREQLYLELSQLTHSITELGPYTLDRDSLYVNGFTHRSSVPTTSTGVVSEEPFTLNFTINNLRYMADMGQPGSLKFNITDNVMQHLLSPLFQRSSLGARYTGCRVIALRSVKNGAETRVDLLCTYLQPLSGPGLPIKQVFHELSQQTHGITRLGPYSLDKDSLYLNGYNEPGPDEPPTTPKPATTFLPPLSEATTAMGYHLKTLTLNFTISNLQYSPDMGKGSATFNSTEGVLQHLLRPLFQKSSMGPFYLGCQLISLRPEKDGAATGVDTTCTYHPDPVGPGLDIQQLYWELSQLTHGVTQLGFYVLDRDSLFINGYAPQNLSIRGEYQINFHIVNWNLSNPDPTSSEYITLLRDIQDKVTTLYKGSQLHDTFRFCLVTNLTMDSVLVTVKALFSSNLDPSLVEQVFLDKTLNASFHWLGSTYQLVDIHVTEMESSVYQPTSSSSTQHFYLNFTITNLPYSQDKAQPGTTNYQRNKRNIEDALNQLFRNSSIKSYFSDCQVSTFRSVPNRHHTGVDSLCNFSPLARRVDRVAIYEEFLRMTRNGTQLQNFTLDRSSVLVDGYSPNRNEPLTGNSDLPFWAVILIGLAGLLGVITCLICGVLVTTRRRKKEGEYNVQQQCPGYYQSHLDLEDLQ TTC1PS3 TT Clinical trial TTA4M1N ID TTA4M1N TTA4M1N TN Phosphatidylinositol-3-phosphate 5-kinase (PIP5K3) TTA4M1N UP Q9Y2I7 TTA4M1N UC FYV1_HUMAN TTA4M1N SN Type III PIP kinase; Phosphatidylinositol 3-phosphate 5-kinase type III; PIPkin-III; PIKfyve; FYVE finger-containing phosphoinositide kinase TTA4M1N GN PIKFYVE TTA4M1N FC The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. Plays a role in the biogenesis of endosome carrier vesicles (ECV)/ multivesicular bodies (MVB) transport intermediates from early endosomes. TTA4M1N EC EC 2.7.1.150 TTA4M1N SQ MATDDKTSPTLDSANDLPRSPTSPSHLTHFKPLTPDQDEPPFKSAYSSFVNLFRFNKERAEGGQGEQQPLSGSWTSPQLPSRTQSVRSPTPYKKQLNEELQRRSSALDTRRKAEPTFGGHDPRTAVQLRSLSTVLKRLKEIMEGKSQDSDLKQYWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRKIALSYAHSTDSNSIGEDLNALSDSACSVSVLDPSEPRTPVGSRKASRNIFLEDDLAWQSLIHPDSSNTPLSTRLVSVQEDAGKSPARNRSASITNLSLDRSGSPMVPSYETSVSPQANRTYVRTETTEDERKILLDSVQLKDLWKKICHHSSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDQLFRDEYALYRPLQSTEFSETPSPDSDSVNSVEGHSEPSWFKDIKFDDSDTEQIAEEGDDNLANSASPSKRTSVSSFQSTVDSDSAASISLNVELDNVNFHIKKPSKYPHVPPHPADQKEYLISDTGGQQLSISDAFIKESLFNRRVEEKSKELPFTPLGWHHNNLELLREENGEKQAMERLLSANHNHMMALLQQLLHSDSLSSSWRDIIVSLVCQVVQTVRPDVKNQDDDMDIRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIEYLYREETKFTCIDPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVMSMDQLLTKPHLGTCHKFYMQIFQLPNEQTKTLMFFEGCPQHLGCTIKLRGGSDYELARVKEILIFMICVAYHSQLEISFLMDEFAMPPTLMQNPSFHSLIEGRGHEGAVQEQYGGGSIPWDPDIPPESLPCDDSSLLELRIVFEKGEQENKNLPQAVASVKHQEHSTTACPAGLPCAFFAPVPESLLPLPVDDQQDALGSEQPETLQQTVVLQDPKSQIRAFRDPLQDDTGLYVTEEVTSSEDKRKTYSLAFKQELKDVILCISPVITFREPFLLTEKGMRCSTRDYFAEQVYWSPLLNKEFKEMENRRKKQLLRDLSGLQGMNGSIQAKSIQVLPSHELVSTRIAEHLGDSQSLGRMLADYRARGGRIQPKNSDPFAHSKDASSTSSGQSGSKNEGDEERGLILSDAVWSTKVDCLNPINHQRLCVLFSSSSAQSSNAPSACVSPWIVTMEFYGKNDLTLGIFLERYCFRPSYQCPSMFCDTPMVHHIRRFVHGQGCVQIILKELDSPVPGYQHTILTYSWCRICKQVTPVVALSNESWSMSFAKYLELRFYGHQYTRRANAEPCGHSIHHDYHQYFSYNQMVASFSYSPIRLLEVCVPLPKIFIKRQAPLKVSLLQDLKDFFQKVSQVYVAIDERLASLKTDTFSKTREEKMEDIFAQKEMEEGEFKNWIEKMQARLMSSSVDTPQQLQSVFESLIAKKQSLCEVLQAWNNRLQDLFQQEKGRKRPSVPPSPGRLRQGEESKISAMDASPRNISPGLQNGEKEDRFLTTLSSQSSTSSTHLQLPTPPEVMSEQSVGGPPELDTASSSEDVFDGHLLGSTDSQVKEKSTMKAIFANLLPGNSYNPIPFPFDPDKHYLMYEHERVPIAVCEKEPSSIIAFALSCKEYRNALEELSKATQWNSAEEGLPTNSTSDSRPKSSSPIRLPEMSGGQTNRTTETEPQPTKKASGMLSFFRGTAGKSPDLSSQKRETLRGADSAYYQVGQTGKEGTENQGVEPQDEVDGGDTQKKQLINPHVELQFSDANAKFYCRLYYAGEFHKMREVILDSSEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYITNAVQQKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENLLKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTFTWDKKLEMVVKSTGILGGQGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTGLGLNC TTA4M1N TT Clinical trial TTA4M1N KE hsa00562:Inositol phosphate metabolism; hsa01100:Metabolic pathways; hsa04070:Phosphatidylinositol signaling system; hsa04145:Phagosome; hsa04810:Regulation of actin cytoskeleton TTRLMKF ID TTRLMKF TTRLMKF TN Phospholipase D2 (PLD2) TTRLMKF UP O14939 TTRLMKF UC PLD2_HUMAN TTRLMKF BC Phosphoric diester hydrolase TTRLMKF SN hPLD2; Phosphatidylcholine-hydrolyzing phospholipase D2; PLD1C; PLD 2; Choline phosphatase 2 TTRLMKF GN PLD2 TTRLMKF FC May have a role in signal-induced cytoskeletal regulation and/or endocytosis. TTRLMKF EC EC 3.1.4.4 TTRLMKF SQ MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFAPGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVLMSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVVKDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQARWWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRALMLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSESAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPWRDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQCTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICDDFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQGHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT TTRLMKF TT Clinical trial TTZKPVC ID TTZKPVC TTZKPVC TN Phosphorylated p68 RNA helicase (pDDX5) TTZKPVC UP P17844 (phosphorylated) TTZKPVC UC DDX5_HUMAN TTZKPVC SN RNA helicase p68 (phosphorylated); Probable ATP-dependent RNA helicase DDX5 (phosphorylated); HLR1 (phosphorylated); HELR (phosphorylated); G17P1 (phosphorylated); DEAD box protein 5 (phosphorylated) TTZKPVC GN DDX5 TTZKPVC FC Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. TTZKPVC EC EC 3.6.4.13 TTZKPVC PD 4A4D; 3FE2 TTZKPVC SQ MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ TTZKPVC TT Clinical trial TT87Q2D ID TT87Q2D TT87Q2D TN Picornavirus Capsid protein VP1 (PicVir VP1) TT87Q2D UP Q83884 TT87Q2D UC CAPSD_NVN68 TT87Q2D BC Caliciviridae capsid protein TT87Q2D SN p30; Soluble capsid protein; ORF2; Capsid protein VP1; CP of Norwalk virus TT87Q2D GN PicVir VP1 TT87Q2D FC Soluble capsid protein may play arole in viral immunoevasion. TT87Q2D PD 6H72; 6H71; 6H70; 6H6Z; 6H6Y TT87Q2D SQ MMMASKDATSSVDGASGAGQLVPEVNASDPLAMDPVAGSSTAVATAGQVNPIDPWIINNFVQAPQGEFTISPNNTPGDVLFDLSLGPHLNPFLLHLSQMYNGWVGNMRVRIMLAGNAFTAGKIIVSCIPPGFGSHNLTIAQATLFPHVIADVRTLDPIEVPLEDVRNVLFHNNDRNQQTMRLVCMLYTPLRTGGGTGDSFVVAGRVMTCPSPDFNFLFLVPPTVEQKTRPFTLPNLPLSSLSNSRAPLPISSMGISPDNVQSVQFQNGRCTLDGRLVGTTPVSLSHVAKIRGTSNGTVINLTELDGTPFHPFEGPAPIGFPDLGGCDWHINMTQFGHSSQTQYDVDTTPDTFVPHLGSIQANGIGSGNYVGVLSWISPPSHPSGSQVDLWKIPNYGSSITEATHLAPSVYPPGFGEVLVFFMSKMPGPGAYNLPCLLPQEYISHLASEQAPTVGEAALLHYVDPDTGRNLGEFKAYPDGFLTCVPNGASSGPQQLPINGVFVFVSWVSRFYQLKPVGTASSARGRLGLRR TT87Q2D TT Clinical trial TTQZW34 ID TTQZW34 TTQZW34 TN Plasmodium Apical membrane protein (Malaria AMA-1) TTQZW34 UP P22621 TTQZW34 UC AMA1_PLAFF TTQZW34 BC Apicomplexan parasites AMA1 TTQZW34 SN Merozoite surface antigen; Apical membrane antigen 1; AMA1; AMA-1 TTQZW34 GN Malaria AMA-1 TTQZW34 FC Involved in parasite invasion of erythrocytes. TTQZW34 PD 2Q8B; 2Q8A; 1YXE TTQZW34 SQ MRKLYCVLLLSAFEFTYMINFGRGQNYWEHPYQKSDVYHPINEHREHPKEYQYPLHQEHTYQQEDSGEDENTLQHAYPIDHEGAEPAPQEQNLFSSIEIVERSNYMGNPWTEYMAKYDIEEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSNTTFLTPVATGNQYLKDGGFAFPPTEPLMSPMTLDEMRHFYKDNKYVKNLDELTLCSRHAGNMIPDNDKNSNYKYPAVYDDKDKKCHILYIAAQENNGPRYCNKDESKRNSMFCFRPAKDISFQNYTYLSKNVVDNWEKVCPRKNLQNAKFGLWVDGNCEDIPHVNEFSAIDLFECNKLVFELSASDQPKQYEQHLTDYEKIKEGFKNKNASMIKSAFLPTGAFKADRYKSHGKGYNWGNYNTETQKCEIFNVKPTCLINNSSYIATTALSHPIEVEHNFPCSLYKNEIMKEIERESKRIKLNDNDDEGNKKIIAPRIFISDDKDSLKCPCDPEIVSNSTCNFFVCKCVERRAEVTSNNEVVVKEEYKDEYADIPEHKPTYDKMKIIIASSAAVAVLATILMVYLYKRKGNAEKYDKMDEPQHYGKSNSRNDEMLDPEASFWGEEKRASHTTPVLMEKPYY TTQZW34 TT Clinical trial TTHPFTS ID TTHPFTS TTHPFTS TN Plasmodium Beta-hydroxyacyl-ACP dehydratase (Malaria FabZ) TTHPFTS UP Q965D7 TTHPFTS UC Q965D7_PLAFA TTHPFTS SN fabZ; Fatty acid synthesis protein; Beta-hydroxyacyl-ACP dehydratase; 17 kDa actomyosin component; (3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; (3R)-hydroxymyristoyl-ACP dehydrase TTHPFTS GN Malaria FabZ TTHPFTS FC Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. TTHPFTS PD 3AZB; 3AZA; 3AZ9; 3AZ8; 2OKI TTHPFTS SQ MRFLIIHIAVIVLPFVLMIDVKRENSFFLRHSPKRLYKKADYNNMYDKIIKKQQNRIYDVSSQINQDNINGQNISFNLTFPNYDTSIDIEDIKKILPHRYPFLLVDKVIYMQPNKTIIGLKQVSTNEPFFNGHFPQKQIMPGVLQIEALAQLAGILCLKSDDSQKNNLFLFAGVDGVRWKKPVLPGDTLTMQANLISFKSSLGIAKLSGVGYVNGKVVINISEMTFALSK TTHPFTS TT Clinical trial TTHPFTS FM Thioester dehydratase family TTHPFTS KE pfa00061:Fatty acid biosynthesis; pfa00780:Biotin metabolism; pfa01100:Metabolic pathways; pfa01212:Fatty acid metabolism TTVB0Q9 ID TTVB0Q9 TTVB0Q9 TN Platelet glycoprotein Ib alpha (CD42b) TTVB0Q9 UP P07359 TTVB0Q9 UC GP1BA_HUMAN TTVB0Q9 SN Platelet glycoprotein Ib alpha chain; Glycoprotein Ibalpha; Glycocalicin; GPIbalpha; GPIbA; GPIb-alpha; GPIb alpha; GP-Ib alpha; Antigen CD42balpha; Antigen CD42b-alpha TTVB0Q9 GN GP1BA TTVB0Q9 FC GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium. TTVB0Q9 PD 4YR6; 4MGX; 4CH8; 4CH2; 4C2B TTVB0Q9 SQ MPLLLLLLLLPSPLHPHPICEVSKVASHLEVNCDKRNLTALPPDLPKDTTILHLSENLLYTFSLATLMPYTRLTQLNLDRCELTKLQVDGTLPVLGTLDLSHNQLQSLPLLGQTLPALTVLDVSFNRLTSLPLGALRGLGELQELYLKGNELKTLPPGLLTPTPKLEKLSLANNNLTELPAGLLNGLENLDTLLLQENSLYTIPKGFFGSHLLPFAFLHGNPWLCNCEILYFRRWLQDNAENVYVWKQGVDVKAMTSNVASVQCDNSDKFPVYKYPGKGCPTLGDEGDTDLYDYYPEEDTEGDKVRATRTVVKFPTKAHTTPWGLFYSWSTASLDSQMPSSLHPTQESTKEQTTFPPRWTPNFTLHMESITFSKTPKSTTEPTPSPTTSEPVPEPAPNMTTLEPTPSPTTPEPTSEPAPSPTTPEPTSEPAPSPTTPEPTSEPAPSPTTPEPTPIPTIATSPTILVSATSLITPKSTFLTTTKPVSLLESTKKTIPELDQPPKLRGVLQGHLESSRNDPFLHPDFCCLLPLGFYVLGLFWLLFASVVLILLLSWVGHVKPQALDSGQGAALTTATQTTHLELQRGRQVTVPRAWLLFLRGSLPTFRSSLFLWVRPNGRVGPLVAGRRPSALSQGRGQDLLSTVSIRYSGHSL TTVB0Q9 TT Clinical trial TTVB0Q9 FM Leucine rich repeat TTVB0Q9 KE hsa04512:ECM-receptor interaction; hsa04611:Platelet activation; hsa04640:Hematopoietic cell lineage TTVB0Q9 RC R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-430116:GP1b-IX-V activation signalling; R-HSA-75892:Platelet Adhesion to exposed collagen TTSM78N ID TTSM78N TTSM78N TN Platelet-derived growth factor A (PDGFA) TTSM78N UP P04085 TTSM78N UC PDGFA_HUMAN TTSM78N BC Growth factor TTSM78N SN Platelet-derived growth factor subunit A; Platelet-derived growth factor alpha polypeptide; Platelet-derived growth factor A chain; Platelet derived growth factor; PDGF1; PDGF-1; PDGF subunit A; PDGF; C-SIS oncogene TTSM78N GN PDGFA TTSM78N FC Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. TTSM78N PD 3MJK TTSM78N SQ MRTLACLLLLGCGYLAHVLAEEAEIPREVIERLARSQIHSIRDLQRLLEIDSVGSEDSLDTSLRAHGVHATKHVPEKRPLPIRRKRSIEEAVPAVCKTRTVIYEIPRSQVDPTSANFLIWPPCVEVKRCTGCCNTSSVKCQPSRVHHRSVKVAKVEYVRKKPKLKEVQVRLEEHLECACATTSLNPDYREEDTGRPRESGKKRKRKRLKPT TTSM78N TT Clinical trial TTSM78N FM Growth factor TTQ7ABG ID TTQ7ABG TTQ7ABG TN Positive transcription elongation factor b (P-TEFb) TTQ7ABG UP P50750-O60563 TTQ7ABG UC CDK9_HUMAN-CCNT1_HUMAN TTQ7ABG BC S-phase kinase-associated protein TTQ7ABG SN P-TEFb TTQ7ABG GN CDK9-CCNT1 TTQ7ABG FC The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC- box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes. TTQ7ABG SQ MEGERKNNNKRWYFTREQLENSPSRRFGVDPDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMIQSFTQFPGNSVAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPDTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATNSLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTHEFLQILEKTPNRLKRIWNWRACEAAKKTKADDRGTDEKTSEQTILNMISQSSSDTTIAGLMSMSTSTTSAVPSLPVSEESSSNLTSVEMLPGKRWLSSQPSFKLEPTQGHRTSENLALTGVDHSLPQDGSNAFISQKQNSKSVPSAKVSLKEYRAKHAEELAAQKRQLENMEANVKSQYAYAAQNLLSHHDSHSSVILKMPIEGSENPERPFLEKADKTALKMRIPVAGGDKAASSKPEEIKMRIKVHAAADKHNSVEDSVTKSREHKEKHKTHPSNHHHHHNHHSHKHSHSQLPVGTGNKRPGDPKHSSQTSNLAHKTYSLSSSFSSSSSTRKRGPSEETGGAVFDHPAKIAKSTKSSSLNFSFPSLPTMGQMPGHSSDTSGLSFSQPSCKTRVPHSKLDKGPTGANGHNTTQTIDYQDTVNMLHSLLSAQGVQPTQPTAFEFVRPYSDYLNPRSGGISSRSGNTDKPRPPPLPSEPPPPLPPLPKMAKQYDSVECPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVLVKFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLALISQLCGSITPEVWPNVDNYELYEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKGMLSTHLTSMFEYLAPPRRKGSQITQQSTNQSRNPATTNQTEFERVF TTQ7ABG TT Clinical trial TTQ7ABG KE hsa04066:HIF-1 signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa05200:Pathways in cancer; hsa05211:Renal cell carcinoma TTLG1PD ID TTLG1PD TTLG1PD TN Proliferating cell nuclear antigen (PCNA) TTLG1PD UP P12004 TTLG1PD UC PCNA_HUMAN TTLG1PD SN Cyclin TTLG1PD GN PCNA TTLG1PD FC Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion. Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. TTLG1PD PD 6QCG; 6QC0; 6HVO; 6GWS; 6GIS TTLG1PD SQ MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS TTLG1PD TT Clinical trial TTLG1PD FM Proliferating cell nuclear antigen TTLG1PD KE hsa03030:DNA replication; hsa03410:Base excision repair; hsa03420:Nucleotide excision repair; hsa03430:Mismatch repair; hsa04110:Cell cycle; hsa05161:Hepatitis B; hsa05166:HTLV-I infection TTLG1PD RC R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-1538133:G0 and Early G1; R-HSA-5358565:Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha); R-HSA-5358606:Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta); R-HSA-5685942:HDR through Homologous Recombination (HRR); R-HSA-5696400:Dual Incision in GG-NER; R-HSA-6782135:Dual incision in TC-NER; R-HSA-6782210:Gap-filling DNA repair synthesis and ligation in TC-NER; R-HSA-69205:G1/S-Specific Transcription TTEH395 ID TTEH395 TTEH395 TN Pro-neuregulin-1 (Pro-NRG1) TTEH395 UP Q02297 TTEH395 UC NRG1_HUMAN TTEH395 SN SMDF (20-241); Pro-neuregulin-1, membrane-bound isoform (20-241); NDF (20-241); Heregulin (20-241); HRGA (20-241); HGL (20-241); GGF (20-241) TTEH395 GN NRG1 TTEH395 FC Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Isoform 10 may play a role in motor and sensory neuron development. Binds to ERBB4. Binds to ERBB3. Acts as a ligand for integrins and binds (via EGF domain) to integrins ITGAV:ITGB3 or ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and ERRB3 are essential for NRG1-ERBB signaling. Induces the phosphorylation and activation of MAPK3/ERK1, MAPK1/ERK2 and AKT1. Ligand-dependent ERBB4 endocytosis is essential for the NRG1-mediated activation of these kinases in neurons. Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. TTEH395 PD 3U7U; 1HRF; 1HRE; 1HAF; 1HAE TTEH395 SQ MSERKEGRGKGKGKKKERGSGKKPESAAGSQSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNEIITGMPASTEGAYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCQPGFTGARCTENVPMKVQNQEKAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRKKLHDRLRQSLRSERNNMMNIANGPHHPNPPPENVQLVNQYVSKNVISSEHIVEREAETSFSTSHYTSTAHHSTTVTQTPSHSWSNGHTESILSESHSVIVMSSVENSRHSSPTGGPRGRLNGTGGPRECNSFLRHARETPDSYRDSPHSERYVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVSMPSMAVSPFMEEERPLLLVTPPRLREKKFDHHPQQFSSFHHNPAHDSNSLPASPLRIVEDEEYETTQEYEPAQEPVKKLANSRRAKRTKPNGHIANRLEVDSNTSSQSSNSESETEDERVGEDTPFLGIQNPLAASLEATPAFRLADSRTNPAGRFSTQEEIQARLSSVIANQDPIAV TTEH395 TT Clinical trial TTEH395 KE hsa04012:ErbB signaling pathway TTEH395 RC R-HSA-1250196:SHC1 events in ERBB2 signaling; R-HSA-1250342:PI3K events in ERBB4 signaling; R-HSA-1250347:SHC1 events in ERBB4 signaling; R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1963640:GRB2 events in ERBB2 signaling; R-HSA-1963642:PI3K events in ERBB2 signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5673001:RAF/MAP kinase cascade TTXCSDR ID TTXCSDR TTXCSDR TN Protein bactericidal permeability-increasing (BPI) TTXCSDR UP P17213 TTXCSDR UC BPI_HUMAN TTXCSDR BC Bactericidal permeability increasing protein TTXCSDR SN CAP 57; BPI TTXCSDR GN BPI TTXCSDR FC The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. {ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:2722846}. TTXCSDR PD 1EWF; 1BP1 TTXCSDR SQ MRENMARGPCNAPRWASLMVLVAIGTAVTAAVNPGVVVRISQKGLDYASQQGTAALQKELKRIKIPDYSDSFKIKHLGKGHYSFYSMDIREFQLPSSQISMVPNVGLKFSISNANIKISGKWKAQKRFLKMSGNFDLSIEGMSISADLKLGSNPTSGKPTITCSSCSSHINSVHVHISKSKVGWLIQLFHKKIESALRNKMNSQVCEKVTNSVSSELQPYFQTLPVMTKIDSVAGINYGLVAPPATTAETLDVQMKGEFYSENHHNPPPFAPPVMEFPAAHDRMVYLGLSDYFFNTAGLVYQEAGVLKMTLRDDMIPKESKFRLTTKFFGTFLPEVAKKFPNMKIQIHVSASTPPHLSVQPTGLTFYPAVDVQAFAVLPNSSLASLFLIGMHTTGSMEVSAESNRLVGELKLDRLLLELKHSNIGPFPVELLQDIMNYIVPILVLPRVNEKLQKGFPLPTPARVQLYNVVLQPHQNFLLFGADVVYK TTXCSDR TT Clinical trial TT9AH0M ID TT9AH0M TT9AH0M TN Protein C-ets-2 (ETS2) TT9AH0M UP P15036 TT9AH0M UC ETS2_HUMAN TT9AH0M BC E26 transformation-specific ETS TT9AH0M SN ETS2IT1; ETS proto-oncogene 2, transcription factor TT9AH0M GN ETS2 TT9AH0M FC Binds specifically the DNA GGAA/T core motif (Ets-binding site or EBS) in gene promoters and stimulates transcription. Transcription factor activating transcription. TT9AH0M PD 4MHV; 4BQA TT9AH0M SQ MNDFGIKNMDQVAPVANSYRGTLKRQPAFDTFDGSLFAVFPSLNEEQTLQEVPTGLDSISHDSANCELPLLTPCSKAVMSQALKATFSGFKKEQRRLGIPKNPWLWSEQQVCQWLLWATNEFSLVNVNLQRFGMNGQMLCNLGKERFLELAPDFVGDILWEHLEQMIKENQEKTEDQYEENSHLTSVPHWINSNTLGFGTEQAPYGMQTQNYPKGGLLDSMCPASTPSVLSSEQEFQMFPKSRLSSVSVTYCSVSQDFPGSNLNLLTNNSGTPKDHDSPENGADSFESSDSLLQSWNSQSSLLDVQRVPSFESFEDDCSQSLCLNKPTMSFKDYIQERSDPVEQGKPVIPAAVLAGFTGSGPIQLWQFLLELLSDKSCQSFISWTGDGWEFKLADPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTSGKRYVYRFVCDLQNLLGFTPEELHAILGVQPDTED TT9AH0M TT Clinical trial TTNFBTO ID TTNFBTO TTNFBTO TN Protein-serine O-palmitoleoyltransferase porcupine (PORCN) TTNFBTO UP Q9H237 TTNFBTO UC PORCN_HUMAN TTNFBTO BC Acyltransferase TTNFBTO SN Protein-cysteine N-palmitoyltransferase porcupine; Protein MG61; PORCN TTNFBTO GN PORCN TTNFBTO FC protein-cysteine N-palmitoyltransferase that modulates the processingof Wnt proteins by mediating serine palmitoylation of Wnt family members. TTNFBTO EC EC 2.3.1.250 TTNFBTO SQ MATFSRQEFFQQLLQGCLLPTAQQGLDQIWLLLAICLACRLLWRLGLPSYLKHASTVAGGFFSLYHFFQLHMVWVVLLSLLCYLVLFLCRHSSHRGVFLSVTILIYLLMGEMHMVDTVTWHKMRGAQMIVAMKAVSLGFDLDRGEVGTVPSPVEFMGYLYFVGTIVFGPWISFHSYLQAVQGRPLSCRWLQKVARSLALALLCLVLSTCVGPYLFPYFIPLNGDRLLRNKKRKARGTMVRWLRAYESAVSFHFSNYFVGFLSEATATLAGAGFTEEKDHLEWDLTVSKPLNVELPRSMVEVVTSWNLPMSYWLNNYVFKNALRLGTFSAVLVTYAASALLHGFSFHLAAVLLSLAFITYVEHVLRKRLARILSACVLSKRCPPDCSHQHRLGLGVRALNLLFGALAIFHLAYLGSLFDVDVDDTTEEQGYGMAYTVHKWSELSWASHWVTFGCWIFYRLIG TTNFBTO TT Clinical trial TTS5K8U ID TTS5K8U TTS5K8U TN P-selectin glycoprotein ligand 1 (SELPLG) TTS5K8U UP Q14242 TTS5K8U UC SELPL_HUMAN TTS5K8U SN Selectin P ligand; SPSGL-1; SELPLG; PSGL-1; P-selectin glycoprotein ligand-1; CD162 antigen TTS5K8U GN SELPLG TTS5K8U FC A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture. TTS5K8U PD 1G1S TTS5K8U SQ MPLQLLLLLILLGPGNSLQLWDTWADEAEKALGPLLARDRRQATEYEYLDYDFLPETEPPEMLRNSTDTTPLTGPGTPESTTVEPAARRSTGLDAGGAVTELTTELANMGNLSTDSAAMEIQTTQPAATEAQTTQPVPTEAQTTPLAATEAQTTRLTATEAQTTPLAATEAQTTPPAATEAQTTQPTGLEAQTTAPAAMEAQTTAPAAMEAQTTPPAAMEAQTTQTTAMEAQTTAPEATEAQTTQPTATEAQTTPLAAMEALSTEPSATEALSMEPTTKRGLFIPFSVSSVTHKGIPMAASNLSVNYPVGAPDHISVKQCLLAILILALVATIFFVCTVVLAVRLSRKGHMYPVRNYSPTEMVCISSLLPDGGEGPSATANGGLSKAKSPGLTPEPREDREGDDLTLHSFLP TTS5K8U TT Clinical trial TTS5K8U KE hsa04514:Cell adhesion molecules (CAMs); hsa05150:Staphylococcus aureus infection TTS5K8U RC R-HSA-202733:Cell surface interactions at the vascular wall TTJZ7GF ID TTJZ7GF TTJZ7GF TN Pseudomonas LPS-assembly protein LptD (Pseudo lptD) TTJZ7GF UP Q9I5U2 TTJZ7GF UC LPTD_PSEAE TTJZ7GF BC LptD family TTJZ7GF SN ostA; Pseudo imp TTJZ7GF GN Pseudo lptD TTJZ7GF FC Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. TTJZ7GF PD 5IVA TTJZ7GF SQ MAVKSLVFRRKFPLLVTGSLLALQPVAALTVQAADQFDCKVSATGGWDCSPLQNANANLPPRPAHTATSVSTAAAGSSVSGSGGETVEAEPTQRLVTESGGRALKSRSADYSHLDWIPREKLTAAQLAEIGPYCGGSYIEPVRPGMDDGAPSDESPTYVSAKASRYEQEKQIATLAGDVVLRQGSMQVEGDEANLHQLENRGELVGNVKLRDKGMLVVGDHAQVQLDNGEAQVDNAEYVIHKAHARGSALYAKRSENAIIMLKDGTYTRCEPSSNAWTLKGNNVKLNPATGFGTATNATLRVKDFPVFYTPYIYFPIDDRRQSGFLPPSFSSTSDTGFTLVTPYYFNLAPNYDATLYPRYMAKRGMMLEGEFRYLTHSSEGIVNAAYLNDKDDHREGFPDYSKDRWLYGLKNTTGLDSRWLAEVDYTRISDPYYFQDLDTDLGVGSTTYVNQRGTLTYRGDTFTGRLNAQAYQLATTTDVTPYDRLPQITFDGFLPYNPGGMQFTYGTEFVRFDRDLDENIYFNDDGSIRGKRPDASLQGLARATGDRMHLEPGMSLPMTRSWGYVTPTLKYLYTKYDLDLDSQGKTDLNKRDESFDSNQDRSLPLVKVDSGLYFDRDTTFAGTPFRQTLEPRAMYLYVPYKDQDSLPVFDTSEPSFSYDSLWRENRFTGKDRIGDANQLSLGVTSRFIEENGFERASISAGQIYYFRDRRVQLPGLTEKDLKRLNLDPSGLDNDSWRSPYAFAGQYRFNRDWRINSDFNWNPNTSRTESGSAIFHYQPEVDPGKVVNVGYRYRADARRFDSSRGTFRYGNENDIIKQHDFSVIWPLVPQWSVLARWQYDYNKNRTLEAFGGFEYDSCCWKLRLINRYWLDVDDDAFLVQSEKADRGIFLQIVLKGLGGIVGNKTEMFLDKGIQGYRQREDQAM TTJZ7GF TT Clinical trial TTL4H8N ID TTL4H8N TTL4H8N TN Regenerating human pro-islet peptide (REG3A) TTL4H8N UP Q06141 TTL4H8N UC REG3A_HUMAN TTL4H8N SN Regenerating islet-derived protein III-alpha; Regenerating islet-derived protein 3-alpha 15 kDa form; Regenerating islet-derived protein 3-alpha; Reg III-alpha; REG3A; REG-3-alpha; Pancreatitis-associated protein 1; Human proislet peptide; Hepatointestinal pancreatic protein; HIP/PAP TTL4H8N GN REG3A TTL4H8N FC Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Regulates keratinocyte proliferation and differentiation after skin injury via activation of EXTL3-PI3K-AKT signaling pathway. TTL4H8N PD 4MTH; 2GO0; 1UV0 TTL4H8N SQ MLPPMALPSVSWMLLSCLMLLSQVQGEEPQRELPSARIRCPKGSKAYGSHCYALFLSPKSWTDADLACQKRPSGNLVSVLSGAEGSFVSSLVKSIGNSYSYVWIGLHDPTQGTEPNGEGWEWSSSDVMNYFAWERNPSTISSPGHCASLSRSTAFLRWKDYNCNVRLPYVCKFTD TTL4H8N TT Clinical trial TTMAHD1 ID TTMAHD1 TTMAHD1 TN Relaxin receptor 1 (RXFP1) TTMAHD1 UP Q9HBX9 TTMAHD1 UC RXFP1_HUMAN TTMAHD1 BC GPCR rhodopsin TTMAHD1 SN Relaxin family peptide receptor 1; RXFP1; Leucine-rich repeat-containing G-protein coupled receptor 7 TTMAHD1 GN RXFP1 TTMAHD1 FC Receptor for relaxins. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. Binding of the ligand may also activate a tyrosine kinase pathway that inhibits the activity of a phosphodiesterase that degrades cAMP. TTMAHD1 PD 2M7P; 2JM4 TTMAHD1 SQ MTSGSVFFYILIFGKYFSHGGGQDVKCSLGYFPCGNITKCLPQLLHCNGVDDCGNQADEDNCGDNNGWSLQFDKYFASYYKMTSQYPFEAETPECLVGSVPVQCLCQGLELDCDETNLRAVPSVSSNVTAMSLQWNLIRKLPPDCFKNYHDLQKLYLQNNKITSISIYAFRGLNSLTKLYLSHNRITFLKPGVFEDLHRLEWLIIEDNHLSRISPPTFYGLNSLILLVLMNNVLTRLPDKPLCQHMPRLHWLDLEGNHIHNLRNLTFISCSNLTVLVMRKNKINHLNENTFAPLQKLDELDLGSNKIENLPPLIFKDLKELSQLNLSYNPIQKIQANQFDYLVKLKSLSLEGIEISNIQQRMFRPLMNLSHIYFKKFQYCGYAPHVRSCKPNTDGISSLENLLASIIQRVFVWVVSAVTCFGNIFVICMRPYIRSENKLYAMSIISLCCADCLMGIYLFVIGGFDLKFRGEYNKHAQLWMESTHCQLVGSLAILSTEVSVLLLTFLTLEKYICIVYPFRCVRPGKCRTITVLILIWITGFIVAFIPLSNKEFFKNYYGTNGVCFPLHSEDTESIGAQIYSVAIFLGINLAAFIIIVFSYGSMFYSVHQSAITATEIRNQVKKEMILAKRFFFIVFTDALCWIPIFVVKFLSLLQVEIPGTITSWVVIFILPINSALNPILYTLTTRPFKEMIHRFWYNYRQRKSMDSKGQKTYAPSFIWVEMWPLQEMPPELMKPDLFTYPCEMSLISQSTRLNSYS TTMAHD1 TT Clinical trial TT25A0I ID TT25A0I TT25A0I TN Respiratory syncytial virus protein N (RSV N) TT25A0I UP P03418 TT25A0I UC NCAP_HRSVA TT25A0I BC Paramyxoviruses nucleocapsid TT25A0I SN RSV Protein N; RSV Nucleoprotein; RSV Nucleocapsid protein; N TT25A0I GN RSV N TT25A0I FC Encapsidates the genome, protecting it from nucleases. The nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases. TT25A0I PD 4UCE; 4UCD; 4UCC; 4UCB; 4UCA TT25A0I SQ MALSKVKLNDTLNKDQLLSSSKYTIQRSTGDSIDTPNYDVQKHINKLCGMLLITEDANHKFTGLIGMLYAMSRLGREDTIKILRDAGYHVKANGVDVTTHRQDINGKEMKFEVLTLASLTTEIQINIEIESRKSYKKMLKEMGEVAPEYRHDSPDCGMIILCIAALVITKLAAGDRSGLTAVIRRANNVLKNEMKRYKGLLPKDIANSFYEVFEKHPHFIDVFVHFGIAQSSTRGGSRVEGIFAGLFMNAYGAGQVMLRWGVLAKSVKNIMLGHASVQAEMEQVVEVYEYAQKLGGEAGFYHILNNPKASLLSLTQFPHFSSVVLGNAAGLGIMGEYRGTPRNQDLYDAAKAYAEQLKENGVINYSVLDLTAEELEAIKHQLNPKDNDVEL TT25A0I TT Clinical trial TT7GXMU ID TT7GXMU TT7GXMU TN Reticulon-4 (RTN4) TT7GXMU UP Q9NQC3 TT7GXMU UC RTN4_HUMAN TT7GXMU SN SP1507; My043 TT7GXMU GN RTN4 TT7GXMU FC Required to induce the formation and stabilization of endoplasmic reticulum (ER) tubules. They regulate membrane morphogenesis in the ER by promoting tubular ER production. They influence nuclear envelope expansion, nuclear pore complex formation and proper localization of inner nuclear membrane proteins. However each isoform have specific functions mainly depending on their tissue expression specificities. TT7GXMU PD 2JV5; 2G31 TT7GXMU SQ MEDLDQSPLVSSSDSPPRPQPAFKYQFVREPEDEEEEEEEEEEDEDEDLEELEVLERKPAAGLSAAPVPTAPAAGAPLMDFGNDFVPPAPRGPLPAAPPVAPERQPSWDPSPVSSTVPAPSPLSAAAVSPSKLPEDDEPPARPPPPPPASVSPQAEPVWTPPAPAPAAPPSTPAAPKRRGSSGSVDETLFALPAASEPVIRSSAENMDLKEQPGNTISAGQEDFPSVLLETAASLPSLSPLSAASFKEHEYLGNLSTVLPTEGTLQENVSEASKEVSEKAKTLLIDRDLTEFSELEYSEMGSSFSVSPKAESAVIVANPREEIIVKNKDEEEKLVSNNILHNQQELPTALTKLVKEDEVVSSEKAKDSFNEKRVAVEAPMREEYADFKPFERVWEVKDSKEDSDMLAAGGKIESNLESKVDKKCFADSLEQTNHEKDSESSNDDTSFPSTPEGIKDRSGAYITCAPFNPAATESIATNIFPLLGDPTSENKTDEKKIEEKKAQIVTEKNTSTKTSNPFLVAAQDSETDYVTTDNLTKVTEEVVANMPEGLTPDLVQEACESELNEVTGTKIAYETKMDLVQTSEVMQESLYPAAQLCPSFEESEATPSPVLPDIVMEAPLNSAVPSAGASVIQPSSSPLEASSVNYESIKHEPENPPPYEEAMSVSLKKVSGIKEEIKEPENINAALQETEAPYISIACDLIKETKLSAEPAPDFSDYSEMAKVEQPVPDHSELVEDSSPDSEPVDLFSDDSIPDVPQKQDETVMLVKESLTETSFESMIEYENKEKLSALPPEGGKPYLESFKLSLDNTKDTLLPDEVSTLSKKEKIPLQMEELSTAVYSNDDLFISKEAQIRETETFSDSSPIEIIDEFPTLISSKTDSFSKLAREYTDLEVSHKSEIANAPDGAGSLPCTELPHDLSLKNIQPKVEEKISFSDDFSKNGSATSKVLLLPPDVSALATQAEIESIVKPKVLVKEAEKKLPSDTEKEDRSPSAIFSAELSKTSVVDLLYWRDIKKTGVVFGASLFLLLSLTVFSIVSVTAYIALALLSVTISFRIYKGVIQAIQKSDEGHPFRAYLESEVAISEELVQKYSNSALGHVNCTIKELRRLFLVDDLVDSLKFAVLMWVFTYVGALFNGLTLLILALISLFSVPVIYERHQAQIDHYLGLANKNVKDAMAKIQAKIPGLKRKAE TT7GXMU TT Clinical trial TT7GXMU RC R-HSA-193634:Axonal growth inhibition (RHOA activation) TTGW0DV ID TTGW0DV TTGW0DV TN Rhinovirus Protease 3C (HRV P3C) TTGW0DV UP P04936 (1515-1696) TTGW0DV UC POLG_HRV2 TTGW0DV SN Rhinovirus P3C TTGW0DV GN HRV P3C TTGW0DV FC Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host VLDLR to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity). TTGW0DV EC EC 3.4.22.28 TTGW0DV PD 6FFS; 6FFN; 5FX6; 5FX5; 4L3B TTGW0DV SQ MSLIKHNSCVITTENGKFTGLGVYDRFVVVPTHADPGKEIQVDGITTKVIDSYDLYNKNGIKLEITVLKLDRNEKFRDIRRYIPNNEDDYPNCNLALLANQPEPTIINVGDVVSYGNILLSGNQTARMLKYSYPTKSGYCGGVLYKIGQVLGIHVGGNGRDGFSAMLLRSYFTDVQGQITLS TTGW0DV TT Clinical trial TT7HJTF ID TT7HJTF TT7HJTF TN R-spondin-3 (RSPO3) TT7HJTF UP Q9BXY4 TT7HJTF UC RSPO3_HUMAN TT7HJTF BC R-spondin family TT7HJTF SN hRspo3; hPWTSR; Thrombospondin type-1 domain-containing protein 2; Roof plate-specific spondin-3; Protein with TSP type-1 repeat TT7HJTF GN RSPO3 TT7HJTF FC Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors, which acts as a key regulator of angiogenesis. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Acts as a key regulator of angiogenesis by controlling vascular stability and pruning: acts by activating the non-canonical Wnt signaling pathway in endothelial cells. Can also amplify Wnt signaling pathway independently of LGR4-6 receptors, possibly by acting as a direct antagonistic ligand to RNF43 and ZNRF3. TT7HJTF SQ MHLRLISWLFIILNFMEYIGSQNASRGRRQRRMHPNVSQGCQGGCATCSDYNGCLSCKPRLFFALERIGMKQIGVCLSSCPSGYYGTRYPDINKCTKCKADCDTCFNKNFCTKCKSGFYLHLGKCLDNCPEGLEANNHTMECVSIVHCEVSEWNPWSPCTKKGKTCGFKRGTETRVREIIQHPSAKGNLCPPTNETRKCTVQRKKCQKGERGKKGRERKRKKPNKGESKEAIPDSKSLESSKEIPEQRENKQQQKKRKVQDKQKSVSVSTVH TT7HJTF TT Clinical trial TT7HJTF KE hsa04310:Wnt signaling pathway TTQ0V86 ID TTQ0V86 TTQ0V86 TN S100 calcium-binding protein B (S100B) TTQ0V86 UP P04271 TTQ0V86 UC S100B_HUMAN TTQ0V86 BC S100 calcium-binding protein TTQ0V86 SN S-100 protein subunit beta; S-100 protein beta chain; Protein S100-B TTQ0V86 GN S100B TTQ0V86 FC Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity. Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. TTQ0V86 PD 5D7F; 5CSN; 5CSJ; 5CSI; 5CSF TTQ0V86 SQ MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE TTQ0V86 TT Clinical trial TTVYIH7 ID TTVYIH7 TTVYIH7 TN Schistosoma Purine nucleoside phosphorylase (sch PNP) TTVYIH7 UP Q9BMI9 TTVYIH7 UC Q9BMI9_SCHMA TTVYIH7 SN sch Purine nucleoside phosphorylase; sch Inosine-guanosine phosphorylase TTVYIH7 GN sch PNP TTVYIH7 FC The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. TTVYIH7 EC EC 2.4.2.1 TTVYIH7 PD 3IEX; 3FNQ; 3FB1; 3FAZ; 3F8W TTVYIH7 SQ MHESVTANIENVKKVAHHIQKLTSIVPEIGIICGSGLGKLADGVKDKITIPYTKIPNFPQTSVVGHSGNLIFGTLSGRKVVVMQGRFHMYEGYSNDTVALPIRVMKLLGVKILMVSNAAGGLNRSLKLGDFVILKDHIYLPGLGLNNILVGPNQEAFGTRFPALSNAYDRDLRKLAVQVAEENGFGNLVHQGVYVMNGGPCYETPAECTMLLNMGCDVVGMSTIPEVVIARHCGIQVFAVSLVTNISVLDVESDLKPNHEEVLATGAQRAELMQSWFEKIIEKLPKD TTVYIH7 TT Clinical trial TT32NQ1 ID TT32NQ1 TT32NQ1 TN Short transient receptor potential channel 5 (TRPC5) TT32NQ1 UP Q9UL62 TT32NQ1 UC TRPC5_HUMAN TT32NQ1 BC Transient receptor potential catioin channel TT32NQ1 SN hTRP5; hTRP-5; TrpC5; Transient receptor protein 5; TRP-5 TT32NQ1 GN TRPC5 TT32NQ1 FC Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective. May also be activated by intracellular calcium store depletion. TT32NQ1 SQ MAQLYYKKVNYSPYRDRIPLQIVRAETELSAEEKAFLNAVEKGDYATVKQALQEAEIYYNVNINCMDPLGRSALLIAIENENLEIMELLLNHSVYVGDALLYAIRKEVVGAVELLLSYRRPSGEKQVPTLMMDTQFSEFTPDITPIMLAAHTNNYEIIKLLVQKRVTIPRPHQIRCNCVECVSSSEVDSLRHSRSRLNIYKALASPSLIALSSEDPILTAFRLGWELKELSKVENEFKAEYEELSQQCKLFAKDLLDQARSSRELEIILNHRDDHSEELDPQKYHDLAKLKVAIKYHQKEFVAQPNCQQLLATLWYDGFPGWRRKHWVVKLLTCMTIGFLFPMLSIAYLISPRSNLGLFIKKPFIKFICHTASYLTFLFMLLLASQHIVRTDLHVQGPPPTVVEWMILPWVLGFIWGEIKEMWDGGFTEYIHDWWNLMDFAMNSLYLATISLKIVAYVKYNGSRPREEWEMWHPTLIAEALFAISNILSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYETRAIDEPNNCKGIRCEKQNNAFSTLFETLQSLFWSVFGLLNLYVTNVKARHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFDEGGTLPPPFNIIPSPKSFLYLGNWFNNTFCPKRDPDGRRRRRNLRSFTERNADSLIQNQHYQEVIRNLVKRYVAAMIRNSKTHEGLTEENFKELKQDISSFRYEVLDLLGNRKHPRSFSTSSTELSQRDDNNDGSGGARAKSKSVSFNLGCKKKTCHGPPLIRTMPRSSGAQGKSKAESSSKRSFMGPSLKKLGLLFSKFNGHMSEPSSEPMYTISDGIVQQHCMWQDIRYSQMEKGKAEACSQSEINLSEVELGEVQGAAQSSECPLACSSSLHCASSICSSNSKLLDSSEDVFETWGEACDLLMHKWGDGQEEQVTTRL TT32NQ1 TT Clinical trial TT32NQ1 RC R-HSA-3295583:TRP channels; R-HSA-418890:Role of second messengers in netrin-1 signaling TTCF05Y ID TTCF05Y TTCF05Y TN Small-inducible cytokine A11 (CCL11) TTCF05Y UP P51671 TTCF05Y UC CCL11_HUMAN TTCF05Y BC Cytokine: CC chemokine TTCF05Y SN Smallinducible cytokine A11; SCYA11; Eotaxin; Eosinophil chemotactic protein; CC motif chemokine 11; C-C motif chemokine 11 TTCF05Y GN CCL11 TTCF05Y FC Binds to CCR3. In response to the presence of allergens, this protein directly promotes the accumulation of eosinophils, a prominent feature of allergic inflammatory reactions. TTCF05Y PD 2MPM; 2EOT; 1EOT TTCF05Y SQ MKVSAALLWLLLIAAAFSPQGLAGPASVPTTCCFNLANRKIPLQRLESYRRITSGKCPQKAVIFKTKLAKDICADPKKKWVQDSMKYLDQKSPTPKP TTCF05Y TT Clinical trial TTWZRY5 ID TTWZRY5 TTWZRY5 TN Sodium/bile acid cotransporter (SLC10A1) TTWZRY5 UP Q14973 TTWZRY5 UC NTCP_HUMAN TTWZRY5 BC Bile acid:sodium symporter (BASS) (TC 2.A.28) family TTWZRY5 SN Solute carrier family 10 member 1; Sodium/taurocholate cotransporting polypeptide; Na(+)/taurocholate transport protein; Na(+)/bile acid cotransporter; Cell growth-inhibiting gene 29 protein TTWZRY5 GN SLC10A1 TTWZRY5 FC The hepatic sodium/bile acid uptake system exhibits broad substrate specificity and transports various non-bile acid organic compounds as well. It is strictly dependent on the extracellular presence of sodium. TTWZRY5 SQ MEAHNASAPFNFTLPPNFGKRPTDLALSVILVFMLFFIMLSLGCTMEFSKIKAHLWKPKGLAIALVAQYGIMPLTAFVLGKVFRLKNIEALAILVCGCSPGGNLSNVFSLAMKGDMNLSIVMTTCSTFCALGMMPLLLYIYSRGIYDGDLKDKVPYKGIVISLVLVLIPCTIGIVLKSKRPQYMRYVIKGGMIIILLCSVAVTVLSAINVGKSIMFAMTPLLIATSSLMPFIGFLLGYVLSALFCLNGRCRRTVSMETGCQNVQLCSTILNVAFPPEVIGPLFFFPLLYMIFQLGEGLLLIAIFWCYEKFKTPKDKTKMIYTAATTEETIPGALGNGTYKGEDCSPCTA TTWZRY5 TT Successful TTWZRY5 KE hsa04976:Bile secretion; hsa05161:Hepatitis B TTW7HI9 ID TTW7HI9 TTW7HI9 TN Sodium/iodide cotransporter (SLC5A5) TTW7HI9 UP Q92911 TTW7HI9 UC SC5A5_HUMAN TTW7HI9 BC Solute:sodium symporter TTW7HI9 SN Solute carrier family 5 member 5; Sodium/iodide symporter; Sodium-iodide symporter; Na+/I-symporter; Na(+)/I(-) symporter; Na(+)/I(-) cotransporter; NIS TTW7HI9 GN SLC5A5 TTW7HI9 FC Mediates iodide uptake in the thyroid gland. TTW7HI9 SQ MEAVETGERPTFGAWDYGVFALMLLVSTGIGLWVGLARGGQRSAEDFFTGGRRLAALPVGLSLSASFMSAVQVLGVPSEAYRYGLKFLWMCLGQLLNSVLTALLFMPVFYRLGLTSTYEYLEMRFSRAVRLCGTLQYIVATMLYTGIVIYAPALILNQVTGLDIWASLLSTGIICTFYTAVGGMKAVVWTDVFQVVVMLSGFWVVLARGVMLVGGPRQVLTLAQNHSRINLMDFNPDPRSRYTFWTFVVGGTLVWLSMYGVNQAQVQRYVACRTEKQAKLALLINQVGLFLIVSSAACCGIVMFVFYTDCDPLLLGRISAPDQYMPLLVLDIFEDLPGVPGLFLACAYSGTLSTASTSINAMAAVTVEDLIKPRLRSLAPRKLVIISKGLSLIYGSACLTVAALSSLLGGGVLQGSFTVMGVISGPLLGAFILGMFLPACNTPGVLAGLGAGLALSLWVALGATLYPPSEQTMRVLPSSAARCVALSVNASGLLDPALLPANDSSRAPSSGMDASRPALADSFYAISYLYYGALGTLTTVLCGALISCLTGPTKRSTLAPGLLWWDLARQTASVAPKEEVAILDDNLVKGPEELPTGNKKPPGFLPTNEDRLFFLGQKELEGAGSWTPCVGHDGGRDQQETNL TTW7HI9 TT Clinical trial TTW7HI9 FM Solute:sodium symporter TTZN1CF ID TTZN1CF TTZN1CF TN Solute carrier family 39 member 6 (SLC39A6) TTZN1CF UP Q13433 TTZN1CF UC S39A6_HUMAN TTZN1CF SN Zrt- and Irt-like protein 6; ZIP-6; SLC39A6; Estrogen-regulated protein LIV-1 TTZN1CF GN SLC39A6 TTZN1CF FC May act as a zinc-influx transporter. TTZN1CF SQ MARKLSVILILTFALSVTNPLHELKAAAFPQTTEKISPNWESGINVDLAISTRQYHLQQLFYRYGENNSLSVEGFRKLLQNIGIDKIKRIHIHHDHDHHSDHEHHSDHERHSDHEHHSEHEHHSDHDHHSHHNHAASGKNKRKALCPDHDSDSSGKDPRNSQGKGAHRPEHASGRRNVKDSVSASEVTSTVYNTVSEGTHFLETIETPRPGKLFPKDVSSSTPPSVTSKSRVSRLAGRKTNESVSEPRKGFMYSRNTNENPQECFNASKLLTSHGMGIQVPLNATEFNYLCPAIINQIDARSCLIHTSEKKAEIPPKTYSLQIAWVGGFIAISIISFLSLLGVILVPLMNRVFFKFLLSFLVALAVGTLSGDAFLHLLPHSHASHHHSHSHEEPAMEMKRGPLFSHLSSQNIEESAYFDSTWKGLTALGGLYFMFLVEHVLTLIKQFKDKKKKNQKKPENDDDVEIKKQLSKYESQLSTNEEKVDTDDRTEGYLRADSQEPSHFDSQQPAVLEEEEVMIAHAHPQEVYNEYVPRGCKNKCHSHFHDTLGQSDDLIHHHHDYHHILHHHHHQNHHPHSHSQRYSREELKDAGVATLAWMVIMGDGLHNFSDGLAIGAAFTEGLSSGLSTSVAVFCHELPHELGDFAVLLKAGMTVKQAVLYNALSAMLAYLGMATGIFIGHYAENVSMWIFALTAGLFMYVALVDMVPEMLHNDASDHGCSRWGYFFLQNAGMLLGFGIMLLISIFEHKIVFRINF TTZN1CF TT Clinical trial TTS9BDA ID TTS9BDA TTS9BDA TN Spectrin non-erythroid beta chain 1 (SPTBN1) TTS9BDA UP Q01082 TTS9BDA UC SPTB2_HUMAN TTS9BDA SN Spectrin, non-erythroid beta chain 1; Spectrin beta chain, non-erythrocytic 1; SPTB2; Fodrin beta chain; Beta-II spectrin TTS9BDA GN SPTBN1 TTS9BDA FC Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. TTS9BDA PD 3EDV; 1BKR; 1AA2 TTS9BDA SQ MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDISVDHPDEKSIITYVVTYYHYFSKMKALAVEGKRIGKVLDNAIETEKMIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAFNTYRTVEKPPKFTEKGNLEVLLFTIQSKMRANNQKVYMPREGKLISDINKAWERLEKAEHERELALRNELIRQEKLEQLARRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAENYHDIKRITARKDNVIRLWEYLLELLRARRQRLEMNLGLQKIFQEMLYIMDWMDEMKVLVLSQDYGKHLLGVEDLLQKHTLVEADIGIQAERVRGVNASAQKFATDGEGYKPCDPQVIRDRVAHMEFCYQELCQLAAERRARLEESRRLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERIIYIREQWANLEQLSAIRKKRLEEASLLHQFQADADDIDAWMLDILKIVSSSDVGHDEYSTQSLVKKHKDVAEEIANYRPTLDTLHEQASALPQEHAESPDVRGRLSGIEERYKEVAELTRLRKQALQDTLALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHSGHPSEKEIKAQQDKLNTRWSQFRELVDRKKDALLSALSIQNYHLECNETKSWIREKTKVIESTQDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGEASKLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMVTQGQTDAQYMFLRQRLQALDTGWNELHKMWENRQNLLSQSHAYQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKVDSIDDRHRKNRETASELLMRLKDNRDLQKFLQDCQELSLWINEKMLTAQDMSYDEARNLHSKWLKHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDEVDSKRLTVQTKFMELLEPLNERKHNLLASKEIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIVTDSSSLSAEAIRQRLADLKQLWGLLIEETEKRHRRLEEAHRAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNHLADELINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQILAASYELHKFYHDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACESRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTTCIELGKSLLARKHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLELLEVRRQQEEEERKRRPPSPEPSTKVSEEAESQQQWDTSKGEQVSQNGLPAEQGSPRMAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKTALPAQSAATLPARTQETPSAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKTAASGIPYHSEVPVSLKEAVCEVALDYKKKKHVFKLRLNDGNEYLFQAKDDEEMNTWIQAISSAISSDKHEVSASTQSTPASSRAQTLPTSVVTITSESSPGKREKDKEKDKEKRFSLFGKKK TTS9BDA TT Clinical trial TTS9BDA FM Spectrin TTS9BDA RC R-HSA-373753:Nephrin interactions; R-HSA-375165:NCAM signaling for neurite out-growth; R-HSA-445095:Interaction between L1 and Ankyrins; R-HSA-5673001:RAF/MAP kinase cascade TT7W5OT ID TT7W5OT TT7W5OT TN STMN1 messenger RNA (STMN1 mRNA) TT7W5OT UP P16949 TT7W5OT UC STMN1_HUMAN TT7W5OT BC mRNA target TT7W5OT SN pp19 (mRNA); pp17 (mRNA); Stathmin (mRNA); Protein Pr22 (mRNA); Prosolin (mRNA); Phosphoprotein p19 (mRNA); Op18 (mRNA); Oncoprotein 18 (mRNA); Metablastin (mRNA); Leukemia-associated phosphoprotein p18 (mRNA); LAP18 (mRNA); C1orf215 (mRNA) TT7W5OT GN STMN1 TT7W5OT FC Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate fear. Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. TT7W5OT SQ MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHIEEVRKNKESKDPADETEAD TT7W5OT TT Clinical trial TT7W5OT FM mRNA target TT7W5OT KE hsa04010:MAPK signaling pathway; hsa05206:MicroRNAs in cancer TT2VCLI ID TT2VCLI TT2VCLI TN Streptococcus Streptokinase (Stre-coc skc) TT2VCLI UP P00779 TT2VCLI UC STRP_STREQ TT2VCLI BC Staphylokinase streptokinase TT2VCLI SN skc; Streptokinase C TT2VCLI GN Stre-coc skc TT2VCLI FC This protein is not a protease, but it activates plasminogen by complexing with it. As a potential virulence factor, it is thought to prevent the formation of effective fibrin barriers around the site of infection, thereby contributing to the invasiveness of the cells. TT2VCLI PD 1QQR; 1L4Z; 1L4D; 1BML TT2VCLI SQ MKNYLSFGMFALLFALTFGTVNSVQAIAGPEWLLDRPSVNNSQLVVSVAGTVEGTNQDISLKFFEIDLTSRPAHGGKTEQGLSPKSKPFATDSGAMSHKLEKADLLKAIQEQLIANVHSNDDYFEVIDFASDATITDRNGKVYFADKDGSVTLPTQPVQEFLLSGHVRVRPYKEKPIQNQAKSVDVEYTVQFTPLNPDDDFRPGLKDTKLLKTLAIGDTITSQELLAQAQSILNKNHPGYTIYERDSSIVTHDNDIFRTILPMDQEFTYRVKNREQAYRINKKSGLNEEINNTDLISEKYYVLKKGEKPYDPFDRSHLKLFTIKYVDVDTNELLKSEQLLTASERNLDFRDLYDPRDKAKLLYNNLDAFGIMDYTLTGKVEDNHDDTNRIITVYMGKRPEGENASYHLAYDKDRYTEEEREVYSYLRYTGTPIPDNPNDK TT2VCLI TT Clinical trial TT8QL6X ID TT8QL6X TT8QL6X TN Survival motor neuron protein (SMN1) TT8QL6X UP Q16637 TT8QL6X UC SMN_HUMAN TT8QL6X SN SMNT; SMNC; SMN2; SMN; Gemin-1; Component of gems 1 TT8QL6X GN SMN1 TT8QL6X FC Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. TT8QL6X PD 5XJU; 5XJT; 5XJS; 5XJR; 5XJQ TT8QL6X SQ MAMSSGGSGGGVPEQEDSVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDICETSGKPKTTPKRKPAKKNKSQKKNTAASLQQWKVGDKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDLLSPICEVANNIEQNAQENENESQVSTDESENSRSPGNKSDNIKPKSAPWNSFLPPPPPMPGPRLGPGKPGLKFNGPPPPPPPPPPHLLSCWLPPFPSGPPIIPPPPPICPDSLDDADALGSMLISWYMSGYHTGYYMGFRQNQKEGRCSHSLN TT8QL6X TT Successful TT8QL6X FM Survival motor neuron protein TT8QL6X KE hsa03013:RNA transport TTBXAHS ID TTBXAHS TTBXAHS TN T-box transcription factor T (TBXT) TTBXAHS UP O15178 TTBXAHS UC TBXT_HUMAN TTBXAHS SN T; Protein T TTBXAHS GN T TTBXAHS FC Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Binds to a palindromic site (called T site) and activates gene transcription when bound to such a site. TTBXAHS PD 6F59; 6F58 TTBXAHS SQ MSSPGTESAGKSLQYRVDHLLSAVENELQAGSEKGDPTERELRVGLEESELWLRFKELTNEMIVTKNGRRMFPVLKVNVSGLDPNAMYSFLLDFVAADNHRWKYVNGEWVPGGKPEPQAPSCVYIHPDSPNFGAHWMKAPVSFSKVKLTNKLNGGGQIMLNSLHKYEPRIHIVRVGGPQRMITSHCFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERSDHKEMMEEPGDSQQPGYSQWGWLLPGTSTLCPPANPHPQFGGALSLPSTHSCDRYPTLRSHRSSPYPSPYAHRNNSPTYSDNSPACLSMLQSHDNWSSLGMPAHPSMLPVSHNASPPTSSSQYPSLWSVSNGAVTPGSQAAAVSNGLGAQFFRGSPAHYTPLTHPVSAPSSSGSPLYEGAAAATDIVDSQYDAAAQGRLIASWTPVSPPSM TTBXAHS TT Clinical trial TTMF6KC ID TTMF6KC TTMF6KC TN T-cell differentiation antigen CD6 (TP120) TTMF6KC UP P30203 TTMF6KC UC CD6_HUMAN TTMF6KC SN T12 TTMF6KC GN CD6 TTMF6KC FC Contributes to signaling cascades triggered by activation of the TCR/CD3 complex. Functions as costimulatory molecule; promotes T-cell activation and proliferation. Contributes to the formation and maturation of the immunological synapse. Functions as calcium-dependent pattern receptor that binds and aggregates both Gram-positive and Gram-negative bacteria. Binds both lipopolysaccharide (LPS) from Gram-negative bacteria and lipoteichoic acid from Gram-positive bacteria. LPS binding leads to the activation of signaling cascades and down-stream MAP kinases. Mediates activation of the inflammatory response and the secretion of pro-inflammatory cytokines in response to LPS. Cell adhesion molecule that mediates cell-cell contacts and regulates T-cell responses via its interaction with ALCAM/CD166. TTMF6KC PD 5A2E TTMF6KC SQ MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGGAEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHGEWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGGADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLCSASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYALPVMVNHQHLPTTIPAGSNSYQPVPITIPKEVFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQNFQPPPQPPSEEQFGCPGSPSPQPDSTDNDDYDDISAA TTMF6KC TT Clinical trial TTMF6KC KE hsa04514:Cell adhesion molecules (CAMs) TTJDUNO ID TTJDUNO TTJDUNO TN T-cell surface antigen CD2 (CD2) TTJDUNO UP P06729 TTJDUNO UC CD2_HUMAN TTJDUNO SN T-cell surface antigen T11/Leu-5; SRBC; Rosette receptor; LFA-3 receptor; LFA-2; Erythrocyte receptor TTJDUNO GN CD2 TTJDUNO FC CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function. CD2 interacts with lymphocyte function-associated antigen CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. TTJDUNO PD 2J7I; 2J6O; 1QA9; 1L2Z; 1HNF TTJDUNO SQ MSFPCKFVASFLLIFNVSSKGAVSKEITNALETWGALGQDINLDIPSFQMSDDIDDIKWEKTSDKKKIAQFRKEKETFKEKDTYKLFKNGTLKIKHLKTDDQDIYKVSIYDTKGKNVLEKIFDLKIQERVSKPKISWTCINTTLTCEVMNGTDPELNLYQDGKHLKLSQRVITHKWTTSLSAKFKCTAGNKVSKESSVEPVSCPEKGLDIYLIIGICGGGSLLMVFVALLVFYITKRKKQRSRRNDEELETRAHRVATEERGRKPHQIPASTPQNPATSQHPPPPPGHRSQAPSHRPPPPGHRVQHQPQKRPPAPSGTQVHQQKGPPLPRPRVQPKPPHGAAENSLSPSSN TTJDUNO TT Clinical trial TTJDUNO FM Transmembrane protein TTJDUNO KE hsa04514:Cell adhesion molecules (CAMs); hsa04640:Hematopoietic cell lineage TTJDUNO RC R-HSA-202733:Cell surface interactions at the vascular wall TTV3XPL ID TTV3XPL TTV3XPL TN T-cell surface glycoprotein CD3 gamma (CD3G) TTV3XPL UP P09693 TTV3XPL UC CD3G_HUMAN TTV3XPL SN T3G; T-cell surface glycoprotein CD3 gamma chain; T-cell receptor T3 gamma chain; CD3g TTV3XPL GN CD3G TTV3XPL FC When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition to this role of signal transduction in T-cell activation, CD3G plays an essential role in the dynamic regulation of TCR expression at the cell surface. Indeed, constitutive TCR cycling is dependent on the di-leucine-based (diL) receptor-sorting motif present in CD3G. Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. TTV3XPL PD 1SY6 TTV3XPL SQ MEQGKGLAVLILAIILLQGTLAQSIKGNHLVKVYDYQEDGSVLLTCDAEAKNITWFKDGKMIGFLTEDKKKWNLGSNAKDPRGMYQCKGSQNKSKPLQVYYRMCQNCIELNAATISGFLFAEIVSIFVLAVGVYFIAGQDGVRQSRASDKQTLLPNDQLYQPLKDREDDQYSHLQGNQLRRN TTV3XPL TT Clinical trial TTV3XPL KE hsa04640:Hematopoietic cell lineage; hsa04660:T cell receptor signaling pathway; hsa05142:Chagas disease (American trypanosomiasis); hsa05162:Measles; hsa05166:HTLV-I infection TTV3XPL RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202427:Phosphorylation of CD3 and TCR zeta chains; R-HSA-202430:Translocation of ZAP-70 to Immunological synapse; R-HSA-202433:Generation of second messenger molecules; R-HSA-2029481:FCGR activation; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-389948:PD-1 signaling TTN7HMG ID TTN7HMG TTN7HMG TN Teratocarcinoma-derived growth factor 1 (TDGF1) TTN7HMG UP P13385 TTN7HMG UC TDGF1_HUMAN TTN7HMG BC Growth factor TTN7HMG SN TDGF1; Epidermal growth factor-like cripto protein CR1; Cripto-1 growth factor; Cripto; CRGF TTN7HMG GN TDGF1 TTN7HMG FC Could play a role in the determination of the epiblastic cells that subsequently give rise to the mesoderm. TTN7HMG SQ MDCRKMARFSYSVIWIMAISKVFELGLVAGLGHQEFARPSRGYLAFRDDSIWPQEEPAIRPRSSQRVPPMGIQHSKELNRTCCLNGGTCMLGSFCACPPSFYGRNCEHDVRKENCGSVPHDTWLPKKCSLCKCWHGQLRCFPQAFLPGCDGLVMDEHLVASRTPELPPSARTTTFMLVGICLSIQSYY TTN7HMG TT Clinical trial TTN7HMG RC R-HSA-1433617:Regulation of signaling by NODAL; R-HSA-2892247:POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation TTKI0H1 ID TTKI0H1 TTKI0H1 TN Thrombospondin-1 (THBS1) TTKI0H1 UP P07996 TTKI0H1 UC TSP1_HUMAN TTKI0H1 SN TSP1; TSP; Glycoprotein G TTKI0H1 GN THBS1 TTKI0H1 FC Binds heparin. May play a role in dentinogenesis and/or maintenance of dentin and dental pulp. Ligand for CD36 mediating antiangiogenic properties. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors. Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. TTKI0H1 PD 5FOE; 3R6B; 2OUJ; 2OUH; 2ES3 TTKI0H1 SQ MGLAWGLGVLFLMHVCGTNRIPESGGDNSVFDIFELTGAARKGSGRRLVKGPDPSSPAFRIEDANLIPPVPDDKFQDLVDAVRAEKGFLLLASLRQMKKTRGTLLALERKDHSGQVFSVVSNGKAGTLDLSLTVQGKQHVVSVEEALLATGQWKSITLFVQEDRAQLYIDCEKMENAELDVPIQSVFTRDLASIARLRIAKGGVNDNFQGVLQNVRFVFGTTPEDILRNKGCSSSTSVLLTLDNNVVNGSSPAIRTNYIGHKTKDLQAICGISCDELSSMVLELRGLRTIVTTLQDSIRKVTEENKELANELRRPPLCYHNGVQYRNNEEWTVDSCTECHCQNSVTICKKVSCPIMPCSNATVPDGECCPRCWPSDSADDGWSPWSEWTSCSTSCGNGIQQRGRSCDSLNNRCEGSSVQTRTCHIQECDKRFKQDGGWSHWSPWSSCSVTCGDGVITRIRLCNSPSPQMNGKPCEGEARETKACKKDACPINGGWGPWSPWDICSVTCGGGVQKRSRLCNNPTPQFGGKDCVGDVTENQICNKQDCPIDGCLSNPCFAGVKCTSYPDGSWKCGACPPGYSGNGIQCTDVDECKEVPDACFNHNGEHRCENTDPGYNCLPCPPRFTGSQPFGQGVEHATANKQVCKPRNPCTDGTHDCNKNAKCNYLGHYSDPMYRCECKPGYAGNGIICGEDTDLDGWPNENLVCVANATYHCKKDNCPNLPNSGQEDYDKDGIGDACDDDDDNDKIPDDRDNCPFHYNPAQYDYDRDDVGDRCDNCPYNHNPDQADTDNNGEGDACAADIDGDGILNERDNCQYVYNVDQRDTDMDGVGDQCDNCPLEHNPDQLDSDSDRIGDTCDNNQDIDEDGHQNNLDNCPYVPNANQADHDKDGKGDACDHDDDNDGIPDDKDNCRLVPNPDQKDSDGDGRGDACKDDFDHDSVPDIDDICPENVDISETDFRRFQMIPLDPKGTSQNDPNWVVRHQGKELVQTVNCDPGLAVGYDEFNAVDFSGTFFINTERDDDYAGFVFGYQSSSRFYVVMWKQVTQSYWDTNPTRAQGYSGLSVKVVNSTTGPGEHLRNALWHTGNTPGQVRTLWHDPRHIGWKDFTAYRWRLSHRPKTGFIRVVMYEGKKIMADSGPIYDKTYAGGRLGLFVFSQEMVFFSDLKYECRDP TTKI0H1 TT Clinical trial TTKI0H1 FM Thrombospondin TTKI0H1 KE hsa04015:Rap1 signaling pathway; hsa04115:p53 signaling pathway; hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04350:TGF-beta signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa05144:Malaria; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05219:Bladder cancer TTKI0H1 RC R-HSA-114608:Platelet degranulation; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000170:Syndecan interactions; R-HSA-5173214:O-glycosylation of TSR domain-containing proteins TTBTDM1 ID TTBTDM1 TTBTDM1 TN TNF-related weak inducer of apoptosis (TWEAK) TTBTDM1 UP O43508 TTBTDM1 UC TNF12_HUMAN TTBTDM1 BC Cytokine: tumor necrosis factor TTBTDM1 SN Tumor necrosis factor ligand superfamily member 12; TWEAK; DR3LG; APO3L; APO3 ligand TTBTDM1 GN TNFSF12 TTBTDM1 FC Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion. TTBTDM1 PD 4HT1 TTBTDM1 SQ MAARRSQRRRGRRGEPGTALLVPLALGLGLALACLGLLLAVVSLGSRASLSAQEPAQEELVAEEDQDPSELNPQTEESQDPAPFLNRLVRPRRSAPKGRKTRARRAIAAHYEVHPRPGQDGAQAGVDGTVSGWEEARINSSSPLRYNRQIGEFIVTRAGLYYLYCQVHFDEGKAVYLKLDLLVDGVLALRCLEEFSATAASSLGPQLRLCQVSGLLALRPGSSLRIRTLPWAHLKAAPFLTYFGLFQVH TTBTDM1 TT Clinical trial TTNOJIZ ID TTNOJIZ TTNOJIZ TN Trefoil factor-1 (TFF1) TTNOJIZ UP P04155 TTNOJIZ UC TFF1_HUMAN TTNOJIZ SN hP1.A; Trefoil factor 1; Protein pS2; Polypeptide P1.A; PS2; PNR-2; Breast cancer estrogen-inducible protein; BCEI TTNOJIZ GN TFF1 TTNOJIZ FC May inhibit the growth of calcium oxalate crystals in urine. Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TTNOJIZ PD 1PS2; 1HI7 TTNOJIZ SQ MATMENKVICALVLVSMLALGTLAEAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFYPNTIDVPPEEECEF TTNOJIZ TT Clinical trial TT63KYR ID TT63KYR TT63KYR TN Tubulin beta-1 chain (TUBB1) TT63KYR UP Q9H4B7 TT63KYR UC TBB1_HUMAN TT63KYR BC Tubulin family TT63KYR SN TUBB1 TT63KYR GN TUBB1 TT63KYR FC Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TT63KYR SQ MREIVHIQIGQCGNQIGAKFWEMIGEEHGIDLAGSDRGASALQLERISVYYNEAYGRKYVPRAVLVDLEPGTMDSIRSSKLGALFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVLEVVRHESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRIMNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENADACFCIDNEALYDICFRTLKLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNTMAACDLRRGRYLTVACIFRGKMSTKEVDQQLLSVQTRNSSCFVEWIPNNVKVAVCDIPPRGLSMAATFIGNNTAIQEIFNRVSEHFSAMFKRKAFVHWYTSEGMDINEFGEAENNIHDLVSEYQQFQDAKAVLEEDEEVTEEAEMEPEDKGH TT63KYR TT Clinical trial TT63KYR KE hsa04145:Phagosome; hsa04540:Gap junction; hsa05130:Pathogenic Escherichia coli infection TT63KYR RC R-HSA-1445148:Translocation of GLUT4 to the plasma membrane; R-HSA-190840:Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane; R-HSA-190861:Gap junction assembly; R-HSA-2132295:MHC class II antigen presentation; R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-380320:Recruitment of NuMA to mitotic centrosomes; R-HSA-389977:Post-chaperonin tubulin folding pathway; R-HSA-437239:Recycling pathway of L1; R-HSA-5610787:Hedgehog 'off' state; R-HSA-5617833:Assembly of the primary cilium; R-HSA-5626467:RHO GTPases activate IQGAPs; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-68877:Mitotic Prometaphase; R-HSA-983189:Kinesins TTJ8O14 ID TTJ8O14 TTJ8O14 TN Tumor suppressor candidate 2 (TUSC2) TTJ8O14 UP O75896 TTJ8O14 UC TUSC2_HUMAN TTJ8O14 SN PDGFA-associated protein 2; PDAP2; LGCC; Fusion 1 protein; Fus-1 protein; FUS1; C3orf11 TTJ8O14 GN TUSC2 TTJ8O14 FC May function as a tumor suppressor, inhibiting colony formation, causing G1 arrest and ultimately inducing apoptosis in homozygous 3p21. 3 120-kb region-deficient cells. TTJ8O14 SQ MGASGSKARGLWPFASAAGGGGSEAAGAEQALVRPRGRAVPPFVFTRRGSMFYDEDGDLAHEFYEETIVTKNGQKRAKLRRVHKNLIPQGIVKLDHPRIHVDFPVILYEV TTJ8O14 TT Clinical trial TTZ8WH4 ID TTZ8WH4 TTZ8WH4 TN Tumor-associated calcium signal transducer 1 (EPCAM) TTZ8WH4 UP P16422 TTZ8WH4 UC EPCAM_HUMAN TTZ8WH4 SN hEGP314; TROP1; TACSTD1; Major gastrointestinal tumor-associated protein GA733-2; MIC18; M4S1; M1S2; KSA; KS 1/4 antigen; Gastrointestinal carcinoma antigen GA733; GA733-2; Epithelial glycoprotein 314; Epithelial glycoprotein; Epithelial cell surface antigen; Epithelial cell adhesion molecule; Ep-CAM; EGP314; EGP; Cell surface glycoprotein Trop-1; CD326; Adenocarcinoma-associated antigen TTZ8WH4 GN EPCAM TTZ8WH4 FC Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E. May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. TTZ8WH4 PD 6I07; 4MZV TTZ8WH4 SQ MAPPQVLAFGLLLAAATATFAAAQEECVCENYKLAVNCFVNNNRQCQCTSVGAQNTVICSKLAAKCLVMKAEMNGSKLGRRAKPEGALQNNDGLYDPDCDESGLFKAKQCNGTSMCWCVNTAGVRRTDKDTEITCSERVRTYWIIIELKHKAREKPYDSKSLRTALQKEITTRYQLDPKFITSILYENNVITIDLVQNSSQKTQNDVDIADVAYYFEKDVKGESLFHSKKMDLTVNGEQLDLDPGQTLIYYVDEKAPEFSMQGLKAGVIAVIVVVVIAVVAGIVVLVISRKKRMAKYEKAEIKEMGEMHRELNA TTZ8WH4 TT Clinical trial TTBZOTY ID TTBZOTY TTBZOTY TN Tyrosine-protein kinase MELK (MELK) TTBZOTY UP Q14680 TTBZOTY UC MELK_HUMAN TTBZOTY SN pEg3 kinase; hPK38; hMELK; MELK TTBZOTY GN MELK TTBZOTY FC Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 andZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis. {ECO:0000269|PubMed:11802789, ECO:0000269|PubMed:12400006, ECO:0000269|PubMed:14699119, ECO:0000269|PubMed:15908796, ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:17280616}. TTBZOTY EC EC 2.7.11.1 TTBZOTY PD 5TX3; 5TWZ; 5TWY; 5TWU; 5TWL TTBZOTY SQ MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV TTBZOTY TT Clinical trial TTNDC4K ID TTNDC4K TTNDC4K TN Ubiquitin-like protein Nedd8 (NEDD8) TTNDC4K UP Q15843 TTNDC4K UC NEDD8_HUMAN TTNDC4K BC Ubiquitin family TTNDC4K SN Neural precursor cell expressed developmentally down-regulated protein 8; Neddylin; NEDD-8 TTNDC4K GN NEDD8 TTNDC4K FC Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M. Attachment of NEDD8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins. TTNDC4K PD 4P5O; 4HCP; 4FBJ; 4F8C; 3GZN TTNDC4K SQ MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGGGGLRQ TTNDC4K TT Clinical trial TT54ERL ID TT54ERL TT54ERL TN Voltage-gated sodium channel alpha Nav1.6 (SCN8A) TT54ERL UP Q9UQD0 TT54ERL UC SCN8A_HUMAN TT54ERL BC Voltage-gated ion channel TT54ERL SN Voltage-gated sodium channel subunit alpha Nav1.6; Sodium channel protein type VIII subunit alpha; Sodium channel protein type 8 subunit alpha; SCN8A TT54ERL GN SCN8A TT54ERL FC Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. In macrophages and melanoma cells, isoform 5 may participate in the control of podosome and invadopodia formation. TT54ERL SQ MAARLLAPPGPDSFKPFTPESLANIERRIAESKLKKPPKADGSHREDDEDSKPKPNSDLEAGKSLPFIYGDIPQGLVAVPLEDFDPYYLTQKTFVVLNRGKTLFRFSATPALYILSPFNLIRRIAIKILIHSVFSMIIMCTILTNCVFMTFSNPPDWSKNVEYTFTGIYTFESLVKIIARGFCIDGFTFLRDPWNWLDFSVIMMAYITEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVVWPINFNESYLENGTKGFDWEEYINNKTNFYTVPGMLEPLLCGNSSDAGQCPEGYQCMKAGRNPNYGYTSFDTFSWAFLALFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFVGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFKAMLEQLKKQQEEAQAAAMATSAGTVSEDAIEEEGEEGGGSPRSSSEISKLSSKSAKERRNRRKKRKQKELSEGEEKGDPEKVFKSESEDGMRRKAFRLPDNRIGRKFSIMNQSLLSIPGSPFLSRHNSKSSIFSFRGPGRFRDPGSENEFADDEHSTVEESEGRRDSLFIPIRARERRSSYSGYSGYSQGSRSSRIFPSLRRSVKRNSTVDCNGVVSLIGGPGSHIGGRLLPEATTEVEIKKKGPGSLLVSMDQLASYGRKDRINSIMSVVTNTLVEELEESQRKCPPCWYKFANTFLIWECHPYWIKLKEIVNLIVMDPFVDLAITICIVLNTLFMAMEHHPMTPQFEHVLAVGNLVFTGIFTAEMFLKLIAMDPYYYFQEGWNIFDGFIVSLSLMELSLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINQDCELPRWHMHDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDGEMNNLQISVIRIKKGVAWTKLKVHAFMQAHFKQREADEVKPLDELYEKKANCIANHTGADIHRNGDFQKNGNGTTSGIGSSVEKYIIDEDHMSFINNPNLTVRVPIAVGESDFENLNTEDVSSESDPEGSKDKLDDTSSSEGSTIDIKPEVEEVPVEQPEEYLDPDACFTEGCVQRFKCCQVNIEEGLGKSWWILRKTCFLIVEHNWFETFIIFMILLSSGALAFEDIYIEQRKTIRTILEYADKVFTYIFILEMLLKWTAYGFVKFFTNAWCWLDFLIVAVSLVSLIANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKYHYCFNETSEIRFEIEDVNNKTECEKLMEGNNTEIRWKNVKINFDNVGAGYLALLQVATFKGWMDIMYAAVDSRKPDEQPKYEDNIYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKIQGIVFDFVTQQAFDIVIMMLICLNMVTMMVETDTQSKQMENILYWINLVFVIFFTCECVLKMFALRHYYFTIGWNIFDFVVVILSIVGMFLADIIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIFSIFGMSNFAYVKHEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLLPILNRPPDCSLDKEHPGSGFKGDCGNPSVGIFFFVSYIIISFLIVVNMYIAIILENFSVATEESADPLSEDDFETFYEIWEKFDPDATQFIEYCKLADFADALEHPLRVPKPNTIELIAMDLPMVSGDRIHCLDILFAFTKRVLGDSGELDILRQQMEERFVASNPSKVSYEPITTTLRRKQEEVSAVVLQRAYRGHLARRGFICKKTTSNKLENGGTHREKKESTPSTASLPSYDSVTKPEKEKQQRAEEGRRERAKRQKEVRESKC TT54ERL TT Clinical trial TT54ERL RC R-HSA-445095:Interaction between L1 and Ankyrins TTWNL74 ID TTWNL74 TTWNL74 TN V-set and immunoglobulin domain-containing protein 9 (TIGIT) TTWNL74 UP Q495A1 TTWNL74 UC TIGIT_HUMAN TTWNL74 SN VSTM3; VSIG9; V-set and transmembrane domain-containing protein 3; T-cell immunoreceptor with Ig and ITIM domains TTWNL74 GN TIGIT TTWNL74 FC Binds with high affinity to the poliovirus receptor (PVR) which causes increased secretion of IL10 and decreased secretion of IL12B and suppresses T-cell activation by promoting the generation of mature immunoregulatory dendritic cells. TTWNL74 PD 5V52; 3UDW; 3UCR; 3RQ3; 3Q0H TTWNL74 SQ MRWCLLLIWAQGLRQAPLASGMMTGTIETTGNISAEKGGSIILQCHLSSTTAQVTQVNWEQQDQLLAICNADLGWHISPSFKDRVAPGPGLGLTLQSLTVNDTGEYFCIYHTYPDGTYTGRIFLEVLESSVAEHGARFQIPLLGAMAATLVVICTAVIVVVALTRKKKALRIHSVEGDLRRKSAGQEEWSPSAPSPPGSCVQAEAAPAGLCGEQRGEDCAELHDYFNVLSYRSLGNCSFFTETG TTWNL74 TT Clinical trial TTWNL74 KE hsa04514:Cell adhesion molecules (CAMs) TTE8T73 ID TTE8T73 TTE8T73 TN Wiskott-Aldrich syndrome protein (WAS) TTE8T73 UP P42768 TTE8T73 UC WASP_HUMAN TTE8T73 SN WASp; IMD2 TTE8T73 GN WAS TTE8T73 FC Important for efficient actin polymerization. Possible regulator of lymphocyte and platelet function. Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria. In addition to its role in the cytoplasmic cytoskeleton, also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. Promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). Effector protein for Rho-type GTPases that regulates actin filament reorganization via its interaction with the Arp2/3 complex. TTE8T73 PD 2OT0; 2K42; 2A3Z; 1T84; 1EJ5 TTE8T73 SQ MSGGPMGGRPGGRGAPAVQQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQAGLNFADEDEAQAFRALVQEKIQKRNQRQSGDRRQLPPPPTPANEERRGGLPPLPLHPGGDQGGPPVGPLSLGLATVDIQNPDITSSRYRGLPAPGPSPADKKRSGKKKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQGGLEAVRQEMRRQEPLPPPPPPSRGGNQLPRPPIVGGNKGRSGPLPPVPLGIAPPPPTPRGPPPPGRGGPPPPPPPATGRSGPLPPPPPGAGGPPMPPPPPPPPPPPSSGNGPAPPPLPPALVPAGGLAPGGGRGALLDQIRQGIQLNKTPGAPESSALQPPPQSSEGLVGALMHVMQKRSRAIHSSDEGEDQAGDEDEDDEWDD TTE8T73 TT Clinical trial TTE8T73 KE hsa04062:Chemokine signaling pathway; hsa04520:Adherens junction; hsa04666:Fc gamma R-mediated phagocytosis; hsa04810:Regulation of actin cytoskeleton; hsa05100:Bacterial invasion of epithelial cells; hsa05130:Pathogenic Escherichia coli infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05231:Choline metabolism in cancer TTE8T73 RC R-HSA-202433:Generation of second messenger molecules; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-5663213:RHO GTPases Activate WASPs and WAVEs TTHCF4J ID TTHCF4J TTHCF4J TN Alpha-glucosidase (GLA) TTHCF4J UP P10253; Q14697; Q8TET4 TTHCF4J UC LYAG_HUMAN; GANAB_HUMAN; GANC_HUMAN TTHCF4J SN Maltase-glucoamylase; Maltase; Glucosidosucrase; Glucosidoinvertase; Glucoinvertase; Alpha-glucoside hydrolase; Alpha-glucopyranosidase; Alpha-D-glucoside glucohydrolase; Alpha-D-glucosidase; Alpha-1;4-glucosidase TTHCF4J GN GAA; GANAB; GANC TTHCF4J FC Breaks down starch and disaccharides to glucose. TTHCF4J SQ MGVRHPPCSHRLLAVCALVSLATAALLGHILLHDFLLVPRELSGSSPVLEETHPAHQQGASRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLFFADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPVEALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQPMALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQLQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC TTHCF4J TT Clinical trial TTT2KE3 ID TTT2KE3 TTT2KE3 TN Alpha-mannosidase (MANA) TTT2KE3 UP O00754; Q9Y2E5; Q9NTJ4 TTT2KE3 UC MA2B1_HUMAN; MA2B2_HUMAN; MA2C1_HUMAN TTT2KE3 BC Glycosylase TTT2KE3 SN Mannosidase alpha class 2 TTT2KE3 GN MAN2B1; MAN2B2; MAN2C1 TTT2KE3 FC Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages. TTT2KE3 SQ MGAYARASGVCARGCLDSAGPWTMSRALRPPLPPLCFFLLLLAAAGARAGGYETCPTVQPNMLNVHLLPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGNDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKWVRMQKLEMEQVWRASTSLKPPTADLFTGVLPNGYNPPRNLCWDVLCVDQPLVEDPRSPEYNAKELVDYFLNVATAQGRYYRTNHTVMTMGSDFQYENANMWFKNLDKLIRLVNAQQAKGSSVHVLYSTPACYLWELNKANLTWSVKHDDFFPYADGPHQFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGLAANVGPYGSGDSAPLNEAMAVLQHHDAVSGTSRQHVANDYARQLAAGWGPCEVLLSNALARLRGFKDHFTFCQQLNISICPLSQTAARFQVIVYNPLGRKVNWMVRLPVSEGVFVVKDPNGRTVPSDVVIFPSSDSQAHPPELLFSASLPALGFSTYSVAQVPRWKPQARAPQPIPRRSWSPALTIENEHIRATFDPDTGLLMEIMNMNQQLLLPVRQTFFWYNASIGDNESDQASGAYIFRPNQQKPLPVSRWAQIHLVKTPLVQEVHQNFSAWCSQVVRLYPGQRHLELEWSVGPIPVGDTWGKEVISRFDTPLETKGRFYTDSNGREILERRRDYRPTWKLNQTEPVAGNYYPVNTRIYITDGNMQLTVLTDRSQGGSSLRDGSLELMVHRRLLKDDGRGVSEPLMENGSGAWVRGRHLVLLDTAQAAAAGHRLLAEQEVLAPQVVLAPGGGAAYNLGAPPRTQFSGLRRDLPPSVHLLTLASWGPEMVLLRLEHQFAVGEDSGRNLSAPVTLNLRDLFSTFTITRLQETTLVANQLREAASRLKWTTNTGPTPHQTPYQLDPANITLEPMEIRTFLASVQWKEVDG TTT2KE3 TT Clinical trial TTJ8E43 ID TTJ8E43 TTJ8E43 TN Apelin receptor (APLNR) TTJ8E43 UP P35414 TTJ8E43 UC APJ_HUMAN TTJ8E43 SN G-protein coupled receptor HG11; G-protein coupled receptor APJ; Angiotensin receptor-like 1; APJ; AGTRL1 TTJ8E43 GN APLNR TTJ8E43 FC Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone (By similarity). May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Plays also a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure. TTJ8E43 PD 5VBL; 2LOW; 2LOV; 2LOU; 2LOT TTJ8E43 SQ MEEGGDFDNYYGADNQSECEYTDWKSSGALIPAIYMLVFLLGTTGNGLVLWTVFRSSREKRRSADIFIASLAVADLTFVVTLPLWATYTYRDYDWPFGTFFCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAMPVMVLRTTGDLENTTKVQCYMDYSMVATVSSEWAWEVGLGVSSTTVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDLFLMNIFPYCTCISYVNSCLNPFLYAFFDPRFRQACTSMLCCGQSRCAGTSHSSSGEKSASYSSGHSQGPGPNMGKGGEQMHEKSIPYSQETLVVD TTJ8E43 TT Clinical trial TT1HYOF ID TT1HYOF TT1HYOF TN Bacterial Shiga toxin 2 subunit B (Bact stxII) TT1HYOF UP Q7DJJ2 TT1HYOF UC Q7DJJ2_ECOLX TT1HYOF SN Stx2B protein; Stx2B; Stx2 holotoxin subunit B; Stx2 holotoxin B subunit; Shiga-like toxin type II B subunit; Shiga toxin subunit B; Shiga toxin 2v subunit A; Shiga toxin 2B; Shiga toxin 2, subunit B; Shiga toxin 2 B subunit TT1HYOF GN Bact stxII TT1HYOF FC Shiga toxin, one of the most potent bacterial toxins known. Binds to the cellular receptor, globotriaosylceramide, Gb3, found primarily on endothelial cells. TT1HYOF PD 4M1U TT1HYOF SQ MKKMFMAVLFALVSVNAMAADCAKGKIEFSKYNEDDTFTVKVDGKEYWTSRWNLQPLLQSAQLTGMTVTIKSSTCESGSGFAEVQFNND TT1HYOF TT Clinical trial TTZ3P4W ID TTZ3P4W TTZ3P4W TN B-cell maturation protein (TNFRSF17) TTZ3P4W UP Q02223 TTZ3P4W UC TNR17_HUMAN TTZ3P4W SN Tumor necrosis factor receptor superfamily member 17; CD269; BCMA; BCM TTZ3P4W GN TNFRSF17 TTZ3P4W FC Promotes B-cell survival and plays a role in the regulation of humoral immunity. Activates NF-kappa-B and JNK. Receptor for TNFSF13B/BLyS/BAFF and TNFSF13/APRIL. TTZ3P4W PD 6J7W; 4ZFO; 2KN1; 1XU2; 1OQD TTZ3P4W SQ MLQMAGQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVTNSVKGTNAILWTCLGLSLIISLAVFVLMFLLRKINSEPLKDEFKNTGSGLLGMANIDLEKSRTGDEIILPRGLEYTVEECTCEDCIKSKPKVDSDHCFPLPAMEEGATILVTTKTNDYCKSLPAALSATEIEKSISAR TTZ3P4W TT Successful TT9R6BE ID TT9R6BE TT9R6BE TN Calcium-activated potassium channel KCa2.1 (KCNN1) TT9R6BE UP Q92952 TT9R6BE UC KCNN1_HUMAN TT9R6BE BC Voltage-gated ion channel TT9R6BE SN Small conductance calcium-activated potassium channel protein 1; SKCa1; SKCa 1; SK1; SK; KCa2.1 TT9R6BE GN KCNN1 TT9R6BE FC Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin (By similarity). TT9R6BE SQ MNSHSYNGSVGRPLGSGPGALGRDPPDPEAGHPPQPPHSPGLQVVVAKSEPARPSPGSPRGQPQDQDDDEDDEEDEAGRQRASGKPSNVGHRLGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSWGVYTKESLYSFALKCLISLSTAILLGLVVLYHAREIQLFMVDNGADDWRIAMTCERVFLISLELAVCAIHPVPGHYRFTWTARLAFTYAPSVAEADVDVLLSIPMFLRLYLLGRVMLLHSKIFTDASSRSIGALNKITFNTRFVMKTLMTICPGTVLLVFSISSWIIAAWTVRVCERYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQAQKLRSVKIEQGKLNDQANTLTDLAKTQTVMYDLVSELHAQHEELEARLATLESRLDALGASLQALPGLIAQAIRPPPPPLPPRPGPGPQDQAARSSPCRWTPVAPSDCG TT9R6BE TT Clinical trial TT9JH25 ID TT9JH25 TT9JH25 TN Calcium-activated potassium channel KCa2.3 (KCNN3) TT9JH25 UP Q9UGI6 TT9JH25 UC KCNN3_HUMAN TT9JH25 BC Voltage-gated ion channel TT9JH25 SN Small conductance calcium-activated potassium channel protein 3; SKCa3; SKCa 3; SK3; KCa2.3; K3 TT9JH25 GN KCNN3 TT9JH25 FC Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin. TT9JH25 SQ MDTSGHFHDSGVGDLDEDPKCPCPSSGDEQQQQQQQQQQQQPPPPAPPAAPQQPLGPSLQPQPPQLQQQQQQQQQQQQQQPPHPLSQLAQLQSQPVHPGLLHSSPTAFRAPPSSNSTAILHPSSRQGSQLNLNDHLLGHSPSSTATSGPGGGSRHRQASPLVHRRDSNPFTEIAMSSCKYSGGVMKPLSRLSASRRNLIEAETEGQPLQLFSPSNPPEIVISSREDNHAHQTLLHHPNATHNHQHAGTTASSTTFPKANKRKNQNIGYKLGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSWGLYSKDSMFSLALKCLISLSTIILLGLIIAYHTREVQLFVIDNGADDWRIAMTYERILYISLEMLVCAIHPIPGEYKFFWTARLAFSYTPSRAEADVDIILSIPMFLRLYLIARVMLLHSKLFTDASSRSIGALNKINFNTRFVMKTLMTICPGTVLLVFSISLWIIAAWTVRVCERYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRIKNAAANVLRETWLIYKHTKLLKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLSDQANTLVDLSKMQNVMYDLITELNDRSEDLEKQIGSLESKLEHLTASFNSLPLLIADTLRQQQQQLLSAIIEARGVSVAVGTTHTPISDSPIGVSSTSFPTPYTSSSSC TT9JH25 TT Clinical trial TTGJFK1 ID TTGJFK1 TTGJFK1 TN Calcium-activated potassium channel KCa4.1 (KCNT1) TTGJFK1 UP Q5JUK3 TTGJFK1 UC KCNT1_HUMAN TTGJFK1 BC Voltage-gated ion channel TTGJFK1 SN Potassium channel subfamily T member 1; KIAA1422; KCa4.1 TTGJFK1 GN KCNT1 TTGJFK1 FC Outwardly rectifying potassium channel subunit that may coassemble with other Slo-type channel subunits. Activated by high intracellular sodium or chloride levels. Activated upon stimulation of G-protein coupled receptors, such as CHRM1 and GRIA1. May be regulated by calcium in the absence of sodium ions (in vitro) (By similarity). TTGJFK1 SQ MARAKLPRSPSEGKAGPGGAPAGAAAPEEPHGLSPLLPARGGGSVGSDVGQRLPVEDFSLDSSLSQVQVEFYVNENTFKERLKLFFIKNQRSSLRIRLFNFSLKLLTCLLYIVRVLLDDPALGIGCWGCPKQNYSFNDSSSEINWAPILWVERKMTLWAIQVIVAIISFLETMLLIYLSYKGNIWEQIFRVSFVLEMINTLPFIITIFWPPLRNLFIPVFLNCWLAKHALENMINDFHRAILRTQSAMFNQVLILFCTLLCLVFTGTCGIQHLERAGENLSLLTSFYFCIVTFSTVGYGDVTPKIWPSQLLVVIMICVALVVLPLQFEELVYLWMERQKSGGNYSRHRAQTEKHVVLCVSSLKIDLLMDFLNEFYAHPRLQDYYVVILCPTEMDVQVRRVLQIPLWSQRVIYLQGSALKDQDLMRAKMDNGEACFILSSRNEVDRTAADHQTILRAWAVKDFAPNCPLYVQILKPENKFHVKFADHVVCEEECKYAMLALNCICPATSTLITLLVHTSRGQEGQESPEQWQRMYGRCSGNEVYHIRMGDSKFFREYEGKSFTYAAFHAHKKYGVCLIGLKREDNKSILLNPGPRHILAASDTCFYINITKEENSAFIFKQEEKRKKRAFSGQGLHEGPARLPVHSIIASMGTVAMDLQGTEHRPTQSGGGGGGSKLALPTENGSGSRRPSIAPVLELADSSALLPCDLLSDQSEDEVTPSDDEGLSVVEYVKGYPPNSPYIGSSPTLCHLLPVKAPFCCLRLDKGCKHNSYEDAKAYGFKNKLIIVSAETAGNGLYNFIVPLRAYYRSRKELNPIVLLLDNKPDHHFLEAICCFPMVYYMEGSVDNLDSLLQCGIIYADNLVVVDKESTMSAEEDYMADAKTIVNVQTMFRLFPSLSITTELTHPSNMRFMQFRAKDSYSLALSKLEKRERENGSNLAFMFRLPFAAGRVFSISMLDTLLYQSFVKDYMITITRLLLGLDTTPGSGYLCAMKITEGDLWIRTYGRLFQKLCSSSAEIPIGIYRTESHVFSTSESQISVNVEDCEDTREVKGPWGSRAGTGGSSQGRHTGGGDPAEHPLLRRKSLQWARRLSRKAPKQAGRAAAAEWISQQRLSLYRRSERQELSELVKNRMKHLGLPTTGYEDVANLTASDVMNRVNLGYLQDEMNDHQNTLSYVLINPPPDTRLEPSDIVYLIRSDPLAHVASSSQSRKSSCSHKLSSCNPETRDETQL TTGJFK1 TT Clinical trial TTLU5FO ID TTLU5FO TTLU5FO TN Calcium-activated potassium channel KCa4.2 (KCNT2) TTLU5FO UP Q6UVM3 TTLU5FO UC KCNT2_HUMAN TTLU5FO BC Voltage-gated ion channel TTLU5FO SN Sodium and chloride-activated ATP-sensitive potassium channel Slo2.1; Sequence like an intermediate conductance potassium channel subunit; SLICK; Potassium channel subfamily T member 2 TTLU5FO GN KCNT2 TTLU5FO FC Outward rectifying potassium channel. Produces rapidly activating outward rectifier K(+) currents. Activated by high intracellular sodium and chloride levels. Channel activity is inhibited by ATP and by inhalation anesthetics, such as isoflurane (By similarity). Inhibited upon stimulation of G-protein coupled receptors, such as CHRM1 and GRM1. TTLU5FO SQ MVDLESEVPPLPPRYRFRDLLLGDQGWQNDDRVQVEFYMNENTFKERLKLFFIKNQRSSLRIRLFNFSLKLLSCLLYIIRVLLENPSQGNEWSHIFWVNRSLPLWGLQVSVALISLFETILLGYLSYKGNIWEQILRIPFILEIINAVPFIISIFWPSLRNLFVPVFLNCWLAKHALENMINDLHRAIQRTQSAMFNQVLILISTLLCLIFTCICGIQHLERIGKKLNLFDSLYFCIVTFSTVGFGDVTPETWSSKLFVVAMICVALVVLPIQFEQLAYLWMERQKSGGNYSRHRAQTEKHVVLCVSSLKIDLLMDFLNEFYAHPRLQDYYVVILCPTEMDVQVRRVLQIPMWSQRVIYLQGSALKDQDLLRAKMDDAEACFILSSRCEVDRTSSDHQTILRAWAVKDFAPNCPLYVQILKPENKFHIKFADHVVCEEEFKYAMLALNCICPATSTLITLLVHTSRGQEGQQSPEQWQKMYGRCSGNEVYHIVLEESTFFAEYEGKSFTYASFHAHKKFGVCLIGVRREDNKNILLNPGPRYIMNSTDICFYINITKEENSAFKNQDQQRKSNVSRSFYHGPSRLPVHSIIASMGTVAIDLQDTSCRSASGPTLSLPTEGSKEIRRPSIAPVLEVADTSSIQTCDLLSDQSEDETTPDEEMSSNLEYAKGYPPYSPYIGSSPTFCHLLHEKVPFCCLRLDKSCQHNYYEDAKAYGFKNKLIIVAAETAGNGLYNFIVPLRAYYRPKKELNPIVLLLDNPPDMHFLDAICWFPMVYYMVGSIDNLDDLLRCGVTFAANMVVVDKESTMSAEEDYMADAKTIVNVQTLFRLFSSLSIITELTHPANMRFMQFRAKDCYSLALSKLEKKERERGSNLAFMFRLPFAAGRVFSISMLDTLLYQSFVKDYMISITRLLLGLDTTPGSGFLCSMKITADDLWIRTYARLYQKLCSSTGDVPIGIYRTESQKLTTSESQISISVEEWEDTKDSKEQGHHRSNHRNSTSSDQSDHPLLRRKSMQWARRLSRKGPKHSGKTAEKITQQRLNLYRRSERQELAELVKNRMKHLGLSTVGYDEMNDHQSTLSYILINPSPDTRIELNDVVYLIRPDPLAYLPNSEPSRRNSICNVTGQDSREETQL TTLU5FO TT Clinical trial TTE5ITK ID TTE5ITK TTE5ITK TN Cancer/testis antigen 1 (NY-ESO-1) TTE5ITK UP P78358 TTE5ITK UC CTG1B_HUMAN TTE5ITK SN LAGE2B; LAGE2A; LAGE2; LAGE-2; L antigen family member 2; ESO1; Cancer/testis antigen 6.1; CTAG1B; CTAG1; CTAG; CT6.1; Autoimmunogenic cancer/testis antigen NYESO1; Autoimmunogenic cancer/testis antigen NY-ESO-1 TTE5ITK GN CTAG1A TTE5ITK FC Immunogenic protein. Its aberrant re-expression is induced by molecular mechanisms including: DNA demethylation, histone post-translational modification, and microRNA-mediated regulation. The effect of DNA demethylation is evident by the capability of demethylating agents, like 5-aza-2-deoxycytidine, to induce the re-expression of NY-ESO-1 in tumour cells but not in normal epithelial cells. TTE5ITK PD 6AVG; 6AVF; 6AT5; 3KLA; 3HAE TTE5ITK SQ MQAEGRGTGGSTGDADGPGGPGIPDGPGGNAGGPGEAGATGGRGPRGAGAARASGPGGGAPRGPHGGAASGLNGCCRCGARGPESRLLEFYLAMPFATPMEAELARRSLAQDAPPLPVPGVLLKEFTVSGNILTIRLTAADHRQLQLSISSCLQQLSLLMWITQCFLPVFLAQPPSGQRR TTE5ITK TT Clinical trial TT4EN8X ID TT4EN8X TT4EN8X TN Caterpiller protein 1.1 (NLRP3) TT4EN8X UP Q96P20 TT4EN8X UC NLRP3_HUMAN TT4EN8X SN PYRIN-containing APAF1-like protein 1; PYPAF1; NALP3; NACHT, LRR and PYD domains-containing protein 3; Cryopyrin; Cold-induced autoinflammatory syndrome 1 protein; CLR1.1; CIAS1; C1orf7; Angiotensin/vasopressin receptor AII/AVP-like TT4EN8X GN NLRP3 TT4EN8X FC In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP3, PYCARD and CASP1 (and possibly CASP4 and CASP5). Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP3 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. Under resting conditions, NLRP3 is autoinhibited. NLRP3 activation stimuli include extracellular ATP, reactive oxygen species, K(+) efflux, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, cytosolic dsRNA, etc. However, it is unclear what constitutes the direct NLRP3 activator. Activation in presence of cytosolic dsRNA is mediated by DHX33. Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth. During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF. As the sensor component of the NLRP3 inflammasome, plays a crucial role in innate immunity and inflammation. TT4EN8X PD 3QF2; 2NAQ TT4EN8X SQ MKMASTRCKLARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKRDEPKWGSDNARVSNPTVICQEDSIEEEWMGLLEYLSRISICKMKKDYRKKYRKYVRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREQELLAIGKTKTCESPVSPIKMELLFDPDDEHSEPVHTVVFQGAAGIGKTILARKMMLDWASGTLYQDRFDYLFYIHCREVSLVTQRSLGDLIMSCCPDPNPPIHKIVRKPSRILFLMDGFDELQGAFDEHIGPLCTDWQKAERGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFSEAKRKEYFFKYFSDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCTGLKQQMESGKSLAQTSKTTTAVYVFFLSSLLQPRGGSQEHGLCAHLWGLCSLAADGIWNQKILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSFIHMTFQEFFAAMYYLLEEEKEGRTNVPGSRLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQEEDFVQRAMDYFPKIEINLSTRMDHMVSSFCIENCHRVESLSLGFLHNMPKEEEEEEKEGRHLDMVQCVLPSSSHAACSHGLVNSHLTSSFCRGLFSVLSTSQSLTELDLSDNSLGDPGMRVLCETLQHPGCNIRRLWLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLLCNLKKLWLVSCCLTSACCQDLASVLSTSHSLTRLYVGENALGDSGVAILCEKAKNPQCNLQKLGLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSCLLQNLGLSEMYFNYETKSALETLQEEKPELTVVFEPSW TT4EN8X TT Clinical trial TTKF4WV ID TTKF4WV TTKF4WV TN Connecting peptide (C-peptide) TTKF4WV UP P02765 (301-340) TTKF4WV UC FETUA_HUMAN TTKF4WV BC Fetuin family TTKF4WV SN Fetuin-A; Alpha-2-Z-globulin; Alpha-2-HS-glycoprotein chainB; Alpha-2-HS-glycoprotein (301-340); AHSG TTKF4WV GN AHSG TTKF4WV FC Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions. TTKF4WV SQ LAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSHPRKTR TTKF4WV TT Clinical trial TTIW59R ID TTIW59R TTIW59R TN C-X-C chemokine receptor type 5 (CXCR5) TTIW59R UP P32302 TTIW59R UC CXCR5_HUMAN TTIW59R BC GPCR rhodopsin TTIW59R SN Monocyte-derived receptor15; Monocyte-derived receptor 15; MDR15; MDR-15; Chemokine receptor CXCR5; CXCR-5; CXC-R5; CD185; Burkitt'S lymphoma receptor 1; Burkitt lymphoma receptor 1; BLR1 TTIW59R GN CXCR5 TTIW59R FC Involved in B-cell migration into B-cell follicles of spleen and Peyer patches but not into those of mesenteric or peripheral lymph nodes. May have a regulatory function in Burkitt lymphoma (BL) lymphomagenesis and/or B-cell differentiation. Cytokine receptor that binds to B-lymphocyte chemoattractant (BLC). TTIW59R SQ MNYPLTLEMDLENLEDLFWELDRLDNYNDTSLVENHLCPATEGPLMASFKAVFVPVAYSLIFLLGVIGNVLVLVILERHRQTRSSTETFLFHLAVADLLLVFILPFAVAEGSVGWVLGTFLCKTVIALHKVNFYCSSLLLACIAVDRYLAIVHAVHAYRHRRLLSIHITCGTIWLVGFLLALPEILFAKVSQGHHNNSLPRCTFSQENQAETHAWFTSRFLYHVAGFLLPMLVMGWCYVGVVHRLRQAQRRPQRQKAVRVAILVTSIFFLCWSPYHIVIFLDTLARLKAVDNTCKLNGSLPVAITMCEFLGLAHCCLNPMLYTFAGVKFRSDLSRLLTKLGCTGPASLCQLFPSWRRSSLSESENATSLTTF TTIW59R TT Clinical trial TTIW59R FM GPCR rhodopsin TT1C9K6 ID TT1C9K6 TT1C9K6 TN Delta-like protein 3 (DLL3) TT1C9K6 UP Q9NYJ7 TT1C9K6 UC DLL3_HUMAN TT1C9K6 SN pudgy; pu; delta like canonical Notch ligand 3; SCDO1; Drosophila Delta homolog 3; Delta3 TT1C9K6 GN DLL3 TT1C9K6 FC May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm. Inhibits primary neurogenesis. TT1C9K6 SQ MVSPRMSGLLSQTVILALIFLPQTRPAGVFELQIHSFGPGPGPGAPRSPCSARLPCRLFFRVCLKPGLSEEAAESPCALGAALSARGPVYTEQPGAPAPDLPLPDGLLQVPFRDAWPGTFSFIIETWREELGDQIGGPAWSLLARVAGRRRLAAGGPWARDIQRAGAWELRFSYRARCEPPAVGTACTRLCRPRSAPSRCGPGLRPCAPLEDECEAPLVCRAGCSPEHGFCEQPGECRCLEGWTGPLCTVPVSTSSCLSPRGPSSATTGCLVPGPGPCDGNPCANGGSCSETPRSFECTCPRGFYGLRCEVSGVTCADGPCFNGGLCVGGADPDSAYICHCPPGFQGSNCEKRVDRCSLQPCRNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGAHRCSCALGFGGRDCRERADPCAARPCAHGGRCYAHFSGLVCACAPGYMGARCEFPVHPDGASALPAAPPGLRPGDPQRYLLPPALGLLVAAGVAGAALLLVHVRRRGHSQDAGSRLLAGTPEPSVHALPDALNNLRTQEGSGDGPSSSVDWNRPEDVDPQGIYVISAPSIYAREVATPLFPPLHTGRAGQRQHLLFPYPSSILSVK TT1C9K6 TT Clinical trial TT1C9K6 KE hsa01522:Endocrine resistance; hsa04330:Notch signaling pathway; hsa04658:Th1 and Th2 cell differentiation; hsa05200:Pathways in cancer; hsa05224:Breast cancer TT2TNRM ID TT2TNRM TT2TNRM TN Dystrophin nonsense mutant (DMD) TT2TNRM UP P11532 TT2TNRM UC DMD_HUMAN TT2TNRM SN MRX85 nonsense mutant; DXS272 nonsense mutant; DXS270 nonsense mutant; DXS269 nonsense mutant; DXS268 nonsense mutant; DXS239 nonsense mutant; DXS230 nonsense mutant; DXS206 nonsense mutant; DXS164 nonsense mutant; DXS142 nonsense mutant; CMD3B nonsense mutant; BMD nonsense mutant TT2TNRM GN DMD TT2TNRM FC Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. Anchors the extracellular matrix to the cytoskeleton via F-actin. TT2TNRM PD 3UUN; 1EG4; 1EG3; 1DXX TT2TNRM SQ MLWWEEVEDCYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQVLPQQVSIEAIQEVEMLPRPPKVTKEEHFQLHHQMHYSQQITVSLAQGYERTSSPKPRFKSYAYTQAAYVTTSDPTRSPFPSQHLEAPEDKSFGSSLMESEVNLDRYQTALEEVLSWLLSAEDTLQAQGEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIGTGKLSEDEETEVQEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQNQKLKELNDWLTKTEERTRKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDILLKWQRLTEEQCLFSAWLSEKEDAVNKIHTTGFKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSVTQKTEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQEELPPPPPQKKRQITVDSEIRKRLDVDITELHSWITRSEAVLQSPEFAIFRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEGVNADSIKQASEQLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIALKEKGQGPMFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETKLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNEVEFKLKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVREETMMVMTEDMPLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRSVEKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPVVTKETAISKLEMPSSLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKLYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLQELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRDFGPASQHFLSTSVQGPWERAISPNKVPYYINHETQTTCWDHPKMTELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEYCTPTTSGEDVRDFAKVLKNKFRTKRYFAKHPRMGYLPVQTVLEGDNMETPVTLINFWPVDSAPASSPQLSHDDTHSRIEHYASRLAEMENSNGSYLNDSISPNESIDDEHLLIQHYCQSLNQDSPLSQPRSPAQILISLESEERGELERILADLEEENRNLQAEYDRLKQQHEHKGLSPLPSPPEMMPTSPQSPRDAELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPQAEAKVNGTTVSSPSTSLQRSDSSQPMLLRVVGSQTSDSMGEEDLLSPPQDTSTGLEEVMEQLNNSFPSSRGRNTPGKPMREDTM TT2TNRM TT Clinical trial TT3Z102 ID TT3Z102 TT3Z102 TN Ebola virus VP35 messenger RNA (EV VP35 mRNA) TT3Z102 UP Q5XX07 TT3Z102 UC VP35_EBOSU TT3Z102 BC mRNA target TT3Z102 SN VP35 (mRNA); Polymerase cofactor VP35 (mRNA) TT3Z102 GN EV VP35 mRNA TT3Z102 FC Prevents establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of interferon regulatory factor 3 (IRF3), a transcription factor critical for the induction of interferons alpha and beta. This blockage is produced through the interaction with and inhibition host IKBKE and TBK1 producing a strong inhibition of the phosphorylation and activation of IRF3. Also inhibits the antiviral effect mediated by the interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2/PKR. Acts as a polymerase cofactor in the RNA polymerase transcription and replication complex. TT3Z102 SQ MQQDRTYRHHGPEVSGWFSEQLMTGKIPLTEVFVDVENKPSPAPITIISKNPKTTRKSDKQVQTDDASSLLTEEVKAAINSVISAVRRQTNAIESLEGRVTTLEASLKPVQDMAKTISSLNRSCAEMVAKYDLLVMTTGRATATAAATEAYWNEHGQAPPGPSLYEDDAIKAKLKDPNGKVPESVKQAYINLDSTSALNEENFGRPYISAKDLKEIIYDHLPGFGTAFHQLVQVICKIGKDNNILDIIHAEFQASLAEGDSPQCALIQITKRIPAFQDASPPIVHIKSRGDIPKACQKSLRPVPPSPKIDRGWVCIFQFQDGKALGLKI TT3Z102 TT Clinical trial TT3Z102 FM mRNA target TTFNJ4R ID TTFNJ4R TTFNJ4R TN Embryonic ectoderm development protein (EED) TTFNJ4R UP O75530 TTFNJ4R UC EED_HUMAN TTFNJ4R SN hEED; WD protein associating with integrin cytoplasmic tails 1; WAIT-1 TTFNJ4R GN EED TTFNJ4R FC Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A. TTFNJ4R PD 6C24; 6C23; 6B3W; 5WUK; 5WP3 TTFNJ4R SQ MSEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR TTFNJ4R TT Clinical trial TTYJWT7 ID TTYJWT7 TTYJWT7 TN Endosialin (CD248) TTYJWT7 UP Q9HCU0 TTYJWT7 UC CD248_HUMAN TTYJWT7 SN Tumor endothelial marker 1; Tumor Endothelial Marker 1 (TEM-1); TEM1; CD164L1 TTYJWT7 GN CD248 TTYJWT7 FC May play a role in tumor angiogenesis. TTYJWT7 SQ MLLRLLLAWAAAGPTLGQDPWAAEPRAACGPSSCYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGPASRLLWIGLQRQARQCQLQRPLRGFTWTTGDQDTAFTNWAQPASGGPCPAQRCVALEASGEHRWLEGSCTLAVDGYLCQFGFEGACPALQDEAGQAGPAVYTTPFHLVSTEFEWLPFGSVAAVQCQAGRGASLLCVKQPEGGVGWSRAGPLCLGTGCSPDNGGCEHECVEEVDGHVSCRCTEGFRLAADGRSCEDPCAQAPCEQQCEPGGPQGYSCHCRLGFRPAEDDPHRCVDTDECQIAGVCQQMCVNYVGGFECYCSEGHELEADGISCSPAGAMGAQASQDLGDELLDDGEDEEDEDEAWKAFNGGWTEMPGILWMEPTQPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIPATHPALSRDHQIPVIAANYPDLPSAYQPGILSVSHSAQPPAHQPPMISTKYPELFPAHQSPMFPDTRVAGTQTTTHLPGIPPNHAPLVTTLGAQLPPQAPDALVLRTQATQLPIIPTAQPSLTTTSRSPVSPAHQISVPAATQPAALPTLLPSQSPTNQTSPISPTHPHSKAPQIPREDGPSPKLALWLPSPAPTAAPTALGEAGLAEHSQRDDRWLLVALLVPTCVFLVVLLALGIVYCTRCGPHAPNKRITDCYRWVIHAGSKSPTEPMPPRGSLTGVQTCRTSV TTYJWT7 TT Clinical trial TTHSZXO ID TTHSZXO TTHSZXO TN Endothelial lipase (LIPG) TTHSZXO UP Q9Y5X9 TTHSZXO UC LIPE_HUMAN TTHSZXO SN Endothelial cell-derived lipase; EL; EDL TTHSZXO GN LIPG TTHSZXO FC Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin. TTHSZXO EC EC 3.1.1.3 TTHSZXO SQ MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHIDIYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWFRKCRDGWRMKNETSPTVELP TTHSZXO TT Clinical trial TTTRS9B ID TTTRS9B TTTRS9B TN Fascin (FSCN1) TTTRS9B UP Q16658 TTTRS9B UC FSCN1_HUMAN TTTRS9B SN Singed-like protein; SNL; HSN; FAN1; 55 kDa actin-bundling protein; 55 kDa actin bundling protein TTTRS9B GN FSCN1 TTTRS9B FC Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. Organizes filamentous actin into bundles with a minimum of 4. 1:1 actin/fascin ratio. TTTRS9B PD 6I18; 6I17; 6I16; 6I15; 6I14 TTTRS9B SQ MTANGTAEAVQIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPGPDCRFLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTADHRFLRHDGRLVARPEPATGYTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTATGGVQSTASSKNASCYFDIEWRDRRITLRASNGKFVTSKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVAIKVGGRYLKGDHAGVLKASAETVDPASLWEY TTTRS9B TT Clinical trial TT8RXO5 ID TT8RXO5 TT8RXO5 TN GABA transporter-3 (SLC6A11) TT8RXO5 UP P48066 TT8RXO5 UC S6A11_HUMAN TT8RXO5 SN Solute carrier family 6 member 11; Sodium- and chloride-dependent GABA transporter 3; GAT3; GAT-3; GABT3 TT8RXO5 GN SLC6A11 TT8RXO5 FC Terminates the action of GABA by its high affinity sodium-dependent reuptake into presynaptic terminals. TT8RXO5 SQ MTAEKALPLGNGKAAEEARESEAPGGGCSSGGAAPARHPRVKRDKAVHERGHWNNKVEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFLIPYVVFFICCGIPVFFLETALGQFTSEGGITCWRKVCPLFEGIGYATQVIEAHLNVYYIIILAWAIFYLSNCFTTELPWATCGHEWNTENCVEFQKLNVSNYSHVSLQNATSPVMEFWEHRVLAISDGIEHIGNLRWELALCLLAAWTICYFCIWKGTKSTGKVVYVTATFPYIMLLILLIRGVTLPGASEGIKFYLYPDLSRLSDPQVWVDAGTQIFFSYAICLGCLTALGSYNNYNNNCYRDCIMLCCLNSGTSFVAGFAIFSVLGFMAYEQGVPIAEVAESGPGLAFIAYPKAVTMMPLSPLWATLFFMMLIFLGLDSQFVCVESLVTAVVDMYPKVFRRGYRRELLILALSVISYFLGLVMLTEGGMYIFQLFDSYAASGMCLLFVAIFECICIGWVYGSNRFYDNIEDMIGYRPPSLIKWCWMIMTPGICAGIFIFFLIKYKPLKYNNIYTYPAWGYGIGWLMALSSMLCIPLWICITVWKTEGTLPEKLQKLTTPSTDLKMRGKLGVSPRMVTVNDCDAKLKSDGTIAAITEKETHF TT8RXO5 TT Clinical trial TT63XRS ID TT63XRS TT63XRS TN GDNF receptor alpha-3 (GFRA3) TT63XRS UP O60609 TT63XRS UC GFRA3_HUMAN TT63XRS SN UNQ339/PRO538/PRO3664; GFR-alpha-3; GDNFR-alpha-3; GDNF family receptor alpha-3 TT63XRS GN GFRA3 TT63XRS FC Mediates the artemin-induced autophosphorylation and activation of the RET receptor tyrosine kinase. Receptor for the glial cell line-derived neurotrophic factor, ARTN (artemin). TT63XRS PD 2GH0 TT63XRS SQ MVRPLNPRPLPPVVLMLLLLLPPSPLPLAAGDPLPTESRLMNSCLQARRKCQADPTCSAAYHHLDSCTSSISTPLPSEEPSVPADCLEAAQQLRNSSLIGCMCHRRMKNQVACLDIYWTVHRARSLGNYELDVSPYEDTVTSKPWKMNLSKLNMLKPDSDLCLKFAMLCTLNDKCDRLRKAYGEACSGPHCQRHVCLRQLLTFFEKAAEPHAQGLLLCPCAPNDRGCGERRRNTIAPNCALPPVAPNCLELRRLCFSDPLCRSRLVDFQTHCHPMDILGTCATEQSRCLRAYLGLIGTAMTPNFVSNVNTSVALSCTCRGSGNLQEECEMLEGFFSHNPCLTEAIAAKMRFHSQLFSQDWPHPTFAVMAHQNENPAVRPQPWVPSLFSCTLPLILLLSLW TT63XRS TT Clinical trial TT63XRS FM GDNFR family TT2D1J6 ID TT2D1J6 TT2D1J6 TN Haemophilus influenzae Acetylglucosamine deacetylase (Hae-influ lpxC) TT2D1J6 UP Q4QLF2 TT2D1J6 UC LPXC_HAEI8 TT2D1J6 SN UDP-3-O-acyl-N-acetylglucosamine deacetylase; UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase; Hae-influ UDP-3-O-acyl-GlcNAc deacetylase TT2D1J6 GN Hae-influ lpxC TT2D1J6 FC Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. TT2D1J6 EC EC 3.5.1.108 TT2D1J6 SQ MIKQRTLKQSIKVTGVGLHSGNKVTLTLRPAMPNTGVVYYRTDLNPAVAFPADPNSVRDTMLCTALINDQGVRISTVEHLNAALAGLGIDNIIIEVDAPEIPIMDGSASPFIYLLLDAGIEEQNAAKKFIRIKEYVRVEDGDKWAEFKPYNGFRLDFTIDFDHPAIGKDVRNYEMNFSAQAFVHQISRARTFGFMKDIEYLQSQGLALGGSLDNAIVLDDYRILNEDGLRFKDELVRHKMLDAIGDLYMAGYNIIGDFKAYKSGHGLNNKLLRAVLANQEAWEFVTFEDKEQVPQGYVAPAQVLI TT2D1J6 TT Clinical trial TTZAVYN ID TTZAVYN TTZAVYN TN Hematopoietic progenitor cell antigen CD34 (CD34) TTZAVYN UP P28906 TTZAVYN UC CD34_HUMAN TTZAVYN SN CD34 molecule TTZAVYN GN CD34 TTZAVYN FC Could act as a scaffold for the attachment of lineage specific glycans, allowing stem cells to bind to lectins expressed by stromal cells or other marrow components. Presents carbohydrate ligands to selectins. Possible adhesion molecule with a role in early hematopoiesis by mediating the attachment of stem cells to the bone marrow extracellular matrix or directly to stromal cells. TTZAVYN SQ MLVRRGARAGPRMPRGWTALCLLSLLPSGFMSLDNNGTATPELPTQGTFSNVSTNVSYQETTTPSTLGSTSLHPVSQHGNEATTNITETTVKFTSTSVITSVYGNTNSSVQSQTSVISTVFTTPANVSTPETTLKPSLSPGNVSDLSTTSTSLATSPTKPYTSSSPILSDIKAEIKCSGIREVKLTQGICLEQNKTSSCAEFKKDRGEGLARVLCGEEQADADAGAQVCSLLLAQSEVRPQCLLLVLANRTEISSKLQLMKKHQSDLKKLGILDFTEQDVASHQSYSQKTLIALVTSGALLAVLGITGYFLMNRRSWSPTGERLGEDPYYTENGGGQGYSSGPGTSPEAQGKASVNRGAQENGTGQATSRNGHSARQHVVADTEL TTZAVYN TT Clinical trial TTDBG95 ID TTDBG95 TTDBG95 TN Hepatitis C virus Envelope glycoprotein E2 (HCV NS1) TTDBG95 UP P26662 (384-746) TTDBG95 UC POLG_HCV1 TTDBG95 SN Hepacivirus polyprotein TTDBG95 GN HCV NS1 TTDBG95 FC NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication. TTDBG95 PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TTDBG95 SQ ETHVTGGSAGHTVSGFVSLLAPGAKQNVQLINTNGSWHLNSTALNCNDSLNTGWLAGLFYHHKFNSSGCPERLASCRPLTDFDQGWGPISYANGSGPDQRPYCWHYPPKPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGENDTDVFVLNNTRPPLGNWFGCTWMNSTGFTKVCGAPPCVIGGAGNNTLHCPTDCFRKHPDATYSRCGSGPWITPRCLVDYPYRLWHYPCTINYTIFKIRMYVGGVEHRLEAACNWTRGERCDLEDRDRSELSPLLLTTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVVLLFLLLADARVCSCLWMMLLISQAEA TTDBG95 TT Clinical trial TTRHUKY ID TTRHUKY TTRHUKY TN Hepatitis C virus Serine protease NS4A (HCV NS4A) TTRHUKY UP P26664 (1658-1711) TTRHUKY UC POLG_HCV1 TTRHUKY SN HCV p8 TTRHUKY GN HCV NS4A TTRHUKY FC Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). TTRHUKY PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TTRHUKY SQ STWVLVGGVLAALAAYCLSTGCVVIVGRVVLSGKPAIIPDREVLYREFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTASRQAEVIAPAVQTNWQKLETFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTSQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAAIGSVGLGKVLIDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPC TTRHUKY TT Clinical trial TT0AWFK ID TT0AWFK TT0AWFK TN HIF-1 responsive protein RTP801 (DDIT4) TT0AWFK UP Q9NX09 TT0AWFK UC DDIT4_HUMAN TT0AWFK SN RTP801; REDD1; REDD-1; Protein regulated in development and DNA damage response 1; DNA damage-inducible transcript 4 protein TT0AWFK GN DDIT4 TT0AWFK FC Regulates cell growth, proliferation and survival via inhibition of the activity of the mammalian target of rapamycin complex 1 (mTORC1). Inhibition of mTORC1 is mediated by a pathway that involves DDIT4/REDD1, AKT1, the TSC1-TSC2 complex and the GTPase RHEB. Plays an important role in responses to cellular energy levels and cellular stress, including responses to hypoxia and DNA damage. Regulates p53/TP53-mediated apoptosis in response to DNA damage via its effect on mTORC1 activity. Its role in the response to hypoxia depends on the cell type; it mediates mTORC1 inhibition in fibroblasts and thymocytes, but not in hepatocytes (By similarity). Required for mTORC1-mediated defense against viral protein synthesis and virus replication (By similarity). Inhibits neuronal differentiation and neurite outgrowth mediated by NGF via its effect on mTORC1 activity. Required for normal neuron migration during embryonic brain development. Plays a role in neuronal cell death. TT0AWFK PD 3LQ9 TT0AWFK SQ MPSLWDRFSSSSTSSSPSSLPRTPTPDRPPRSAWGSATREEGFDRSTSLESSDCESLDSSNSGFGPEEDTAYLDGVSLPDFELLSDPEDEHLCANLMQLLQESLAQARLGSRRPARLLMPSQLVSQVGKELLRLAYSEPCGLRGALLDVCVEQGKSCHSVGQLALDPSLVPTFQLTLVLRLDSRLWPKIQGLFSSANSPFLPGFSQSLTLSTGFRVIKKKLYSSEQLLIEEC TT0AWFK TT Clinical trial TTTWS2G ID TTTWS2G TTTWS2G TN Human immunodeficiency virus Capsid p24 (HIV p24) TTTWS2G UP P03366 (133-363) TTTWS2G UC POL_HV1B1 TTTWS2G SN CA TTTWS2G GN HIV p24 TTTWS2G FC Integrase: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre- integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This processis mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration. TTTWS2G PD 6OE3; 6HAK; 6ELI; 6DUH; 6DUG TTTWS2G SQ PIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVL TTTWS2G TT Clinical trial TTBYP1X ID TTBYP1X TTBYP1X TN Human immunodeficiency virus Envelope glycoprotein gp120 (HIV gp120) TTBYP1X UP P04578 (512-856) TTBYP1X UC ENV_HV1H2 TTBYP1X SN Env polyprotein gp120 (33-511) TTBYP1X GN HIV gp120 TTBYP1X FC Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C- terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin- dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. TTBYP1X PD 6DLN; 6DE7; 6BXQ; 6BXP; 6B9K TTBYP1X SQ AVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL TTBYP1X TT Successful TTEC2T3 ID TTEC2T3 TTEC2T3 TN Human immunodeficiency virus Envelope glycoprotein gp160 (HIV env) TTEC2T3 UP P04578 TTEC2T3 UC ENV_HV1H2 TTEC2T3 SN Envelope glycoprotein gp160; Env polyprotein TTEC2T3 GN HIV env TTEC2T3 FC Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. TTEC2T3 PD 6DLN; 6DE7; 6BXQ; 6BXP; 6B9K TTEC2T3 SQ MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL TTEC2T3 TT Clinical trial TT8Z1OP ID TT8Z1OP TT8Z1OP TN Human immunodeficiency virus Nucleocapsid p7 (HIV p7) TT8Z1OP UP P03366 (378-432) TT8Z1OP UC POL_HV1B1 TT8Z1OP SN HIV NC TT8Z1OP GN HIV p7 TT8Z1OP FC Gag-Pol polyprotein: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. TT8Z1OP PD 6OE3; 6HAK; 6ELI; 6DUH; 6DUG TT8Z1OP SQ MQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQAN TT8Z1OP TT Clinical trial TTRP4JT ID TTRP4JT TTRP4JT TN Human immunodeficiency virus Rev messenger RNA (HIV rev mRNA) TTRP4JT UP P04618 TTRP4JT UC REV_HV1H2 TTRP4JT BC mRNA target TTRP4JT SN rev (mRNA); Regulator of expression of viral proteins (mRNA); Protein Rev (mRNA); Anti-repression transactivator (mRNA); ART/TRS (mRNA) TTRP4JT GN HIV rev mRNA TTRP4JT FC These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs. Rev itself is translated from a fully spliced mRNA that readily exits the nucleus. Rev's nuclear localization signal (NLS) binds directly to KPNB1/Importin beta-1 without previous binding to KPNA1/Importin alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran-GDP) and targets Rev to the nucleus. In the nucleus, the conversion from Ran-GDP to Ran-GTP dissociates Rev from KPNB1 and allows Rev's binding to the RRE in viral pre-mRNAs. Rev multimerization on the RRE via cooperative assembly exposes its nuclear export signal (NES) to the surface. Rev can then form a complex with XPO1/CRM1 and Ran-GTP, leading to nuclear export of the complex. Conversion from Ran-GTP to Ran-GDP mediates dissociation of the Rev/RRE/XPO1/RAN complex, so that Rev can return to the nucleus for a subsequent round of export. Beside KPNB1, also seems to interact with TNPO1/Transportin-1, RANBP5/IPO5 and IPO7/RANBP7 for nuclear import. The nucleoporin-like HRB/RIP is an essential cofactor that probably indirectly interacts with Rev to release HIV RNAs from the perinuclear region to the cytoplasm. Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. TTRP4JT SQ MAGRSGDSDEELIRTVRLIKLLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILGTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGTKE TTRP4JT TT Clinical trial TTRP4JT FM mRNA target TTF7I5O ID TTF7I5O TTF7I5O TN Human immunodeficiency virus Rev protein (HIV rev) TTF7I5O UP P04618 TTF7I5O UC REV_HV1H2 TTF7I5O SN rev; Regulator of expression of viral proteins; Anti-repression transactivator; ART/TRS TTF7I5O GN HIV rev TTF7I5O FC Escorts unspliced or incompletely spliced viral pre- mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs. Rev itself is translated from a fully spliced mRNA that readily exits the nucleus. Rev's nuclear localization signal (NLS) bindsdirectly to KPNB1/Importin beta-1 without previous binding to KPNA1/Importin alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran-GDP) and targets Rev to the nucleus. In the nucleus, the conversionfrom Ran-GDP to Ran-GTP dissociates Rev from KPNB1 and allows Rev's binding to the RRE in viral pre-mRNAs. Rev multimerization on the RRE via cooperative assembly exposes its nuclear export signal (NES) to the surface. Rev can then form a complex with XPO1/CRM1 and Ran-GTP, leading to nuclear export of the complex. Conversion from Ran-GTP to Ran-GDP mediates dissociation of the Rev/RRE/XPO1/RAN complex, so that Rev can return to the nucleus for a subsequent round of export. Beside KPNB1, also seems to interact with TNPO1/Transportin-1, RANBP5/IPO5 and IPO7/RANBP7 for nuclear import. The nucleoporin-like HRB/RIP is an essential cofactor that probably indirectly interacts with Rev to release HIV RNAs from the perinuclear region to the cytoplasm. Interacts with DDX1; the interaction is necessary for proper subcellular localization of this protein. TTF7I5O SQ MAGRSGDSDEELIRTVRLIKLLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILGTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGTKE TTF7I5O TT Clinical trial TTF7I5O RC R-HSA-162585:Uncoating of the HIV Virion; R-HSA-162588:Budding and maturation of HIV virion; R-HSA-162592:Integration of provirus; R-HSA-162594:Early Phase of HIV Life Cycle; R-HSA-164516:Minus-strand DNA synthesis; R-HSA-164525:Plus-strand DNA synthesis; R-HSA-164843:2-LTR circle formation; R-HSA-173107:Binding and entry of HIV virion; R-HSA-175474:Assembly Of The HIV Virion; R-HSA-175567:Integration of viral DNA into host genomic DNA; R-HSA-177539:Autointegration results in viral DNA circles; R-HSA-180689:APOBEC3G mediated resistance to HIV-1 infection; R-HSA-180910:Vpr-mediated nuclear import of PICs TT0T5HK ID TT0T5HK TT0T5HK TN Immunoglobulin gamma-1 heavy NIE (NIE) TT0T5HK UP P0DOX5 TT0T5HK UC IGG1_HUMAN TT0T5HK SN Immunoglobulin gamma-1 heavy chain NIE TT0T5HK GN NIE TT0T5HK FC Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:20176268, PubMed:17576170). TT0T5HK PD 6OGE; 6N35; 6N32; 6N2X; 6MUB TT0T5HK SQ QVQLVQSGGGVVQPGRSLRLSCAASGFTFSRYTIHWVRQAPGKGLEWVAVMSYNGNNKHYADSVNGRFTISRNDSKNTLYLNMNSLRPEDTAVYYCARIRDTAMFFAHWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK TT0T5HK TT Clinical trial TTXH2ZN ID TTXH2ZN TTXH2ZN TN Inactive tyrosine-protein kinase 7 (PTK7) TTXH2ZN UP Q13308 TTXH2ZN UC PTK7_HUMAN TTXH2ZN BC Protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily TTXH2ZN SN Tyrosine-protein kinase-like 7; Pseudo tyrosine kinase receptor 7; Protein-tyrosine kinase 7; Colon carcinoma kinase 4; CCK-4 TTXH2ZN GN PTK7 TTXH2ZN FC Inactive tyrosine kinase involved in Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathway. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis. TTXH2ZN SQ MGAARGSPARPRRLPLLSVLLLPLLGGTQTAIVFIKQPSSQDALQGRRALLRCEVEAPGPVHVYWLLDGAPVQDTERRFAQGSSLSFAAVDRLQDSGTFQCVARDDVTGEEARSANASFNIKWIEAGPVVLKHPASEAEIQPQTQVTLRCHIDGHPRPTYQWFRDGTPLSDGQSNHTVSSKERNLTLRPAGPEHSGLYSCCAHSAFGQACSSQNFTLSIADESFARVVLAPQDVVVARYEEAMFHCQFSAQPPPSLQWLFEDETPITNRSRPPHLRRATVFANGSLLLTQVRPRNAGIYRCIGQGQRGPPIILEATLHLAEIEDMPLFEPRVFTAGSEERVTCLPPKGLPEPSVWWEHAGVRLPTHGRVYQKGHELVLANIAESDAGVYTCHAANLAGQRRQDVNITVATVPSWLKKPQDSQLEEGKPGYLDCLTQATPKPTVVWYRNQMLISEDSRFEVFKNGTLRINSVEVYDGTWYRCMSSTPAGSIEAQARVQVLEKLKFTPPPQPQQCMEFDKEATVPCSATGREKPTIKWERADGSSLPEWVTDNAGTLHFARVTRDDAGNYTCIASNGPQGQIRAHVQLTVAVFITFKVEPERTTVYQGHTALLQCEAQGDPKPLIQWKGKDRILDPTKLGPRMHIFQNGSLVIHDVAPEDSGRYTCIAGNSCNIKHTEAPLYVVDKPVPEESEGPGSPPPYKMIQTIGLSVGAAVAYIIAVLGLMFYCKKRCKAKRLQKQPEGEEPEMECLNGGPLQNGQPSAEIQEEVALTSLGSGPAATNKRHSTSDKMHFPRSSLQPITTLGKSEFGEVFLAKAQGLEEGVAETLVLVKSLQSKDEQQQLDFRRELEMFGKLNHANVVRLLGLCREAEPHYMVLEYVDLGDLKQFLRISKSKDEKLKSQPLSTKQKVALCTQVALGMEHLSNNRFVHKDLAARNCLVSAQRQVKVSALGLSKDVYNSEYYHFRQAWVPLRWMSPEAILEGDFSTKSDVWAFGVLMWEVFTHGEMPHGGQADDEVLADLQAGKARLPQPEGCPSKLYRLMQRCWALSPKDRPSFSEIASALGDSTVDSKP TTXH2ZN TT Clinical trial TT62KQV ID TT62KQV TT62KQV TN Influenza Polymerase basic protein 2 (Influ PB2) TT62KQV UP P03428 TT62KQV UC PB2_I34A1 TT62KQV SN RNA-directed RNA polymerase subunit P3; Polymerase basic protein 2 TT62KQV GN Influ PB2 TT62KQV FC Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. In addition, participates in the inhibition of type I interferon induction through interaction with and inhibition of the host mitochondrial antiviral signaling protein MAVS. TT62KQV PD 4U6O; 4J2R; 4ENF; 3WI1; 3WI0 TT62KQV SQ MERIKELRNLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRITEMIPERNEQGQTLWSKMNDAGSDRVMVSPLAVTWWNRNGPITNTVHYPKIYKTYFERVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRAAVSADPLASLLEMCHSTQIGGIRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGSSVKREEEVLTGNLQTLKIRVHEGYEEFTMVGRRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGVEPIDNVMGMIGILPDMTPSIEMSMRGVRISKMGVDEYSSTERVVVSIDRFLRIRDQRGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQNPTMLYNKMEFEPFQSLVPKAIRGQYSGFVRTLFQQMRDVLGTFDTAQIIKLLPFAAAPPKQSRMQFSSFTVNVRGSGMRILVRGNSPVFNYNKATKRLTVLGKDAGTLTEDPDEGTAGVESAVLRGFLILGKEDKRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN TT62KQV TT Clinical trial TTT6LOU ID TTT6LOU TTT6LOU TN Insulin-like growth factor-I (IGF1) TTT6LOU UP P05019 TTT6LOU UC IGF1_HUMAN TTT6LOU SN SomatomedinC; Somatomedin-C; Mechano growth factor; Insulin-like growth factor I; IGFI; IGF-I TTT6LOU GN IGF1 TTT6LOU FC May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation. Ca(2+)-dependent exocytosis of IGF1 is required for sensory perception of smell in the olfactory bulb. Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiatiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling. Induces the phosphorylation and activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and AKT1. The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. TTT6LOU PD 6FF3; 5U8Q; 4XSS; 3LRI; 3GF1 TTT6LOU SQ MGKISSLPTQLFKCCFCDFLKVKMHTMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKTQKYQPPSTNKNTKSQRRKGWPKTHPGGEQKEGTEASLQIRGKKKEQRREIGSRNAECRGKKGK TTT6LOU TT Clinical trial TTT6LOU FM Insulin family TTE8WGO ID TTE8WGO TTE8WGO TN Insulin-like growth factor-II (IGF2) TTE8WGO UP P01344 TTE8WGO UC IGF2_HUMAN TTE8WGO SN T3M-11-derived growth factor; Somatomedin-A; Somatomedin A; PP1446; Insulin-like growth factor II; Insulin-like growth factor 2; IGF-II TTE8WGO GN IGF2 TTE8WGO FC Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF-II is influenced by placental lactogen. Also involved in tissue differentiation. Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation. In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver. Acts as a ligand for integrin which is required for IGF2 signaling. The insulin-like growth factors possess growth-promoting activity. TTE8WGO PD 5L3N; 5L3M; 5L3L; 3KR3; 3E4Z TTE8WGO SQ MGIPMGKSMLVLLTFLAFASCCIAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSTPPTVLPDNFPRYPVGKFFQYDTWKQSTQRLRRGLPALLRARRGHVLAKELEAFREAKRHRPLIALPTQDPAHGGAPPEMASNRK TTE8WGO TT Clinical trial TTE8WGO FM Insulin family TTIQSVM ID TTIQSVM TTIQSVM TN Integrin alpha-V/beta-6 (ITGAV/B6) TTIQSVM UP P06756-P18564 TTIQSVM UC ITAV_HUMAN-ITB6_HUMAN TTIQSVM BC Integrin TTIQSVM SN alpha(V)beta(6) integrin; Alpha V beta 6 integrin TTIQSVM GN ITGAV-ITGB6 TTIQSVM FC It is expressed exclusively on subsets of epithelial cells, especially during development, after injury or inflammation, or on many carcinomas. TTIQSVM SQ MGIELLCLFFLFLGRNDHVQGGCALGGAETCEDCLLIGPQCAWCAQENFTHPSGVGERCDTPANLLAKGCQLNFIENPVSQVEILKNKPLSVGRQKNSSDIVQIAPQSLILKLRPGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTVNIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCECGEDMLSTDSCKEAPDHPSCSGRGDCYCGQCICHLSPYGNIYGPYCQCDNFSCVRHKGLLCGGNGDCDCGECVCRSGWTGEYCNCTTSTDSCVSEDGVLCSGRGDCVCGKCVCTNPGASGPTCERCPTCGDPCNSKRSCIECHLSAAGQAREECVDKCKLAGATISEEEDFSKDGSVSCSLQGENECLITFLITTDNEGKTIIHSINEKDCPKPPNIPMIMLGVSLAILLIGVVLLCIWKLLVSFHDRKEVAKFEAERSKAKWQTGTNPLYRGSTSTFKNVTYKHREKQKVDLSTDCMAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET TTIQSVM TT Clinical trial TT9HPX0 ID TT9HPX0 TT9HPX0 TN Interleukin 31 receptor (IL31R) TT9HPX0 UP Q8NI17 TT9HPX0 UC IL31R_HUMAN TT9HPX0 BC Cytokine receptor TT9HPX0 SN hGLM-R; ZcytoR17; UNQ6368/PRO21073/PRO21384; Interleukin-31 receptor subunit alpha; IL-31RA; IL-31R-alpha; IL-31R subunit alpha; IL-31R; IL-31 receptor subunit alpha; Gp130-like receptor; Gp130-like monocyte receptor; GPL; GLM-R; Cytokine receptor-like 3; CRL3 TT9HPX0 GN IL31RA TT9HPX0 FC May function in skin immunity. Mediates IL31-induced itch, probably in a manner dependent on cation channels TRPA1 and TRPV1. Positively regulates numbers and cycling status of immature subsets of myeloid progenitor cells in bone marrow in vivo and enhances myeloid progenitor cell survival in vitro. Associates with OSMR to form the interleukin-31 receptor which activates STAT3 and to a lower extent STAT1 and STAT5. TT9HPX0 SQ MMWTWALWMLPSLCKFSLAALPAKPENISCVYYYRKNLTCTWSPGKETSYTQYTVKRTYAFGEKHDNCTTNSSTSENRASCSFFLPRITIPDNYTIEVEAENGDGVIKSHMTYWRLENIAKTEPPKIFRVKPVLGIKRMIQIEWIKPELAPVSSDLKYTLRFRTVNSTSWMEVNFAKNRKDKNQTYNLTGLQPFTEYVIALRCAVKESKFWSDWSQEKMGMTEEEAPCGLELWRVLKPAEADGRRPVRLLWKKARGAPVLEKTLGYNIWYYPESNTNLTETMNTTNQQLELHLGGESFWVSMISYNSLGKSPVATLRIPAIQEKSFQCIEVMQACVAEDQLVVKWQSSALDVNTWMIEWFPDVDSEPTTLSWESVSQATNWTIQQDKLKPFWCYNISVYPMLHDKVGEPYSIQAYAKEGVPSEGPETKVENIGVKTVTITWKEIPKSERKGIICNYTIFYQAEGGKGFSKTVNSSILQYGLESLKRKTSYIVQVMASTSAGGTNGTSINFKTLSFSVFEIILITSLIGGGLLILIILTVAYGLKKPNKLTHLCWPTVPNPAESSIATWHGDDFKDKLNLKESDDSVNTEDRILKPCSTPSDKLVIDKLVVNFGNVLQEIFTDEARTGQENNLGGEKNGYVTCPFRPDCPLGKSFEELPVSPEIPPRKSQYLRSRMPEGTRPEAKEQLLFSGQSLVPDHLCEEGAPNPYLKNSVTAREFLVSEKLPEHTKGEV TT9HPX0 TT Clinical trial TT1RJXK ID TT1RJXK TT1RJXK TN Interleukin-31 (IL31) TT1RJXK UP Q6EBC2 TT1RJXK UC IL31_HUMAN TT1RJXK BC Cytokine: interleukin TT1RJXK SN Interleukin31; IL-31 TT1RJXK GN IL31 TT1RJXK FC May function in skin immunity. Enhances myeloid progenitor cell survival in vitro. Induces RETNLA and serum amyloid A protein expression in macrophages. Activates STAT3 and possibly STAT1 and STAT5 through the IL31 heterodimeric receptor composed of IL31RA and OSMR. TT1RJXK SQ MASHSGPSTSVLFLFCCLGGWLASHTLPVRLLRPSDDVQKIVEELQSLSKMLLKDVEEEKGVLVSQNYTLPCLSPDAQPPNNIHSPAIRAYLKTIRQLDNKSVIDEIIEHLDKLIFQDAPETNISVPTDTHECKRFILTISQQFSECMDLALKSLTSGAQQATT TT1RJXK TT Clinical trial TTR2TXZ ID TTR2TXZ TTR2TXZ TN Jun N terminal kinase (JNK) TTR2TXZ UP P45983; P45984; P53779 TTR2TXZ UC MK08_HUMAN; MK09_HUMAN; MK10_HUMAN TTR2TXZ BC Kinase TTR2TXZ SN c-Jun N-terminal kinase; Stress-activated protein kinase JNK; SAPK1; PRKM; MAP kinase; JNK TTR2TXZ GN MAPK8; MAPK9; MAPK10 TTR2TXZ FC Associates with scaffold proteins JNK interacting proteins as well as their upstream kinases JNKK1 and JNKK2 following their activation. Modifies the activity of numerous proteins that reside at the mitochondria or act in the nucleus. Downstream molecules that are activated by JNK include c-Jun, ATF2, ELK1, SMAD4, p53 and HSF1. Involved in apoptosis, neurodegeneration, cell differentiation and proliferation, inflammatory conditions and cytokine production mediated by AP-1 (activation protein 1) such as RANTES, IL-8 and GM-CSF. TTR2TXZ SQ MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEERTKNGVIRGQPSPLGAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR TTR2TXZ TT Clinical trial TTFY134 ID TTFY134 TTFY134 TN Keratinocyte growth factor (FGF7) TTFY134 UP P21781 TTFY134 UC FGF7_HUMAN TTFY134 BC Growth factor TTFY134 SN KGF; Heparin-binding growth factor 7; HBGF-7; Fibroblast growth factor 7; FGF-7 TTFY134 GN FGF7 TTFY134 FC Required for normal branching morphogenesis. Growth factor active on keratinocytes. Possible major paracrine effector of normal epithelial cell proliferation. Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. TTFY134 SQ MHKWILTWILPTLLYRSCFHIICLVGTISLACNDMTPEQMATNVNCSSPERHTRSYDYMEGGDIRVRRLFCRTQWYLRIDKRGKVKGTQEMKNNYNIMEIRTVAVGIVAIKGVESEFYLAMNKEGKLYAKKECNEDCNFKELILENHYNTYASAKWTHNGGEMFVALNQKGIPVRGKKTKKEQKTAHFLPMAIT TTFY134 TT Clinical trial TTTI53X ID TTTI53X TTTI53X TN Kruppel like factor 4 (KLF4) TTTI53X UP O43474 TTTI53X UC KLF4_HUMAN TTTI53X SN Krueppellike factor 4; Krueppel-like factor 4; Gutenriched krueppellike factor; Gut-enriched krueppel-like factor; GKLF; Epithelial zinc finger protein EZF; EZF TTTI53X GN KLF4 TTTI53X FC Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription. Transcription factor; can act both as activator and as repressor. TTTI53X SQ MRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRQAGAPNNRWREELSHMKRLPPVLPGRPYDLAAATVATDLESGGAGAACGGSNLAPLPRRETEEFNDLLDLDFILSNSLTHPPESVAATVSSSASASSSSSPSSSGPASAPSTCSFTYPIRAGNDPGVAPGGTGGGLLYGRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLSAPGSEYGSPSVISVSKGSPDGSHPVVVAPYNGGPPRTCPKIKQEAVSSCTHLGAGPPLSNGHRPAAHDFPLGRQLPSRTTPTLGLEEVLSSRDCHPALPLPPGFHPHPGPNYPSFLPDQMQPQVPPLHYQGQSRGFVARAGEPCVCWPHFGTHGMMLTPPSSPLELMPPGSCMPEEPKPKRGRRSWPRKRTATHTCDYAGCGKTYTKSSHLKAHLRTHTGEKPYHCDWDGCGWKFARSDELTRHYRKHTGHRPFQCQKCDRAFSRSDHLALHMKRHF TTTI53X TT Clinical trial TTTI53X KE hsa04550:Signaling pathways regulating pluripotency of stem cells TTTI53X RC R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-452723:Transcriptional regulation of pluripotent stem cells TT2WOUQ ID TT2WOUQ TT2WOUQ TN Laminin beta-3 chain (LAMB3) TT2WOUQ UP Q13751 TT2WOUQ UC LAMB3_HUMAN TT2WOUQ SN Nicein subunit beta; Laminin5beta3; Laminin-5 subunit beta; Laminin subunit beta-3; Laminin B1k chain; Laminin 5 beta 3; LAMNB1; Kalinin subunit beta; Kalinin B1 chain; Epiligrin subunit bata TT2WOUQ GN LAMB3 TT2WOUQ FC Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. TT2WOUQ SQ MRPFFLLCFALPGLLHAQQACSRGACYPPVGDLLVGRTRFLRASSTCGLTKPETYCTQYGEWQMKCCKCDSRQPHNYYSHRVENVASSSGPMRWWQSQNDVNPVSLQLDLDRRFQLQEVMMEFQGPMPAGMLIERSSDFGKTWRVYQYLAADCTSTFPRVRQGRPQSWQDVRCQSLPQRPNARLNGGKVQLNLMDLVSGIPATQSQKIQEVGEITNLRVNFTRLAPVPQRGYHPPSAYYAVSQLRLQGSCFCHGHADRCAPKPGASAGPSTAVQVHDVCVCQHNTAGPNCERCAPFYNNRPWRPAEGQDAHECQRCDCNGHSETCHFDPAVFAASQGAYGGVCDNCRDHTEGKNCERCQLHYFRNRRPGASIQETCISCECDPDGAVPGAPCDPVTGQCVCKEHVQGERCDLCKPGFTGLTYANPQGCHRCDCNILGSRRDMPCDEESGRCLCLPNVVGPKCDQCAPYHWKLASGQGCEPCACDPHNSLSPQCNQFTGQCPCREGFGGLMCSAAAIRQCPDRTYGDVATGCRACDCDFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGYCNRYPVCVACHPCFQTYDADLREQALRFGRLRNATASLWSGPGLEDRGLASRILDAKSKIEQIRAVLSSPAVTEQEVAQVASAILSLRRTLQGLQLDLPLEEETLSLPRDLESLDRSFNGLLTMYQRKREQFEKISSADPSGAFRMLSTAYEQSAQAAQQVSDSSRLLDQLRDSRREAERLVRQAGGGGGTGSPKLVALRLEMSSLPDLTPTFNKLCGNSRQMACTPISCPGELCPQDNGTACGSRCRGVLPRAGGAFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFLTDPDTDAATIQEVSEAVLALWLPTDSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAELKDRLGQSSMLGEQGARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRDHINGRVLYYATCK TT2WOUQ TT Clinical trial TT2WOUQ KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05200:Pathways in cancer; hsa05222:Small cell lung cancer TT2WOUQ RC R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures; R-HSA-2214320:Anchoring fibril formation; R-HSA-3000157:Laminin interactions; R-HSA-3000171:Non-integrin membrane-ECM interactions TTNJKC3 ID TTNJKC3 TTNJKC3 TN Leishmania DNA topoisomerase I (Leishm TOP1) TTNJKC3 UP Q9NJG8 TTNJKC3 UC Q9NJG8_LEIDO TTNJKC3 SN Leishm DNA topoisomerase I; DNA topoisomerase 1 TTNJKC3 GN Leishm TOP1 TTNJKC3 FC Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. TTNJKC3 EC EC 5.6.2.2 TTNJKC3 SQ MPLPGGGTEVLKGITLLTQHHGLKPVQPMSFCYLSFLNRHTHEHHLRLHCCRPHAYARAHPCTCLIDFPLTSYPISQQCAPRLLPLPRQPPLSSQPAEAPSQIGTKDGLLLFRVSNRPQWVFCVCVCVRACPSFPLPRSCDFNRRGAVSPLSSPPRRAPVCCWRFFFHSCSFFFLVLYLLSAPYFCSLWARCANEEDKQNKLRIKQHETKKETPFRVCGGDCPSCCVGLSSHLFFPRWRLLVPPLPYTLDSNNSIFCVFHLFIYFLVCLFVSLAPSTYPFVPLCQLRTLHLYEPRPHIGTPLRCFCCHRDSIRRIMKVENSKMGVKREQSHSNEDEEINEEDLNWWEQENLRIAMKGERRWETLAHNGVLFPPEYEPHGIPIFYDGREFKMTPEEEEVATMFAVMKEHDYYRMEVFRRNFFESWREILDKRQHPIRRLELCDFEPIYQWHLVQREKKLSRTKEEKKAIKEKQDAEAEPYRYCVWDGRREQVANFRVEPPGLFRGRGKHPLMGKLKVRVQPEDITINIGETAEVPVPPAGHKWAAVQHDHTVTWLAMWRDSVAGNMKYVMLAPSSSVKGQSDMVKFEKARKLKDKVDDIRASYMEDFKSNDLHVAQRAVAMYIDRLALRVGNEKGEDEADTVGCCSLRVEHIQLMPDNIVRFDFLGKDSIRYQNDVAVLPEVYALLQRFTRRKSPGMDIFDQLNPTQLNDHLKSFMDGLSAKVFRTYNASITLDRWFKEKPVDPKWSTADKLAYFNKANTEVAILCNHQKSVSKNFKLQMMQLTTKSEYTRKTIELLEKAEVTAKKKSVEEAAKEFLEEQDRMQREWLESYGTEEQKKEFEEIVAKRAAPRVRSEKKKSTSGAKKAESASGKKRAAKKKKSAKKGGKMLSKKAASKSSKKAPKKLKEEDEDDVPLVSVAAKTKKTAGVKRQRANKVVSDDDDVPLAALRV TTNJKC3 TT Clinical trial TTNVXAW ID TTNVXAW TTNVXAW TN Lymphocyte activation gene 3 protein (LAG3) TTNVXAW UP P18627 TTNVXAW UC LAG3_HUMAN TTNVXAW BC Immunoglobulin TTNVXAW SN Protein FDC; LAG-3; FDC; CD223 TTNVXAW GN LAG3 TTNVXAW FC Delivers inhibitory signals upon binding to ligands, such as FGL1. FGL1 constitutes a major ligand of LAG3 and is responsible for LAG3 T-cell inhibitory function. Following TCR engagement, LAG3 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation. May inhibit antigen-specific T-cell activation in synergy with PDCD1/PD-1, possibly by acting as a coreceptor for PDCD1/PD-1. Negatively regulates the proliferation, activation, effector function and homeostasis of both CD8(+) and CD4(+) T-cells. Also mediates immune tolerance: constitutively expressed on a subset of regulatory T-cells (Tregs) and contributes to their suppressive function. Also acts as a negative regulator of plasmacytoid dendritic cell (pDCs) activation. Binds MHC class II (MHC-II); the precise role of MHC-II-binding is however unclear. Lymphocyte activation gene 3 protein: Inhibitory receptor on antigen activated T-cells. TTNVXAW SQ MWEAQFLGLLFLQPLWVAPVKPLQPGAEVPVVWAQEGAPAQLPCSPTIPLQDLSLLRRAGVTWQHQPDSGPPAAAPGHPLAPGPHPAAPSSWGPRPRRYTVLSVGPGGLRSGRLPLQPRVQLDERGRQRGDFSLWLRPARRADAGEYRAAVHLRDRALSCRLRLRLGQASMTASPPGSLRASDWVILNCSFSRPDRPASVHWFRNRGQGRVPVRESPHHHLAESFLFLPQVSPMDSGPWGCILTYRDGFNVSIMYNLTVLGLEPPTPLTVYAGAGSRVGLPCRLPAGVGTRSFLTAKWTPPGGGPDLLVTGDNGDFTLRLEDVSQAQAGTYTCHIHLQEQQLNATVTLAIITVTPKSFGSPGSLGKLLCEVTPVSGQERFVWSSLDTPSQRSFSGPWLEAQEAQLLSQPWQCQLYQGERLLGAAVYFTELSSPGAQRSGRAPGALPAGHLLLFLILGVLSLLLLVTGAFGFHLWRRQWRPRRFSALEQGIHPPQAQSKIEELEQEPEPEPEPEPEPEPEPEPEQL TTNVXAW TT Clinical trial TTNVXAW FM Immunoglobulin superfamily TTU2O6T ID TTU2O6T TTU2O6T TN Metastasis-suppressor KiSS-1 (KISS1) TTU2O6T UP Q15726 TTU2O6T UC KISS1_HUMAN TTU2O6T SN KiSS-1; KISS1 TTU2O6T GN KISS1 TTU2O6T FC Metastasis suppressor protein in malignant melanomas and in some breast cancers. May regulate events downstream of cell- matrix adhesion, perhaps involving cytoskeletal reorganization. Generates a C-terminally amidated peptide, metastin which functions as the endogenous ligand of the G-protein coupled receptor GPR54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. Kp-10 is a decapeptide derived from the primary translation product, isolated in conditioned medium of first trimester trophoblast. Kp-10, but not other kisspeptins, increased intracellular Ca(2+) levels in isolated first trimester trophoblasts. Kp-10 is a paracrine/endocrine regulator in fine- tuning trophoblast invasion generated by the trophoblast itself. The receptor is also essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/GPR54 system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. TTU2O6T SQ MNSLVSWQLLLFLCATHFGEPLEKVASVGNSRPTGQQLESLGLLAPGEQSLPCTERKPAATARLSRRGTSLSPPPESSGSPQQPGLSAPHSRQIPAPQGAVLVQREKDLPNYNWNSFGLRFGKREAAPGNHGRSAGRG TTU2O6T TT Clinical trial TTVWAGF ID TTVWAGF TTVWAGF TN MHC class I NK cell receptor 2DS1 (CD158h) TTVWAGF UP Q14954 TTVWAGF UC KI2S1_HUMAN TTVWAGF BC Immunoglobulin TTVWAGF SN MHC class I NK cell receptor Eb6 ActI; Killer cell immunoglobulin-like receptor 2DS1; CD158h; CD158 antigen-like family member H TTVWAGF GN KIR2DS1 TTVWAGF FC Receptor on natural killer (NK) cells for some HLA-C alleles such as w6. Does not inhibit the activity of NK cells. TTVWAGF SQ MSLTVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGRLVKSEETVILQCWSDVMFEHFLLHREGMFNDTLRLIGEHHDGVSKANFSISRMKQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVIIGLYEKPSLSAQPGPTVLAGENVTLSCSSRSSYDMYHLSREGEAHERRLPAGTKVNGTFQANFPLGPATHGGTYRCFGSFRDSPYEWSKSSDPLLVSVTGNPSNSWPSPTEPSSETGNPRHLHVLIGTSVVKIPFTILLFFLLHRWCSDKKNAAVMDQEPAGNRTVNSEDSDEQDHQEVSYA TTVWAGF TT Clinical trial TTQH3N0 ID TTQH3N0 TTQH3N0 TN MHC class I NK cell receptor 3DL2 (CD158k) TTQH3N0 UP P43630 TTQH3N0 UC KI3L2_HUMAN TTQH3N0 BC Immunoglobulin TTQH3N0 SN p70 natural killer cell receptor clone CL5; p70 NK receptor CL5; Natural killerassociated transcript 4; NKAT4; KIR3DL2; CD158k; CD158 antigenlike family member K TTQH3N0 GN KIR3DL2 TTQH3N0 FC Receptor on natural killer (NK) cells for HLA-A alleles. Inhibits the activity of NK cells thus preventing cell lysis. TTQH3N0 SQ MSLTVVSMACVGFFLLQGAWPLMGGQDKPFLSARPSTVVPRGGHVALQCHYRRGFNNFMLYKEDRSHVPIFHGRIFQESFIMGPVTPAHAGTYRCRGSRPHSLTGWSAPSNPLVIMVTGNHRKPSLLAHPGPLLKSGETVILQCWSDVMFEHFFLHREGISEDPSRLVGQIHDGVSKANFSIGPLMPVLAGTYRCYGSVPHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVQAGENVTLSCSSWSSYDIYHLSREGEAHERRLRAVPKVNRTFQADFPLGPATHGGTYRCFGSFRALPCVWSNSSDPLLVSVTGNPSSSWPSPTEPSSKSGICRHLHVLIGTSVVIFLFILLLFFLLYRWCSNKKNAAVMDQEPAGDRTVNRQDSDEQDPQEVTYAQLDHCVFIQRKISRPSQRPKTPLTDTSVYTELPNAEPRSKVVSCPRAPQSGLEGVF TTQH3N0 TT Clinical trial TTRU1NG ID TTRU1NG TTRU1NG TN Mitochondrial complex I (NDUFA13) TTRU1NG UP Q9P0J0 TTRU1NG UC NDUAD_HUMAN TTRU1NG SN NADH-ubiquinone oxidoreductase B16.6 subunit; NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13; Gene associated with retinoic and interferon-induced mortality 19 protein; Gene associated with retinoic and IFN-induced mortality 19 protein; GRIM19; GRIM-19; Complex I-B16.6; Cell death regulatory protein GRIM-19; CI-B16.6; CGI-39; CDA016 TTRU1NG GN NDUFA13 TTRU1NG FC Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. TTRU1NG PD 5XTI; 5XTH; 5XTD; 5XTC; 5XTB TTRU1NG SQ MAASKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMLAIGIGTLIYGHWSIMKWNRERRRLQIEDFEARIALLPLLQAETDRRTLQMLRENLEEEAIIMKDVPDWKVGESVFHTTRWVPPLIGELYGLRTTEEALHASHGFMWYT TTRU1NG TT Clinical trial TTRHMTC ID TTRHMTC TTRHMTC TN Mutated KRAS (mKRAS) TTRHMTC UP P01116 (mutated) TTRHMTC UC RASK_HUMAN TTRHMTC SN c-Ki-ras (mutated); c-K-ras (mutated); RASK2 (mutated); Ki-Ras (mutated); KRAS2 (mutated); K-Ras 2 (mutated); GTPase KRas (mutated) TTRHMTC GN KRAS TTRHMTC FC Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the regulation of cell proliferation. Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner. TTRHMTC PD 6N2K; 6N2J; 6H47; 6H46; 6GQY TTRHMTC SQ MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM TTRHMTC TT Clinical trial TTM8I2X ID TTM8I2X TTM8I2X TN Myostatin (MSTN) TTM8I2X UP O14793 TTM8I2X UC GDF8_HUMAN TTM8I2X SN GDF-8 TTM8I2X GN MSTN TTM8I2X FC Acts specifically as a negative regulator of skeletal muscle growth. TTM8I2X PD 5NXS; 5NTU; 5F3H; 5F3B TTM8I2X SQ MQKLQLCVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS TTM8I2X TT Clinical trial TTHRM39 ID TTHRM39 TTHRM39 TN Myristoylated alanine-rich C-kinase substrate (MARCKS) TTHRM39 UP P29966 TTHRM39 UC MARCS_HUMAN TTHRM39 SN Protein kinase C substrate, 80 kDa protein, light chain; PRKCSL; PKCSL; Myristoylated alaninerich Ckinase substrate; MACS; 80KL protein; 80K-L protein TTHRM39 GN MARCKS TTHRM39 FC MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein. TTHRM39 SQ MGAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAESGAKEELQANGSAPAADKEEPAAAGSGAASPSAAEKGEPAAAAAPEAGASPVEKEAPAEGEAAEPGSPTAAEGEAASAASSTSSPKAEDGATPSPSNETPKKKKKRFSFKKSFKLSGFSFKKNKKEAGEGGEAEAPAAEGGKDEAAGGAAAAAAEAGAASGEQAAAPGEEAAAGEEGAAGGDPQEAKPQEAAVAPEKPPASDETKAAEEPSKVEEKKAEEAGASAAACEAPSAAGPGAPPEQEAAPAEEPAAAAASSACAAPSQEAQPECSPEAPPAEAAE TTHRM39 TT Clinical trial TTMA3VF ID TTMA3VF TTMA3VF TN NCK adaptor protein 1 (NCK1) TTMA3VF UP P16333 TTMA3VF UC NCK1_HUMAN TTMA3VF SN SH2/SH3 adaptor protein NCKalpha; SH2/SH3 adaptor protein NCK-alpha; Nck1; Nck-1; NCK; Cytoplasmic protein NCK1 TTMA3VF GN NCK1 TTMA3VF FC Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA. May play a role in cell adhesion and migration through interaction with ephrin receptors. Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. TTMA3VF PD 2JW4; 2JS2; 2JS0; 2CUB; 2CI9 TTMA3VF SQ MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLGIGKVKRKPSVPDSASPADDSFVDPGERLYDLNMPAYVKFNYMAEREDELSLIKGTKVIVMEKCSDGWWRGSYNGQVGWFPSNYVTEEGDSPLGDHVGSLSEKLAAVVNNLNTGQVLHVVQALYPFSSSNDEELNFEKGDVMDVIEKPENDPEWWKCRKINGMVGLVPKNYVTVMQNNPLTSGLEPSPPQCDYIRPSLTGKFAGNPWYYGKVTRHQAEMALNERGHEGDFLIRDSESSPNDFSVSLKAQGKNKHFKVQLKETVYCIGQRKFSTMEELVEHYKKAPIFTSEQGEKLYLVKHLS TTMA3VF TT Clinical trial TTLRN4A ID TTLRN4A TTLRN4A TN NKG2 D activating NK receptor (KLRK1) TTLRN4A UP P26718 TTLRN4A UC NKG2D_HUMAN TTLRN4A SN NKG2Dactivating NK receptor; NKG2D type II integral membrane protein; NKG2D; NKG2-D-activating NK receptor; NKG2-D type II integral membrane protein; NK cell receptor D; Killer cell lectinlike receptor subfamily K member 1; Killer cell lectin-like receptor subfamily K member 1; D12S2489E; CD314 TTLRN4A GN KLRK1 TTLRN4A FC Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including MICA, MICB, RAET1E, RAET1G, RAET1L/ULBP6, ULBP1, ULBP2, ULBP3 (ULBP2>ULBP1>ULBP3) and ULBP4. Function as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. TTLRN4A PD 4S0U; 4PDC; 1MPU; 1KCG; 1HYR TTLRN4A SQ MGWIRGRRSRHSWEMSEFHNYNLDLKKSDFSTRWQKQRCPVVKSKCRENASPFFFCCFIAVAMGIRFIIMVAIWSAVFLNSLFNQEVQIPLTESYCGPCPKNWICYKNNCYQFFDESKNWYESQASCMSQNASLLKVYSKEDQDLLKLVKSYHWMGLVHIPTNGSWQWEDGSILSPNLLTIIEMQKGDCALYASSFKGYIENCSTPNTYICMQRTV TTLRN4A TT Clinical trial TT6A5ZL ID TT6A5ZL TT6A5ZL TN Nucleobindin-1 (NUCB1) TT6A5ZL UP Q02818 TT6A5ZL UC NUCB1_HUMAN TT6A5ZL SN NUC; CALNUC TT6A5ZL GN NUCB1 TT6A5ZL FC Major calcium-binding protein of the Golgi. May have a role in calcium homeostasis (By similarity). TT6A5ZL PD 1SNL TT6A5ZL SQ MPPSGPRGTLLLLPLLLLLLLRAVLAVPLERGAPNKEETPATESPDTGLYYHRYLQEVIDVLETDGHFREKLQAANAEDIKSGKLSRELDFVSHHVRTKLDELKRQEVSRLRMLLKAKMDAEQDPNVQVDHLNLLKQFEHLDPQNQHTFEARDLELLIQTATRDLAQYDAAHHEEFKRYEMLKEHERRRYLESLGEEQRKEAERKLEEQQRRHREHPKVNVPGSQAQLKEVWEELDGLDPNRFNPKTFFILHDINSDGVLDEQELEALFTKELEKVYDPKNEEDDMREMEEERLRMREHVMKNVDTNQDRLVTLEEFLASTQRKEFGDTGEGWETVEMHPAYTEEELRRFEEELAAREAELNAKAQRLSQETEALGRSQGRLEAQKRELQQAVLHMEQRKQQQQQQQGHKAPAAHPEGQLKFHPDTDDVPVPAPAGDQKEVDTSEKKLLERLPEVEVPQHL TT6A5ZL TT Literature-reported TT6IEYX ID TT6IEYX TT6IEYX TN Opioid receptor zeta (OGFR) TT6IEYX UP Q9NZT2 TT6IEYX UC OGFR_HUMAN TT6IEYX BC GPCR rhodopsin TT6IEYX SN Zetatype opioid receptor; Zeta-type opioid receptor; Protein 760; Protein 7-60; Opioid growth factor receptor; OGFr TT6IEYX GN OGFR TT6IEYX FC Seems to be involved in growth regulation. Receptor for opioid growth factor (OGF), also known as Met-enkephalin. TT6IEYX SQ MDDPDCDSTWEEDEEDAEDAEDEDCEDGEAAGARDADAGDEDEESEEPRAARPSSFQSRMTGSRNWRATRDMCRYRHNYPDLVERDCNGDTPNLSFYRNEIRFLPNGCFIEDILQNWTDNYDLLEDNHSYIQWLFPLREPGVNWHAKPLTLREVEVFKSSQEIQERLVRAYELMLGFYGIRLEDRGTGTVGRAQNYQKRFQNLNWRSHNNLRITRILKSLGELGLEHFQAPLVRFFLEETLVRRELPGVRQSALDYFMFAVRCRHQRRQLVHFAWEHFRPRCKFVWGPQDKLRRFKPSSLPHPLEGSRKVEEEGSPGDPDHEASTQGRTCGPEHSKGGGRVDEGPQPRSVEPQDAGPLERSQGDEAGGHGEDRPEPLSPKESKKRKLELSRREQPPTEPGPQSASEVEKIALNLEGCALSQGSLRTGTQEVGGQDPGEAVQPCRQPLGARVADKVRKRRKVDEGAGDSAAVASGGAQTLALAGSPAPSGHPKAGHSENGVEEDTEGRTGPKEGTPGSPSETPGPSPAGPAGDEPAESPSETPGPRPAGPAGDEPAESPSETPGPRPAGPAGDEPAESPSETPGPSPAGPTRDEPAESPSETPGPRPAGPAGDEPAESPSETPGPRPAGPAGDEPAESPSETPGPSPAGPTRDEPAKAGEAAELQDAEVESSAKSGKP TT6IEYX TT Clinical trial TT5OREU ID TT5OREU TT5OREU TN PACAP type I receptor (PAC1R) TT5OREU UP P41586 TT5OREU UC PACR_HUMAN TT5OREU SN Pituitary adenylate cyclase-activating polypeptide type I receptor; PACAP-R1; PACAP-R-1 TT5OREU GN ADCYAP1R1 TT5OREU FC This is a receptor for PACAP-27 and PACAP-38. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. May regulate the release of adrenocorticotropin, luteinizing hormone, growth hormone, prolactin, epinephrine, and catecholamine. May play a role in spermatogenesis and sperm motility. Causes smooth muscle relaxation and secretion in the gastrointestinal tract. TT5OREU PD 3N94; 2JOD TT5OREU SQ MAGVVHVSLAALLLLPMAPAMHSDCIFKKEQAMCLEKIQRANELMGFNDSSPGCPGMWDNITCWKPAHVGEMVLVSCPELFRIFNPDQVWETETIGESDFGDSNSLDLSDMGVVSRNCTEDGWSEPFPHYFDACGFDEYESETGDQDYYYLSVKALYTVGYSTSLVTLTTAMVILCRFRKLHCTRNFIHMNLFVSFMLRAISVFIKDWILYAEQDSNHCFISTVECKAVMVFFHYCVVSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTVCVTVWATLRLYFDDTGCWDMNDSTALWWVIKGPVVGSIMVNFVLFIGIIVILVQKLQSPDMGGNESSIYLRLARSTLLLIPLFGIHYTVFAFSPENVSKRERLVFELGLGSFQGFVVAVLYCFLNGEVQAEIKRKWRSWKVNRYFAVDFKHRHPSLASSGVNGGTQLSILSKSSSQIRMSGLPADNLAT TT5OREU TT Clinical trial TTYPUHA ID TTYPUHA TTYPUHA TN Pattern recognition receptor NOD2 (NOD2) TTYPUHA UP Q9HC29 TTYPUHA UC NOD2_HUMAN TTYPUHA SN Nucleotidebinding oligomerization domaincontaining protein 2; Nucleotide-binding oligomerization domain-containing protein 2; Inflammatory bowel disease protein 1; IBD1; Caspase recruitment domaincontaining protein 15; Caspase recruitment domain-containing protein 15; CARD15 TTYPUHA GN NOD2 TTYPUHA FC Upon stimulation by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, binds the proximal adapter receptor-interacting RIPK2, which recruits ubiquitin ligases as XIAP, BIRC2, BIRC3, INAVA and the LUBAC complex, triggering activation of MAP kinases and activation of NF-kappa-B signaling. This in turn leads to the transcriptional activation of hundreds of genes involved in immune response. Required for MDP-induced NLRP1-dependent CASP1 activation and IL1B release in macrophages. Component of an autophagy-mediated antibacterial pathway together with ATG16L1. Plays also a role in sensing single-stranded RNA (ssRNA) from viruses. Interacts with mitochondrial antiviral signaling/MAVS, leading to activation of interferon regulatory factor-3/IRF3 and expression of type I interferon. Involved in gastrointestinal immunity. TTYPUHA SQ MGEEGGSASHDEEERASVLLGHSPGCEMCSQEAFQAQRSQLVELLVSGSLEGFESVLDWLLSWEVLSWEDYEGFHLLGQPLSHLARRLLDTVWNKGTWACQKLIAAAQEAQADSQSPKLHGCWDPHSLHPARDLQSHRPAIVRRLHSHVENMLDLAWERGFVSQYECDEIRLPIFTPSQRARRLLDLATVKANGLAAFLLQHVQELPVPLALPLEAATCKKYMAKLRTTVSAQSRFLSTYDGAETLCLEDIYTENVLEVWADVGMAGPPQKSPATLGLEELFSTPGHLNDDADTVLVVGEAGSGKSTLLQRLHLLWAAGQDFQEFLFVFPFSCRQLQCMAKPLSVRTLLFEHCCWPDVGQEDIFQLLLDHPDRVLLTFDGFDEFKFRFTDRERHCSPTDPTSVQTLLFNLLQGNLLKNARKVVTSRPAAVSAFLRKYIRTEFNLKGFSEQGIELYLRKRHHEPGVADRLIRLLQETSALHGLCHLPVFSWMVSKCHQELLLQEGGSPKTTTDMYLLILQHFLLHATPPDSASQGLGPSLLRGRLPTLLHLGRLALWGLGMCCYVFSAQQLQAAQVSPDDISLGFLVRAKGVVPGSTAPLEFLHITFQCFFAAFYLALSADVPPALLRHLFNCGRPGNSPMARLLPTMCIQASEGKDSSVAALLQKAEPHNLQITAAFLAGLLSREHWGLLAECQTSEKALLRRQACARWCLARSLRKHFHSIPPAAPGEAKSVHAMPGFIWLIRSLYEMQEERLARKAARGLNVGHLKLTFCSVGPTECAALAFVLQHLRRPVALQLDYNSVGDIGVEQLLPCLGVCKALYLRDNNISDRGICKLIECALHCEQLQKLALFNNKLTDGCAHSMAKLLACRQNFLALRLGNNYITAAGAQVLAEGLRGNTSLQFLGFWGNRVGDEGAQALAEALGDHQSLRWLSLVGNNIGSVGAQALALMLAKNVMLEELCLEENHLQDEGVCSLAEGLKKNSSLKILKLSNNCITYLGAEALLQALERNDTILEVWLRGNTFSLEEVDKLGCRDTRLLL TTYPUHA TT Clinical trial TTYPUHA KE hsa04621:NOD-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa05131:Shigellosis; hsa05152:Tuberculosis; hsa05321:Inflammatory bowel disease (IBD) TTYPUHA RC R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-446652:Interleukin-1 signaling; R-HSA-450302:activated TAK1 mediates p38 MAPK activation; R-HSA-450321:JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 TT2MN5K ID TT2MN5K TT2MN5K TN Phosphorylated protein kinase B (pAKT) TT2MN5K UP P31749; P31751; Q9Y243 TT2MN5K UC AKT1_HUMAN; AKT2_HUMAN; AKT3_HUMAN TT2MN5K BC Kinase TT2MN5K SN RAC-serine/threonine-protein kinase; RAC-PK; Protein kinase B; Protein kinase Akt; PKB TT2MN5K GN AKT1; AKT2; AKT3 TT2MN5K FC AKT kinases are 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3), and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53. TT2MN5K SQ MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA TT2MN5K TT Clinical trial TT5QA2I ID TT5QA2I TT5QA2I TN Plasminogen activator inhibitor (PAI) TT5QA2I UP P05121; P05120; P05154 TT5QA2I UC PAI1_HUMAN; PAI2_HUMAN; IPSP_HUMAN TT5QA2I SN Serpin; PAI TT5QA2I GN SERPINE1; SERPINB2; SERPINA5 TT5QA2I FC Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation offibrinolysis. TT5QA2I SQ MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP TT5QA2I TT Clinical trial TT5QA2I KE hsa04066:HIF-1 signaling pathway; hsa04115:p53 signaling pathway; hsa04390:Hippo signaling pathway; hsa04610:Complement and coagulation cascades; hsa05142:Chagas disease (American trypanosomiasis) TTG45NU ID TTG45NU TTG45NU TN Plasmodium Elongation factor 1-alpha 1 (Malaria MEF-1) TTG45NU UP Q00080 TTG45NU UC EF1A_PLAFK TTG45NU BC Acid anhydrides hydrolase TTG45NU SN MEF-1; Elongation factor Tu of Plasmodium falciparum; Elongation factor 1 A-1; EF-Tu; EF-1-alpha-1 of Plasmodium falciparum; EEF1A-1 TTG45NU GN Malaria MEF-1 TTG45NU FC This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. TTG45NU SQ MGKEKTHINLVVIGHVDSGKSTTTGHIIYKLGGIDRRTIEKFEKESAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFFTVIDAPGHKDFIKNMITGTSQADVALLVVPADVGGFDGAFSKEGQTKEHVLLAFTLGVKQIVVGVNKMDTVKYSEDRYEEIKKEVKDYLKKVGYQADKVDFIPISGFEGDNLIEKSDKTPWYKGRTLIEALDTMQPPKRPYDKPLRIPLQGVYKIGGIGTVPVGRVETGILKAGMVLNFAPSAVVSECKSVEMHKEVLEEARPGDNIGFNVKNVSVKEIKRGYVASDTKNEPAKGCSKFTAQVIILNHPGEIKNGYTPLLDCHTSHISCKFLNIDSKIDKRSGKVVEENPKAIKSGDSALVSLEPKKPMVVETFTEYPPLGRFAIRDMRQTIAVGIINQLKRKNLGAVTAKAPAKK TTG45NU TT Clinical trial TTDUK07 ID TTDUK07 TTDUK07 TN Plasmodium Thrombospondin relate anonymous protein (Plasm TRAP) TTDUK07 UP P16893 TTDUK07 UC TRAP_PLAFA TTDUK07 SN Thrombospondin-related anonymous protein TTDUK07 GN Plasm TRAP TTDUK07 FC A type 1 membrane protein that possesses multiple adhesive domains in its extracellular region. Essential for sporozoite motility and for liver cell invasion. TTDUK07 PD 2BBX TTDUK07 SQ MNHLGNVKYLVIVFLIFFDLFLVNGRDVQNNIVDEIKYSEEVCNDQVDLYLLMDCSGSIRRHNWVNHAVPLAMKLIQQLNLNDNAIHLYVNVFSNNAKEIIRLHSDASKNKEKALIIIRSLLSTNLPYGRTNLTDALLQVRKHLNDRINRENANQLVVILTDGIPDSIQDSLKESRKLSDRGVKIAVFGIGQGINVAFNRFLVGCHPSDGKCNLYADSAWENVKNVIGPFMKAVCVEVEKTASCGVWDEWSPCSVTCGKGTRSRKREILHEGCTSEIQEQCEEERCPPKWEPLDVPDEPEDDQPRPRGDNSSVQKPEENIIDNNPQEPSPNPEEGKDENPNGFDLDENPENPPNPDIPEQKPNIPEDSEKEVPSDVPKNPEDDREENFDIPKKPENKHDNQNNLPNDKSDRNIPYSPLPPKVLDNERKQSDPQSQDNNGNRHVPNSEDRETRPHGRNNENRSYNRKYNDTPKHPEREEHEKPDNNKKKGESDNKYKIAGGIAGGLALLACAGLAYKFVVPGAATPYAGEPAPFDETLGEEDKDLDEPEQFRLPEENEWN TTDUK07 TT Clinical trial TTYOVWN ID TTYOVWN TTYOVWN TN Programmed cell death protein 2 (PD-2) TTYOVWN UP Q16342 TTYOVWN UC PDCD2_HUMAN TTYOVWN SN Zinc finger protein Rp8; Zinc finger protein Rp-8; Zinc finger MYND domaincontaining protein 7; Zinc finger MYND domain-containing protein 7; ZMYND7; RP8 TTYOVWN GN PDCD2 TTYOVWN FC May play an important role in cell death and/or in regulation of cell proliferation. May be a DNA-binding protein with a regulatory function. TTYOVWN SQ MAAAGARPVELGFAESAPAWRLRSEQFPSKVGGRPAWLGAAGLPGPQALACELCGRPLSFLLQVYAPLPGRPDAFHRCIFLFCCREQPCCAGLRVFRNQLPRKNDFYSYEPPSENPPPETGESVCLQLKSGAHLCRVCGCLGPKTCSRCHKAYYCSKEHQTLDWRLGHKQACAQPDHLDHIIPDHNFLFPEFEIVIETEDEIMPEVVEKEDYSEIIGSMGEALEEELDSMAKHESREDKIFQKFKTQIALEPEQILRYGRGIAPIWISGENIPQEKDIPDCPCGAKRILEFQVMPQLLNYLKADRLGKSIDWGILAVFTCAESCSLGTGYTEEFVWKQDVTDTP TTYOVWN TT Clinical trial TTYOVWN FM MYND-type zinc finger TTXMZ81 ID TTXMZ81 TTXMZ81 TN Prominin-1 (PROM1) TTXMZ81 UP O43490 TTXMZ81 UC PROM1_HUMAN TTXMZ81 SN Promininlike protein 1; Prominin1; Prominin-like protein 1; PROML1; MSTP061; CD133; Antigen AC133 TTXMZ81 GN PROM1 TTXMZ81 FC Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner. May play a role in cell differentiation, proliferation and apoptosis. TTXMZ81 SQ MALVLGSLLLLGLCGNSFSGGQPSSTDAPKAWNYELPATNYETQDSHKAGPIGILFELVHIFLYVVQPRDFPEDTLRKFLQKAYESKIDYDKPETVILGLKIVYYEAGIILCCVLGLLFIILMPLVGYFFCMCRCCNKCGGEMHQRQKENGPFLRKCFAISLLVICIIISIGIFYGFVANHQVRTRIKRSRKLADSNFKDLRTLLNETPEQIKYILAQYNTTKDKAFTDLNSINSVLGGGILDRLRPNIIPVLDEIKSMATAIKETKEALENMNSTLKSLHQQSTQLSSSLTSVKTSLRSSLNDPLCLVHPSSETCNSIRLSLSQLNSNPELRQLPPVDAELDNVNNVLRTDLDGLVQQGYQSLNDIPDRVQRQTTTVVAGIKRVLNSIGSDIDNVTQRLPIQDILSAFSVYVNNTESYIHRNLPTLEEYDSYWWLGGLVICSLLTLIVIFYYLGLLCGVCGYDRHATPTTRGCVSNTGGVFLMVGVGLSFLFCWILMIIVVLTFVFGANVEKLICEPYTSKELFRVLDTPYLLNEDWEYYLSGKLFNKSKMKLTFEQVYSDCKKNRGTYGTLHLQNSFNISEHLNINEHTGSISSELESLKVNLNIFLLGAAGRKNLQDFAACGIDRMNYDSYLAQTGKSPAGVNLLSFAYDLEAKANSLPPGNLRNSLKRDAQTIKTIHQQRVLPIEQSLSTLYQSVKILQRTGNGLLERVTRILASLDFAQNFITNNTSSVIIEETKKYGRTIIGYFEHYLQWIEFSISEKVASCKPVATALDTAVDVFLCSYIIDPLNLFWFGIGKATVFLLPALIFAVKLAKYYRRMDSEDVYDDVETIPMKNMENGNNGYHKDHVYGIHNPVMTSPSQH TTXMZ81 TT Clinical trial TTXMZ81 FM Prominin TTXMZ81 KE hsa05202:Transcriptional misregulation in cancer TTDKGTC ID TTDKGTC TTDKGTC TN Protein cereblon (CRBN) TTDKGTC UP Q96SW2 TTDKGTC UC CRBN_HUMAN TTDKGTC SN Protein cereblon TTDKGTC GN CRBN TTDKGTC FC Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8. May play a role in memory and learning by regulating the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1. Binding of pomalidomide and other thalidomide-related drugs changes the substrate specificity of the human protein, leading to decreased degradation of MEIS2 and other target proteins and increased degradation of MYC, IRF4, IKZF1 and IKZF3. TTDKGTC PD 6H0G; 6H0F; 6BOY; 6BNB; 6BN9 TTDKGTC SQ MAGEGDQQDAAHNMGNHLPLLPAESEEEDEMEVEDQDSKEAKKPNIINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL TTDKGTC TT Clinical trial TTW3P4R ID TTW3P4R TTW3P4R TN Protein kinase N3 (PKN3) TTW3P4R UP Q6P5Z2 TTW3P4R UC PKN3_HUMAN TTW3P4R SN Serine/threonine-protein kinase N3; Protein-kinase C-related kinase 3; Protein kinase PKN-beta; PKNBETA TTW3P4R GN PKN3 TTW3P4R FC Contributes to invasiveness in malignant prostate cancer. TTW3P4R EC EC 2.7.11.13 TTW3P4R SQ MEEGAPRQPGPSQWPPEDEKEVIRRAIQKELKIKEGVENLRRVATDRRHLGHVQQLLRSSNRRLEQLHGELRELHARILLPGPGPGPAEPVASGPRPWAEQLRARHLEALRRQLHVELKVKQGAENMTHTCASGTPKERKLLAAAQQMLRDSQLKVALLRMKISSLEASGSPEPGPELLAEELQHRLHVEAAVAEGAKNVVKLLSSRRTQDRKALAEAQAQLQESSQKLDLLRLALEQLLEQLPPAHPLRSRVTRELRAAVPGYPQPSGTPVKPTALTGTLQVRLLGCEQLLTAVPGRSPAAALASSPSEGWLRTKAKHQRGRGELASEVLAVLKVDNRVVGQTGWGQVAEQSWDQTFVIPLERARELEIGVHWRDWRQLCGVAFLRLEDFLDNACHQLSLSLVPQGLLFAQVTFCDPVIERRPRLQRQERIFSKRRGQDFLRASQMNLGMAAWGRLVMNLLPPCSSPSTISPPKGCPRTPTTLREASDPATPSNFLPKKTPLGEEMTPPPKPPRLYLPQEPTSEETPRTKRPHMEPRTRRGPSPPASPTRKPPRLQDFRCLAVLGRGHFGKVLLVQFKGTGKYYAIKALKKQEVLSRDEIESLYCEKRILEAVGCTGHPFLLSLLACFQTSSHACFVTEFVPGGDLMMQIHEDVFPEPQARFYVACVVLGLQFLHEKKIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEEEVFDCIVNMDAPYPGFLSVQGLEFIQKLLQKCPEKRLGAGEQDAEEIKVQPFFRTTNWQALLARTIQPPFVPTLCGPADLRYFEGEFTGLPPALTPPAPHSLLTARQQAAFRDFDFVSERFLEP TTW3P4R TT Clinical trial TTTPDRC ID TTTPDRC TTTPDRC TN Pseudomonas Psl exopolysaccharide (Pseudo pslG) TTTPDRC UP Q9I1N2 TTTPDRC UC Q9I1N2_PSEAE TTTPDRC SN PslG TTTPDRC GN Pseudo pslG TTTPDRC FC A extracellular matrix component of P. aeruginosa biofilms. A galactose-rich and mannose-rich exopolysaccharide. TTTPDRC PD 5BXA; 5BX9; 4ZN2 TTTPDRC SQ MARKGLYLGGSALLLAVVLLLVFWGRPADAEIQVLKAPRAVVWKDFLGVNAQFLWFSPERYNKQIDRLQDLGLEWVRLDLHWDRLETAEDQYQLASLDQLVKDLEARQLKSVFYLVGSARFITTAPFYSPFQDQYPPRDPEVFARRMAMLSQRYPSVAAWQVWNEPNLIGFWRPKADPEGYAKLLQASTIALRMVDPEKPVVSAGMAFFSEMPDGRTMFDALGHLGVESLGTIATYHPYTQLPEGNYPWNLDFVSHANQINRALRNAGVPAIWSTEWGWSAYKGPKELQDIIGVEGQADYVLRRLALMSALDYDRIFLFTLSDLDQRASVRDRDYGLLDLDANPKPVYLALQRFLKVTGPKLRPADPPVTEDLPDGSFSIGWTREDGRNVWLFWSARGGNVRLPKLKEATLHDPLSGKVTPLSGSDGLEVPVKSSLQMLVWE TTTPDRC TT Clinical trial TT8R3VP ID TT8R3VP TT8R3VP TN Rhinovirus Capsid protein (HRV VP) TT8R3VP UP P23008 (2-857) TT8R3VP UC POLG_HRV1A TT8R3VP SN Rhinovirus Virion protein TT8R3VP GN HRV VP TT8R3VP FC Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity). TT8R3VP PD 2HWF; 2HWE; 2HWD; 1R1A; 1AYN TT8R3VP SQ GAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASSGASRLDFSQDPSKFTDPVKDVLEKGIPTLQSPSVEACGYSDRIMQITRGDSTITSQDVANAVVGYGVWPHYLTPQDATAIDKPTQPDTSSNRFYTLESKHWNGSSKGWWWKLPDALKDMGIFGENMYYHFLGRSGYTVHVQCNASKFHQGTLLVAMIPEHQLASAKHGSVTAGYKLTHPGEAGRDVSQERDASLRQPSDDSWLNFDGTLLGNLLIFPHQFINLRSNNSATLIVPYVNAVPMDSMLRHNNWSLVIIPISPLRSETTSSNIVPITVSISPMCAEFSGARAKNIKQGLPVYITPGSGQFMTTDDMQSPCALPWYHPTKEISIPGEVKNLIEMCQVDTLIPVNNVGNNVGNVSMYTVQLGNQTGMAQKVFSIKVDITSQPLATTLIGEIASYYTHWTGSLRFSFMFCGTANTTLKLLLAYTPPGIDEPTTRKDAMLGTHVVWDVGLQSTISLVVPWVSASHFRLTADNKYSMAGYITCWYQTNLVVPPSTPQTADMLCFVSACKDFCLRMARDTDLHIQSGPIEQNPVENYIDEVLNEVLVVPNIKESHHTTSNSAPLLDAAETGHTSNVQPEDAIETRYVITSQTRDEMSIESFLGRSGCVHISRIKVDYTDYNGQDINFTKWKITLQEMAQIRRKFELFTYVRFDSEITLVPCIAGRGDDIGHIVMQYMYVPPGAPIPSKRNDFSWQSGTNMSIFWQHGQPFPRFSLPFLSIASAYYMFYDGYDGDNTSSKYGSVVTNDMGTICSRIVTEKQKHSVVITTHIYHKAKHTKAWCPRPPRAVPYTHSHVTNYMPETGDVTTAIVRRNTITTA TT8R3VP TT Clinical trial TTS9Q5V ID TTS9Q5V TTS9Q5V TN Sarcoglycan alpha (SGCA) TTS9Q5V UP Q16586 TTS9Q5V UC SGCA_HUMAN TTS9Q5V BC Sarcoglycan TTS9Q5V SN SGCA; Dystroglycan2; Alphasarcoglycan; AlphaSG; Adhalin; 50DAG; 50 kDa dystrophinassociated glycoprotein TTS9Q5V GN SGCA TTS9Q5V FC Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. TTS9Q5V SQ MAETLFWTPLLVVLLAGLGDTEAQQTTLHPLVGRVFVHTLDHETFLSLPEHVAVPPAVHITYHAHLQGHPDLPRWLRYTQRSPHHPGFLYGSATPEDRGLQVIEVTAYNRDSFDTTRQRLVLEIGDPEGPLLPYQAEFLVRSHDAEEVLPSTPASRFLSALGGLWEPGELQLLNVTSALDRGGRVPLPIEGRKEGVYIKVGSASPFSTCLKMVASPDSHARCAQGQPPLLSCYDTLAPHFRVDWCNVTLVDKSVPEPADEVPTPGDGILEHDPFFCPPTEAPDRDFLVDALVTLLVPLLVALLLTLLLAYVMCCRREGRLKRDLATSDIQMVHHCTIHGNTEELRQMAASREVPRPLSTLPMFNVHTGERLPPRVDSAQVPLILDQH TTS9Q5V TT Clinical trial TTX0H5W ID TTX0H5W TTX0H5W TN Short transient receptor potential channel 4 (TRPC4) TTX0H5W UP Q9UBN4 TTX0H5W UC TRPC4_HUMAN TTX0H5W BC Transient receptor potential catioin channel TTX0H5W SN hTrp4; hTrp-4; TrpC4; Trp-related protein 4 TTX0H5W GN TRPC4 TTX0H5W FC Form a receptor-activated non-selective calcium permeant cation channel. Acts as a cell-cell contact-dependent endothelial calcium entry channel. Probably operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Mediates cation entry, with an enhanced permeability to barium over calcium. May also be activated by intracellular calcium store depletion. TTX0H5W SQ MAQFYYKRNVNAPYRDRIPLRIVRAESELSPSEKAYLNAVEKGDYASVKKSLEEAEIYFKININCIDPLGRTALLIAIENENLELIELLLSFNVYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQVPPILLDKQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSVPRPHEVRCNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVENEFKSEYEELSRQCKQFAKDLLDQTRSSRELEIILNYRDDNSLIEEQSGNDLARLKLAIKYRQKEFVAQPNCQQLLASRWYDEFPGWRRRHWAVKMVTCFIIGLLFPVFSVCYLIAPKSPLGLFIRKPFIKFICHTASYLTFLFLLLLASQHIDRSDLNRQGPPPTIVEWMILPWVLGFIWGEIKQMWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYSALNPRESWDMWHPTLVAEALFAIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYEETKGLTCKGIRCEKQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFEEGGTLPTPFNVIPSPKSLWYLIKWIWTHLCKKKMRRKPESFGTIGRRAADNLRRHHQYQEVMRNLVKRYVAAMIRDAKTEEGLTEENFKELKQDISSFRFEVLGLLRGSKLSTIQSANASKESSNSADSDEKSDSEGNSKDKKKNFSLFDLTTLIHPRSAAIASERHNISNGSALVVQEPPREKQRKVNFVTDIKNFGLFHRRSKQNAAEQNANQIFSVSEEVARQQAAGPLERNIQLESRGLASRGDLSIPGLSEQCVLVDHRERNTDTLGLQVGKRVCPFKSEKVVVEDTVPIIPKEKHAKEEDSSIDYDLNLPDTVTHEDYVTTRL TTX0H5W TT Clinical trial TT9NXW4 ID TT9NXW4 TT9NXW4 TN Sigma intracellular receptor 2 (TMEM97) TT9NXW4 UP Q5BJF2 TT9NXW4 UC SGMR2_HUMAN TT9NXW4 BC TMEM97/sigma-2 receptor TT9NXW4 SN Transmembrane protein 97; Sigma2 receptor; Sigma-2 receptor; Meningioma-associated protein 30; MAC30 TT9NXW4 GN TMEM97 TT9NXW4 FC Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cancer cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. Under investigation for its potential diagnostic and therapeutic uses. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins. TT9NXW4 SQ MGAPATRRCVEWLLGLYFLSHIPITLFMDLQAVLPRELYPVEFRNLLKWYAKEFKDPLLQEPPAWFKSFLFCELVFQLPFFPIATYAFLKGSCKWIRTPAIIYSVHTMTTLIPILSTFLFEDFSKASGFKGQRPETLHERLTLVSVYAPYLLIPFILLIFMLRSPYYKYEEKRKKK TT9NXW4 TT Clinical trial TT9NXW4 FM TMEM97/sigma-2 receptor family TTTVEKI ID TTTVEKI TTTVEKI TN SLIT and NTRK-like family member 6 (SLITRK6) TTTVEKI UP Q9H5Y7 TTTVEKI UC SLIK6_HUMAN TTTVEKI SN SLITRK6; SLIT and NTRK-like protein 6 TTTVEKI GN SLITRK6 TTTVEKI FC Regulator of neurite outgrowth required for normal hearing and vision. TTTVEKI SQ MKLWIHLFYSSLLACISLHSQTPVLSSRGSCDSLCNCEEKDGTMLINCEAKGIKMVSEISVPPSRPFQLSLLNNGLTMLHTNDFSGLTNAISIHLGFNNIADIEIGAFNGLGLLKQLHINHNSLEILKEDTFHGLENLEFLQADNNFITVIEPSAFSKLNRLKVLILNDNAIESLPPNIFRFVPLTHLDLRGNQLQTLPYVGFLEHIGRILDLQLEDNKWACNCDLLQLKTWLENMPPQSIIGDVVCNSPPFFKGSILSRLKKESICPTPPVYEEHEDPSGSLHLAATSSINDSRMSTKTTSILKLPTKAPGLIPYITKPSTQLPGPYCPIPCNCKVLSPSGLLIHCQERNIESLSDLRPPPQNPRKLILAGNIIHSLMKSDLVEYFTLEMLHLGNNRIEVLEEGSFMNLTRLQKLYLNGNHLTKLSKGMFLGLHNLEYLYLEYNAIKEILPGTFNPMPKLKVLYLNNNLLQVLPPHIFSGVPLTKVNLKTNQFTHLPVSNILDDLDLLTQIDLEDNPWDCSCDLVGLQQWIQKLSKNTVTDDILCTSPGHLDKKELKALNSEILCPGLVNNPSMPTQTSYLMVTTPATTTNTADTILRSLTDAVPLSVLILGLLIMFITIVFCAAGIVVLVLHRRRRYKKKQVDEQMRDNSPVHLQYSMYGHKTTHHTTERPSASLYEQHMVSPMVHVYRSPSFGPKHLEEEEERNEKEGSDAKHLQRSLLEQENHSPLTGSNMKYKTTNQSTEFLSFQDASSLYRNILEKERELQQLGITEYLRKNIAQLQPDMEAHYPGAHEELKLMETLMYSRPRKVLVEQTKNEYFELKANLHAEPDYLEVLEQQT TTTVEKI TT Clinical trial TTBOE28 ID TTBOE28 TTBOE28 TN Sphingomyelin synthase (SMS) TTBOE28 UP Q86VZ5; Q8NHU3 TTBOE28 UC SMS1_HUMAN; SMS2_HUMAN TTBOE28 BC Sphingomyelin synthase TTBOE28 SN SMS; Phosphatidylcholine:ceramide cholinephosphotransferase TTBOE28 GN SGMS1; SGMS2 TTBOE28 FC Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide. Golgi apparatus SMS1 directly and specifically recognizes the choline head group on the substrate, requiring two fatty chains on the choline-P donor molecule inorder to be recognized efficiently as a substrate. Major form in macrophages. Required for cell growth in certain cell types such as HeLa cells. Suppresses BAX-mediated apoptosis and also prevents cell death in response to stimuli such as hydrogen peroxide, osmotic stress, elevated temperature and exogenously supplied sphingolipids. May protect against cell death by reversing the stress-inducibleincrease in levels of proapoptotic ceramide. TTBOE28 SQ MKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLCRVSSDNGQRLLDMIETLKMEHHLEAHKNGHANGHLNIGVDIPTPDGSFSIKIKPNGMPNGYRKEMIKIPMPELERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFFDHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTTLPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQVLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPFPWPVVHLSRQVKYSRLVNDT TTBOE28 TT Clinical trial TTWGZ64 ID TTWGZ64 TTWGZ64 TN Staphylococcus Clumping factor A (Stap-coc ClfA) TTWGZ64 UP Q2G015 TTWGZ64 UC CLFA_STAA8 TTWGZ64 SN Fibrinogen-binding protein A; Fibrinogen receptor A; Clumping factor A TTWGZ64 GN Stap-coc ClfA TTWGZ64 FC Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen cell proliferative response in vitro, contributing significantly to the immunostimulatory activity of S.aureus. TTWGZ64 PD 2VR3 TTWGZ64 SQ MNMKKKEKHAIRKKSIGVASVLVGTLIGFGLLSSKEADASENSVTQSDSASNESKSNDSSSVSAAPKTDDTNVSDTKTSSNTNNGETSVAQNPAQQETTQSSSTNATTEETPVTGEATTTTTNQANTPATTQSSNTNAEELVNQTSNETTSNDTNTVSSVNSPQNSTNAENVSTTQDTSTEATPSNNESAPQSTDASNKDVVNQAVNTSAPRMRAFSLAAVAADAPVAGTDITNQLTNVTVGIDSGTTVYPHQAGYVKLNYGFSVPNSAVKGDTFKITVPKELNLNGVTSTAKVPPIMAGDQVLANGVIDSDGNVIYTFTDYVNTKDDVKATLTMPAYIDPENVKKTGNVTLATGIGSTTANKTVLVDYEKYGKFYNLSIKGTIDQIDKTNNTYRQTIYVNPSGDNVIAPVLTGNLKPNTDSNALIDQQNTSIKVYKVDNAADLSESYFVNPENFEDVTNSVNITFPNPNQYKVEFNTPDDQITTPYIVVVNGHIDPNSKGDLALRSTLYGYNSNIIWRSMSWDNEVAFNNGSGSGDGIDKPVVPEQPDEPGEIEPIPEDSDSDPGSDSGSDSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSDNDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSDSDSDSDSDSDSDSDSDSDSASDSDSGSDSDSSSDSDSESDSNSDSESVSNNNVVPPNSPKNGTNASNKNEAKDSKEPLPDTGSEDEANTSLIWGLLASIGSLLLFRRKKENKDKK TTWGZ64 TT Clinical trial TTYQIFM ID TTYQIFM TTYQIFM TN Staphylococcus Elongation factor Tu (Stap-coc tuf) TTYQIFM UP Q6GBT9 TTYQIFM UC EFTU_STAAS TTYQIFM BC TRAFAC class translation factor GTPase TTYQIFM SN tuf; Elongation factor Tu of Staphylococcus aureus; EFTu TTYQIFM GN Stap-coc tuf TTYQIFM FC This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. TTYQIFM SQ MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVIAGSALKALEGDAQYEEKILELMEAVDTYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGLHDTSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTEFKAEVYVLSKDEGGRHTPFFSNYRPQFYFRTTDVTGVVHLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGSGVVTEIIK TTYQIFM TT Clinical trial TTE0AHP ID TTE0AHP TTE0AHP TN Staphylococcus Iron-regulated surface determinant B (Stap-coc isdB) TTE0AHP UP Q8NX66 TTE0AHP UC ISDB_STAAW TTE0AHP SN isdB; Staphylococcus aureus surface protein J; Staphylococcal ironregulated protein H; Ironregulated surface determinant protein B; Furregulated protein B TTE0AHP GN Stap-coc isdB TTE0AHP FC Seems to function as the primary receptor for hemoglobin since its inactivation inhibits the ability of S.aureus to bind hemoglobin. Binds hemoglobin in a dose-dependent way. Required for S.aureus growth using hemoglobin as the sole iron source. Also required for virulence. IsdA and/or IsdB promote resistance to hydrogen peroxide and killing by neutrophils. TTE0AHP PD 2MOQ TTE0AHP SQ MNKQQKEFKSFYSIRKSSLGVASVAISTLLLLMSNGEAQAAAEETGGTNTEAQPKTEAVASPTTTSEKAPETKPVANAVSVSNKEVEAPTSETKEAKEVKEVKAPKETKEVKPAAKATNNTYPILNQELREAIKNPAIKDKDHSAPNSRPIDFEMKKKDGTQQFYHYASSVKPARVIFTDSKPEIELGLQSGQFWRKFEVYEGDKKLPIKLVSYDTVKDYAYIRFSVSNGTKAVKIVSSTHFNNKEEKYDYTLMEFAQPIYNSADKFKTEEDYKAEKLLAPYKKAKTLERQVYELNKIQDKLPEKLKAEYKKKLEDTKKALDEQVKSAITEFQNVQPTNEKMTDLQDTKYVVYESVENNESMMDTFVKHPIKTGMLNGKKYMVMETTNDDYWKDFMVEGQRVRTISKDAKNNTRTIIFPYVEGKTLYDAIVKVHVKTIDYDGQYHVRIVDKEAFTKANTDKSNKKEQQDNSAKKEATPATPSKPTPSPVEKESQKQDSQKDDNKQLPSVEKENDASSESGKDKTPATKPTKGEVESSSTTPTKVVSTTQNVAKPTTASSKTTKDVVQTSAGSSEAKDSAPLQKANIKNTNDGHTQSQNNKNTQENKAKSLPQTGEESNKDMTLPLMALLALSSIVAFVLPRKRKN TTE0AHP TT Clinical trial TTBWX8P ID TTBWX8P TTBWX8P TN Staphylococcus Manganese transporter C (Stap-coc MntC) TTBWX8P UP W8TNQ9 TTBWX8P UC W8TNQ9_STAAU TTBWX8P SN Metal ABC transporter substrate-binding protein; Manganese ABC transporter substrate-binding protein; Manganese ABC transporter substrate-binding lipoprotein; ABC transporter substrate-binding protein; ABC superfamily ATP binding cassette transporter, binding protein TTBWX8P GN Stap-coc MntC TTBWX8P FC A component of Mnt comples, conserved across the staphylococcal species group. Expressed on the cell surface of S. aureus in biofilms generated in in vivo models of infection. TTBWX8P PD 5HDQ TTBWX8P SQ MKKLVPLLLALLLLVAACGTGGKQSSDKSNGKLKVVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLETGNGWFEKALEQAGKSLKDKKVIAVSKDVKPIYLNGEEGNKDKQDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEKLNNDSKDKFNDIPKEQRAMITSEGAFKYFSKQYGITPGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVDKKAMESLSEETKKDIFGEVYTDSIGKEGTKGDSYYKMMKSNIETVHGSMK TTBWX8P TT Clinical trial TT9RZ03 ID TT9RZ03 TT9RZ03 TN TAR DNA binding protein 43 (TARDBP) TT9RZ03 UP Q13148 TT9RZ03 UC TADBP_HUMAN TT9RZ03 SN TDP43; TDP-43; TAR DNA-binding protein 43 TT9RZ03 GN TARDBP TT9RZ03 FC RNA-binding protein that is involved in various steps of RNA biogenesis and processing. Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs. In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases. Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts. Regulates also mRNA stability by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail deadenylation and thus shortening. In response to oxidative insult, associates with stalled ribosomes localized to stress granules (SGs) and contributes to cell survival. Participates also in the normal skeletal muscle formation and regeneration, forming cytoplasmic myo-granules and binding mRNAs that encode sarcomeric proteins. Plays a role in the maintenance of the circadian clock periodicity via stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner. TT9RZ03 PD 6CFH; 6CF4; 6B1G; 5X4F; 5WKD TT9RZ03 SQ MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRGGGAGLGNNQGSNMGGGMNFGAFSINPAMMAAAQAALQSSWGMMGMLASQQNQSGPSGNNQNQGNMQREPNQAFGSGNNSYSGSNSGAAIGWGSASNAGSGSGFNGGFGSSMDSKSSGWGM TT9RZ03 TT Clinical trial TT9RZ03 FM RNA recognition motif TTWDKCL ID TTWDKCL TTWDKCL TN Target of rapamycin complex 2 MAPKAP1 (MTORC2) TTWDKCL UP Q9BPZ7 TTWDKCL UC SIN1_HUMAN TTWDKCL SN mSIN1; Target of rapamycin complex 2 subunit MAPKAP1; TORC2 subunit MAPKAP1; Stress-activated map kinase-interacting protein 1; SIN1; SAPK-interacting protein 1; Mitogen-activated protein kinase 2-associated protein 1; MIP1 TTWDKCL GN MAPKAP1 TTWDKCL FC mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex. Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. TTWDKCL PD 5ZCS; 3VOQ TTWDKCL SQ MAFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGETQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSLKEKPPISGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVYLPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVTMKEILLKAVKRRKGSQKVSGPQYRLEKQSEPNVAVDLDSTLESQSAWEFCLVRENSSRADGVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKASTKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVLKVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQ TTWDKCL TT Clinical trial TT1DHW2 ID TT1DHW2 TT1DHW2 TN T-cell receptor beta constant 1 (TRBC1) TT1DHW2 UP P01850 TT1DHW2 UC TRBC1_HUMAN TT1DHW2 SN TCRBC1; BV05S1J2.2 TT1DHW2 GN TRBC1 TT1DHW2 FC Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens. Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation. The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity. Constant region of T cell receptor (TR) alpha chain. TT1DHW2 PD 4ZDH; 4X6D; 4X6C; 4X6B; 4PRP TT1DHW2 SQ DLNKVFPPEVAVFEPSEAEISHTQKATLVCLATGFFPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRADCGFTSVSYQQGVLSATILYEILLGKATLYAVLVSALVLMAMVKRKDF TT1DHW2 TT Clinical trial TTMHA6L ID TTMHA6L TTMHA6L TN T-cell surface glycoprotein CD8 (CD8) TTMHA6L UP P01732; P10966 TTMHA6L UC CD8A_HUMAN; CD8B_HUMAN TTMHA6L SN T-lymphocyte differentiation antigen T8/Leu-2; CD8 TTMHA6L GN CD8A; CD8B TTMHA6L FC Identifies cytotoxic/suppressor T-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of T-cell mediated killing. CD8 alpha chains binds to class I MHC molecules alpha-3 domains. TTMHA6L SQ MALPVTALLLPLALLLHAARPSQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKAAEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV TTMHA6L TT Clinical trial TTMHA6L KE hsa04514:Cell adhesion molecules (CAMs); hsa04612:Antigen processing and presentation; hsa04640:Hematopoietic cell lineage; hsa04660:T cell receptor signaling pathway; hsa05340:Primary immunodeficiency TT2Z39D ID TT2Z39D TT2Z39D TN Thyrotropin-releasing hormone (TRH) TT2Z39D UP P20396 TT2Z39D UC TRH_HUMAN TT2Z39D SN Prothyroliberin; Pro-thyrotropin-releasing hormone; Pro-TRH TT2Z39D GN TRH TT2Z39D FC As a component of the hypothalamic-pituitary-thyroid axis, it controls the secretion of thyroid-stimulating hormone (TSH) and is involved in thyroid hormone synthesis regulation. It also operates as modulator of hair growth. It promotes hair-shaft elongation, prolongs the hair cycle growth phase (anagen) and antagonizes its termination (catagen) by TGFB2. It stimulates proliferation and inhibits apoptosis of hair matrix keratinocytes. TT2Z39D SQ MPGPWLLLALALTLNLTGVPGGRAQPEAAQQEAVTAAEHPGLDDFLRQVERLLFLRENIQRLQGDQGEHSASQIFQSDWLSKRQHPGKREEEEEEGVEEEEEEEGGAVGPHKRQHPGRREDEASWSVDVTQHKRQHPGRRSPWLAYAVPKRQHPGRRLADPKAQRSWEEEEEEEEREEDLMPEKRQHPGKRALGGPCGPQGAYGQAGLLLGLLDDLSRSQGAEEKRQHPGRRAAWVREPLEE TT2Z39D TT Clinical trial TTZEP6S ID TTZEP6S TTZEP6S TN Transcription factor Sp1 (SP1) TTZEP6S UP P08047 TTZEP6S UC SP1_HUMAN TTZEP6S SN TSFP1 TTZEP6S GN SP1 TTZEP6S FC Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component ARNTL/BMAL1. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity). TTZEP6S PD 1VA3; 1VA2; 1VA1; 1SP2; 1SP1 TTZEP6S SQ MSDQDHSMDEMTAVVKIEKGVGGNNGGNGNGGGAFSQARSSSTGSSSSTGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGSSTNGSNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSGSQESGSQPVTSGTTISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTTSGSSGTNSQGQTPQRVSGLQGSDALNIQQNQTSGGSLQAGQQKEGEQNQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAGGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALSVGTLPLDSGAGSEGSGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVADLQSINISGNGF TTZEP6S TT Clinical trial TTZEP6S FM Sp1 C2H2-type zinc-finger TTL9OD4 ID TTL9OD4 TTL9OD4 TN Transmembrane activator and CAML interactor (TNFRSF13B) TTL9OD4 UP O14836 TTL9OD4 UC TR13B_HUMAN TTL9OD4 SN Tumor necrosis factor receptor superfamily member 13B; TACI; CD267 TTL9OD4 GN TNFRSF13B TTL9OD4 FC Mediates calcineurin-dependent activation of NF-AT, as well as activation of NF-kappa-B and AP-1. Involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that binds both ligands with similar high affinity. TTL9OD4 PD 1XUT; 1XU1 TTL9OD4 SQ MSGLGRSRRGGRSRVDQEERFPQGLWTGVAMRSCPEEQYWDPLLGTCMSCKTICNHQSQRTCAAFCRSLSCRKEQGKFYDHLLRDCISCASICGQHPKQCAYFCENKLRSPVNLPPELRRQRSGEVENNSDNSGRYQGLEHRGSEASPALPGLKLSADQVALVYSTLGLCLCAVLCCFLVAVACFLKKRGDPCSCQPRSRPRQSPAKSSQDHAMEAGSPVSTSPEPVETCSFCFPECRAPTQESAVTPGTPDPTCAGRWGCHTRTTVLQPCPHIPDSGLGIVCVPAQEGGPGA TTL9OD4 TT Clinical trial TTL9OD4 FM Transmembrane protein TTGR91N ID TTGR91N TTGR91N TN TWIK-related acid-sensitive potassium channel 1 (TASK1) TTGR91N UP O14649 TTGR91N UC KCNK3_HUMAN TTGR91N SN Two pore potassium channel KT3.1; Two pore K(+) channel KT3.1; TWIK-related acid-sensitive K(+) channel 1; Acid-sensitive potassium channel protein TASK-1 TTGR91N GN KCNK3 TTGR91N FC pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward. TTGR91N SQ MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPELIERQRLELRQQELRARYNLSQGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTLVRYLLHRAKKGLGMRRADVSMANMVLIGFFSCISTLCIGAAAFSHYEHWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTRNGQAGGGGGGGSAHTTDTASSTAAAGGGGFRNVYAEVLHFQSMCSCLWYKSREKLQYSIPMIIPRDLSTSDTCVEQSHSSPGGGGRYSDTPSRRCLCSGAPRSAISSVSTGLHSLSTFRGLMKRRSSV TTGR91N TT Clinical trial TTGR91N KE hsa04925:Aldosterone synthesis and secretion; hsa04927:Cortisol synthesis and secretion; hsa04934:Cushing syndrome TT51SK8 ID TT51SK8 TT51SK8 TN V-set immunoregulatory receptor (VSIR) TT51SK8 UP Q9H7M9 TT51SK8 UC VISTA_HUMAN TT51SK8 SN VISTA; V-set domain-containing immunoregulatory receptor; Stress-induced secreted protein-1; Sisp-1; SISP1; Platelet receptor Gi24; C10orf54 TT51SK8 GN VSIR TT51SK8 FC Immunoregulatory receptor which inhibits the T-cell response (PubMed:24691993). May promote differentiation of embryonic stem cells, by inhibiting BMP4 signaling. May stimulate MMP14-mediated MMP2 activation (PubMed:20666777). TT51SK8 SQ MGVPTALEAGSWRWGSLLFALFLAASLGPVAAFKVATPYSLYVCPEGQNVTLTCRLLGPVDKGHDVTFYKTWYRSSRGEVQTCSERRPIRNLTFQDLHLHHGGHQAANTSHDLAQRHGLESASDHHGNFSITMRNLTLLDSGLYCCLVVEIRHHHSEHRVHGAMELQVQTGKDAPSNCVVYPSSSQDSENITAAALATGACIVGILCLPLILLLVYKQRQAASNRRAQELVRMDSNIQGIENPGFEASPPAQGIPEAKVRHPLSYVAQRQPSESGRHLLSEPSTPLSPPGPGDVFFPSLDPVPDSPNFEVI TT51SK8 TT Clinical trial TT51SK8 KE hsa04514:Cell adhesion molecules (CAMs) TT9RV4P ID TT9RV4P TT9RV4P TN Activin (ACT) TT9RV4P UP P08476; P09529; P55103; P58166 TT9RV4P UC INHBA_HUMAN; INHBB_HUMAN; INHBC_HUMAN; INHBE_HUMAN TT9RV4P SN Inhibin beta; Activin beta TT9RV4P GN INHBA; INHBB; INHBC; INHBE TT9RV4P FC Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins. TT9RV4P SQ MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEEEGEGKKKGGGEGGAGADEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS TT9RV4P TT Clinical trial TTSANDR ID TTSANDR TTSANDR TN Arginase (ARG) TTSANDR UP P05089; P78540 TTSANDR UC ARGI1_HUMAN; ARGI2_HUMAN TTSANDR SN L-arginase; Canavanase; Arginine transamidinase; Arginine amidinase TTSANDR GN ARG1; ARG2 TTSANDR FC Arginase I functions in the urea cycle, and is located primarily in the cytoplasm of hepatocytes (liver cells); Arginase II, implicated in the regulation of intracellular arginine/ornithine levels is located in mitochondria of several tissues in the body, with most abundance in the kidney and prostate. TTSANDR SQ MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACFGLAREGNHKPIDYLNPPK TTSANDR TT Clinical trial TTTKCMH ID TTTKCMH TTTKCMH TN Bacterial Penicillin binding protein 1 (Bact pbp) TTTKCMH UP P02918; P02919; P76577 TTTKCMH UC PBPA_ECOLI; PBPB_ECOLI; PBPC_ECOLI TTTKCMH SN Penicillin-binding protein 1; PBP1; PBP-1; Bact pon TTTKCMH GN Bact mrcA; Bact mrcB; Bact pbpC TTTKCMH FC Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). TTTKCMH SQ MKFVKYFLILAVCCILLGAGSIYGLYRYIEPQLPDVATLKDVRLQIPMQIYSADGELIAQYGEKRRIPVTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEVFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLNEMAVIAGLPKAPSTFNPLYSMDRAVARRNVVLSRMLDEGYITQQQFDQTRTEAINANYHAPEIAFSAPYLSEMVRQEMYNRYGESAYEDGYRIYTTITRKVQQAAQQAVRNNVLDYDMRHGYRGPANVLWKVGESAWDNNKITDTLKALPTYGPLLPAAVTSANPQQATAMLADGSTVALSMEGVRWARPYRSDTQQGPTPRKVTDVLQTGQQIWVRQVGDAWWLAQVPEVNSALVSINPQNGAVMALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGLTLASMLNDVPISRWDASAGSDWQPKNSPPQYAGPIRLRQGLGQSKNVVMVRAMRAMGVDYAAEYLQRFGFPAQNIVHTESLALGSASFTPMQVARGYAVMANGGFLVDPWFISKIENDQGGVIFEAKPKVACPECDIPVIYGDTQKSNVLENNDVEDVAISREQQNVSVPMPQLEQANQALVAKTGAQEYAPHVINTPLAFLIKSALNTNIFGEPGWQGTGWRAGRDLQRRDIGGKTGTTNSSKDAWFSGYGPGVVTSVWIGFDDHRRNLGHTTASGAIKDQISGYEGGAKSAQPAWDAYMKAVLEGVPEQPLTPPPGIVTVNIDRSTGQLANGGNSREEYFIEGTQPTQQAVHEVGTTIIDNGEAQELF TTTKCMH TT Clinical trial TT731LW ID TT731LW TT731LW TN Colony stimulating factor-1 receptor (CSF-1R) TT731LW UP E9PEK4 TT731LW UC E9PEK4_HUMAN TT731LW SN Macrophage colony-stimulating factor 1 receptor TT731LW GN CSF1R TT731LW FC A cytokine which controls the production, differentiation, and function of macrophages. TT731LW SQ MGPGVLLLLLVATAWHGQGIPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGAHTHPPDEFLFTPVVVACMSIMALLLLLLLLLLYKYKQKPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGTVASPARVWTPMWR TT731LW TT Clinical trial TTHIQMC ID TTHIQMC TTHIQMC TN Cyclic nucleotide-gated channel alpha-1 (CNGA1) TTHIQMC UP P29973 TTHIQMC UC CNGA1_HUMAN TTHIQMC SN cGMP-gated cation channel alpha-1; Rod photoreceptor cGMP-gated channel subunit alpha; Cyclic nucleotide-gated channel, photoreceptor; Cyclic nucleotide-gated cation channel 1; CNG1; CNG-1; CNG channel alpha-1; CNCG1; CNCG TTHIQMC GN CNGA1 TTHIQMC FC Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. TTHIQMC SQ MKLSMKNNIINTQQSFVTMPNVIVPDIEKEIRRMENGACSSFSEDDDSASTSEESENENPHARGSFSYKSLRKGGPSQREQYLPGAIALFNVNNSSNKDQEPEEKKKKKKEKKSKSDDKNENKNDPEKKKKKKDKEKKKKEEKSKDKKEEEKKEVVVIDPSGNTYYNWLFCITLPVMYNWTMVIARACFDELQSDYLEYWLILDYVSDIVYLIDMFVRTRTGYLEQGLLVKEELKLINKYKSNLQFKLDVLSLIPTDLLYFKLGWNYPEIRLNRLLRFSRMFEFFQRTETRTNYPNIFRISNLVMYIVIIIHWNACVFYSISKAIGFGNDTWVYPDINDPEFGRLARKYVYSLYWSTLTLTTIGETPPPVRDSEYVFVVVDFLIGVLIFATIVGNIGSMISNMNAARAEFQARIDAIKQYMHFRNVSKDMEKRVIKWFDYLWTNKKTVDEKEVLKYLPDKLRAEIAINVHLDTLKKVRIFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVVLSDGSYFGEISILNIKGSKAGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPDAKTMLEEKGKQILMKDGLLDLNIANAGSDPKDLEEKVTRMEGSVDLLQTRFARILAEYESMQQKLKQRLTKVEKFLKPLIDTEFSSIEGPGAESGPIDST TTHIQMC TT Clinical trial TT8SJGB ID TT8SJGB TT8SJGB TN Cyclic nucleotide-gated channel alpha-2 (CNGA2) TT8SJGB UP Q16280 TT8SJGB UC CNGA2_HUMAN TT8SJGB SN Cyclic nucleotide-gated olfactory channel; Cyclic nucleotide-gated cation channel 2; CNG2; CNG-2; CNG channel alpha-2; CNCG2; CNCA1; CNCA TT8SJGB GN CNGA2 TT8SJGB FC Odorant signal transduction is probably mediated by a G-protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons. TT8SJGB SQ MTEKTNGVKSSPANNHNHHAPPAIKANGKDDHRTSSRPHSAADDDTSSELQRLADVDAPQQGRSGFRRIVRLVGIIREWANKNFREEEPRPDSFLERFRGPELQTVTTQEGDGKGDKDGEDKGTKKKFELFVLDPAGDWYYCWLFVIAMPVLYNWCLLVARACFSDLQKGYYLVWLVLDYVSDVVYIADLFIRLRTGFLEQGLLVKDTKKLRDNYIHTLQFKLDVASIIPTDLIYFAVDIHSPEVRFNRLLHFARMFEFFDRTETRTNYPNIFRISNLVLYILVIIHWNACIYYAISKSIGFGVDTWVYPNITDPEYGYLAREYIYCLYWSTLTLTTIGETPPPVKDEEYLFVIFDFLIGVLIFATIVGNVGSMISNMNATRAEFQAKIDAVKHYMQFRKVSKGMEAKVIRWFDYLWTNKKTVDEREILKNLPAKLRAEIAINVHLSTLKKVRIFHDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVADDGVTQYALLSAGSCFGEISILNIKGSKMGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVLEERGREILMKEGLLDENEVATSMEVDVQEKLGQLETNMETLYTRFGRLLAEYTGAQQKLKQRITVLETKMKQNNEDDYLSDGMNSPELAAADEP TT8SJGB TT Clinical trial TTH13AB ID TTH13AB TTH13AB TN Cyclic pyranopterin monophosphate synthase (MOCS1) TTH13AB UP Q9NZB8 TTH13AB UC MOCS1_HUMAN TTH13AB SN Molybdenum cofactor synthesis-step 1 protein A-B (414-636); Molybdenum cofactor biosynthesis protein 1 (414-636); MOCS1 (414-636); MIG11 (414-636); Cell migration-inducing gene 11 protein (414-636) TTH13AB GN MOCS1 TTH13AB FC MOCS1A catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate and MOCS1B catalyzes the subsequent conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cPMP. Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP). TTH13AB SQ MAARPLSRMLRRLLRSSARSCSSGAPVTQPCPGESARAASEEVSRRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSISQMKNRPMILIELFLMFPNSPPANPSIFSWDPLHVQGLRPRMSFSSQVATLWKGCRVPQTPPLAQQRLGSGSFQRHYTSRADSDANSKCLSPGSWASAAPSGPQLTSEQLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGDFHRA TTH13AB TT Clinical trial TTRIM0E ID TTRIM0E TTRIM0E TN Cyclin-dependent kinase 13 (CDK13) TTRIM0E UP Q14004 TTRIM0E UC CDK13_HUMAN TTRIM0E SN CDC2-related protein kinase 5; Cell division cycle 2-like protein kinase 5; Cell division protein kinase 13; hCDK13; Cholinesterase-related cell division controller TTRIM0E GN CDK13 TTRIM0E FC Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. TTRIM0E EC EC 2.7.11.22 TTRIM0E SQ MPSSSDTALGGGGGLSWAEKKLEERRKRRRFLSPQQPPLLLPLLQPQLLQPPPPPPPLLFLAAPGTAAAAAAAAAASSSCFSPGPPLEVKRLARGKRRAGGRQKRRRGPRAGQEAEKRRVFSLPQPQQDGGGGASSGGGVTPLVEYEDVSSQSEQGLLLGGASAATAATAAGGTGGSGGSPASSSGTQRRGEGSERRPRRDRRSSSGRSKERHREHRRRDGQRGGSEASKSRSRHSHSGEERAEVAKSGSSSSSGGRRKSASATSSSSSSRKDRDSKAHRSRTKSSKEPPSAYKEPPKAYREDKTEPKAYRRRRSLSPLGGRDDSPVSHRASQSLRSRKSPSPAGGGSSPYSRRLPRSPSPYSRRRSPSYSRHSSYERGGDVSPSPYSSSSWRRSRSPYSPVLRRSGKSRSRSPYSSRHSRSRSRHRLSRSRSRHSSISPSTLTLKSSLAAELNKNKKARAAEAARAAEAAKAAEATKAAEAAAKAAKASNTSTPTKGNTETSASASQTNHVKDVKKIKIEHAPSPSSGGTLKNDKAKTKPPLQVTKVENNLIVDKATKKAVIVGKESKSAATKEESVSLKEKTKPLTPSIGAKEKEQHVALVTSTLPPLPLPPMLPEDKEADSLRGNISVKAVKKEVEKKLRCLLADLPLPPELPGGDDLSKSPEEKKTATQLHSKRRPKICGPRYGETKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPPPDLPLWQDCHELWSKKRRRQKQMGMTDDVSTIKAPRKDLSLGLDDSRTNTPQGVLPSSQLKSQGSSNVAPVKTGPGQHLNHSELAILLNLLQSKTSVNMADFVQVLNIKVNSETQQQLNKINLPAGILATGEKQTDPSTPQQESSKPLGGIQPSSQTIQPKVETDAAQAAVQSAFAVLLTQLIKAQQSKQKDVLLEERENGSGHEASLQLRPPPEPSTPVSGQDDLIQHQDMRILELTPEPDRPRILPPDQRPPEPPEPPPVTEEDLDYRTENQHVPTTSSSLTDPHAGVKAALLQLLAQHQPQDDPKREGGIDYQAGDTYVSTSDYKDNFGSSSFSSAPYVSNDGLGSSSAPPLERRSFIGNSDIQSLDNYSTASSHSGGPPQPSAFSESFPSSVAGYGDIYLNAGPMLFSGDKDHRFEYSHGPIAVLANSSDPSTGPESTHPLPAKMHNYNYGGNLQENPSGPSLMHGQTWTSPAQGPGYSQGYRGHISTSTGRGRGRGLPY TTRIM0E TT Literature-reported TTATL6Y ID TTATL6Y TTATL6Y TN DNA-dependent DNA polymerase (DPOL) TTATL6Y UP O75417; Q7Z5Q5; P06746; Q9UHN1; P54098; P56282; Q9HCU8; P28340 TTATL6Y UC DPOLQ_HUMAN; DPOLN_HUMAN; DPOLB_HUMAN; DPOG2_HUMAN; DPOG1_HUMAN; DPOE2_HUMAN; DPOD4_HUMAN; DPOD1_HUMAN TTATL6Y SN DNA polymerase TTATL6Y GN POLQ; POLN; POLB; POLG2; POLG; POLE2; POLD4; ;POLD1 TTATL6Y FC Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Repair polymerase that plays a key role in base-excision repair. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. TTATL6Y SQ MNLLRRSGKRRRSESGSDSFSGSGGDSSASPQFLSGSVLSPPPGLGRCLKAAAAGECKPTVPDYERDKLLLANWGLPKAVLEKYHSFGVKKMFEWQAECLLLGQVLEGKNLVYSAPTSAGKTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPSRHFSSLDIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYITRKSASCQADLASSLSNAVQIVGMSATLPNLELVASWLNAELYHTDFRPVPLLESVKVGNSIYDSSMKLVREFEPMLQVKGDEDHVVSLCYETICDNHSVLLFCPSKKWCEKLADIIAREFYNLHHQAEGLVKPSECPPVILEQKELLEVMDQLRRLPSGLDSVLQKTVPWGVAFHHAGLTFEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPIFGGRPLDILTYKQMVGRAGRKGVDTVGESILICKNSEKSKGIALLQGSLKPVRSCLQRREGEEVTGSMIRAILEIIVGGVASTSQDMHTYAACTFLAASMKEGKQGIQRNQESVQLGAIEACVMWLLENEFIQSTEASDGTEGKVYHPTHLGSATLSSSLSPADTLDIFADLQRAMKGFVLENDLHILYLVTPMFEDWTTIDWYRFFCLWEKLPTSMKRVAELVGVEEGFLARCVKGKVVARTERQHRQMAIHKRFFTSLVLLDLISEVPLREINQKYGCNRGQIQSLQQSAAVYAGMITVFSNRLGWHNMELLLSQFQKRLTFGIQRELCDLVRVSLLNAQRARVLYASGFHTVADLARANIVEVEVILKNAVPFKSARKAVDEEEEAVEERRNMRTIWVTGRKGLTEREAAALIVEEARMILQQDLVEMGVQWNPCALLHSSTCSLTHSESEVKEHTFISQTKSSYKKLTSKNKSNTIFSDSYIKHSPNIVQDLNKSREHTSSFNCNFQNGNQEHQTCSIFRARKRASLDINKEKPGASQNEGKTSDKKVVQTFSQKTKKAPLNFNSEKMSRSFRSWKRRKHLKRSRDSSPLKDSGACRIHLQGQTLSNPSLCEDPFTLDEKKTEFRNSGPFAKNVSLSGKEKDNKTSFPLQIKQNCSWNITLTNDNFVEHIVTGSQSKNVTCQATSVVSEKGRGVAVEAEKINEVLIQNGSKNQNVYMKHHDIHPINQYLRKQSHEQTSTITKQKNIIERQMPCEAVSSYINRDSNVTINCERIKLNTEENKPSHFQALGDDISRTVIPSEVLPSAGAFSKSEGQHENFLNISRLQEKTGTYTTNKTKNNHVSDLGLVLCDFEDSFYLDTQSEKIIQQMATENAKLGAKDTNLAAGIMQKSLVQQNSMNSFQKECHIPFPAEQHPLGATKIDHLDLKTVGTMKQSSDSHGVDILTPESPIFHSPILLEENGLFLKKNEVSVTDSQLNSFLQGYQTQETVKPVILLIPQKRTPTGVEGECLPVPETSLNMSDSLLFDSFSDDYLVKEQLPDMQMKEPLPSEVTSNHFSDSLCLQEDLIKKSNVNENQDTHQQLTCSNDESIIFSEMDSVQMVEALDNVDIFPVQEKNHTVVSPRALELSDPVLDEHHQGDQDGGDQDERAEKSKLTGTRQNHSFIWSGASFDLSPGLQRILDKVSSPLENEKLKSMTINFSSLNRKNTELNEEQEVISNLETKQVQGISFSSNNEVKSKIEMLENNANHDETSSLLPRKESNIVDDNGLIPPTPIPTSASKLTFPGILETPVNPWKTNNVLQPGESYLFGSPSDIKNHDLSPGSRNGFKDNSPISDTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIGSRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSCLRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQSLGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALHPLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQAVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETVKNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQSDQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV TTATL6Y TT Clinical trial TTP7TQA ID TTP7TQA TTP7TQA TN DNA-directed RNA polymerase II (RNAP II) TTP7TQA UP P24928; P30876; P19387 TTP7TQA UC RPB1_HUMAN; RPB2_HUMAN; RPB3_HUMAN TTP7TQA SN RPB; RNA-directed RNA polymerase II; RNA polymerase II TTP7TQA GN POLR2A; POLR2B; POLR2C TTP7TQA FC DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1/RPB2/RPB3 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. TTP7TQA SQ MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPASPKYTPTSPSYSPSSPEYTPTSPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN TTP7TQA TT Literature-reported TT0BI4Q ID TT0BI4Q TT0BI4Q TN Epstein-Barr virus Latent membrane protein 1 (EBV LMP1) TT0BI4Q UP P0C741 TT0BI4Q UC LMP1_EBVG TT0BI4Q SN Protein p63; P63; Latent membrane protein 1; LMP1; LMP-1; BNLF1 TT0BI4Q GN EBV LMP1 TT0BI4Q FC Functions as a constitutively active tumor necrosis factor receptor that induces the activation of several signaling pathways, including those of the NF-kappa-B family. LMP1 signaling leads to up-regulation of antiapoptotic proteins and provide growth signals in latently infected cells. Interacts with host UBE2I and subsequently affects the sumoylation state of several cellular proteins. For example, induces the sumoylation of host IRF7 thereby limiting its transcriptional activity and modulating the activation of innate immune responses. Acts as a CD40 functional homolog to prevent apoptosis of infected B-lymphocytes and drive their proliferation. TT0BI4Q SQ MERDLERGPPGPPRPPLGPPLSSSIGLALLLLLLALLFWLYIVLSNWTGGALLVLYSFALMLIIIILIIFIFRRDLLCPLGGLGLLLLMVTLLLIALWNLHGQALYLGIVLFIFGCLLVLGLWIYFLEILWRLGATIWQLLAFILAFFLAIILLIIALYLQQNWWTLLVDLLWLLLFMAILIWMYFHGPRHTDEHHHDDSLPHPQQATDDSSHESDSNSNEGRHHLLVSGAGDGPPLCSQNLGAPGGGPDNGPQDPDNTDDNGPQDPDNTDDNGNTDDNGPQDPDNTDDNGPHDPLPHNPSDSAGNDGGPPNLTEEVENKGGDRGPPSMTDGGGGDPHLPTLLLGTSGSGGDDDDPHGPVQLSYYD TT0BI4Q TT Clinical trial TTFPD8J ID TTFPD8J TTFPD8J TN Fusion protein FGFR3-TACC3 (FGFR3-TACC3) TTFPD8J UP P22607-Q9Y6A5 TTFPD8J UC FGFR3_HUMAN-TACC3_HUMAN TTFPD8J SN FGFR3-TACC3 gene fusion; FGFR3-TACC3 TTFPD8J GN FGFR3-TACC3 TTFPD8J FC An oncogenic function in respiratory epithelium. TTFPD8J SQ MSLQVLNDKNVSNEKNTENCDFLFSPPEVTGRSSVLRVSQKENVPPKNLAKAMKVTFQTPLRDPQTHRILSPSMASKLEAPFTQDDTLGLENSHPVWTQKENQQLIKEVDAKTTHGILQKPVEADTDLLGDASPAFGSGSSSESGPGALADLDCSSSSQSPGSSENQMVSPGKVSGSPEQAVEENLSSYSLDRRVTPASETLEDPCRTESQHKAETPHGAEEECKAETPHGAEEECRHGGVCAPAAVATSPPGAIPKEACGGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPESTAPTNHLVAGRAMTLSPQEEVAAGQMASSSRSGPVKLEFDVSDGATSKRAPPPRRLGERSGLKPPLRKAAVRQQKAPQEVEEDDGRSGAGEDPPMPASRGSYHLDWDKMDDPNFIPFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGPCLSQQLHSASAEDTPVVQLAAETPTAESKERALNSASTSLPTSCPGSEPVPTHQQGQPALELKEESFRDPAEVLGTGAEVDYLEQFGTSSFKESALRKQSLYLKFDPLLRDSPGRPVPVATETSSMHGANETPSGRPREAKLVEFDFLGALDIPVPGPPPGVPAPGGPPLSTGPIVDLLQYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKIMGAPACALALCVAVAIVAGASSESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGEDEAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELVEADEAGSVYAGILSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKISRFPLKRQVSLESNASMSSNTPLVRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTPSSSSSGDDSVFAHDLLPPAPPSSGGSRT TTFPD8J TT Clinical trial TTOL9B0 ID TTOL9B0 TTOL9B0 TN G-protein-coupled receptor PGR3 (GPR139) TTOL9B0 UP Q6DWJ6 TTOL9B0 UC GP139_HUMAN TTOL9B0 SN Probable G-protein coupled receptor 139; PGR3; GPRG1; G(q)-coupled orphan receptor GPRg1 TTOL9B0 GN GPR139 TTOL9B0 FC Orphan receptor. Seems to act through a G(q/11)-mediated pathway. TTOL9B0 SQ MEHTHAHLAANSSLSWWSPGSACGLGFVPVVYYSLLLCLGLPANILTVIILSQLVARRQKSSYNYLLALAAADILVLFFIVFVDFLLEDFILNMQMPQVPDKIIEVLEFSSIHTSIWITVPLTIDRYIAVCHPLKYHTVSYPARTRKVIVSVYITCFLTSIPYYWWPNIWTEDYISTSVHHVLIWIHCFTVYLVPCSIFFILNSIIVYKLRRKSNFRLRGYSTGKTTAILFTITSIFATLWAPRIIMILYHLYGAPIQNRWLVHIMSDIANMLALLNTAINFFLYCFISKRFRTMAAATLKAFFKCQKQPVQFYTNHNFSITSSPWISPANSHCIKMLVYQYDKNGKPIKVSP TTOL9B0 TT Clinical trial TTKIGZF ID TTKIGZF TTKIGZF TN Guanine nucleotide exchange factor (GNEF) TTKIGZF UP Q14232; P49770 TTKIGZF UC EI2BA_HUMAN; EI2BB_HUMAN TTKIGZF SN eIF-2B GDP-GTP exchange factor; Translation initiation factor eIF-2B; EIF2B TTKIGZF GN EIF2B1; EIF2B2 TTKIGZF FC Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. TTKIGZF SQ MDDKELIEYFKSQMKEDPDMASAVAAIRTLLEFLKRDKGETIQGLRANLTSAIETLCGVDSSVAVSSGGELFLRFISLASLEYSDYSKCKKIMIERGELFLRRISLSRNKIADLCHTFIKDGATILTHAYSRVVLRVLEAAVAAKKRFSVYVTESQPDLSGKKMAKALCHLNVPVTVVLDAAVGYIMEKADLVIVGAEGVVENGGIINKIGTNQMAVCAKAQNKPFYVVAESFKFVRLFPLNQQDVPDKFKYKADTLKVAQTGQDLKEEHPWVDYTAPSLITLLFTDLGVLTPSAVSDELIKLYL TTKIGZF TT Clinical trial TT8WFXV ID TT8WFXV TT8WFXV TN Hydroxycarboxylic acid receptor 3 (HCAR3) TT8WFXV UP P49019 TT8WFXV UC HCAR3_HUMAN TT8WFXV SN Nicotinic acid receptor 2; Niacin receptor 2; NIACR2; HM74B; HCA3; GPR109B; G-protein coupled receptor HM74B; G-protein coupled receptor HM74; G-protein coupled receptor 109B TT8WFXV GN HCAR3 TT8WFXV FC Receptor for 3-OH-octanoid acid mediates a negative feedback regulation of adipocyte lipolysis to counteract prolipolytic influences under conditions of physiological or pathological increases in beta-oxidation rates. Acts as a low affinity receptor for nicotinic acid. This pharmacological effect requires nicotinic acid doses that are much higher than those provided by a normal diet. TT8WFXV SQ MNRHHLQDHFLEIDKKNCCVFRDDFIAKVLPPVLGLEFIFGLLGNGLALWIFCFHLKSWKSSRIFLFNLAVADFLLIICLPFVMDYYVRRSDWKFGDIPCRLVLFMFAMNRQGSIIFLTVVAVDRYFRVVHPHHALNKISNWTAAIISCLLWGITVGLTVHLLKKKLLIQNGTANVCISFSICHTFRWHEAMFLLEFFLPLGIILFCSARIIWSLRQRQMDRHAKIKRAITFIMVVAIVFVICFLPSVVVRIHIFWLLHTSGTQNCEVYRSVDLAFFITLSFTYMNSMLDPVVYYFSSPSFPNFFSTLINRCLQRKITGEPDNNRSTSVELTGDPNKTRGAPEALIANSGEPWSPSYLGPTSNNHSKKGHCHQEPASLEKQLGCCIE TT8WFXV TT Clinical trial TTS74QB ID TTS74QB TTS74QB TN Inhibitor of apoptosis protein (hIAP) TTS74QB UP P98170; Q13490; Q13489; Q13075; Q96CA5; O15392 TTS74QB UC XIAP_HUMAN; BIRC2_HUMAN; BIRC3_HUMAN; BIRC1_HUMAN; BIRC7_HUMAN; BIRC5_HUMAN TTS74QB SN Baculoviral IAP repeat-containing protein TTS74QB GN XIAP; BIRC2; BIRC3; NAIP; BIRC5; BIRC7 TTS74QB FC A class of key apoptosis regulators. Influences a multitude of other cellular processes, such as ubiquitin (Ub) dependent signaling events that regulate activation of nuclear factor B (NFB), which in turn drive the expression of genes important for inflammation, immunity, cell migration and cell survival. Modulates signaling events that promote the activation of cell motility kinases and metastasis11 and they regulate mitogenic kinase signaling, proliferation and mitosis. TTS74QB SQ MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS TTS74QB TT Clinical trial TTX4GLS ID TTX4GLS TTX4GLS TN Mammalian target of rapamycin complex 1 (mTORC1) TTX4GLS UP P42345-Q8N122-Q9BVC4-Q96B36-Q8TB45 TTX4GLS UC MTOR_HUMAN-RPTOR_HUMAN-LST8_HUMAN-AKTS1_HUMAN-DPTOR_HUMAN TTX4GLS SN mTORC1; Mechanistic target of rapamycin complex 1 TTX4GLS GN MTOR-RPTORA-MLST8-KT1S1-DEPTOR TTX4GLS FC Functions as a nutrient/energy/redox sensor and controls protein synthesis. Activate translation of proteins. Invovled in autophagy, lysosomal damage and reactive oxygen species. TTX4GLS SQ MNTSPGTVGSDPVILATAGYDHTVRFWQAHSGICTRTVQHQDSQVNALEVTPDRSMIAAAGYQHIRMYDLNSNNPNPIISYDGVNKNIASVGFHEDGRWMYTGGEDCTARIWDLRSRNLQCQRIFQVNAPINCVCLHPNQAELIVGDQSGAIHIWDLKTDHNEQLIPEPEVSITSAHIDPDASYMAAVNSTGNCYVWNLTGGIGDEVTQLIPKTKIPAHTRYALQCRFSPDSTLLATCSADQTCKIWRTSNFSLMTELSIKSGNPGESSRGWMWGCAFSGDSQYIVTASSDNLARLWCVETGEIKREYGGHQKAVVCLAFNDSVLGMLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFWMESEMLQSPLLGLGEEDEADLTDWNLPLAFMKKRHCEKIEGSKSLAQSWRMKDRMKTVSVALVLCLNVGVDPPDVVKTTPCARLECWIDPLSMGPQKALETIGANLQKQYENWQPRARYKQSLDPTVDEVKKLCTSLRRNAKEERVLFHYNGHGVPRPTVNGEVWVFNKNYTQYIPLSIYDLQTWMGSPSIFVYDCSNAGLIVKSFKQFALQREQELEVAAINPNHPLAQMPLPPSMKNCIQLAACEATELLPMIPDLPADLFTSCLTTPIKIALRWFCMQKCVSLVPGVTLDLIEKIPGRLNDRRTPLGELNWIFTAITDTIAWNVLPRDLFQKLFRQDLLVASLFRNFLLAERIMRSYNCTPVSSPRLPPTYMHAMWQAWDLAVDICLSQLPTIIEEGTAFRHSPFFAEQLTAFQVWLTMGVENRNPPEQLPIVLQVLLSQVHRLRALDLLGRFLDLGPWAVSLALSVGIFPYVLKLLQSSARELRPLLVFIWAKILAVDSSCQADLVKDNGHKYFLSVLADPYMPAEHRTMTAFILAVIVNSYHTGQEACLQGNLIAICLEQLNDPHPLLRQWVAICLGRIWQNFDSARWCGVRDSAHEKLYSLLSDPIPEVRCAAVFALGTFVGNSAERTDHSTTIDHNVAMMLAQLVSDGSPMVRKELVVALSHLVVQYESNFCTVALQFIEEEKNYALPSPATTEGGSLTPVRDSPCTPRLRSVSSYGNIRAVATARSLNKSLQNLSLTEESGGAVAFSPGNLSTSSSASSTLGSPENEEHILSFETIDKMRRASSYSSLNSLIGVSFNSVYTQIWRVLLHLAADPYPEVSDVAMKVLNSIAYKATVNARPQRVLDTSSLTQSAPASPTNKGVHIHQAGGSPPASSTSSSSLTNDVAKQPVSRDLPSGRPGTTGPAGAQYTPHSHQFPRTRKMFDKGPEQTADDADDAAGHKSFISATVQTGFCDWSARYFAQPVMKIPEEHDLESQIRKEREWRFLRNSRVRRQAQQVIQKGITRLDDQIFLNRNPGVPSVVKFHPFTPCIAVADKDSICFWDWEKGEKLDYFHNGNPRYTRVTAMEYLNGQDCSLLLTATDDGAIRVWKNFADLEKNPEMVTAWQGLSDMLPTTRGAGMVVDWEQETGLLMSSGDVRIVRIWDTDREMKVQDIPTGADSCVTSLSCDSHRSLIVAGLGDGSIRVYDRRMALSECRVMTYREHTAWVVKASLQKRPDGHIVSVSVNGDVRIFDPRMPESVNVLQIVKGLTALDIHPQADLIACGSVNQFTAIYNSSGELINNIKYYDGFMGQRVGAISCLAFHPHWPHLAVGSNDYYISVYSVEKRVRMEEGGSTGSAGSDSSTSGSGGAQQRELERMAEVLVTGEQLRLRLHEEKVIKDRRHHLKTYPNCFVAKELIDWLIEHKEASDRETAIKLMQKLADRGIIHHVCDEHKEFKDVKLFYRFRKDDGTFPLDNEVKAFMRGQRLYEKLMSPENTLLQPREEEGVKYERTFMASEFLDWLVQEGEATTRKEAEQLCHRLMEHGIIQHVSNKHPFVDSNLLYQFRMNFRRRRRLMELLNEKSPSSQETHDSPFCLRKQSHDNRKSTSFMSVSPSKEIKIVSAVRRSSMSSCGSSGYFSSSPTLSSSPPVLCNPKSVLKRPVTSEELLTPGAPYARKTFTIVGDAVGWGFVVRGSKPCHIQAVDPSGPAAAAGMKVCQFVVSVNGLNVLHVDYRTVSNLILTGPRTIVMEVMEELECMASGRPEELWEAVVGAAERFRARTGTELVLLTAAPPPPPRPGPCAYAAHGRGALAEAARRCLHDIALAHRAATAARPPAPPPAPQPPSPTPSPPRPTLAREDNEEDEDEPTETETSGEQLGISDNGGLFVMDEDATLQDLPPFCESDPESTDDGSLSEETPAGPPTCSVPPASALPTQQYAKSLPVSVPVWGFKEKRTEARSSDEENGPPSSPDLDRIAASMRALVLREAEDTQVFGDLPRPRLNTSDFQKLKRKY TTX4GLS TT Clinical trial TTVH0YQ ID TTVH0YQ TTVH0YQ TN Mycobacterium Fusion protein Rv2608-Rv3619-Rv3620-Rv1813 (MycB antigens) TTVH0YQ UP P9WHZ5-P0DOA7-P9WNI3-P9WLS1 TTVH0YQ UC PPE42_MYCTU-ESXV_MYCTU-ESXW_MYCTU-Y1813_MYCTU TTVH0YQ SN Mycobacterium Fusion protein PPE42-esxV-esxW-MTY16F9.01 TTVH0YQ GN MycB antigens TTVH0YQ FC Invovled in immune response. TTVH0YQ SQ MTSRFMTDPHAMRDMAGRFEVHAQTVEDEARRMWASAQNISGAGWSGMAEATSLDTMTQMNQAFRNIVNMLHGVRDGLVRDANNYEQQEQASQQILSSMTINYQFGDVDAHGAMIRAQAGSLEAEHQAIISDVLTASDFWGGAGSAACQGFITQLGRNFQVIYEQANAHGQKVQAAGNNMAQTDSAVGSSWAMNFAVLPPEVNSARIFAGAGLGPMLAAASAWDGLAEELHAAAGSFASVTTGLAGDAWHGPASLAMTRAASPYVGWLNTAAGQAAQAAGQARLAASAFEATLAATVSPAMVAANRTRLASLVAANLLGQNAPAIAAAEAEYEQIWAQDVAAMFGYHSAASAVATQLAPIQEGLQQQLQNVLAQLASGNLGSGNVGVGNIGNDNIGNANIGFGNRGDANIGIGNIGDRNLGIGNTGNWNIGIGITGNGQIGFGKPANPDVLVVGNGGPGVTALVMGGTDSLLPLPNIPLLEYAARFITPVHPGYTATFLETPSQFFPFTGLNSLTYDVSVAQGVTNLHTAIMAQLAAGNEVVVFGTSQSATIATFEMRYLQSLPAHLRPGLDELSFTLTGNPNRPDGGILTRFGFSIPQLGFTLSGATPADAYPTVDYAFQYDGVNDFPKYPLNVFATANAIAGILFLHSGLIALPPDLASGVVQPVSSPDVLTTYILLPSQDLPLLVPLRAIPLLGNPLADLIQPDLRVLVELGYDRTAHQDVPSPFGLFPDVDWAEVAADLQQGAVQGVNDALSGLGLPPPWQPALPRLFMITNLRRRTAMAAAGLGAALGLGILLVPTVDAHLANGSMSEVMMSEIAGLPIPPIIHYGAIAYAPSGASGKAWHQRTPARAEQVALEKCGDKTCKVVSRFTRCGAVAYNGSKYQGGTGLTRRAAEDDAVNRLEGGRIVNWACN TTVH0YQ TT Clinical trial TTTLB3R ID TTTLB3R TTTLB3R TN Mycobacterium Membrane protein mmpL3 (MycB mmpL3) TTTLB3R UP P9WJV5 TTTLB3R UC MMPL3_MYCTU TTTLB3R SN Trehalose monomycolate exporter MmpL3; TMM exporter MmpL3 TTTLB3R GN MycB mmpL3 TTTLB3R FC Transports trehalose monomycolate (TMM) across the inner membrane. Could also be part of a heme-iron acquisition system. TTTLB3R SQ MFAWWGRTVYRYRFIVIGVMVALCLGGGVFGLSLGKHVTQSGFYDDGSQSVQASVLGDQVYGRDRSGHIVAIFQAPAGKTVDDPAWSKKVVDELNRFQQDHPDQVLGWAGYLRASQATGMATADKKYTFVSIPLKGDDDDTILNNYKAIAPDLQRLDGGTVKLAGLQPVAEALTGTIATDQRRMEVLALPLVAVVLFFVFGGVIAAGLPVMVGGLCIAGALGIMRFLAIFGPVHYFAQPVVSLIGLGIAIDYGLFIVSRFREEIAEGYDTETAVRRTVITAGRTVTFSAVLIVASAIGLLLFPQGFLKSLTYATIASVMLSAILSITVLPACLGILGKHVDALGVRTLFRVPFLANWKISAAYLNWLADRLQRTKTREEVEAGFWGKLVNRVMKRPVLFAAPIVIIMILLIIPVGKLSLGGISEKYLPPTNSVRQAQEEFDKLFPGYRTNPLTLVIQTSNHQPVTDAQIADIRSKAMAIGGFIEPDNDPANMWQERAYAVGASKDPSVRVLQNGLINPADASKKLTELRAITPPKGITVLVGGTPALELDSIHGLFAKMPLMVVILLTTTIVLMFLAFGSVVLPIKATLMSALTLGSTMGILTWIFVDGHFSKWLNFTPTPLTAPVIGLIIALVFGLSTDYEVFLVSRMVEARERGMSTQEAIRIGTAATGRIITAAALIVAVVAGAFVFSDLVMMKYLAFGLMAALLLDATVVRMFLVPSVMKLLGDDCWWAPRWARRLQTRIGLGEIHLPDERKRPVSNGRPARPPVTAGLVAARAAGDPRPPHDPTHPLAESPRPARSSPASSPELTPALEATAAPAAPSGASTTRMQIGSSTEPPTTRLAAAGRSVQSPASTPPPTPTPPSAPSAGQTRAMPLAANRSTDAAGDPAEPTAALPIIRSDGDDSEAATEQLNARGTSDKTRQRRRGGGALSAQDLLRREGRL TTTLB3R TT Clinical trial TT70N8V ID TT70N8V TT70N8V TN Myeloid inhibitory C-type lectin-like receptor (CD371) TT70N8V UP Q5QGZ9 TT70N8V UC CL12A_HUMAN TT70N8V SN MICL; Dendritic cell-associated lectin 2; DCAL2; DCAL-2; CLL1; CLL-1; C-type lectin-like molecule 1; C-type lectin domain family 12 member A TT70N8V GN CLEC12A TT70N8V FC Cell surface receptor that modulates signaling cascades and mediates tyrosine phosphorylation of target MAP kinases. TT70N8V SQ MSEEVTYADLQFQNSSEMEKIPEIGKFGEKAPPAPSHVWRPAALFLTLLCLLLLIGLGVLASMFHVTLKIEMKKMNKLQNISEELQRNISLQLMSNMNISNKIRNLSTTLQTIATKLCRELYSKEQEHKCKPCPRRWIWHKDSCYFLSDDVQTWQESKMACAAQNASLLKINNKNALEFIKSQSRSYDYWLGLSPEEDSTRGMRVDNIINSSAWVIRNAPDLNNMYCGYINRLYVQYYHCTYKKRMICEKMANPVQLGSTYFREA TT70N8V TT Clinical trial TTWN7KV ID TTWN7KV TTWN7KV TN Na-K-Cl cotransporter (NKCC) TTWN7KV UP Q13621; P55011 TTWN7KV UC S12A1_HUMAN; S12A2_HUMAN TTWN7KV SN Solute carrier family 12; Na-K-Cl symporter; NKCC; Bumetanide-sensitive sodium-(potassium)-chloride cotransporter TTWN7KV GN SLC12A1; SLC12A2 TTWN7KV FC Electrically silent transporter system. Mediates sodium and chloride reabsorption. Plays a vital role in the regulation of ionic balance and cell volume. TTWN7KV SQ MSLNNSSNVFLDSVPSNTNRFQVSVINENHESSAAADDNTDPPHYEETSFGDEAQKRLRISFRPGNQECYDNFLQSGETAKTDASFHAYDSHTNTYYLQTFGHNTMDAVPKIEYYRNTGSISGPKVNRPSLLEIHEQLAKNVAVTPSSADRVANGDGIPGDEQAENKEDDQAGVVKFGWVKGVLVRCMLNIWGVMLFIRLSWIVGEAGIGLGVLIILLSTMVTSITGLSTSAIATNGFVRGGGAYYLISRSLGPEFGGSIGLIFAFANAVAVAMYVVGFAETVVDLLKESDSMMVDPTNDIRIIGSITVVILLGISVAGMEWEAKAQVILLVILLIAIANFFIGTVIPSNNEKKSRGFFNYQASIFAENFGPRFTKGEGFFSVFAIFFPAATGILAGANISGDLEDPQDAIPRGTMLAIFITTVAYLGVAICVGACVVRDATGNMNDTIISGMNCNGSAACGLGYDFSRCRHEPCQYGLMNNFQVMSMVSGFGPLITAGIFSATLSSALASLVSAPKVFQALCKDNIYKALQFFAKGYGKNNEPLRGYILTFLIAMAFILIAELNTIAPIISNFFLASYALINFSCFHASYAKSPGWRPAYGIYNMWVSLFGAVLCCAVMFVINWWAAVITYVIEFFLYVYVTCKKPDVNWGSSTQALSYVSALDNALELTTVEDHVKNFRPQCIVLTGGPMTRPALLDITHAFTKNSGLCICCEVFVGPRKLCVKEMNSGMAKKQAWLIKNKIKAFYAAVAADCFRDGVRSLLQASGLGRMKPNTLVIGYKKNWRKAPLTEIENYVGIIHDAFDFEIGVVIVRISQGFDISQVLQVQEELERLEQERLALEATIKDNECEEESGGIRGLFKKAGKLNITKTTPKKDGSINTSQSMHVGEFNQKLVEASTQFKKKQEKGTIDVWWLFDDGGLTLLIPYILTLRKKWKDCKLRIYVGGKINRIEEEKIVMASLLSKFRIKFADIHIIGDINIRPNKESWKVFEEMIEPYRLHESCKDLTTAEKLKRETPWKITDAELEAVKEKSYRQVRLNELLQEHSRAANLIVLSLPVARKGSISDLLYMAWLEILTKNLPPVLLVRGNHKNVLTFYS TTWN7KV TT Clinical trial TTVKOPM ID TTVKOPM TTVKOPM TN NEDD8-activating enzyme (NAE) TTVKOPM UP Q13564; Q8TBC4 TTVKOPM UC ULA1_HUMAN; UBA3_HUMAN TTVKOPM SN NEDD8-activating enzyme E1 TTVKOPM GN NAE1; UBA3 TTVKOPM FC Subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression. TTVKOPM SQ MAQLGKLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILKNENGAPEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEGQGNLPVRGTIPDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAEEYGLDTINKDEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL TTVKOPM TT Clinical trial TTRGWZC ID TTRGWZC TTRGWZC TN Osteoblast cadherin (CDH11) TTRGWZC UP P55287 TTRGWZC UC CAD11_HUMAN TTRGWZC SN OSF4; OSF-4; OBcadherin; OB-cadherin; Cadherin-11 TTRGWZC GN CDH11 TTRGWZC FC Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. TTRGWZC SQ MKENYCLQAALVCLGMLCHSHAFAPERRGHLRPSFHGHHEKGKEGQVLQRSKRGWVWNQFFVIEEYTGPDPVLVGRLHSDIDSGDGNIKYILSGEGAGTIFVIDDKSGNIHATKTLDREERAQYTLMAQAVDRDTNRPLEPPSEFIVKVQDINDNPPEFLHETYHANVPERSNVGTSVIQVTASDADDPTYGNSAKLVYSILEGQPYFSVEAQTGIIRTALPNMDREAKEEYHVVIQAKDMGGHMGGLSGTTKVTITLTDVNDNPPKFPQSVYQMSVSEAAVPGEEVGRVKAKDPDIGENGLVTYNIVDGDGMESFEITTDYETQEGVIKLKKPVDFETKRAYSLKVEAANVHIDPKFISNGPFKDTVTVKISVEDADEPPMFLAPSYIHEVQENAAAGTVVGRVHAKDPDAANSPIRYSIDRHTDLDRFFTINPEDGFIKTTKPLDREETAWLNITVFAAEIHNRHQEAKVPVAIRVLDVNDNAPKFAAPYEGFICESDQTKPLSNQPIVTISADDKDDTANGPRFIFSLPPEIIHNPNFTVRDNRDNTAGVYARRGGFSRQKQDLYLLPIVISDGGIPPMSSTNTLTIKVCGCDVNGALLSCNAEAYILNAGLSTGALIAILACIVILLVIVVLFVTLRRQKKEPLIVFEEEDVRENIITYDDEGGGEEDTEAFDIATLQNPDGINGFIPRKDIKPEYQYMPRPGLRPAPNSVDVDDFINTRIQEADNDPTAPPYDSIQIYGYEGRGSVAGSLSSLESATTDSDLDYDYLQNWGPRFKKLADLYGSKDTFDDDS TTRGWZC TT Clinical trial TT9T4AV ID TT9T4AV TT9T4AV TN Prostate stem cell antigen (PSCA) TT9T4AV UP O43653 TT9T4AV UC PSCA_HUMAN TT9T4AV SN UNQ206/PRO232 TT9T4AV GN PSCA TT9T4AV FC Has a cell-proliferation inhibition activity in vitro. May be involved in the regulation of cell proliferation. TT9T4AV SQ MAGLALQPGTALLCYSCKAQVSNEDCLQVENCTQLGEQCWTARIRAVGLLTVISKGCSLNCVDDSQDYYVGKKNITCCDTDLCNASGAHALQPAAAILALLPALGLLLWGPGQL TT9T4AV TT Clinical trial TTF4AVB ID TTF4AVB TTF4AVB TN Protein delta homolog 1 (DLK1) TTF4AVB UP P80370 TTF4AVB UC DLK1_HUMAN TTF4AVB SN pG2; DLK-1 TTF4AVB GN DLK1 TTF4AVB FC May have a role in neuroendocrine differentiation. TTF4AVB SQ MTATEALLRVLLLLLAFGHSTYGAECFPACNPQNGFCEDDNVCRCQPGWQGPLCDQCVTSPGCLHGLCGEPGQCICTDGWDGELCDRDVRACSSAPCANNRTCVSLDDGLYECSCAPGYSGKDCQKKDGPCVINGSPCQHGGTCVDDEGRASHASCLCPPGFSGNFCEIVANSCTPNPCENDGVCTDIGGDFRCRCPAGFIDKTCSRPVTNCASSPCQNGGTCLQHTQVSYECLCKPEFTGLTCVKKRALSPQQVTRLPSGYGLAYRLTPGVHELPVQQPEHRILKVSMKELNKKTPLLTEGQAICFTILGVLTSLVVLGTVGIVFLNKCETWVSNLRYNHMLRKKKNLLLQYNSGEDLAVNIIFPEKIDMTTFSKEAGDEEI TTF4AVB TT Clinical trial TTLK9NJ ID TTLK9NJ TTLK9NJ TN Pseudomonas PcrV protein type III (Pseudo pcrV) TTLK9NJ UP O30527 TTLK9NJ UC O30527_PSEAI TTLK9NJ SN Type III secretion protein PcrV; Pseudo Virulence-associated V antigen; Pseudo Low calcium response locus protein V; PcrV TTLK9NJ GN Pseudo pcrV TTLK9NJ FC Essential for cytotoxicity. Found both within the bacterial cytoplasm and localized extracellularly. TTLK9NJ SQ MEVRNLNAARELFLDELLAASAAPASAEQEELLALLRSERIVLAHAGQPLSEAQVLKALAWLLAANPSAPPGQGLEVLREVLQARRQPGAQWDLREFLVSAYFSLHGRLDEDVIGVYKDVLQTQDGKRKALLDELKALTAELKVYSVIQSQINAALSAKQGIRIDAGGIDLVDPTLYGYAVGDPRWKDSPEYALLSNLDTFSGKLSIKDFLSGSPKQSGELKGLSDEYPFEKDNNPVGNFATTVSDRSRPLNDKVNEKTTLLNDTSSRYNSAVEALNRFIQKYDSVLRDILSAI TTLK9NJ TT Clinical trial TTQ9K3Y ID TTQ9K3Y TTQ9K3Y TN Serine/threonine-protein kinase Raf (RAF) TTQ9K3Y UP P10398; P15056; P04049 TTQ9K3Y UC ARAF_HUMAN; BRAF_HUMAN; RAF1_HUMAN TTQ9K3Y SN Proto-oncogene Raf TTQ9K3Y GN ARAF; BRAF; RAF1 TTQ9K3Y FC Participate in the RAS-RAF-MEK-ERK signal transduction cascade, also referred to as the mitogen-activated protein kinase (MAPK) cascade. Activation of RAF kinases requires interaction with RAS-GTPases. TTQ9K3Y SQ MEPPRGPPANGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRQQFYHSVQDLSGGSRQHEAPSNRPLNELLTPQGPSPRTQHCDPEHFPFPAPANAPLQRIRSTSTPNVHMVSTTAPMDSNLIQLTGQSFSTDAAGSRGGSDGTPRGSPSPASVSSGRKSPHSKSPAEQRERKSLADDKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGSFGTVFRGRWHGDVAVKVLKVSQPTAEQAQAFKNEMQVLRKTRHVNILLFMGFMTRPGFAIITQWCEGSSLYHHLHVADTRFDMVQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGAQPLEQPSGSVLWMAAEVIRMQDPNPYSFQSDVYAYGVVLYELMTGSLPYSHIGCRDQIIFMVGRGYLSPDLSKISSNCPKAMRRLLSDCLKFQREERPLFPQILATIELLQRSLPKIERSASEPSLHRTQADELPACLLSAARLVP TTQ9K3Y TT Clinical trial TTKE96O ID TTKE96O TTKE96O TN Staphylococcus Five leukocidin toxins (Stap-coc lukF) TTKE96O UP P31715 TTKE96O UC LUKF_STAAU TTKE96O SN lukF TTKE96O GN Stap-coc lukF TTKE96O FC Leukocidin causes cytotoxic changes in polymorphonuclear leukocytes. Gamma-hemolysin causes hemolysis in red blood cells. TTKE96O SQ MKMNKLVKSSVATSMALLLLSGTANAEGKITPVSVKKVDDKVTLYKTTATADSDKFKISQILTFNFIKDKSYDKDTLVLKATGNINSGFVKPNPNDYDFSKLYWGAKYNVSISSQSNDSVNAVDYAPKNQNEEFQVQNTLGYTFGGDISISNGLSGGLNGNTAFSETINYKQESYRTLSRNTNYKNVGWGVEAHKIMNGWGPYGRDSFHPTYGNELFLAGRQSSAYAGQNFIAQHQMPLLSRSNFNPEFLSVLSHRQDRAKKSKITVTYQREMDLYQIRWNGFYWAGANYKNFKTRTFKSTYEIDWENHKVKLLDTKETENNK TTKE96O TT Clinical trial TT4V7ST ID TT4V7ST TT4V7ST TN Sterol O-acyltransferase (SOAT) TT4V7ST UP P35610; O75908 TT4V7ST UC SOAT1_HUMAN; SOAT2_HUMAN TT4V7ST SN Cholesterol acyltransferase; Acyl-coenzyme A:cholesterol acyltransferase; ACAT; ACACT TT4V7ST GN SOAT1; SOAT2 TT4V7ST FC Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa. TT4V7ST SQ MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAEELKPFFMKEVGSHFDDFVTNLIEKSASLDNGGCALTTFSVLEGEKNNHRAKDLRAPPEQGKIFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRLVLEFSLLSYAFGKFPTVVWTWWIMFLSTFSVPYFLFQHWATGYSKSSHPLIRSLFHGFLFMIFQIGVLGFGPTYVVLAYTLPPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYFLFAPTLIYRDSYPRNPTVRWGYVAMKFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVFNSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTWNVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAVFAVSAVVHEYALAVCLSFFYPVLFVLFMFFGMAFNFIVNDSRKKPIWNVLMWTSLFLGNGVLLCFYSQEWYARQHCPLKNPTFLDYVRPRSWTCRYVF TT4V7ST TT Clinical trial TTP6B8O ID TTP6B8O TTP6B8O TN T-cell antigen CD7 (CD7) TTP6B8O UP P09564 TTP6B8O UC CD7_HUMAN TTP6B8O SN Tp40; TP41; T-cell surface antigen Leu-9; T-cell leukemia antigen; LEU-9; GP40; CD7 molecule TTP6B8O GN CD7 TTP6B8O FC Not yet known. TTP6B8O SQ MAGPPRLLLLPLLLALARGLPGALAAQEVQQSPHCTTVPVGASVNITCSTSGGLRGIYLRQLGPQPQDIIYYEDGVVPTTDRRFRGRIDFSGSQDNLTITMHRLQLSDTGTYTCQAITEVNVYGSGTLVLVTEEQSQGWHRCSDAPPRASALPAPPTGSALPDPQTASALPDPPAASALPAALAVISFLLGLGLGVACVLARTQIKKLCSWRDKNSAACVVYEDMSHSRCNTLSSPNQYQ TTP6B8O TT Clinical trial TT2H5WQ ID TT2H5WQ TT2H5WQ TN Werner syndrome ATP-dependent helicase (WRN) TT2H5WQ UP Q14191 TT2H5WQ UC WRN_HUMAN TT2H5WQ SN DNA helicase, RecQ-like type 3; RecQ3; Exonuclease WRN; RecQ protein-like 2 TT2H5WQ GN WRN TT2H5WQ FC Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity). Plays a role in double-strand break repair after gamma-irradiation. TT2H5WQ EC EC 3.1.-.- TT2H5WQ SQ MSEKKLETTAQQRKCPEWMNVQNKRCAVEERKACVRKSVFEDDLPFLEFTGSIVYSYDASDCSFLSEDISMSLSDGDVVGFDMEWPPLYNRGKLGKVALIQLCVSESKCYLFHVSSMSVFPQGLKMLLENKAVKKAGVGIEGDQWKLLRDFDIKLKNFVELTDVANKKLKCTETWSLNSLVKHLLGKQLLKDKSIRCSNWSKFPLTEDQKLYAATDAYAGFIIYRNLEILDDTVQRFAINKEEEILLSDMNKQLTSISEEVMDLAKHLPHAFSKLENPRRVSILLKDISENLYSLRRMIIGSTNIETELRPSNNLNLLSFEDSTTGGVQQKQIREHEVLIHVEDETWDPTLDHLAKHDGEDVLGNKVERKEDGFEDGVEDNKLKENMERACLMSLDITEHELQILEQQSQEEYLSDIAYKSTEHLSPNDNENDTSYVIESDEDLEMEMLKHLSPNDNENDTSYVIESDEDLEMEMLKSLENLNSGTVEPTHSKCLKMERNLGLPTKEEEEDDENEANEGEEDDDKDFLWPAPNEEQVTCLKMYFGHSSFKPVQWKVIHSVLEERRDNVAVMATGYGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEYCSGNMGLLQQLEADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFDRPNLYLEVRRKTGNILQDLQPFLVKTSSHWEFEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNEKFRLYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQVQKASLGIMGTEKCCDNCRSRLDHCYSMDDSEDTSWDFGPQAFKLLSAVDILGEKFGIGLPILFLRGSNSQRLADQYRRHSLFGTGKDQTESWWKAFSRQLITEGFLVEVSRYNKFMKICALTKKGRNWLHKANTESQSLILQANEELCPKKLLLPSSKTVSSGTKEHCYNQVPVELSTEKKSNLEKLYSYKPCDKISSGSNISKKSIMVQSPEKAYSSSQPVISAQEQETQIVLYGKLVEARQKHANKMDVPPAILATNKILVDMAKMRPTTVENVKRIDGVSEGKAAMLAPLLEVIKHFCQTNSVQTDLFSSTKPQEEQKTSLVAKNKICTLSQSMAITYSLFQEKKMPLKSIAESRILPLMTIGMHLSQAVKAGCPLDLERAGLTPEVQKIIADVIRNPPVNSDMSKISLIRMLVPENIDTYLIHMAIEILKHGPDSGLQPSCDVNKRRCFPGSEEICSSSKRSKEEVGINTETSSAERKRRLPVWFAKGSDTSKKLMDKTKRGGLFS TT2H5WQ TT Literature-reported TT80ARU ID TT80ARU TT80ARU TN Ganglioside GD2 (GD2) TT80ARU UP Other Molecule TT80ARU UC NOUNIPROTAC TT80ARU SN Ganglioside G2; GD2 TT80ARU GN NO-GeName TT80ARU TT Clinical trial TTP03CE ID TTP03CE TTP03CE TN Hepatitis C virus microRNA miR-122 (HCV MIR122) TTP03CE UP microRNA/lncRNA TTP03CE UC NOUNIPROTAC TTP03CE BC Non-coding RNA target TTP03CE GN NO-GeName TTP03CE TT Clinical trial TT1GNRQ ID TT1GNRQ TT1GNRQ TN microRNA hsa-miR-155 (MIR155) TT1GNRQ UP microRNA/lncRNA TT1GNRQ UC NOUNIPROTAC TT1GNRQ BC Non-coding RNA target TT1GNRQ GN NO-GeName TT1GNRQ TT Clinical trial TT96IGO ID TT96IGO TT96IGO TN microRNA hsa-miR-34 (MIR34) TT96IGO UP microRNA/lncRNA TT96IGO UC NOUNIPROTAC TT96IGO BC Non-coding RNA target TT96IGO GN NO-GeName TT96IGO TT Clinical trial TTK938H ID TTK938H TTK938H TN Cytomegalovirus Deoxyribonucleic acid (CMV DNA) TTK938H UP Other molecule TTK938H UC NOUNIPROTAC TTK938H GN NO-GeName TTK938H TT Clinical trial TT8E7Z0 ID TT8E7Z0 TT8E7Z0 TN Free radical (FRD) TT8E7Z0 UP Other molecule TT8E7Z0 UC NOUNIPROTAC TT8E7Z0 GN NO-GeName TT8E7Z0 TT Clinical trial TT0OV9N ID TT0OV9N TT0OV9N TN Haematin (HA) TT0OV9N UP Other molecule TT0OV9N UC NOUNIPROTAC TT0OV9N GN NO-GeName TT0OV9N TT Clinical trial TTZYW5V ID TTZYW5V TTZYW5V TN Hepatitis C virus Deoxyribonucleic acid (HCV DNA) TTZYW5V UP Other molecule TTZYW5V UC NOUNIPROTAC TTZYW5V GN NO-GeName TTZYW5V TT Clinical trial TTXPQW1 ID TTXPQW1 TTXPQW1 TN Hormone unspecific (HOM) TTXPQW1 UP Other molecule TTXPQW1 UC NOUNIPROTAC TTXPQW1 GN NO-GeName TTXPQW1 TT Clinical trial TTOVXHF ID TTOVXHF TTOVXHF TN Human Deoxyribonucleic acid minor groove (hDNA min) TTOVXHF UP Other molecule TTOVXHF UC NOUNIPROTAC TTOVXHF GN NO-GeName TTOVXHF TT Successful TT3NH7G ID TT3NH7G TT3NH7G TN Human immunodeficiency virus Deoxyribonucleic acid (HIV DNA) TT3NH7G UP Other molecule TT3NH7G UC NOUNIPROTAC TT3NH7G GN NO-GeName TT3NH7G TT Clinical trial TTZEX7Y ID TTZEX7Y TTZEX7Y TN Malondialdehyde (MDA) TTZEX7Y UP Other molecule TTZEX7Y UC NOUNIPROTAC TTZEX7Y GN NO-GeName TTZEX7Y TT Clinical trial TTAFD3Y ID TTAFD3Y TTAFD3Y TN Poly-N-acetyl glucosamine (PNAG) TTAFD3Y UP Other molecule TTAFD3Y UC NOUNIPROTAC TTAFD3Y GN NO-GeName TTAFD3Y TT Clinical trial TTHL6YX ID TTHL6YX TTHL6YX TN Progesterone (PG) TTHL6YX UP Other molecule TTHL6YX UC NOUNIPROTAC TTHL6YX GN NO-GeName TTHL6YX TT Clinical trial TT4ESMB ID TT4ESMB TT4ESMB TN Pseudomonas Lipopolysaccharide (Pseudo LPS) TT4ESMB UP Other molecule TT4ESMB UC NOUNIPROTAC TT4ESMB GN NO-GeName TT4ESMB TT Clinical trial TTE6QWF ID TTE6QWF TTE6QWF TN Staphylococcus Capsular polysaccharide CP5 (Stap-coc CP5) TTE6QWF UP Other molecule TTE6QWF UC NOUNIPROTAC TTE6QWF GN NO-GeName TTE6QWF TT Clinical trial TT4SVB7 ID TT4SVB7 TT4SVB7 TN Staphylococcus Capsular polysaccharide CP8 (Stap-coc CP8) TT4SVB7 UP Other molecule TT4SVB7 UC NOUNIPROTAC TT4SVB7 GN NO-GeName TT4SVB7 TT Clinical trial TTAD7UL ID TTAD7UL TTAD7UL TN Superoxide anion (SPA) TTAD7UL UP Other molecule TTAD7UL UC NOUNIPROTAC TTAD7UL GN NO-GeName TTAD7UL TT Clinical trial TTUZ2L5 ID TTUZ2L5 TTUZ2L5 TN Matrix metalloproteinase-3 (MMP-3) TTUZ2L5 UP P08254 TTUZ2L5 UC MMP3_HUMAN TTUZ2L5 BC Peptidase TTUZ2L5 SN Transin-1; Stromelysin-1; STMY1; SL-1; MMP-3 TTUZ2L5 GN MMP3 TTUZ2L5 FC Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. TTUZ2L5 EC EC 3.4.24.17 TTUZ2L5 PD 6N9D; 6MAV; 4JA1; 4G9L; 4DPE TTUZ2L5 SQ MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC TTUZ2L5 TT Patented-recorded TTUZ2L5 FM Peptidase TTUZ2L5 KE hsa04668:TNF signaling pathway; hsa05202:Transcriptional misregulation in cancer; hsa05323:Rheumatoid arthritis TTUZ2L5 RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures; R-HSA-2179392:EGFR Transactivation by Gastrin TTZHY6R ID TTZHY6R TTZHY6R TN Glycogen phosphorylase muscle form (GP) TTZHY6R UP P11217 TTZHY6R UC PYGM_HUMAN TTZHY6R BC Glycosyltransferases TTZHY6R SN Muscle glycogen phosphorylase; Glycogen phosphorylase, muscle form; Glycogen phosphorylase b TTZHY6R GN PYGM TTZHY6R FC Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. TTZHY6R EC EC 2.4.1.1 TTZHY6R PD 1Z8D TTZHY6R SQ MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERMDWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFVPRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDKLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEDYIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEAI TTZHY6R TT Patented-recorded TTZHY6R FM Glycogen phosphorylase family TTZHY6R KE hsa00500:Starch and sucrose metabolism; hsa01100:Metabolic pathways; hsa04910:Insulin signaling pathway; hsa04922:Glucagon signaling pathway TTT6LFV ID TTT6LFV TTT6LFV TN Histone deacetylase 8 (HDAC8) TTT6LFV UP Q9BY41 TTT6LFV UC HDAC8_HUMAN TTT6LFV BC Carbon-nitrogen hydrolase TTT6LFV SN Histone deacetylase-8; HDACL1; HD8; CDA07 TTT6LFV GN HDAC8 TTT6LFV FC Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). TTT6LFV EC EC 3.5.1.98 TTT6LFV PD 6HSK; 5VI6; 5THV; 5THU; 5THT TTT6LFV SQ MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV TTT6LFV TT Clinical trial TTT6LFV FM Carbon-nitrogen hydrolase TTT6LFV KE hsa05034:Alcoholism; hsa05203:Viral carcinogenesis TTT6LFV RC R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-3214815:HDACs deacetylate histones TTN9T81 ID TTN9T81 TTN9T81 TN Arachidonate 15-lipoxygenase (15-LOX) TTN9T81 UP P16050 TTN9T81 UC LOX15_HUMAN TTN9T81 BC Oxygenase TTN9T81 SN LOG15; Arachidonate omega-6 lipoxygenase; Arachidonate 12-lipoxygenase, leukocyte-type; 15-Lipoxygenase; 15-LOX-1; 12/15-lipoxygenase; 12-LOX TTN9T81 GN ALOX15 TTN9T81 FC Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. In addition to its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass. Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. TTN9T81 EC EC 1.13.11.33 TTN9T81 PD 2ABT TTN9T81 SQ MGLYRIRVSTGASLYAGSNNQVQLWLVGQHGEAALGKRLWPARGKETELKVEVPEYLGPLLFVKLRKRHLLKDDAWFCNWISVQGPGAGDEVRFPCYRWVEGNGVLSLPEGTGRTVGEDPQGLFQKHREEELEERRKLYRWGNWKDGLILNMAGAKLYDLPVDERFLEDKRVDFEVSLAKGLADLAIKDSLNVLTCWKDLDDFNRIFWCGQSKLAERVRDSWKEDALFGYQFLNGANPVVLRRSAHLPARLVFPPGMEELQAQLEKELEGGTLFEADFSLLDGIKANVILCSQQHLAAPLVMLKLQPDGKLLPMVIQLQLPRTGSPPPPLFLPTDPPMAWLLAKCWVRSSDFQLHELQSHLLRGHLMAEVIVVATMRCLPSIHPIFKLIIPHLRYTLEINVRARTGLVSDMGIFDQIMSTGGGGHVQLLKQAGAFLTYSSFCPPDDLADRGLLGVKSSFYAQDALRLWEIIYRYVEGIVSLHYKTDVAVKDDPELQTWCREITEIGLQGAQDRGFPVSLQARDQVCHFVTMCIFTCTGQHASVHLGQLDWYSWVPNAPCTMRLPPPTTKDATLETVMATLPNFHQASLQMSITWQLGRRQPVMVAVGQHEEEYFSGPEPKAVLKKFREELAALDKEIEIRNAKLDMPYEYLRPSVVENSVAI TTN9T81 TT Patented-recorded TTN9T81 FM Oxidoreductases acting on single donors TTN9T81 KE hsa00590:Arachidonic acid metabolism; hsa00591:Linoleic acid metabolism; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse TTEVCT0 ID TTEVCT0 TTEVCT0 TN Caspase-8 (CASP8) TTEVCT0 UP Q14790 TTEVCT0 UC CASP8_HUMAN TTEVCT0 BC Peptidase TTEVCT0 SN MORT1-associated CED-3 homolog; MCH5; MACH; ICE-like apoptotic protease 5; FLICE; FADD-like ICE; FADD-homologous ICE/CED-3-like protease; CASP-8; CAP4; Apoptotic protease Mch-5; Apoptotic cysteine protease TTEVCT0 GN CASP8 TTEVCT0 FC Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex. Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. TTEVCT0 EC EC 3.4.22.61 TTEVCT0 PD 5L08; 5JQE; 5H33; 5H31; 4ZBW TTEVCT0 SQ MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFTLRKKLVFPSD TTEVCT0 TT Patented-recorded TTEVCT0 FM Peptidase TTEVCT0 KE hsa04115:p53 signaling pathway; hsa04210:Apoptosis; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05010:Alzheimer's disease; hsa05016:Huntington's disease; hsa05134:Legionellosis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05168:Herpes simplex infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05416:Viral myocarditis TTEVCT0 RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-140534:Ligand-dependent caspase activation; R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-2562578:TRIF-mediated programmed cell death; R-HSA-264870:Caspase-mediated cleavage of cytoskeletal proteins; R-HSA-3371378:Regulation by c-FLIP; R-HSA-5213460:RIPK1-mediated regulated necrosis; R-HSA-5218900:CASP8 activity is inhibited; R-HSA-5357786:TNFR1-induced proapoptotic signaling; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5660668:CLEC7A/inflammasome pathway; R-HSA-5675482:Regulation of necroptotic cell death; R-HSA-69416:Dimerization of procaspase-8; R-HSA-75157:FasL/ CD95L signaling; R-HSA-75158:TRAIL signaling; R-HSA-933543:NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 TTF2LRI ID TTF2LRI TTF2LRI TN Cathepsin B (CTSB) TTF2LRI UP P07858 TTF2LRI UC CATB_HUMAN TTF2LRI BC Peptidase TTF2LRI SN Ctsb; Cathepsins B; Cathepsin-B; Cathepsin B1; CPSB; APPS; APP secretase TTF2LRI GN CTSB TTF2LRI FC Cleaves matrix extracellular phosphoglycoprotein MEPE. Has also been implicated in tumor invasion and metastasis. Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. TTF2LRI EC EC 3.4.22.1 TTF2LRI PD 6AY2; 5MBM; 5MBL; 3PBH; 3K9M TTF2LRI SQ MWQLWASLCCLLVLANARSRPSFHPLSDELVNYVNKRNTTWQAGHNFYNVDMSYLKRLCGTFLGGPKPPQRVMFTEDLKLPASFDAREQWPQCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHTNAHVSVEVSAEDLLTCCGSMCGDGCNGGYPAEAWNFWTRKGLVSGGLYESHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYSPTYKQDKHYGYNSYSVSNSEKDIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVTGEMMGGHAIRILGWGVENGTPYWLVANSWNTDWGDNGFFKILRGQDHCGIESEVVAGIPRTDQYWEKI TTF2LRI TT Preclinical TTF2LRI FM Peptidase TTF2LRI KE hsa04142:Lysosome; hsa04612:Antigen processing and presentation TTF2LRI RC R-HSA-1442490:Collagen degradation; R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures; R-HSA-2132295:MHC class II antigen presentation TTJOKD1 ID TTJOKD1 TTJOKD1 TN Cathepsin F (CTSF) TTJOKD1 UP Q9UBX1 TTJOKD1 UC CATF_HUMAN TTJOKD1 BC Peptidase TTJOKD1 SN CATSF TTJOKD1 GN CTSF TTJOKD1 FC Has also been implicated in tumor invasion and metastasis. Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. TTJOKD1 EC EC 3.4.22.41 TTJOKD1 PD 1M6D; 1D5U TTJOKD1 SQ MAPWLQLLSLLGLLPGAVAAPAQPRAASFQAWGPPSPELLAPTRFALEMFNRGRAAGTRAVLGLVRGRVRRAGQGSLYSLEATLEEPPCNDPMVCRLPVSKKTLLCSFQVLDELGRHVLLRKDCGPVDTKVPGAGEPKSAFTQGSAMISSLSQNHPDNRNETFSSVISLLNEDPLSQDLPVKMASIFKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQALDRGTAQYGVTKFSDLTEEEFRTIYLNTLLRKEPGNKMKQAKSVGDLAPPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSNAYSAIKNLGGLETEDDYSYQGHMQSCNFSAEKAKVYINDSVELSQNEQKLAAWLAKRGPISVAINAFGMQFYRHGISRPLRPLCSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSAVVD TTJOKD1 TT Patented-recorded TTJOKD1 FM Peptidase TTJOKD1 KE hsa04142:Lysosome TTJOKD1 RC R-HSA-2132295:MHC class II antigen presentation TTL4Q97 ID TTL4Q97 TTL4Q97 TN Cyclin-dependent kinase 5 (CDK5) TTL4Q97 UP Q00535 TTL4Q97 UC CDK5_HUMAN TTL4Q97 BC Kinase TTL4Q97 SN Tau protein kinase II catalytic subunit; TPKII catalytic subunit; Serine/threonine-protein kinase PSSALRE; Serine/threonine protein kinase PSSALRE; Proline-directed protein kinase F(A) (PDPK F(A)); Proline-directed protein kinase 33 kDa subunit; PDPK; Cyclin-dependent-like kinase 5; Cyclin-dependent kinase 5 (CDK5); Cell division protein kinase 5; CDKN5 TTL4Q97 GN CDK5 TTL4Q97 FC Interacts with D1 and D3-type G1 cyclins. Phosphorylates SRC, NOS3, VIM/vimentin, p35/CDK5R1, MEF2A, SIPA1L1, SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5, SYN1, DNM1, AMPH, SYNJ1, CDK16, RAC1, RHOA, CDC42, TONEBP/NFAT5, MAPT/TAU, MAP1B, histone H1, p53/TP53, HDAC1, APEX1, PTK2/FAK1, huntingtin/HTT, ATM, MAP2, NEFH and NEFM. Regulates several neuronal development and physiological processes including neuronal survival, migration and differentiation, axonal and neurite growth, synaptogenesis, oligodendrocyte differentiation, synaptic plasticity and neurotransmission, by phosphorylating key proteins. Activated by interaction with CDK5R1 (p35) and CDK5R2 (p39), especially in post-mitotic neurons, and promotes CDK5R1 (p35) expression in an autostimulation loop. Phosphorylates many downstream substrates such as Rho and Ras family small GTPases (e. g. PAK1, RAC1, RHOA, CDC42) or microtubule-binding proteins (e. g. MAPT/TAU, MAP2, MAP1B), and modulates actin dynamics to regulate neurite growth and/or spine morphogenesis. Phosphorylates also exocytosis associated proteins such as MCAM/MUC18, SEPT5, SYN1, and CDK16/PCTAIRE1 as well as endocytosis associated proteins such as DNM1, AMPH and SYNJ1 at synaptic terminals. In the mature central nervous system (CNS), regulates neurotransmitter movements by phosphorylating substrates associated with neurotransmitter release and synapse plasticity; synaptic vesicle exocytosis, vesicles fusion with the presynaptic membrane, and endocytosis. Promotes cell survival by activating anti-apoptotic proteins BCL2 and STAT3, and negatively regulating of JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response to genotoxic and oxidative stresses enhances its stabilization by preventing ubiquitin ligase-mediated proteasomal degradation, and induces transactivation of p53/TP53 target genes, thus regulating apoptosis. Phosphorylation of p35/CDK5R1 enhances its stabilization by preventing calpain-mediated proteolysis producing p25/CDK5R1 and avoiding ubiquitin ligase-mediated proteasomal degradation. During aberrant cell-cycle activity and DNA damage, p25/CDK5 activity elicits cell-cycle activity and double-strand DNA breaks that precedes neuronal death by deregulating HDAC1. DNA damage triggered phosphorylation of huntingtin/HTT in nuclei of neurons protects neurons against polyglutamine expansion as well as DNA damage mediated toxicity. Phosphorylation of PXN reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Negative regulator of Wnt/beta-catenin signaling pathway. Activator of the GAIT (IFN-gamma-activated inhibitor of translation) pathway, which suppresses expression of a post-transcriptional regulon of proinflammatory genes in myeloid cells; phosphorylates the linker domain of glutamyl-prolyl tRNA synthetase (EPRS) in a IFN-gamma-dependent manner, the initial event in assembly of the GAIT complex. Phosphorylation of SH3GLB1 is required for autophagy induction in starved neurons. Phosphorylation of TONEBP/NFAT5 in response to osmotic stress mediates its rapid nuclear localization. MEF2 is inactivated by phosphorylation in nucleus in response to neurotoxin, thus leading to neuronal apoptosis. APEX1 AP-endodeoxyribonuclease is repressed by phosphorylation, resulting in accumulation of DNA damage and contributing to neuronal death. NOS3 phosphorylation down regulates NOS3-derived nitrite (NO) levels. SRC phosphorylation mediates its ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. May regulate endothelial cell migration and angiogenesis via the modulation of lamellipodia formation. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. Proline-directed serine/threonine-protein kinase essential for neuronal cell cycle arrest and differentiation and may be involved in apoptotic cell death in neuronal diseases by triggering abortive cell cycle re-entry. TTL4Q97 EC EC 2.7.11.1 TTL4Q97 PD 4AU8; 3O0G; 1UNL; 1UNH; 1UNG TTL4Q97 SQ MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFCDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNLLINRNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPYPMYPATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDFCPP TTL4Q97 TT Patented-recorded TTL4Q97 FM Kinase TTL4Q97 KE hsa04360:Axon guidance; hsa05010:Alzheimer's disease; hsa05030:Cocaine addiction TTL4Q97 RC R-HSA-180024:DARPP-32 events; R-HSA-399956:CRMPs in Sema3A signaling; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTQWAU1 ID TTQWAU1 TTQWAU1 TN GSK3A messenger RNA (GSK3A mRNA) TTQWAU1 UP P49840 TTQWAU1 UC GSK3A_HUMAN TTQWAU1 BC mRNA target TTQWAU1 SN Serine/threonineprotein kinase GSK3A (mRNA); Serine/threonine-protein kinase GSK3A (mRNA); Glycogen synthase kinase3 alpha (mRNA); Glycogen synthase kinase 3 (mRNA); GSK3 alpha (mRNA); GSK-3 alpha (mRNA); GSK-3 (mRNA) TTQWAU1 GN GSK3A TTQWAU1 FC Requires primed phosphorylation of the majority of its substrates. Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. Regulates glycogen metabolism in liver, but not in muscle. May also mediate the development of insulin resistance by regulating activation of transcription factors. In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin. Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease. May be involved in the regulation of replication in pancreatic beta-cells. Is necessary for the establishment of neuronal polarity and axon outgrowth. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, leading to activate KAT5/TIP60 acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer. Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1. TTQWAU1 EC EC 2.7.11.26 TTQWAU1 PD 2DFM TTQWAU1 SQ MSGGGPSGGGPGGSGRARTSSFAEPGGGGGGGGGGPGGSASGPGGTGGGKASVGAMGGGVGASSSGGGPGGSGGGGSGGPGAGTSFPPPGVKLGRDSGKVTTVVATLGQGPERSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNLVLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDELRCLGTQLPNNRPLPPLFNFSAGELSIQPSLNAILIPPHLRSPAGTTTLTPSSQALTETPTSSDWQSTDATPTLTNSS TTQWAU1 TT Literature-reported TTQWAU1 FM mRNA target TTQWAU1 KE hsa04062:Chemokine signaling pathway; hsa04728:Dopaminergic synapse; hsa04932:Non-alcoholic fatty liver disease (NAFLD) TTQWAU1 RC R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-381038:XBP1(S) activates chaperone genes; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer TTYHPU6 ID TTYHPU6 TTYHPU6 TN Histone deacetylase 10 (HDAC10) TTYHPU6 UP Q969S8 TTYHPU6 UC HDA10_HUMAN TTYHPU6 BC Carbon-nitrogen hydrolase TTYHPU6 SN Polyamine deacetylase HDAC10; HD10 TTYHPU6 GN HDAC10 TTYHPU6 FC Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine. Histone deacetylase activity has been observed in vitro. Has also been shown to be involved in MSH2 deacetylation. The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak. May play a role in the promotion of late stages of autophagy, possibly autophagosome-lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells. May play a role in homologous recombination. May promote DNA mismatch repair. Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine. TTYHPU6 EC EC 3.5.1.48 TTYHPU6 SQ MGTALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQSALESIQSARAAQAPHWKSLQQQDVTAVPMSPSSHSPEGRPPPLLPGGPVCKAAASAPSSLLDQPCLCPAPSVRTAVALTTPDITLVLPPDVIQQEASALREETEAWARPHESLAREEALTALGKLLYLLDGMLDGQVNSGIAATPASAAAATLDVAVRRGLSHGAQRLLCVALGQLDRPPDLAHDGRSLWLNIRGKEAAALSMFHVSTPLPVMTGGFLSCILGLVLPLAYGFQPDLVLVALGPGHGLQGPHAALLAAMLRGLAGGRVLALLEENSTPQLAGILARVLNGEAPPSLGPSSVASPEDVQALMYLRGQLEPQWKMLQCHPHLVA TTYHPU6 TT Patented-recorded TTT2SVW ID TTT2SVW TTT2SVW TN PPAR-gamma messenger RNA (PPARG mRNA) TTT2SVW UP P37231 TTT2SVW UC PPARG_HUMAN TTT2SVW BC mRNA target TTT2SVW SN Transcription factor PPAR gamma receptor (mRNA); Peroxisome proliferator-activated receptor gamma (mRNA); PPARgamma (mRNA); PPAR-gamma (mRNA); Nuclear receptor subfamily 1 group C member 3 (mRNA); NR1C3 (mRNA) TTT2SVW GN PPARG TTT2SVW FC Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels. Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. TTT2SVW PD 6MD4; 6MD2; 6MD1; 6MD0; 6MCZ TTT2SVW SQ MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY TTT2SVW TT Literature-reported TTT2SVW FM mRNA target TTT2SVW KE hsa03320:PPAR signaling pathway; hsa04152:AMPK signaling pathway; hsa04380:Osteoclast differentiation; hsa05016:Huntington's disease; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05216:Thyroid cancer TTT2SVW RC R-HSA-1989781:PPARA activates gene expression; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-383280:Nuclear Receptor transcription pathway TT056SO ID TT056SO TT056SO TN Stress-activated protein kinase JNK3 (JNK3) TT056SO UP P53779 TT056SO UC MK10_HUMAN TT056SO BC Kinase TT056SO SN Stress-activated protein kinase 1b; SAPK1b; PRKM10; Mitogen-activated protein kinase 10; MAPK 10; MAP kinase p49 3F12; MAP kinase 10; JNK3A; C-Jun N-terminal kinase 3 TT056SO GN MAPK10 TT056SO FC Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the amyloid-beta precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the photic regulation of the circadian clock. Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. TT056SO EC EC 2.7.11.24 TT056SO PD 6EQ9; 6EMH; 6EKD; 4Z9L; 4Y5H TT056SO SQ MSLHFLYYCSEPTLDVKIAFCQGFDKQVDVSYIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMNSEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR TT056SO TT Patented-recorded TT056SO FM Kinase TT056SO KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04024:cAMP signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04141:Protein processing in endoplasmic reticulum; hsa04310:Wnt signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04723:Retrograde endocannabinoid signaling; hsa04728:Dopaminergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04917:Prolactin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05210:Colorectal cancer; hsa05212:Pancreatic cancer; hsa05231:Choline metabolism in cancer TT056SO RC R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-450321:JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1; R-HSA-450341:Activation of the AP-1 family of transcription factors TT2F4OL ID TT2F4OL TT2F4OL TN Tissue transglutaminase (TG2) TT2F4OL UP P21980 TT2F4OL UC TGM2_HUMAN TT2F4OL BC Acyltransferase TT2F4OL SN Transglutaminase-2; Transglutaminase H; Transglutaminase C; Transglutaminase 2; Tranglutaminase 2; TTg; TGase-H; TGase-2; TGase H; TGase C; TGC; TG(C)Protein-glutamine gamma-glutamyltransferase; TG(C); Protein-glutamine gamma-glutamyltransferase 2 TT2F4OL GN TGM2 TT2F4OL FC Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. TT2F4OL EC EC 2.3.2.13 TT2F4OL PD 6A8P; 4PYG; 3S3S; 3S3P; 3S3J TT2F4OL SQ MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYEASVDSLTFSVVTGPAPSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYVLTQQGFIYQGSAKFIKNIPWNFGQFEDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLNLEPFSEKSVPLCILYEKYRDCLTESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPDPVEAGEEVKVRMDLLPLHMGLHKLVVNFESDKLKAVKGFRNVIIGPA TT2F4OL TT Preclinical TT2F4OL FM Transglutaminase superfamily TT2F4OL KE hsa05016:Huntington's disease TT1OPCB ID TT1OPCB TT1OPCB TN Caspase-6 (CASP6) TT1OPCB UP P55212 TT1OPCB UC CASP6_HUMAN TT1OPCB BC Peptidase TT1OPCB SN MCH2; Caspase-6 subunit p18; Caspase-6 subunit p11; CASP-6; Apoptotic protease Mch-2 TT1OPCB GN CASP6 TT1OPCB FC Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death. Involved in the activation cascade of caspases responsible for apoptosis execution. TT1OPCB EC EC 3.4.22.59 TT1OPCB PD 6DEV; 6DEU; 4NBN; 4NBL; 4NBK TT1OPCB SQ MSSASGLRRGHPAGGEENMTETDAFYKREMFDPAEKYKMDHRRRGIALIFNHERFFWHLTLPERRGTCADRDNLTRRFSDLGFEVKCFNDLKAEELLLKIHEVSTVSHADADCFVCVFLSHGEGNHIYAYDAKIEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVVDNQTEKLDTNITEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSQRRVDFCKDPSAIGKKQVPCFASMLTKKLHFFPKSN TT1OPCB TT Patented-recorded TT1OPCB FM Peptidase C14A family TT1OPCB KE hsa04210:Apoptosis TTSD9T1 ID TTSD9T1 TTSD9T1 TN Cathepsin V (CTSV) TTSD9T1 UP O60911 TTSD9T1 UC CATL2_HUMAN TTSD9T1 BC Peptidase TTSD9T1 SN UNQ268/PRO305; Cathepsin U; Cathepsin L2; CTSU; CTSL2; CATL2 TTSD9T1 GN CTSV TTSD9T1 FC May have an important role in corneal physiology. Cysteine protease. TTSD9T1 EC EC 3.4.22.43 TTSD9T1 PD 3KFQ; 3H6S; 1FH0 TTSD9T1 SQ MNLSLVLAAFCLGIASAVPKFDQNLDTKWYQWKATHRRLYGANEEGWRRAVWEKNMKMIELHNGEYSQGKHGFTMAMNAFGDMTNEEFRQMMGCFRNQKFRKGKVFREPLFLDLPKSVDWRKKGYVTPVKNQKQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRPQGNQGCNGGFMARAFQYVKENGGLDSEESYPYVAVDEICKYRPENSVANDTGFTVVAPGKEKALMKAVATVGPISVAMDAGHSSFQFYKSGIYFEPDCSSKNLDHGVLVVGYGFEGANSNNSKYWLVKNSWGPEWGSNGYVKIAKDKNNHCGIATAASYPNV TTSD9T1 TT Patented-recorded TTSD9T1 FM Peptidase TTSD9T1 KE hsa04142:Lysosome TTSD9T1 RC R-HSA-1236977:Endosomal/Vacuolar pathway; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures; R-HSA-2132295:MHC class II antigen presentation TTE6YDG ID TTE6YDG TTE6YDG TN CDC-like kinase 1 (CLK1) TTE6YDG UP P49759 TTE6YDG UC CLK1_HUMAN TTE6YDG BC Kinase TTE6YDG SN Dual specificity protein kinase CLK1; CLK; CDClike kinase 1 TTE6YDG GN CLK1 TTE6YDG FC Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA. Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. TTE6YDG EC EC 2.7.12.1 TTE6YDG PD 6RAA; 6Q8P; 6Q8K; 6I5L; 6I5K TTE6YDG SQ MRHSKRTYCPDWDDKDWDYGKWRSSSSHKRRKRSHSSAQENKRCKYNHSKMCDSHYLESRSINEKDYHSRRYIDEYRNDYTQGCEPGHRQRDHESRYQNHSSKSSGRSGRSSYKSKHRIHHSTSHRRSHGKSHRRKRTRSVEDDEEGHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRITLREALKHPFFDLLKKSI TTE6YDG TT Patented-recorded TTXI2RA ID TTXI2RA TTXI2RA TN Coagulation factor XIIIA (F13A1) TTXI2RA UP P00488 TTXI2RA UC F13A_HUMAN TTXI2RA BC Acyltransferase TTXI2RA SN Transglutaminase A chain; Protein-glutamine gamma-glutamyltransferase A chain; F13A; Coagulation factor XIII A chain TTXI2RA GN F13A1 TTXI2RA FC Cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. TTXI2RA EC EC 2.3.2.13 TTXI2RA PD 5MHO; 5MHN; 5MHM; 5MHL; 4KTY TTXI2RA SQ MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDTNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETDTYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGNVNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKHGHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITDTYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITFRNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLLEQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVQFTNPLKETLRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYGELDVQIQRRPSM TTXI2RA TT Patented-recorded TTXI2RA FM Transglutaminase superfamily TTXI2RA KE hsa04610:Complement and coagulation cascades TTBJR4L ID TTBJR4L TTBJR4L TN Cyclin-dependent kinase 8 (CDK8) TTBJR4L UP P49336 TTBJR4L UC CDK8_HUMAN TTBJR4L BC Kinase TTBJR4L SN Protein kinase K35; Mediator of RNA polymerase II transcription subunit CDK8; Mediator complex subunit CDK8; Cell division protein kinase 8 TTBJR4L GN CDK8 TTBJR4L FC Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex. Phosphorylates CCNH leading to down-regulation of the TFIIH complex and transcriptional repression. Recruited through interaction with MAML1 to hyperphosphorylate the intracellular domain of NOTCH, leading to its degradation. Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. TTBJR4L EC EC 2.7.11.22 TTBJR4L PD 5XS2; 5XQX; 5IDP; 5IDN; 5ICP TTBJR4L SQ MDYDFKVKLSSERERVEDLFEYEGCKVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRELKHPNVISLQKVFLSHADRKVWLLFDYAEHDLWHIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKMPEHSTLMKDFRRNTYTNCSLIKYMEKHKVKPDSKAFHLLQKLLTMDPIKRITSEQAMQDPYFLEDPLPTSDVFAGCQIPYPKREFLTEEEPDDKGDKKNQQQQQGNNHTNGTGHPGNQDSSHTQGPPLKKVRVVPPTTTSGGLIMTSDYQRSNPHAAYPNPGPSTSQPQSSMGYSATSQQPPQYSHQTHRY TTBJR4L TT Clinical trial TTBJR4L FM Kinase TTBJR4L RC R-HSA-1989781:PPARA activates gene expression; R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2173796:SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation TTJUALD ID TTJUALD TTJUALD TN DNA [cytosine-5]-methyltransferase 3A (DNMT3A) TTJUALD UP Q9Y6K1 TTJUALD UC DNM3A_HUMAN TTJUALD BC Methyltransferase TTJUALD SN M.HsaIIIA; Dnmt3a; DNA methyltransferase HsaIIIA; DNA MTase HsaIIIA; DNA (cytosine-5)-methyltransferase 3A TTJUALD GN DNMT3A TTJUALD FC DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity. Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. TTJUALD EC EC 2.1.1.37 TTJUALD PD 6F57; 6BRR; 5YX2; 4U7T; 4U7P TTJUALD SQ MPAMPSSGPGDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGRPGRKRKHPPVESGDTPKDPAVISKSPSMAQDSGASELLPNGDLEKRSEPQPEEGSPAGGQKGGAPAEGEGAAETLPEASRAVENGCCTPKEGRGAPAEAGKEQKETNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAGMNAVEENQGPGESQKVEEASPPAVQQPTDPASPTVATTPEPVGSDAGDKNATKAGDDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTAEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV TTJUALD TT Patented-recorded TTJUALD FM Class I-like SAM-binding methyltransferase superfamily TTJUALD KE hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways; hsa05206:MicroRNAs in cancer TTYM8DJ ID TTYM8DJ TTYM8DJ TN Ectonucleoside triphosphate diphosphohydrolase 1 (CD39) TTYM8DJ UP P49961 TTYM8DJ UC ENTP1_HUMAN TTYM8DJ BC Acid anhydride hydrolase TTYM8DJ SN NTPDase1; NTPDase 1; Lymphoid cell activation antigen; Ecto-nucleotidase CD-39; Ecto-apyrase; Ecto-ATPase 1; Ecto-ATPDase 1; Ecto-ATP diphosphohydrolase 1; Ecto-ATP diphosphohydrolase; CD39 antigen; ATPDase TTYM8DJ GN ENTPD1 TTYM8DJ FC Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well. In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. TTYM8DJ EC EC 3.6.1.5 TTYM8DJ SQ MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTPCTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAFSAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYILSLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFLMVLFSLVLFTVAIIGLLIFHKPSYFWKDMV TTYM8DJ TT Clinical trial TTYM8DJ FM Acid anhydrides hydrolase TTYM8DJ KE hsa00230:Purine metabolism; hsa00240:Pyrimidine metabolism; hsa05169:Epstein-Barr virus infection TTSCIM2 ID TTSCIM2 TTSCIM2 TN Extracellular lysophospholipase D (E-NPP2) TTSCIM2 UP Q13822 TTSCIM2 UC ENPP2_HUMAN TTSCIM2 BC Phosphoric diester hydrolase TTSCIM2 SN LysoPLD; Ectonucleotide pyrophosphatase/phosphodiesterase family member 2; E-NPP 2; Autotaxin; ATX TTSCIM2 GN ENPP2 TTSCIM2 FC Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development (Probable). Tumor cell motility-stimulating factor. TTSCIM2 EC EC 3.1.4.39 TTSCIM2 PD 5MHP; 5M7M; 5KXA; 4ZGA; 4ZG9 TTSCIM2 SQ MARRSSFQSCQIISLFTFAVGVNICLGFTAHRIKRAEGWEEGPPTVLSDSPWTNISGSCKGRCFELQEAGPPDCRCDNLCKSYTSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKAAECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLRGREKFNHRWWGGQPLWITATKQGVKAGTFFWSVVIPHERRILTILQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAKYDPKAIIANLTCKKPDQHFKPYLKQHLPKRLHYANNRRIEDIHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTMPEEVTRPNYPGIMYLQSDFDLGCTCDDKVEPKNKLDELNKRLHTKGSTEERHLLYGRPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVSPSFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDKIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNEESCNSSEDESKWVEELMKMHTARVRDIEHLTSLDFFRKTSRSYPEILTLKTYLHTYESEI TTSCIM2 TT Patented-recorded TTSCIM2 FM Nucleotide pyrophosphatase/phosphodiesterase family TTSCIM2 KE hsa00565:Ether lipid metabolism TTHWMFZ ID TTHWMFZ TTHWMFZ TN Fatty acid-binding protein 4 (FABP4) TTHWMFZ UP P15090 TTHWMFZ UC FABP4_HUMAN TTHWMFZ BC Fatty acid binding protein TTHWMFZ SN Fatty acid-binding protein, adipocyte; Adipocyte-type fatty acid-binding protein; Adipocyte lipid-binding protein; Adipocyte fatty-acid-binding protein; Adipocyte fatty binding protein; ALBP; AFABP; A-FABP TTHWMFZ GN FABP4 TTHWMFZ FC Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus. Lipid transport protein in adipocytes. TTHWMFZ PD 6AYL; 5Y13; 5Y12; 5Y0X; 5Y0G TTHWMFZ SQ MCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA TTHWMFZ TT Patented-recorded TTHWMFZ FM Calycin family TTHWMFZ KE hsa03320:PPAR signaling pathway TTHWMFZ RC R-HSA-163560:Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation TTNT2S6 ID TTNT2S6 TTNT2S6 TN Fatty acid-binding protein 5 (FABP5) TTNT2S6 UP Q01469 TTNT2S6 UC FABP5_HUMAN TTNT2S6 BC Fatty acid binding protein TTNT2S6 SN Psoriasis-associated fatty acid-binding protein homolog; PA-FABP; Fatty acid-binding protein, epidermal; Fatty Acid BindingProtein mal1; Epidermal-type fatty acid-binding protein; E-FABP TTNT2S6 GN FABP5 TTNT2S6 FC Intracellular carrier for long-chain fatty acids and related active lipids, such as the endocannabinoid, that regulates the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors. Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation. May be involved in keratinocyte differentiation. TTNT2S6 PD 5UR9; 5HZ5; 4LKT; 4LKP; 4AZR TTNT2S6 SQ MATVQQLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTVCNFTDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNVTCTRIYEKVE TTNT2S6 TT Patented-recorded TTNT2S6 FM Fatty acid bindingprotein TTNT2S6 KE hsa03320:PPAR signaling pathway TTNT2S6 RC R-HSA-163560:Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis TT9P6OW ID TT9P6OW TT9P6OW TN G2/mitotic-specific cyclin B1 (CCNB1) TT9P6OW UP P14635 TT9P6OW UC CCNB1_HUMAN TT9P6OW BC Eukaryotic nuclear pore complex TT9P6OW SN G2/mitotic-specific cyclin-B1; Cyclin B1; CCNB TT9P6OW GN CCNB1 TT9P6OW FC Essential for the control of the cell cycle at the G2/M (mitosis) transition. TT9P6OW PD 6GU4; 6GU3; 6GU2; 5LQF; 5HQ0 TT9P6OW SQ MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTVKNKYATSKHAKISTLPQLNSALVQDLAKAVAKV TT9P6OW TT Patented-recorded TT9P6OW KE hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04114:Oocyte meiosis; hsa04115:p53 signaling pathway; hsa04914:Progesterone-mediated oocyte maturation TT9P6OW RC R-HSA-156711:Polo-like kinase mediated events; R-HSA-162658:Golgi Cisternae Pericentriolar Stack Reorganization; R-HSA-176408:Regulation of APC/C activators between G1/S and early anaphase; R-HSA-176412:Phosphorylation of the APC/C; R-HSA-176417:Phosphorylation of Emi1; R-HSA-2299718:Condensation of Prophase Chromosomes; R-HSA-2465910:MASTL Facilitates Mitotic Progression; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-2514853:Condensation of Prometaphase Chromosomes; R-HSA-2565942:Regulation of PLK1 Activity at G2/M Transition; R-HSA-2980767:Activation of NIMA Kinases NEK9, NEK6, NEK7; R-HSA-380320:Recruitment of NuMA to mitotic centrosomes; R-HSA-4419969:Depolymerisation of the Nuclear Lamina; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition; R-HSA-69478:G2/M DNA replication checkpoint; R-HSA-75035:Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex TTEP6RV ID TTEP6RV TTEP6RV TN Glutathione reductase (GR) TTEP6RV UP P00390 TTEP6RV UC GSHR_HUMAN TTEP6RV BC Sulfur donor oxidoreductase TTEP6RV SN Glutathione reductase, mitochondrial; GRase; GRD1; GLUR TTEP6RV GN GSR TTEP6RV FC Maintains high levels of reduced glutathione in the cytosol. TTEP6RV EC EC 1.8.1.7 TTEP6RV PD 5GRT; 4GRT; 4GR1; 3SQP; 3GRT TTEP6RV SQ MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAGAVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR TTEP6RV TT Patented-recorded TTEP6RV FM Oxidoreductases acting on a sulfur group of donors TTEP6RV KE hsa00480:Glutathione metabolism; hsa04918:Thyroid hormone synthesis TTE6GTB ID TTE6GTB TTE6GTB TN Kallikrein-7 (KLK7) TTE6GTB UP P49862 TTE6GTB UC KLK7_HUMAN TTE6GTB BC Peptidase TTE6GTB SN hK7; Stratum corneum chymotryptic enzyme; Serine protease 6; SCCE; PRSS6; HSCCE TTE6GTB GN KLK7 TTE6GTB FC Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines. May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. TTE6GTB EC EC 3.4.21.117 TTE6GTB PD 5YJK; 5Y9L; 5FAH; 3BSQ; 2QXJ TTE6GTB SQ MARSLLLPLQILLLSLALETAGEEAQGDKIIDGAPCARGSHPWQVALLSGNQLHCGGVLVNERWVLTAAHCKMNEYTVHLGSDTLGDRRAQRIKASKSFRHPGYSTQTHVNDLMLVKLNSQARLSSMVKKVRLPSRCEPPGTTCTVSGWGTTTSPDVTFPSDLMCVDVKLISPQDCTKVYKDLLENSMLCAGIPDSKKNACNGDSGGPLVCRGTLQGLVSWGTFPCGQPNDPGVYTQVCKFTKWINDTMKKHR TTE6GTB TT Patented-recorded TTE6GTB FM Peptidase TTE6GTB RC R-HSA-1474228:Degradation of the extracellular matrix TTJOW1I ID TTJOW1I TTJOW1I TN Mannoside acetylglucosaminyltransferase 2 (MGAT2) TTJOW1I UP Q10469 TTJOW1I UC MGAT2_HUMAN TTJOW1I BC Glycosyltransferases TTJOW1I SN N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II; GlcNAc-T II; GNT-II; Beta-1,2-N-acetylglucosaminyltransferase II; Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase TTJOW1I GN MGAT2 TTJOW1I FC Catalyzes the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal mannose moiety in the core structure of the nascent N-linked glycan chain, giving rise to the second branch in complex glycans. Plays an essential role in protein N-glycosylation. TTJOW1I EC EC 2.4.1.143 TTJOW1I PD 5VCS; 5VCR; 5VCM TTJOW1I SQ MRFRIYKRKVLILTLVVAACGFVLWSSNGRQRKNEALAPPLLDAEPARGAGGRGGDHPSVAVGIRRVSNVSAASLVPAVPQPEADNLTLRYRSLVYQLNFDQTLRNVDKAGTWAPRELVLVVQVHNRPEYLRLLLDSLRKAQGIDNVLVIFSHDFWSTEINQLIAGVNFCPVLQVFFPFSIQLYPNEFPGSDPRDCPRDLPKNAALKLGCINAEYPDSFGHYREAKFSQTKHHWWWKLHFVWERVKILRDYAGLILFLEEDHYLAPDFYHVFKKMWKLKQQECPECDVLSLGTYSASRSFYGMADKVDVKTWKSTEHNMGLALTRNAYQKLIECTDTFCTYDDYNWDWTLQYLTVSCLPKFWKVLVPQIPRIFHAGDCGMHHKKTCRPSTQSAQIESLLNNNKQYMFPETLTISEKFTVVAISPPRKNGGWGDIRDHELCKSYRRLQ TTJOW1I TT Patented-recorded TTJOW1I FM Glycosyltransferase 16 (GT16) protein family TTJOW1I KE hsa00510:N-Glycan biosynthesis; hsa01100:Metabolic pathways TTQ4V96 ID TTQ4V96 TTQ4V96 TN Poly [ADP-ribose] polymerase 2 (PARP2) TTQ4V96 UP Q9UGN5 TTQ4V96 UC PARP2_HUMAN TTQ4V96 BC Glycosyltransferases TTQ4V96 SN pADPRT-2; hPARP-2; Protein poly-ADP-ribosyltransferase PARP2; Poly[ADP-ribose] synthase 2; PARP-2; NAD(+) ADP-ribosyltransferase 2; DNA ADP-ribosyltransferase PARP2; ARTD2; ADPRTL2; ADPRT2; ADPRT-2; ADP-ribosyltransferase diphtheria toxin-like 2 TTQ4V96 GN PARP2 TTQ4V96 FC Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of glutamate and aspartate residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Also mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity. In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex. Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. TTQ4V96 EC EC 2.4.2.30 TTQ4V96 PD 6F5F; 6F5B; 6F1K; 5DSY; 5D5K TTQ4V96 SQ MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALMEACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGPASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW TTQ4V96 TT Clinical trial TTQ4V96 KE hsa03410:Base excision repair; hsa04210:Apoptosis; hsa04217:Necroptosis TTPNACM ID TTPNACM TTPNACM TN Proteasome beta-10 (PS beta-10) TTPNACM UP P40306 TTPNACM UC PSB10_HUMAN TTPNACM BC Peptidase TTPNACM SN Proteasome subunit beta-2i; Proteasome subunit beta type-10; Proteasome MECl-1; Multicatalytic endopeptidase complex subunit MECl-1; Macropain subunit MECl-1; MECL1; Low molecular mass protein 10; LMP10 TTPNACM GN PSMB10 TTPNACM FC The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. TTPNACM EC EC 3.4.25.1 TTPNACM PD 6HVW; 6HVV; 6HVU; 6HVT; 6HVS TTPNACM SQ MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE TTPNACM TT Patented-recorded TTPNACM FM Peptidase T1B family TTPNACM KE hsa03050:Proteasome TT49BVC ID TT49BVC TT49BVC TN Proteasome beta-2 (PS beta-2) TT49BVC UP Q99436 TT49BVC UC PSB7_HUMAN TT49BVC BC Peptidase TT49BVC SN Proteasome subunit beta type-7; Proteasome subunit Z; Multicatalytic endopeptidase complex chain Z; Macropain chain Z TT49BVC GN PSMB7 TT49BVC FC Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a trypsin-like activity. TT49BVC EC EC 3.4.25.1 TT49BVC PD 6MSK; 6MSJ; 6MSH; 6MSG; 6MSE TT49BVC SQ MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS TT49BVC TT Patented-recorded TT49BVC KE hsa03050:Proteasome TT68GPI ID TT68GPI TT68GPI TN Proteasome beta-5 (PS beta-5) TT68GPI UP P28074 TT68GPI UC PSB5_HUMAN TT68GPI BC Peptidase TT68GPI SN Proteasome subunit beta type-5; Proteasome subunit X; Proteasome subunit MB1; Proteasome epsilon chain; Proteasome chain 6; Multicatalytic endopeptidase complex epsilon chain; Macropain epsilon chain; MB1; LMPX TT68GPI GN PSMB5 TT68GPI FC Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity. TT68GPI EC EC 3.4.25.1 TT68GPI PD 6MSK; 6MSJ; 6MSH; 6MSG; 6MSE TT68GPI SQ MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP TT68GPI TT Patented-recorded TTOUSTQ ID TTOUSTQ TTOUSTQ TN Proteasome beta-9 (PS beta-9) TTOUSTQ UP P28065 TTOUSTQ UC PSB9_HUMAN TTOUSTQ BC Peptidase TTOUSTQ SN Really interesting new gene 12 protein; RING12; Proteasome subunit beta-1i; Proteasome subunit beta type-9; Proteasome chain 7; PSMB6i; Multicatalytic endopeptidase complex chain 7; Macropain chain 7; Low molecular mass protein 2; LMP2 TTOUSTQ GN PSMB9 TTOUSTQ FC The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. TTOUSTQ EC EC 3.4.25.1 TTOUSTQ PD 6AVO TTOUSTQ SQ MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE TTOUSTQ TT Patented-recorded TTOUSTQ FM Peptidase T1B family TTOUSTQ KE hsa03050:Proteasome TTCZOF2 ID TTCZOF2 TTCZOF2 TN Pyruvate dehydrogenase kinase 1 (PDHK1) TTCZOF2 UP Q15118 TTCZOF2 UC PDK1_HUMAN TTCZOF2 BC Kinase TTCZOF2 SN Pyruvate dehydrogenase kinase isoform 1; Pyruvate dehydrogenase (acetyl-transferring) kinase isozyme 1, mitochondrial; PDHK1; PDH kinase 1 TTCZOF2 GN PDK1 TTCZOF2 FC Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress. TTCZOF2 EC EC 2.7.11.2 TTCZOF2 PD 2Q8H; 2Q8G; 2Q8F TTCZOF2 SQ MRLARLLRGAALAGPGPGLRAAGFSRSFSSDSGSSPASERGVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAKAIYDFTDTVIRIRNRHNDVIPTMAQGVIEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGKGSPSHRKHIGSINPNCNVLEVIKDGYENARRLCDLYYINSPELELEELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHANRGVYPPIQVHVTLGNEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTDSIERLPVYNKAAWKHYNTNHEADDWCVPSREPKDMTTFRSA TTCZOF2 TT Clinical trial TTCZOF2 FM PDK/BCKDK protein kinase family TTCZOF2 KE hsa04066:HIF-1 signaling pathway; hsa04360:Axon guidance; hsa05230:Central carbon metabolism in cancer TTTW7FJ ID TTTW7FJ TTTW7FJ TN Serine/threonine-protein phosphatase 5 (PPP5C) TTTW7FJ UP P53041 TTTW7FJ UC PPP5_HUMAN TTTW7FJ BC Phosphoric monoester hydrolase TTTW7FJ SN Protein phosphatase T; PPT protein; PPP5; PP5; PP-T TTTW7FJ GN PPP5C TTTW7FJ FC Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function. Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1. Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2. Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. TTTW7FJ EC EC 3.1.3.16 TTTW7FJ PD 5WG8; 5UI1; 5HPE; 4ZX2; 4ZVZ TTTW7FJ SQ MAMAEGERTECAEPPRDEPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQKAFERAIAGDEHKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM TTTW7FJ TT Patented-recorded TTTW7FJ FM PPP phosphatase family TTTW7FJ KE hsa04010:MAPK signaling pathway TTN7R6K ID TTN7R6K TTN7R6K TN Signal transducer and activator of transcription 1 (STAT1) TTN7R6K UP P42224 TTN7R6K UC STAT1_HUMAN TTN7R6K BC Transcription factor TTN7R6K SN Transcription factor ISGF-3 components p91/p84; Signal transducers and activators of transcription factor; Signal transducer and activator of transcription 1-alpha/beta; STAT-1; P91 TTN7R6K GN STAT1 TTN7R6K FC Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. TTN7R6K PD 3WWT; 2KA6; 1YVL; 1BF5 TTN7R6K SQ MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNTV TTN7R6K TT Patented-recorded TTN7R6K FM Transcription factor TTN7R6K KE hsa04062:Chemokine signaling pathway; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05140:Leishmaniasis; hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05200:Pathways in cancer; hsa05212:Pancreatic cancer; hsa05321:Inflammatory bowel disease (IBD) TTN7R6K RC R-HSA-1169408:ISG15 antiviral mechanism TTHS0U8 ID TTHS0U8 TTHS0U8 TN Stress-activated protein kinase JNK2 (JNK2) TTHS0U8 UP P45984 TTHS0U8 UC MK09_HUMAN TTHS0U8 BC Kinase TTHS0U8 SN Stress-activated protein kinase 1a; SAPK1a; PRKM9; Mitogen-activated protein kinase 9; Mitogen-activated protein kinase 8-interacting protein 2; MAPK 9; MAP kinase 9; Jun-N-terminal kinase 2; JNK-interacting protein 2; JNK-55; JNK MAP kinase scaffold protein 2; JIP-2; Islet-brain-2; IB-2; C-jun-amino-terminal kinase interacting protein 2; C-Jun N-terminal kinase 2 TTHS0U8 GN MAPK9 TTHS0U8 FC Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation. Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. TTHS0U8 EC EC 2.7.11.24 TTHS0U8 PD 3NPC; 3E7O TTHS0U8 SQ MSDSKCDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGCVIFQGTDHIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVVKDQPSDAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR TTHS0U8 TT Preclinical TTHS0U8 FM Kinase TTHS0U8 KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04024:cAMP signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04141:Protein processing in endoplasmic reticulum; hsa04310:Wnt signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04723:Retrograde endocannabinoid signaling; hsa04728:Dopaminergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04917:Prolactin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05210:Colorectal cancer; hsa05212:Pancreatic cancer; hsa05231:Choline metabolism in cancer TTHS0U8 RC R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-450321:JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1; R-HSA-450341:Activation of the AP-1 family of transcription factors TTXNCBV ID TTXNCBV TTXNCBV TN Tryptophan 2,3-dioxygenase (TDO) TTXNCBV UP P48775 TTXNCBV UC T23O_HUMAN TTXNCBV BC Oxygenase TTXNCBV SN Tryptophanase; Tryptophan pyrrolase; Tryptophan oxygenase; Tryptamin 2,3-dioxygenase; TRPO; TO TTXNCBV GN TDO2 TTXNCBV FC Catalyzes the oxidative cleavage of the indole moiety. Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. TTXNCBV EC EC 1.13.11.11 TTXNCBV PD 6A4I; 5TIA; 5TI9; 4PW8 TTXNCBV SQ MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD TTXNCBV TT Clinical trial TTXNCBV FM Tryptophan 2,3-dioxygenase family TTXNCBV KE hsa00380:Tryptophan metabolism; hsa01100:Metabolic pathways TTZJTWA ID TTZJTWA TTZJTWA TN ABL T315I mutant (ABL T315I) TTZJTWA UP P00519 TTZJTWA UC ABL1_HUMAN TTZJTWA BC Kinase TTZJTWA SN p150 T315I; T315I Abl; Proto-oncogene tyrosine-protein kinase ABL1 T315I; Proto-oncogene c-Abl T315I; JTK7 T315I; C-ABL T315I; Abl T315I; Abelson tyrosine-protein kinase 1 T315I; Abelson murine leukemia viral oncogene homolog 1 T315I TTZJTWA GN ABL1 TTZJTWA FC Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717'. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E. coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H. pylori, or AnkA (ankyrin repeat-containing protein A) of A. phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner. Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity. Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. TTZJTWA EC EC 2.7.10.2 TTZJTWA PD 6NPV; 6NPU; 6NPE; 6BL8; 6AMW TTZJTWA SQ MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR TTZJTWA TT Patented-recorded TTJNBQA ID TTJNBQA TTJNBQA TN Activin receptor-like kinase 2 (ALK-2) TTJNBQA UP Q04771 TTJNBQA UC ACVR1_HUMAN TTJNBQA BC Kinase TTJNBQA SN TSR-I; TGF-B superfamily receptor type I; Serine/threonine-protein kinase receptor R1; SKR1; Activin receptor type-1; Activin receptor type I; ACVRLK2; ACTR-I TTJNBQA GN ACVR1 TTJNBQA FC Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. TTJNBQA EC EC 2.7.11.30 TTJNBQA PD 6GIP; 6GIN; 6GI6; 6EIX; 6ACR TTJNBQA SQ MVDGVMILPVLIMIALPSPSMEDEKPKVNPKLYMCVCEGLSCGNEDHCEGQQCFSSLSINDGFHVYQKGCFQVYEQGKMTCKTPPSPGQAVECCQGDWCNRNITAQLPTKGKSFPGTQNFHLEVGLIILSVVFAVCLLACLLGVALRKFKRRNQERLNPRDVEYGTIEGLITTNVGDSTLADLLDHSCTSGSGSGLPFLVQRTVARQITLLECVGKGRYGEVWRGSWQGENVAVKIFSSRDEKSWFRETELYNTVMLRHENILGFIASDMTSRHSSTQLWLITHYHEMGSLYDYLQLTTLDTVSCLRIVLSIASGLAHLHIEIFGTQGKPAIAHRDLKSKNILVKKNGQCCIADLGLAVMHSQSTNQLDVGNNPRVGTKRYMAPEVLDETIQVDCFDSYKRVDIWAFGLVLWEVARRMVSNGIVEDYKPPFYDVVPNDPSFEDMRKVVCVDQQRPNIPNRWFSDPTLTSLAKLMKECWYQNPSARLTALRIKKTLTKIDNSLDKLKTDC TTJNBQA TT Clinical trial TT1WBIJ ID TT1WBIJ TT1WBIJ TN Calpain-1 (CAPN1) TT1WBIJ UP P07384 TT1WBIJ UC CAN1_HUMAN TT1WBIJ BC Peptidase TT1WBIJ SN muCANP; PIG30; Micromolar-calpain; Cell proliferation-inducing gene 30 protein; Calpain-1 large subunit; Calpain-1 catalytic subunit; Calpain mu-type; Calcium-activated neutral proteinase 1; CANPL1; CANP 1 TT1WBIJ GN CAPN1 TT1WBIJ FC Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. TT1WBIJ EC EC 3.4.22.52 TT1WBIJ SQ MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA TT1WBIJ TT Patented-recorded TT1WBIJ FM Peptidase C2 family TT1WBIJ KE hsa04141:Protein processing in endoplasmic reticulum; hsa04210:Apoptosis; hsa04217:Necroptosis; hsa04218:Cellular senescence; hsa05010:Alzheimer disease TTJC376 ID TTJC376 TTJC376 TN Carbonic anhydrase VII (CA-VII) TTJC376 UP P43166 TTJC376 UC CAH7_HUMAN TTJC376 BC Alpha-carbonic anhydrase TTJC376 SN Carbonic anhydrase 7; Carbonate dehydratase VII TTJC376 GN CA7 TTJC376 FC Reversible hydration of carbon dioxide. TTJC376 EC EC 4.2.1.1 TTJC376 PD 6H38; 6H37; 6H36; 6G4T; 3ML5 TTJC376 SQ MTGHHGWGYGQDDGPSHWHKLYPIAQGDRQSPINIISSQAVYSPSLQPLELSYEACMSLSITNNGHSVQVDFNDSDDRTVVTGGPLEGPYRLKQFHFHWGKKHDVGSEHTVDGKSFPSELHLVHWNAKKYSTFGEAASAPDGLAVVGVFLETGDEHPSMNRLTDALYMVRFKGTKAQFSCFNPKCLLPASRHYWTYPGSLTTPPLSESVTWIVLREPICISERQMGKFRSLLFTSEDDERIHMVNNFRPPQPLKGRVVKASFRA TTJC376 TT Patented-recorded TTJC376 FM Alpha-carbonic anhydrase family TTX5HEK ID TTX5HEK TTX5HEK TN Caspase-10 (CASP10) TTX5HEK UP Q92851 TTX5HEK UC CASPA_HUMAN TTX5HEK BC Peptidase TTX5HEK SN MCH4; ICE-like apoptotic protease 4; FLICE2; FAS-associated death domain protein interleukin-1B-converting enzyme 2; Caspase-10 subunit p23/17; Caspase-10 subunit p12; CASP-10; Apoptotic protease Mch-4 TTX5HEK GN CASP10 TTX5HEK FC Recruited to both Fas- and TNFR-1 receptors in a FADD dependent manner. May participate in the granzyme B apoptotic pathways. Cleaves and activates caspase-3, -4, -6, -7, -8, and -9. Hydrolyzes the small- molecule substrates, Tyr-Val-Ala-Asp-|-AMC and Asp-Glu-Val-Asp-|-AMC. Involved in the activation cascade of caspases responsible for apoptosis execution. TTX5HEK EC EC 3.4.22.63 TTX5HEK SQ MKSQGQHWYSSSDKNCKVSFREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNCTKEEVERLLPTRQRVSLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTEMTSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEKYKREKAIQIVTPPVDKEAESYQGEEELVSQTDVKTFLEALPQESWQNKHAGSNGNRATNGAPSLVSRGMQGASANTLNSETSTKRAAVYRMNRNHRGLCVIVNNHSFTSLKDRQGTHKDAEILSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCNPAHADGDCFVFCILTHGRFGAVYSSDEALIPIREIMSHFTALQCPRLAEKPKLFFIQACQGEEIQPSVSIEADALNPEQAPTSLQDSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSLCNHLKKLVPRMLKFLEKTMEIRGRKRTVWGAKQISATSLPTAISAQTPRPPMRRWSSVS TTX5HEK TT Patented-recorded TTX5HEK FM Peptidase C14A family TTX5HEK KE hsa04210:Apoptosis; hsa04622:RIG-I-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa05152:Tuberculosis; hsa05161:Hepatitis B TT85TPS ID TT85TPS TT85TPS TN CDC-like kinase 2 (CLK2) TT85TPS UP P49760 TT85TPS UC CLK2_HUMAN TT85TPS BC Kinase TT85TPS SN Dual specificity protein kinase CLK2 TT85TPS GN CLK2 TT85TPS FC Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. TT85TPS EC EC 2.7.12.1 TT85TPS PD 6FYL; 6FYK; 6FYI; 5UNP; 3NR9 TT85TPS SQ MPHPRRYHSSERGSRGSYREHYRSRKHKRRRSRSWSSSSDRTRRRRREDSYHVRSRSSYDDRSSDRRVYDRRYCGSYRRNDYSRDRGDAYYDTDYRHSYEYQRENSSYRSQRSSRRKHRRRRRRSRTFSRSSSQHSSRRAKSVEDDAEGHLIYHVGDWLQERYEIVSTLGEGTFGRVVQCVDHRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPDNKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKDNNYLPYPIHQVRHMAFQLCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTAVRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPIPSRMIRKTRKQKYFYRGRLDWDENTSAGRYVRENCKPLRRYLTSEAEEHHQLFDLIESMLEYEPAKRLTLGEALQHPFFARLRAEPPNKLWDSSRDISR TT85TPS TT Patented-recorded TT0GV3R ID TT0GV3R TT0GV3R TN DGAT1 messenger RNA (DGAT1 mRNA) TT0GV3R UP O75907 TT0GV3R UC DGAT1_HUMAN TT0GV3R BC mRNA target TT0GV3R SN Retinol O-fatty-acyltransferase (mRNA); Diglyceride acyltransferase (mRNA); Diacylglycerol O-acyltransferase 1 (mRNA); DGAT (mRNA); Acyl-CoA retinol O-fatty-acyltransferase (mRNA); ARAT (mRNA); AGRP1 (mRNA); ACAT-related gene product 1 (mRNA) TT0GV3R GN DGAT1 TT0GV3R FC In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders. Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. TT0GV3R EC EC 2.3.1.20 TT0GV3R SQ MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVGSGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPAAVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHTVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWMVPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREFYRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVSVPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLNYEAPAAEA TT0GV3R TT Literature-reported TT0GV3R FM mRNA target TT0GV3R KE hsa00561:Glycerolipid metabolism; hsa00830:Retinol metabolism; hsa01100:Metabolic pathways; hsa04975:Fat digestion and absorption TT0GV3R RC R-HSA-1482883:Acyl chain remodeling of DAG and TAG; R-HSA-75109:Triglyceride Biosynthesis TTSBVFO ID TTSBVFO TTSBVFO TN Dual-specificity tyrosine-phosphorylation regulated kinase 1A (DYRK1A) TTSBVFO UP Q13627 TTSBVFO UC DYR1A_HUMAN TTSBVFO BC Kinase TTSBVFO SN hMNB; Protein kinase minibrain homolog; MNBH; MNB; HP86; Dual specificity tyrosine-phosphorylation-regulated kinase 1A; Dual specificity YAK1-related kinase; DYRK TTSBVFO GN DYRK1A TTSBVFO FC Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Exhibits a substrate preference for proline at position P+1 and arginine at position P-3. Has pro-survival function and negatively regulates the apoptotic process. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits TP53 activity and apoptosis (By similarity). TTSBVFO EC EC 2.7.12.1 TTSBVFO PD 6EJ4; 6EIV; 6EIS; 6EIR; 6EIQ TTSBVFO SQ MHTGGETSACKPSSVRLAPSFSFHAAGLQMAGQMPHSHQYSDRRQPNISDQQVSALSYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFTAAVQAMDCETHSPQVRQQFPAPLGWSGTEAPTQVTVETHPVQETTFHVAPQQNALHHHHGNSSHHHHHHHHHHHHHGQQALGNRTRPRVYNSPTNSSSTQDSMEVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGAMDVNLTVYSNPRQETGIAGHPTYQFSANTGPAHYMTEGHLTMRQGADREESPMTGVCVQQSPVASS TTSBVFO TT Patented-recorded TT84OS6 ID TT84OS6 TT84OS6 TN Dual-specificity tyrosine-phosphorylation regulated kinase 2 (DYRK2) TT84OS6 UP Q92630 TT84OS6 UC DYRK2_HUMAN TT84OS6 BC Kinase TT84OS6 SN Dual specificity tyrosine-phosphorylation-regulated kinase 2 TT84OS6 GN DYRK2 TT84OS6 FC Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser-641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX and DPYSL2. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro). Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. TT84OS6 EC EC 2.7.12.1 TT84OS6 PD 5ZTN; 5LXD; 5LXC; 4AZF; 3KVW TT84OS6 SQ MLTRKPSAAAPAAYPTGRGGDSAVRQLQASPGLGAGATRSGVGTGPPSPIALPPLRASNAAAAAHTIGGSKHTMNDHLHVGSHAHGQIQVQQLFEDNSNKRTVLTTQPNGLTTVGKTGLPVVPERQLDSIHRRQGSSTSLKSMEGMGKVKATPMTPEQAMKQYMQKLTAFEHHEIFSYPEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTTLSDGSVVLNGGRSRRGKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLRRRLPKPPTGEKTSVKRITESTGAITSISKLPPPSSSASKLRTNLAQMTDANGNIQQRTVLPKLVS TT84OS6 TT Patented-recorded TTV4EX0 ID TTV4EX0 TTV4EX0 TN Dual-specificity tyrosine-phosphorylation regulated kinase 3 (DYRK3) TTV4EX0 UP O43781 TTV4EX0 UC DYRK3_HUMAN TTV4EX0 BC Kinase TTV4EX0 SN Regulatory erythroid kinase; REDK; Dual specificity tyrosine-phosphorylation-regulated kinase 3 TTV4EX0 GN DYRK3 TTV4EX0 FC Dual-specificity tyrosine-regulated kinases (DYRKs) autophosphorylate a critical tyrosine residue in their activation loop and phosphorylate their substrate on serine and threonine residues. Acts as a central dissolvase of membraneless organelles during the G2-to-M transition, after the nuclear-envelope breakdown: acts by mediating phosphorylation of multiple serine and threonine residues in unstructured domains of proteins, such as SRRM1 and PCM1. Does not mediate disassembly of all membraneless organelles: disassembly of P-body and nucleolus is not regulated by DYRK3. Dissolution of membraneless organelles at the onset of mitosis is also required to release mitotic regulators, such as ZNF207, from liquid-unmixed organelles where they are sequestered and keep them dissolved during mitosis. Regulates mTORC1 by mediating the dissolution of stress granules: during stressful conditions, DYRK3 partitions from the cytosol to the stress granule, together with mTORC1 components, which prevents mTORC1 signaling. When stress signals are gone, the kinase activity of DYRK3 is required for the dissolution of stress granule and mTORC1 relocation to the cytosol: acts by mediating the phosphorylation of the mTORC1 inhibitor AKT1S1, allowing full reactivation of mTORC1 signaling. Also acts as a negative regulator of EPO-dependent erythropoiesis: may place an upper limit on red cell production during stress erythropoiesis. Inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1: this in turn inhibits p53/TP53 activity and apoptosis. Dual-specificity protein kinase that promotes disassembly of several types of membraneless organelles during mitosis, such as stress granules, nuclear speckles and pericentriolar material. TTV4EX0 EC EC 2.7.12.1 TTV4EX0 PD 5Y86 TTV4EX0 SQ MGGTARGPGRKDAGPPGAGLPPQQRRLGDGVYDTFMMIDETKCPPCSNVLCNPSEPPPPRRLNMTTEQFTGDHTQHFLDGGEMKVEQLFQEFGNRKSNTIQSDGISDSEKCSPTVSQGKSSDCLNTVKSNSSSKAPKVVPLTPEQALKQYKHHLTAYEKLEIINYPEIYFVGPNAKKRHGVIGGPNNGGYDDADGAYIHVPRDHLAYRYEVLKIIGKGSFGQVARVYDHKLRQYVALKMVRNEKRFHRQAAEEIRILEHLKKQDKTGSMNVIHMLESFTFRNHVCMAFELLSIDLYELIKKNKFQGFSVQLVRKFAQSILQSLDALHKNKIIHCDLKPENILLKHHGRSSTKVIDFGSSCFEYQKLYTYIQSRFYRAPEIILGSRYSTPIDIWSFGCILAELLTGQPLFPGEDEGDQLACMMELLGMPPPKLLEQSKRAKYFINSKGIPRYCSVTTQADGRVVLVGGRSRRGKKRGPPGSKDWGTALKGCDDYLFIEFLKRCLHWDPSARLTPAQALRHPWISKSVPRPLTTIDKVSGKRVVNPASAFQGLGSKLPPVVGIANKLKANLMSETNGSIPLCSVLPKLIS TTV4EX0 TT Patented-recorded TTZ04AF ID TTZ04AF TTZ04AF TN EGFR T790M mutant (EGFR T790M) TTZ04AF UP P00533 TTZ04AF UC EGFR_HUMAN TTZ04AF BC Kinase TTZ04AF SN Receptor tyrosine-protein kinase erbB-1 T790M mutant; Proto-oncogene c-ErbB-1 T790M mutant; HER1 T790M mutant; Epidermal growth factor receptor T790M mutant; ERBB1 T790M mutant; ERBB T790M mutant TTZ04AF GN EGFR TTZ04AF FC Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Plays a role in enhancing learning and memory performance. TTZ04AF EC EC 2.7.10.1 TTZ04AF PD 6D8E; 6B3S; 6ARU; 5ZWJ; 5YU9 TTZ04AF SQ MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA TTZ04AF TT Patented-recorded TTZ04AF FM Protein kinase superfamily. Tyr protein kinase family TTU6FSC ID TTU6FSC TTU6FSC TN Extracellular signal-regulated kinase 5 (ERK5) TTU6FSC UP Q13164 TTU6FSC UC MK07_HUMAN TTU6FSC BC Kinase TTU6FSC SN PRKM7; Mitogen-activated protein kinase 7; MAPK 7; MAP kinase 7; ERK-5; Big MAP kinase 1; BMK1; BMK-1 TTU6FSC GN MAPK7 TTU6FSC FC The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction. Plays a role in various cellular processes such as proliferation, differentiation and cell survival. TTU6FSC EC EC 2.7.11.24 TTU6FSC PD 6HKN; 6HKM; 5O7I; 5BYZ; 5BYY TTU6FSC SQ MAEPLKEEDGEDGSAEPPGPVKAEPAHTAASVAAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGIRQQIRFQPSLQPVASEPGCPDVEMPSPWAPSGDCAMESPPPAPPPCPGPAPDTIDLTLQPPPPVSEPAPPKKDGAISDNTKAALKAALLKSLRSRLRDGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERGAGASGGPSTDPLAGLVLSDNDRSLLERWTRMARPAAPALTSVPAPAPAPTPTPTPVQPTSPPPGPVAQPTGPQPQSAGSTSGPVPQPACPPPGPAPHPTGPPGPIPVPAPPQIATSTSLLAAQSLVPPPGLPGSSTPGVLPYFPPGLPPPDAGGAPQSSMSESPDVNLVTQQLSKSQVEDPLPPVFSGTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLADWLEGHGMNPADIESLQREIQMDSPMLLADLPDLQDP TTU6FSC TT Patented-recorded TTGX13H ID TTGX13H TTGX13H TN Fatty-acid amide hydrolase 1 (FAAH1) TTGX13H UP O08914 TTGX13H UC FAAH1_HUMAN TTGX13H BC Carbon-nitrogen hydrolase TTGX13H SN Oleamide hydrolase 1 of mouse; Oleamide hydrolase 1; FAAH; Anandamide amidohydrolase 1 of mouse; Anandamide amidohydrolase 1 TTGX13H GN FAAH1 TTGX13H FC Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates. Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. TTGX13H EC EC 3.5.1.99 TTGX13H SQ MVQYELWAALPGASGVALACCFVAAAVALRWSGRRTARGAVVRARQRQRAGLENMDRAAQRFRLQNPDLDSEALLALPLPQLVQKLHSRELAPEAVLFTYVGKAWEVNKGTNCVTSYLADCETQLSQAPRQGLLYGVPVSLKECFTYKGQDSTLGLSLNEGVPAECDSVVVHVLKLQGAVPFVHTNVPQSMFSYDCSNPLFGQTVNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSSFCGICGLKPTGNRLSKSGLKGCVYGQEAVRLSVGPMARDVESLALCLRALLCEDMFRLDPTVPPLPFREEVYTSSQPLRVGYYETDNYTMPSPAMRRAVLETKQSLEAAGHTLVPFLPSNIPHALETLSTGGLFSDGGHTFLQNFKGDFVDPCLGDLVSILKLPQWLKGLLAFLVKPLLPRLSAFLSNMKSRSAGKLWELQHEIEVYRKTVIAQWRALDLDVVLTPMLAPALDLNAPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDEAQMEHYRGYFGDIWDKMLQKGMKKSVGLPVAVQCVALPWQEELCLRFMREVERLMTPEKQSS TTGX13H TT Patented-recorded TTGX13H FM Amidase family TTGX13H KE hsa04723:Retrograde endocannabinoid signaling TTXU3EQ ID TTXU3EQ TTXU3EQ TN Herpesvirus ubiquitin-specific protease (HAUSP) TTXU3EQ UP Q93009 TTXU3EQ UC UBP7_HUMAN TTXU3EQ BC Peptidase TTXU3EQ SN Ubiquitin-specific-processing protease 7; Ubiquitin thioesterase 7; Ubiquitin carboxyl-terminal hydrolase 7; Herpesvirus-associated ubiquitin-specific protease; Deubiquitinating enzyme 7 TTXU3EQ GN USP7 TTXU3EQ FC Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regulation, cell growth repression and apoptosis. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Deubiquitinates KMT2E/MLL5 preventing KMT2E/MLL5 proteasomal-mediated degradation. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions. Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex. Able to mediate deubiquitination of histone H2B; it is however unsure whether this activity takes place in vivo. Exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function. Plays a role in the maintenance of the circadian clock periodicity via deubiquitination and stabilization of the CRY1 and CRY2 proteins. Deubiquitinates REST, thereby stabilizing REST and promoting the maintenance of neural progenitor cells. Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and DAXX. TTXU3EQ EC EC 3.4.19.12 TTXU3EQ PD 6F5H; 5WHC; 5VSK; 5VSB; 5VS6 TTXU3EQ SQ MNHQQQQQQQKAGEQQLSEPEDMEMEAGDTDDPPRITQNPVINGNVALSDGHNTAEEDMEDDTSWRSEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRFYPDRPHQKSVGFFLQCNAESDSTSWSCHAQAVLKIINYRDDEKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKGFIDDDKVTFEVFVQADAPHGVAWDSKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKTDPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDDLSVRHCTNAYMLVYIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQKRKERQEAHLYMQVQIVAEDQFCGHQGNDMYDEEKVKYTVFKVLKNSSLAEFVQSLSQTMGFPQDQIRLWPMQARSNGTKRPAMLDNEADGNKTMIELSDNENPWTIFLETVDPELAASGATLPKFDKDHDVMLFLKMYDPKTRSLNYCGHIYTPISCKIRDLLPVMCDRAGFIQDTSLILYEEVKPNLTERIQDYDVSLDKALDELMDGDIIVFQKDDPENDNSELPTAKEYFRDLYHRVDVIFCDKTIPNDPGFVVTLSNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRHNYEGTLRDLLQFFKPRQPKKLYYQQLKMKITDFENRRSFKCIWLNSQFREEEITLYPDKHGCVRDLLEECKKAVELGEKASGKLRLLEIVSYKIIGVHQEDELLECLSPATSRTFRIEEIPLDQVDIDKENEMLVTVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEKEFEKFKFAIVMMGRHQYINEDEYEVNLKDFEPQPGNMSHPRPWLGLDHFNKAPKRSRYTYLEKAIKIHN TTXU3EQ TT Preclinical TTXU3EQ FM Peptidase TT8K17W ID TT8K17W TT8K17W TN Histone deacetylase 11 (HDAC11) TT8K17W UP Q96DB2 TT8K17W UC HDA11_HUMAN TT8K17W BC Carbon-nitrogen hydrolase TT8K17W SN HD11 TT8K17W GN HDAC11 TT8K17W FC Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). TT8K17W EC EC 3.5.1.98 TT8K17W SQ MLHTTQLYQHVPETRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLFGLGLIGPESPSVSAQNSDTPLLPPAVP TT8K17W TT Patented-recorded TT8K17W FM Histone deacetylase family TT8K17W KE hsa05034:Alcoholism; hsa05203:Viral carcinogenesis TTUELN5 ID TTUELN5 TTUELN5 TN Histone deacetylase 5 (HDAC5) TTUELN5 UP Q9UQL6 TTUELN5 UC HDAC5_HUMAN TTUELN5 BC Carbon-nitrogen hydrolase TTUELN5 SN KIAA0600; HD5; Antigen NY-CO-9 TTUELN5 GN HDAC5 TTUELN5 FC Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). TTUELN5 EC EC 3.5.1.98 TTUELN5 PD 5UWI TTUELN5 SQ MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL TTUELN5 TT Patented-recorded TTMUEK1 ID TTMUEK1 TTMUEK1 TN Histone deacetylase 7 (HDAC7) TTMUEK1 UP Q8WUI4 TTMUEK1 UC HDAC7_HUMAN TTMUEK1 BC Carbon-nitrogen hydrolase TTMUEK1 SN Histone deacetylase 7A; HDAC7A; HD7a; HD7 TTMUEK1 GN HDAC7 TTMUEK1 FC Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Positively regulates the transcriptional repressor activity of FOXP3. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). TTMUEK1 EC EC 3.5.1.98 TTMUEK1 PD 3ZNS; 3ZNR; 3C10; 3C0Z; 3C0Y TTMUEK1 SQ MDLRVGQRPPVEPPPEPTLLALQRPQRLHHHLFLAGLQQQRSVEPMRLSMDTPMPELQVGPQEQELRQLLHKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPNSPGIPYRTLEPLETEGATRSMLSSFLPPVPSLPSDPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPILGSEALLGQRLRLQETSVAPFALPTVSLLPAITLGLPAPARADSDRRTHPTLGPRGPILGSPHTPLFLPHGLEPEAGGTLPSRLQPILLLDPSGSHAPLLTVPGLGPLPFHFAQSLMTTERLSGSGLHWPLSRTRSEPLPPSATAPPPPGPMQPRLEQLKTHVQVIKRSAKPSEKPRLRQIPSAEDLETDGGGPGQVVDDGLEHRELGHGQPEARGPAPLQQHPQVLLWEQQRLAGRLPRGSTGDTVLLPLAQGGHRPLSRAQSSPAAPASLSAPEPASQARVLSSSETPARTLPFTTGLIYDSVMLKHQCSCGDNSRHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQSKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNRVDPLSEEGWKQKPNLNAIRSLEAVIRVHSKYWGCMQRLASCPDSWVPRVPGADKEEVEAVTALASLSVGILAEDRPSEQLVEEEEPMNL TTMUEK1 TT Patented-recorded TTXAJWN ID TTXAJWN TTXAJWN TN IL-1 receptor-associated kinase 1 (IRAK1) TTXAJWN UP P51617 TTXAJWN UC IRAK1_HUMAN TTXAJWN BC Kinase TTXAJWN SN Interleukin-1 receptor-associated kinase 1; IRAK-1; IRAK TTXAJWN GN IRAK1 TTXAJWN FC Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3. Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. TTXAJWN EC EC 2.7.11.1 TTXAJWN PD 6BFN TTXAJWN SQ MAGGPGPGEPAAPGAQHFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSGQRTASVLWPWINRNARVADLVHILTHLQLLRARDIITAWHPPAPLPSPGTTAPRPSSIPAPAEAEAWSPRKLPSSASTFLSPAFPGSQTHSGPELGLVPSPASLWPPPPSPAPSSTKPGPESSVSLLQGARPFPFCWPLCEISRGTHNFSEELKIGEGGFGCVYRAVMRNTVYAVKRLKENADLEWTAVKQSFLTEVEQLSRFRHPNIVDFAGYCAQNGFYCLVYGFLPNGSLEDRLHCQTQACPPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLTPKLGDFGLARFSRFAGSSPSQSSMVARTQTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVVLETLAGQRAVKTHGARTKYLKDLVEEEAEEAGVALRSTQSTLQAGLAADAWAAPIAMQIYKKHLDPRPGPCPPELGLGLGQLACCCLHRRAKRRPPMTQVYERLEKLQAVVAGVPGHSEAASCIPPSPQENSYVSSTGRAHSGAAPWQPLAAPSGASAQAAEQLQRGPNQPVESDESLGGLSAALRSWHLTPSCPLDPAPLREAGCPQGDTAGESSWGSGPGSRPTAVEGLALGSSASSSSEPPQIIINPARQKMVQKLALYEDGALDSLQLLSSSSLPGLGLEQDRQGPEESDEFQS TTXAJWN TT Patented-recorded TTALN9W ID TTALN9W TTALN9W TN Indoleamine 2,3-dioxygenase 2 (IDO2) TTALN9W UP Q6ZQW0 TTALN9W UC I23O2_HUMAN TTALN9W BC Oxygenase TTALN9W SN Indoleamine-pyrrole 2,3-dioxygenase-like protein 1; Indoleamine 2,3-dioxygenase-like protein 1; INDOL1; IDO-2 TTALN9W GN IDO2 TTALN9W FC Involved in immune regulation. May not play a significant role in tryptophan-related tumoral resistance. Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. TTALN9W EC EC 1.13.11.- TTALN9W SQ MLHFHYYDTSNKIMEPHRPNVKTAVPLSLESYHISEEYGFLLPDSLKELPDHYRPWMEIANKLPQLIDAHQLQAHVDKMPLLSCQFLKGHREQRLAHLVLSFLTMGYVWQEGEAQPAEVLPRNLALPFVEVSRNLGLPPILVHSDLVLTNWTKKDPDGFLEIGNLETIISFPGGESLHGFILVTALVEKEAVPGIKALVQATNAILQPNQEALLQALQRLRLSIQDITKTLGQMHDYVDPDIFYAGIRIFLSGWKDNPAMPAGLMYEGVSQEPLKYSGGSAAQSTVLHAFDEFLGIRHSKESGDFLYRMRDYMPPSHKAFIEDIHSAPSLRDYILSSGQDHLLTAYNQCVQALAELRSYHITMVTKYLITAAAKAKHGKPNHLPGPPQALKDRGTGGTAVMSFLKSVRDKTLESILHPRG TTALN9W TT Patented-recorded TTALN9W FM Indoleamine 2,3-dioxygenase family TTALN9W KE hsa00380:Tryptophan metabolism; hsa01100:Metabolic pathways; hsa05143:African trypanosomiasis TT4319X ID TT4319X TT4319X TN Kallikrein-4 (KLK4) TT4319X UP Q9Y5K2 TT4319X UC KLK4_HUMAN TT4319X BC Peptidase TT4319X SN Serine protease 17; Prostase; PSTS; PRSS17; Kallikreinlike protein 1; Kallikrein4; Kallikrein-like protein 1; KLKL1; KLK-L1; Enamel matrix serine proteinase 1; EMSP1 TT4319X GN KLK4 TT4319X FC Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix. Has a major role in enamel formation. TT4319X EC EC 3.4.21.- TT4319X PD 4KGA; 4KEL; 4K8Y; 4K1E; 2BDI TT4319X SQ MATAGNPWGWFLGYLILGVAGSLVSGSCSQIINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIGLGLHSLEADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRSISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYDPLYHPSMFCAGGGHDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQVGVPGVYTNLCKFTEWIEKTVQAS TT4319X TT Patented-recorded TT4319X FM Peptidase TTULSEW ID TTULSEW TTULSEW TN Kallikrein-5 (KLK5) TTULSEW UP Q9Y337 TTULSEW UC KLK5_HUMAN TTULSEW BC Peptidase TTULSEW SN UNQ570/PRO1132; Stratum corneum tryptic enzyme; SCTE; Kallikrein-like protein 2; KLK-L2 TTULSEW GN KLK5 TTULSEW FC May be involved in desquamation. TTULSEW EC EC 3.4.21.- TTULSEW PD 6QFE; 2PSY; 2PSX TTULSEW SQ MATARPPWMWVLCALITALLLGVTEHVLANNDVSCDHPSNTVPSGSNQDLGAGAGEDARSDDSSSRIINGSDCDMHTQPWQAALLLRPNQLYCGAVLVHPQWLLTAAHCRKKVFRVRLGHYSLSPVYESGQQMFQGVKSIPHPGYSHPGHSNDLMLIKLNRRIRPTKDVRPINVSSHCPSAGTKCLVSGWGTTKSPQVHFPKVLQCLNISVLSQKRCEDAYPRQIDDTMFCAGDKAGRDSCQGDSGGPVVCNGSLQGLVSWGDYPCARPNRPGVYTNLCKFTKWIQETIQANS TTULSEW TT Patented-recorded TTIY56R ID TTIY56R TTIY56R TN Kynurenine 3-hydroxylase (KMO) TTIY56R UP O15229 TTIY56R UC KMO_HUMAN TTIY56R BC Paired donor oxygen oxidoreductase TTIY56R SN Kynurenine 3monooxygenase; Kynurenine 3-monooxygenase TTIY56R GN KMO TTIY56R FC Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract. Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). TTIY56R EC EC 1.14.13.9 TTIY56R PD 5X68 TTIY56R SQ MDSSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTRGRSINLALSHRGRQALKAVGLEDQIVSQGIPMRARMIHSLSGKKSAIPYGTKSQYILSVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITVLGSDKVPKDVTCDLIVGCDGAYSTVRSHLMKKPRFDYSQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTCTLFMPFEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKSHCVLLGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFSNDLSLCLPVFSRLRIPDDHAISDLSMYNYIEMRAHVNSSWFIFQKNMERFLHAIMPSTFIPLYTMVTFSRIRYHEAVQRWHWQKKVINKGLFFLGSLIAISSTYLLIHYMSPRSFLRLRRPWNWIAHFRNTTCFPAKAVDSLEQISNLISR TTIY56R TT Clinical trial TTIY56R FM Oxidoreductases acting on paired donors TT6AXLY ID TT6AXLY TT6AXLY TN Leucine-rich repeat kinase 2 G2019S mutant (LRRK2 G2019S) TT6AXLY UP Q5S007 TT6AXLY UC LRRK2_HUMAN TT6AXLY BC Kinase TT6AXLY SN PARK8 G2019S mutant; LRRK2 G2019S mutant; Dardarin G2019S mutant TT6AXLY GN LRRK2 TT6AXLY FC The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). Plays a role in synaptic vesicle trafficking. Phosphorylates PRDX3. Has GTPase activity. May play a role in the phosphorylation of proteins central to Parkinson disease. Plays an important role in recuiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization. Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway. TT6AXLY EC EC 2.7.11.1 TT6AXLY PD 6DLP; 6DLO; 5MYC; 5MY9; 3D6T TT6AXLY SQ MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE TT6AXLY TT Patented-recorded TT6AXLY FM Protein kinase superfamily. TKL Ser/Thr protein kinase family TTC7A6G ID TTC7A6G TTC7A6G TN Leucine-rich repeat kinase 2 S935 phosphorylation (LRRK2 pS935) TTC7A6G UP Q5S007 TTC7A6G UC LRRK2_HUMAN TTC7A6G BC Kinase TTC7A6G SN PARK8 S935 phosphorylation; LRRK2 S935 phosphorylation; Dardarin S935 phosphorylation TTC7A6G GN LRRK2 TTC7A6G FC The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). Plays a role in synaptic vesicle trafficking. Phosphorylates PRDX3. Has GTPase activity. May play a role in the phosphorylation of proteins central to Parkinson disease. Plays an important role in recuiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization. Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway. TTC7A6G EC EC 2.7.11.1 TTC7A6G PD 6DLP; 6DLO; 5MYC; 5MY9; 3D6T TTC7A6G SQ MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE TTC7A6G TT Patented-recorded TTC7A6G FM Protein kinase superfamily. TKL Ser/Thr protein kinase family TTZHPB8 ID TTZHPB8 TTZHPB8 TN Lysine-specific demethylase 4A (KDM4A) TTZHPB8 UP O75164 TTZHPB8 UC KDM4A_HUMAN TTZHPB8 BC Paired donor oxygen oxidoreductase TTZHPB8 SN KIAA0677; Jumonji domain-containing protein 2A; JmjC domain-containing histone demethylation protein 3A; JMJD2A; JMJD2; JHDM3A TTZHPB8 GN KDM4A TTZHPB8 FC Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively. TTZHPB8 EC EC 1.14.11.- TTZHPB8 PD 6H8P; 6G5X; 6G5W; 6CG2; 6CG1 TTZHPB8 SQ MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESELPPRAGNEEECPEEDMEGVEDGEEGDLKTSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEDLSSEQYEMTECPAALAPVRPTHSSVRQVEDGLTFPDYSDSTEVKFEELKNVKLEEEDEEEEQAAAALDLSVNPASVGGRLVFSGSKKKSSSSLGSGSSRDSISSDSETSEPLSCRAQGQTGVLTVHSYAKGDGRVTVGEPCTRKKGSAARSFSERELAEVADEYMFSLEENKKSKGRRQPLSKLPRHHPLVLQECVSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNETMAQQAPHCAVCMIFQTYHQVEFGGFNQNCGNASDLAPQKQRTKPLIPEMCFTSTGCSTDINLSTPYLEEDGTSILVSCKKCSVRVHASCYGVPPAKASEDWMCSRCSANALEEDCCLCSLRGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCIFCKKRRKRTAGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKIPNLERAKGALQSITAGQKVISKHKNGRFYQCEVVRLTTETFYEVNFDDGSFSDNLYPEDIVSQDCLQFGPPAEGEVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVKRDDVYTLDEELPKRVKSRLSVASDMRFNEIFTEKEVKQEKKRQRVINSRYREDYIEPALYRAIME TTZHPB8 TT Patented-recorded TTZHPB8 FM JHDM3 histone demethylase family TTV8CRH ID TTV8CRH TTV8CRH TN Lysine-specific demethylase 4C (KDM4C) TTV8CRH UP Q9H3R0 TTV8CRH UC KDM4C_HUMAN TTV8CRH BC Paired donor oxygen oxidoreductase TTV8CRH SN KIAA0780; Jumonji domain-containing protein 2C; JmjC domain-containing histone demethylation protein 3C; JMJD2C; JHDM3C; Gene amplified in squamous cell carcinoma 1 protein; GASC1; GASC-1 protein TTV8CRH GN KDM4C TTV8CRH FC Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. TTV8CRH EC EC 1.14.11.- TTV8CRH PD 5KR7; 5FJK; 5FJH; 4XDP; 4XDO TTV8CRH SQ MEVAEVESPLNPSCKIMTFRPSMEEFREFNKYLAYMESKGAHRAGLAKVIPPKEWKPRQCYDDIDNLLIPAPIQQMVTGQSGLFTQYNIQKKAMTVKEFRQLANSGKYCTPRYLDYEDLERKYWKNLTFVAPIYGADINGSIYDEGVDEWNIARLNTVLDVVEEECGISIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAQGFFPSSSQGCDAFLRHKMTLISPSVLKKYGIPFDKITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATVRWIDYGKVAKLCTCRKDMVKISMDIFVRKFQPDRYQLWKQGKDIYTIDHTKPTPASTPEVKAWLQRRRKVRKASRSFQCARSTSKRPKADEEEEVSDEVDGAEVPNPDSVTDDLKVSEKSEAAVKLRNTEASSEEESSASRMQVEQNLSDHIKLSGNSCLSTSVTEDIKTEDDKAYAYRSVPSISSEADDSIPLSSGYEKPEKSDPSELSWPKSPESCSSVAESNGVLTEGEESDVESHGNGLEPGEIPAVPSGERNSFKVPSIAEGENKTSKSWRHPLSRPPARSPMTLVKQQAPSDEELPEVLSIEEEVEETESWAKPLIHLWQTKSPNFAAEQEYNATVARMKPHCAICTLLMPYHKPDSSNEENDARWETKLDEVVTSEGKTKPLIPEMCFIYSEENIEYSPPNAFLEEDGTSLLISCAKCCVRVHASCYGIPSHEICDGWLCARCKRNAWTAECCLCNLRGGALKQTKNNKWAHVMCAVAVPEVRFTNVPERTQIDVGRIPLQRLKLKCIFCRHRVKRVSGACIQCSYGRCPASFHVTCAHAAGVLMEPDDWPYVVNITCFRHKVNPNVKSKACEKVISVGQTVITKHRNTRYYSCRVMAVTSQTFYEVMFDDGSFSRDTFPEDIVSRDCLKLGPPAEGEVVQVKWPDGKLYGAKYFGSNIAHMYQVEFEDGSQIAMKREDIYTLDEELPKRVKARFSTASDMRFEDTFYGADIIQGERKRQRVLSSRFKNEYVADPVYRTFLKSSFQKKCQKRQ TTV8CRH TT Patented-recorded TTWAQBO ID TTWAQBO TTWAQBO TN Lysine-specific demethylase 4E (KDM4E) TTWAQBO UP B2RXH2 TTWAQBO UC KDM4E_HUMAN TTWAQBO BC Paired donor oxygen oxidoreductase TTWAQBO SN Lysine-specific demethylase 4D-like; KDM4DL; KDM4D-like protein TTWAQBO GN KDM4E TTWAQBO FC Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. TTWAQBO EC EC 1.14.11.- TTWAQBO PD 2W2I TTWAQBO SQ MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL TTWAQBO TT Patented-recorded TTWAQBO FM JHDM3 histone demethylase family TT8VP2T ID TT8VP2T TT8VP2T TN Lysine-specific histone demethylase 1B (KDM1B) TT8VP2T UP Q8NB78 TT8VP2T UC KDM1B_HUMAN TT8VP2T BC CH-NH(2) donor oxidoreductase TT8VP2T SN Lysine-specific histone demethylase 2; LSD2; Flavin-containing amine oxidase domain-containing protein 1; C6orf193; AOF1 TT8VP2T GN KDM1B TT8VP2T FC Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4. Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. TT8VP2T EC EC 1.-.-.- TT8VP2T PD 6R25; 6R1U; 4HSU; 4GUU; 4GUT TT8VP2T SQ MATPRGRTKKKASFDHSPDSLPLRSSGRQAKKKATETTDEDEDGGSEKKYRKCEKAGCTATCPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDGYDKYTTWKKIWTSNGKTEPSPKAFMADQQLPYWVQCTKPECRKWRQLTKEIQLTPQIAKTYRCGMKPNTAIKPETSDHCSLPEDLRVLEVSNHWWYSMLILPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTNRAAATGNASPGKLEHSKAALSVHVPGMNRYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLSVGADQYLLPKDYHNKSVIIIGAGPAGLAAARQLHNFGIKVTVLEAKDRIGGRVWDDKSFKGVTVGRGAQIVNGCINNPVALMCEQLGISMHKFGERCDLIQEGGRITDPTIDKRMDFHFNALLDVVSEWRKDKTQLQDVPLGEKIEEIYKAFIKESGIQFSELEGQVLQFHLSNLEYACGSNLHQVSARSWDHNEFFAQFAGDHTLLTPGYSVIIEKLAEGLDIQLKSPVQCIDYSGDEVQVTTTDGTGYSAQKVLVTVPLALLQKGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASKRGLFAVFYDMDPQKKHSVLMSVIAGEAVASVRTLDDKQVLQQCMATLRELFKEQEVPDPTKYFVTRWSTDPWIQMAYSFVKTGGSGEAYDIIAEDIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF TT8VP2T TT Patented-recorded TT8VP2T FM Flavin monoamine oxidase family TTHZ8TA ID TTHZ8TA TTHZ8TA TN Melanoma inhibitor of apoptosis protein (ML-IAP) TTHZ8TA UP Q96CA5 TTHZ8TA UC BIRC7_HUMAN TTHZ8TA BC Acyltransferase TTHZ8TA SN UNQ5800/PRO19607/PRO21344; RNF50; RING-type E3 ubiquitin transferase BIRC7; RING finger protein 50; MLIAP; Livin; Kidney inhibitor of apoptosis protein; KIAP; Baculoviral IAP repeat-containing protein 7 TTHZ8TA GN BIRC7 TTHZ8TA FC Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and NR2C2/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9. Isoform 1 blocks staurosporine-induced apoptosis. Isoform 2 blocks etoposide-induced apoptosis. Isoform 2 protects against natural killer (NK) cell killing whereas isoform 1 augments killing. Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. TTHZ8TA EC EC 2.3.2.27 TTHZ8TA PD 4AUQ; 3UW5; 3GTA; 3GT9; 3F7I TTHZ8TA SQ MGPKDSAKCLHRGPQPSHWAAGDGPTQERCGPRSLGSPVLGLDTCRAWDHVDGQILGQLRPLTEEEEEEGAGATLSRGPAFPGMGSEELRLASFYDWPLTAEVPPELLAAAGFFHTGHQDKVRCFFCYGGLQSWKRGDDPWTEHAKWFPSCQFLLRSKGRDFVHSVQETHSQLLGSWDPWEEPEDAAPVAPSVPASGYPELPTPRREVQSESAQEPGGVSPAEAQRAWWVLEPPGARDVEAQLRRLQEERTCKVCLDRAVSIVFVPCGHLVCAECAPGLQLCPICRAPVRSRVRTFLS TTHZ8TA TT Patented-recorded TTSINOV ID TTSINOV TTSINOV TN Monoacylglycerol lipase ABHD6 (ABHD6) TTSINOV UP Q9BV23 TTSINOV UC ABHD6_HUMAN TTSINOV BC Carboxylic ester hydrolase TTSINOV SN Abhydrolase domain-containing protein 6; 2-arachidonoylglycerol hydrolase TTSINOV GN ABHD6 TTSINOV FC Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol. Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways. Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids. Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism. BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting. TTSINOV EC EC 3.1.1.23 TTSINOV SQ MDLDVVNMFVIAGGTLAIPILAFVASFLLWPSALIRIYYWYWRRTLGMQVRYVHHEDYQFCYSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEKIPLIPSTPEEMSEMLQLCSYVRFKVPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASVHNTDNNKKLD TTSINOV TT Patented-recorded TTSINOV FM AB hydrolase superfamily TTSINOV KE hsa04723:Retrograde endocannabinoid signaling TTH5TC2 ID TTH5TC2 TTH5TC2 TN NF-kappa-B-activating kinase (TBK1) TTH5TC2 UP Q9UHD2 TTH5TC2 UC TBK1_HUMAN TTH5TC2 BC Kinase TTH5TC2 SN TANK-binding kinase 1; T2K; Serine/threonine-protein kinase TBK1; NAK TTH5TC2 GN TBK1 TTH5TC2 FC Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB. In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli. Plays a key role in IRF3 activation: acts by first phosphorylating innate adapter proteins MAVS, TMEM173/STING and TICAM1 on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1. Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce expression of interferons. Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes. Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus. Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy. Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation. Phosphorylates and activates AKT1. Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C. Phosphorylates Borna disease virus (BDV) P protein. Plays an essential role in the TLR3- and IFN-dependent control of herpes virus HSV-1 and HSV-2 infections in the central nervous system. Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents. TTH5TC2 EC EC 2.7.11.1 TTH5TC2 PD 6O8B; 6NT9; 6CQ5; 6CQ4; 6CQ0 TTH5TC2 SQ MQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPVDVQMREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQFFAETSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSREPLNTIGLIYEKISLPKVHPRYDLDGDASMAKAITGVVCYACRIASTLLLYQELMRKGIRWLIELIKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEKLMKINLEAAELGEISDIHTKLLRLSSSQGTIETSLQDIDSRLSPGGSLADAWAHQEGTHPKDRNVEKLQVLLNCMTEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAMTHFTDECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTNELQETLPQKMFTASSGIKHTMTPIYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL TTH5TC2 TT Patented-recorded TTSFWA7 ID TTSFWA7 TTSFWA7 TN Plasmodium CDK Pfmrk (Malaria Pfmrk) TTSFWA7 UP P90584 TTSFWA7 UC P90584_PLAFA TTSFWA7 BC Kinase TTSFWA7 SN Pfmrk; MO15-related protein kinase Pfmrk TTSFWA7 GN Malaria Pfmrk TTSFWA7 FC Association of Pfmrk with human cyclin H (the cyclin partner for hCDK7) or Pfcyc-1 (a cyclin homologue in P. falciparum) stimulates kinase activity in vitro. TTSFWA7 EC EC 2.7.1.37 TTSFWA7 SQ MENNSTERYIFKPNFLGEGSYGKVYKAYDTILKKEVAIKKMKLNEISNYIDDCGINFVLLREIKIMKEIKHKNIMSALDLYCEKDYINLVMEIMDYDLSKIINRKIFLTDSQKKCILLQILNGLNVLHKYYFMHRDLSPANIFINKKGEVKLADFGLCTKYGYDMYSDKLFRDKYKKNLNLTSKVVTLWYRAPELLLGSNKYNSSIDMWSFGCIFAELLLQKALFPGENEIDQLGKIFFLLGTPNENNWPEALCLPLYTEFTKATKKDFKTYFKIDDDDCIDLLTSFLKLNAHERISAEDAMKHRYFFNDPLPCDISQLPFNDL TTSFWA7 TT Patented-recorded TTD8MEH ID TTD8MEH TTD8MEH TN Poly [ADP-ribose] polymerase 3 (PARP3) TTD8MEH UP Q9Y6F1 TTD8MEH UC PARP3_HUMAN TTD8MEH BC Glycosyltransferases TTD8MEH SN pADPRT-3; hPARP-3; Protein mono-ADP-ribosyltransferase PARP3; Poly[ADP-ribose] synthase 3; PARP-3; NAD(+) ADP-ribosyltransferase 3; IRT1; DNA ADP-ribosyltransferase PARP3; ARTD3; ADPRTL3; ADPRT3; ADPRT-3; ADP-ribosyltransferase diphtheria toxin-like 3 TTD8MEH GN PARP3 TTD8MEH FC Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins. In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation. Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks. Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). Cooperates with the XRRC6-XRCC5 (Ku70-Ku80) heterodimer to limit end-resection thereby promoting accurate NHEJ. Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as XRRC5 and XRCC6. ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks. Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin. Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage. TTD8MEH EC EC 2.4.2.- TTD8MEH PD 4L7U; 4L7R; 4L7P; 4L7O; 4L7N TTD8MEH SQ MAPKPKPWVQTEGPEKKKGRQAGREEDPFRSTAEALKAIPAEKRIIRVDPTCPLSSNPGTQVYEDYNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNRWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTKNNWAERDHFVSHPGKYTLIEVQAEDEAQEAVVKVDRGPVRTVTKRVQPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEALKGPTDGGQSLEELSSHFYTVIPHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQAVSEQEKTVEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQTGSNHRCPTLQHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHSGGRVGKGIYFASENSKSAGYVIGMKCGAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPTQDTELELDGQQVVVPQGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVHL TTD8MEH TT Patented-recorded TT5OU0D ID TT5OU0D TT5OU0D TN PRKR-like endoplasmic reticulum kinase (PERK) TT5OU0D UP Q9NZJ5 TT5OU0D UC E2AK3_HUMAN TT5OU0D BC Kinase TT5OU0D SN PEK TT5OU0D GN EIF2AK3 TT5OU0D FC Converts phosphorylated eIF-2-alpha/EIF2S1 either in a global protein synthesis inhibitor, leading to a reduced overall utilization of amino acids, or to a translation initiation activator of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function. Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' during the unfolded protein response (UPR) and in response to low amino acid availability. TT5OU0D EC EC 2.7.11.1 TT5OU0D PD 5SV7; 4YZS; 4X7O; 4X7N; 4X7L TT5OU0D SQ MERAISPGLLVRALLLLLLLLGLAARTVAAGRARGLPAPTAEAAFGLGAAAAPTSATRVPAAGAVAAAEVTVEDAEALPAAAGEQEPRGPEPDDETELRPRGRSLVIISTLDGRIAALDPENHGKKQWDLDVGSGSLVSSSLSKPEVFGNKMIIPSLDGALFQWDQDRESMETVPFTVESLLESSYKFGDDVVLVGGKSLTTYGLSAYSGKVRYICSALGCRQWDSDEMEQEEDILLLQRTQKTVRAVGPRSGNEKWNFSVGHFELRYIPDMETRAGFIESTFKPNENTEESKIISDVEEQEAAIMDIVIKVSVADWKVMAFSKKGGHLEWEYQFCTPIASAWLLKDGKVIPISLFDDTSYTSNDDVLEDEEDIVEAARGATENSVYLGMYRGQLYLQSSVRISEKFPSSPKALESVTNENAIIPLPTIKWKPLIHSPSRTPVLVGSDEFDKCLSNDKFSHEEYSNGALSILQYPYDNGYYLPYYKRERNKRSTQITVRFLDNPHYNKNIRKKDPVLLLHWWKEIVATILFCIIATTFIVRRLFHPHPHRQRKESETQCQTENKYDSVSGEANDSSWNDIKNSGYISRYLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAIKRIRLPNRELAREKVMREVKALAKLEHPGIVRYFNAWLEAPPEKWQEKMDEIWLKDESTDWPLSSPSPMDAPSVKIRRMDPFATKEHIEIIAPSPQRSRSFSVGISCDQTSSSESQFSPLEFSGMDHEDISESVDAAYNLQDSCLTDCDVEDGTMDGNDEGHSFELCPSEASPYVRSRERTSSSIVFEDSGCDNASSKEEPKTNRLHIGNHCANKLTAFKPTSSKSSSEATLSISPPRPTTLSLDLTKNTTEKLQPSSPKVYLYIQMQLCRKENLKDWMNGRCTIEERERSVCLHIFLQIAEAVEFLHSKGLMHRDLKPSNIFFTMDDVVKVGDFGLVTAMDQDEEEQTVLTPMPAYARHTGQVGTKLYMSPEQIHGNSYSHKVDIFSLGLILFELLYPFSTQMERVRTLTDVRNLKFPPLFTQKYPCEYVMVQDMLSPSPMERPEAINIIENAVFEDLDFPGKTVLRQRSRSLSSSGTKHSRQSNNSHSPLPSN TT5OU0D TT Patented-recorded TTTJZ4M ID TTTJZ4M TTTJZ4M TN Prolylcarboxypeptidase (PRCP) TTTJZ4M UP P42785 TTTJZ4M UC PCP_HUMAN TTTJZ4M BC Peptidase TTTJZ4M SN Proline carboxypeptidase; PCP; Lysosomal carboxypeptidase C; Lysosomal Pro-X carboxypeptidase; Angiotensinase C TTTJZ4M GN PRCP TTTJZ4M FC Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. TTTJZ4M EC EC 3.4.16.2 TTTJZ4M PD 3N2Z TTTJZ4M SQ MGRRALLLLLLSFLAPWATIALRPALRALGSLHLPTNPTSLPAVAKNYSVLYFQQKVDHFGFNTVKTFNQRYLVADKYWKKNGGSILFYTGNEGDIIWFCNNTGFMWDVAEELKAMLVFAEHRYYGESLPFGDNSFKDSRHLNFLTSEQALADFAELIKHLKRTIPGAENQPVIAIGGSYGGMLAAWFRMKYPHMVVGALAASAPIWQFEDLVPCGVFMKIVTTDFRKSGPHCSESIHRSWDAINRLSNTGSGLQWLTGALHLCSPLTSQDIQHLKDWISETWVNLAMVDYPYASNFLQPLPAWPIKVVCQYLKNPNVSDSLLLQNIFQALNVYYNYSGQVKCLNISETATSSLGTLGWSYQACTEVVMPFCTNGVDDMFEPHSWNLKELSDDCFQQWGVRPRPSWITTMYGGKNISSHTNIVFSNGELDPWSGGGVTKDITDTLVAVTISEGAHHLDLRTKNALDPMSVLLARSLEVRHMKNWIRDFYDSAGKQH TTTJZ4M TT Patented-recorded TT8EPLT ID TT8EPLT TT8EPLT TN Proteasome beta-1 (PS beta-1) TT8EPLT UP P28072 TT8EPLT UC PSB6_HUMAN TT8EPLT BC Peptidase TT8EPLT SN Proteasome subunit beta type-6; Proteasome subunit Y; Proteasome delta chain; Multicatalytic endopeptidase complex delta chain; Macropain delta chain; LMPY TT8EPLT GN PSMB6 TT8EPLT FC Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB6 displays a peptidylglutamyl-hydrolizing activity also termed postacidic or caspase-like activity, meaning that the peptides bond hydrolysis occurs directly after acidic residues. TT8EPLT EC EC 3.4.25.1 TT8EPLT PD 6MSK; 6MSJ; 6MSH; 6MSG; 6MSE TT8EPLT SQ MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA TT8EPLT TT Patented-recorded TTEAD9J ID TTEAD9J TTEAD9J TN Proteasome beta-8 (PS beta-8) TTEAD9J UP P28062 TTEAD9J UC PSB8_HUMAN TTEAD9J BC Peptidase TTEAD9J SN Y2; Really interesting new gene 10 protein; RING10; Proteasome subunit beta-5i; Proteasome subunit beta type-8; Proteasome component C13; PSMB5i; Multicatalytic endopeptidase complex subunit C13; Macropain subunit C13; Low molecular mass protein 7; LMP7 TTEAD9J GN PSMB8 TTEAD9J FC The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. TTEAD9J EC EC 3.4.25.1 TTEAD9J PD 6AVO; 5M2B; 5LTT; 5L5V; 5L5U TTEAD9J SQ MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ TTEAD9J TT Clinical trial TTXQ54R ID TTXQ54R TTXQ54R TN Protein phosphatase methylesterase 1 (PME-1) TTXQ54R UP Q9Y570 TTXQ54R UC PPME1_HUMAN TTXQ54R BC Carboxylic ester hydrolase TTXQ54R SN PRO0750; PP2593; PME1 TTXQ54R GN PPME1 TTXQ54R FC Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme. Demethylates proteins that have been reversibly carboxymethylated. TTXQ54R EC EC 3.1.1.89 TTXQ54R PD 3C5W; 3C5V TTXQ54R SQ MSALEKSMHLGRLPSRPPLPGSGGSQSGAKMRMGPGRKRDFSPVPWSQYFESMEDVEVENETGKDTFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETKVKNPEDLSAETMAKDVGNVVEAMYGDLPPPIMLIGHSMGGAIAVHTASSNLVPSLLGLCMIDVVEGTAMDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNLESARVSMVGQVKQCEGITSPEGSKSIVEGIIEEEEEDEEGSESISKRKKEDDMETKKDHPYTWRIELAKTEKYWDGWFRGLSNLFLSCPIPKLLLLAGVDRLDKDLTIGQMQGKFQMQVLPQCGHAVHEDAPDKVAEAVATFLIRHRFAEPIGGFQCVFPGC TTXQ54R TT Patented-recorded TTQR74A ID TTQR74A TTQR74A TN Proteinase activated receptor 2 (PAR2) TTQR74A UP P55085 TTQR74A UC PAR2_HUMAN TTQR74A BC GPCR rhodopsin TTQR74A SN Thrombin receptor-like 1; Proteinase-activated receptor-2; Proteinase-activated receptor 2; Protease activated receptor 2; PAR-2; GPR11; G-protein coupled receptor 11; Coagulation factor II receptor-like 1 TTQR74A GN F2RL1 TTQR74A FC Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho. Can also be transactivated by cleaved F2R/PAR1. Involved in modulation of inflammatory responses and regulation of innate and adaptive immunity, and acts as a sensor for proteolytic enzymes generated during infection. Generally is promoting inflammation. Can signal synergistically with TLR4 and probably TLR2 in inflammatory responses and modulates TLR3 signaling. Has a protective role in establishing the endothelial barrier; the activity involves coagulation factor X. Regulates endothelial cell barrier integrity during neutrophil extravasation, probably following proteolytic cleavage by PRTN3. Proposed to have a bronchoprotective role in airway epithelium, but also shown to compromise the airway epithelial barrier by interrupting E-cadherin adhesion. Involved in the regulation of vascular tone; activation results in hypotension presumably mediated by vasodilation. Associates with a subset of G proteins alpha subunits such as GNAQ, GNA11, GNA14, GNA12 and GNA13, but probably not with G(o) alpha, G(i) subunit alpha-1 and G(i) subunit alpha-2. However, according to can signal through G(i) subunit alpha. Believed to be a class B receptor which internalizes as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptor, for extended periods of time. Mediates inhibition of TNF-alpha stimulated JNK phosphorylation via coupling to GNAQ and GNA11; the function involves dissociation of RIPK1 and TRADD from TNFR1. Mediates phosphorylation of nuclear factor NF-kappa-B RELA subunit at 'Ser-536'; the function involves IKBKB and is predominantly independent of G proteins. Involved in cellular migration. Involved in cytoskeletal rearrangement and chemotaxis through beta-arrestin-promoted scaffolds; the function is independent of GNAQ and GNA11 and involves promotion of cofilin dephosphorylation and actin filament severing. Induces redistribution of COPS5 from the plasma membrane to the cytosol and activation of the JNK cascade is mediated by COPS5. Involved in the recruitment of leukocytes to the sites of inflammation and is the major PAR receptor capable of modulating eosinophil function such as proinflammatory cytokine secretion, superoxide production and degranulation. During inflammation promotes dendritic cell maturation, trafficking to the lymph nodes and subsequent T-cell activation. Involved in antimicrobial response of innate immnune cells; activation enhances phagocytosis of Gram-positive and killing of Gram-negative bacteria. Acts synergistically with interferon-gamma in enhancing antiviral responses. Implicated in a number of acute and chronic inflammatory diseases such as of the joints, lungs, brain, gastrointestinal tract, periodontium, skin, and vascular systems, and in autoimmune disorders. Receptor for trypsin and trypsin-like enzymes coupled to G proteins. TTQR74A PD 5NJ6; 5NDZ; 5NDD TTQR74A SQ MRSPSAAWLLGAAILLAASLSCSGTIQGTNRSSKGRSLIGKVDGTSHVTGKGVTVETVFSVDEFSASVLTGKLTTVFLPIVYTIVFVVGLPSNGMALWVFLFRTKKKHPAVIYMANLALADLLSVIWFPLKIAYHIHGNNWIYGEALCNVLIGFFYGNMYCSILFMTCLSVQRYWVIVNPMGHSRKKANIAIGISLAIWLLILLVTIPLYVVKQTIFIPALNITTCHDVLPEQLLVGDMFNYFLSLAIGVFLFPAFLTASAYVLMIRMLRSSAMDENSEKKRKRAIKLIVTVLAMYLICFTPSNLLLVVHYFLIKSQGQSHVYALYIVALCLSTLNSCIDPFVYYFVSHDFRDHAKNALLCRSVRTVKQMQVSLTSKKHSRKSSSYSSSSTTVKTSY TTQR74A TT Patented-recorded TTQR74A FM GPCR rhodopsin TTQR74A KE hsa04080:Neuroactive ligand-receptor interaction; hsa04750:Inflammatory mediator regulation of TRP channels; hsa05143:African trypanosomiasis TTQR74A RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTY0WT7 ID TTY0WT7 TTY0WT7 TN RET G691S mutant (RET G691S) TTY0WT7 UP P07949 TTY0WT7 UC RET_HUMAN TTY0WT7 BC Kinase TTY0WT7 SN RET51 G691S mutant; Proto-oncogene tyrosine-protein kinase receptor Ret G691S mutant; Proto-oncogene c-Ret G691S mutant; PTC G691S mutant; Cadherin family member 12 G691S mutant; CDHR16 G691S mutant; CDHF12 G691S mutant TTY0WT7 GN RET TTY0WT7 FC Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e. g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration. Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways. Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL. Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. TTY0WT7 EC EC 2.7.10.1 TTY0WT7 PD 6FEK; 5FM3; 5FM2; 5AMN; 4UX8 TTY0WT7 SQ MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNRNLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPRGIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCRTVIAAAVLFSFIVSVLLSAFCIHCYHKFAHKPPISSAEMTFRRPAQAFPVSYSSSGARRPSLDSMENQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPSDSLIYDDGLSEEETPLVDCNNAPLPRALPSTWIENKLYGMSDPNWPGESPVPLTRADGTNTGFPRYPNDSVYANWMLSPSAAKLMDTFDS TTY0WT7 TT Patented-recorded TTY0WT7 FM Protein kinase superfamily. Tyr protein kinase family TT5XA6U ID TT5XA6U TT5XA6U TN RET M918T mutant (RET M918T) TT5XA6U UP P07949 TT5XA6U UC RET_HUMAN TT5XA6U BC Kinase TT5XA6U SN RET51 M918T mutant; Proto-oncogene tyrosine-protein kinase receptor Ret M918T mutant; Proto-oncogene c-Ret M918T mutant; PTC M918T mutant; Cadherin family member 12 M918T mutant; CDHR16 M918T mutant; CDHF12 M918T mutant TT5XA6U GN RET TT5XA6U FC Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e. g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration. Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways. Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL. Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. TT5XA6U EC EC 2.7.10.1 TT5XA6U PD 6FEK; 5FM3; 5FM2; 5AMN; 4UX8 TT5XA6U SQ MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNRNLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPRGIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCRTVIAAAVLFSFIVSVLLSAFCIHCYHKFAHKPPISSAEMTFRRPAQAFPVSYSSSGARRPSLDSMENQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPSDSLIYDDGLSEEETPLVDCNNAPLPRALPSTWIENKLYGMSDPNWPGESPVPLTRADGTNTGFPRYPNDSVYANWMLSPSAAKLMDTFDS TT5XA6U TT Patented-recorded TT5XA6U FM Protein kinase superfamily. Tyr protein kinase family TT8BF4A ID TT8BF4A TT8BF4A TN RET S891A mutant (RET S891A) TT8BF4A UP P07949 TT8BF4A UC RET_HUMAN TT8BF4A BC Kinase TT8BF4A SN RET51 S891A mutant; Proto-oncogene tyrosine-protein kinase receptor Ret S891A mutant; Proto-oncogene c-Ret S891A mutant; PTC S891A mutant; Cadherin family member 12 S891A mutant; CDHR16 S891A mutant; CDHF12 S891A mutant TT8BF4A GN RET TT8BF4A FC Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e. g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration. Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways. Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL. Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. TT8BF4A EC EC 2.7.10.1 TT8BF4A PD 6FEK; 5FM3; 5FM2; 5AMN; 4UX8 TT8BF4A SQ MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNRNLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPRGIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCRTVIAAAVLFSFIVSVLLSAFCIHCYHKFAHKPPISSAEMTFRRPAQAFPVSYSSSGARRPSLDSMENQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPSDSLIYDDGLSEEETPLVDCNNAPLPRALPSTWIENKLYGMSDPNWPGESPVPLTRADGTNTGFPRYPNDSVYANWMLSPSAAKLMDTFDS TT8BF4A TT Patented-recorded TT8BF4A FM Protein kinase superfamily. Tyr protein kinase family TT2RTDH ID TT2RTDH TT2RTDH TN RET V804L mutant (RET V804L) TT2RTDH UP P07949 TT2RTDH UC RET_HUMAN TT2RTDH BC Kinase TT2RTDH SN RET51 V804L mutant; Proto-oncogene tyrosine-protein kinase receptor Ret V804L mutant; Proto-oncogene c-Ret V804L mutant; PTC V804L mutant; Cadherin family member 12 V804L mutant; CDHR16 V804L mutant; CDHF12 V804L mutant TT2RTDH GN RET TT2RTDH FC Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e. g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration. Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways. Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL. Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. TT2RTDH EC EC 2.7.10.1 TT2RTDH PD 6FEK; 5FM3; 5FM2; 5AMN; 4UX8 TT2RTDH SQ MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNRNLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPRGIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCRTVIAAAVLFSFIVSVLLSAFCIHCYHKFAHKPPISSAEMTFRRPAQAFPVSYSSSGARRPSLDSMENQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPSDSLIYDDGLSEEETPLVDCNNAPLPRALPSTWIENKLYGMSDPNWPGESPVPLTRADGTNTGFPRYPNDSVYANWMLSPSAAKLMDTFDS TT2RTDH TT Patented-recorded TT2RTDH FM Protein kinase superfamily. Tyr protein kinase family TTQV3NX ID TTQV3NX TTQV3NX TN RET V804M mutant (RET V804M) TTQV3NX UP P07949 TTQV3NX UC RET_HUMAN TTQV3NX BC Kinase TTQV3NX SN RET51 V804M mutant; Proto-oncogene tyrosine-protein kinase receptor Ret V804M mutant; Proto-oncogene c-Ret V804M mutant; PTC V804M mutant; Cadherin family member 12 V804M mutant; CDHR16 V804M mutant; CDHF12 V804M mutant TTQV3NX GN RET TTQV3NX FC Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e. g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration. Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways. Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL. Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. TTQV3NX EC EC 2.7.10.1 TTQV3NX PD 6FEK; 5FM3; 5FM2; 5AMN; 4UX8 TTQV3NX SQ MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNRNLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPRGIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCRTVIAAAVLFSFIVSVLLSAFCIHCYHKFAHKPPISSAEMTFRRPAQAFPVSYSSSGARRPSLDSMENQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPSDSLIYDDGLSEEETPLVDCNNAPLPRALPSTWIENKLYGMSDPNWPGESPVPLTRADGTNTGFPRYPNDSVYANWMLSPSAAKLMDTFDS TTQV3NX TT Patented-recorded TTQV3NX FM Protein kinase superfamily. Tyr protein kinase family TTB0IO2 ID TTB0IO2 TTB0IO2 TN RET Y791F mutant (RET Y791F) TTB0IO2 UP P07949 TTB0IO2 UC RET_HUMAN TTB0IO2 BC Kinase TTB0IO2 SN RET51 Y791F mutant; Proto-oncogene tyrosine-protein kinase receptor Ret Y791F mutant; Proto-oncogene c-Ret Y791F mutant; PTC Y791F mutant; Cadherin family member 12 Y791F mutant; CDHR16 Y791F mutant; CDHF12 Y791F mutant TTB0IO2 GN RET TTB0IO2 FC Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e. g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration. Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways. Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL. Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. TTB0IO2 EC EC 2.7.10.1 TTB0IO2 PD 6FEK; 5FM3; 5FM2; 5AMN; 4UX8 TTB0IO2 SQ MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNRNLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPRGIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCRTVIAAAVLFSFIVSVLLSAFCIHCYHKFAHKPPISSAEMTFRRPAQAFPVSYSSSGARRPSLDSMENQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPSDSLIYDDGLSEEETPLVDCNNAPLPRALPSTWIENKLYGMSDPNWPGESPVPLTRADGTNTGFPRYPNDSVYANWMLSPSAAKLMDTFDS TTB0IO2 TT Patented-recorded TTB0IO2 FM Protein kinase superfamily. Tyr protein kinase family TTIXKA4 ID TTIXKA4 TTIXKA4 TN Ribosomal protein S6 kinase alpha-1 (RSK1) TTIXKA4 UP Q15418 TTIXKA4 UC KS6A1_HUMAN TTIXKA4 BC Kinase TTIXKA4 SN p90S6K; p90RSK1; p90-RSK 1; S6K-alpha-1; Ribosomal S6 kinase 1; RSK-1; MAPKAPK1A; MAPKAPK-1a; MAPKAP kinase 1a; MAPK-activated protein kinase 1a; MAP kinase-activated protein kinase 1a; 90 kDa ribosomal protein S6 kinase 1 TTIXKA4 GN RPS6KA1 TTIXKA4 FC In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB. Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration. Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. TTIXKA4 EC EC 2.7.11.1 TTIXKA4 PD 5V62; 5V61; 5N7G; 5N7F; 5N7D TTIXKA4 SQ MPLAQLKEPWPLMELVPLDPENGQTSGEEAGLQPSKDEGVLKEISITHHVKAGSEKADPSHFELLKVLGQGSFGKVFLVRKVTRPDSGHLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFVVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALGLDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEAIDHEKKAYSFCGTVEYMAPEVVNRQGHSHSADWWSYGVLMFEMLTGSLPFQGKDRKETMTLILKAKLGMPQFLSTEAQSLLRALFKRNPANRLGSGPDGAEEIKRHVFYSTIDWNKLYRREIKPPFKPAVAQPDDTFYFDTEFTSRTPKDSPGIPPSAGAHQLFRGFSFVATGLMEDDGKPRAPQAPLHSVVQQLHGKNLVFSDGYVVKETIGVGSYSECKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASFVLHTIGKTVEYLHSQGVVHRDLKPSNILYVDESGNPECLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSETAKDLVSKMLHVDPHQRLTAKQVLQHPWVTQKDKLPQSQLSHQDLQLVKGAMAATYSALNSSKPTPQLKPIESSILAQRRVRKLPSTTL TTIXKA4 TT Patented-recorded TTUM2ZR ID TTUM2ZR TTUM2ZR TN Ribosomal protein S6 kinase alpha-3 (RSK3) TTUM2ZR UP P51812 TTUM2ZR UC KS6A3_HUMAN TTUM2ZR BC Kinase TTUM2ZR SN pp90RSK2; p90RSK3; p90-RSK 3; S6K-alpha-3; Ribosomal S6 kinase 2; RSK2; RSK-2; MAPKAPK1B; MAPKAPK-1b; MAPKAP kinase 1b; MAPK-activated protein kinase 1b; MAP kinase-activated protein kinase 1b; Insulin-stimulated protein kinase 1; ISPK1; ISPK-1; 90 kDa ribosomal protein S6 kinase 3 TTUM2ZR GN RPS6KA3 TTUM2ZR FC In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1. Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation. Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration. Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. TTUM2ZR EC EC 2.7.11.1 TTUM2ZR PD 5D9L; 5D9K; 4NW6; 4NW5; 4NUS TTUM2ZR SQ MPLAQLADPWQKMAVESPSDSAENGQQIMDEPMGEEEINPQTEEVSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQAMQTVGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQRRGIKKITSTAL TTUM2ZR TT Patented-recorded TTVUSO7 ID TTVUSO7 TTVUSO7 TN Tankyrase-1 (TNKS-1) TTVUSO7 UP O95271 TTVUSO7 UC TNKS1_HUMAN TTVUSO7 BC Glycosyltransferases TTVUSO7 SN Tankyrase I; TRF1-interacting ankyrin-related ADP-ribose polymerase; TNKS1; TINF1; TIN1; TANK1; Protein poly-ADP-ribosyltransferase tankyrase-1; Poly [ADP-ribose] polymerase tankyrase-1; Poly [ADP-ribose] polymerase 5A; PARPL; PARP5A; ARTD5; ADP-ribosyltransferase diphtheria toxin-like 5 TTVUSO7 GN TNKS TTVUSO7 FC Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Stimulates 26S proteasome activity. Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. TTVUSO7 EC EC 2.4.2.30 TTVUSO7 PD 5KNI; 5JU5; 5JTI; 5JHQ; 5GP7 TTVUSO7 SQ MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPRHGLALPEGDGSRDPPDRPRSPDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNPAGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVSSTAPLGPGAAGPGTGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILSESTPIRTSDVDYRLLEASKAGDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDLLRGDAALLDAAKKGCLARVQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEALPTCFKPQATVVSASLISPASTPSCLSAASSIDNLTGPLAELAVGGASNAGDGAAGTERKEGEVAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTATAAEQKT TTVUSO7 TT Clinical trial TTFQI4H ID TTFQI4H TTFQI4H TN Tankyrase-2 (TNKS-2) TTFQI4H UP Q9H2K2 TTFQI4H UC TNKS2_HUMAN TTFQI4H BC Glycosyltransferases TTFQI4H SN Tankyrase-related protein; Tankyrase-like protein; Tankyrase II; TRF1-interacting ankyrin-related ADP-ribose polymerase 2; TNKL; TANK2; Protein poly-ADP-ribosyltransferase tankyrase-2; Poly [ADP-ribose] polymerase tankyrase-2; Poly [ADP-ribose] polymerase 5B; PARP5B; ARTD6; ADP-ribosyltransferase diphtheria toxin-like 6 TTFQI4H GN TNKS2 TTFQI4H FC Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. Stimulates 26S proteasome activity. Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. TTFQI4H EC EC 2.4.2.30 TTFQI4H PD 5OWT; 5OWS; 5NUT; 5NSP; 5NOB TTFQI4H SQ MSGRRCAGGGAACASAAAEAVEPAARELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQMGNENVQQLLQEGISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAALLDAAKKGCLARVKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTAAMPPSALPSCYKPQVLNGVRSPGATADALSSGPSSPSSLSAASSLDNLSGSFSELSSVVSSSGTEGASSLEKKEVPGVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISGQQGLNPYLTLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRPEGMVDG TTFQI4H TT Clinical trial TTW14D0 ID TTW14D0 TTW14D0 TN Toll-like receptor 1 (TLR1) TTW14D0 UP Q15399 TTW14D0 UC TLR1_HUMAN TTW14D0 BC Toll-like receptor TTW14D0 SN Toll/interleukin-1 receptor-like protein; TIL; KIAA0012; CD281 TTW14D0 GN TLR1 TTW14D0 FC Specifically recognizes diacylated and triacylated lipopeptides. Cooperates with TLR2 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Forms the activation cluster TLR2:TLR1:CD14 in response to triacylated lipopeptides, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Participates in the innate immune response to microbial agents. TTW14D0 PD 6NIH; 2Z7X; 1FYV TTW14D0 SQ MTSIFHFAIIFMLILQIRIQLSEESEFLVDRSKNGLIHVPKDLSQKTTILNISQNYISELWTSDILSLSKLRILIISHNRIQYLDISVFKFNQELEYLDLSHNKLVKISCHPTVNLKHLDLSFNAFDALPICKEFGNMSQLKFLGLSTTHLEKSSVLPIAHLNISKVLLVLGETYGEKEDPEGLQDFNTESLHIVFPTNKEFHFILDVSVKTVANLELSNIKCVLEDNKCSYFLSILAKLQTNPKLSNLTLNNIETTWNSFIRILQLVWHTTVWYFSISNVKLQGQLDFRDFDYSGTSLKALSIHQVVSDVFGFPQSYIYEIFSNMNIKNFTVSGTRMVHMLCPSKISPFLHLDFSNNLLTDTVFENCGHLTELETLILQMNQLKELSKIAEMTTQMKSLQQLDISQNSVSYDEKKGDCSWTKSLLSLNMSSNILTDTIFRCLPPRIKVLDLHSNKIKSIPKQVVKLEALQELNVAFNSLTDLPGCGSFSSLSVLIIDHNSVSHPSADFFQSCQKMRSIKAGDNPFQCTCELGEFVKNIDQVSSEVLEGWPDSYKCDYPESYRGTLLKDFHMSELSCNITLLIVTIVATMLVLAVTVTSLCSYLDLPWYLRMVCQWTQTRRRARNIPLEELQRNLQFHAFISYSGHDSFWVKNELLPNLEKEGMQICLHERNFVPGKSIVENIITCIEKSYKSIFVLSPNFVQSEWCHYELYFAHHNLFHEGSNSLILILLEPIPQYSIPSSYHKLKSLMARRTYLEWPKEKSKRGLFWANLRAAINIKLTEQAKK TTW14D0 TT Patented-recorded TTW14D0 FM Toll-like receptor family TTW14D0 KE hsa04620:Toll-like receptor signaling pathway; hsa05152:Tuberculosis TT1ZV49 ID TT1ZV49 TT1ZV49 TN Tyrosine-protein kinase Tec (PSCTK4) TT1ZV49 UP P42680 TT1ZV49 UC TEC_HUMAN TT1ZV49 BC Kinase TT1ZV49 SN Tec protein tyrosine kinase TT1ZV49 GN TEC TT1ZV49 FC Plays a redundant role to ITK in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. Required for TCR-dependent IL2 gene induction. Phosphorylates DOK1, one CD28-specific substrate, and contributes to CD28-signaling. Mediates signals that negatively regulate IL2RA expression induced by TCR cross-linking. Plays a redundant role to BTK in BCR-signaling for B-cell development and activation, especially by phosphorylating STAP1, a BCR-signaling protein. Required in mast cells for efficient cytokine production. Involved in both growth and differentiation mechanisms of myeloid cells through activation by the granulocyte colony-stimulating factor CSF3, a critical cytokine to promoting the growth, differentiation, and functional activation of myeloid cells. Participates in platelet signaling downstream of integrin activation. Cooperates with JAK2 through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. GRB10, a negative modifier of the FOS activation pathway, is another substrate of TEC. TEC is involved in G protein-coupled receptor- and integrin-mediated signalings in blood platelets. Plays a role in hepatocyte proliferation and liver regeneration and is involved in HGF-induced ERK signaling pathway. TEC regulates also FGF2 unconventional secretion (endoplasmic reticulum (ER)/Golgi-independent mechanism) under various physiological conditions through phosphorylation of FGF2 'Tyr-215'. May also be involved in the regulation of osteoclast differentiation. Non-receptor tyrosine kinase that contributes to signaling from many receptors and participates as a signal transducer in multiple downstream pathways, including regulation of the actin cytoskeleton. TT1ZV49 EC EC 2.7.10.2 TT1ZV49 PD 2LUL TT1ZV49 SQ MNFNTILEEILIKRSQQKKKTSPLNYKERLFVLTKSMLTYYEGRAEKKYRKGFIDVSKIKCVEIVKNDDGVIPCQNKYPFQVVHDANTLYIFAPSPQSRDLWVKKLKEEIKNNNNIMIKYHPKFWTDGSYQCCRQTEKLAPGCEKYNLFESSIRKALPPAPETKKRRPPPPIPLEEEDNSEEIVVAMYDFQAAEGHDLRLERGQEYLILEKNDVHWWRARDKYGNEGYIPSNYVTGKKSNNLDQYEWYCRNMNRSKAEQLLRSEDKEGGFMVRDSSQPGLYTVSLYTKFGGEGSSGFRHYHIKETTTSPKKYYLAEKHAFGSIPEIIEYHKHNAAGLVTRLRYPVSVKGKNAPTTAGFSYEKWEINPSELTFMRELGSGLFGVVRLGKWRAQYKVAIKAIREGAMCEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMERGCLLNFLRQRQGHFSRDVLLSMCQDVCEGMEYLERNSFIHRDLAARNCLVSEAGVVKVSDFGMARYVLDDQYTSSSGAKFPVKWCPPEVFNYSRFSSKSDVWSFGVLMWEVFTEGRMPFEKYTNYEVVTMVTRGHRLYQPKLASNYVYEVMLRCWQEKPEGRPSFEDLLRTIDELVECEETFGR TT1ZV49 TT Patented-recorded TT64IHJ ID TT64IHJ TT64IHJ TN Tyrosyl-DNA phosphodiesterase 1 (TDP1) TT64IHJ UP Q9NUW8 TT64IHJ UC TYDP1_HUMAN TT64IHJ BC Phosphoric diester hydrolase TT64IHJ SN Tyr-DNA phosphodiesterase 1 TT64IHJ GN TDP1 TT64IHJ FC Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. Has low 3'exonuclease activity and can remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate. DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. TT64IHJ EC EC 3.1.4.- TT64IHJ PD 5NWA; 5NW9; 1RH0; 1RGU; 1RGT TT64IHJ SQ MSQEGDYGRWTISSSDESEEEKPKPDKPSTSSLLCARQGAANEPRYTCSEAQKAAHKRKISPVKFSNTDSVLPPKRQKSGSQEDLGWCLSSSDDELQPEMPQKQAEKVVIKKEKDISAPNDGTAQRTENHGAPACHRLKEEEDEYETSGEGQDIWDMLDKGNPFQFYLTRVSGVKPKYNSGALHIKDILSPLFGTLVSSAQFNYCFDVDWLVKQYPPEFRKKPILLVHGDKREAKAHLHAQAKPYENISLCQAKLDIAFGTHHTKMMLLLYEEGLRVVIHTSNLIHADWHQKTQGIWLSPLYPRIADGTHKSGESPTHFKADLISYLMAYNAPSLKEWIDVIHKHDLSETNVYLIGSTPGRFQGSQKDNWGHFRLKKLLKDHASSMPNAESWPVVGQFSSVGSLGADESKWLCSEFKESMLTLGKESKTPGKSSVPLYLIYPSVENVRTSLEGYPAGGSLPYSIQTAEKQNWLHSYFHKWSAETSGRSNAMPHIKTYMRPSPDFSKIAWFLVTSANLSKAAWGALEKNGTQLMIRSYELGVLFLPSAFGLDSFKVKQKFFAGSQEPMATFPVPYDLPPELYGSKDRPWIWNIPYVKAPDTHGNMWVPS TT64IHJ TT Patented-recorded TT64IHJ FM Phosphoric diester hydrolases TTVSYP9 ID TTVSYP9 TTVSYP9 TN Ubiquitin carboxyl-terminal hydrolase 14 (USP14) TTVSYP9 UP P54578 TTVSYP9 UC UBP14_HUMAN TTVSYP9 BC Peptidase TTVSYP9 SN Ubiquitin-specific-processing protease 14; Ubiquitin thioesterase 14; TGT; Deubiquitinating enzyme 14 TTVSYP9 GN USP14 TTVSYP9 FC Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation. Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. TTVSYP9 EC EC 3.4.19.12 TTVSYP9 PD 6IIN; 6IIM; 6IIL; 6IIK; 5GJQ TTVSYP9 SQ MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGNIKIKNGMTLLMMGSADALPEEPSAKTVFVEDMTEEQLASAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSDKKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ TTVSYP9 TT Preclinical TTVSYP9 FM Peptidase C19 family TTSX29Z ID TTSX29Z TTSX29Z TN Ubiquitin C-terminal hydrolase UCH37 (UCHL5) TTSX29Z UP Q9Y5K5 TTSX29Z UC UCHL5_HUMAN TTSX29Z BC Peptidase TTSX29Z SN Ubiquitin thioesterase L5; Ubiquitin carboxyl-terminal hydrolase isozyme L5; UCH37; UCH-L5; CGI-70; AD-019 TTSX29Z GN UCHL5 TTSX29Z FC Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1. Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. TTSX29Z EC EC 3.4.19.12 TTSX29Z PD 4WLP; 4UF6; 4UF5; 4UEM; 4UEL TTSX29Z SQ MTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEEPMDTDQGNSMLSAIQSEVAKNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKAKEKQNAKKAQETK TTSX29Z TT Patented-recorded TTSX29Z FM Peptidase C12 family TT4E85Q ID TT4E85Q TT4E85Q TN VHL-interacting deubiquitinating enzyme 1 (VDU1) TT4E85Q UP Q8TEY7 TT4E85Q UC UBP33_HUMAN TT4E85Q BC Peptidase TT4E85Q SN hVDU1; Ubiquitin-specific-processing protease 33; Ubiquitin thioesterase 33; Ubiquitin carboxyl-terminal hydrolase 33; KIAA1097; Deubiquitinating enzyme 33 TT4E85Q GN USP33 TT4E85Q FC Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. TT4E85Q EC EC 3.4.19.12 TT4E85Q PD 2UZG TT4E85Q SQ MTGSNSHITILTLKVLPHFESLGKQEKIPNKMSAFRNHCPHLDSVGEITKEDLIQKSLGTCQDCKVQGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEVFLDRKLGTQPSLPHVRQPHQIQENSVQDFKIPSNTTLKTPLVAVFDDLDIEADEEDELRARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQVMEVEEDPQTITTEETMEEDKSQSDVDFQSCESCSNSDRAENENGSRCFSEDNNETTMLIQDDENNSEMSKDWQKEKMCNKINKVNSEGEFDKDRDSISETVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQILPSNEGVNPRLSASPPKSGNLWPGLAPPHKKAQSASPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPSWFWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQKERRRISNLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPAVNHLYICHTCQIEAEKIEKRRKTELEIFIRLNRAFQKEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCGNVMLRQGADSGQISEETWNFLQSIYGGGPEVILRPPVVHVDPDILQAEEKIEVETRSL TT4E85Q TT Patented-recorded TT4E85Q FM Peptidase C19 family TTZC0KV ID TTZC0KV TTZC0KV TN Zinc finger-containing ubiquitin peptidase 1 (ZUP1) TTZC0KV UP Q96AP4 TTZC0KV UC ZUP1_HUMAN TTZC0KV BC Peptidase TTZC0KV SN Zinc finger with UFM1-specific peptidase domain protein; ZUFSP; Lys-63-specific deubiquitinase ZUFSP; DUB; C6orf113 TTZC0KV GN ZUP1 TTZC0KV FC Shows only weak activity against 'Lys-11' and 'Lys-48'-linked chains. Plays an important role in genome stability pathways, functioning to prevent spontaneous DNA damage and also promote cellular survival in response to exogenous DNA damage. Modulates the ubiquitination status of replication protein A (RPA) complex proteins in response to replication stress. Deubiquitinase with endodeubiquitinase activity that specifically interacts with and cleaves 'Lys-63'-linked long polyubiquitin chains. TTZC0KV EC EC 3.4.19.12 TTZC0KV PD 6FGE; 6EI1 TTZC0KV SQ MLSCNICGETVTSEPDMKAHLIVHMESEIICPFCKLSGVNYDEMCFHIETAHFEQNTLERNFERINTVQYGTSDNKKDNTLQCGMEVNSSILSGCASNHPKNSAQNLTKDSTLKHEGFYSENLTESRKFLKSREKQSSLTEIKGSVYETTYSPPECPFCGKIEEHSEDMETHVKTKHANLLDIPLEDCDQPLYDCPMCGLICTNYHILQEHVDLHLEENSFQQGMDRVQCSGDLQLAHQLQQEEDRKRRSEESRQEIEEFQKLQRQYGLDNSGGYKQQQLRNMEIEVNRGRMPPSEFHRRKADMMESLALGFDDGKTKTSGIIEALHRYYQNAATDVRRVWLSSVVDHFHSSLGDKGWGCGYRNFQMLLSSLLQNDAYNDCLKGMLIPCIPKIQSMIEDAWKEGFDPQGASQLNNRLQGTKAWIGACEVYILLTSLRVKCHIVDFHKSTGPLGTHPRLFEWILNYYSSEGEGSPKVVCTSKPPIYLQHQGHSRTVIGIEEKKNRTLCLLILDPGCPSREMQKLLKQDIEASSLKQLRKSMGNLKHKQYQILAVEGALSLEEKLARRQASQVFTAEKIP TTZC0KV TT Patented-recorded TTZC0KV FM Peptidase C78 family TTNDSC3 ID TTNDSC3 TTNDSC3 TN B lymphocyte kinase (BLK) TTNDSC3 UP P51451 TTNDSC3 UC BLK_HUMAN TTNDSC3 BC Kinase TTNDSC3 SN p55-Blk; Tyrosine-protein kinase Blk TTNDSC3 GN BLK TTNDSC3 FC B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. Signaling through BLK plays an important role in transmitting signals through surface immunoglobulins and supports the pro-B to pre-B transition, as well as the signaling for growth arrest and apoptosis downstream of B-cell receptor. Specifically binds and phosphorylates CD79A at 'Tyr-188'and 'Tyr-199', as well as CD79B at 'Tyr-196' and 'Tyr-207'. Phosphorylates also the immunoglobulin G receptors FCGR2A, FCGR2B and FCGR2C. With FYN and LYN, plays an essential role in pre-B-cell receptor (pre-BCR)-mediated NF-kappa-B activation. Contributes also to BTK activation by indirectly stimulating BTK intramolecular autophosphorylation. In pancreatic islets, acts as a modulator of beta-cells function through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose. Phosphorylates CGAS, promoting retention of CGAS in the cytosol. Non-receptor tyrosine kinase involved in B-lymphocyte development, differentiation and signaling. TTNDSC3 EC EC 2.7.10.2 TTNDSC3 SQ MGLVSSKKPDKEKPIKEKDKGQWSPLKVSAQDKDAPPLPPLVVFNHLTPPPPDEHLDEDKHFVVALYDYTAMNDRDLQMLKGEKLQVLKGTGDWWLARSLVTGREGYVPSNFVARVESLEMERWFFRSQGRKEAERQLLAPINKAGSFLIRESETNKGAFSLSVKDVTTQGELIKHYKIRCLDEGGYYISPRITFPSLQALVQHYSKKGDGLCQRLTLPCVRPAPQNPWAQDEWEIPRQSLRLVRKLGSGQFGEVWMGYYKNNMKVAIKTLKEGTMSPEAFLGEANVMKALQHERLVRLYAVVTKEPIYIVTEYMARGCLLDFLKTDEGSRLSLPRLIDMSAQIAEGMAYIERMNSIHRDLRAANILVSEALCCKIADFGLARIIDSEYTAQEGAKFPIKWTAPEAIHFGVFTIKADVWSFGVLLMEVVTYGRVPYPGMSNPEVIRNLERGYRMPRPDTCPPELYRGVIAECWRSRPEERPTFEFLQSVLEDFYTATERQYELQP TTNDSC3 TT Patented-recorded TTC6S84 ID TTC6S84 TTC6S84 TN Caspase-2 (CASP2) TTC6S84 UP P42575 TTC6S84 UC CASP2_HUMAN TTC6S84 BC Peptidase TTC6S84 SN Protease ICH1; Protease ICH-1; Neural precursor cell expressed developmentally downregulated protein 2; Neural precursor cell expressed developmentally down-regulated protein 2; NEDD2; NEDD-2; ICH1; Caspase2 subunit p12; CASP-2 TTC6S84 GN CASP2 TTC6S84 FC Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival. Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress. Involved in the activation cascade of caspases responsible for apoptosis execution. TTC6S84 EC EC 3.4.22.55 TTC6S84 SQ MAAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT TTC6S84 TT Patented-recorded TTC6S84 FM Peptidase TT3VZ8D ID TT3VZ8D TT3VZ8D TN Caspase-4 (CASP4) TT3VZ8D UP P49662 TT3VZ8D UC CASP4_HUMAN TT3VZ8D BC Peptidase TT3VZ8D SN Protease TX; Mih1; ICH2; ICH-2; ICE(rel)-II; ICE and Ced-3 homolog 2; CASP-4 TT3VZ8D GN CASP4 TT3VZ8D FC Essential effector of NLRP3 inflammasome-dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation, cholera enterotoxin subunit B and cytosolic LPS. Independently of NLRP3 inflammasome and CASP1, promotes pyroptosis, through GSDMD cleavage and activation, and IL1A, IL18 and HMGB1 release in response to non-canonical inflammasome activators. Plays a crucial role in the restriction of Salmonella typhimurium replication in colonic epithelial cells during infection. In later stages of the infection, LPS from cytosolic Salmonella triggers CASP4 activation, which ultimately results in pyroptosis of infected cells and their extrusion into the gut lumen, as well as in IL18 secretion. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation. Involved in LPS-induced IL6 secretion; this activity may not require caspase enzymatic activity. Involved in cell death induced by endoplasmic reticulum stress and by treatment with cytotoxic APP peptides found Alzheimer's patient brains. Activated by direct binding to LPS without the need of an upstream sensor. Does not directly process IL1B. During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation. Inflammatory caspase. TT3VZ8D EC EC 3.4.22.57 TT3VZ8D SQ MAEGNHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQISPNKKAHPNMEAGPPESGESTDALKLCPHEEFLRLCKERAEEIYPIKERNNRTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFLVLMSHGILEGICGTVHDEKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGANRGELWVRDSPASLEVASSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPRAKAQMPTIERLSMTRYFYLFPGN TT3VZ8D TT Patented-recorded TTWR48J ID TTWR48J TTWR48J TN Caspase-5 (CASP5) TTWR48J UP P51878 TTWR48J UC CASP5_HUMAN TTWR48J BC Peptidase TTWR48J SN Protease TY; Protease ICH-3; ICH3; ICE(rel)-III; CASP-5 TTWR48J GN CASP5 TTWR48J FC During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation. Mediator of programmed cell death (apoptosis). TTWR48J EC EC 3.4.22.58 TTWR48J SQ MAEDSGKKKRRKNFEAMFKGILQSGLDNFVINHMLKNNVAGQTSIQTLVPNTDQKSTSVKKDNHKKKTVKMLEYLGKDVLHGVFNYLAKHDVLTLKEEEKKKYYDTKIEDKALILVDSLRKNRVAHQMFTQTLLNMDQKITSVKPLLQIEAGPPESAESTNILKLCPREEFLRLCKKNHDEIYPIKKREDRRRLALIICNTKFDHLPARNGAHYDIVGMKRLLQGLGYTVVDEKNLTARDMESVLRAFAARPEHKSSDSTFLVLMSHGILEGICGTAHKKKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGEKHGELWVRDSPASLALISSQSSENLEADSVCKIHEEKDFIAFCSSTPHNVSWRDRTRGSIFITELITCFQKYSCCCHLMEIFRKVQKSFEVPQAKAQMPTIERATLTRDFYLFPGN TTWR48J TT Patented-recorded TTRQ6UD ID TTRQ6UD TTRQ6UD TN Diacylglycerol lipase alpha (DAGLA) TTRQ6UD UP Q9Y4D2 TTRQ6UD UC DGLA_HUMAN TTRQ6UD BC Carboxylic ester hydrolase TTRQ6UD SN Sn1-specific diacylglycerol lipase alpha; Neural stem cell-derived dendrite regulator; NSDDR; KIAA0659; DGL-alpha; C11orf11 TTRQ6UD GN DAGLA TTRQ6UD FC Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses. TTRQ6UD EC EC 3.1.1.- TTRQ6UD SQ MPGIVVFRRRWSVGSDDLVLPAIFLFLLHTTWFVILSVVLFGLVYNPHEACSLNLVDHGRGYLGILLSCMIAEMAIIWLSMRGGILYTEPRDSMQYVLYVRLAILVIEFIYAIVGIVWLTQYYTSCNDLTAKNVTLGMVVCNWVVILSVCITVLCVFDPTGRTFVKLRATKRRQRNLRTYNLRHRLEEGQATSWSRRLKVFLCCTRTKDSQSDAYSEIAYLFAEFFRDLDIVPSDIIAGLVLLRQRQRAKRNAVLDEANNDILAFLSGMPVTRNTKYLDLKNSQEMLRYKEVCYYMLFALAAYGWPMYLMRKPACGLCQLARSCSCCLCPARPRFAPGVTIEEDNCCGCNAIAIRRHFLDENMTAVDIVYTSCHDAVYETPFYVAVDHDKKKVVISIRGTLSPKDALTDLTGDAERLPVEGHHGTWLGHKGMVLSAEYIKKKLEQEMVLSQAFGRDLGRGTKHYGLIVVGHSLGAGTAAILSFLLRPQYPTLKCFAYSPPGGLLSEDAMEYSKEFVTAVVLGKDLVPRIGLSQLEGFRRQLLDVLQRSTKPKWRIIVGATKCIPKSELPEEVEVTTLASTRLWTHPSDLTIALSASTPLYPPGRIIHVVHNHPAEQCCCCEQEEPTYFAIWGDNKAFNEVIISPAMLHEHLPYVVMEGLNKVLENYNKGKTALLSAAKVMVSPTEVDLTPELIFQQQPLPTGPPMPTGLALELPTADHRNSSVRSKSQSEMSLEGFSEGRLLSPVVAAAARQDPVELLLLSTQERLAAELQARRAPLATMESLSDTESLYSFDSRRSSGFRSIRGSPSLHAVLERDEGHLFYIDPAIPEENPSLSSRTELLAADSLSKHSQDTQPLEAALGSGGVTPERPPSAAANDEEEEVGGGGGGPASRGELALHNGRLGDSPSPQVLEFAEFIDSLFNLDSKSSSFQDLYCMVVPESPTSDYAEGPKSPSQQEILLRAQFEPNLVPKPPRLFAGSADPSSGISLSPSFPLSSSGELMDLTPTGLSSQECLAADKIRTSTPTGHGASPAKQDELVISAR TTRQ6UD TT Patented-recorded TTRQ6UD FM AB hydrolase superfamily TTYGQ8A ID TTYGQ8A TTYGQ8A TN Dual-specificity tyrosine-phosphorylation regulated kinase 1B (DYRK1B) TTYGQ8A UP Q9Y463 TTYGQ8A UC DYR1B_HUMAN TTYGQ8A BC Kinase TTYGQ8A SN Minibrain-related kinase; MIRK; Dual specificity tyrosine-phosphorylation-regulated kinase 1B TTYGQ8A GN DYRK1B TTYGQ8A FC Enhances the transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits epithelial cell migration. Mediates colon carcinoma cell survival in mitogen-poor environments. Inhibits the SHH and WNT1 pathways, thereby enhancing adipogenesis. In addition, promotes expression of the gluconeogenic enzyme glucose-6-phosphatase (G6PC). Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. TTYGQ8A EC EC 2.7.12.1 TTYGQ8A SQ MAVPPGHGPFSGFPGPQEHTQVLPDVRLLPRRLPLAFRDATSAPLRKLSVDLIKTYKHINEVYYAKKKRRAQQAPPQDSSNKKEKKVLNHGYDDDNHDYIVRSGERWLERYEIDSLIGKGSFGQVVKAYDHQTQELVAIKIIKNKKAFLNQAQIELRLLELMNQHDTEMKYYIVHLKRHFMFRNHLCLVFELLSYNLYDLLRNTHFRGVSLNLTRKLAQQLCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGTPYDLAIDMWSLGCILVEMHTGEPLFSGSNEVDQMNRIVEVLGIPPAAMLDQAPKARKYFERLPGGGWTLRRTKELRKDYQGPGTRRLQEVLGVQTGGPGGRRAGEPGHSPADYLRFQDLVLRMLEYEPAARISPLGALQHGFFRRTADEATNTGPAGSSASTSPAPLDTCPSSSTASSISSSGGSSGSSSDNRTYRYSNRYCGGPGPPITDCEMNSPQVPPSQPLRPWAGGDVPHKTHQAPASASSLPGTGAQLPPQPRYLGRPPSPTSPPPPELMDVSLVGGPADCSPPHPAPAPQHPAASALRTRMTGGRPPLPPPDDPATLGPHLGLRGVPQSTAASS TTYGQ8A TT Patented-recorded TTJBYRU ID TTJBYRU TTJBYRU TN EZH2 Y641F mutant (EZH2 Y641F) TTJBYRU UP Q15910 TTJBYRU UC EZH2_HUMAN TTJBYRU SN Lysine Nmethyltransferase 6 Y641F mutant; Lysine N-methyltransferase 6 Y641F mutant; KMT6 Y641F mutant; Histonelysine Nmethyltransferase EZH2 Y641F mutant; Histone-lysine N-methyltransferase EZH2 Y641F mutant; EZH2 Y641F mutations; ENX1 Y641F mutant; ENX-1 Y641F mutant TTJBYRU GN EZH2 TTJBYRU FC Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2. Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-ARNTL/BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription. Polycomb group (PcG) protein. TTJBYRU EC EC 2.1.1.43 TTJBYRU PD 6C24; 6C23; 5WUK; 5WG6; 5U62 TTJBYRU SQ MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP TTJBYRU TT Patented-recorded TTJBYRU FM Class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily. TTJW2UQ ID TTJW2UQ TTJW2UQ TN EZH2 Y641N mutant (EZH2 Y641N) TTJW2UQ UP Q15910 TTJW2UQ UC EZH2_HUMAN TTJW2UQ SN Lysine Nmethyltransferase 6 Y641N mutant; Lysine N-methyltransferase 6 Y641N mutant; KMT6 Y641N mutant; Histonelysine Nmethyltransferase EZH2 Y641N mutant; Histone-lysine N-methyltransferase EZH2 Y641N mutant; EZH2 Y641N mutations; ENX1 Y641N mutant; ENX-1 Y641N mutant TTJW2UQ GN EZH2 TTJW2UQ FC Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2. Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-ARNTL/BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription. Polycomb group (PcG) protein. TTJW2UQ EC EC 2.1.1.43 TTJW2UQ PD 6C24; 6C23; 5WUK; 5WG6; 5U62 TTJW2UQ SQ MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP TTJW2UQ TT Patented-recorded TTJW2UQ FM Class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily. TTSYOWR ID TTSYOWR TTSYOWR TN Ghrelin O acyltransferase (GOAT) TTSYOWR UP Q96T53 TTSYOWR UC MBOA4_HUMAN TTSYOWR BC Acyltransferase TTSYOWR SN Oacyltransferase domaincontaining protein 4; OACT4; O-acyltransferase domain-containing protein 4; Membranebound Oacyltransferase domaincontaining protein 4; Membrane-bound O-acyltransferase domain-containing protein 4; Ghrelin Oacyltransferase; Ghrelin O-acyltransferase; FKSG89 TTSYOWR GN MBOAT4 TTSYOWR FC Can use a variety of fatty acids as substrates including octanoic acid, decanoic acid and tetradecanoic acid. Mediates the octanoylation of ghrelin at 'Ser-3'. TTSYOWR EC EC 2.3.1.- TTSYOWR SQ MEWLWLFFLHPISFYQGAAFPFALLFNYLCIMDSFSTRARYLFLLTGGGALAVAAMGSYAVLVFTPAVCAVALLCSLAPQQVHRWTFCFQMSWQTLCHLGLHYTEYYLHEPPSVRFCITLSSLMLLTQRVTSLSLDICEGKVKAASGGFRSRSSLSEHVCKALPYFSYLLFFPALLGGSLCSFQRFQARVQGSSALHPRHSFWALSWRGLQILGLECLNVAVSRVVDAGAGLTDCQQFECIYVVWTTAGLFKLTYYSHWILDDSLLHAAGFGPELGQSPGEEGYVPDADIWTLERTHRISVFSRKWNQSTARWLRRLVFQHSRAWPLLQTFAFSAWWHGLHPGQVFGFVCWAVMVEADYLIHSFANEFIRSWPMRLFYRTLTWAHTQLIIAYIMLAVEVRSLSSLWLLCNSYNSVFPMVYCILLLLLAKRKHKCN TTSYOWR TT Patented-recorded TTSYOWR FM Acyltransferase TT08JVB ID TT08JVB TT08JVB TN G-protein coupled receptor 120 (GPR120) TT08JVB UP Q5NUL3 TT08JVB UC FFAR4_HUMAN TT08JVB BC GPCR rhodopsin TT08JVB SN PGR4; Omega3 fatty acid receptor 1; Omega-3 fatty acid receptor 1; O3FAR1; Gprotein coupled receptor PGR4; Gprotein coupled receptor GT01; Gprotein coupled receptor 129; GPR129; G-protein coupled receptor PGR4; G-protein coupled receptor GT01; G-protein coupled receptor 129; Free fatty acid receptor 4 TT08JVB GN FFAR4 TT08JVB FC Signals via a G(q)/G(11)-coupled pathway. Acts as a receptor for omega-3 fatty acids and mediates robust anti-inflammatory effects, particularly in macrophages and fat cells. The anti-inflammatory effects involve inhibition of TAK1 through a beta-arrestin 2 (ARRB2)/TAB1-dependent effect, but independent of the G(q)/G(11)-coupled pathway. Mediates potent insulin sensitizing and antidiabetic effects by repressing macrophage-induced tissue inflammation. May mediate the taste of fatty acids. Mediates FFA-induced inhibition of apoptosis in enteroendocrine cells. May play a role in the regulation of adipocyte development and differentiation. Receptor for medium and long-chain free fatty acids (FFAs). TT08JVB SQ MSPECARAAGDAPLRSLEQANRTRFPFFSDVKGDHRLVLAAVETTVLVLIFAVSLLGNVCALVLVARRRRRGATACLVLNLFCADLLFISAIPLVLAVRWTEAWLLGPVACHLLFYVMTLSGSVTILTLAAVSLERMVCIVHLQRGVRGPGRRARAVLLALIWGYSAVAALPLCVFFRVVPQRLPGADQEISICTLIWPTIPGEISWDVSFVTLNFLVPGLVIVISYSKILQITKASRKRLTVSLAYSESHQIRVSQQDFRLFRTLFLLMVSFFIMWSPIIITILLILIQNFKQDLVIWPSLFFWVVAFTFANSALNPILYNMTLCRNEWKKIFCCFWFPEKGAILTDTSVKRNDLSIISG TT08JVB TT Literature-reported TT08JVB FM GPCR rhodopsin TT8M4E1 ID TT8M4E1 TT8M4E1 TN Histone deacetylase 9 (HDAC9) TT8M4E1 UP Q9UKV0 TT8M4E1 UC HDAC9_HUMAN TT8M4E1 BC Carbon-nitrogen hydrolase TT8M4E1 SN MITR; MEF2-interacting transcription repressor MITR; KIAA0744; Histone deacetylase-related protein; Histone deacetylase 7B; HDRP; HDAC7B; HDAC7; HD9; HD7b TT8M4E1 GN HDAC9 TT8M4E1 FC Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). TT8M4E1 EC EC 3.5.1.98 TT8M4E1 SQ MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVSRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDAKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNVVTSFKKRMFEVTESSVSSSSPGSGPSSPNNGPTGSVTENETSVLPPTPHAEQMVSQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSQLNASNSLKEKQKCETQTLRQGVPLPGQYGGSIPASSSHPHVTLEGKPPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMQEDRAPSSGNSTRSDSSACVDDTLGQVGAVKVKEEPVDSDEDAQIQEMESGEQAAFMQQPFLEPTHTRALSVRQAPLAAVGMDGLEKHRLVSRTHSSPAASVLPHPAMDRPLQPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSMSLKFS TT8M4E1 TT Patented-recorded TTXKZ8Q ID TTXKZ8Q TTXKZ8Q TN JNK-interacting protein 1 peptide (pepJIP1) TTXKZ8Q UP Q9UQF2 TTXKZ8Q UC JIP1_HUMAN TTXKZ8Q SN PRKM8IP; Mitogen-activated protein kinase 8-interacting protein 1; JNK-interacting protein 1; JNK MAP kinase scaffold protein 1; JIP1; JIP-1; Islet-brain 1; IB1; IB-1; C-Jun-amino-terminal kinase-interacting protein 1 TTXKZ8Q GN MAPK8IP1 TTXKZ8Q FC Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response. Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells. The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. TTXKZ8Q PD 6FUZ; 5LW1; 4IZY; 4HYU; 4HYS TTXKZ8Q SQ MAERESGGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGGGGAGSRLQAEMLQMDLIDATGDTPGAEDDEEDDDEERAARRPGAGPPKAESGQEPASRGQGQSQGQSQGPGSGDTYRPKRPTTLNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQSGPAPTTDRGTSTDSPCRRSTATQMAPPGGPPAAPPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDAAEPTSAFLPPTESRMSVSSDPDPAAYPSTAGRPHPSISEEEEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDYSDESDSATVYDNCASVSSPYESAIGEEYEEAPRPQPPACLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLFSCIINGEEQEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKNSDWVDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDSQEAKGNKCSHFFQLKNISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE TTXKZ8Q TT Patented-recorded TTXKZ8Q FM JIP scaffold family TTXKZ8Q KE hsa04010:MAPK signaling pathway TTDA81R ID TTDA81R TTDA81R TN Kallikrein-14 (KLK14) TTDA81R UP Q9P0G3 TTDA81R UC KLK14_HUMAN TTDA81R BC Peptidase TTDA81R SN hK14; Kallikrein-like protein 6; KLKL6; KLK-L6 TTDA81R GN KLK14 TTDA81R FC May activate/inactivate the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a process by which the most superficial corneocytes are shed from the skin surface. May be involved in several aspects of tumor progression including growth, invasion and angiogenesis. Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. TTDA81R EC EC 3.4.21.- TTDA81R SQ MSLRVLGSGTWPSAPKMFLLLTALQVLAIAMTQSQEDENKIIGGHTCTRSSQPWQAALLAGPRRRFLCGGALLSGQWVITAAHCGRPILQVALGKHNLRRWEATQQVLRVVRQVTHPNYNSRTHDNDLMLLQLQQPARIGRAVRPIEVTQACASPGTSCRVSGWGTISSPIARYPASLQCVNINISPDEVCQKAYPRTITPGMVCAGVPQGGKDSCQGDSGGPLVCRGQLQGLVSWGMERCALPGYPGVYTNLCKYRSWIEETMRDK TTDA81R TT Patented-recorded TTLUW5B ID TTLUW5B TTLUW5B TN Laminin receptor 37/67kDa (LRP/LR) TTLUW5B UP P08865 TTLUW5B UC RSSA_HUMAN TTLUW5B SN Small ribosomal subunit protein uS2; NEM/1CHD4; Multidrug resistance-associated protein MGr1-Ag; Laminin-binding protein precursor p40; Laminin receptor 1; LamR; LBP/p40; LAMR1; LAMBR; Colon carcinoma laminin-binding protein; 67LR; 67 kDa laminin receptor; 40S ribosomal protein SA; 37LRP; 37/67 kDa laminin receptor; 37 kDa laminin receptor precursor TTLUW5B GN RPSA TTLUW5B FC Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA. Required for the assembly and/or stability of the 40S ribosomal subunit. TTLUW5B PD 6QZP; 6G5I; 6G5H; 6G53; 6G51 TTLUW5B SQ MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTATQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTDWS TTLUW5B TT Patented-recorded TTLUW5B FM Universal ribosomal protein uS2 family TTLUW5B KE hsa03010:Ribosome TTQFRP0 ID TTQFRP0 TTQFRP0 TN MEK kinase kinase 2 (MAP4K2) TTQFRP0 UP Q12851 TTQFRP0 UC M4K2_HUMAN TTQFRP0 BC Kinase TTQFRP0 SN Rab8-interacting protein; RAB8IP; Mitogen-activated protein kinase kinase kinase kinase 2; MEKKK 2; MAPK/ERK kinase kinase kinase 2; Germinal center kinase; GCK; GC kinase; B lymphocyte serine/threonine-protein kinase TTQFRP0 GN MAP4K2 TTQFRP0 FC Acts as a MAPK kinase kinase kinase (MAP4K) and is an upstream activator of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway and to a lesser extent of the p38 MAPKs signaling pathway. Required for the efficient activation of JNKs by TRAF6-dependent stimuli, including pathogen-associated molecular patterns (PAMPs) such as polyinosine-polycytidine (poly(IC)), lipopolysaccharides (LPS), lipid A, peptidoglycan (PGN), or bacterial flagellin. To a lesser degree, IL-1 and engagement of CD40 also stimulate MAP4K2-mediated JNKs activation. The requirement for MAP4K2/GCK is most pronounced for LPS signaling, and extends to LPS stimulation of c-Jun phosphorylation and induction of IL-8. Enhances MAP3K1 oligomerization, which may relieve N-terminal mediated MAP3K1 autoinhibition and lead to activation following autophosphorylation. Mediates also the SAP/JNK signaling pathway and the p38 MAPKs signaling pathway through activation of the MAP3Ks MAP3K10/MLK2 and MAP3K11/MLK3. May play a role in the regulation of vesicle targeting or fusion. regulation of vesicle targeting or fusion. Serine/threonine-protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. TTQFRP0 EC EC 2.7.11.1 TTQFRP0 SQ MALLRDVSLQDPRDRFELLQRVGAGTYGDVYKARDTVTSELAAVKIVKLDPGDDISSLQQEITILRECRHPNVVAYIGSYLRNDRLWICMEFCGGGSLQEIYHATGPLEERQIAYVCREALKGLHHLHSQGKIHRDIKGANLLLTLQGDVKLADFGVSGELTASVAKRRSFIGTPYWMAPEVAAVERKGGYNELCDVWALGITAIELGELQPPLFHLHPMRALMLMSKSSFQPPKLRDKTRWTQNFHHFLKLALTKNPKKRPTAEKLLQHPFTTQQLPRALLTQLLDKASDPHLGTPSPEDCELETYDMFPDTIHSRGQHGPAERTPSEIQFHQVKFGAPRRKETDPLNEPWEEEWTLLGKEELSGSLLQSVQEALEERSLTIRSASEFQELDSPDDTMGTIKRAPFLGPLPTDPPAEEPLSSPPGTLPPPPSGPNSSPLLPTAWATMKQREDPERSSCHGLPPTPKVHMGACFSKVFNGCPLRIHAAVTWIHPVTRDQFLVVGAEEGIYTLNLHELHEDTLEKLISHRCSWLYCVNNVLLSLSGKSTHIWAHDLPGLFEQRRLQQQVPLSIPTNRLTQRIIPRRFALSTKIPDTKGCLQCRVVRNPYTGATFLLAALPTSLLLLQWYEPLQKFLLLKNFSSPLPSPAGMLEPLVLDGKELPQVCVGAEGPEGPGCRVLFHVLPLEAGLTPDILIPPEGIPGSAQQVIQVDRDTILVSFERCVRIVNMQGEPTATLAPELTFDFPIETVVCLQDSVLAFWSHGMQGRSLDTNEVTQEITDETRIFRVLGAHRDIILESIPTDNPEAHSNLYILTGHQSTY TTQFRP0 TT Patented-recorded TTB6Q2O ID TTB6Q2O TTB6Q2O TN Myeloid differentiation primary response protein MyD88 (MYD88) TTB6Q2O UP Q99836 TTB6Q2O UC MYD88_HUMAN TTB6Q2O SN MyD88 TTB6Q2O GN MYD88 TTB6Q2O FC Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Increases IL-8 transcription. Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine. Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. TTB6Q2O PD 4EO7; 4DOM; 3MOP; 2Z5V; 2JS7 TTB6Q2O SQ MAAGGPGAGSAAPVSSTSSLPLAALNMRVRRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQADPTGRLLDAWQGRPGASVGRLLELLTKLGRDDVLLELGPSIEEDCQKYILKQQQEEAEKPLQVAAVDSSVPRTAELAGITTLDDPLGHMPERFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGAHQKRLIPIKYKAMKKEFPSILRFITVCDYTNPCTKSWFWTRLAKALSLP TTB6Q2O TT Literature-reported TTBP3XA ID TTBP3XA TTBP3XA TN Polyubiquitin-C (UBC) TTBP3XA UP P0CG48 TTBP3XA UC UBC_HUMAN TTBP3XA SN ubiquitin C; HMG20 TTBP3XA GN UBC TTBP3XA FC When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). TTBP3XA PD 6OI4; 6NQA; 6N13; 6EQI; 6B7O TTBP3XA SQ MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGV TTBP3XA TT Patented-recorded TTBP3XA FM Ubiquitin family TTBP3XA KE hsa03320:PPAR signaling pathway TTW14O3 ID TTW14O3 TTW14O3 TN Programmed cell death 1 ligand 2 (PD-L2) TTW14O3 UP Q9BQ51 TTW14O3 UC PD1L2_HUMAN TTW14O3 BC Immunoglobulin TTW14O3 SN Programmed death ligand 2; PDL2; PDCD1L2; PDCD1 ligand 2; PD-1 ligand 2; CD273; Butyrophilin B7-DC; B7DC; B7-DC TTW14O3 GN PDCD1LG2 TTW14O3 FC Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production. Involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. TTW14O3 SQ MIFLLLMLSLELQLHQIAALFTVTVPKELYIIEHGSNVTLECNFDTGSHVNLGAITASLQKVENDTSPHRERATLLEEQLPLGKASFHIPQVQVRDEGQYQCIIIYGVAWDYKYLTLKVKASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQSQMEPRTHPTWLLHIFIPFCIIAFIFIATVIALRKQLCQKLYSSKDTTKRPVTTTKREVNSAI TTW14O3 TT Patented-recorded TTW14O3 FM Immunoglobulin superfamily TTW14O3 KE hsa04514:Cell adhesion molecules (CAMs) TTKVTQO ID TTKVTQO TTKVTQO TN Prostaglandin transporter (SLC21A2) TTKVTQO UP Q92959 TTKVTQO UC SO2A1_HUMAN TTKVTQO BC Organo anion transporter TTKVTQO SN Solute carrier organic anion transporter family member 2A1; Solute carrier family 21 member 2; PGT; OATP2A1 TTKVTQO GN SLCO2A1 TTKVTQO FC Transports PGD2, as well as PGE1, PGE2 and PGF2A. May mediate the release of newly synthesized prostaglandins from cells, the transepithelial transport of prostaglandins, and the clearance of prostaglandins from the circulation. TTKVTQO PD 3MRR TTKVTQO SQ MGLLPKLGASQGSDTSTSRAGRCARSVFGNIKVFVLCQGLLQLCQLLYSAYFKSSLTTIEKRFGLSSSSSGLISSLNEISNAILIIFVSYFGSRVHRPRLIGIGGLFLAAGAFILTLPHFLSEPYQYTLASTGNNSRLQAELCQKHWQDLPPSKCHSTTQNPQKETSSMWGLMVVAQLLAGIGTVPIQPFGISYVDDFSEPSNSPLYISILFAISVFGPAFGYLLGSVMLQIFVDYGRVNTAAVNLVPGDPRWIGAWWLGLLISSALLVLTSFPFFFFPRAMPIGAKRAPATADEARKLEEAKSRGSLVDFIKRFPCIFLRLLMNSLFVLVVLAQCTFSSVIAGLSTFLNKFLEKQYGTSAAYANFLIGAVNLPAAALGMLFGGILMKRFVFSLQAIPRIATTIITISMILCVPLFFMGCSTPTVAEVYPPSTSSSIHPQSPACRRDCSCPDSIFHPVCGDNGIEYLSPCHAGCSNINMSSATSKQLIYLNCSCVTGGSASAKTGSCPVPCAHFLLPAIFLISFVSLIACISHNPLYMMVLRVVNQEEKSFAIGVQFLLMRLLAWLPSPALYGLTIDHSCIRWNSLCLGRRGACAYYDNDALRDRYLGLQMGYKALGMLLLCFISWRVKKNKEYNVQKAAGLI TTKVTQO TT Patented-recorded TT0ZW9O ID TT0ZW9O TT0ZW9O TN Ribosomal protein S6 kinase alpha-2 (RSK2) TT0ZW9O UP Q15349 TT0ZW9O UC KS6A2_HUMAN TT0ZW9O BC Kinase TT0ZW9O SN pp90RSK3; p90RSK2; p90-RSK 2; S6K-alpha-2; Ribosomal S6 kinase 3; RSK3; RSK-3; MAPKAPK1C; MAPKAPK-1c; MAPKAP kinase 1c; MAPK-activated protein kinase 1c; MAP kinase-activated protein kinase 1c; 90 kDa ribosomal protein S6 kinase 2 TT0ZW9O GN RPS6KA2 TT0ZW9O FC May function as tumor suppressor in epithelial ovarian cancer cells. Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of transcription factors, regulates translation, and mediates cellular proliferation, survival, and differentiation. TT0ZW9O EC EC 2.7.11.1 TT0ZW9O SQ MDLSMKKFAVRRFFSVYLRRKSRSKSSSLSRLEEEGVVKEIDISHHVKEGFEKADPSQFELLKVLGQGSYGKVFLVRKVKGSDAGQLYAMKVLKKATLKVRDRVRSKMERDILAEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKITDFGLSKEAIDHDKRAYSFCGTIEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMALILKAKLGMPQFLSGEAQSLLRALFKRNPCNRLGAGIDGVEEIKRHPFFVTIDWNTLYRKEIKPPFKPAVGRPEDTFHFDPEFTARTPTDSPGVPPSANAHHLFRGFSFVASSLIQEPSQQDLHKVPVHPIVQQLHGNNIHFTDGYEIKEDIGVGSYSVCKRCVHKATDTEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMRGGELLDRILRQRYFSEREASDVLCTITKTMDYLHSQGVVHRDLKPSNILYRDESGSPESIRVCDFGFAKQLRAGNGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEILARIGSGKYALSGGNWDSISDAAKDVVSKMLHVDPHQRLTAMQVLKHPWVVNREYLSPNQLSRQDVHLVKGAMAATYFALNRTPQAPRLEPVLSSNLAQRRGMKRLTSTRL TT0ZW9O TT Literature-reported TTW6JVU ID TTW6JVU TTW6JVU TN Smoothened D473H mutant (SMO D473H) TTW6JVU UP Q99835 TTW6JVU UC SMO_HUMAN TTW6JVU BC GPCR frizzled TTW6JVU SN Smo-D473H mutant; SMOH D473H mutant; Protein Gx D473H mutant TTW6JVU GN SMO TTW6JVU FC Binding of sonic hedgehog (SHH) to its receptor patched is thought to prevent normal inhibition by patched of smoothened (SMO). Required for the accumulation of KIF7, GLI2 and GLI3 in the cilia. Interacts with DLG5 at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation. G protein-coupled receptor that probably associates with the patched protein (PTCH) to transduce the hedgehog's proteins signal. TTW6JVU PD 5V57; 5V56; 5L7I; 5L7D; 4QIN TTW6JVU SQ MAAARPARGPELPLLGLLLLLLLGDPGRGAASSGNATGPGPRSAGGSARRSAAVTGPPPPLSHCGRAAPCEPLRYNVCLGSVLPYGATSTLLAGDSDSQEEAHGKLVLWSGLRNAPRCWAVIQPLLCAVYMPKCENDRVELPSRTLCQATRGPCAIVERERGWPDFLRCTPDRFPEGCTNEVQNIKFNSSGQCEVPLVRTDNPKSWYEDVEGCGIQCQNPLFTEAEHQDMHSYIAAFGAVTGLCTLFTLATFVADWRNSNRYPAVILFYVNACFFVGSIGWLAQFMDGARREIVCRADGTMRLGEPTSNETLSCVIIFVIVYYALMAGVVWFVVLTYAWHTSFKALGTTYQPLSGKTSYFHLLTWSLPFVLTVAILAVAQVDGDSVSGICFVGYKNYRYRAGFVLAPIGLVLIVGGYFLIRGVMTLFSIKSNHPGLLSEKAASKINETMLRLGIFGFLAFGFVLITFSCHFYDFFNQAEWERSFRDYVLCQANVTIGLPTKQPIPDCEIKNRPSLLVEKINLFAMFGTGIAMSTWVWTKATLLIWRRTWCRLTGQSDDEPKRIKKSKMIAKAFSKRHELLQNPGQELSFSMHTVSHDGPVAGLAFDLNEPSADVSSAWAQHVTKMVARRGAILPQDISVTPVATPVPPEEQANLWLVEAEISPELQKRLGRKKKRRKRKKEVCPLAPPPELHPPAPAPSTIPRLPQLPRQKCLVAAGAWGAGDSCRQGAWTLVSNPFCPEPSPPQDPFLPSAPAPVAWAHGRRQGLGPIHSRTNLMDTELMDADSDF TTW6JVU TT Patented-recorded TTW6JVU FM G-protein coupled receptor Fz/Smo family TTRHJA3 ID TTRHJA3 TTRHJA3 TN SPS1/STE20-related protein kinase YSK4 (YSK4) TTRHJA3 UP Q56UN5 TTRHJA3 UC M3K19_HUMAN TTRHJA3 BC Kinase TTRHJA3 SN Regulated in COPD, protein kinase; RCK; Mitogen-activated protein kinase kinase kinase 19 TTRHJA3 GN MAP3K19 TTRHJA3 FC Protein serine/threonine kinase activity, activation of protein kinase activity, signal transduction by protein phosphorylation, stress-activated protein kinase signaling cascade. TTRHJA3 EC EC 2.7.11.1 TTRHJA3 SQ MSSMPKPERHAESLLDICHDTNSSPTDLMTVTKNQNIILQSISRSEEFDQDGDCSHSTLVNEEEDPSGGRQDWQPRTEGVEITVTFPRDVSPPQEMSQEDLKEKNLINSSLQEWAQAHAVSHPNEIETVELRKKKLTMRPLVLQKEESSRELCNVNLGFLLPRSCLELNISKSVTREDAPHFLKEQQRKSEEFSTSHMKYSGRSIKFLLPPLSLLPTRSGVLTIPQNHKFPKEKERNIPSLTSFVPKLSVSVRQSDELSPSNEPPGALVKSLMDPTLRSSDGFIWSRNMCSFPKTNHHRQCLEKEENWKSKEIEECNKIEITHFEKGQSLVSFENLKEGNIPAVREEDIDCHGSKTRKPEEENSQYLSSRKNESSVAKNYEQDPEIVCTIPSKFQETQHSEITPSQDEEMRNNKAASKRVSLHKNEAMEPNNILEECTVLKSLSSVVFDDPIDKLPEGCSSMETNIKISIAERAKPEMSRMVPLIHITFPVDGSPKEPVIAKPSLQTRKGTIHNNHSVNIPVHQENDKHKMNSHRSKLDSKTKTSKKTPQNFVISTEGPIKPTMHKTSIKTQIFPALGLVDPRPWQLPRFQKKMPQIAKKQSTHRTQKPKKQSFPCICKNPGTQKSCVPLSVQPTEPRLNYLDLKYSDMFKEINSTANGPGIYEMFGTPVYCHVRETERDENTYYREICSAPSGRRITNKCRSSHSERKSNIRTRLSQKKTHMKCPKTSFGIKQEHKVLISKEKSSKAVHSNLHDIENGDGISEPDWQIKSSGNEFLSSKDEIHPMNLAQTPEQSMKQNEFPPVSDLSIVEEVSMEESTGDRDISNNQILTTSLRDLQELEELHHQIPFIPSEDSWAVPSEKNSNKYVQQEKQNTASLSKVNASRILTNDLEFDSVSDHSKTLTNFSFQAKQESASSQTYQYWVHYLDHDSLANKSITYQMFGKTLSGTNSISQEIMDSVNNEELTDELLGCLAAELLALDEKDNNSCQKMANETDPENLNLVLRWRGSTPKEMGRETTKVKIQRHSSGLRIYDREEKFLISNEKKIFSENSLKSEEPILWTKGEILGKGAYGTVYCGLTSQGQLIAVKQVALDTSNKLAAEKEYRKLQEEVDLLKALKHVNIVAYLGTCLQENTVSIFMEFVPGGSISSIINRFGPLPEMVFCKYTKQILQGVAYLHENCVVHRDIKGNNVMLMPTGIIKLIDFGCARRLAWAGLNGTHSDMLKSMHGTPYWMAPEVINESGYGRKSDIWSIGCTVFEMATGKPPLASMDRMAAMFYIGAHRGLMPPLPDHFSENAADFVRMCLTRDQHERPSALQLLKHSFLERSH TTRHJA3 TT Patented-recorded TT2GQT6 ID TT2GQT6 TT2GQT6 TN TIR domain-containing adapter molecule 1 (TICAM1) TT2GQT6 UP Q8IUC6 TT2GQT6 UC TCAM1_HUMAN TT2GQT6 SN Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta; TRIF; TIR domain-containing adapter protein inducing IFN-beta; TICAM-1; Putative NF-kappa-B-activating protein 502H; Proline-rich, vinculin and TIR domain-containing protein B; PRVTIRB; MyD88-3 TT2GQT6 GN TICAM1 TT2GQT6 FC Adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis. Ligand binding to these receptors results in TRIF recruitment through its TIR domain. Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively. Phosphorylation by TBK1 on the pLxIS motif leads to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent immunity against invading pathogens. Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of proinflammatory cytokines. Involved in innate immunity against invading pathogens. TT2GQT6 PD 5JEL; 4C0M; 4BSX; 3RC4; 2M63 TT2GQT6 SQ MACTGPSLPSAFDILGAAGQDKLLYLKHKLKTPRPGCQGQDLLHAMVLLKLGQETEARISLEALKADAVARLVARQWAGVDSTEDPEEPPDVSWAVARLYHLLAEEKLCPASLRDVAYQEAVRTLSSRDDHRLGELQDEARNRCGWDIAGDPGSIRTLQSNLGCLPPSSALPSGTRSLPRPIDGVSDWSQGCSLRSTGSPASLASNLEISQSPTMPFLSLHRSPHGPSKLCDDPQASLVPEPVPGGCQEPEEMSWPPSGEIASPPELPSSPPPGLPEVAPDATSTGLPDTPAAPETSTNYPVECTEGSAGPQSLPLPILEPVKNPCSVKDQTPLQLSVEDTTSPNTKPCPPTPTTPETSPPPPPPPPSSTPCSAHLTPSSLFPSSLESSSEQKFYNFVILHARADEHIALRVREKLEALGVPDGATFCEDFQVPGRGELSCLQDAIDHSAFIILLLTSNFDCRLSLHQVNQAMMSNLTRQGSPDCVIPFLPLESSPAQLSSDTASLLSGLVRLDEHSQIFARKVANTFKPHRLQARKAMWRKEQDTRALREQSQHLDGERMQAAALNAAYSAYLQSYLSYQAQMEQLQVAFGSHMSFGTGAPYGARMPFGGQVPLGAPPPFPTWPGCPQPPPLHAWQAGTPPPPSPQPAAFPQSLPFPQSPAFPTASPAPPQSPGLQPLIIHHAQMVQLGLNNHMWNQRGSQAPEDKTQEAE TT2GQT6 TT Patented-recorded TT2GQT6 KE hsa04064:NF-kappa B signaling pathway; hsa04217:Necroptosis; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa05133:Pertussis; hsa05135:Yersinia infection; hsa05142:Chagas disease (American trypanosomiasis); hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05165:Human papillomavirus infection; hsa05167:Kaposi sarcoma-associated herpesvirus infection; hsa05168:Herpes simplex virus 1 infection; hsa05235:PD-L1 expression and PD-1 checkpoint pathway in cancer TTKU0LS ID TTKU0LS TTKU0LS TN Toll/interleukin-1 receptor domain-containing adapter (TIRAP) TTKU0LS UP P58753 TTKU0LS UC TIRAP_HUMAN TTKU0LS SN Toll/interleukin-1 receptor domain-containing adapter protein; TIR domain-containing adapter protein; MyD88-2; MyD88 adapter-like protein; MAL; Adaptor protein Wyatt TTKU0LS GN TIRAP TTKU0LS FC Acts via IRAK2 and TRAF-6, leading to the activation of NF-kappa-B, MAPK1, MAPK3 and JNK, and resulting in cytokine secretion and the inflammatory response. Positively regulates the production of TNF-alpha and interleukin-6. Adapter involved in TLR2 and TLR4 signaling pathways in the innate immune response. TTKU0LS PD 5UZB; 5T7Q; 4LQD; 4FZ5; 3UB4 TTKU0LS SQ MASSTSLPAPGSRPKKPLGKMADWFRQTLLKKPKKRPNSPESTSSDASQPTSQDSPLPPSLSSVTSPSLPPTHASDSGSSRWSKDYDVCVCHSEEDLVAAQDLVSYLEGSTASLRCFLQLRDATPGGAIVSELCQALSSSHCRVLLITPGFLQDPWCKYQMLQALTEAPGAEGCTIPLLSGLSRAAYPPELRFMYYVDGRGPDGGFRQVKEAVMRYLQTLS TTKU0LS TT Patented-recorded TTKU0LS KE hsa04064:NF-kappa B signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa05133:Pertussis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05235:PD-L1 expression and PD-1 checkpoint pathway in cancer TT2ME4S ID TT2ME4S TT2ME4S TN Transcription regulator protein BACH1 (Bach1) TT2ME4S UP O14867 TT2ME4S UC BACH1_HUMAN TT2ME4S BC Basic leucine zipper bZIP TT2ME4S SN HA2303; BTB and CNC homolog 1 TT2ME4S GN BACH1 TT2ME4S FC Binds to NF-E2 DNA binding sites. Play important roles in coordinating transcription activation and repression by MAFK. Together with MAF, represses the transcription of genes under the control of the NFE2L2 oxidative stress pathway. Transcriptional regulator that acts as repressor or activator, depending on the context. TT2ME4S PD 2IHC TT2ME4S SQ MSLSENSVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIVGQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQFLKFKFLDSTADQQECPRKKCFSSHCQKTDLKLSLLDQRDLETDEVEEFLENKNVQTPQCKLRRYQGNAKASPPLQDSASQTYESMCLEKDAALALPSLCPKYRKFQKAFGTDRVRTGESSVKDIHASVQPNERSENECLGGVPECRDLQVMLKCDESKLAMEPEETKKDPASQCPTEKSEVTPFPHNSSIDPHGLYSLSLLHTYDQYGDLNFAGMQNTTVLTEKPLSGTDVQEKTFGESQDLPLKSDLGTREDSSVASSDRSSVEREVAEHLAKGFWSDICSTDTPCQMQLSPAVAKDGSEQISQKRSECPWLGIRISESPEPGQRTFTTLSSVNCPFISTLSTEGCSSNLEIGNDDYVSEPQQEPCPYACVISLGDDSETDTEGDSESCSAREQECEVKLPFNAQRIISLSRNDFQSLLKMHKLTPEQLDCIHDIRRRSKNRIAAQRCRKRKLDCIQNLESEIEKLQSEKESLLKERDHILSTLGETKQNLTGLCQKVCKEAALSQEQIQILAKYSAADCPLSFLISEKDKSTPDGELALPSIFSLSDRPPAVLPPCARGNSEPGYARGQESQQMSTATSEQAGPAEQCRQSGGISDFCQQMTDKCTTDE TT2ME4S TT Patented-recorded TT2ME4S FM BZIP family TTER58P ID TTER58P TTER58P TN B- and T-lymphocyte attenuator (BTLA) TTER58P UP Q7Z6A9 TTER58P UC BTLA_HUMAN TTER58P SN CD272; B- and T-lymphocyte-associated protein TTER58P GN BTLA TTER58P FC May interact in cis (on the same cell) or in trans (on other cells) with TNFRSF14. In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells. Inhibitory receptor on lymphocytes that negatively regulates antigen receptor signaling via PTPN6/SHP-1 and PTPN11/SHP-2. TTER58P PD 2AW2 TTER58P SQ MKTLPAMLGTGKLFWVFFLIPYLDIWNIHGKESCDVQLYIKRQSEHSILAGDPFELECPVKYCANRPHVTWCKLNGTTCVKLEDRQTSWKEEKNISFFILHFEPVLPNDNGSYRCSANFQSNLIESHSTTLYVTDVKSASERPSKDEMASRPWLLYRLLPLGGLPLLITTCFCLFCCLRRHQGKQNELSDTAGREINLVDAHLKSEQTEASTRQNSQVLLSETGIYDNDPDLCFRMQEGSEVYSNPCLEENKPGIVYASLNHSVIGPNSRLARNVKEAPTEYASICVRS TTER58P TT Clinical trial TTTCRU2 ID TTTCRU2 TTTCRU2 TN Bacterial Fimbrin D-mannose adhesin (Bact FimH) TTTCRU2 UP P08191 TTTCRU2 UC FIMH_ECOLI TTTCRU2 SN fimH; b4320; Type 1 fimbrin D-mannose specific adhesin; Protein FimH; JW4283 TTTCRU2 GN Bact FimH TTTCRU2 FC Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed. Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). TTTCRU2 PD 6GTY; 6GTX; 6G2S; 6G2R; 6.00E+15 TTTCRU2 SQ MKRVITLFAVLLMGWSVNAWSFACKTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYPFPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRQTNNYNSDDFQFVWNIYANNDVVVPTGGCDVSARDVTVTLPDYPGSVPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTASFSPAQGVGVQLTRNGTIIPANNTVSLGAVGTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ TTTCRU2 TT Clinical trial TTTCRU2 FM Fimbrial protein family TT3Z6Y9 ID TT3Z6Y9 TT3Z6Y9 TN Cysteines of Keap1 (KEAP1 Cysteines) TT3Z6Y9 UP Q14145 TT3Z6Y9 UC KEAP1_HUMAN TT3Z6Y9 SN Kelch-like protein 19-Cysteines; Kelch-like ECH-associated protein 1-Cysteines; KLHL19-Cysteines; KIAA0132-Cysteines; INrf2-Cysteines; Cytosolic inhibitor of Nrf2-Cysteines TT3Z6Y9 GN KEAP1 TT3Z6Y9 FC Retains NFE2L2/NRF2 and may also retain BPTF in the cytosol. Targets PGAM5 for ubiquitination and degradation by the proteasome. Acts as a substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. TT3Z6Y9 PD 6FMQ; 6FMP; 6FFM; 5X54; 5WIY TT3Z6Y9 SQ MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTC TT3Z6Y9 TT Clinical trial TT3FDAV ID TT3FDAV TT3FDAV TN DNA [cytosine-5]-methyltransferase 3-like (DNMT3L) TT3FDAV UP Q9UJW3 TT3FDAV UC DNM3L_HUMAN TT3FDAV SN DNA (cytosine-5)-methyltransferase 3-like TT3FDAV GN DNMT3L TT3FDAV FC Essential for the function of DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their catalytic domain. Acts by accelerating the binding of DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases. Recognizes unmethylated histone H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by recruitment or activation of DNMT3. Plays a key role in embryonic stem cells and germ cells. In germ cells, required for the methylation of imprinted loci together with DNMT3A. In male germ cells, specifically required to methylate retrotransposons, preventing their mobilization. Plays a key role in embryonic stem cells (ESCs) by acting both as an positive and negative regulator of DNA methylation. While it promotes DNA methylation of housekeeping genes together with DNMT3A and DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter of bivalent genes. Interacts with the EZH2 component of the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B with the PRC2/EED-EZH2 complex, leading to maintain low methylation levels at the promoters of bivalent genes. Promotes differentiation of ESCs into primordial germ cells by inhibiting DNA methylation at the promoter of RHOX5, thereby activating its expression. Catalytically inactive regulatory factor of DNA methyltransferases that can either promote or inhibit DNA methylation depending on the context. TT3FDAV PD 6F57; 6BRR; 5YX2; 4U7T; 4U7P TT3FDAV SQ MAAIPALDPEAEPSMDVILVGSSELSSSVSPGTGRDLIAYEVKANQRNIEDICICCGSLQVHTQHPLFEGGICAPCKDKFLDALFLYDDDGYQSYCSICCSGETLLICGNPDCTRCYCFECVDSLVGPGTSGKVHAMSNWVCYLCLPSSRSGLLQRRRKWRSQLKAFYDRESENPLEMFETVPVWRRQPVRVLSLFEDIKKELTSLGFLESGSDPGQLKHVVDVTDTVRKDVEEWGPFDLVYGATPPLGHTCDRPPSWYLFQFHRLLQYARPKPGSPRPFFWMFVDNLVLNKEDLDVASRFLEMEPVTIPDVHGGSLQNAVRVWSNIPAIRSRHWALVSEEELSLLAQNKQSSKLAAKWPTKLVKNCFLPLREYFKYFSTELTSSL TT3FDAV TT Patented-recorded TTIV39N ID TTIV39N TTIV39N TN Fusion protein Bcr-Abl T315I mutant (Bcr-Abl T315I) TTIV39N UP P11274-P00519 TTIV39N UC BCR_HUMAN-ABL1_HUMAN TTIV39N BC Kinase TTIV39N SN T315I BCR-ABL; BCR-ABL T315I mutant TTIV39N GN BCR-ABL1 TTIV39N FC Difficult to inhibit with ATP mimetics. The mutation eliminates a critical hydrogen bonding interaction required for high-affinity binding of imatinib, nilotinib, and dasatinib and alters the topology of the ATP-binding pocket. TTIV39N SQ MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEVMLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR TTIV39N TT Patented-recorded TTXPTJE ID TTXPTJE TTXPTJE TN Gelatinase (GEL) TTXPTJE UP P08253; P14780 TTXPTJE UC MMP2_HUMAN; MMP9_HUMAN TTXPTJE BC Peptidase TTXPTJE SN Matrix metalloproteinase GEL; Gelatinase B; Gelatinase A; Collagenase IV; CLG4 TTXPTJE GN MMP2; MMP9 TTXPTJE FC A proteolytic enzyme that allows a living organism to hydrolyse gelatin into its sub-compounds (polypeptides, peptides, and amino acids) that can cross the cell membrane and be used by the organism. It is not a pepsin. TTXPTJE SQ MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC TTXPTJE TT Patented-recorded TT8BUGW ID TT8BUGW TT8BUGW TN Glycogen phosphorylase (PYG) TT8BUGW UP P06737; P11217; P11216 TT8BUGW UC PYGL_HUMAN; PYGM_HUMAN; PYGB_HUMAN TT8BUGW BC Glycosyltransferases TT8BUGW SN Glycogen phosphorylase TT8BUGW GN PYGL; PYGM; PYGB TT8BUGW FC Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. TT8BUGW SQ MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDIEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFGSTRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKLPWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFPKDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKFQNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDPKKLFVPRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVAALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEAYVKCQDKVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSDLKISLSNESNKVNGN TT8BUGW TT Patented-recorded TTOUZN5 ID TTOUZN5 TTOUZN5 TN Gremlin-1 (Gremlin-1) TTOUZN5 UP O60565 TTOUZN5 UC GREM1_HUMAN TTOUZN5 SN Proliferation-inducing gene 2; PIG2; Increased in high glucose protein 2; IHG-2; Down-regulated in Mos-transformed cells protein; DRM; DAND2; DAN domain family member 2; Cysteine knot superfamily 1, BMP antagonist 1; Cell proliferation-inducing gene 2 protein; CKTSF1B1 TTOUZN5 GN GREM1 TTOUZN5 FC Down-regulates the BMP4 signaling in a dose-dependent manner. Antagonist of BMP2; inhibits BMP2-mediated differentiation of osteoblasts (in vitro). Acts as inhibitor of monocyte chemotaxis. Can inhibit the growth or viability of normal cells but not transformed cells when is overexpressed. Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as a BMP antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop. TTOUZN5 PD 5AEJ TTOUZN5 SQ MSRTAYTVGALLLLLGTLLPAAEGKKKGSQGAIPPPDKAQHNDSEQTQSPQQPGSRNRGRGQGRGTAMPGEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVKQCRCISIDLD TTOUZN5 TT Patented-recorded TTUKLBM ID TTUKLBM TTUKLBM TN Huntingtin (HTT) TTUKLBM UP P42858 TTUKLBM UC HD_HUMAN TTUKLBM SN IT15; Huntington disease protein; HD protein; HD TTUKLBM GN HTT TTUKLBM FC May play a role in microtubule-mediated transport or vesicle function. TTUKLBM PD 6N8C; 6EZ8; 4RAV; 4FED; 4FEC TTUKLBM SQ MATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQQQQQPPPPPPPPPPPQLPQPPPQAQPLLPQPQPPPPPPPPPPGPAVAEEPLHRPKKELSATKKDRVNHCLTICENIVAQSVRNSPEFQKLLGIAMELFLLCSDDAESDVRMVADECLNKVIKALMDSNLPRLQLELYKEIKKNGAPRSLRAALWRFAELAHLVRPQKCRPYLVNLLPCLTRTSKRPEESVQETLAAAVPKIMASFGNFANDNEIKVLLKAFIANLKSSSPTIRRTAAGSAVSICQHSRRTQYFYSWLLNVLLGLLVPVEDEHSTLLILGVLLTLRYLVPLLQQQVKDTSLKGSFGVTRKEMEVSPSAEQLVQVYELTLHHTQHQDHNVVTGALELLQQLFRTPPPELLQTLTAVGGIGQLTAAKEESGGRSRSGSIVELIAGGGSSCSPVLSRKQKGKVLLGEEEALEDDSESRSDVSSSALTASVKDEISGELAASSGVSTPGSAGHDIITEQPRSQHTLQADSVDLASCDLTSSATDGDEEDILSHSSSQVSAVPSDPAMDLNDGTQASSPISDSSQTTTEGPDSAVTPSDSSEIVLDGTDNQYLGLQIGQPQDEDEEATGILPDEASEAFRNSSMALQQAHLLKNMSHCRQPSDSSVDKFVLRDEATEPGDQENKPCRIKGDIGQSTDDDSAPLVHCVRLLSASFLLTGGKNVLVPDRDVRVSVKALALSCVGAAVALHPESFFSKLYKVPLDTTEYPEEQYVSDILNYIDHGDPQVRGATAILCGTLICSILSRSRFHVGDWMGTIRTLTGNTFSLADCIPLLRKTLKDESSVTCKLACTAVRNCVMSLCSSSYSELGLQLIIDVLTLRNSSYWLVRTELLETLAEIDFRLVSFLEAKAENLHRGAHHYTGLLKLQERVLNNVVIHLLGDEDPRVRHVAAASLIRLVPKLFYKCDQGQADPVVAVARDQSSVYLKLLMHETQPPSHFSVSTITRIYRGYNLLPSITDVTMENNLSRVIAAVSHELITSTTRALTFGCCEALCLLSTAFPVCIWSLGWHCGVPPLSASDESRKSCTVGMATMILTLLSSAWFPLDLSAHQDALILAGNLLAASAPKSLRSSWASEEEANPAATKQEEVWPALGDRALVPMVEQLFSHLLKVINICAHVLDDVAPGPAIKAALPSLTNPPSLSPIRRKGKEKEPGEQASVPLSPKKGSEASAASRQSDTSGPVTTSKSSSLGSFYHLPSYLKLHDVLKATHANYKVTLDLQNSTEKFGGFLRSALDVLSQILELATLQDIGKCVEEILGYLKSCFSREPMMATVCVQQLLKTLFGTNLASQFDGLSSNPSKSQGRAQRLGSSSVRPGLYHYCFMAPYTHFTQALADASLRNMVQAEQENDTSGWFDVLQKVSTQLKTNLTSVTKNRADKNAIHNHIRLFEPLVIKALKQYTTTTCVQLQKQVLDLLAQLVQLRVNYCLLDSDQVFIGFVLKQFEYIEVGQFRESEAIIPNIFFFLVLLSYERYHSKQIIGIPKIIQLCDGIMASGRKAVTHAIPALQPIVHDLFVLRGTNKADAGKELETQKEVVVSMLLRLIQYHQVLEMFILVLQQCHKENEDKWKRLSRQIADIILPMLAKQQMHIDSHEALGVLNTLFEILAPSSLRPVDMLLRSMFVTPNTMASVSTVQLWISGILAILRVLISQSTEDIVLSRIQELSFSPYLISCTVINRLRDGDSTSTLEEHSEGKQIKNLPEETFSRFLLQLVGILLEDIVTKQLKVEMSEQQHTFYCQELGTLLMCLIHIFKSGMFRRITAAATRLFRSDGCGGSFYTLDSLNLRARSMITTHPALVLLWCQILLLVNHTDYRWWAEVQQTPKRHSLSSTKLLSPQMSGEEEDSDLAAKLGMCNREIVRRGALILFCDYVCQNLHDSEHLTWLIVNHIQDLISLSHEPPVQDFISAVHRNSAASGLFIQAIQSRCENLSTPTMLKKTLQCLEGIHLSQSGAVLTLYVDRLLCTPFRVLARMVDILACRRVEMLLAANLQSSMAQLPMEELNRIQEYLQSSGLAQRHQRLYSLLDRFRLSTMQDSLSPSPPVSSHPLDGDGHVSLETVSPDKDWYVHLVKSQCWTRSDSALLEGAELVNRIPAEDMNAFMMNSEFNLSLLAPCLSLGMSEISGGQKSALFEAAREVTLARVSGTVQQLPAVHHVFQPELPAEPAAYWSKLNDLFGDAALYQSLPTLARALAQYLVVVSKLPSHLHLPPEKEKDIVKFVVATLEALSWHLIHEQIPLSLDLQAGLDCCCLALQLPGLWSVVSSTEFVTHACSLIYCVHFILEAVAVQPGEQLLSPERRTNTPKAISEEEEEVDPNTQNPKYITAACEMVAEMVESLQSVLALGHKRNSGVPAFLTPLLRNIIISLARLPLVNSYTRVPPLVWKLGWSPKPGGDFGTAFPEIPVEFLQEKEVFKEFIYRINTLGWTSRTQFEETWATLLGVLVTQPLVMEQEESPPEEDTERTQINVLAVQAITSLVLSAMTVPVAGNPAVSCLEQQPRNKPLKALDTRFGRKLSIIRGIVEQEIQAMVSKRENIATHHLYQAWDPVPSLSPATTGALISHEKLLLQINPERELGSMSYKLGQVSIHSVWLGNSITPLREEEWDEEEEEEADAPAPSSPPTSPVNSRKHRAGVDIHSCSQFLLELYSRWILPSSSARRTPAILISEVVRSLLVVSDLFTERNQFELMYVTLTELRRVHPSEDEILAQYLVPATCKAAAVLGMDKAVAEPVSRLLESTLRSSHLPSRVGALHGVLYVLECDLLDDTAKQLIPVISDYLLSNLKGIAHCVNIHSQQHVLVMCATAFYLIENYPLDVGPEFSASIIQMCGVMLSGSEESTPSIIYHCALRGLERLLLSEQLSRLDAESLVKLSVDRVNVHSPHRAMAALGLMLTCMYTGKEKVSPGRTSDPNPAAPDSESVIVAMERVSVLFDRIRKGFPCEARVVARILPQFLDDFFPPQDIMNKVIGEFLSNQQPYPQFMATVVYKVFQTLHSTGQSSMVRDWVMLSLSNFTQRAPVAMATWSLSCFFVSASTSPWVAAILPHVISRMGKLEQVDVNLFCLVATDFYRHQIEEELDRRAFQSVLEVVAAPGSPYHRLLTCLRNVHKVTTC TTUKLBM TT Literature-reported TTJ13ST ID TTJ13ST TTJ13ST TN Inward rectifier potassium channel Kir1.1 (KCNJ1) TTJ13ST UP P48048 TTJ13ST UC KCNJ1_HUMAN TTJ13ST BC Inward rectifier potassium channel TTJ13ST SN ROMK1; Potassium channel, inwardly rectifying subfamily J member 1; Inward rectifier K(+) channel Kir1.1; ATP-sensitive inward rectifier potassium channel 1 TTJ13ST GN KCNJ1 TTJ13ST FC Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium. In the kidney, probably plays a major role in potassium homeostasis. TTJ13ST SQ MNASSRNVFDTLIRVLTESMFKHLRKWVVTRFFGHSRQRARLVSKDGRCNIEFGNVEAQSRFIFFVDIWTTVLDLKWRYKMTIFITAFLGSWFFFGLLWYAVAYIHKDLPEFHPSANHTPCVENINGLTSAFLFSLETQVTIGYGFRCVTEQCATAIFLLIFQSILGVIINSFMCGAILAKISRPKKRAKTITFSKNAVISKRGGKLCLLIRVANLRKSLLIGSHIYGKLLKTTVTPEGETIILDQININFVVDAGNENLFFISPLTIYHVIDHNSPFFHMAAETLLQQDFELVVFLDGTVESTSATCQVRTSYVPEEVLWGYRFAPIVSKTKEGKYRVDFHNFSKTVEVETPHCAMCLYNEKDVRARMKRGYDNPNFILSEVNETDDTKM TTJ13ST TT Patented-recorded TTXZCO0 ID TTXZCO0 TTXZCO0 TN Microtubule-associated protein tau phosphorylation (MAPT p) TTXZCO0 UP P10636 TTXZCO0 UC TAU_HUMAN TTXZCO0 SN tau phosphorylation; Paired helical filamenttau phosphorylation; Paired helical filament-tau phosphorylation; PHFtau; PHF-tau; Neurofibrillary tangle protein phosphorylation; MTBT1 phosphorylation; MAPTL phosphorylation TTXZCO0 GN MAPT TTXZCO0 FC The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. TTXZCO0 PD 6QJQ; 6QJP; 6QJM; 6QJH; 6NWQ TTXZCO0 SQ MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPAQDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSSDPLIQPSSPAVCPEPPSSPKYVSSVTSRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL TTXZCO0 TT Patented-recorded TTV1C0Z ID TTV1C0Z TTV1C0Z TN Neuropeptide S receptor (NPSR) TTV1C0Z UP Q6W5P4 TTV1C0Z UC NPSR1_HUMAN TTV1C0Z BC GPCR rhodopsin TTV1C0Z SN PGR14; Gprotein coupled receptor for asthma susceptibility; Gprotein coupled receptor PGR14; Gprotein coupled receptor 154; GPRA; GPR154; G-protein coupled receptor for asthma susceptibility; G-protein coupled receptor PGR14; G-protein coupled receptor 154 TTV1C0Z GN NPSR1 TTV1C0Z FC Promotes mobilization of intracellular Ca(2+) stores. Inhibits cell growth in response to NPS binding. Involved in pathogenesis of asthma and other IgE-mediated diseases. G-protein coupled receptor for neuropeptide S (NPS). TTV1C0Z SQ MPANFTEGSFDSSGTGQTLDSSPVACTETVTFTEVVEGKEWGSFYYSFKTEQLITLWVLFVFTIVGNSVVLFSTWRRKKKSRMTFFVTQLAITDSFTGLVNILTDINWRFTGDFTAPDLVCRVVRYLQVVLLYASTYVLVSLSIDRYHAIVYPMKFLQGEKQARVLIVIAWSLSFLFSIPTLIIFGKRTLSNGEVQCWALWPDDSYWTPYMTIVAFLVYFIPLTIISIMYGIVIRTIWIKSKTYETVISNCSDGKLCSSYNRGLISKAKIKAIKYSIIIILAFICCWSPYFLFDILDNFNLLPDTQERFYASVIIQNLPALNSAINPLIYCVFSSSISFPCREQRSQDSRMTFRERTERHEMQILSKPEFI TTV1C0Z TT Patented-recorded TTV1C0Z FM GPCR rhodopsin TTHKW7D ID TTHKW7D TTHKW7D TN Secretory phospholipase A2 receptor (PLA2R) TTHKW7D UP Q13018 TTHKW7D UC PLA2R_HUMAN TTHKW7D SN Soluble secretory phospholipase A2 receptor; Soluble PLA2R; Soluble PLA2-R; PLA2-R; M-type receptor; CLEC13C; C-type lectin domain family 13 member C; 180 kDa secretory phospholipase A2 receptor TTHKW7D GN PLA2R1 TTHKW7D FC Acts as a receptor for phosholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B. Receptor for secretory phospholipase A2 (sPLA2). TTHKW7D SQ MLLSPSLLLLLLLGAPRGCAEGVAAALTPERLLEWQDKGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGDICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWGFCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKKYLNHIDHEIVEKDAWKYYATHCEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENASETWIGLSSNKIPVSFEWSNDSSVIFTNWHTLEPHIFPNRSQLCVSAEQSEGHWKVKNCEERLFYICKKAGHVLSDAESGCQEGWERHGGFCYKIDTVLRSFDQASSGYYCPPALVTITNRFEQAFITSLISSVVKMKDSYFWIALQDQNDTGEYTWKPVGQKPEPVQYTHWNTHQPRYSGGCVAMRGRHPLGRWEVKHCRHFKAMSLCKQPVENQEKAEYEERWPFHPCYLDWESEPGLASCFKVFHSEKVLMKRTWREAEAFCEEFGAHLASFAHIEEENFVNELLHSKFNWTEERQFWIGFNKRNPLNAGSWEWSDRTPVVSSFLDNTYFGEDARNCAVYKANKTLLPLHCGSKREWICKIPRDVKPKIPFWYQYDVPWLFYQDAEYLFHTFASEWLNFEFVCSWLHSDLLTIHSAHEQEFIHSKIKALSKYGASWWIGLQEERANDEFRWRDGTPVIYQNWDTGRERTVNNQSQRCGFISSITGLWGSEECSVSMPSICKRKKVWLIEKKKDTPKQHGTCPKGWLYFNYKCLLLNIPKDPSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFITMNLFGQTTSVWIGLQNDDYETWLNGKPVVYSNWSPFDIINIPSHNTTEVQKHIPLCALLSSNPNFHFTGKWYFEDCGKEGYGFVCEKMQDTSGHGVNTSDMYPMPNTLEYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFTFWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIKFKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLNAQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFICKMEADIHTAEALPEKGPSHSIIPLAVVLTLIVIVAICTLSFCIYKHNGGFFRRLAGFRNPYYPATNFSTVYLEENILISDLEKSDQ TTHKW7D TT Patented-recorded TTHKW7D KE hsa04145:Phagosome; hsa05152:Tuberculosis TT7B4H9 ID TT7B4H9 TT7B4H9 TN TLR1-TLR2 complex (TLR1/2) TT7B4H9 UP Q15399-O60603 TT7B4H9 UC TLR1_HUMAN-TLR2_HUMAN TT7B4H9 BC Toll-like receptor TT7B4H9 SN Toll-like receptor 1 and 2 complex TT7B4H9 GN TLR1-TLR2 TT7B4H9 FC Mediates the innate immune response to bacterial lipoproteins or lipopeptides. TT7B4H9 SQ MTSIFHFAIIFMLILQIRIQLSEESEFLVDRSKNGLIHVPKDLSQKTTILNISQNYISELWTSDILSLSKLRILIISHNRIQYLDISVFKFNQELEYLDLSHNKLVKISCHPTVNLKHLDLSFNAFDALPICKEFGNMSQLKFLGLSTTHLEKSSVLPIAHLNISKVLLVLGETYGEKEDPEGLQDFNTESLHIVFPTNKEFHFILDVSVKTVANLELSNIKCVLEDNKCSYFLSILAKLQTNPKLSNLTLNNIETTWNSFIRILQLVWHTTVWYFSISNVKLQGQLDFRDFDYSGTSLKALSIHQVVSDVFGFPQSYIYEIFSNMNIKNFTVSGTRMVHMLCPSKISPFLHLDFSNNLLTDTVFENCGHLTELETLILQMNQLKELSKIAEMTTQMKSLQQLDISQNSVSYDEKKGDCSWTKSLLSLNMSSNILTDTIFRCLPPRIKVLDLHSNKIKSIPKQVVKLEALQELNVAFNSLTDLPGCGSFSSLSVLIIDHNSVSHPSADFFQSCQKMRSIKAGDNPFQCTCELGEFVKNIDQVSSEVLEGWPDSYKCDYPESYRGTLLKDFHMSELSCNITLLIVTIVATMLVLAVTVTSLCSYLDLPWYLRMVCQWTQTRRRARNIPLEELQRNLQFHAFISYSGHDSFWVKNELLPNLEKEGMQICLHERNFVPGKSIVENIITCIEKSYKSIFVLSPNFVQSEWCHYELYFAHHNLFHEGSNSLILILLEPIPQYSIPSSYHKLKSLMARRTYLEWPKEKSKRGLFWANLRAAINIKLTEQAKKMPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLMVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNIDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS TT7B4H9 TT Patented-recorded TT7B4H9 FM Toll-like receptor family TTEMWSD ID TTEMWSD TTEMWSD TN von Hippel-Lindau disease tumor suppressor (VHL) TTEMWSD UP P40337 TTEMWSD UC VHL_HUMAN TTEMWSD SN pVHL; Protein G7 TTEMWSD GN VHL TTEMWSD FC Seems to act as a target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia-inducible factor (HIF) under normoxic conditions. Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases. Ubiquitinates, in an oxygen-responsive manner, ADRB2. Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex. TTEMWSD PD 6GMX; 6GMR; 6GMQ; 6GMN; 6GFZ TTEMWSD SQ MPRRAENWDEAEVGAEEAGVEEYGPEEDGGEESGAEESGPEESGPEELGAEEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD TTEMWSD TT Patented-recorded TTJOMH6 ID TTJOMH6 TTJOMH6 TN Zinc finger protein GLI1 (Gli1) TTJOMH6 UP P08151 TTJOMH6 UC GLI1_HUMAN TTJOMH6 SN Oncogene GLI; Glioma-associated oncogene; GLI TTJOMH6 GN GLI1 TTJOMH6 FC Binds to the DNA consensus sequence 5'-GACCACCCA-3'. Regulates the transcription of specific genes during normal development. Plays a role in craniofacial development and digital development, as well as development of the central nervous system and gastrointestinal tract. Mediates SHH signaling. Plays a role in cell proliferation and differentiation via its role in SHH signaling. Acts as a transcriptional activator. TTJOMH6 PD 5OM0; 4KMD; 4BLB; 2GLI TTJOMH6 SQ MFNSMTPPPISSYGEPCCLRPLPSQGAPSVGTEGLSGPPFCHQANLMSGPHSYGPARETNSCTEGPLFSSPRSAVKLTKKRALSISPLSDASLDLQTVIRTSPSSLVAFINSRCTSPGGSYGHLSIGTMSPSLGFPAQMNHQKGPSPSFGVQPCGPHDSARGGMIPHPQSRGPFPTCQLKSELDMLVGKCREEPLEGDMSSPNSTGIQDPLLGMLDGREDLEREEKREPESVYETDCRWDGCSQEFDSQEQLVHHINSEHIHGERKEFVCHWGGCSRELRPFKAQYMLVVHMRRHTGEKPHKCTFEGCRKSYSRLENLKTHLRSHTGEKPYMCEHEGCSKAFSNASDRAKHQNRTHSNEKPYVCKLPGCTKRYTDPSSLRKHVKTVHGPDAHVTKRHRGDGPLPRAPSISTVEPKREREGGPIREESRLTVPEGAMKPQPSPGAQSSCSSDHSPAGSAANTDSGVEMTGNAGGSTEDLSSLDEGPCIAGTGLSTLRRLENLRLDQLHQLRPIGTRGLKLPSLSHTGTTVSRRVGPPVSLERRSSSSSSISSAYTVSRRSSLASPFPPGSPPENGASSLPGLMPAQHYLLRARYASARGGGTSPTAASSLDRIGGLPMPPWRSRAEYPGYNPNAGVTRRASDPAQAADRPAPARVQRFKSLGCVHTPPTVAGGGQNFDPYLPTSVYSPQPPSITENAAMDARGLQEEPEVGTSMVGSGLNPYMDFPPTDTLGYGGPEGAAAEPYGARGPGSLPLGPGPPTNYGPNPCPQQASYPDPTQETWGEFPSHSGLYPGPKALGGTYSQCPRLEHYGQVQVKPEQGCPVGSDSTGLAPCLNAHPSEGPPHPQPLFSHYPQPSPPQYLQSGPYTQPPPDYLPSEPRPCLDFDSPTHSTGQLKAQLVCNYVQSQQELLWEGGGREDAPAQEPSYQSPKFLGGSQVSPSRAKAPVNTYGPGFGPNLPNHKSGSYPTPSPCHENFVVGANRASHRAAAPPRLLPPLPTCYGPLKVGGTNPSCGHPEVGRLGGGPALYPPPEGQVCNPLDSLDLDNTQLDFVAILDEPQGLSPPPSHDQRGSSGHTPPPSGPPNMAVGNMSVLLRSLPGETEFLNSSA TTJOMH6 TT Patented-recorded TTJOMH6 FM GLI C2H2-type zinc-finger TT5YPJF ID TT5YPJF TT5YPJF TN CD80-PD-L1 interaction (CD80/PD-L1 PPI) TT5YPJF UP P33681-Q9NZQ7 TT5YPJF UC CD80_HUMAN-PD1L1_HUMAN TT5YPJF SN T-lymphocyte activation antigen CD80/Programmed cell death 1 ligand 1 PPI TT5YPJF GN CD80-CD274 TT5YPJF FC Augments activated alloreactive CD4+ T cell proliferation and apoptosis and ameliorates acute graft versus host disease TT5YPJF SQ MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEETMGHTRRQGTSPSKCPYLNFFQLLVLAGLSHFCSGVIHVTKEVKEVATLSCGHNVSVEELAQTRIYWQKEKKMVLTMMSGDMNIWPEYKNRTIFDITNNLSIVILALRPSDEGTYECVVLKYEKDAFKREHLAEVTLSVKADFPTPSISDFEIPTSNIRRIICSTSGGFPEPHLSWLENGEELNAINTTVSQDPETELYAVSSKLDFNMTTNHSFMCLIKYGHLRVNQTFNWNTTKQEHFPDNLLPSWAITLISVNGIFVICCLTYCFAPRCRERRRNERLRRESVRPV TT5YPJF TT Patented-recorded TTZS04O ID TTZS04O TTZS04O TN Gamma-secretase subunit APH-1A/1B (APH-1) TTZS04O UP Q96BI3-Q8WW43 TTZS04O UC APH1A_HUMAN-APH1B_HUMAN TTZS04O SN Anterior pharynx-defective 1 TTZS04O GN APH1A-APH1B TTZS04O FC The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels. TTZS04O SQ MTAAVFFGCAFIAFGPALALYVFTIATEPLRIIFLIAGAFFWLVSLLISSLVWFMARVIIDNKDGPTQKYLLIFGAFVSVYIQEMFRFAYYKLLKKASEGLKSINPGETAPSMRLLAYVSGLGFGIMSGVFSFVNTLSDSLGPGTVGIHGDSPQFFLYSAFMTLVIILLHVFWGIVFFDGCEKKKWGILLIVLLTHLLVSAQTFISSYYGINLASAFIILVLMGTWAFLAAGGSCRSLKLCLLCQDKNFLLYNQRSRMGAAVFFGCTFVAFGPAFALFLITVAGDPLRVIILVAGAFFWLVSLLLASVVWFILVHVTDRSDARLQYGLLIFGAAVSVLLQEVFRFAYYKLLKKADEGLASLSEDGRSPISIRQMAYVSGLSFGIISGVFSVINILADALGPGVVGIHGDSPYYFLTSAFLTAAIILLHTFWGVVFFDACERRRYWALGLVVGSHLLTSGLTFLNPWYEASLLPIYAVTVSMGLWAFITAGGSLRSIQRSLLCRRQEDSRVMVYSALRIPPED TTZS04O TT Patented-recorded TTZS04O FM APH-1 family TT956B0 ID TT956B0 TT956B0 TN Keap1-Nrf2[DLG] PPI (KEAP1-Nrf2 DLG) TT956B0 UP Q14145-Q16236 TT956B0 UC KEAP1_HUMAN-NF2L2_HUMAN TT956B0 SN Kelch-like protein 19-Nrf2[DLG]; Kelch-like ECH-associated protein 1-Nrf2[DLG]; KLHL19-Nrf2[DLG]; KIAA0132-Nrf2[DLG]; INrf2-Nrf2[DLG]; Cytosolic inhibitor of Nrf2-Nrf2[DLG] TT956B0 GN KEAP1-NFE2L2 TT956B0 FC Retains NFE2L2/NRF2 and may also retain BPTF in the cytosol. Targets PGAM5 for ubiquitination and degradation by the proteasome. Acts as a substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. TT956B0 SQ MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTCMMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN TT956B0 TT Patented-recorded TTGIZLN ID TTGIZLN TTGIZLN TN Keap1-Nrf2[dual DLG and ETGE] PPI (KEAP1-Nrf2 DLG and ETGE) TTGIZLN UP Q14145-Q16236 TTGIZLN UC KEAP1_HUMAN-NF2L2_HUMAN TTGIZLN SN Kelch-like protein 19-Nrf2[dual DLG and ETGE]; Kelch-like ECH-associated protein 1-Nrf2[dual DLG and ETGE]; KLHL19-Nrf2[dual DLG and ETGE]; KIAA0132-Nrf2[dual DLG and ETGE]; INrf2-Nrf2[dual DLG and ETGE]; Cytosolic inhibitor of Nrf2-Nrf2[dual DLG and ETGE] TTGIZLN GN KEAP1-NFE2L2 TTGIZLN FC Retains NFE2L2/NRF2 and may also retain BPTF in the cytosol. Targets PGAM5 for ubiquitination and degradation by the proteasome. Acts as a substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. TTGIZLN SQ MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTCMMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN TTGIZLN TT Patented-recorded TTHQJI6 ID TTHQJI6 TTHQJI6 TN Keap1-Nrf2[ETGE] PPI (KEAP1-Nrf2 ETGE) TTHQJI6 UP Q14145-Q16236 TTHQJI6 UC KEAP1_HUMAN-NF2L2_HUMAN TTHQJI6 SN Kelch-like protein 19-Nrf2[ETGE]; Kelch-like ECH-associated protein 1-Nrf2[ETGE]; KLHL19-Nrf2[ETGE]; KIAA0132-Nrf2[ETGE]; INrf2-Nrf2[ETGE]; Cytosolic inhibitor of Nrf2-Nrf2[ETGE] TTHQJI6 GN KEAP1-NFE2L2 TTHQJI6 FC Retains NFE2L2/NRF2 and may also retain BPTF in the cytosol. Targets PGAM5 for ubiquitination and degradation by the proteasome. Acts as a substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. TTHQJI6 SQ MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTCMMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN TTHQJI6 TT Patented-recorded TT23XQV ID TT23XQV TT23XQV TN PD-1-PD-L1 interaction (PD-1/PD-L1 PPI) TT23XQV UP Q15116-Q9NZQ7 TT23XQV UC PDCD1_HUMAN-PD1L1_HUMAN TT23XQV SN Programmed cell death 1/Programmed cell death 1 ligand 1 PPI TT23XQV GN PDCD1-CD274 TT23XQV FC The PD-1/PD-L1 axis is probably also important for immune evasion of B-cell lymphomas with a viral aetiology, including those associated with human immunodeficiency virus (HIV) and Epstein-Barr virus (EBV). TT23XQV SQ MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEETMQIPQAPWPVVWAVLQLGWRPGWFLDSPDRPWNPPTFSPALLVVTEGDNATFTCSFSNTSESFVLNWYRMSPSNQTDKLAAFPEDRSQPGQDCRFRVTQLPNGRDFHMSVVRARRNDSGTYLCGAISLAPKAQIKESLRAELRVTERRAEVPTAHPSPSPRPAGQFQTLVVGVVGGLLGSLVLLVWVLAVICSRAARGTIGARRTGQPLKEDPSAVPVFSVDYGELDFQWREKTPEPPVPCVPEQTEYATIVFPSGMGTSSPARRGSADGPRSAQPLRPEDGHCSWPL TT23XQV TT Patented-recorded TTLRFIH ID TTLRFIH TTLRFIH TN Signal transducer and activator of transcription 5 (STAT5) TTLRFIH UP P42229; P51692 TTLRFIH UC STA5A_HUMAN; STA5B_HUMAN TTLRFIH SN Signal transducer and activator of transcription 5 TTLRFIH GN STAT5A; STAT5B TTLRFIH FC Involved in cytosolic signalling and in mediating the expression of specific genes. Aberrant STAT5 activity has been shown to be closely connected to a wide range of human cancers, and silencing this aberrant activity is an area of active research in medicinal chemistry. TTLRFIH SQ MAGWIQAQQLQGDALRQMQVLYGQHFPIEVRHYLAQWIESQPWDAIDLDNPQDRAQATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQKTYDRCPLELVRCIRHILYNEQRLVREANNCSSPAGILVDAMSQKHLQINQTFEELRLVTQDTENELKKLQQTQEYFIIQYQESLRIQAQFAQLAQLSPQERLSRETALQQKQVSLEAWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLCQQLPIPGPVEEMLAEVNATITDIISALVTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNECSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRADRRGAESVTEEKFTVLFESQFSVGSNELVFQVKTLSLPVVVIVHGSQDHNATATVLWDNAFAEPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNNSSSHLEDYSGLSVSWSQFNRENLPGWNYTFWQWFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPERNLWNLKPFTTRDFSIRSLADRLGDLSYLIYVFPDRPKDEVFSKYYTPVLAKAVDGYVKPQIKQVVPEFVNASADAGGSSATYMDQAPSPAVCPQAPYNMYPQNPDHVLDQDGEFDLDETMDVARHVEELLRRPMDSLDSRLSPPAGLFTSARGSLS TTLRFIH TT Patented-recorded TTLRFIH FM Transcription factor STAT family TTSJ6Q4 ID TTSJ6Q4 TTSJ6Q4 TN LOX-5 messenger RNA (ALOX5 mRNA) TTSJ6Q4 UP P09917 TTSJ6Q4 UC LOX5_HUMAN TTSJ6Q4 BC mRNA target TTSJ6Q4 SN LOG5 (mRNA); 5-lipoxygenase (mRNA); 5-LO (mRNA) TTSJ6Q4 GN ALOX5 TTSJ6Q4 FC Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. TTSJ6Q4 EC EC 1.13.11.34 TTSJ6Q4 PD 3V99; 3V98; 3V92; 3O8Y; 2ABV TTSJ6Q4 SQ MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGCNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECGLFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWEAIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLTVVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPYYYLSPDRIPNSVAI TTSJ6Q4 TT Discontinued TTSJ6Q4 FM mRNA target TTSJ6Q4 KE hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse; hsa04913:Ovarian steroidogenesis; hsa05145:Toxoplasmosis TTY6EWA ID TTY6EWA TTY6EWA TN Neuropeptide Y receptor type 5 (NPY5R) TTY6EWA UP Q15761 TTY6EWA UC NPY5R_HUMAN TTY6EWA BC GPCR rhodopsin TTY6EWA SN Y5 receptor; Neuropeptide Y receptor Y5; Neuropeptide Y (NPY) Y(5) receptor; NPYY5; NPY5R; NPY5-R; NPY-Y5 receptor TTY6EWA GN NPY5R TTY6EWA FC Receptor for neuropeptide Y and peptide YY. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity. Seems to be associated with food intake. Could be involved in feeding disorders. TTY6EWA PD 2HE6 TTY6EWA SQ MDLELDEYYNKTLATENNTAATRNSDFPVWDDYKSSVDDLQYFLIGLYTFVSLLGFMGNLLILMALMKKRNQKTTVNFLIGNLAFSDILVVLFCSPFTLTSVLLDQWMFGKVMCHIMPFLQCVSVLVSTLILISIAIVRYHMIKHPISNNLTANHGYFLIATVWTLGFAICSPLPVFHSLVELQETFGSALLSSRYLCVESWPSDSYRIAFTISLLLVQYILPLVCLTVSHTSVCRSISCGLSNKENRLEENEMINLTLHPSKKSGPQVKLSGSHKWSYSFIKKHRRRYSKKTACVLPAPERPSQENHSRILPENFGSVRSQLSSSSKFIPGVPTCFEIKPEENSDVHELRVKRSVTRIKKRSRSVFYRLTILILVFAVSWMPLHLFHVVTDFNDNLISNRHFKLVYCICHLLGMMSCCLNPILYGFLNNGIKADLVSLIHCLHM TTY6EWA TT Discontinued TTY6EWA KE hsa04080:Neuroactive ligand-receptor interaction TTY6EWA RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTFQEO5 ID TTFQEO5 TTFQEO5 TN Squalene synthetase (FDFT1) TTFQEO5 UP P37268 TTFQEO5 UC FDFT_HUMAN TTFQEO5 BC Alkyl aryl transferase TTFQEO5 SN Squalene synthase; SS; SQS; Farnesyl-diphosphate farnesyltransferase; FPP:FPP farnesyltransferase TTFQEO5 GN FDFT1 TTFQEO5 FC Participates in the isoprenoid biosynthetic pathway, catalyzing a two-step reaction in which two identical molecules of farnesyl pyrophosphate (FPP) are converted into squalene, with the consumption of NADPH. TTFQEO5 EC EC 2.5.1.21 TTFQEO5 PD 3WSA; 3WEK; 3WEJ; 3WEI; 3WEH TTFQEO5 SQ MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQALDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQVLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVGIGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYVKKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATLAACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTRQIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH TTFQEO5 TT Discontinued TTFQEO5 KE hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics TTFQEO5 RC R-HSA-191273:Cholesterol biosynthesis; R-HSA-1989781:PPARA activates gene expression; R-HSA-2426168:Activation of gene expression by SREBF (SREBP) TTA0P7K ID TTA0P7K TTA0P7K TN Complement factor B (CFB) TTA0P7K UP P00751 TTA0P7K UC CFAB_HUMAN TTA0P7K BC Peptidase TTA0P7K SN Properdin factor B; PBF2; Glycinerich beta glycoprotein; Glycine-rich beta glycoprotein; GBG; Complement factor B Bb fragment; C3/C5 convertase; BFD; BF TTA0P7K GN CFB TTA0P7K FC Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B-lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes. TTA0P7K EC EC 3.4.21.47 TTA0P7K PD 6RAV; 6QSX; 6QSW; 5M6W; 3HS0 TTA0P7K SQ MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL TTA0P7K TT Clinical trial TTA0P7K FM Peptidase TTA0P7K KE hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection TTA0P7K RC R-HSA-173736:Alternative complement activation; R-HSA-174577:Activation of C3 and C5; R-HSA-977606:Regulation of Complement cascade TT1UCIJ ID TT1UCIJ TT1UCIJ TN C-X-C chemokine receptor type 3 (CXCR3) TT1UCIJ UP P49682 TT1UCIJ UC CXCR3_HUMAN TT1UCIJ BC GPCR rhodopsin TT1UCIJ SN Interferon-inducible protein 10 receptor; IP-10 receptor; GPR9; G protein-coupled receptor 9; Chemokine receptor CXCR3/interferon-inducible protein-10; Chemokine receptor CXCR3; CXCR3/IP-10; CXCR-3; CXC-R3; CKR-L2; CD183 antigen; CD183 TT1UCIJ GN CXCR3 TT1UCIJ FC Binds to CCL21. Probably promotes cell chemotaxis response. Isoform 1: Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and mediates the proliferation, survival and angiogenic activity of human mesangial cells (HMC) through a heterotrimeric G-protein signaling pathway. TT1UCIJ SQ MVLEVSDHQVLNDAEVAALLENFSSSYDYGENESDSCCTSPPCPQDFSLNFDRAFLPALYSLLFLLGLLGNGAVAAVLLSRRTALSSTDTFLLHLAVADTLLVLTLPLWAVDAAVQWVFGSGLCKVAGALFNINFYAGALLLACISFDRYLNIVHATQLYRRGPPARVTLTCLAVWGLCLLFALPDFIFLSAHHDERLNATHCQYNFPQVGRTALRVLQLVAGFLLPLLVMAYCYAHILAVLLVSRGQRRLRAMRLVVVVVVAFALCWTPYHLVVLVDILMDLGALARNCGRESRVDVAKSVTSGLGYMHCCLNPLLYAFVGVKFRERMWMLLLRLGCPNQRGLQRQPSSSRRDSSWSETSEASYSGL TT1UCIJ TT Preclinical TT1UCIJ KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway TT1UCIJ RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTOQ9GZ ID TTOQ9GZ TTOQ9GZ TN Cytochrome P450 reductase (P450) TTOQ9GZ UP P16435 TTOQ9GZ UC NCPR_HUMAN TTOQ9GZ BC NADH/NADPH oxidoreductase TTOQ9GZ SN P450R; NADPH--cytochrome P450 reductase; CYPOR; CPR TTOQ9GZ GN POR TTOQ9GZ FC This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. TTOQ9GZ EC EC 1.6.2.4 TTOQ9GZ PD 5FA6; 5EMN; 3QFT; 3QFS; 3QFR TTOQ9GZ SQ MGDSHVDTSSTVSEAVAEEVSLFSMTDMILFSLIVGLLTYWFLFRKKKEEVPEFTKIQTLTSSVRESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDNALVVFCMATYGEGDPTDNAQDFYDWLQETDVDLSGVKFAVFGLGNKTYEHFNAMGKYVDKRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEHFGVEATGEESSIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHPFPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWVVEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYETKAGRINKGVATNWLRAKEPAGENGGRALVPMFVRKSQFRLPFKATTPVIMVGPGTGVAPFIGFIQERAWLRQQGKEVGETLLYYGCRRSDEDYLYREELAQFHRDGALTQLNVAFSREQSHKVYVQHLLKQDREHLWKLIEGGAHIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVDYIKKLMTKGRYSLDVWS TTOQ9GZ TT Discontinued TTOQ9GZ FM Oxidoreductases acting on NADH or NADPH TTURQ2G ID TTURQ2G TTURQ2G TN Glutamate decarboxylase (GLUL) TTURQ2G UP P15104 TTURQ2G UC GLNA_HUMAN TTURQ2G BC Carbon-nitrogen ligase TTURQ2G SN Glutamateammonia ligase TTURQ2G GN GLUL TTURQ2G FC Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia. Essential for proliferation of fetal skin fibroblasts. Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ. Plays a role in ribosomal 40S subunit biogenesis. Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine. TTURQ2G EC EC 6.3.1.2 TTURQ2G PD 2QC8; 2OJW TTURQ2G SQ MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETGDEPFQYKN TTURQ2G TT Discontinued TTURQ2G FM Carbon-nitrogen ligase TTURQ2G KE hsa00250:Alanine, aspartate and glutamate metabolism; hsa00330:Arginine and proline metabolism; hsa00630:Glyoxylate and dicarboxylate metabolism; hsa00910:Nitrogen metabolism; hsa01100:Metabolic pathways; hsa01230:Biosynthesis of amino acids; hsa04724:Glutamatergic synapse; hsa04727:GABAergic synapse TTURQ2G RC R-HSA-70614:Amino acid synthesis and interconversion (transamination) TT9AZWY ID TT9AZWY TT9AZWY TN HSPB1 messenger RNA (HSPB1 mRNA) TT9AZWY UP P04792 TT9AZWY UC HSPB1_HUMAN TT9AZWY BC mRNA target TT9AZWY SN Stress-responsive protein 27 (mRNA); SRP27 (mRNA); HspB1 (mRNA); Heat shock protein beta-1 (mRNA); Heat shock 27 kDa protein (mRNA); HSP28 (mRNA); HSP 27 (mRNA); Estrogen-regulated 24 kDa protein (mRNA); 28 kDa heat shock protein (mRNA) TT9AZWY GN HSPB1 TT9AZWY FC Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins. Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. TT9AZWY PD 4MJH; 3Q9Q; 3Q9P; 2N3J TT9AZWY SQ MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK TT9AZWY TT Discontinued TT9AZWY FM mRNA target TT9AZWY KE hsa04010:MAPK signaling pathway; hsa04370:VEGF signaling pathway; hsa05146:Amoebiasis; hsa05169:Epstein-Barr virus infection TT9AZWY RC R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5687128:MAPK6/MAPK4 signaling TTJA1ZO ID TTJA1ZO TTJA1ZO TN ITGB3 messenger RNA (ITGB3 mRNA) TTJA1ZO UP P05106 TTJA1ZO UC ITB3_HUMAN TTJA1ZO BC mRNA target TTJA1ZO SN Platelet membrane glycoprotein IIIa (mRNA); Integrin beta-3 (mRNA); GPIIIa (mRNA); GP3A (mRNA); CD61 (mRNA) TTJA1ZO GN ITGB3 TTJA1ZO FC Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. Fibrinogen binding enhances SELP expression in activated platelets. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling. ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling. ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling. ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling. ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. TTJA1ZO PD 6CKB; 6BXJ; 6BXF; 6BXB; 6AVU TTJA1ZO SQ MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT TTJA1ZO TT Discontinued TTJA1ZO FM mRNA target TTJA1ZO KE hsa04015:Rap1 signaling pathway; hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04611:Platelet activation; hsa04640:Hematopoietic cell lineage; hsa04810:Regulation of actin cytoskeleton; hsa04919:Thyroid hormone signaling pathway; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTJA1ZO RC R-HSA-114608:Platelet degranulation; R-HSA-1566948:Elastic fibre formation; R-HSA-210990:PECAM1 interactions; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-354194:GRB2:SOS provides linkage to MAPK signaling for Integrins; R-HSA-372708:p130Cas linkage to MAPK signaling for integrins; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5674135:MAP2K and MAPK activation TTVBPDM ID TTVBPDM TTVBPDM TN Metabotropic glutamate receptor 1 (mGluR1) TTVBPDM UP Q13255 TTVBPDM UC GRM1_HUMAN TTVBPDM BC GPCR glutamate TTVBPDM SN mGLUR1; Glutamate receptor mGLU1; GPRC1A TTVBPDM GN GRM1 TTVBPDM FC Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum. G-protein coupled receptor for glutamate. TTVBPDM PD 4OR2; 3KS9 TTVBPDM SQ MVGLLLFFFPAIFLEVSLLPRSPGRKVLLAGASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEAMFHTLDKINADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDEKDGINRCLPDGQSLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDIPQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMDAFKELAAQEGLCIAHSDKIYSNAGEKSFDRLLRKLRERLPKARVVVCFCEGMTVRGLLSAMRRLGVVGEFSLIGSDGWADRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLDTNTRNPWFPEFWQHRFQCRLPGHLLENPNFKRICTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDAMKPIDGSKLLDFLIKSSFIGVSGEEVWFDEKGDAPGRYDIMNLQYTEANRYDYVHVGTWHEGVLNIDDYKIQMNKSGVVRSVCSEPCLKGQIKVIRKGEVSCCWICTACKENEYVQDEFTCKACDLGWWPNADLTGCEPIPVRYLEWSNIESIIAIAFSCLGILVTLFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTLVVTLIIMEPPMPILSYPSIKEVYLICNTSNLGVVAPLGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVGDGKLPCRSNTFLNIFRRKKAGAGNANSNGKSVSWSEPGGGQVPKGQHMWHRLSVHVKTNETACNQTAVIKPLTKSYQGSGKSLTFSDTSTKTLYNVEEEEDAQPIRFSPPGSPSMVVHRRVPSAATTPPLPSHLTAEETPLFLAEPALPKGLPPPLQQQQQPPPQQKSLMDQLQGVVSNFSTAIPDFHAVLAGPGGPGNGLRSLYPPPPPPQHLQMLPLQLSTFGEELVSPPADDDDDSERFKLLQEYVYEHEREGNTEEDELEEEEEDLQAASKLTPDDSPALTPPSPFRDSVASGSSVPSSPVSESVLCTPPNVSYASVILRDYKQSSSTL TTVBPDM TT Discontinued TTVBPDM FM GPCR glutamate TTVBPDM KE hsa04020:Calcium signaling pathway; hsa04068:FoxO signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04720:Long-term potentiation; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04730:Long-term depression; hsa04915:Estrogen signaling pathway TTVBPDM RC R-HSA-416476:G alpha (q) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors) TTN3GBV ID TTN3GBV TTN3GBV TN Transcription factor AP-1 (JUN) TTN3GBV UP P05412 TTN3GBV UC JUN_HUMAN TTN3GBV BC Basic leucine zipper bZIP TTN3GBV SN V-jun avian sarcoma virus 17 oncogene homolog; Proto-oncogene c-jun; P39; C-jun proto-oncogene; Activator protein-1; Activator protein 1; AP1; AP-1 transcription factor TTN3GBV GN JUN TTN3GBV FC Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells. Binds to the USP28 promoter in colorectal cancer (CRC) cells. Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. TTN3GBV PD 5T01; 5FV8; 1T2K; 1S9K; 1JNM TTN3GBV SQ MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF TTN3GBV TT Discontinued TTN3GBV KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04024:cAMP signaling pathway; hsa04310:Wnt signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04620:Toll-like receptor signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05231:Choline metabolism in cancer; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis TTN3GBV RC R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-450341:Activation of the AP-1 family of transcription factors; R-HSA-5687128:MAPK6/MAPK4 signaling TTR6K75 ID TTR6K75 TTR6K75 TN 5-HT 3B receptor (HTR3B) TTR6K75 UP O95264 TTR6K75 UC 5HT3B_HUMAN TTR6K75 BC GPCR rhodopsin TTR6K75 SN Serotonin receptor 3B; 5-hydroxytryptamine receptor 3B; 5-HT3B; 5-HT3-B; 5-HT-3B TTR6K75 GN HTR3B TTR6K75 FC This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel. TTR6K75 SQ MLSSVMAPLWACILVAAGILATDTHHPQDSALYHLSKQLLQKYHKEVRPVYNWTKATTVYLDLFVHAILDVDAENQILKTSVWYQEVWNDEFLSWNSSMFDEIREISLPLSAIWAPDIIINEFVDIERYPDLPYVYVNSSGTIENYKPIQVVSACSLETYAFPFDVQNCSLTFKSILHTVEDVDLAFLRSPEDIQHDKKAFLNDSEWELLSVSSTYSILQSSAGGFAQIQFNVVMRRHPLVYVVSLLIPSIFLMLVDLGSFYLPPNCRARIVFKTSVLVGYTVFRVNMSNQVPRSVGSTPLIGHFFTICMAFLVLSLAKSIVLVKFLHDEQRGGQEQPFLCLRGDTDADRPRVEPRAQRAVVTESSLYGEHLAQPGTLKEVWSQLQSISNYLQTQDQTDQQEAEWLVLLSRFDRLLFQSYLFMLGIYTITLCSLWALWGGV TTR6K75 TT Discontinued TTR6K75 KE hsa04726:Serotonergic synapse TTR6K75 RC R-HSA-975298:Ligand-gated ion channel transport TT6B75U ID TT6B75U TT6B75U TN ABL messenger RNA (ABL mRNA) TT6B75U UP P00519 TT6B75U UC ABL1_HUMAN TT6B75U BC mRNA target TT6B75U SN p150 (mRNA); Proto-oncogene tyrosine-protein kinase ABL1 (mRNA); Proto-oncogene c-Abl (mRNA); JTK7 (mRNA); C-ABL (mRNA); Abl (mRNA); Abelson tyrosine-protein kinase 1 (mRNA); Abelson murine leukemia viral oncogene homolog 1 (mRNA) TT6B75U GN ABL1 TT6B75U FC Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717'. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E. coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H. pylori, or AnkA (ankyrin repeat-containing protein A) of A. phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner. Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity. Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. TT6B75U EC EC 2.7.10.2 TT6B75U PD 6NPV; 6NPU; 6NPE; 6BL8; 6AMW TT6B75U SQ MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR TT6B75U TT Discontinued TT6B75U FM mRNA target TT6B75U KE hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04110:Cell cycle; hsa04360:Axon guidance; hsa04722:Neurotrophin signaling pathway; hsa05130:Pathogenic Escherichia coli infection; hsa05131:Shigellosis; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05220:Chronic myeloid leukemia; hsa05416:Viral myocarditis TT6B75U RC R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-375170:CDO in myogenesis; R-HSA-5663213:RHO GTPases Activate WASPs and WAVEs; R-HSA-5685938:HDR through Single Strand Annealing (SSA); R-HSA-5693565:Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTDMBF5 ID TTDMBF5 TTDMBF5 TN Arachidonate 5-lipoxygenase activating protein (FLAP) TTDMBF5 UP P20292 TTDMBF5 UC AL5AP_HUMAN TTDMBF5 SN MK-886-binding protein; FLAP; ALOX5AP TTDMBF5 GN ALOX5AP TTDMBF5 FC Required for leukotrienebiosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes. TTDMBF5 PD 2Q7R; 2Q7M TTDMBF5 SQ MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTISTTISPLLLIP TTDMBF5 TT Discontinued TTD3XFU ID TTD3XFU TTD3XFU TN C-C chemokine receptor type 3 (CCR3) TTD3XFU UP P51677 TTD3XFU UC CCR3_HUMAN TTD3XFU BC GPCR rhodopsin TTD3XFU SN Eosinophil eotaxin receptor; Chemokine receptor CCR3; CMKBR3; CKR3; CD193; CCR-3; CC-CKR-3; C-C CKR-3 TTD3XFU GN CCR3 TTD3XFU FC Binds to eotaxin, eotaxin-3, MCP-3, MCP-4, RANTES and MIP-1 delta. Subsequently transduces a signal by increasing the intracellular calcium ions level. Alternative coreceptor with CD4 for HIV-1 infection. Receptor for a C-C type chemokine. TTD3XFU SQ MTTSLDTVETFGTTSYYDDVGLLCEKADTRALMAQFVPPLYSLVFTVGLLGNVVVVMILIKYRRLRIMTNIYLLNLAISDLLFLVTLPFWIHYVRGHNWVFGHGMCKLLSGFYHTGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGVITSIVTWGLAVLAALPEFIFYETEELFEETLCSALYPEDTVYSWRHFHTLRMTIFCLVLPLLVMAICYTGIIKTLLRCPSKKKYKAIRLIFVIMAVFFIFWTPYNVAILLSSYQSILFGNDCERSKHLDLVMLVTEVIAYSHCCMNPVIYAFVGERFRKYLRHFFHRHLLMHLGRYIPFLPSEKLERTSSVSPSTAEPELSIVF TTD3XFU TT Discontinued TTD3XFU KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa05203:Viral carcinogenesis TTD3XFU RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTE836A ID TTE836A TTE836A TN C-C chemokine receptor type 8 (CCR8) TTE836A UP P51685 TTE836A UC CCR8_HUMAN TTE836A BC GPCR rhodopsin TTE836A SN TER1; GPRCY6; GPR-CY6; Chemokine receptor-like 1; Chemokine receptor CCR8; CMKBRL2; CMKBR8; CKRL1; CKR-L1; CDw198; CCR-8; CC-chemokine receptor CHEMR1; CC-CKR-8; CC chemokine receptor CHEMR1; C-C CKR-8 TTE836A GN CCR8 TTE836A FC May regulate monocyte chemotaxis and thymic cell line apoptosis. Alternative coreceptor with CD4 for HIV-1 infection. Receptor for the chemokine CCL1/SCYA1/I-309. TTE836A SQ MDYTLDLSVTTVTDYYYPDIFSSPCDAELIQTNGKLLLAVFYCLLFVFSLLGNSLVILVLVVCKKLRSITDVYLLNLALSDLLFVFSFPFQTYYLLDQWVFGTVMCKVVSGFYYIGFYSSMFFITLMSVDRYLAVVHAVYALKVRTIRMGTTLCLAVWLTAIMATIPLLVFYQVASEDGVLQCYSFYNQQTLKWKIFTNFKMNILGLLIPFTIFMFCYIKILHQLKRCQNHNKTKAIRLVLIVVIASLLFWVPFNVVLFLTSLHSMHILDGCSISQQLTYATHVTEIISFTHCCVNPVIYAFVGEKFKKHLSEIFQKSCSQIFNYLGRQMPRESCEKSSSCQQHSSRSSSVDYIL TTE836A TT Discontinued TTE836A KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa05203:Viral carcinogenesis TTE836A RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TT3KBZY ID TT3KBZY TT3KBZY TN G-protein coupled receptor 54 (KISS1R) TT3KBZY UP Q969F8 TT3KBZY UC KISSR_HUMAN TT3KBZY BC GPCR rhodopsin TT3KBZY SN KiSS-1 receptor GPR54; KISS1R; GPR54 TT3KBZY GN KISS1R TT3KBZY FC Receptor for metastin(kisspeptin-54 or kp-54), a C- terminally amidated peptide of KiSS1. KiSS1 is a metastasis suppressor protein that suppresses metastases in malignant melanomas and in some breast carcinomas without affecting tumorigenicity. The metastasis suppressor properties may be mediated in part by cell cycle arrest and induction of apoptosis in malignant cells. The receptor is essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/KISS1R system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. The receptor is also probably involved in the regulation and fine- tuning of trophoblast invasion generated by the trophoblast itself. Analysis of the transduction pathways activated by the receptor identifies couplingto phospholipase C and intracellular calcium release through pertussis toxin-insensitive G(q) proteins. TT3KBZY SQ MHTVATSGPNASWGAPANASGCPGCGANASDGPVPSPRAVDAWLVPLFFAALMLLGLVGNSLVIYVICRHKPMRTVTNFYIANLAATDVTFLLCCVPFTALLYPLPGWVLGDFMCKFVNYIQQVSVQATCATLTAMSVDRWYVTVFPLRALHRRTPRLALAVSLSIWVGSAAVSAPVLALHRLSPGPRAYCSEAFPSRALERAFALYNLLALYLLPLLATCACYAAMLRHLGRVAVRPAPADSALQGQVLAERAGAVRAKVSRLVAAVVLLFAACWGPIQLFLVLQALGPAGSWHPRSYAAYALKTWAHCMSYSNSALNPLLYAFLGSHFRQAFRRVCPCAPRRPRRPRRPGPSDPAAPHAELLRLGSHPAPARAQKPGSSGLAARGLCVLGEDNAPL TT3KBZY TT Discontinued TT3KBZY KE hsa04080:Neuroactive ligand-receptor interaction TT3KBZY RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TTIJWR7 ID TTIJWR7 TTIJWR7 TN Integrin beta-2 (ITGB2) TTIJWR7 UP P05107 TTIJWR7 UC ITB2_HUMAN TTIJWR7 BC Integrin TTIJWR7 SN MFI7; Integrin alpha-M/beta-2; Complement receptor C3 subunit beta; Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta; CD18 TTIJWR7 GN ITGB2 TTIJWR7 FC Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural killer cell cytotoxicity. Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation. Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages. In association with alpha subunit ITGAM/CD11b, required for CD177-PRTN3-mediated activation of TNF primed neutrophils. Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. TTIJWR7 PD 5ZAZ; 5XR1; 5ES4; 5E6X; 5E6W TTIJWR7 SQ MLGLRPPLLALVGLLSLGCVLSQECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVQLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTINCERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEGCLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPGCPSPCGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTCKERDSEGCWVAYTLEQQDGMDRYLIYVDESRECVAGPNIAAIVGGTVAGIVLIGILLLVIWKALIHLSDLREYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES TTIJWR7 TT Clinical trial TTIJWR7 FM Integrin TTIJWR7 KE hsa04015:Rap1 signaling pathway; hsa04145:Phagosome; hsa04390:Hippo signaling pathway; hsa04514:Cell adhesion molecules (CAMs); hsa04650:Natural killer cell mediated cytotoxicity; hsa04670:Leukocyte transendothelial migration; hsa04810:Regulation of actin cytoskeleton; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05144:Malaria; hsa05146:Amoebiasis; hsa05150:Staphylococcus aureus infection; hsa05152:Tuberculosis; hsa05166:HTLV-I infection; hsa05323:Rheumatoid arthritis; hsa05416:Viral myocarditis TTIJWR7 RC R-HSA-166016:Toll Like Receptor 4 (TLR4) Cascade; R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-216083:Integrin cell surface interactions TT3UJ7Z ID TT3UJ7Z TT3UJ7Z TN MAPK-activated protein kinase 5 (MAPKAPK5) TT3UJ7Z UP Q8IW41 TT3UJ7Z UC MAPK5_HUMAN TT3UJ7Z BC Kinase TT3UJ7Z SN p38regulated/activated protein kinase; p38-regulated/activated protein kinase; PRAK; MK5; MK-5; MAPKactivated protein kinase 5; MAPKAPK-5; MAPKAP-K5; MAPKAP kinase 5; MAP kinaseactivated protein kinase 5; MAP kinase-activated protein kinase 5 TT3UJ7Z GN MAPKAPK5 TT3UJ7Z FC Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement. Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. TT3UJ7Z EC EC 2.7.11.1 TT3UJ7Z SQ MSEESDMDKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALRHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKIDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPILRKRKLLGTKPKDSVYIHDHENGAEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQEAWKYNRECKLLRDTLQSFSWNGRGFTDKVDRLKLAEIVKQVIEEQTTSHESQ TT3UJ7Z TT Discontinued TT3UJ7Z FM Kinase TT3UJ7Z RC R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-5687128:MAPK6/MAPK4 signaling TTJUXV6 ID TTJUXV6 TTJUXV6 TN Multidrug resistance protein 3 (ABCB4) TTJUXV6 UP P21439 TTJUXV6 UC MDR3_HUMAN TTJUXV6 BC Acid anhydrides hydrolase TTJUXV6 SN PGY3; P-gp; MDR3; ATP-binding cassette sub-family B member 4; ABCB4 TTJUXV6 GN ABCB4 TTJUXV6 FC Mediates ATP-dependent export of organic anions and drugs from the cytoplasm. Hydrolyzes ATP with low efficiency. Not capable of conferring drug resistance. Mediates the translocation of phosphatidylcholine across the canalicular membrane of the hepatocyte. TTJUXV6 EC EC 7.6.2.1 TTJUXV6 SQ MDLEAAKNGTAWRPTSAEGDFELGISSKQKRKKTKTVKMIGVLTLFRYSDWQDKLFMSLGTIMAIAHGSGLPLMMIVFGEMTDKFVDTAGNFSFPVNFSLSLLNPGKILEEEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQTSGSQIQSEEFELNDEKAATRMAPNGWKSRLFRHSTQKNLKNSQMCQKSLDVETDGLEANVPPVSFLKVLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDVILVFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFMLFERQPLIDSYSEEGLKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGFQLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGTQNL TTJUXV6 TT Clinical trial TTJUXV6 KE hsa02010:ABC transporters; hsa04976:Bile secretion TTJUXV6 RC R-HSA-1989781:PPARA activates gene expression; R-HSA-382556:ABC-family proteins mediated transport TTZHKV9 ID TTZHKV9 TTZHKV9 TN Neurotrophin-3 (NTF3) TTZHKV9 UP P20783 TTZHKV9 UC NTF3_HUMAN TTZHKV9 BC Growth factor TTZHKV9 SN Neurotrophic factor; Nerve growth factor 2; NT-3; NGF-2; HDNF TTZHKV9 GN NTF3 TTZHKV9 FC Seems to promote the survival of visceral and proprioceptive sensory neurons. TTZHKV9 PD 3BUK; 1NT3; 1BND; 1B8K TTZHKV9 SQ MSILFYVIFLAYLRGIQGNNMDQRSLPEDSLNSLIIKLIQADILKNKLSKQMVDVKENYQSTLPKAEAPREPERGGPAKSAFQPVIAMDTELLRQQRRYNSPRVLLSDSTPLEPPPLYLMEDYVGSPVVANRTSRRKRYAEHKSHRGEYSVCDSESLWVTDKSSAIDIRGHQVTVLGEIKTGNSPVKQYFYETRCKEARPVKNGCRGIDDKHWNSQCKTSQTYVRALTSENNKLVGWRWIRIDTSCVCALSRKIGRT TTZHKV9 TT Discontinued TTZHKV9 FM NGF-beta family TTZHKV9 KE hsa04010:MAPK signaling pathway; hsa04722:Neurotrophin signaling pathway TT1BC3A ID TT1BC3A TT1BC3A TN Phosphodiesterase 7A (PDE7A) TT1BC3A UP Q13946 TT1BC3A UC PDE7A_HUMAN TT1BC3A BC Phosphoric diester hydrolase TT1BC3A SN TM22; High affinity cAMPspecific 3',5'cyclic phosphodiesterase 7A; High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A TT1BC3A GN PDE7A TT1BC3A FC May have a role in muscle signal transduction. Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. TT1BC3A EC EC 3.1.4.53 TT1BC3A PD 4Y2B; 4PM0; 3G3N; 1ZKL TT1BC3A SQ MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPNPRQLSQRRGAISYDSSDQTALYIRMLGDVRVRSRAGFESERRGSHPYIDFRIFHSQSEIEVSVSARNIRRLLSFQRYLRSSRFFRGTAVSNSLNILDDDYNGQAKCMLEKVGNWNFDIFLFDRLTNGNSLVSLTFHLFSLHGLIEYFHLDMMKLRRFLVMIQEDYHSQNPYHNAVHAADVTQAMHCYLKEPKLANSVTPWDILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNTSVLENHHWRSAVGLLRESGLFSHLPLESRQQMETQIGALILATDISRQNEYLSLFRSHLDRGDLCLEDTRHRHLVLQMALKCADICNPCRTWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRHTESIANIQIGFMTYLVEPLFTEWARFSNTRLSQTMLGHVGLNKASWKGLQREQSSSEDTDAAFELNSQLLPQENRLS TT1BC3A TT Discontinued TT1BC3A KE hsa00230:Purine metabolism; hsa05032:Morphine addiction TT1BC3A RC R-HSA-418555:G alpha (s) signalling events TTWIEY9 ID TTWIEY9 TTWIEY9 TN Phosphodiesterase 7B (PDE7B) TTWIEY9 UP Q9NP56 TTWIEY9 UC PDE7B_HUMAN TTWIEY9 BC Phosphoric diester hydrolase TTWIEY9 SN cAMPspecific 3',5'cyclic phosphodiesterase 7B; cAMP-specific 3',5'-cyclic phosphodiesterase 7B TTWIEY9 GN PDE7B TTWIEY9 FC May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain. Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. TTWIEY9 EC EC 3.1.4.53 TTWIEY9 PD 1LXW TTWIEY9 SQ MSCLMVERCGEILFENPDQNAKCVCMLGDIRLRGQTGVRAERRGSYPFIDFRLLNSTTYSGEIGTKKKVKRLLSFQRYFHASRLLRGIIPQAPLHLLDEDYLGQARHMLSKVGMWDFDIFLFDRLTNGNSLVTLLCHLFNTHGLIHHFKLDMVTLHRFLVMVQEDYHSQNPYHNAVHAADVTQAMHCYLKEPKLASFLTPLDIMLGLLAAAAHDVDHPGVNQPFLIKTNHHLANLYQNMSVLENHHWRSTIGMLRESRLLAHLPKEMTQDIEQQLGSLILATDINRQNEFLTRLKAHLHNKDLRLEDAQDRHFMLQIALKCADICNPCRIWEMSKQWSERVCEEFYRQGELEQKFELEISPLCNQQKDSIPSIQIGFMSYIVEPLFREWAHFTGNSTLSENMLGHLAHNKAQWKSLLPRQHRSRGSSGSGPDHDHAGQGTESEEQEGDSP TTWIEY9 TT Discontinued TTWIEY9 KE hsa00230:Purine metabolism; hsa05032:Morphine addiction TTWIEY9 RC R-HSA-418555:G alpha (s) signalling events TTJ2TSA ID TTJ2TSA TTJ2TSA TN Prolactin (PRL) TTJ2TSA UP P01236 TTJ2TSA UC PRL_HUMAN TTJ2TSA BC Somatotropin/prolactin TTJ2TSA SN GHA1 TTJ2TSA GN PRL TTJ2TSA FC Prolactin acts primarily on the mammary gland by promoting lactation. TTJ2TSA PD 3NPZ; 3NCF; 3NCE; 3NCC; 3NCB TTJ2TSA SQ MNIKGSPWKGSLLLLLVSNLLLCQSVAPLPICPGGAARCQVTLRDLFDRAVVLSHYIHNLSSEMFSEFDKRYTHGRGFITKAINSCHTSSLATPEDKEQAQQMNQKDFLSLIVSILRSWNEPLYHLVTEVRGMQEAPEAILSKAVEIEEQTKRLLEGMELIVSQVHPETKENEIYPVWSGLPSLQMADEESRLSAYYNLLHCLRRDSHKIDNYLKLLKCRIIHNNNC TTJ2TSA TT Discontinued TTJ2TSA FM Hormone TTJ2TSA KE hsa04060:Cytokine-cytokine receptor interaction; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04917:Prolactin signaling pathway TTJ2TSA RC R-HSA-1170546:Prolactin receptor signaling; R-HSA-977225:Amyloid formation; R-HSA-982772:Growth hormone receptor signaling TTWP0NS ID TTWP0NS TTWP0NS TN RRM1 messenger RNA (RRM1 mRNA) TTWP0NS UP P23921 TTWP0NS UC RIR1_HUMAN TTWP0NS BC mRNA target TTWP0NS SN Ribonucleotide reductase large subunit (mRNA); Ribonucleoside-diphosphate reductase subunit M1 (mRNA); Ribonucleoside-diphosphate reductase large subunit (mRNA); RR1 (mRNA) TTWP0NS GN RRM1 TTWP0NS FC Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Provides the precursors necessary for DNA synthesis. TTWP0NS EC EC 1.17.4.1 TTWP0NS PD 6AUI; 5TUS; 5D1Y; 4X3V; 3HNF TTWP0NS SQ MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCSLENRDECLMCGS TTWP0NS TT Discontinued TTWP0NS FM mRNA target TTWP0NS KE hsa00230:Purine metabolism; hsa00240:Pyrimidine metabolism; hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways TTZSJIV ID TTZSJIV TTZSJIV TN Sphingomyelin phosphodiesterase 4 (SMPD4) TTZSJIV UP Q9NXE4 TTZSJIV UC NSMA3_HUMAN TTZSJIV BC Phosphoric diester hydrolase TTZSJIV SN nSMase3; nSMase-3; SKNY; Neutral sphingomyelinase III; Neutral sphingomyelinase 3; KIAA1418 TTZSJIV GN SMPD4 TTZSJIV FC Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. May sensitize cells to DNA damage-induced apoptosis. TTZSJIV EC EC 3.1.4.12 TTZSJIV SQ MTTFGAVAEWRLPSLRRATLWIPQWFAKKAIFNSPLEAAMAFPHLQQPSFLLASLKADSINKPFAQQCQDLVKVIEDFPAKELHTIFPWLVESIFGSLDGVLVGWNLRCLQGRVNPVEYSIVMEFLDPGGPMMKLVYKLQAEDYKFDFPVSYLPGPVKASIQECILPDSPLYHNKVQFTPTGGLGLNLALNPFEYYIFFFALSLITQKPLPVSLHVRTSDCAYFILVDRYLSWFLPTEGSVPPPLSSSPGGTSPSPPPRTPAIPFASYGLHHTSLLKRHISHQTSVNADPASHEIWRSETLLQVFVEMWLHHYSLEMYQKMQSPHAKLEVLHYRLSVSSALYSPAQPSLQALHAYQESFTPTEEHVLVVRLLLKHLHAFANSLKPEQASPSAHSHATSPLEEFKRAAVPRFVQQKLYLFLQHCFGHWPLDASFRAVLEMWLSYLQPWRYAPDKQAPGSDSQPRCVSEKWAPFVQENLLMYTKLFVGFLNRALRTDLVSPKHALMVFRVAKVFAQPNLAEMIQKGEQLFLEPELVIPHRQHRLFTAPTFTGSFLSPWPPAVTDASFKVKSHVYSLEGQDCKYTPMFGPEARTLVLRLAQLITQAKHTAKSISDQCAESPAGHSFLSWLGFSSMDTNGSYTANDLDEMGQDSVRKTDEYLEKALEYLRQIFRLSEAQLRQFTLALGTTQDENGKKQLPDCIVGEDGLILTPLGRYQIINGLRRFEIEYQGDPELQPIRSYEIASLVRTLFRLSSAINHRFAGQMAALCSRDDFLGSFCRYHLTEPGLASRHLLSPVGRRQVAGHTRGPRLSLRFLGSYRTLVSLLLAFFVASLFCVGPLPCTLLLTLGYVLYASAMTLLTERGKLHQP TTZSJIV TT Discontinued TTZSJIV KE hsa00600:Sphingolipid metabolism; hsa01100:Metabolic pathways TTZSJIV RC R-HSA-1660662:Glycosphingolipid metabolism TTFNDGV ID TTFNDGV TTFNDGV TN Transforming protein RhoA (RHOA) TTFNDGV UP P61586 TTFNDGV UC RHOA_HUMAN TTFNDGV BC Small GTPase TTFNDGV SN h12; Rho cDNA clone 12; RHO12; ARHA; ARH12 TTFNDGV GN RHOA TTFNDGV FC Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. TTFNDGV EC EC 3.6.5.2 TTFNDGV PD 6R3V; 6BCB; 6BCA; 6BC0; 5ZHX TTFNDGV SQ MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKKSGCLVL TTFNDGV TT Discontinued TTFNDGV FM Small GTPase superfamily TTFNDGV KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04144:Endocytosis; hsa04270:Vascular smooth muscle contraction; hsa04310:Wnt signaling pathway; hsa04350:TGF-beta signaling pathway; hsa04360:Axon guidance; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04530:Tight junction; hsa04611:Platelet activation; hsa04660:T cell receptor signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa04921:Oxytocin signaling pathway; hsa04972:Pancreatic secretion; hsa05100:Bacterial invasion of epithelial cells; hsa05130:Pathogenic Escherichia coli infection; hsa05133:Pertussis; hsa05152:Tuberculosis; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer TTFNDGV RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-193634:Axonal growth inhibition (RHOA activation); R-HSA-194840:Rho GTPase cycle; R-HSA-198203:PI3K/AKT activation; R-HSA-209563:Axonal growth stimulation; R-HSA-2173791:TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition); R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-4086400:PCP/CE pathway; R-HSA-416482:G alpha (12/13) signalling events; R-HSA-416550:Sema4D mediated inhibition of cell attachment and migration; R-HSA-416572:Sema4D induced cell migration and growth-cone collapse; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5625740:RHO GTPases activate PKNs; R-HSA-5625900:RHO GTPases activate CIT; R-HSA-5627117:RHO GTPases Activate ROCKs; R-HSA-5663220:RHO GTPases Activate Formins TTQ7R2V ID TTQ7R2V TTQ7R2V TN Tripeptidyl-peptidase II (TPP2) TTQ7R2V UP P29144 TTQ7R2V UC TPP2_HUMAN TTQ7R2V BC Peptidase TTQ7R2V SN Tripeptidyl aminopeptidase; TPP2; TPP-II; TPP II; CCK-inactivating peptidase tripeptidyl peptidase TTQ7R2V GN TPP2 TTQ7R2V FC Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis. TTQ7R2V EC EC 3.4.14.10 TTQ7R2V SQ MATAATEEPFPFHGLLPKKETGAASFLCRYPEYDGRGVLIAVLDTGVDPGAPGMQVTTDGKPKIVDIIDTTGSGDVNTATEVEPKDGEIVGLSGRVLKIPASWTNPSGKYHIGIKNGYDFYPKALKERIQKERKEKIWDPVHRVALAEACRKQEEFDVANNGSSQANKLIKEELQSQVELLNSFEKKYSDPGPVYDCLVWHDGEVWRACIDSNEDGDLSKSTVLRNYKEAQEYGSFGTAEMLNYSVNIYDDGNLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSYGEATHWPNSGRICEVINEAVWKHNIIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMVAEYSLREKLPANQYTWSSRGPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALILSGLKANNIDYTVHSVRRALENTAVKADNIEVFAQGHGIIQVDKAYDYLVQNTSFANKLGFTVTVGNNRGIYLRDPVQVAAPSDHGVGIEPVFPENTENSEKISLQLHLALTSNSSWVQCPSHLELMNQCRHINIRVDPRGLREGLHYTEVCGYDIASPNAGPLFRVPITAVIAAKVNESSHYDLAFTDVHFKPGQIRRHFIEVPEGATWAEVTVCSCSSEVSAKFVLHAVQLVKQRAYRSHEFYKFCSLPEKGTLTEAFPVLGGKAIEFCIARWWASLSDVNIDYTISFHGIVCTAPQLNIHASEGINRFDVQSSLKYEDLAPCITLKNWVQTLRPVSAKTKPLGSRDVLPNNRQLYEMVLTYNFHQPKSGEVTPSCPLLCELLYESEFDSQLWIIFDQNKRQMGSGDAYPHQYSLKLEKGDYTIRLQIRHEQISDLERLKDLPFIVSHRLSNTLSLDIHENHSFALLGKKKSSNLTLPPKYNQPFFVTSLPDDKIPKGAGPGCYLAGSLTLSKTELGKKADVIPVHYYLIPPPTKTKNGSKDKEKDSEKEKDLKEEFTEALRDLKIQWMTKLDSSDIYNELKETYPNYLPLYVARLHQLDAEKERMKRLNEIVDAANAVISHIDQTALAVYIAMKTDPRPDAATIKNDMDKQKSTLVDALCRKGCALADHLLHTQAQDGAISTDAEGKEEEGESPLDSLAETFWETTKWTDLFDNKVLTFAYKHALVNKMYGRGLKFATKLVEEKPTKENWKNCIQLMKLLGWTHCASFTENWLPIMYPPDYCVF TTQ7R2V TT Discontinued TTQ7R2V RC R-HSA-983168:Antigen processing: Ubiquitination & Proteasome degradation TTPFN62 ID TTPFN62 TTPFN62 TN VEGFR2 messenger RNA (VEGFR2 mRNA) TTPFN62 UP P35968 TTPFN62 UC VGFR2_HUMAN TTPFN62 BC mRNA target TTPFN62 SN VEGFR2 (mRNA); VEGFR-2 (mRNA); VEGF-2 receptor (mRNA); Protein-tyrosine kinase receptor flk-1 (mRNA); Kinase insert domain receptor (mRNA); Fetal liver kinase 1 (mRNA); FLK1 (mRNA); FLK-1 (mRNA); CD309 (mRNA) TTPFN62 GN KDR TTPFN62 FC Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC. Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. TTPFN62 EC EC 2.7.10.1 TTPFN62 PD 6GQQ; 6GQP; 6GQO; 5OYJ; 5EW3 TTPFN62 SQ MQSKVLLAVALWLCVETRAASVGLPSVSLDLPRLSIQKDILTIKANTTLQITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGAYKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRSDQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRIPAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVILTNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAIPPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVNKNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRGPEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPTPVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTKKRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIIEGAQEKTNLEIIILVGTAVIAMFFWLLLVIILRTVKRANGGELKTGYLSIVMDPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYKTKGARFRQGKDYVGAIPVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEAPEDLYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQDGKDYIVLPISETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISQYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDDNQTDSGMVLASEELKTLEDRTKLSPSFGGMVPSKSRESVASEGSNQTSGYQSGYHSDDTDTTVYSSEEAELLKLIEIGVQTGSTAQILQPDSGTTLSSPPV TTPFN62 TT Discontinued TTPFN62 FM mRNA target TTC8M31 ID TTC8M31 TTC8M31 TN Carnitine acyltransferase (CRAT) TTC8M31 UP P43155 TTC8M31 UC CACP_HUMAN TTC8M31 BC Acyltransferase TTC8M31 SN Carnitine acetylase; Carnitine O-acetyltransferase; CRAT TTC8M31 GN CRAT TTC8M31 FC Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Plays an important role in triglyceride metabolism. TTC8M31 EC EC 2.3.1.7 TTC8M31 PD 1S5O; 1NM8 TTC8M31 SQ MLAFAARTVVKPLGFLKPFSLMKASSRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSEEEWAHTKQLVDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQYRQPVVIYSSPGVMLPKQDFVDLQGQLRFAAKLIEGVLDFKVMIDNETLPVEYLGGKPLCMNQYYQILSSCRVPGPKQDTVSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQIFVQLEKIWNSSLQTNKEPVGILTSNHRNSWAKAYNTLIKDKVNRDSVRSIQKSIFTVCLDATMPRVSEDVYRSHVAGQMLHGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGPPIVTLLDYVIEYTKKPELVRSPLVPLPMPKKLRFNITPEIKSDIEKAKQNLSIMIQDLDITVMVFHHFGKDFPKSEKLSPDAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASMDSLTFVKAMDDSSVTEHQKVELLRKAVQAHRGYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMDTSYAIAMHFHLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSLSAYNSCAETNAARLAHYLEKALLDMRALLQSHPRAKL TTC8M31 TT Discontinued TTS92NQ ID TTS92NQ TTS92NQ TN Cytomegalovirus DNA polymerase messenger RNA (CMV DNA polymerase mRNA) TTS92NQ UP P08546 TTS92NQ UC DPOL_HCMVA TTS92NQ BC mRNA target TTS92NQ SN UL54 (mRNA); HFLF2 (mRNA); DNA polymerase catalytic subunit (mRNA) TTS92NQ GN CMV DNA polymerase mRNA TTS92NQ FC The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein. Replicates viral genomic DNA in the late phase of lytic infection, producing long concatemeric DNA. TTS92NQ EC EC 2.7.7.7 TTS92NQ PD 1YYP TTS92NQ SQ MFFNPYLSGGVTGGAVAGGRRQRSQPGSAQGSGKRPPQKQFLQIVPRGVMFDGQTGLIKHKTGRLPLMFYREIKHLLSHDMVWPCPWRETLVGRVVGPIRFHTYDQTDAVLFFDSPENVSPRYRQHLVPSGNVLRFFGATEHGYSICVNVFGQRSYFYCEYSDTDRLREVIASVGELVPEPRTPYAVSVTPATKTSIYGYGTRPVPDLQCVSISNWTMARKIGEYLLEQGFPVYEVRVDPLTRLVIDRRITTFGWCSVNRYDWRQQGRASTCDIEVDCDVSDLVAVPDDSSWPRYRCLSFDIECMSGEGGFPCAEKSDDIVIQISCVCYETGGNTAVDQGIPNGNDGRGCTSEGVIFGHSGLHLFTIGTCGQVGPDVDVYEFPSEYELLLGFMLFFQRYAPAFVTGYNINSFDLKYILTRLEYLYKVDSQRFCKLPTAQGGRFFLHSPAVGFKRQYAAAFPSASHNNPASTAATKVYIAGSVVIDMYPVCMAKTNSPNYKLNTMAELYLRQRKDDLSYKDIPRCFVANAEGRAQVGRYCLQDAVLVRDLFNTINFHYEAGAIARLAKIPLRRVIFDGQQIRIYTSLLDECACRDFILPNHYSKGTTVPETNSVAVSPNAAIISTAAVPGDAGSVAAMFQMSPPLQSAPSSQDGVSPGSGSNSSSSVGVFSVGSGSSGGVGVSNDNHGAGGTAAVSYQGATVFEPEVGYYNDPVAVFDFASLYPSIIMAHNLCYSTLLVPGGEYPVDPADVYSVTLENGVTHRFVRASVRVSVLSELLNKWVSQRRAVRECMRECQDPVRRMLLDKEQMALKVTCNAFYGFTGVVNGMMPCLPIAASITRIGRDMLERTARFIKDNFSEPCFLHNFFNQEDYVVGTREGDSEESSALPEGLETSSGGSNERRVEARVIYGDTDSVFVRFRGLTPQALVARGPSLAHYVTACLFVEPVKLEFEKVFVSLMMICKKRYIGKVEGASGLSMKGVDLVRKTACEFVKGVTRDVLSLLFEDREVSEAAVRLSRLSLDEVKKYGVPRGFWRILRRLVQARDDLYLHRVRVEDLVLSSVLSKDISLYRQSNLPHIAVIKRLAARSEELPSVGDRVFYVLTAPGVRTAPQGSSDNGDSVTAGVVSRSDAIDGTDDDADGGGVEESNRRGGEPAKKRARKPPSAVCNYEVAEDPSYVREHGVPIHADKYFEQVLKAVTNVLSPVFPGGETARKDKFLHMVLPRRLHLEPAFLPYSVKAHECC TTS92NQ TT Discontinued TTS92NQ FM mRNA target TTGPJ0U ID TTGPJ0U TTGPJ0U TN DNA polymerase alpha catalytic p180 (POLA1) TTGPJ0U UP P09884 TTGPJ0U UC DPOLA_HUMAN TTGPJ0U BC Kinase TTGPJ0U SN POLA; DNA polymerase alpha catalytic subunit p180; DNA polymerase alpha catalytic subunit TTGPJ0U GN POLA1 TTGPJ0U FC During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes. In the cytosol, responsible for a substantial proportion of the physiological concentration of cytosolic RNA:DNA hybrids, which are necessary to prevent spontaneous activation of type I interferon responses. Plays an essential role in the initiation of DNA replication. TTGPJ0U EC EC 2.7.7.7 TTGPJ0U PD 6AS7; 5IUD; 5EXR; 4Y97; 4QCL TTGPJ0U SQ MAPVHGDDSLSDSGSFVSSRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDFTGVYEEVDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDADEKGKDGKARNKDKRNVKKLAVTKPNNIKSMFIACAGKKTADKAVDLSKDGLLGDILQDLNTETPQITPPPVMILKKKRSIGASPNPFSVHTATAVPSGKIASPVSRKEPPLTPVPLKRAEFAGDDVQVESTEEEQESGAMEFEDGDFDEPMEVEEVDLEPMAAKAWDKESEPAEEVKQEADSGKGTVSYLGSFLPDVSCWDIDQEGDSSFSVQEVQVDSSHLPLVKGADEEQVFHFYWLDAYEDQYNQPGVVFLFGKVWIESAETHVSCCVMVKNIERTLYFLPREMKIDLNTGKETGTPISMKDVYEEFDEKIATKYKIMKFKSKPVEKNYAFEIPDVPEKSEYLEVKYSAEMPQLPQDLKGETFSHVFGTNTSSLELFLMNRKIKGPCWLEVKSPQLLNQPVSWCKVEAMALKPDLVNVIKDVSPPPLVVMAFSMKTMQNAKNHQNEIIAMAALVHHSFALDKAAPKPPFQSHFCVVSKPKDCIFPYAFKEVIEKKNVKVEVAATERTLLGFFLAKVHKIDPDIIVGHNIYGFELEVLLQRINVCKAPHWSKIGRLKRSNMPKLGGRSGFGERNATCGRMICDVEISAKELIRCKSYHLSELVQQILKTERVVIPMENIQNMYSESSQLLYLLEHTWKDAKFILQIMCELNVLPLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQKLGDEDEEIDGDTNKYKKGRKKAAYAGGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNICFTTVQRVASEAQKVTEDGEQEQIPELPDPSLEMGILPREIRKLVERRKQVKQLMKQQDLNPDLILQYDIRQKALKLTANSMYGCLGFSYSRFYAKPLAALVTYKGREILMHTKEMVQKMNLEVIYGDTDSIMINTNSTNLEEVFKLGNKVKSEVNKLYKLLEIDIDGVFKSLLLLKKKKYAALVVEPTSDGNYVTKQELKGLDIVRRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKRLIEIGENVLNGSVPVSQFEINKALTKDPQDYPDKKSLPHVHVALWINSQGGRKVKAGDTVSYVICQDGSNLTASQRAYAPEQLQKQDNLTIDTQYYLAQQIHPVVARICEPIDGIDAVLIATWLGLDPTQFRVHHYHKDEENDALLGGPAQLTDEEKYRDCERFKCPCPTCGTENIYDNVFDGSGTDMEPSLYRCSNIDCKASPLTFTVQLSNKLIMDIRRFIKKYYDGWLICEEPTCRNRTRHLPLQFSRTGPLCPACMKATLQPEYSDKSLYTQLCFYRYIFDAECALEKLTTDHEKDKLKKQFFTPKVLQDYRKLKNTAEQFLSRSGYSEVNLSKLFAGCAVKS TTGPJ0U TT Discontinued TTNPEFX ID TTNPEFX TTNPEFX TN Fibroblast growth factor-10 (FGF10) TTNPEFX UP O15520 TTNPEFX UC FGF10_HUMAN TTNPEFX BC Growth factor TTNPEFX SN Fibroblast growth factor 10; FGF10 TTNPEFX GN FGF10 TTNPEFX FC Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. May play a role in wound healing. TTNPEFX PD 1NUN TTNPEFX SQ MWKWILTHCASAFPHLPGCCCCCFLLLFLVSSVPVTCQALGQDMVSPEATNSSSSSFSSPSSAGRHVRSYNHLQGDVRWRKLFSFTKYFLKIEKNGKVSGTKKENCPYSILEITSVEIGVVAVKAINSNYYLAMNKKGKLYGSKEFNNDCKLKERIEENGYNTYASFNWQHNGRQMYVALNGKGAPRRGQKTRRKNTSAHFLPMVVHS TTNPEFX TT Discontinued TTNPEFX KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa05200:Pathways in cancer; hsa05218:Melanoma TTNPEFX RC R-HSA-109704:PI3K Cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-190377:FGFR2b ligand binding and activation; R-HSA-2033519:Activated point mutants of FGFR2; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5654219:Phospholipase C-mediated cascade: FGFR1; R-HSA-5654221:Phospholipase C-mediated cascade; R-HSA-5654688:SHC-mediated cascade:FGFR1; R-HSA-5654689:PI-3K cascade:FGFR1; R-HSA-5654693:FRS-mediated FGFR1 signaling; R-HSA-5654695:PI-3K cascade:FGFR2; R-HSA-5654699:SHC-mediated cascade:FGFR2; R-HSA-5654700:FRS-mediated FGFR2 signaling; R-HSA-5654726:Negative regulation of FGFR1 signaling; R-HSA-5654727:Negative regulation of FGFR2 signaling; R-HSA-5673001:RAF/MAP kinase cascade TT34DCN ID TT34DCN TT34DCN TN Golgi alpha-mannosidase II (MAN2A1) TT34DCN UP Q16706 TT34DCN UC MA2A1_HUMAN TT34DCN BC Glycosylase TT34DCN SN Mannosyloligosaccharide 1,31,6alphamannosidase; Mannosidase alpha class 2A member 1; Man II; MAN2A1; Alphamannosidase 2; AMan II TT34DCN GN MAN2A1 TT34DCN FC Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway. TT34DCN EC EC 3.2.1.114 TT34DCN SQ MKLSRQFTVFGSAIFCVVIFSLYLMLDRGHLDYPRNPRREGSFPQGQLSMLQEKIDHLERLLAENNEIISNIRDSVINLSESVEDGPKSSQSNFSQGAGSHLLPSQLSLSVDTADCLFASQSGSHNSDVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRDKGQSMFPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAHKYKINKFLSSSLYTALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKIIGNSAFLLILKDKLTYDSYSPDTFLEMDLKQKSQDSLPQKNIIRLSAEPRYLVVYNPLEQDRISLVSVYVSSPTVQVFSASGKPVEVQVSAVWDTANTISETAYEISFRAHIPPLGLKVYKILESASSNSHLADYVLYKNKVEDSGIFTIKNMINTEEGITLENSFVLLRFDQTGLMKQMMTKEDGKHHEVNVQFSWYGTTIKRDKSGAYLFLPDGNAKPYVYTTPPFVRVTHGRIYSEVTCFFDHVTHRVRLYHIQGIEGQSVEVSNIVDIRKVYNREIAMKISSDIKSQNRFYTDLNGYQIQPRMTLSKLPLQANVYPMTTMAYIQDAKHRLTLLSAQSLGVSSLNSGQIEVIMDRRLMQDDNRGLEQGIQDNKITANLFRILLEKRSAVNTEEEKKSVSYPSLLSHITSSLMNHPVIPMANKFSSPTLELQGEFSPLQSSLPCDIHLVNLRTIQSKVGNGHSNEAALILHRKGFDCRFSSKGTGLFCSTTQGKILVQKLLNKFIVESLTPSSLSLMHSPPGTQNISEINLSPMEISTFRIQLR TT34DCN TT Discontinued TT34DCN KE hsa00510:N-Glycan biosynthesis; hsa01100:Metabolic pathways TT20AHC ID TT20AHC TT20AHC TN Hepatitis C virus NS3 helicase messenger RNA (HCV NS3 mRNA) TT20AHC UP P26664 (1027-1657) TT20AHC UC POLG_HCV1 TT20AHC SN HCV Hepacivirin mRNA; HCV NS3P mRNA; HCV p70 Mrna TT20AHC GN HCV NS3 mRNA TT20AHC FC Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). TT20AHC EC EC 3.4.21.98 TT20AHC PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TT20AHC SQ APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVVT TT20AHC TT Discontinued TT28ZON ID TT28ZON TT28ZON TN H-ras messenger RNA (HRAS mRNA) TT28ZON UP P01112 TT28ZON UC RASH_HUMAN TT28ZON BC mRNA target TT28ZON SN p21ras (mRNA); cHras (mRNA); c-H-ras (mRNA); Transforming protein p21 (mRNA); HaRas (mRNA); Ha-Ras (mRNA); H-Ras-1 (mRNA); GTPase HRas, Nterminally processed (mRNA); GTPase HRas (mRNA) TT28ZON GN HRAS TT28ZON FC Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Involved in the activation of Ras protein signal transduction. TT28ZON PD 821P; 721P; 6Q21; 6D5W; 6D5V TT28ZON SQ MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS TT28ZON TT Discontinued TT28ZON FM mRNA target TT28ZON KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04062:Chemokine signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04360:Axon guidance; hsa04370:VEGF signaling pathway; hsa04510:Focal adhesion; hsa04530:Tight junction; hsa04540:Gap junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05034:Alcoholism; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TT28ZON RC R-HSA-112412:SOS-mediated signalling; R-HSA-1169092:Activation of RAS in B cells; R-HSA-1236382:Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1250196:SHC1 events in ERBB2 signaling; R-HSA-1250347:SHC1 events in ERBB4 signaling; R-HSA-171007:p38MAPK events; R-HSA-179812:GRB2 events in EGFR signaling; R-HSA-180336:SHC1 events in EGFR signaling; R-HSA-1963640:GRB2 events in ERBB2 signaling; R-HSA-210993:Tie2 Signaling; R-HSA-2179392:EGFR Transactivation by Gastrin; R-HSA-2424491:DAP12 signaling; R-HSA-2428933:SHC-related events triggered by IGF1R; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-375165:NCAM signaling for neurite out-growth; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-442982:Ras activation uopn Ca2+ infux through NMDA receptor; R-HSA-5218921:VEGFR2 mediated cell proliferation; R-HSA-5621575:CD209 (DC-SIGN) signaling; R-HSA-5637810:Constitutive Signaling by EGFRvIII; R-HSA-5654688:SHC-mediated cascade:FGFR1; R-HSA-5654693:FRS-mediated FGFR1 signaling; R-HSA-5654699:SHC-mediated cascade:FGFR2; R-HSA-5654700:FRS-mediated FGFR2 signaling; R-HSA-5654704:SHC-mediated cascade:FGFR3; R-HSA-5654706:FRS-mediated FGFR3 signaling; R-HSA-5654712:FRS-mediated FGFR4 signaling; R-HSA-5654719:SHC-mediated cascade:FGFR4; R-HSA-5658442:Regulation of RAS by GAPs; R-HSA-5673000:RAF activation; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5675221:Negative regulation of MAPK pathway; R-HSA-74751:Insulin receptor signalling cascade TTK025N ID TTK025N TTK025N TN Human papillomavirus E1 region messenger RNA (HPV E1 mRNA) TTK025N UP P04014 TTK025N UC VE1_HPV11 TTK025N BC mRNA target TTK025N SN Replication protein E1 (mRNA); E1 (mRNA); ATP-dependent helicase E1 (mRNA) TTK025N GN HPV E1 mRNA TTK025N FC It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication. ATP-dependent DNA helicase required for initiation of viral DNA replication. TTK025N EC EC 3.6.4.12 TTK025N SQ MADDSGTENEGSGCTGWFMVEAIVEHTTGTQISEDEEEEVEDSGYDMVDFIDDRHITQNSVEAQALFNRQEADAHYATVQDLKRKYLGSPYVSPISNVANAVESEISPRLDAIKLTTQPKKVKRRLFETRELTDSGYGYSEVEAATQVEKHGDPENGGDGQERDTGRDIEGEGVEHREAEAVDDSTREHADTSGILELLKCKDIRSTLHGKFKDCFGLSFVDLIRPFKSDRTTCADWVVAGFGIHHSIADAFQKLIEPLSLYAHIQWLTNAWGMVLLVLIRFKVNKSRCTVARTLGTLLNIPENHMLIEPPKIQSGVRALYWFRTGISNASTVIGEAPEWITRQTVIEHSLADSQFKLTEMVQWAYDNDICEESEIAFEYAQRGDFDSNARAFLNSNMQAKYVKDCAIMCRHYKHAEMKKMSIKQWIKYRGTKVDSVGNWKPIVQFLRHQNIEFIPFLSKLKLWLHGTPKKNCIAIVGPPDTGKSCFCMSLIKFLGGTVISYVNSCSHFWLQPLTDAKVALLDDATQPCWTYMDTYMRNLLDGNPMSIDRKHRALTLIKCPPLLVTSNIDISKEEKYKYLHSRVTTFTFPNPFPFDRNGNAVYELSDANWKCFFERLSSSLDIEDSEDEEDGSNSQAFRCVPGSVVRTL TTK025N TT Discontinued TTK025N FM mRNA target TTPRDH7 ID TTPRDH7 TTPRDH7 TN Integrin alpha-V/beta-5 (ITGAV/B5) TTPRDH7 UP P06756-P18084 TTPRDH7 UC ITAV_HUMAN-ITB5_HUMAN TTPRDH7 BC Integrin TTPRDH7 SN Integrin; Vitronectin receptor TTPRDH7 GN ITGAV-ITGB5 TTPRDH7 FC Binds to matrix macromolecules and proteinases and thereby stimulates angiogenesis. However, it inhibits angiogenesis. TTPRDH7 SQ MPRAPAPLYACLLGLCALLPRLAGLNICTSGSATSCEECLLIHPKCAWCSKEDFGSPRSITSRCDLRANLVKNGCGGEIESPASSFHVLRSLPLSSKGSGSAGWDVIQMTPQEIAVNLRPGDKTTFQLQVRQVEDYPVDLYYLMDLSLSMKDDLDNIRSLGTKLAEEMRKLTSNFRLGFGSFVDKDISPFSYTAPRYQTNPCIGYKLFPNCVPSFGFRHLLPLTDRVDSFNEEVRKQRVSRNRDAPEGGFDAVLQAAVCKEKIGWRKDALHLLVFTTDDVPHIALDGKLGGLVQPHDGQCHLNEANEYTASNQMDYPSLALLGEKLAENNINLIFAVTKNHYMLYKNFTALIPGTTVEILDGDSKNIIQLIINAYNSIRSKVELSVWDQPEDLNLFFTATCQDGVSYPGQRKCEGLKIGDTASFEVSLEARSCPSRHTEHVFALRPVGFRDSLEVGVTYNCTCGCSVGLEPNSARCNGSGTYVCGLCECSPGYLGTRCECQDGENQSVYQNLCREAEGKPLCSGRGDCSCNQCSCFESEFGKIYGPFCECDNFSCARNKGVLCSGHGECHCGECKCHAGYIGDNCNCSTDISTCRGRDGQICSERGHCLCGQCQCTEPGAFGEMCEKCPTCPDACSTKRDCVECLLLHSGKPDNQTCHSLCRDEVITWVDTIVKDDQEAVLCFYKTAKDCVMMFTYVELPSGKSNLTVLREPECGNTPNAMTILLAVVGSILLVGLALLAIWKLLVTIHDRREFAKFQSERSRARYEMASNPLYRKPISTHTVDFTFNKFNKSYNGTVDMAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET TTPRDH7 TT Discontinued TTPRDH7 FM Integrin TTPRDH7 RC R-HSA-1236973:Cross-presentation of particulate exogenous antigens (phagosomes); R-HSA-1566948:Elastic fibre formation; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000157:Laminin interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-445355:Smooth Muscle Contraction TT5UM29 ID TT5UM29 TT5UM29 TN Perlecan (HSPG) TT5UM29 UP P98160 TT5UM29 UC PGBM_HUMAN TT5UM29 SN LG3 peptide; Basement membranespecific heparan sulfate proteoglycan coreprotein; Basement membrane-specific heparan sulfate proteoglycan core protein TT5UM29 GN HSPG2 TT5UM29 FC Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development. Integral component of basement membranes. TT5UM29 PD 3SH5; 3SH4 TT5UM29 SQ MGWRAAGALLLALLLHGRLLAVTHGLRAYDGLSLPEDIETVTASQMRWTHSYLSDDEDMLADSISGDDLGSGDLGSGDFQMVYFRALVNFTRSIEYSPQLEDAGSREFREVSEAVVDTLESEYLKIPGDQVVSVVFIKELDGWVFVELDVGSEGNADGAQIQEMLLRVISSGSVASYVTSPQGFQFRRLGTVPQFPRACTEAEFACHSYNECVALEYRCDRRPDCRDMSDELNCEEPVLGISPTFSLLVETTSLPPRPETTIMRQPPVTHAPQPLLPGSVRPLPCGPQEAACRNGHCIPRDYLCDGQEDCEDGSDELDCGPPPPCEPNEFPCGNGHCALKLWRCDGDFDCEDRTDEANCPTKRPEEVCGPTQFRCVSTNMCIPASFHCDEESDCPDRSDEFGCMPPQVVTPPRESIQASRGQTVTFTCVAIGVPTPIINWRLNWGHIPSHPRVTVTSEGGRGTLIIRDVKESDQGAYTCEAMNARGMVFGIPDGVLELVPQRGPCPDGHFYLEHSAACLPCFCFGITSVCQSTRRFRDQIRLRFDQPDDFKGVNVTMPAQPGTPPLSSTQLQIDPSLHEFQLVDLSRRFLVHDSFWALPEQFLGNKVDSYGGSLRYNVRYELARGMLEPVQRPDVVLMGAGYRLLSRGHTPTQPGALNQRQVQFSEEHWVHESGRPVQRAELLQVLQSLEAVLIQTVYNTKMASVGLSDIAMDTTVTHATSHGRAHSVEECRCPIGYSGLSCESCDAHFTRVPGGPYLGTCSGCNCNGHASSCDPVYGHCLNCQHNTEGPQCNKCKAGFFGDAMKATATSCRPCPCPYIDASRRFSDTCFLDTDGQATCDACAPGYTGRRCESCAPGYEGNPIQPGGKCRPVNQEIVRCDERGSMGTSGEACRCKNNVVGRLCNECADGSFHLSTRNPDGCLKCFCMGVSRHCTSSSWSRAQLHGASEEPGHFSLTNAASTHTTNEGIFSPTPGELGFSSFHRLLSGPYFWSLPSRFLGDKVTSYGGELRFTVTQRSQPGSTPLHGQPLVVLQGNNIILEHHVAQEPSPGQPSTFIVPFREQAWQRPDGQPATREHLLMALAGIDTLLIRASYAQQPAESRVSGISMDVAVPEETGQDPALEVEQCSCPPGYRGPSCQDCDTGYTRTPSGLYLGTCERCSCHGHSEACEPETGACQGCQHHTEGPRCEQCQPGYYGDAQRGTPQDCQLCPCYGDPAAGQAAHTCFLDTDGHPTCDACSPGHSGRHCERCAPGYYGNPSQGQPCQRDSQVPGPIGCNCDPQGSVSSQCDAAGQCQCKAQVEGLTCSHCRPHHFHLSASNPDGCLPCFCMGITQQCASSAYTRHLISTHFAPGDFQGFALVNPQRNSRLTGEFTVEPVPEGAQLSFGNFAQLGHESFYWQLPETYQGDKVAAYGGKLRYTLSYTAGPQGSPLSDPDVQITGNNIMLVASQPALQGPERRSYEIMFREEFWRRPDGQPATREHLLMALADLDELLIRATFSSVPLAASISAVSLEVAQPGPSNRPRALEVEECRCPPGYIGLSCQDCAPGYTRTGSGLYLGHCELCECNGHSDLCHPETGACSQCQHNAAGEFCELCAPGYYGDATAGTPEDCQPCACPLTNPENMFSRTCESLGAGGYRCTACEPGYTGQYCEQCGPGYVGNPSVQGGQCLPETNQAPLVVEVHPARSIVPQGGSHSLRCQVSGSPPHYFYWSREDGRPVPSGTQQRHQGSELHFPSVQPSDAGVYICTCRNLHQSNTSRAELLVTEAPSKPITVTVEEQRSQSVRPGADVTFICTAKSKSPAYTLVWTRLHNGKLPTRAMDFNGILTIRNVQLSDAGTYVCTGSNMFAMDQGTATLHVQASGTLSAPVVSIHPPQLTVQPGQLAEFRCSATGSPTPTLEWTGGPGGQLPAKAQIHGGILRLPAVEPTDQAQYLCRAHSSAGQQVARAVLHVHGGGGPRVQVSPERTQVHAGRTVRLYCRAAGVPSATITWRKEGGSLPPQARSERTDIATLLIPAITTADAGFYLCVATSPAGTAQARIQVVVLSASDASPPPVKIESSSPSVTEGQTLDLNCVVAGSAHAQVTWYRRGGSLPPHTQVHGSRLRLPQVSPADSGEYVCRVENGSGPKEASITVSVLHGTHSGPSYTPVPGSTRPIRIEPSSSHVAEGQTLDLNCVVPGQAHAQVTWHKRGGSLPARHQTHGSLLRLHQVTPADSGEYVCHVVGTSGPLEASVLVTIEASVIPGPIPPVRIESSSSTVAEGQTLDLSCVVAGQAHAQVTWYKRGGSLPARHQVRGSRLYIFQASPADAGQYVCRASNGMEASITVTVTGTQGANLAYPAGSTQPIRIEPSSSQVAEGQTLDLNCVVPGQSHAQVTWHKRGGSLPVRHQTHGSLLRLYQASPADSGEYVCRVLGSSVPLEASVLVTIEPAGSVPALGVTPTVRIESSSSQVAEGQTLDLNCLVAGQAHAQVTWHKRGGSLPARHQVHGSRLRLLQVTPADSGEYVCRVVGSSGTQEASVLVTIQQRLSGSHSQGVAYPVRIESSSASLANGHTLDLNCLVASQAPHTITWYKRGGSLPSRHQIVGSRLRIPQVTPADSGEYVCHVSNGAGSRETSLIVTIQGSGSSHVPSVSPPIRIESSSPTVVEGQTLDLNCVVARQPQAIITWYKRGGSLPSRHQTHGSHLRLHQMSVADSGEYVCRANNNIDALEASIVISVSPSAGSPSAPGSSMPIRIESSSSHVAEGETLDLNCVVPGQAHAQVTWHKRGGSLPSHHQTRGSRLRLHHVSPADSGEYVCRVMGSSGPLEASVLVTIEASGSSAVHVPAPGGAPPIRIEPSSSRVAEGQTLDLKCVVPGQAHAQVTWHKRGGNLPARHQVHGPLLRLNQVSPADSGEYSCQVTGSSGTLEASVLVTIEPSSPGPIPAPGLAQPIYIEASSSHVTEGQTLDLNCVVPGQAHAQVTWYKRGGSLPARHQTHGSQLRLHLVSPADSGEYVCRAASGPGPEQEASFTVTVPPSEGSSYRLRSPVISIDPPSSTVQQGQDASFKCLIHDGAAPISLEWKTRNQELEDNVHISPNGSIITIVGTRPSNHGTYRCVASNAYGVAQSVVNLSVHGPPTVSVLPEGPVWVKVGKAVTLECVSAGEPRSSARWTRISSTPAKLEQRTYGLMDSHAVLQISSAKPSDAGTYVCLAQNALGTAQKQVEVIVDTGAMAPGAPQVQAEEAELTVEAGHTATLRCSATGSPAPTIHWSKLRSPLPWQHRLEGDTLIIPRVAQQDSGQYICNATSPAGHAEATIILHVESPPYATTVPEHASVQAGETVQLQCLAHGTPPLTFQWSRVGSSLPGRATARNELLHFERAAPEDSGRYRCRVTNKVGSAEAFAQLLVQGPPGSLPATSIPAGSTPTVQVTPQLETKSIGASVEFHCAVPSDRGTQLRWFKEGGQLPPGHSVQDGVLRIQNLDQSCQGTYICQAHGPWGKAQASAQLVIQALPSVLINIRTSVQTVVVGHAVEFECLALGDPKPQVTWSKVGGHLRPGIVQSGGVVRIAHVELADAGQYRCTATNAAGTTQSHVLLLVQALPQISMPQEVRVPAGSAAVFPCIASGYPTPDISWSKLDGSLPPDSRLENNMLMLPSVRPQDAGTYVCTATNRQGKVKAFAHLQVPERVVPYFTQTPYSFLPLPTIKDAYRKFEIKITFRPDSADGMLLYNGQKRVPGSPTNLANRQPDFISFGLVGGRPEFRFDAGSGMATIRHPTPLALGHFHTVTLLRSLTQGSLIVGDLAPVNGTSQGKFQGLDLNEELYLGGYPDYGAIPKAGLSSGFIGCVRELRIQGEEIVFHDLNLTAHGISHCPTCRDRPCQNGGQCHDSESSSYVCVCPAGFTGSRCEHSQALHCHPEACGPDATCVNRPDGRGYTCRCHLGRSGLRCEEGVTVTTPSLSGAGSYLALPALTNTHHELRLDVEFKPLAPDGVLLFSGGKSGPVEDFVSLAMVGGHLEFRYELGSGLAVLRSAEPLALGRWHRVSAERLNKDGSLRVNGGRPVLRSSPGKSQGLNLHTLLYLGGVEPSVPLSPATNMSAHFRGCVGEVSVNGKRLDLTYSFLGSQGIGQCYDSSPCERQPCQHGATCMPAGEYEFQCLCRDGFKGDLCEHEENPCQLREPCLHGGTCQGTRCLCLPGFSGPRCQQGSGHGIAESDWHLEGSGGNDAPGQYGAYFHDDGFLAFPGHVFSRSLPEVPETIELEVRTSTASGLLLWQGVEVGEAGQGKDFISLGLQDGHLVFRYQLGSGEARLVSEDPINDGEWHRVTALREGRRGSIQVDGEELVSGRSPGPNVAVNAKGSVYIGGAPDVATLTGGRFSSGITGCVKNLVLHSARPGAPPPQPLDLQHRAQAGANTRPCPS TT5UM29 TT Discontinued TT5UM29 KE hsa04512:ECM-receptor interaction; hsa05161:Hepatitis B; hsa05205:Proteoglycans in cancer TT5UM29 RC R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-1971475:A tetrasaccharide linker sequence is required for GAG synthesis; R-HSA-2024096:HS-GAG degradation; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000157:Laminin interactions; R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-975634:Retinoid metabolism and transport; R-HSA-977225:Amyloid formation TTU5CIX ID TTU5CIX TTU5CIX TN Ryanodine receptor 1 (RYR1) TTU5CIX UP P21817 TTU5CIX UC RYR1_HUMAN TTU5CIX BC Ryanodine-inositol 1,4,5-triphosphate receptor calcium channel TTU5CIX SN Type 1 ryanodine receptor; Skeletal muscle-type ryanodine receptor; Skeletal muscle ryanodine receptor; Skeletal muscle calcium release channel; RyR1; RyR; RYR-1; RYDR; Cardiac muscleryanodine receptor-calcium release channel; Cardiac muscle-type ryanodine receptor; Brain-type ryanodine receptor; Brain ryanodine receptor-calcium release channel TTU5CIX GN RYR1 TTU5CIX FC Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis. Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. TTU5CIX SQ MGDAEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFVLEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDIILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSRCEEGFVTGGHVLRLFHGHMDECLTISPADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRVRHVTTGQYLALTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAMLHQEGHMDDALSLTRCQQEESQAARMIHSTNGLYNQFIKSLDSFSGKPRGSGPPAGTALPIEGVILSLQDLIIYFEPPSEDLQHEEKQSKLRSLRNRQSLFQEEGMLSMVLNCIDRLNVYTTAAHFAEFAGEEAAESWKEIVNLLYELLASLIRGNRSNCALFSTNLDWLVSKLDRLEASSGILEVLYCVLIESPEVLNIIQENHIKSIISLLDKHGRNHKVLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNLINYVTSIRPNIFVGRAEGTTQYSKWYFEVMVDEVTPFLTAQATHLRVGWALTEGYTPYPGAGEGWGGNGVGDDLYSYGFDGLHLWTGHVARPVTSPGQHLLAPEDVISCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGVKVRFLLGGRHGEFKFLPPPGYAPCHEAVLPRERLHLEPIKEYRREGPRGPHLVGPSRCLSHTDFVPCPVDTVQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVDFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKLPKTYMMSNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVGQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVENQSRCDRVRIFRAEKSYTVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLGSEPFGRPWQPGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLGQDVSSLRFFAICGLQEGFEPFAINMQRPVTTWFSKGLPQFEPVPLEHPHYEVSRVDGTVDTPPCLRLTHRTWGSQNSLVEMLFLRLSLPVQFHQHFRCTAGATPLAPPGLQPPAEDEARAAEPDPDYENLRRSAGGWSEAENGKEGTAKEGAPGGTPQAGGEAQPARAENEKDATTEKNKKRGFLFKAKKVAMMTQPPATPTLPRLPHDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWAGWVTPDYHQHDMSFDLSKVRVVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVIQFELGKQKNIMPLSAAMFQSERKNPAPQCPPRLEMQMLMPVSWSRMPNHFLQVETRRAGERLGWAVQCQEPLTMMALHIPEENRCMDILELSERLDLQRFHSHTLRLYRAVCALGNNRVAHALCSHVDQAQLLHALEDAHLPGPLRAGYYDLLISIHLESACRSRRSMLSEYIVPLTPETRAITLFPPGRSTENGHPRHGLPGVGVTTSLRPPHHFSPPCFVAALPAAGAAEAPARLSPAIPLEALRDKALRMLGEAVRDGGQHARDPVGGSVEFQFVPVLKLVSTLLVMGIFGDEDVKQILKMIEPEVFTEEEEEEDEEEEGEEEDEEEKEEDEEETAQEKEDEEKEEEEAAEGEKEEGLEEGLLQMKLPESVKLQMCHLLEYFCDQELQHRVESLAAFAERYVDKLQANQRSRYGLLIKAFSMTAAETARRTREFRSPPQEQINMLLQFKDGTDEEDCPLPEEIRQDLLDFHQDLLAHCGIQLDGEEEEPEEETTLGSRLMSLLEKVRLVKKKEEKPEEERSAEESKPRSLQELVSHMVVRWAQEDFVQSPELVRAMFSLLHRQYDGLGELLRALPRAYTISPSSVEDTMSLLECLGQIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGESKEIRFPKMVTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGIGLGMQGSTPLDVAAASVIDNNELALALQEQDLEKVVSYLAGCGLQSCPMLVAKGYPDIGWNPCGGERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALRGEGGSGLLAAIEEAIRISEDPARDGPGIRRDRRREHFGEEPPEENRVHLGHAIMSFYAALIDLLGRCAPEMHLIQAGKGEALRIRAILRSLVPLEDLVGIISLPLQIPTLGKDGALVQPKMSASFVPDHKASMVLFLDRVYGIENQDFLLHVLDVGFLPDMRAAASLDTATFSTTEMALALNRYLCLAVLPLITKCAPLFAGTEHRAIMVDSMLHTVYRLSRGRSLTKAQRDVIEDCLMSLCRYIRPSMLQHLLRRLVFDVPILNEFAKMPLKLLTNHYERCWKYYCLPTGWANFGVTSEEELHLTRKLFWGIFDSLAHKKYDPELYRMAMPCLCAIAGALPPDYVDASYSSKAEKKATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTIEKAREGEEEKTEKKKTRKISQSAQTYDPREGYNPQPPDLSAVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGTHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRGLKDMELDSSSIEKRFAFGFLQQLLRWMDISQEFIAHLEAVVSSGRVEKSPHEQEIKFFAKILLPLINQYFTNHCLYFLSTPAKVLGSGGHASNKEKEMITSLFCKLAALVRHRVSLFGTDAPAVVNCLHILARSLDARTVMKSGPEIVKAGLRSFFESASEDIEKMVENLRLGKVSQARTQVKGVGQNLTYTTVALLPVLTTLFQHIAQHQFGDDVILDDVQVSCYRTLCSIYSLGTTKNTYVEKLRPALGECLARLAAAMPVAFLEPQLNEYNACSVYTTKSPRERAILGLPNSVEEMCPDIPVLERLMADIGGLAESGARYTEMPHVIEITLPMLCSYLPRWWERGPEAPPSALPAGAPPPCTAVTSDHLNSLLGNILRIIVNNLGIDEASWMKRLAVFAQPIVSRARPELLQSHFIPTIGRLRKRAGKVVSEEEQLRLEAKAEAQEGELLVRDEFSVLCRDLYALYPLLIRYVDNNRAQWLTEPNPSAEELFRMVGEIFIYWSKSHNFKREEQNFVVQNEINNMSFLTADNKSKMAKAGDIQSGGSDQERTKKKRRGDRYSVQTSLIVATLKKMLPIGLNMCAPTDQDLITLAKTRYALKDTDEEVREFLHNNLHLQGKVEGSPSLRWQMALYRGVPGREEDADDPEKIVRRVQEVSAVLYYLDQTEHPYKSKKAVWHKLLSKQRRRAVVACFRMTPLYNLPTHRACNMFLESYKAAWILTEDHSFEDRMIDDLSKAGEQEEEEEEVEEKKPDPLHQLVLHFSRTALTEKSKLDEDYLYMAYADIMAKSCHLEEGGENGEAEEEVEVSFEEKQMEKQRLLYQQARLHTRGAAEMVLQMISACKGETGAMVSSTLKLGISILNGGNAEVQQKMLDYLKDKKEVGFFQSIQALMQTCSVLDLNAFERQNKAEGLGMVNEDGTVINRQNGEKVMADDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISDFYWYYSGKDVIEEQGKRNFSKAMSVAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMMMKLAQDSSQIELLKELLDLQKDMVVMLLSLLEGNVVNGMIARQMVDMLVESSSNVEMILKFFDMFLKLKDIVGSEAFQDYVTDPRGLISKKDFQKAMDSQKQFSGPEIQFLLSCSEADENEMINCEEFANRFQEPARDIGFNVAVLLTNLSEHVPHDPRLHNFLELAESILEYFRPYLGRIEIMGASRRIERIYFEISETNRAQWEMPQVKESKRQFIFDVVNEGGEAEKMELFVSFCEDTIFEMQIAAQISEPEGEPETDEDEGAGAAEAGAEGAEEGAAGLEGTAATAAAGATARVVAAAGRALRGLSYRSLRRRVRRLRRLTAREAATAVAALLWAAVTRAGAAGAGAAAGALGLLWGSLFGGGLVEGAKKVTVTELLAGMPDPTSDEVHGEQPAGPGGDADGEGASEGAGDAAEGAGDEEEAVHEAGPGGADGAVAVTDGGPFRPEGAGGLGDMGDTTPAEPPTPEGSPILKRKLGVDGVEEELPPEPEPEPEPELEPEKADAENGEKEEVPEPTPEPPKKQAPPSPPPKKEEAGGEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDMEGSAAGDVSGAGSGGSSGWGLGAGEEAEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVIFKREKELARKLEFDGLYITEQPEDDDVKGQWDRLVLNTPSFPSNYWDKFVKRKVLDKHGDIYGRERIAELLGMDLATLEITAHNERKPNPPPGLLTWLMSIDVKYQIWKFGVIFTDNSFLYLGWYMVMSLLGHYNNFFFAAHLLDIAMGVKTLRTILSSVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDEYELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGSDYFDTTPHGFETHTLEEHNLANYMFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLS TTU5CIX TT Discontinued TTU5CIX FM Calcium channel TTU5CIX RC R-HSA-2672351:Stimuli-sensing channels TTAPV67 ID TTAPV67 TTAPV67 TN Thrombomodulin (THBD) TTAPV67 UP P07204 TTAPV67 UC TRBM_HUMAN TTAPV67 BC Growth factor TTAPV67 SN TM; THRM; Fetomodulin; CD141 antigen; CD141 TTAPV67 GN THBD TTAPV67 FC Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated. TTAPV67 PD 5TO3; 3GIS; 2ADX; 1ZAQ; 1TMR TTAPV67 SQ MLGVLVLGALALAGLGFPAPAEPQPGGSQCVEHDCFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGDGGVGRRRLWIGLQLPPGCGDPKRLGPLRGFQWVTGDNNTSYSRWARLDLNGAPLCGPLCVAVSAAEATVPSEPIWEEQQCEVKADGFLCEFHFPATCRPLAVEPGAAAAAVSITYGTPFAARGADFQALPVGSSAAVAPLGLQLMCTAPPGAVQGHWAREAPGAWDCSVENGGCEHACNAIPGAPRCQCPAGAALQADGRSCTASATQSCNDLCEHFCVPNPDQPGSYSCMCETGYRLAADQHRCEDVDDCILEPSPCPQRCVNTQGGFECHCYPNYDLVDGECVEPVDPCFRANCEYQCQPLNQTSYLCVCAEGFAPIPHEPHRCQMFCNQTACPADCDPNTQASCECPEGYILDDGFICTDIDECENGGFCSGVCHNLPGTFECICGPDSALARHIGTDCDSGKVDGGDSGSGEPPPSPTPGSTLTPPAVGLVHSGLLIGISIASLCLVVALLALLCHLRKKQGAARAKMEYKCAAPSKEVVLQHVRTERTPQRL TTAPV67 TT Discontinued TTAPV67 FM Growth factor TTAPV67 KE hsa04610:Complement and coagulation cascades TTAPV67 RC R-HSA-140875:Common Pathway of Fibrin Clot Formation; R-HSA-202733:Cell surface interactions at the vascular wall TTC97NF ID TTC97NF TTC97NF TN TNFA messenger RNA (TNF mRNA) TTC97NF UP P01375 TTC97NF UC TNFA_HUMAN TTC97NF BC mRNA target TTC97NF SN Tumour necrosis factor alpha (mRNA); Tumour necrosis factor (mRNA); Tumor necrosis factor ligand superfamily member 2 (mRNA); Tumor necrosis factor (mRNA); TNFalpha (mRNA); TNFSF2 (mRNA); TNFA (mRNA); TNF-alpha (mRNA); TNF-a (mRNA); TNF alpha (mRNA); Cachectin (mRNA) TTC97NF GN TNF TTC97NF FC It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Upregulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective. Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line. Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance. Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. TTC97NF PD 5YOY; 5WUX; 5UUI; 5TSW; 5MU8 TTC97NF SQ MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL TTC97NF TT Discontinued TTC97NF FM mRNA target TT3PTB6 ID TT3PTB6 TT3PTB6 TN Translationally-controlled tumor protein (TPT1) TT3PTB6 UP P13693 TT3PTB6 UC TCTP_HUMAN TT3PTB6 SN p23; TPT1; TCTP; Histamine-releasing factor; HRF; Fortilin TT3PTB6 GN TPT1 TT3PTB6 FC Involved in calcium binding and microtubule stabilization. TT3PTB6 PD 5O9M; 5O9L; 4Z9V; 3EBM; 2HR9 TT3PTB6 SQ MIIYRDLISHDEMFSDIYKIREIADGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFFIGENMNPDGMVALLDYREDGVTPYMIFFKDGLEMEKC TT3PTB6 TT Discontinued TTOM5H4 ID TTOM5H4 TTOM5H4 TN Vascular endothelial growth factor D (VEGFD) TTOM5H4 UP O43915 TTOM5H4 UC VEGFD_HUMAN TTOM5H4 BC Growth factor TTOM5H4 SN c-Fos-induced growth factor; VEGFD; VEGF-D; FIGF TTOM5H4 GN VEGFD TTOM5H4 FC Growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in the formationof the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors. TTOM5H4 PD 2XV7 TTOM5H4 SQ MYREWVVVNVFMMLYVQLVQGSSNEHGPVKRSSQSTLERSEQQIRAASSLEELLRITHSEDWKLWRCRLRLKSFTSMDSRSASHRSTRFAATFYDIETLKVIDEEWQRTQCSPRETCVEVASELGKSTNTFFKPPCVNVFRCGGCCNEESLICMNTSTSYISKQLFEISVPLTSVPELVPVKVANHTGCKCLPTAPRHPYSIIRRSIQIPEEDRCSHSKKLCPIDMLWDSNKCKCVLQEENPLAGTEDHSHLQEPALCGPHMMFDEDRCECVCKTPCPKDLIQHPKNCSCFECKESLETCCQKHKLFHPDTCSCEDRCPFHTRPCASGKTACAKHCRFPKEKRAAQGPHSRKNP TTOM5H4 TT Clinical trial TTOM5H4 KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa05200:Pathways in cancer TTOM5H4 RC R-HSA-114608:Platelet degranulation; R-HSA-194313:VEGF ligand-receptor interactions; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization TTG9CFY ID TTG9CFY TTG9CFY TN Bacterial Dihydroneopterinaldolase (Bact folB) TTG9CFY UP P0AC16 TTG9CFY UC FOLB_ECOLI TTG9CFY BC Carbon-carbon lyase TTG9CFY SN folB of Escherichia coli; FOLB of Escherichia coli; DHNA of Escherichia coli; 7,8-Dihydroneopterin aldolase TTG9CFY GN Bact folB TTG9CFY FC Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin,but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin at appreciable velocity. TTG9CFY PD 2O90 TTG9CFY SQ MDIVFIEQLSVITTIGVYDWEQTIEQKLVFDIEMAWDNRKAAKSDDVADCLSYADIAETVVSHVEGARFALVERVAEEVAELLLARFNSPWVRIKLSKPGAVARAANVGVIIERGNNLKENN TTG9CFY TT Discontinued TT2OUI9 ID TT2OUI9 TT2OUI9 TN Beta-2-glycoprotein 1 (APOH) TT2OUI9 UP P02749 TT2OUI9 UC APOH_HUMAN TT2OUI9 SN Beta-2-glycoprotein I; Beta(2)GPI; B2GPI; Apolipoprotein H; Apo-H; Anticardiolipin cofactor; Activated protein C-binding protein; APOH; APC inhibitor TT2OUI9 GN APOH TT2OUI9 FC Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. TT2OUI9 PD 4JHS; 3OP8; 2KRI; 1QUB; 1G4G TT2OUI9 SQ MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPIICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTIEVPKCFKEHSSLAFWKTDASDVKPC TT2OUI9 TT Discontinued TTTHCPF ID TTTHCPF TTTHCPF TN Cholesterol 24-monooxygenase (CYP46A1) TTTHCPF UP Q9Y6A2 TTTHCPF UC CP46A_HUMAN TTTHCPF SN Cytochrome P450 46A1; Cholesterol 24S-hydroxylase; CYP46; CH24H TTTHCPF GN CYP46A1 TTTHCPF FC P450 monooxygenase that plays a major role in cholesterol homeostasis in the brain. Primarily catalyzes the hydroxylation (with S stereochemistry) at C-24 of cholesterol side chain, triggering cholesterol diffusion out of neurons and its further degradation. By promoting constant cholesterol elimination in neurons, may activate the mevalonate pathway and coordinate the synthesis of new cholesterol and nonsterol isoprenoids involved in synaptic activity and learning (By similarity). Further hydroxylates cholesterol derivatives and hormone steroids on both the ring and side chain of these molecules, converting them into active oxysterols involved in lipid signaling and biosynthesis. Acts as an epoxidase converting cholesta-5,24-dien-3beta-ol/desmosterol into (24S),25-epoxycholesterol, an abundant lipid ligand of nuclear NR1H2 and NR1H3 receptors shown to promote neurogenesis in developing brain. May also catalyze the oxidative metabolism of xenobiotics, such as clotrimazole. TTTHCPF EC EC 1.14.14.25 TTTHCPF PD 4J14; 4FIA; 4ENH; 3MDV; 3MDT TTTHCPF SQ MSPGLLLLGSAVLLAFGLCCTFVHRARSRYEHIPGPPRPSFLLGHLPCFWKKDEVGGRVLQDVFLDWAKKYGPVVRVNVFHKTSVIVTSPESVKKFLMSTKYNKDSKMYRALQTVFGERLFGQGLVSECNYERWHKQRRVIDLAFSRSSLVSLMETFNEKAEQLVEILEAKADGQTPVSMQDMLTYTAMDILAKAAFGMETSMLLGAQKPLSQAVKLMLEGITASRNTLAKFLPGKRKQLREVRESIRFLRQVGRDWVQRRREALKRGEEVPADILTQILKAEEGAQDDEGLLDNFVTFFIAGHETSANHLAFTVMELSRQPEIVARLQAEVDEVIGSKRYLDFEDLGRLQYLSQVLKESLRLYPPAWGTFRLLEEETLIDGVRVPGNTPLLFSTYVMGRMDTYFEDPLTFNPDRFGPGAPKPRFTYFPFSLGHRSCIGQQFAQMEVKVVMAKLLQRLEFRLVPGQRFGLQEQATLKPLDPVLCTLRPRGWQPAPPPPPC TTTHCPF TT Discontinued TTRQJTC ID TTRQJTC TTRQJTC TN C-X-C chemokine receptor type 7 (ACKR3) TTRQJTC UP P25106 TTRQJTC UC ACKR3_HUMAN TTRQJTC BC GPCR rhodopsin TTRQJTC SN RDC1; RDC-1; Gprotein coupled receptor RDC1 homolog; Gprotein coupled receptor 159; GPR159; G-protein coupled receptor RDC1 homolog; G-protein coupled receptor 159; Chemokine orphan receptor 1; CXCR7; CXCR-7; CXC-R7; CXC chemokine receptor type 7; CMKOR1; Atypical chemokine receptor 3 TTRQJTC GN ACKR3 TTRQJTC FC Known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates. Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. TTRQJTC SQ MDLHLFDYSEPGNFSDISWPCNSSDCIVVDTVMCPNMPNKSVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVLTIPVWVVSLVQHNQWPMGELTCKVTHLIFSINLFGSIFFLTCMSVDRYLSITYFTNTPSSRKKMVRRVVCILVWLLAFCVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVVLGFAVPFSIIAVFYFLLARAISASSDQEKHSSRKIIFSYVVVFLVCWLPYHVAVLLDIFSILHYIPFTCRLEHALFTALHVTQCLSLVHCCVNPVLYSFINRNYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALEQSTK TTRQJTC TT Preclinical TTRQJTC FM GPCR rhodopsin TTRQJTC KE hsa04060:Cytokine-cytokine receptor interaction TTRQJTC RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTRV7FQ ID TTRV7FQ TTRV7FQ TN Enterobacteria Shiga-like toxin 2B (EntBac stxB2) TTRV7FQ UP P09386 TTRV7FQ UC STXB_BP933 TTRV7FQ BC Shiga-like toxin beta TTRV7FQ SN stxB2; Verotoxin 2 subunit B; Verocytotoxin 2 subunit B; Shiga-like toxin 2 subunit B; SLT-IIb; SLT-2b; SLT-2 B subunit TTRV7FQ GN EntBac stxB2 TTRV7FQ FC TheB subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli. TTRV7FQ PD 6FE4; 2GA4; 1R4P TTRV7FQ SQ MKKMFMAVLFALASVNAMAADCAKGKIEFSKYNEDDTFTVKVDGKEYWTSRWNLQPLLQSAQLTGMTVTIKSSTCESGSGFAEVQFNND TTRV7FQ TT Discontinued TTMJX4U ID TTMJX4U TTMJX4U TN Herpes simplex virus Ribonucleoside-diphosphate reductase (HSV RIR1) TTMJX4U UP P08543 TTMJX4U UC RIR1_HHV11 TTMJX4U BC CH/CH(2) oxidoreductase TTMJX4U SN HSV Ribonucleotide reductase; HSV Ribonucleoside diphosphate reductase; HSV RIR1 TTMJX4U GN HSV RIR1 TTMJX4U FC Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. The N-terminal region confers antiapoptotic activity in differentiated cells such as neurons and is importantfor viral reactivation to increase neural survivability. TTMJX4U SQ MASRPAASSPVEARAPVGGQEAGGPSAATQGEAAGAPLAHGHHVYCQRVNGVMVLSDKTPGSASYRISDNNFVQCGSNCTMIIDGDVVRGRPQDPGAAASPAPFVAVTNIGAGSDGGTAVVAFGGTPRRSAGTSTGTQTADVPTEALGGPPPPPRFTLGGGCCSCRDTRRRSAVFGGEGDPVGPAEFVSDDRSSDSDSDDSEDTDSETLSHASSDVSGGATYDDALDSDSSSDDSLQIDGPVCRPWSNDTAPLDVCPGTPGPGADAGGPSAVDPHAPTPEAGAGLAADPAVARDDAEGLSDPRPRLGTGTAYPVPLELTPENAEAVARFLGDAVNREPALMLEYFCRCAREETKRVPPRTFGSPPRLTEDDFGLLNYALVEMQRLCLDVPPVPPNAYMPYYLREYVTRLVNGFKPLVSRSARLYRILGVLVHLRIRTREASFEEWLRSKEVALDFGLTERLREHEAQLVILAQALDHYDCLIHSTPHTLVERGLQSALKYEEFYLKRFGGHYMESVFQMYTRIAGFLACRATRGMRHIALGREGSWWEMFKFFFHRLYDHQIVPSTPAMLNLGTRNYYTSSCYLVNPQATTNKATLRAITSNVSAILARNGGIGLCVQAFNDSGPGTASVMPALKVLDSLVAAHNKESARPTGACVYLEPWHTDVRAVLRMKGVLAGEEAQRCDNIFSALWMPDLFFKRLIRHLDGEKNVTWTLFDRDTSMSLADFHGEEFEKLYQHLEVMGFGEQIPIQELAYGIVRSAATTGSPFVMFKDAVNRHYIYDTQGAAIAGSNLCTEIVHPASKRSSGVCNLGSVNLARCVSRQTFDFGRLRDAVQACVLMVNIMIDSTLQPTPQCTRGNDNLRSMGIGMQGLHTACLKLGLDLESAEFQDLNKHIAEVMLLSAMKTSNALCVRGARPFNHFKRSMYRAGRFHWERFPDARPRYEGEWEMLRQSMMKHGLRNSQFVALMPTAASAQISDVSEGFAPLFTNLFSKVTRDGETLRPNTLLLKELERTFSGKRLLEVMDSLDAKQWSVAQALPCLEPTHPLRRFKTAFDYDQKLLIDLCADRAPYVDHSQSMTLYVTEKADGTLPASTLVRLLVHAYKRGLKTGMYYCKVRKATNSGVFGGDDNIVCMSCAL TTMJX4U TT Discontinued TTXQPKC ID TTXQPKC TTXQPKC TN Human papillomavirus E2 transactivator messenger RNA (HPV E2 mRNA) TTXQPKC UP P06790 TTXQPKC UC VE2_HPV18 TTXQPKC BC mRNA target TTXQPKC SN Regulatory protein E2 (mRNA) TTXQPKC GN HPV E2 mRNA TTXQPKC FC A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex. Plays a role in the initiation of viral DNA replication. TTXQPKC PD 1TUE; 1QQH; 1JJ4; 1F9F TTXQPKC SQ MQTPKETLSERLSCVQDKIIDHYENDSKDIDSQIQYWQLIRWENAIFFAAREHGIQTLNHQVVPAYNISKSKAHKAIELQMALQGLAQSAYKTEDWTLQDTCEELWNTEPTHCFKKGGQTVQVYFDGNKDNCMTYVAWDSVYYMTDAGTWDKTATCVSHRGLYYVKEGYNTFYIEFKSECEKYGNTGTWEVHFGNNVIDCNDSMCSTSDDTVSATQLVKQLQHTPSPYSSTVSVGTAKTYGQTSAATRPGHCGLAEKQHCGPVNPLLGAATPTGNNKRRKLCSGNTTPIIHLKGDRNSLKCLRYRLRKHSDHYRDISSTWHWTGAGNEKTGILTVTYHSETQRTKFLNTVAIPDSVQILVGYMTM TTXQPKC TT Discontinued TTXQPKC FM mRNA target TTGUJAO ID TTGUJAO TTGUJAO TN Immunoglobulin alpha Fc receptor (FCAR) TTGUJAO UP P24071 TTGUJAO UC FCAR_HUMAN TTGUJAO SN IgA Fc receptor; FCAR; CD89 antigen; CD89 TTGUJAO GN FCAR TTGUJAO FC Binds to the fc region of immunoglobulins alpha. Mediates several functions including cytokine production. TTGUJAO PD 1UCT; 1OW0; 1OVZ TTGUJAO SQ MDPKQTTLLCLVLCLGQRIQAQEGDFPMPFISAKSSPVIPLDGSVKIQCQAIREAYLTQLMIIKNSTYREIGRRLKFWNETDPEFVIDHMDANKAGRYQCQYRIGHYRFRYSDTLELVVTGLYGKPFLSADRGLVLMPGENISLTCSSAHIPFDRFSLAKEGELSLPQHQSGEHPANFSLGPVDLNVSGIYRCYGWYNRSPYLWSFPSNALELVVTDSIHQDYTTQNLIRMAVAGLVLVALLAILVENWHSHTALNKEASADVAEPSWSQQMCQPGLTFARTPSVCK TTGUJAO TT Discontinued TTGUJAO KE hsa04145:Phagosome; hsa05150:Staphylococcus aureus infection TTKSND3 ID TTKSND3 TTKSND3 TN Lectin-like oxidized LDL receptor (OLR1) TTKSND3 UP P78380 TTKSND3 UC OLR1_HUMAN TTKSND3 SN hLOX-1; Oxidized low-density lipoprotein receptor 1; Oxidized low-density lipoprotein receptor; Oxidised low density lipoprotein (Lectin-like) receptor 1; Ox-LDL receptor 1; Lectin-type oxidized LDL receptor 1; Lectin-type oxidized LDL receptor; Lectin-like oxidized low-density lipoprotein receptor-1; Lectin-like oxidized LDL receptor-1; Lectin-like oxidized LDL receptor 1; Lectin-like oxLDL receptor 1; LOX1; LOX-1; CLEC8A; C-type lectin domain family 8 member A TTKSND3 GN OLR1 TTKSND3 FC OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria. Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. TTKSND3 PD 3VLG; 1YXK; 1YXJ; 1YPU; 1YPQ TTKSND3 SQ MTFDDLKIQTVKDQPDEKSNGKKAKGLQFLYSPWWCLAAATLGVLCLGLVVTIMVLGMQLSQVSDLLTQEQANLTHQKKKLEGQISARQQAEEASQESENELKEMIETLARKLNEKSKEQMELHHQNLNLQETLKRVANCSAPCPQDWIWHGENCYLFSSGSFNWEKSQEKCLSLDAKLLKINSTADLDFIQQAISYSSFPFWMGLSRRNPSYPWLWEDGSPLMPHLFRVRGAVSQTYPSGTCAYIQRGAVYAENCILAAFSICQKKANLRAQ TTKSND3 TT Discontinued TTKSND3 FM Transmembrane protein TT31JXP ID TT31JXP TT31JXP TN Myophosphorylase (PYGM) TT31JXP UP P11217 TT31JXP UC PYGM_HUMAN TT31JXP SN Glycogen phosphorylase, muscle form; Myophosphorylase TT31JXP GN PYGM TT31JXP FC Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. TT31JXP EC EC 2.4.1.1 TT31JXP PD 1Z8D TT31JXP SQ MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERMDWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFVPRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDKLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEDYIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEAI TT31JXP TT Discontinued TTAT87F ID TTAT87F TTAT87F TN Amylin receptor (IAPPR) TTAT87F UP P30988-O60894/O60895/O60896 TTAT87F UC CALCR_HUMAN-RAMP1_HUMAN/RAMP2_HUMAN/RAMP3_HUMAN TTAT87F SN Complex of Calcitonin receptor and Receptor activity-modifying protein TTAT87F GN CALCR-RAMP1/RAMP2/RAMP3 TTAT87F FC Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL. TTAT87F SQ MRFTFTSRCLALFLLLNHPTPILPAFSNQTYPTIEPKPFLYVVGRKKMMDAQYKCYDRMQQLPAYQGEGPYCNRTWDGWLCWDDTPAGVLSYQFCPDYFPDFDPSEKVTKYCDEKGVWFKHPENNRTWSNYTMCNAFTPEKLKNAYVLYYLAIVGHSLSIFTLVISLGIFVFFRSLGCQRVTLHKNMFLTYILNSMIIIIHLVEVVPNGELVRRDPVSCKILHFFHQYMMACNYFWMLCEGIYLHTLIVVAVFTEKQRLRWYYLLGWGFPLVPTTIHAITRAVYFNDNCWLSVETHLLYIIHGPVMAALVVNFFFLLNIVRVLVTKMRETHEAESHMYLKAVKATMILVPLLGIQFVVFPWRPSNKMLGKIYDYVMHSLIHFQGFFVATIYCFCNNEVQTTVKRQWAQFKIQWNQRWGRRPSNRSARAAAAAAEAGDIPIYICHQEPRNEPANNQGEESAEIIPLNIIEQESSAMARALCRLPRRGLWLLLAHHLFMTTACQEANYGALLRELCLTQFQVDMEAVGETLWCDWGRTIRSYRELADCTWHMAEKLGCFWPNAEVDRFFLAVHGRYFRSCPISGRAVRDPPGSILYPFIVVPITVTLLVTALVVWQSKRTEGIV TTAT87F TT Clinical trial TTAT87F KE hsa04270:Vascular smooth muscle contraction TT5XOKS ID TT5XOKS TT5XOKS TN Leishmania Carbamoyl-phosphate synthase (Leishm CPS) TT5XOKS UP E9BCR2 TT5XOKS UC E9BCR2_LEIDB TT5XOKS BC Carbon-nitrogen ligase TT5XOKS SN Carbamoyl-phosphate synthase, putative TT5XOKS GN Leishm CPS TT5XOKS FC Catalyses the formation of carbamoyl phosphate from L-glutamine, bicarbonate, and 2 moles of MgATP. TT5XOKS SQ MEHYAKAELVLHGGERFEGYSFGYEESVAGEVVFATGMVGYPESLSDPSYHGQILVLTSPMVGNYGVPRVEEDLFGVTKYFESTDGQIHVSAVVVQEYCDQPDHWEMYETLGTWLRKNKVPGMMMVDTRSIVLKLRDMGTALGKVLVAGNDVPFMDPNTRNLVAEVSTKTRVTHGHGTLRILVIDMGVKLNTLRCLLKHDVTLIVVPHDWDITTEVYDGLFITNGPGNPQICTSTIRSVRWALQQDKPIFGICMGNQMLCLAAGGTTYKMKYGHRGQNQPCKCNIDGRVVITTQNHGFAVDFKTLPSGEWEEYFTNSNDGSNEGLWHKTKPFCSVQFHPEGRCGPQDTEYLFSEYVCRVKESKVREVAKFKPRKVLVLGAGGIVIAQAGEFDYSGSQCLKSLREEGMETVLINPNIATVQTDDEMADHIYFVPLTVEAVERVIEKERPDGILLGWGGQTALNCGVKLDELGVLKKYNVQVLGTPVSVIAVTEDRELFRDTLLQINEQVAKSAAVMSVEEAVAASKDIGFPMMVRAAYCLGGQGSGIVENMEELRHKVEVALAASPQVLLEESVAGWKEIEYEVVRDIYDNCITVCNMENFDPMGVHTGESIVVAPSQTLSNDEFHMLRSASIKIIRHLGIVGECNIQYGLDPFSHRYVVIEVNARLSRSSALASKATGYPLAHVATKIALGKGLFEITNGVTKTTMACFEPSMDYIAVKMPRWDLHKFNMVSEEIGSMMKSVGEVMSIGRTFEEALQKAIRMVDPSYTGFSLPDRFAGVDFDYMEHIRHPTPYRLFALCRALLDGHSAEELYQMTKITRFFLYKLEKLVRLSKATSTLYANKLTEMPRENLLNMKAHGFSDRQLAQLLNSTAADVRARRVELNVMPLIKQIDTVAGEYPAAQCCYLYSTYNAQRDDVPFTERMYAVLGCGVYRIGNSVEFDYGGVLVARELRRLGNKVILINYNPETVSTDYDECDRLYFDEVSEETVLDILTKERVRGVVISLGGQIVQNMALSLKKSGLPILGTDPANIDMAEDRNKFSKMCDELGVPQPEWISATSVEQVHEFCDTVGYPALVRPSYVLSGSAMAVIANKEDVTRYLKEASFVSGEHPVVVSKYYEAATEYDVDIVAHHGRVLCYAICEHVENAGVHSGDATMFLPPQNTDKDTMKRIYDSVNRIAEKLDVVGPMNVQFLLTAEGQLRVIEANVRSSRSVPFVSKTLGISFPSVMVSAFLARKDQNLVPIKRAKMTHIGCKASMFSFNRLAGADPILGVEMASTGEIGVFGRDKHEVFLKAMLCQNFKIPQKGVFFSSDVDSQTEALCPYIQHLVRRGLKVYGTTKTAAVLHEYGIQCEVLLQRGELPSGDASESNRLAVYDEEVAKKEKFDLVIQLRDKRRDFVLRRCTRETAPPDYWVRRLAVDYNIPLLTEPSIVKMFCECMDLPASSIEIEPFRHYVPKIYHKVENNNCAMLRCHKVGLMITNNNDSKVLALRLSQEGLNITCFHAYLGGSDIDHFEQAFQSLNVPVEVVDLRSEIANSAFDLIMCQSADERHNWHLSKLSWYIFGKYLIPVMRQRRMSVVAQTSKQNKKEAGFEKYVQSNCPEMGVYNAWRDARLMEDFETVADQISFLRKHGIKATVKSNVQVHSSVCGSTYYGDDMRSLPAPSLVKPVRECSVTPEFVSLTFRGARCVNINGIDVTPLLALQMANEIAGRNGVGITRTREGAMYETPGMNLLSVGLQFLYDVSFDRCAADLFRIYSRHVSQNIGAGQLSEKHTQSAIEAVRFLTSDVSGVVELELHQGEIIFLKLSHVQNPVDRRVAPQLVTEEELEEVFQPGNGSFSDVQW TT5XOKS TT Discontinued TTMT0HG ID TTMT0HG TTMT0HG TN Neuronal acetylcholine receptor alpha-2/alpha-3 (CHRNA2/A3) TTMT0HG UP Q15822-P32297 TTMT0HG UC ACHA2_HUMAN; ACHA3_HUMAN TTMT0HG BC Neurotransmitter receptor TTMT0HG SN CHRNA; nAChR TTMT0HG GN CHRNA2-CHRNA3 TTMT0HG FC After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. TTMT0HG SQ MGPSCPVFLSFTKLSLWWLLLTPAGGEEAKRPPPRAPGDPLSSPSPTALPQGGSHTETEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSDCGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHTMPHWVRGALLGCVPRWLLMNRPPPPVELCHPLRLKLSPSYHWLESNVDAEEREVVVEEEDRWACAGHVAPSVGTLCSHGHLHSGASGPKAEALLQEGELLLSPHMQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVIDRIFLWLFIIVCFLGTIGLFLPPFLAGMI TTMT0HG TT Discontinued TT0R12H ID TT0R12H TT0R12H TN Neuron-specific vesicular protein calcyon (CALY) TT0R12H UP Q9NYX4 TT0R12H UC CALY_HUMAN TT0R12H SN Neuronspecific vesicular protein calcyon; CALY TT0R12H GN CALY TT0R12H FC Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis. TT0R12H SQ MVKLGCSFSGKPGKDPGDQDGAAMDSVPLISPLDISQLQPPLPDQVVIKTQTEYQLSSPDQQNFPDLEGQRLNCSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTETPAAWGDGYRAAKEERKGPTQAGAAAAATEPPGKPSAKAEKEAARKAAGSAAPPPAQ TT0R12H TT Discontinued TT0R12H KE hsa04728:Dopaminergic synapse TTYXPCO ID TTYXPCO TTYXPCO TN P2Y purinoceptor 11 (P2RY11) TTYXPCO UP Q96G91 TTYXPCO UC P2Y11_HUMAN TTYXPCO SN P2Y11 TTYXPCO GN P2RY11 TTYXPCO FC Receptor for ATP and ADP coupled to G-proteins that activate both phosphatidylinositol-calcium and adenylyl cyclase second messenger systems. Not activated by UTP or UDP. TTYXPCO PD 2B6S TTYXPCO SQ MAANVSGAKSCPANFLAAADDKLSGFQGDFLWPILVVEFLVAVASNGLALYRFSIRKQRPWHPAVVFSVQLAVSDLLCALTLPPLAAYLYPPKHWRYGEAACRLERFLFTCNLLGSVIFITCISLNRYLGIVHPFFARSHLRPKHAWAVSAAGWVLAALLAMPTLSFSHLKRPQQGAGNCSVARPEACIKCLGTADHGLAAYRAYSLVLAGLGCGLPLLLTLAAYGALGRAVLRSPGMTVAEKLRVAALVASGVALYASSYVPYHIMRVLNVDARRRWSTRCPSFADIAQATAALELGPYVGYQVMRGLMPLAFCVHPLLYMAAVPSLGCCCRHCPGYRDSWNPEDAKSTGQALPLNATAAPKPSEPQSRELSQ TTYXPCO TT Discontinued TT24DGP ID TT24DGP TT24DGP TN P2Y purinoceptor 4 (P2RY4) TT24DGP UP P51582 TT24DGP UC P2RY4_HUMAN TT24DGP SN Uridine nucleotide receptor; UNR; P2Y4; P2P; NRU TT24DGP GN P2RY4 TT24DGP FC Receptor for UTP and UDP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. Not activated by ATP or ADP. TT24DGP PD 2B6Q TT24DGP SQ MASTESSLLRSLGLSPGPGSSEVELDCWFDEDFKFILLPVSYAVVFVLGLGLNAPTLWLFIFRLRPWDATATYMFHLALSDTLYVLSLPTLIYYYAAHNHWPFGTEICKFVRFLFYWNLYCSVLFLTCISVHRYLGICHPLRALRWGRPRLAGLLCLAVWLVVAGCLVPNLFFVTTSNKGTTVLCHDTTRPEEFDHYVHFSSAVMGLLFGVPCLVTLVCYGLMARRLYQPLPGSAQSSSRLRSLRTIAVVLTVFAVCFVPFHITRTIYYLARLLEADCRVLNIVNVVYKVTRPLASANSCLDPVLYLLTGDKYRRQLRQLCGGGKPQPRTAASSLALVSLPEDSSCRWAATPQDSSCSTPRADRL TT24DGP TT Discontinued TT1D5X3 ID TT1D5X3 TT1D5X3 TN Pneumocystis jirovecii DNA topoisomerase 2 (PJ top2) TT1D5X3 UP L0P818 TT1D5X3 UC L0P818_PNEJ8 TT1D5X3 SN PJ DNA topoisomerase 2 TT1D5X3 GN PJ top2 TT1D5X3 FC Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. TT1D5X3 EC EC 5.6.2.3 TT1D5X3 SQ MLRETSSDDSDMSFSLKRKYTNVSKNIKKIRNADVGFDSERQLCSEIASVGRTISENLSYSRHENFSDTVDTIESKNHLLATKTTSEIYQKLSQLEHILKRPDTYIGSIEFTSQHIWVYDDNTNAMKYRQVSIVPGLYKIFDEILVNAADNKIRDPNMDTIKVEFSREKNVISIYNNGRGIPIEIHNKEKVWIPELIFGHLLTSSNYDDEEKKVTGGRNGYGAKLCNIFSTEFIVETADRATKKTYKQVFLNNMTKKKDPVIKENKKDEEYTRITFKPDLERFGMKEIDSDLESVFKRRVYDLAGSVKNVKVFLNGERIKVKSFKQYIEMYLNSDDSENNLKPTIIHEVVNDRWEVAFTVSDGQFNQVSFVNSIATTRGGTHVNYVSDQIVLKLIEAVKKKNKNIPIKPFQVKNHIWVFINSLIENPSFDSQTKETLTLKQTAFGSKCILSDDFIKKVLKTPIMEKILDTAQKKADQLMKKTDGSKKMRITGLPKLEDANKAGTKEGHKCTLILTEGDSAKSLAMSGIGVVGRDYFGVYPLRGKLLNVREASHEQISKNAEINAIKQIMGLQHKKVYTSTSELRYGHLMIMTDQDHDGSHIKGLIINYLESSFPSLLEIPGFLIEFITPIVKATKGTQEKTFFTIPEYEYWKESVDNAKGWKIKYYKGLGTSYGNDVKKYFSDLDTHLKEFHSIREGDKELIDMAFSKKKADERKEWLRLFKPGTYMDHTLDKIPISDFINKELILFSMADNIRSIPSVVDGLKPGQRKVIFGCFKRKLKSEIKVAQLSGYISEHTAYHHGEQSLTQTIIGLAQTFVGSNNINLMKPNGQFGTRLQGGKDAASPRYIFTELSPLTRKIFVESDDALLNYLNEDGQSIEPLWYVPIIPLILVNGCEGIGTGWSSYIPNFNPIDLVNNIRRMMNGEKLEPMHPWYRGFNGSIEKQGDKYKISGCIRQIDDTTVEITELPIRFWTQDMKEFLELSVVGSDKVQPFIKDYSEYHTDTVVHFIIKLTEKGMAESLAQGLEEKFKLIKIQNMTNMVAFDSSGRIKKYNSVEEILLEFYNIRLQFYQKRKDYLVNELESQYNKLSNQVRFVKMVINKEQDFLNRKRKDLLDDLKLKGFIPFPKNKHISVDNATETSNNLAENDDDDATGYDYLLSMPLWSLTAEKVEKLLKDKLDKENELESLLKLTVKDLWNKDLDNFVEEWEMFLKHDENLTSKVKNLKKDKRNSQKLGIVTQKSVVKKRAVNSQNKPSDVDYKPFSKKTLLSAKQTTLPFSVKNVKDTDVDFLKNQESSNKVINESVVAVENDQVFAKTDATAERKYGANAIIVPSLKGDLSDDSDTDYMDDLVKKYTINPSGGKSMTSYIKSVSPSPKKTKIALSTKSRSPPKMSTLLDSSPDYVVPITKSSTKTIHKKKKTLARKININDSEIDIPVRSDISQRPRRQVAVQARQRVVAIINSDDNDTTLDRSSLSSEFDGSSS TT1D5X3 TT Discontinued TT2Y1AN ID TT2Y1AN TT2Y1AN TN Rhinovirus Protein 1 (HRV P1D) TT2Y1AN UP P12916 (567-857) TT2Y1AN UC POLG_HRV1B TT2Y1AN SN Rhinovirus Capsid protein VP1; Rhinovirus P1D; Rhinovirus Virion protein 1 TT2Y1AN GN HRV P1D TT2Y1AN FC Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity). TT2Y1AN PD 1XR6 TT2Y1AN SQ PIEQNPVENYIDEVLNEVLVVPNIKESHHTTSNSAPLLDAAETGHTSNVQPEDAIETRYVMTSQTRDEMSIESFLGRSGCVHISRIKVDYNDYNGVNKNFTTWKITLQEMAQIRRKFELFTYVRFDSEVTLVPCIAGRGDDIGHVVMQYMYVPPGAPIPKTRNDFSWQSGTNMSIFWQHGQPFPRFSLPFLSIASAYYMFYDGYDGDNSSSKYGSIVTNDMGTICSRIVTEKQEHPVVITTHIYHKAKHTKAWCPRPPRAVPYTHSRVTNYVPKTGDVTTAIVPRASMKTV TT2Y1AN TT Discontinued TT4PTJ7 ID TT4PTJ7 TT4PTJ7 TN Ribonuclease P protein (RPP) TT4PTJ7 UP O95059; Q9H633 TT4PTJ7 UC RPP14_HUMAN; RPP21_HUMAN TT4PTJ7 BC Endoribonucleases TT4PTJ7 SN Ribonuclease P protein TT4PTJ7 GN RPP14; RPP21 TT4PTJ7 FC Acts as a catalyst in the same way that a protein-based enzyme would. Its function is to cleave off an extra, or precursor, sequence of RNA on tRNA molecules. TT4PTJ7 SQ MPAPAATYERVVYKNPSEYHYMKVCLEFQDCGVGLNAAQFKQLLISAVKDLFGEVDAALPLDILTYEEKTLSAILRICSSGLVKLWSSLTLLGSYKGKKCAFRVIQVSPFLLALSGNSRELVLD TT4PTJ7 TT Discontinued TTTXQF6 ID TTTXQF6 TTTXQF6 TN RNA-binding protein Musashi-2 (MSI2) TTTXQF6 UP Q96DH6 TTTXQF6 UC MSI2H_HUMAN TTTXQF6 SN RNA-binding protein Musashi homolog 2; Musashi-2 TTTXQF6 GN MSI2 TTTXQF6 FC May play a role in the proliferation and maintenance of stem cells in the central nervous system. RNA binding protein that regulates the expression of target mRNAs at the translation level. TTTXQF6 PD 6DBP; 6C8U TTTXQF6 SQ MEANGSQGTSGSANDSQHDPGKMFIGGLSWQTSPDSLRDYFSKFGEIRECMVMRDPTTKRSRGFGFVTFADPASVDKVLGQPHHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSANTVVEDVKQYFEQFGKVEDAMLMFDKTTNRHRGFGFVTFENEDVVEKVCEIHFHEINNKMVECKKAQPKEVMFPPGTRGRARGLPYTMDAFMLGMGMLGYPNFVATYGRGYPGFAPSYGYQFPGFPAAAYGPVAAAAVAAARGSGSNPARPGGFPGANSPGPVADLYGPASQDSGVGNYISAASPQPGSGFGHGIAGPLIATAFTNGYH TTTXQF6 TT Discontinued TTTXQF6 FM RNA recognition motif TTV8KWS ID TTV8KWS TTV8KWS TN Vesicular acetylcholine transporter (SLC18A3) TTV8KWS UP Q16572 TTV8KWS UC VACHT_HUMAN TTV8KWS SN VAChT; Solute carrier family 18 member 3 TTV8KWS GN SLC18A3 TTV8KWS FC Involved in acetylcholine transport into synaptic vesicles. TTV8KWS SQ MESAEPAGQARAAATKLSEAVGAALQEPRRQRRLVLVIVCVALLLDNMLYMVIVPIVPDYIAHMRGGGEGPTRTPEVWEPTLPLPTPANASAYTANTSASPTAAWPAGSALRPRYPTESEDVKIGVLFASKAILQLLVNPLSGPFIDRMSYDVPLLIGLGVMFASTVLFAFAEDYATLFAARSLQGLGSAFADTSGIAMIADKYPEEPERSRALGVALAFISFGSLVAPPFGGILYEFAGKRVPFLVLAAVSLFDALLLLAVAKPFSAAARARANLPVGTPIHRLMLDPYIAVVAGALTTCNIPLAFLEPTIATWMKHTMAASEWEMGMAWLPAFVPHVLGVYLTVRLAARYPHLQWLYGALGLAVIGASSCIVPACRSFAPLVVSLCGLCFGIALVDTALLPTLAFLVDVRHVSVYGSVYAIADISYSVAYALGPIVAGHIVHSLGFEQLSLGMGLANLLYAPVLLLLRNVGLLTRSRSERDVLLDEPPQGLYDAVRLRERPVSGQDGEPRSPPGPFDACEDDYNYYYTRS TTV8KWS TT Discontinued TTKOBY0 ID TTKOBY0 TTKOBY0 TN Bone resorption factor (BRF) TTKOBY0 UP P08833; P18065; P17936 TTKOBY0 UC IBP1_HUMAN; IBP2_HUMAN; IBP3_HUMAN TTKOBY0 SN Insulin-like growth factor-binding protein; IGFBP; IGF-binding protein; IBP TTKOBY0 GN IGFBP1; IGFBP2; IGFBP3 TTKOBY0 FC IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R. TTKOBY0 SQ MSEVPVARVWLVLLLLTVQVGVTAGAPWQCAPCSAEKLALCPPVSASCSEVTRSAGCGCCPMCALPLGAACGVATARCARGLSCRALPGEQQPLHALTRGQGACVQESDASAPHAAEAGSPESPESTEITEEELLDNFHLMAPSEEDHSILWDAISTYDGSKALHVTNIKKWKEPCRIELYRVVESLAKAQETSGEEISKFYLPNCNKNGFYHSRQCETSMDGEAGLCWCVYPWNGKRIPGSPEIRGDPNCQIYFNVQN TTKOBY0 TT Discontinued TTIF3GB ID TTIF3GB TTIF3GB TN Glucose transporter type 9 (GLUT9) TTIF3GB UP Q9NRM0 TTIF3GB UC GTR9_HUMAN TTIF3GB SN Urate transporter; Solute carrier family 2, facilitated glucose transporter member 9; GLUT9; GLUT-9 TTIF3GB GN SLC2A9 TTIF3GB FC Urate transporter, which may play a role in the urate reabsorption by proximal tubules. Does not transport glucose, fructose or galactose. TTIF3GB SQ MARKQNRNSKELGLVPLTDDTSHAGPPGPGRALLECDHLRSGVPGGRRRKDWSCSLLVASLAGAFGSSFLYGYNLSVVNAPTPYIKAFYNESWERRHGRPIDPDTLTLLWSVTVSIFAIGGLVGTLIVKMIGKVLGRKHTLLANNGFAISAALLMACSLQAGAFEMLIVGRFIMGIDGGVALSVLPMYLSEISPKEIRGSLGQVTAIFICIGVFTGQLLGLPELLGKESTWPYLFGVIVVPAVVQLLSLPFLPDSPRYLLLEKHNEARAVKAFQTFLGKADVSQEVEEVLAESRVQRSIRLVSVLELLRAPYVRWQVVTVIVTMACYQLCGLNAIWFYTNSIFGKAGIPPAKIPYVTLSTGGIETLAAVFSGLVIEHLGRRPLLIGGFGLMGLFFGTLTITLTLQDHAPWVPYLSIVGILAIIASFCSGPGGIPFILTGEFFQQSQRPAAFIIAGTVNWLSNFAVGLLFPFIQKSLDTYCFLVFATICITGAIYLYFVLPETKNRTYAEISQAFSKRNKAYPPEEKIDSAVTDGKINGRP TTIF3GB TT Discontinued TTVQGI2 ID TTVQGI2 TTVQGI2 TN Mycobacterium Heat shock protein 65 (MycB groL2) TTVQGI2 UP P0A521 TTVQGI2 UC CH602_MYCBO TTVQGI2 SN Protein Cpn60-2; Heat shock protein 65; GroEL protein 2; Cell wall protein A; Antigen A; 65 kDa antigen; 60 kDa chaperonin 2 TTVQGI2 GN MycB groL2 TTVQGI2 FC Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. TTVQGI2 SQ MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKGAKEVETKEQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDPERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIGAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLTLENADLSLLGKARKVVVTKDETTIVEGAGDTDAIAGRVAQIRQEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVTLLQAAPTLDELKLEGDEATGANIVKVALEAPLKQIAFNSGLEPGVVAEKVRNLPAGHGLNAQTGVYEDLLAAGVADPVKVTRSALQNAASIAGLFLTTEAVVADKPEKEKASVPGGGDMGGMDF TTVQGI2 TT Discontinued TT0DBAO ID TT0DBAO TT0DBAO TN Polyamine unspecific (PLA) TT0DBAO UP Other molecule TT0DBAO UC NOUNIPROTAC TT0DBAO GN NO-GeName TT0DBAO TT Discontinued TTVXEGU ID TTVXEGU TTVXEGU TN ADAM10 messenger RNA (ADAM10 mRNA) TTVXEGU UP O14672 TTVXEGU UC ADA10_HUMAN TTVXEGU BC mRNA target TTVXEGU SN Mammalian disintegrinmetalloprotease (mRNA); MADM (mRNA); Kuzbanian protein homolog (mRNA); KUZ (mRNA); Disintegrin and metalloproteinase domaincontaining protein 10 (mRNA); Disintegrin and metalloproteinase domain-containing protein 10 (mRNA); CDw156 (mRNA); CD156c (mRNA); ADAM 10 (mRNA) TTVXEGU GN ADAM10 TTVXEGU FC Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3. May regulate the EFNA5-EPHA3 signaling. Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. TTVXEGU EC EC 3.4.24.81 TTVXEGU PD 6BE6; 6BDZ; 1M1I TTVXEGU SQ MVLLRVLILLLSWAAGMGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLRLDFHAHGRHFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIQTRGGTFYVEPAERYIKDRTLPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEVTQIPQEEHAANGPELLRKKRTTSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMDPSTCASTGSVQWSRHFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPQRQRPRESYQMGHMRR TTVXEGU TT Literature-reported TTVXEGU FM mRNA target TTVXEGU KE hsa05010:Alzheimer's disease; hsa05120:Epithelial cell signaling in Helicobacter pylori infection TTVXEGU RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-2122948:Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2660826:Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant; R-HSA-2691232:Constitutive Signaling by NOTCH1 HD Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-2979096:NOTCH2 Activation and Transmission of Signal to the Nucleus; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TT6SZNG ID TT6SZNG TT6SZNG TN Caspase 8 messenger RNA (CASP8 mRNA) TT6SZNG UP Q14790 TT6SZNG UC CASP8_HUMAN TT6SZNG BC mRNA target TT6SZNG SN MORT1-associated CED-3 homolog (mRNA); MCH5 (mRNA); MACH (mRNA); ICE-like apoptotic protease 5 (mRNA); FLICE (mRNA); FADD-like ICE (mRNA); FADD-homologous ICE/CED-3-like protease (mRNA); CASP-8 (mRNA); CAP4 (mRNA); Apoptotic protease Mch-5 (mRNA); Apoptotic cysteine protease (mRNA) TT6SZNG GN CASP8 TT6SZNG FC Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex. Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. TT6SZNG EC EC 3.4.22.61 TT6SZNG PD 5L08; 5JQE; 5H33; 5H31; 4ZBW TT6SZNG SQ MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFTLRKKLVFPSD TT6SZNG TT Literature-reported TT6SZNG FM mRNA target TT6SZNG KE hsa04115:p53 signaling pathway; hsa04210:Apoptosis; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05010:Alzheimer's disease; hsa05016:Huntington's disease; hsa05134:Legionellosis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05168:Herpes simplex infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05416:Viral myocarditis TT6SZNG RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-140534:Ligand-dependent caspase activation; R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-2562578:TRIF-mediated programmed cell death; R-HSA-264870:Caspase-mediated cleavage of cytoskeletal proteins; R-HSA-3371378:Regulation by c-FLIP; R-HSA-5213460:RIPK1-mediated regulated necrosis; R-HSA-5218900:CASP8 activity is inhibited; R-HSA-5357786:TNFR1-induced proapoptotic signaling; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5660668:CLEC7A/inflammasome pathway; R-HSA-5675482:Regulation of necroptotic cell death; R-HSA-69416:Dimerization of procaspase-8; R-HSA-75157:FasL/ CD95L signaling; R-HSA-75158:TRAIL signaling; R-HSA-933543:NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 TTXZEUS ID TTXZEUS TTXZEUS TN NEDD8-activating enzyme E1C (UBA3) TTXZEUS UP Q8TBC4 TTXZEUS UC UBA3_HUMAN TTXZEUS BC Carbon-sulfur ligase TTXZEUS SN Ubiquitin-like modifier-activating enzyme 3; Ubiquitin-activating enzyme E1C; Ubiquitin-activating enzyme 3; UBE1C; NEDD8-activating enzyme E1 catalytic subunit TTXZEUS GN UBA3 TTXZEUS FC E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression. Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. TTXZEUS EC EC 6.2.1.- TTXZEUS PD 5JJM; 3GZN; 3FN1; 3DBR; 3DBL TTXZEUS SQ MADGEEPEKKRRRIEELLAEKMAVDGGCGDTGDWEGRWNHVKKFLERSGPFTHPDFEPSTESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEHCIEYVRMLQWPKEQPFGEGVPLDGDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACSQLPQNIQFSPSAKLQEVLDYLTNSASLQMKSPAITATLEGKNRTLYLQSVTSIEERTRPNLSKTLKELGLVDGQELAVADVTTPQTVLFKLHFTS TTXZEUS TT Literature-reported TTXZEUS FM Carbon-nitrogen ligase TTXZEUS KE hsa04120:Ubiquitin mediated proteolysis TTXZEUS RC R-HSA-5607761:Dectin-1 mediated noncanonical NF-kB signaling; R-HSA-5676590:NIK-->noncanonical NF-kB signaling; R-HSA-983168:Antigen processing: Ubiquitination & Proteasome degradation TTE2KUJ ID TTE2KUJ TTE2KUJ TN Adenosylhomocysteinase (AHCY) TTE2KUJ UP P23526 TTE2KUJ UC SAHH_HUMAN TTE2KUJ BC Ether bond hydrolase TTE2KUJ SN SAHH; SAH hydrolase; S-adenosyl-L-homocysteine hydrolase TTE2KUJ GN AHCY TTE2KUJ FC Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. TTE2KUJ EC EC 3.3.1.1 TTE2KUJ PD 5W4B; 5W49; 4YVF; 4PGF; 4PFJ TTE2KUJ SQ MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHYRY TTE2KUJ TT Literature-reported TTE2KUJ FM Ether hydrolase TTE2KUJ KE hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways TTYG6BU ID TTYG6BU TTYG6BU TN Aggrecanase-1 (ADAMTS4) TTYG6BU UP O75173 TTYG6BU UC ATS4_HUMAN TTYG6BU BC Peptidase TTYG6BU SN Aggrecanase 1; ADMP-1; ADAMTS4; ADAM-TS4; ADAM-TS 4; A disintegrin and metalloproteinase with thrombospondin motifs 4 TTYG6BU GN ADAMTS4 TTYG6BU FC Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the '392-Glu-|-Ala-393' site. TTYG6BU EC EC 3.4.24.82 TTYG6BU PD 4WKI; 4WKE; 4WK7; 3B2Z; 2RJP TTYG6BU SQ MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK TTYG6BU TT Patented-recorded TTYG6BU RC R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-5173214:O-glycosylation of TSR domain-containing proteins TTO6SGY ID TTO6SGY TTO6SGY TN AKT3 messenger RNA (AKT3 mRNA) TTO6SGY UP Q9Y243 TTO6SGY UC AKT3_HUMAN TTO6SGY BC mRNA target TTO6SGY SN STK-2 (mRNA); RAC-PK-gamma (mRNA); Protein kinase B gamma (mRNA); Protein kinase Akt-3 (mRNA); PKBG (mRNA); PKB gamma (mRNA) TTO6SGY GN AKT3 TTO6SGY FC AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. TTO6SGY EC EC 2.7.11.1 TTO6SGY PD 2X18 TTO6SGY SQ MSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE TTO6SGY TT Literature-reported TTO6SGY FM mRNA target TTO6SGY KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04530:Tight junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04728:Dopaminergic synapse; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04922:Glucagon signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04973:Carbohydrate digestion and absorption; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTO6SGY RC R-HSA-111447:Activation of BAD and translocation to mitochondria; R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-198693:AKT phosphorylates targets in the nucleus; R-HSA-199418:Negative regulation of the PI3K/AKT network; R-HSA-211163:AKT-mediated inactivation of FOXO1A; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-5218920:VEGFR2 mediated vascular permeability; R-HSA-5628897:TP53 Regulates Metabolic Genes; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer TTAIWZN ID TTAIWZN TTAIWZN TN Apoptosis-2 messenger RNA (BIRC3 mRNA) TTAIWZN UP Q13489 TTAIWZN UC BIRC3_HUMAN TTAIWZN BC mRNA target TTAIWZN SN hIAP1 (mRNA); hIAP-1 (mRNA); TNFR2TRAFsignaling complex protein 1 (mRNA); TNFR2-TRAF-signaling complex protein 1 (mRNA); RNF49 (mRNA); RING-type E3 ubiquitin transferase BIRC3 (mRNA); RING finger protein 49 (mRNA); MIHC (mRNA); Inhibitor of apoptosis protein 1 (mRNA); IAP1 (mRNA); IAP homolog C (mRNA); CIAP2 (mRNA); C-IAP2 (mRNA); Baculoviral IAP repeatcontaining protein3 (mRNA); Baculoviral IAP repeat-containing protein 3 (mRNA); Apoptosis inhibitor 2 (mRNA); API2 (mRNA) TTAIWZN GN BIRC3 TTAIWZN FC Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. TTAIWZN EC EC 2.3.2.27 TTAIWZN PD 3M0D; 3M0A; 3EB6; 3EB5; 2UVL TTAIWZN SQ MNIVENSIFLSNLMKSANTFELKYDLSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKRGDSPTEKHKKLYPSCRFVQSLNSVNNLEATSQPTFPSSVTNSTHSLLPGTENSGYFRGSYSNSPSNPVNSRANQDFSALMRSSYHCAMNNENARLLTFQTWPLTFLSPTDLAKAGFYYIGPGDRVACFACGGKLSNWEPKDNAMSEHLRHFPKCPFIENQLQDTSRYTVSNLSMQTHAARFKTFFNWPSSVLVNPEQLASAGFYYVGNSDDVKCFCCDGGLRCWESGDDPWVQHAKWFPRCEYLIRIKGQEFIRQVQASYPHLLEQLLSTSDSPGDENAESSIIHFEPGEDHSEDAIMMNTPVINAAVEMGFSRSLVKQTVQRKILATGENYRLVNDLVLDLLNAEDEIREEERERATEEKESNDLLLIRKNRMALFQHLTCVIPILDSLLTAGIINEQEHDVIKQKTQTSLQARELIDTILVKGNIAATVFRNSLQEAEAVLYEHLFVQQDIKYIPTEDVSDLPVEEQLRRLQEERTCKVCMDKEVSIVFIPCGHLVVCKDCAPSLRKCPICRSTIKGTVRTFLS TTAIWZN TT Literature-reported TTAIWZN FM mRNA target TTAIWZN KE hsa04064:NF-kappa B signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa04210:Apoptosis; hsa04510:Focal adhesion; hsa04621:NOD-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa05145:Toxoplasmosis; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05222:Small cell lung cancer TTAIWZN RC R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-5213460:RIPK1-mediated regulated necrosis; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5675482:Regulation of necroptotic cell death; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway; R-HSA-937041:IKK complex recruitment mediated by RIP1 TT12ABZ ID TT12ABZ TT12ABZ TN Arachidonate 12-lipoxygenase (12-LOX) TT12ABZ UP P18054 TT12ABZ UC LOX12_HUMAN TT12ABZ BC Oxygenase TT12ABZ SN Platelet-type lipoxygenase 12; Lipoxin synthase 12-LO; LOG12; Arachidonate 12-lipoxygenase, 12S-type; 12S-lipoxygenase; 12S-LOX; 12LO; 12-lipoxygenase TT12ABZ GN ALOX12 TT12ABZ FC Mainly converts arachidonic acid to (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE but can also metabolize linoleic acid. Has a dual activity since it also converts leukotriene A4/LTA4 into both the bioactive lipoxin A4/LXA4 and lipoxin B4/LXB4. Through the production of specific bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation. It also probably positively regulates angiogenesis through regulation of the expression of the vascular endothelial growth factor. Plays a role in apoptotic process, promoting the survival of vascular smooth muscle cells for instance. May also play a role in the control of cell migration and proliferation. Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. TT12ABZ EC EC 1.13.11.31 TT12ABZ PD 3D3L; 2ABU TT12ABZ SQ MGRYRIRVATGAWLFSGSYNRVQLWLVGTRGEAELELQLRPARGEEEEFDHDVAEDLGLLQFVRLRKHHWLVDDAWFCDRITVQGPGACAEVAFPCYRWVQGEDILSLPEGTARLPGDNALDMFQKHREKELKDRQQIYCWATWKEGLPLTIAADRKDDLPPNMRFHEEKRLDFEWTLKAGALEMALKRVYTLLSSWNCLEDFDQIFWGQKSALAEKVRQCWQDDELFSYQFLNGANPMLLRRSTSLPSRLVLPSGMEELQAQLEKELQNGSLFEADFILLDGIPANVIRGEKQYLAAPLVMLKMEPNGKLQPMVIQIQPPNPSSPTPTLFLPSDPPLAWLLAKSWVRNSDFQLHEIQYHLLNTHLVAEVIAVATMRCLPGLHPIFKFLIPHIRYTMEINTRARTQLISDGGIFDKAVSTGGGGHVQLLRRAAAQLTYCSLCPPDDLADRGLLGLPGALYAHDALRLWEIIARYVEGIVHLFYQRDDIVKGDPELQAWCREITEVGLCQAQDRGFPVSFQSQSQLCHFLTMCVFTCTAQHAAINQGQLDWYAWVPNAPCTMRMPPPTTKEDVTMATVMGSLPDVRQACLQMAISWHLSRRQPDMVPLGHHKEKYFSGPKPKAVLNQFRTDLEKLEKEITARNEQLDWPYEYLKPSCIENSVTI TT12ABZ TT Literature-reported TT12ABZ FM Oxidoreductases acting on single donors TT12ABZ KE hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels TT0Z6Y2 ID TT0Z6Y2 TT0Z6Y2 TN ATP-citrate synthase (ACLY) TT0Z6Y2 UP P53396 TT0Z6Y2 UC ACLY_HUMAN TT0Z6Y2 BC Acyltransferase TT0Z6Y2 SN Citrate cleavage enzyme; ATP-citrate (pro-S-)-lyase; ACL TT0Z6Y2 GN ACLY TT0Z6Y2 FC ATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine. TT0Z6Y2 EC EC 2.3.3.8 TT0Z6Y2 PD 6QFB; 6O0H; 6HXM; 6HXL; 6HXK TT0Z6Y2 SQ MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALGHRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMSM TT0Z6Y2 TT Successful TT0Z6Y2 FM Acyltransferase TT0Z6Y2 KE hsa00020:Citrate cycle (TCA cycle); hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics TT0Z6Y2 RC R-HSA-163765:ChREBP activates metabolic gene expression; R-HSA-75105:Fatty Acyl-CoA Biosynthesis TTRVTMX ID TTRVTMX TTRVTMX TN Bacterial Beta-ketoacyl-ACP synthase III (Bact fabH) TTRVTMX UP P0A6R0 TTRVTMX UC FABH_ECOLI TTRVTMX BC Acyltransferase TTRVTMX SN KAS III; FabH; EcFabH; Condensing enzyme FabH; Beta-ketoacyl-acyl carrier protein synthase III; Acetoacetyl-acyl carrier protein synthase; Acetoacetyl-ACP synthase; 3-oxoacyl-[acyl-carrier-protein] synthase III TTRVTMX GN Bact fabH TTRVTMX FC Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain. TTRVTMX EC EC 2.3.1.180 TTRVTMX PD 5BNS; 5BNR; 5BNM; 4Z8D; 3IL9 TTRVTMX SQ MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPGIISTHLHADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF TTRVTMX TT Literature-reported TTRE6AX ID TTRE6AX TTRE6AX TN Bcl-x messenger RNA (BCL2L1 mRNA) TTRE6AX UP Q07817 TTRE6AX UC B2CL1_HUMAN TTRE6AX BC mRNA target TTRE6AX SN Bcl2like protein 1 (mRNA); Bcl2L1 (mRNA); Bcl2-L-1 (mRNA); Bcl-XL (mRNA); Bcl-2-like protein 1 (mRNA); BCLX (mRNA); BCL2L (mRNA); Apoptosis regulator Bcl-X (mRNA) TTRE6AX GN BCL2L1 TTRE6AX FC Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Potent inhibitor of cell death. TTRE6AX PD 6IJQ; 6F46; 6DCO; 6DCN; 6BF2 TTRE6AX SQ MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK TTRE6AX TT Literature-reported TTRE6AX FM mRNA target TTRE6AX KE hsa04014:Ras signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04630:Jak-STAT signaling pathway; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05145:Toxoplasmosis; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05212:Pancreatic cancer; hsa05220:Chronic myeloid leukemia; hsa05222:Small cell lung cancer TTRE6AX RC R-HSA-111453:BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members; R-HSA-844455:The NLRP1 inflammasome TT0L58T ID TT0L58T TT0L58T TN Bone morphogenetic protein 1 (BMP1) TT0L58T UP P13497 TT0L58T UC BMP1_HUMAN TT0L58T BC Peptidase TT0L58T SN Procollagen C-proteinase; PCP protein; PCOLC; Mammalian tolloid protein; MTld; BMP-1 TT0L58T GN BMP1 TT0L58T FC Induces cartilage and bone formation. May participate in dorsoventral patterning during early development by cleaving chordin (CHRD). Responsible for the proteolytic activation of lysyl oxidase LOX. Cleaves the C-terminal propeptides of procollagen I, II and III. TT0L58T EC EC 3.4.24.19 TT0L58T PD 6BTQ; 6BTP; 6BTO; 6BTN; 6BSM TT0L58T SQ MPGVARLPLLLGLLLLPRPGRPLDLADYTYDLAEEDDSEPLNYKDPCKAAAFLGDIALDEEDLRAFQVQQAVDLRRHTARKSSIKAAVPGNTSTPSCQSTNGQPQRGACGRWRGRSRSRRAATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCPACGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKLPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEAICGGDVKKDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEKPDDIKSTSSRLWLKFVSDGSINKAGFAVNFFKEVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRCEAACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCKEAGCDHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFMEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLATGSRMFLRFYSDNSVQRKGFQASHATECGGQVRADVKTKDLYSHAQFGDNNYPGGVDCEWVIVAEEGYGVELVFQTFEVEEETDCGYDYMELFDGYDSTAPRLGRYCGSGPPEEVYSAGDSVLVKFHSDDTITKKGFHLRYTSTKFQDTLHSRK TT0L58T TT Literature-reported TT0L58T FM Peptidase TT0L58T RC R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1650814:Collagen biosynthesis and modifying enzymes; R-HSA-2214320:Anchoring fibril formation TTF9OQ6 ID TTF9OQ6 TTF9OQ6 TN Branched-chain-amino-acid transaminase 2 (BCAT2) TTF9OQ6 UP O15382 TTF9OQ6 UC BCAT2_HUMAN TTF9OQ6 BC Transaminase TTF9OQ6 SN Placental protein 18; PP18; ECA39 protein; Branched-chain amino acid aminotransferase; BCAT2; BCAT(m); BCAT TTF9OQ6 GN BCAT2 TTF9OQ6 FC Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids. TTF9OQ6 EC EC 2.6.1.42 TTF9OQ6 PD 5MPR; 5I60; 5I5Y; 5I5X; 5I5W TTF9OQ6 SQ MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSLGVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIPTMENGPELILRFQKELKEIQYGIRAHEWMFPV TTF9OQ6 TT Literature-reported TTF9OQ6 KE hsa00280:Valine, leucine and isoleucine degradation; hsa00290:Valine, leucine and isoleucine biosynthesis; hsa00770:Pantothenate and CoA biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01210:2-Oxocarboxylic acid metabolism; hsa01230:Biosynthesis of amino acids TT7WZIJ ID TT7WZIJ TT7WZIJ TN CAAX farnesyltransferase beta (FNTB) TT7WZIJ UP P49356 TT7WZIJ UC FNTB_HUMAN TT7WZIJ BC Alkyl aryl transferase TT7WZIJ SN RAS proteins prenyltransferasebeta; FTase-beta; FNTB; CAAX farnesyltransferase beta subunit TT7WZIJ GN FNTB TT7WZIJ FC Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C- terminus of several proteins having the C-terminal sequence Cys- aliphatic-aliphatic-X. TT7WZIJ EC EC 2.5.1.58 TT7WZIJ PD 3.00E+37; 2IEJ; 2H6I; 2H6H; 2H6G TT7WZIJ SQ MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPVPGFEELKDETSAEPATD TT7WZIJ TT Literature-reported TT7WZIJ KE hsa00900:Terpenoid backbone biosynthesis; hsa01130:Biosynthesis of antibiotics TT7WZIJ RC R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade TTKW4ML ID TTKW4ML TTKW4ML TN Caspase 6 messenger RNA (CASP6 mRNA) TTKW4ML UP P55212 TTKW4ML UC CASP6_HUMAN TTKW4ML BC mRNA target TTKW4ML SN MCH2 (mRNA); Caspase-6 subunit p18 (mRNA); Caspase-6 subunit p11 (mRNA); CASP-6 (mRNA); Apoptotic protease Mch-2 (mRNA) TTKW4ML GN CASP6 TTKW4ML FC Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death. Involved in the activation cascade of caspases responsible for apoptosis execution. TTKW4ML EC EC 3.4.22.59 TTKW4ML PD 6DEV; 6DEU; 4NBN; 4NBL; 4NBK TTKW4ML SQ MSSASGLRRGHPAGGEENMTETDAFYKREMFDPAEKYKMDHRRRGIALIFNHERFFWHLTLPERRGTCADRDNLTRRFSDLGFEVKCFNDLKAEELLLKIHEVSTVSHADADCFVCVFLSHGEGNHIYAYDAKIEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVVDNQTEKLDTNITEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSQRRVDFCKDPSAIGKKQVPCFASMLTKKLHFFPKSN TTKW4ML TT Literature-reported TTKW4ML FM mRNA target TTKW4ML KE hsa04210:Apoptosis TTKW4ML RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-264870:Caspase-mediated cleavage of cytoskeletal proteins TTGECUM ID TTGECUM TTGECUM TN Cot oncogene messenger RNA (MAP3K8 mRNA) TTGECUM UP P41279 TTGECUM UC M3K8_HUMAN TTGECUM BC mRNA target TTGECUM SN Tumor progression locus 2 (mRNA); TPL-2 (mRNA); Serine/threonine-protein kinase cot (mRNA); Proto-oncogene c-Cot (mRNA); Mitogen-activated protein kinase kinase kinase 8 (mRNA); ESTF (mRNA); Cancer Osaka thyroid oncogene (mRNA); COT (mRNA) TTGECUM GN MAP3K8 TTGECUM FC Involved in the regulation of T-helper cell differentiation and IFNG expression in T-cells. Involved in mediating host resistance to bacterial infection through negative regulation of type I interferon (IFN) production. In vitro, activates MAPK/ERK pathway in response to IL1 in an IRAK1-independent manner, leading to up-regulation of IL8 and CCL4. Transduces CD40 and TNFRSF1A signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. May also play a role in the transduction of TNF signals that activate JNK and NF-kappa-B in some cell types. In adipocytes, activates MAPK/ERK pathway in an IKBKB-dependent manner in response to IL1B and TNF, but not insulin, leading to induction of lipolysis. Plays a role in the cell cycle. Isoform 1 shows some transforming activity, although it is much weaker than that of the activated oncogenic variant. Required for lipopolysaccharide (LPS)-induced, TLR4-mediated activation of the MAPK/ERK pathway in macrophages, thus being critical for production of the proinflammatory cytokine TNF-alpha (TNF) during immune responses. TTGECUM EC EC 2.7.11.25 TTGECUM PD 5IU2; 4Y85; 4Y83 TTGECUM SQ MEYMSTGSDNKEEIDLLIKHLNVSDVIDIMENLYASEEPAVYEPSLMTMCQDSNQNDERSKSLLLSGQEVPWLSSVRYGTVEDLLAFANHISNTAKHFYGQRPQESGILLNMVITPQNGRYQIDSDVLLIPWKLTYRNIGSDFIPRGAFGKVYLAQDIKTKKRMACKLIPVDQFKPSDVEIQACFRHENIAELYGAVLWGETVHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKKVIHHDIKPSNIVFMSTKAVLVDFGLSVQMTEDVYFPKDLRGTEIYMSPEVILCRGHSTKADIYSLGATLIHMQTGTPPWVKRYPRSAYPSYLYIIHKQAPPLEDIADDCSPGMRELIEASLERNPNHRPRAADLLKHEALNPPREDQPRCQSLDSALLERKRLLSRKELELPENIADSSCTGSTEESEMLKRQRSLYIDLGALAGYFNLVRGPPTLEYG TTGECUM TT Literature-reported TTGECUM FM mRNA target TTGECUM KE hsa04010:MAPK signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04668:TNF signaling pathway TTGECUM RC R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-5684264:MAP3K8 (TPL2)-dependent MAPK1/3 activation TTVW6QL ID TTVW6QL TTVW6QL TN CSF1R messenger RNA (CSF1R mRNA) TTVW6QL UP P07333 TTVW6QL UC CSF1R_HUMAN TTVW6QL BC mRNA target TTVW6QL SN Proto-oncogene c-Fms (mRNA); M-CSF-R (mRNA); FMS (mRNA); CSF-1R (mRNA); CSF-1-R (mRNA); CSF-1 receptor (mRNA); CD115 (mRNA) TTVW6QL GN CSF1R TTVW6QL FC Promotes the release of proinflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor. Tyrosine-protein kinase that acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. TTVW6QL EC EC 2.7.10.1 TTVW6QL PD 4WRM; 4WRL; 4R7I; 4R7H; 4LIQ TTVW6QL SQ MGPGVLLLLLVATAWHGQGIPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGAHTHPPDEFLFTPVVVACMSIMALLLLLLLLLLYKYKQKPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGVDYKNIHLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSNDSFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQAQEDRRERDYTNLPSSSRSGGSGSSSSELEEESSSEHLTCCEQGDIAQPLLQPNNYQFC TTVW6QL TT Literature-reported TTVW6QL FM mRNA target TTBO2A9 ID TTBO2A9 TTBO2A9 TN Deoxyhypusine synthase (DHPS) TTBO2A9 UP P49366 TTBO2A9 UC DHYS_HUMAN TTBO2A9 BC Alkyl aryl transferase TTBO2A9 SN DHS TTBO2A9 GN DHPS TTBO2A9 FC Catalyzes the NAD-dependent oxidativecleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. TTBO2A9 EC EC 2.5.1.46 TTBO2A9 PD 1RQD; 1ROZ; 1RLZ; 1DHS TTBO2A9 SQ MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFGRAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLVQHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFEDWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGSLGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGADYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMDAFMHEKNED TTBO2A9 TT Literature-reported TTZGCP6 ID TTZGCP6 TTZGCP6 TN EIF4E messenger RNA (EIF4E mRNA) TTZGCP6 UP P06730 TTZGCP6 UC IF4E_HUMAN TTZGCP6 BC mRNA target TTZGCP6 SN mRNA capbinding protein (mRNA); mRNA cap-binding protein (mRNA); eIF4F 25 kDa subunit (mRNA); eIF4E (mRNA); eIF-4F 25 kDa subunit (mRNA); eIF-4E (mRNA); Eukaryotic translation initiation factor 4E (mRNA); EIF4F (mRNA); EIF4EL1 (mRNA) TTZGCP6 GN EIF4E TTZGCP6 FC Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates the binding to the mRNA cap. Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. TTZGCP6 PD 5ZML; 5ZK9; 5ZK7; 5ZK5; 5ZJZ TTZGCP6 SQ MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV TTZGCP6 TT Literature-reported TTZGCP6 FM mRNA target TTZGCP6 KE hsa03013:RNA transport; hsa04066:HIF-1 signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04910:Insulin signaling pathway TTZGCP6 RC R-HSA-1169408:ISG15 antiviral mechanism; R-HSA-166208:mTORC1-mediated signalling TTQ9RYT ID TTQ9RYT TTQ9RYT TN Endothelin-converting enzyme 1 (ECE1) TTQ9RYT UP P42892 TTQ9RYT UC ECE1_HUMAN TTQ9RYT BC Peptidase TTQ9RYT SN ECE-1 TTQ9RYT GN ECE1 TTQ9RYT FC Converts big endothelin-1 to endothelin-1. TTQ9RYT EC EC 3.4.24.71 TTQ9RYT PD 3DWB TTQ9RYT SQ MRGVWPPPVSALLSALGMSTYKRATLDEEDLVDSLSEGDAYPNGLQVNFHSPRSGQRCWAARTQVEKRLVVLVVLLAAGLVACLAALGIQYQTRSPSVCLSEACVSVTSSILSSMDPTVDPCHDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILEIKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPPGSPMNPPHKCEVW TTQ9RYT TT Literature-reported TTWALCO ID TTWALCO TTWALCO TN HER4 messenger RNA (ERBB4 mRNA) TTWALCO UP Q15303 TTWALCO UC ERBB4_HUMAN TTWALCO BC mRNA target TTWALCO SN Tyrosine kinase-type cell surface receptor HER4 (mRNA); Receptor tyrosine-protein kinase erbB-4 (mRNA); Proto-oncogene-like protein c-ErbB-4 (mRNA); P180erbB4 (mRNA); HER4 (mRNA) TTWALCO GN ERBB4 TTWALCO FC Required for normal cardiac muscle differentiation during embryonic development, and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system, especially for normal neural crest cell migration and normal axon guidance. Required for mammary gland differentiation, induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1, NRG2, NRG3 and NRG4 and the EGF family members BTC, EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alternative splicing, proteolytic processing, and by the formation of heterodimers with other ERBB family members, thereby creating multiple combinations of intracellular phosphotyrosines that trigger ligand- and context-specific cellular responses. Mediates phosphorylation of SHC1 and activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Isoform JM-A CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the activation of phosphatidylinositol 3-kinase and AKT1 and protect cells against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate reorganization of the actin cytoskeleton and promote cell migration in response to NRG1. Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the phosphotyrosine that mediates interaction with PIK3R1, and hence do not phosphorylate PIK3R1, do not protect cells against apoptosis, and do not promote reorganization of the actin cytoskeleton and cell migration. Proteolytic processing of isoform JM-A CYT-1 and isoform JM-A CYT-2 gives rise to the corresponding soluble intracellular domains (4ICD) that translocate to the nucleus, promote nuclear import of STAT5A, activation of STAT5A, mammary epithelium differentiation, cell proliferation and activation of gene expression. The ERBB4 soluble intracellular domains (4ICD) colocalize with STAT5A at the CSN2 promoter to regulate transcription of milk proteins during lactation. The ERBB4 soluble intracellular domains can also translocate to mitochondria and promote apoptosis. Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart, the central nervous system and the mammary gland, gene transcription, cell proliferation, differentiation, migration and apoptosis. TTWALCO EC EC 2.7.10.1 TTWALCO PD 3U9U; 3U7U; 3U2P; 3BCE; 3BBW TTWALCO SQ MKPATGLWVWVSLLVAAGTVQPSDSQSVCAGTENKLSSLSDLEQQYRALRKYYENCEVVMGNLEITSIEHNRDLSFLRSVREVTGYVLVALNQFRYLPLENLRIIRGTKLYEDRYALAIFLNYRKDGNFGLQELGLKNLTEILNGGVYVDQNKFLCYADTIHWQDIVRNPWPSNLTLVSTNGSSGCGRCHKSCTGRCWGPTENHCQTLTRTVCAEQCDGRCYGPYVSDCCHRECAGGCSGPKDTDCFACMNFNDSGACVTQCPQTFVYNPTTFQLEHNFNAKYTYGAFCVKKCPHNFVVDSSSCVRACPSSKMEVEENGIKMCKPCTDICPKACDGIGTGSLMSAQTVDSSNIDKFINCTKINGNLIFLVTGIHGDPYNAIEAIDPEKLNVFRTVREITGFLNIQSWPPNMTDFSVFSNLVTIGGRVLYSGLSLLILKQQGITSLQFQSLKEISAGNIYITDNSNLCYYHTINWTTLFSTINQRIVIRDNRKAENCTAEGMVCNHLCSSDGCWGPGPDQCLSCRRFSRGRICIESCNLYDGEFREFENGSICVECDPQCEKMEDGLLTCHGPGPDNCTKCSHFKDGPNCVEKCPDGLQGANSFIFKYADPDRECHPCHPNCTQGCNGPTSHDCIYYPWTGHSTLPQHARTPLIAAGVIGGLFILVIVGLTFAVYVRRKSIKKKRALRRFLETELVEPLTPSGTAPNQAQLRILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVTQLMPHGCLLEYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYLVIQGDDRMKLPSPNDSKFFQNLLDEEDLEDMMDAEEYLVPQAFNIPPPIYTSRARIDSNRSEIGHSPPPAYTPMSGNQFVYRDGGFAAEQGVSVPYRAPTSTIPEAPVAQGATAEIFDDSCCNGTLRKPVAPHVQEDSSTQRYSADPTVFAPERSPRGELDEEGYMTPMRDKPKQEYLNPVEENPFVSRRKNGDLQALDNPEYHNASNGPPKAEDEYVNEPLYLNTFANTLGKAEYLKNNILSMPEKAKKAFDNPDYWNHSLPPRSTLQHPDYLQEYSTKYFYKQNGRIRPIVAENPEYLSEFSLKPGTVLPPPPYRHRNTVV TTWALCO TT Literature-reported TTWALCO FM mRNA target TTWALCO KE hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04144:Endocytosis; hsa05205:Proteoglycans in cancer TT1F8OQ ID TT1F8OQ TT1F8OQ TN IKKA messenger RNA (IKKA mRNA) TT1F8OQ UP O15111 TT1F8OQ UC IKKA_HUMAN TT1F8OQ BC mRNA target TT1F8OQ SN Transcription factor 16 (mRNA); TCF16 (mRNA); TCF-16 (mRNA); Nuclear factor NFkappaB inhibitor kinase alpha (mRNA); Nuclear factor NF-kappa-B inhibitor kinase alpha (mRNA); NFKBIKA (mRNA); Inhibitory kappa B kinasea (mRNA); Inhibitor of nuclear factor kappa-B kinase subunit alpha (mRNA); IkappaB kinase (mRNA); IkBKA (mRNA); IKK1 (mRNA); IKK-alpha (mRNA); IKK-A (mRNA); I-kappa-B kinase alpha (mRNA); I-kappa-B kinase 1 (mRNA); I kappa-B kinase alpha (mRNA); Conserved helix-loop-helix ubiquitous kinase (mRNA) TT1F8OQ GN CHUK TT1F8OQ FC Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Participates also in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities. Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP. Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor. Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. TT1F8OQ EC EC 2.7.11.10 TT1F8OQ PD 5TQY; 5TQX; 5TQW; 5EBZ; 3BRT TT1F8OQ SQ MERPPGLRPGAGGPWEMRERLGTGGFGNVCLYQHRELDLKIAIKSCRLELSTKNRERWCHEIQIMKKLNHANVVKACDVPEELNILIHDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIIHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMSGEVRFSSHLPQPNSLCSLVVEPMENWLQLMLNWDPQQRGGPVDLTLKQPRCFVLMDHILNLKIVHILNMTSAKIISFLLPPDESLHSLQSRIERETGINTGSQELLSETGISLDPRKPASQCVLDGVRGCDSYMVYLFDKSKTVYEGPFASRSLSDCVNYIVQDSKIQLPIIQLRKVWAEAVHYVSGLKEDYSRLFQGQRAAMLSLLRYNANLTKMKNTLISASQQLKAKLEFFHKSIQLDLERYSEQMTYGISSEKMLKAWKEMEEKAIHYAEVGVIGYLEDQIMSLHAEIMELQKSPYGRRQGDLMESLEQRAIDLYKQLKHRPSDHSYSDSTEMVKIIVHTVQSQDRVLKELFGHLSKLLGCKQKIIDLLPKVEVALSNIKEADNTVMFMQGKRQKEIWHLLKIACTQSSARSLVGSSLEGAVTPQTSAWLPPTSAEHDHSLSCVVTPQDGETSAQMIEENLNCLGHLSTIIHEANEEQGNSMMNLDWSWLTE TT1F8OQ TT Literature-reported TT1F8OQ FM mRNA target TT1F8OQ KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04062:Chemokine signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04068:FoxO signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04668:TNF signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05212:Pancreatic cancer; hsa05215:Prostate cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer TT1F8OQ RC R-HSA-1169091:Activation of NF-kappaB in B cells; R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-1810476:RIP-mediated NFkB activation via ZBP1; R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-446652:Interleukin-1 signaling; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5602636:IKBKB deficiency causes SCID; R-HSA-5603027:IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR); R-HSA-5603029:IkBA variant leads to EDA-ID; R-HSA-5607761:Dectin-1 mediated noncanonical NF-kB signaling; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer; R-HSA-5676590:NIK-->noncanonical NF-kB signaling; R-HSA-5684264:MAP3K8 (TPL2)-dependent MAPK1/3 activation; R-HSA-933542:TRAF6 mediated NF-kB activation; R-HSA-933543:NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10; R-HSA-937039:IRAK1 recruits IKK complex; R-HSA-937041:IKK complex recruitment mediated by RIP1; R-HSA-975144:IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation TT329V4 ID TT329V4 TT329V4 TN Inward rectifier potassium channel Kir6.2 (KCNJ11) TT329V4 UP Q14654 TT329V4 UC KCJ11_HUMAN TT329V4 BC Inward rectifier potassium channel TT329V4 SN Potassium channel, inwardly rectifying, subfamily J, member 11; KCNJ11; KATP channel (Kir6.2/SUR2A); Inward rectifier K+ channel Kir6.2; IKATP TT329V4 GN KCNJ11 TT329V4 FC This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium. Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation. TT329V4 PD 6C3P; 6C3O TT329V4 SQ MLSRKGIIPEEYVLTRLAEDPAEPRYRARQRRARFVSKKGNCNVAHKNIREQGRFLQDVFTTLVDLKWPHTLLIFTMSFLCSWLLFAMAWWLIAFAHGDLAPSEGTAEPCVTSIHSFSSAFLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAETLIFSKHAVIALRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPMENGVGGNSIFLVAPLIIYHVIDANSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQARTSYLADEILWGQRFVPIVAEEDGRYSVDYSKFGNTIKVPTPLCTARQLDEDHSLLEALTLASARGPLRKRSVPMAKAKPKFSISPDSLS TT329V4 TT Literature-reported TT329V4 KE hsa04911:Insulin secretion; hsa04930:Type II diabetes mellitus TT329V4 RC R-HSA-382556:ABC-family proteins mediated transport; R-HSA-422356:Regulation of insulin secretion TTILUKB ID TTILUKB TTILUKB TN IRAK4 messenger RNA (IRAK4 mRNA) TTILUKB UP Q9NWZ3 TTILUKB UC IRAK4_HUMAN TTILUKB BC mRNA target TTILUKB SN Renal carcinoma antigenNYREN64 (mRNA); Renal carcinoma antigen NY-REN-64 (mRNA); NY-REN-64 antigen (mRNA); Interleukin1 receptorassociated kinase 4 (mRNA); Interleukin-1 receptor-associated kinase 4 (mRNA); IRAK-4 (mRNA) TTILUKB GN IRAK4 TTILUKB FC Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections. Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. TTILUKB EC EC 2.7.11.1 TTILUKB PD 6O9D; 6O95; 6O94; 6O8U; 6N8G TTILUKB SQ MNKPITPSTYVRCLNVGLIRKLSDFIDPQEGWKKLAVAIKKPSGDDRYNQFHIRRFEALLQTGKSPTSELLFDWGTTNCTVGDLVDLLIQNEFFAPASLLLPDAVPKTANTLPSKEAITVQQKQMPFCDKDRTLMTPVQNLEQSYMPPDSSSPENKSLEVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS TTILUKB TT Literature-reported TTILUKB FM mRNA target TTILUKB KE hsa04064:NF-kappa B signaling pathway; hsa04210:Apoptosis; hsa04620:Toll-like receptor signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05162:Measles; hsa05164:Influenza A TTILUKB RC R-HSA-166058:MyD88:Mal cascade initiated on plasma membrane; R-HSA-446652:Interleukin-1 signaling; R-HSA-5602498:MyD88 deficiency (TLR2/4); R-HSA-5602680:MyD88 deficiency (TLR5); R-HSA-5603037:IRAK4 deficiency (TLR5); R-HSA-5603041:IRAK4 deficiency (TLR2/4); R-HSA-975110:TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling; R-HSA-975138:TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation; R-HSA-975155:MyD88 dependent cascade initiated on endosome; R-HSA-975871:MyD88 cascade initiated on plasma membrane TT3IVG2 ID TT3IVG2 TT3IVG2 TN JNK2 messenger RNA (JNK2 mRNA) TT3IVG2 UP P45984 TT3IVG2 UC MK09_HUMAN TT3IVG2 BC mRNA target TT3IVG2 SN Stress-activated protein kinase 1a (mRNA); SAPK1a (mRNA); PRKM9 (mRNA); Mitogen-activated protein kinase 9 (mRNA); Mitogen-activated protein kinase 8-interacting protein 2 (mRNA); MAPK 9 (mRNA); MAP kinase 9 (mRNA); Jun-N-terminal kinase 2 (mRNA); JNK-interacting protein 2 (mRNA); JNK-55 (mRNA); JNK MAP kinase scaffold protein 2 (mRNA); JIP-2 (mRNA); Islet-brain-2 (mRNA); IB-2 (mRNA); C-jun-amino-terminal kinase interacting protein 2 (mRNA); C-Jun N-terminal kinase 2 (mRNA) TT3IVG2 GN MAPK9 TT3IVG2 FC Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation. Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. TT3IVG2 EC EC 2.7.11.24 TT3IVG2 PD 3NPC; 3E7O TT3IVG2 SQ MSDSKCDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGCVIFQGTDHIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVVKDQPSDAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR TT3IVG2 TT Literature-reported TT3IVG2 FM mRNA target TT3IVG2 KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04024:cAMP signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04141:Protein processing in endoplasmic reticulum; hsa04310:Wnt signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04723:Retrograde endocannabinoid signaling; hsa04728:Dopaminergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04917:Prolactin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05210:Colorectal cancer; hsa05212:Pancreatic cancer; hsa05231:Choline metabolism in cancer TT3IVG2 RC R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-450321:JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1; R-HSA-450341:Activation of the AP-1 family of transcription factors TT7O8ZA ID TT7O8ZA TT7O8ZA TN Lanosterol synthase (LSS) TT7O8ZA UP P48449 TT7O8ZA UC ERG7_HUMAN TT7O8ZA BC Intramolecular transferases TT7O8ZA SN Oxidosqualene--lanosterol cyclase; Oxidosqualene cyclase; OSC; LSS; 2,3-epoxysqualene--lanosterol cyclase TT7O8ZA GN LSS TT7O8ZA FC Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus. TT7O8ZA EC EC 5.4.99.7 TT7O8ZA PD 1W6K; 1W6J TT7O8ZA SQ MTEGTCLRRRGGPYKTEPATDLGRWRLNCERGRQTWTYLQDERAGREQTGLEAYALGLDTKNYFKDLPKAHTAFEGALNGMTFYVGLQAEDGHWTGDYGGPLFLLPGLLITCHVARIPLPAGYREEIVRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVSLRILGVGPDDPDLVRARNILHKKGGAVAIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPDWAPAHPSTLWCHCRQVYLPMSYCYAVRLSAAEDPLVQSLRQELYVEDFASIDWLAQRNNVAPDELYTPHSWLLRVVYALLNLYEHHHSAHLRQRAVQKLYEHIVADDRFTKSISIGPISKTINMLVRWYVDGPASTAFQEHVSRIPDYLWMGLDGMKMQGTNGSQIWDTAFAIQALLEAGGHHRPEFSSCLQKAHEFLRLSQVPDNPPDYQKYYRQMRKGGFSFSTLDCGWIVSDCTAEALKAVLLLQEKCPHVTEHIPRERLCDAVAVLLNMRNPDGGFATYETKRGGHLLELLNPSEVFGDIMIDYTYVECTSAVMQALKYFHKRFPEHRAAEIRETLTQGLEFCRRQQRADGSWEGSWGVCFTYGTWFGLEAFACMGQTYRDGTACAEVSRACDFLLSRQMADGGWGEDFESCEERRYLQSAQSQIHNTCWAMMGLMAVRHPDIEAQERGVRCLLEKQLPNGDWPQENIAGVFNKSCAISYTSYRNIFPIWALGRFSQLYPERALAGHP TT7O8ZA TT Literature-reported TT7O8ZA KE hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics TT7O8ZA RC R-HSA-191273:Cholesterol biosynthesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP) TT9TE0O ID TT9TE0O TT9TE0O TN Mdm2 messenger RNA (MDM2 mRNA) TT9TE0O UP Q00987 TT9TE0O UC MDM2_HUMAN TT9TE0O BC mRNA target TT9TE0O SN RING-type E3 ubiquitin transferase Mdm2 (mRNA); P53-binding protein Mdm2 (mRNA); Oncoprotein Mdm2 (mRNA); MDM2 protein (mRNA); Hdm2 (mRNA); E3 ubiquitin-protein ligase Mdm2 (mRNA); Double minute 2 protein (mRNA) TT9TE0O GN MDM2 TT9TE0O FC Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation. Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells. Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis. E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. TT9TE0O EC EC 2.3.2.27 TT9TE0O PD 6Q9O; 6Q9L; 6Q9H; 6Q96; 6IM9 TT9TE0O SQ MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP TT9TE0O TT Literature-reported TT9TE0O FM mRNA target TT9TE0O KE hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia TT9TE0O RC R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559585:Oncogene Induced Senescence; R-HSA-399719:Trafficking of AMPA receptors; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer; R-HSA-69541:Stabilization of p53 TT8H9GB ID TT8H9GB TT8H9GB TN MEK2 messenger RNA (MEK2 mRNA) TT8H9GB UP P36507 TT8H9GB UC MP2K2_HUMAN TT8H9GB BC mRNA target TT8H9GB SN PRKMK2 (mRNA); MKK2 (mRNA); MEK 2 (mRNA); MAPKK 2 (mRNA); MAPK/ERK kinase 2 (mRNA); MAP kinase kinase 2 (mRNA); Dual specificity mitogenactivated protein kinase kinase 2 (mRNA); Dual specificity mitogen-activated protein kinase kinase 2 (mRNA) TT8H9GB GN MAP2K2 TT8H9GB FC Activates the ERK1 and ERK2 MAP kinases. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. TT8H9GB EC EC 2.7.12.2 TT8H9GB PD 4H3Q; 1S9I TT8H9GB SQ MLARRKPVLPALTINPTIAEGPSPTSEGASEANLVDLQKKLEELELDEQQKKRLEAFLTQKAKVGELKDDDFERISELGAGNGGVVTKVQHRPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMAPERLQGTHYSVQSDIWSMGLSLVELAVGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISPRPRPPGRPVSGHGMDSRPAMAIFELLDYIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERADLKMLTNHTFIKRSEVEEVDFAGWLCKTLRLNQPGTPTRTAV TT8H9GB TT Literature-reported TT8H9GB FM mRNA target TT8H9GB KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04370:VEGF signaling pathway; hsa04540:Gap junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04620:Toll-like receptor signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05020:Prion diseases; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TT8H9GB RC R-HSA-112411:MAPK1 (ERK2) activation; R-HSA-5210891:Uptake and function of anthrax toxins; R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5674499:Negative feedback regulation of MAPK pathway TT6804T ID TT6804T TT6804T TN MIF messenger RNA (MIF mRNA) TT6804T UP P14174 TT6804T UC MIF_HUMAN TT6804T BC mRNA target TT6804T SN Phenylpyruvate tautomerase (mRNA); MMIF (mRNA); L-dopachrome tautomerase (mRNA); L-dopachrome isomerase (mRNA); Glycosylation-inhibiting factor (mRNA); GLIF (mRNA); GIF (mRNA) TT6804T GN MIF TT6804T FC Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity. Pro-inflammatory cytokine. TT6804T EC EC 5.3.2.1 TT6804T PD 6FVH; 6FVE; 6CBH; 6CBG; 6CBF TT6804T SQ MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA TT6804T TT Literature-reported TT6804T FM mRNA target TT6804T KE hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism TT9FN4J ID TT9FN4J TT9FN4J TN Mixed lineage kinase 2 (MAP3K10) TT9FN4J UP Q02779 TT9FN4J UC M3K10_HUMAN TT9FN4J BC Kinase TT9FN4J SN Protein kinase MST; Mitogen-activated protein kinase kinase kinase 10; MST; MLK2 TT9FN4J GN MAP3K10 TT9FN4J FC Activates the JUN N-terminal pathway. TT9FN4J EC EC 2.7.11.25 TT9FN4J PD 2RF0 TT9FN4J SQ MEEEEGAVAKEWGTTPAGPVWTAVFDYEAAGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPGAPAAPAGLQLPQEIPFHELQLEEIIGVGGFGKVYRALWRGEEVAVKAARLDPEKDPAVTAEQVCQEARLFGALQHPNIIALRGACLNPPHLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREMDIVERELHLLMCQLSQEKPRVRKRKGNFKRSRLLKLREGGSHISLPSGFEHKITVQASPTLDKRKGSDGASPPASPSIIPRLRAIRLTPVDCGGSSSGSSSGGSGTWSRGGPPKKEELVGGKKKGRTWGPSSTLQKERVGGEERLKGLGEGSKQWSSSAPNLGKSPKHTPIAPGFASLNEMEEFAEAEDGGSSVPPSPYSTPSYLSVPLPAEPSPGARAPWEPTPSAPPARWGHGARRRCDLALLGCATLLGAVGLGADVAEARAADGEEQRRWLDGLFFPRAGRFPRGLSPPARPHGRREDVGPGLGLAPSATLVSLSSVSDCNSTRSLLRSDSDEAAPAAPSPPPSPPAPTPTPSPSTNPLVDLELESFKKDPRQSLTPTHVTAACAVSRGHRRTPSDGALGQRGPPEPAGHGPGPRDLLDFPRLPDPQALFPARRRPPEFPGRPTTLTFAPRPRPAASRPRLDPWKLVSFGRTLTISPPSRPDTPESPGPPSVQPTLLDMDMEGQNQDSTVPLCGAHGSH TT9FN4J TT Literature-reported TT9FN4J FM Kinase TTETX6Q ID TTETX6Q TTETX6Q TN Mixed lineage kinase 3 (MAP3K11) TTETX6Q UP Q16584 TTETX6Q UC M3K11_HUMAN TTETX6Q BC Kinase TTETX6Q SN Src-homology 3 domain-containing proline-rich kinase; SPRK; SH3 domain-containing proline-rich kinase; Protein-tyrosine kinase PTK1; PTK1; Mixed-lineage protein kinase 3; Mitogen-activated protein kinase kinase kinase 11; MLK3 TTETX6Q GN MAP3K11 TTETX6Q FC Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle. Activates the JUN N-terminal pathway. TTETX6Q EC EC 2.7.11.25 TTETX6Q PD 6CQ7; 6AQB; 5K28; 5K26 TTETX6Q SQ MEPLKSLFLKSPLGSWNGSGSGGGGGGGGGRPEGSPKAAGYANPVWTALFDYEPSGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIESDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEALEAQVLREMPRDSFHSMQEGWKREIQGLFDELRAKEKELLSREEELTRAAREQRSQAEQLRRREHLLAQWELEVFERELTLLLQQVDRERPHVRRRRGTFKRSKLRARDGGERISMPLDFKHRITVQASPGLDRRRNVFEVGPGDSPTFPRFRAIQLEPAEPGQAWGRQSPRRLEDSSNGERRACWAWGPSSPKPGEAQNGRRRSRMDEATWYLDSDDSSPLGSPSTPPALNGNPPRPSLEPEEPKRPVPAERGSSSGTPKLIQRALLRGTALLASLGLGRDLQPPGGPGRERGESPTTPPTPTPAPCPTEPPPSPLICFSLKTPDSPPTPAPLLLDLGIPVGQRSAKSPRREEEPRGGTVSPPPGTSRSAPGTPGTPRSPPLGLISRPRPSPLRSRIDPWSFVSAGPRPSPLPSPQPAPRRAPWTLFPDSDPFWDSPPANPFQGGPQDCRAQTKDMGAQAPWVPEAGP TTETX6Q TT Literature-reported TTETX6Q FM Kinase TTETX6Q KE mmu04010:MAPK signaling pathway; mmu04932:Non-alcoholic fatty liver disease (NAFLD) TTLZS4Q ID TTLZS4Q TTLZS4Q TN M-phase inducer phosphatase 1 (MPIP1) TTLZS4Q UP P30304 TTLZS4Q UC MPIP1_HUMAN TTLZS4Q BC Phosphoric monoester hydrolase TTLZS4Q SN Dual specificity phosphatase Cdc25A; Cdc25A phosphatase TTLZS4Q GN CDC25A TTLZS4Q FC Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro. Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. TTLZS4Q EC EC 3.1.3.48 TTLZS4Q PD 1C25 TTLZS4Q SQ MELGPEPPHRRRLLFACSPPPASQPVVKALFGASAAGGLSPVTNLTVTMDQLQGLGSDYEQPLEVKNNSNLQRMGSSESTDSGFCLDSPGPLDSKENLENPMRRIHSLPQKLLGCSPALKRSHSDSLDHDIFQLIDPDENKENEAFEFKKPVRPVSRGCLHSHGLQEGKDLFTQRQNSAPARMLSSNERDSSEPGNFIPLFTPQSPVTATLSDEDDGFVDLLDGENLKNEEETPSCMASLWTAPLVMRTTNLDNRCKLFDSPSLCSSSTRSVLKRPERSQEESPPGSTKRRKSMSGASPKESTNPEKAHETLHQSLSLASSPKGTIENILDNDPRDLIGDFSKGYLFHTVAGKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSERGPRMCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPMHHEDFKEDLKKFRTKSRTWAGEKSKREMYSRLKKL TTLZS4Q TT Literature-reported TTLZS4Q FM Phosphoric monoester hydrolases TTLZS4Q KE hsa04110:Cell cycle; hsa04914:Progesterone-mediated oocyte maturation; hsa05206:MicroRNAs in cancer TTLZS4Q RC R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-1538133:G0 and Early G1; R-HSA-156711:Polo-like kinase mediated events; R-HSA-157881:Cyclin B2 mediated events; R-HSA-176187:Activation of ATR in response to replication stress; R-HSA-69202:Cyclin E associated events during G1/S transition; R-HSA-69205:G1/S-Specific Transcription; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition; R-HSA-69601:Ubiquitin Mediated Degradation of Phosphorylated Cdc25A; R-HSA-69656:Cyclin A:Cdk2-associated events at S phase entry TTESBNC ID TTESBNC TTESBNC TN M-phase inducer phosphatase 3 (MPIP3) TTESBNC UP P30307 TTESBNC UC MPIP3_HUMAN TTESBNC BC Phosphoric monoester hydrolase TTESBNC SN Dual specificity phosphatase Cdc25C; Cdc25C phosphatase TTESBNC GN CDC25C TTESBNC FC Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity. Functions as a dosage-dependent inducer in mitotic control. TTESBNC EC EC 3.1.3.48 TTESBNC PD 5M37; 5M36; 5M35; 3OP3; 3BZI TTESBNC SQ MSTELFSSTREEGSSGSGPSFRSNQRKMLNLLLERDTSFTVCPDVPRTPVGKFLGDSANLSILSGGTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSPAQLLCSTPNGLDRGHRKRDAMCSSSANKENDNGNLVDSEMKYLGSPITTVPKLDKNPNLGEDQAEEISDELMEFSLKDQEAKVSRSGLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVKKKYFSGQGKLRKGLCLKKTVSLCDITITQMLEEDSNQGHLIGDFSKVCALPTVSGKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQYPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHKTELLRCRSQSKVQEGERQLREQIALLVKDMSP TTESBNC TT Literature-reported TTESBNC FM Phosphoric monoester hydrolases TTESBNC KE hsa04110:Cell cycle; hsa04114:Oocyte meiosis; hsa04914:Progesterone-mediated oocyte maturation; hsa05206:MicroRNAs in cancer TTESBNC RC R-HSA-156711:Polo-like kinase mediated events; R-HSA-157881:Cyclin B2 mediated events; R-HSA-176187:Activation of ATR in response to replication stress; R-HSA-5625740:RHO GTPases activate PKNs; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition; R-HSA-75035:Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex TT58ZYW ID TT58ZYW TT58ZYW TN Mycobacterium Isocitrate lyase (MycB icl) TT58ZYW UP P9WKK7 TT58ZYW UC ACEA_MYCTU TT58ZYW BC Carbon-carbon lyase TT58ZYW SN Isocitratase; Isocitrase; ICL TT58ZYW GN MycB icl TT58ZYW FC Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle. May be involved in the assimilation of one-carbon compounds via the isocitrate lyase- positive serine pathway. TT58ZYW EC EC 4.1.3.1 TT58ZYW PD 5DQL; 1F8M; 1F8I; 1F61 TT58ZYW SQ MSVVGTPKSAEQIQQEWDTNPRWKDVTRTYSAEDVVALQGSVVEEHTLARRGAEVLWEQLHDLEWVNALGALTGNMAVQQVRAGLKAIYLSGWQVAGDANLSGHTYPDQSLYPANSVPQVVRRINNALQRADQIAKIEGDTSVENWLAPIVADGEAGFGGALNVYELQKALIAAGVAGSHWEDQLASEKKCGHLGGKVLIPTQQHIRTLTSARLAADVADVPTVVIARTDAEAATLITSDVDERDQPFITGERTREGFYRTKNGIEPCIARAKAYAPFADLIWMETGTPDLEAARQFSEAVKAEYPDQMLAYNCSPSFNWKKHLDDATIAKFQKELAAMGFKFQFITLAGFHALNYSMFDLAYGYAQNQMSAYVELQEREFAAEERGYTATKHQREVGAGYFDRIATTVDPNSSTTALTGSTEEGQFH TT58ZYW TT Literature-reported TT58ZYW KE mtu00630:Glyoxylate and dicarboxylate metabolism; mtu01100:Metabolic pathways; mtu01110:Biosynthesis of secondary metabolites; mtu01120:Microbial metabolism in diverse environments; mtu01200:Carbon metabolism TTH29K0 ID TTH29K0 TTH29K0 TN Mycobacterium Nicotinate-nucleotide pyrophosphorylase (MycB nadC) TTH29K0 UP P9WJJ7 TTH29K0 UC NADC_MYCTU TTH29K0 BC Pentosyltransferase TTH29K0 SN nadC; Quinolinic acid phosphoribosyltransferase; Quinolinate phosphoribosyltransferase [decarboxylating]; QAPRTase TTH29K0 GN MycB nadC TTH29K0 FC Involved in the catabolism of quinolinic acid (QA). TTH29K0 EC EC 2.4.2.19 TTH29K0 PD 1QPR; 1QPQ; 1QPO; 1QPN TTH29K0 SQ MGLSDWELAAARAAIARGLDEDLRYGPDVTTLATVPASATTTASLVTREAGVVAGLDVALLTLNEVLGTNGYRVLDRVEDGARVPPGEALMTLEAQTRGLLTAERTMLNLVGHLSGIATATAAWVDAVRGTKAKIRDTRKTLPGLRALQKYAVRTGGGVNHRLGLGDAALIKDNHVAAAGSVVDALRAVRNAAPDLPCEVEVDSLEQLDAVLPEKPELILLDNFAVWQTQTAVQRRDSRAPTVMLESSGGLSLQTAATYAETGVDYLAVGALTHSVRVLDIGLDM TTH29K0 TT Literature-reported TTH29K0 KE mtu00760:Nicotinate and nicotinamide metabolism; mtu01100:Metabolic pathways TT5B8AX ID TT5B8AX TT5B8AX TN Mycobacterium Thymidine monophosphate kinase (MycB tmk) TT5B8AX UP P9WKE1 TT5B8AX UC KTHY_MYCTU TT5B8AX BC Kinase TT5B8AX SN tmk; Thymidylic kinase; Thymidylic acid kinase; Thymidylate monophosphate kinase; Thymidylate kinase; Thymidine 5'-monophosphate kinase; TMPK; Deoxythymidine 5'-monophosphate kinase; DTMPkinase TT5B8AX GN MycB tmk TT5B8AX FC Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active withATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP. TT5B8AX EC EC 2.7.4.9 TT5B8AX PD 5NRQ; 5NRN; 5NR7; 5NQ5; 4UNS TT5B8AX SQ MLIAIEGVDGAGKRTLVEKLSGAFRAAGRSVATLAFPRYGQSVAADIAAEALHGEHGDLASSVYAMATLFALDRAGAVHTIQGLCRGYDVVILDRYVASNAAYSAARLHENAAGKAAAWVQRIEFARLGLPKPDWQVLLAVSAELAGERSRGRAQRDPGRARDNYERDAELQQRTGAVYAELAAQGWGGRWLVVGADVDPGRLAATLAPPDVPS TT5B8AX TT Literature-reported TT5B8AX KE mtu00240:Pyrimidine metabolism; mtu01100:Metabolic pathways TT124R0 ID TT124R0 TT124R0 TN Nuclear receptor coactivator 3 (NCOA3) TT124R0 UP Q9Y6Q9 TT124R0 UC NCOA3_HUMAN TT124R0 BC Acyltransferase TT124R0 SN bHLHe42; Thyroid hormone receptor activator molecule 1; TRAM1; TRAM-1; Steroid receptor coactivator protein 3; SRC-3; Receptor-associated coactivator 3; RAC3; RAC-3; PCIP; NCoA-3; Class E basic helix-loop-helix protein 42; CBP-interacting protein; Amplified in breast cancer-1 protein; Amplified in breast cancer 1 protein; AIB1 (SRC-3); AIB1; AIB-1; ACTR TT124R0 GN NCOA3 TT124R0 FC Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit. Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. TT124R0 EC EC 2.3.1.48 TT124R0 PD 6ES7; 3L3Z; 3L3X; 1KBH TT124R0 SQ MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNGVSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGEDLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDRHGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLADPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNIMISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKESSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVSSSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGNVVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQEKDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLKSSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGSSMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPTLPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQVSHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMNQMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTAGGAAVMRPMMQPQVSSQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQPDPAFGRVSSPPNAMMSSRMGPSQNPMMQHPQAASIYQSSEMKGWPSGNLARNSSFSQQQFAHQGNPAVYSMVHMNGSSGHMGQMNMNPMPMSGMPMGPDQKYC TT124R0 TT Literature-reported TT124R0 FM Acyltransferase TT124R0 KE hsa04919:Thyroid hormone signaling pathway TT124R0 RC R-HSA-1989781:PPARA activates gene expression; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-5687128:MAPK6/MAPK4 signaling TTYMGWX ID TTYMGWX TTYMGWX TN PDK-1 messenger RNA (PDK-1 mRNA) TTYMGWX UP O15530 TTYMGWX UC PDPK1_HUMAN TTYMGWX BC mRNA target TTYMGWX SN PDK1 (mRNA); HPDK1 (mRNA); 3-phosphoinositide-dependent protein kinase 1 (mRNA); 3-Phosphoinositide-dependent kinase-1 (mRNA); 3'-phosphoinositide dependent kinase 1 (mRNA) TTYMGWX GN PDPK1 TTYMGWX FC Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. Isoform 3 is catalytically inactive. Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. TTYMGWX EC EC 2.7.11.1 TTYMGWX PD 5MRD; 5LVP; 5LVO; 5LVN; 5LVM TTYMGWX SQ MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ TTYMGWX TT Literature-reported TTYMGWX FM mRNA target TTYMGWX KE hsa03320:PPAR signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04510:Focal adhesion; hsa04660:T cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04910:Insulin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04960:Aldosterone-regulated sodium reabsorption; hsa05145:Toxoplasmosis; hsa05160:Hepatitis C; hsa05205:Proteoglycans in cancer; hsa05213:Endometrial cancer; hsa05215:Prostate cancer; hsa05223:Non-small cell lung cancer; hsa05231:Choline metabolism in cancer TTYMGWX RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-165158:Activation of AKT2; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-5218920:VEGFR2 mediated vascular permeability; R-HSA-5218921:VEGFR2 mediated cell proliferation; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-5625740:RHO GTPases activate PKNs; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer TTN34SQ ID TTN34SQ TTN34SQ TN Phosphodiesterase 3B (PDE3B) TTN34SQ UP Q13370 TTN34SQ UC PDE3B_HUMAN TTN34SQ BC Phosphoric diester hydrolase TTN34SQ SN cGMPinhibited 3',5'cyclic phosphodiesterase B; cGMP-inhibited 3',5'-cyclic phosphodiesterase B; Cyclic GMPinhibited phosphodiesterase B; Cyclic GMP-inhibited phosphodiesterase B; CGIPDE1; CGIPDE B; CGIP1; CGI-PDE B TTN34SQ GN PDE3B TTN34SQ FC May play a role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis. Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. TTN34SQ EC EC 3.1.4.17 TTN34SQ PD 1SOJ; 1SO2 TTN34SQ SQ MRRDERDAKAMRSLQPPDGAGSPPESLRNGYVKSCVSPLRQDPPRGFFFHLCRFCNVELRPPPASPQQPRRCSPFCRARLSLGALAAFVLALLLGAEPESWAAGAAWLRTLLSVCSHSLSPLFSIACAFFFLTCFLTRTKRGPGPGRSCGSWWLLALPACCYLGDFLVWQWWSWPWGDGDAGSAAPHTPPEAAAGRLLLVLSCVGLLLTLAHPLRLRHCVLVLLLASFVWWVSFTSLGSLPSALRPLLSGLVGGAGCLLALGLDHFFQIREAPLHPRLSSAAEEKVPVIRPRRRSSCVSLGETAASYYGSCKIFRRPSLPCISREQMILWDWDLKQWYKPHYQNSGGGNGVDLSVLNEARNMVSDLLTDPSLPPQVISSLRSISSLMGAFSGSCRPKINPLTPFPGFYPCSEIEDPAEKGDRKLNKGLNRNSLPTPQLRRSSGTSGLLPVEQSSRWDRNNGKRPHQEFGISSQGCYLNGPFNSNLLTIPKQRSSSVSLTHHVGLRRAGVLSSLSPVNSSNHGPVSTGSLTNRSPIEFPDTADFLNKPSVILQRSLGNAPNTPDFYQQLRNSDSNLCNSCGHQMLKYVSTSESDGTDCCSGKSGEEENIFSKESFKLMETQQEEETEKKDSRKLFQEGDKWLTEEAQSEQQTNIEQEVSLDLILVEEYDSLIEKMSNWNFPIFELVEKMGEKSGRILSQVMYTLFQDTGLLEIFKIPTQQFMNYFRALENGYRDIPYHNRIHATDVLHAVWYLTTRPVPGLQQIHNGCGTGNETDSDGRINHGRIAYISSKSCSNPDESYGCLSSNIPALELMALYVAAAMHDYDHPGRTNAFLVATNAPQAVLYNDRSVLENHHAASAWNLYLSRPEYNFLLHLDHVEFKRFRFLVIEAILATDLKKHFDFLAEFNAKANDVNSNGIEWSNENDRLLVCQVCIKLADINGPAKVRDLHLKWTEGIVNEFYEQGDEEANLGLPISPFMDRSSPQLAKLQESFITHIVGPLCNSYDAAGLLPGQWLEAEEDNDTESGDDEDGEELDTEDEEMENNLNPKPPRRKSRRRIFCQLMHHLTENHKIWKEIVEEEEKCKADGNKLQVENSSLPQADEIQVIEEADEEE TTN34SQ TT Patented-recorded TT3T17P ID TT3T17P TT3T17P TN Phospholipase D1 (PLD1) TT3T17P UP Q13393 TT3T17P UC PLD1_HUMAN TT3T17P BC Phosphoric diester hydrolase TT3T17P SN Phosphatidylcholine-hydrolyzing phospholipase D1; PLD 1; HPLD1; Choline phosphatase 1 TT3T17P GN PLD1 TT3T17P FC May be involved in the regulation of perinuclear intravesicular membrane traffic. Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. TT3T17P EC EC 3.1.4.4 TT3T17P SQ MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGLKPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT TT3T17P TT Patented-recorded TT3T17P FM Phosphoric diester hydrolase TT3T17P KE hsa00564:Glycerophospholipid metabolism; hsa00565:Ether lipid metabolism; hsa01100:Metabolic pathways; hsa04014:Ras signaling pathway; hsa04024:cAMP signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04144:Endocytosis; hsa04666:Fc gamma R-mediated phagocytosis; hsa04724:Glutamatergic synapse; hsa04912:GnRH signaling pathway; hsa05200:Pathways in cancer; hsa05212:Pancreatic cancer; hsa05231:Choline metabolism in cancer TT3T17P RC R-HSA-2029485:Role of phospholipids in phagocytosis TT7A1BO ID TT7A1BO TT7A1BO TN PKC-delta messenger RNA (PRKCD mRNA) TT7A1BO UP Q05655 TT7A1BO UC KPCD_HUMAN TT7A1BO BC mRNA target TT7A1BO SN nPKC-delta (mRNA); Tyrosine-protein kinase PRKCD (mRNA); SDK1 (mRNA); Protein kinase C delta type catalytic subunit (mRNA); Protein kinase C delta type (mRNA); Protein Kinase C delta (mRNA); PKC-delta (mRNA) TT7A1BO GN PRKCD TT7A1BO FC Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion. Phosphorylates ELAVL1 in response to angiotensin-2 treatment. Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. TT7A1BO EC EC 2.7.11.13 TT7A1BO PD 2YUU; 1YRK TT7A1BO SQ MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED TT7A1BO TT Literature-reported TT7A1BO FM mRNA target TT7A1BO KE hsa04062:Chemokine signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04530:Tight junction; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04722:Neurotrophin signaling pathway; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa04930:Type II diabetes mellitus TT7A1BO RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-111933:Calmodulin induced events; R-HSA-114508:Effects of PIP2 hydrolysis; R-HSA-1489509:DAG and IP3 signaling; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-418597:G alpha (z) signalling events; R-HSA-450520:HuR (ELAVL1) binds and stabilizes mRNA; R-HSA-5218921:VEGFR2 mediated cell proliferation; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-877300:Interferon gamma signaling TT57MT2 ID TT57MT2 TT57MT2 TN PKC-epsilon messenger RNA (PRKCE mRNA) TT57MT2 UP Q02156 TT57MT2 UC KPCE_HUMAN TT57MT2 BC mRNA target TT57MT2 SN Protein kinase C epsilon type (mRNA); Protein Kinase C epsilon (mRNA); PKCE (mRNA); PKC epsilon (mRNA); NPKC-epsilon (mRNA) TT57MT2 GN PRKCE TT57MT2 FC Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. In HeLa cells, contributes to hepatocyte growth factor (HGF)-induced cell migration, and in human corneal epithelial cells, plays a critical role in wound healing after activation by HGF. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2. 2). In prostate cancer cells, interacts with and phosphorylates STAT3, which increases DNA-binding and transcriptional activity of STAT3 and seems to be essential for prostate cancer cell invasion. Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. TT57MT2 EC EC 2.7.11.13 TT57MT2 PD 5LIH; 2WH0 TT57MT2 SQ MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP TT57MT2 TT Literature-reported TT57MT2 FM mRNA target TT57MT2 KE hsa04022:cGMP-PKG signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04530:Tight junction; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04930:Type II diabetes mellitus; hsa05206:MicroRNAs in cancer TT57MT2 RC R-HSA-114508:Effects of PIP2 hydrolysis; R-HSA-1489509:DAG and IP3 signaling; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-418597:G alpha (z) signalling events TTONI0R ID TTONI0R TTONI0R TN PKC-eta messenger RNA (PRKCH mRNA) TTONI0R UP P24723 TTONI0R UC KPCL_HUMAN TTONI0R BC mRNA target TTONI0R SN nPKC-eta (mRNA); Protein kinase C eta type (mRNA); PRKCL (mRNA); PKCL (mRNA); PKC-L (mRNA) TTONI0R GN PRKCH TTONI0R FC In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization. Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. TTONI0R EC EC 2.7.11.13 TTONI0R PD 3TXO; 2FK9 TTONI0R SQ MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP TTONI0R TT Literature-reported TTONI0R FM mRNA target TTONI0R KE hsa04270:Vascular smooth muscle contraction; hsa04530:Tight junction; hsa04750:Inflammatory mediator regulation of TRP channels TTONI0R RC R-HSA-114508:Effects of PIP2 hydrolysis; R-HSA-418597:G alpha (z) signalling events TT1MS7X ID TT1MS7X TT1MS7X TN PKC-theta messenger RNA (PRKCQ mRNA) TT1MS7X UP Q04759 TT1MS7X UC KPCT_HUMAN TT1MS7X BC mRNA target TT1MS7X SN Protein kinase C theta type (mRNA); PRKCT (mRNA); NPKC-theta (mRNA) TT1MS7X GN PRKCQ TT1MS7X FC In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates in the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1. Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. TT1MS7X EC EC 2.7.11.13 TT1MS7X PD 5F9E; 4RA5; 4Q9Z; 2JED; 2ENZ TT1MS7X SQ MSPFLRIGLSNFDCGSCQSCQGEAVNPYCAVLVKEYVESENGQMYIQKKPTMYPPWDSTFDAHINKGRVMQIIVKGKNVDLISETTVELYSLAERCRKNNGKTEIWLELKPQGRMLMNARYFLEMSDTKDMNEFETEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFVWGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYKSPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARCLRDTEQIFREGPVEIGLPCSIKNEARPPCLPTPGKREPQGISWESPLDEVDKMCHLPEPELNKERPSLQIKLKIEDFILHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSRATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTNTFCGTPDYIAPEILLGQKYNHSVDWWSFGVLLYEMLIGQSPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFDCSNFDKEFLNEKPRLSFADRALINSMDQNMFRNFSFMNPGMERLIS TT1MS7X TT Literature-reported TT1MS7X FM mRNA target TT1MS7X KE hsa04064:NF-kappa B signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04530:Tight junction; hsa04660:T cell receptor signaling pathway; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04920:Adipocytokine signaling pathway; hsa05162:Measles TT1MS7X RC R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-114508:Effects of PIP2 hydrolysis; R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade; R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-418597:G alpha (z) signalling events TT5U49F ID TT5U49F TT5U49F TN PRKACA messenger RNA (PRKACA mRNA) TT5U49F UP P17612 TT5U49F UC KAPCA_HUMAN TT5U49F BC mRNA target TT5U49F SN cAMP-dependent protein kinase catalytic subunit alpha (mRNA); PKACA (mRNA); PKA C-alpha (mRNA) TT5U49F GN PRKACA TT5U49F FC Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation. Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock. Phosphorylates a large number of substrates in the cytoplasm and the nucleus. TT5U49F EC EC 2.7.11.11 TT5U49F PD 6FRX; 6C0U; 6BYS; 6BYR; 5UZK TT5U49F SQ MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF TT5U49F TT Patented-recorded TT5U49F FM mRNA target TT5U49F KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04114:Oocyte meiosis; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04310:Wnt signaling pathway; hsa04340:Hedgehog signaling pathway; hsa04540:Gap junction; hsa04611:Platelet activation; hsa04713:Circadian entrainment; hsa04720:Long-term potentiation; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04727:GABAergic synapse; hsa04728:Dopaminergic synapse; hsa04740:Olfactory transduction; hsa04742:Taste transduction; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04910:Insulin signaling pathway; hsa04911:Insulin secretion; hsa04912:GnRH signaling pathway; hsa04913:Ovarian steroidogenesis; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04918:Thyroid hormone synthesis; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04922:Glucagon signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04924:Renin secretion; hsa04961:Endocrine and other factor-regulated calcium reabsorption; hsa04962:Vasopressin-regulated water reabsorption; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04976:Bile secretion; hsa05012:Parkinson's disease; hsa05020:Prion diseases; hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05032:Morphine addiction; hsa05034:Alcoholism; hsa05110:Vibrio cholerae infection; hsa05146:Amoebiasis; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05414:Dilated cardiomyopathy TT5U49F RC R-HSA-163560:Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis; R-HSA-163615:PKA activation; R-HSA-164378:PKA activation in glucagon signalling; R-HSA-180024:DARPP-32 events; R-HSA-2565942:Regulation of PLK1 Activity at G2/M Transition; R-HSA-380259:Loss of Nlp from mitotic centrosomes; R-HSA-380270:Recruitment of mitotic centrosome proteins and complexes; R-HSA-380284:Loss of proteins required for interphase microtubule organization?from the centrosome; R-HSA-381676:Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-422356:Regulation of insulin secretion; R-HSA-432040:Vasopressin regulates renal water homeostasis via Aquaporins; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-5610780:Degradation of GLI1 by the proteasome; R-HSA-5610783:Degradation of GLI2 by the proteasome; R-HSA-5610787:Hedgehog 'off' state; R-HSA-5620912:Anchoring of the basal body to the plasma membrane; R-HSA-5621575:CD209 (DC-SIGN) signaling; R-HSA-5687128:MAPK6/MAPK4 signaling; R-HSA-70263:Gluconeogenesis; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTUWGRA ID TTUWGRA TTUWGRA TN Protein kinase C zeta (PRKCZ) TTUWGRA UP Q05513 TTUWGRA UC KPCZ_HUMAN TTUWGRA BC Kinase TTUWGRA SN Protein kinase C zeta type; PKC2; NPKC-zeta TTUWGRA GN PRKCZ TTUWGRA FC Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. In vein endothelial cells treated with the oxidant peroxynitrite, phosphorylates STK11 leading to nuclear export of STK11, subsequent inhibition of PI3K/Akt signaling, and increased apoptosis. Phosphorylates VAMP2 in vitro. Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). TTUWGRA EC EC 2.7.11.13 TTUWGRA SQ MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV TTUWGRA TT Patented-recorded TTUWGRA FM Kinase TTUWGRA KE hsa04015:Rap1 signaling pathway; hsa04062:Chemokine signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04390:Hippo signaling pathway; hsa04530:Tight junction; hsa04611:Platelet activation; hsa04910:Insulin signaling pathway; hsa04930:Type II diabetes mellitus TTUWGRA RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-2173791:TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition); R-HSA-5218921:VEGFR2 mediated cell proliferation TT369M5 ID TT369M5 TT369M5 TN Protein-tyrosine phosphatase SHP-1 (PTPN6) TT369M5 UP P29350 TT369M5 UC PTN6_HUMAN TT369M5 BC Phosphoric monoester hydrolase TT369M5 SN Tyrosine-protein phosphatase non-receptor type 6; SH-PTP1; Protein-tyrosine phosphatase 1C; PTP1C; PTP-1C; Hematopoietic cell protein-tyrosine phosphatase; HCP TT369M5 GN PTPN6 TT369M5 FC The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis. Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. TT369M5 EC EC 3.1.3.48 TT369M5 PD 4HJQ; 4HJP; 4GS0; 4GRZ; 4GRY TT369M5 SQ MVRWFHRDLSGLDAETLLKGRGVHGSFLARPSRKNQGDFSLSVRVGDQVTHIRIQNSGDFYDLYGGEKFATLTELVEYYTQQQGVLQDRDGTIIHLKYPLNCSDPTSERWYHGHMSGGQAETLLQAKGEPWTFLVRESLSQPGDFVLSVLSDQPKAGPGSPLRVTHIKVMCEGGRYTVGGLETFDSLTDLVEHFKKTGIEEASGAFVYLRQPYYATRVNAADIENRVLELNKKQESEDTAKAGFWEEFESLQKQEVKNLHQRLEGQRPENKGKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYIKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGDLIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTKKKLEVLQSQKGQESEYGNITYPPAMKNAHAKASRTSSKHKEDVYENLHTKNKREEKVKKQRSADKEKSKGSLKRK TT369M5 TT Patented-recorded TT369M5 FM Phosphoric monoester hydrolases TT0OFWN ID TT0OFWN TT0OFWN TN Pseudomonas UDP-3-O-acyl-GlcNAc deacetylase (Pseudo lpxC) TT0OFWN UP P47205 TT0OFWN UC LPXC_PSEAE TT0OFWN BC Carbon-nitrogen hydrolase TT0OFWN SN Pseudo UDP-3-O-acyl-GlcNAc deacetylase; EnvA protein TT0OFWN GN Pseudo lpxC TT0OFWN FC Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. TT0OFWN EC EC 3.5.1.108 TT0OFWN PD 6MAE; 6CAX; 6C9C; 5VWM; 5UPG TT0OFWN SQ MIKQRTLKNIIRATGVGLHSGEKVYLTLKPAPVDTGIVFCRTDLDPVVEIPARAENVGETTMSTTLVKGDVKVDTVEHLLSAMAGLGIDNAYVELSASEVPIMDGSAGPFVFLIQSAGLQEQEAAKKFIRIKREVSVEEGDKRAVFVPFDGFKVSFEIDFDHPVFRGRTQQASVDFSSTSFVKEVSRARTFGFMRDIEYLRSQNLALGGSVENAIVVDENRVLNEDGLRYEDEFVKHKILDAIGDLYLLGNSLIGEFRGFKSGHALNNQLLRTLIADKDAWEVVTFEDARTAPISYMRPAAAV TT0OFWN TT Preclinical TT0OFWN KE pae00540:Lipopolysaccharide biosynthesis; pae01100:Metabolic pathways TT1S4LJ ID TT1S4LJ TT1S4LJ TN RRM2 messenger RNA (RRM2 mRNA) TT1S4LJ UP P31350 TT1S4LJ UC RIR2_HUMAN TT1S4LJ BC mRNA target TT1S4LJ SN Ribonucleotide reductase small subunit (mRNA); Ribonucleotide reductase small chain (mRNA); Ribonucleoside-diphosphate reductase subunit M2 (mRNA); RR2 (mRNA) TT1S4LJ GN RRM2 TT1S4LJ FC Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling. Provides the precursors necessary for DNA synthesis. TT1S4LJ EC EC 1.17.4.1 TT1S4LJ PD 3VPO; 3VPN; 3VPM; 3OLJ; 2UW2 TT1S4LJ SQ MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKTKAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSSPTENSFTLDADF TT1S4LJ TT Literature-reported TT1S4LJ FM mRNA target TT1S4LJ KE hsa00230:Purine metabolism; hsa00240:Pyrimidine metabolism; hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways; hsa04115:p53 signaling pathway TT1S4LJ RC R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-69205:G1/S-Specific Transcription TTAK0IN ID TTAK0IN TTAK0IN TN SOAT2 messenger RNA (SOAT2 mRNA) TTAK0IN UP O75908 TTAK0IN UC SOAT2_HUMAN TTAK0IN BC mRNA target TTAK0IN SN Sterol O-acyltransferase 2 (mRNA); Cholesterol acyltransferase 2 (mRNA); Acyl-coenzyme A:cholesterol acyltransferase 2 (mRNA); ACAT2 (mRNA); ACAT-2 (mRNA); ACACT2 (mRNA) TTAK0IN GN SOAT2 TTAK0IN FC Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa. TTAK0IN EC EC 2.3.1.26 TTAK0IN SQ MEPGGARLRLQRTEGLGGERERQPCGDGNTETHRAPDLVQWTRHMEAVKAQLLEQAQGQLRELLDRAMREAIQSYPSQDKPLPPPPPGSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHFRTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLAPYQALRLWARGTWTQATGLGCALLAAHAVVLCALPVHVAVEHQLPPASRCVLVFEQVRFLMKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYVRWNYVAKNFAQALGCVLYACFILGRLCVPVFANMSREPFSTRALVLSILHATLPGIFMLLLIFFAFLHCWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLRLLGARARGVAMLGVFLVSAVAHEYIFCFVLGFFYPVMLILFLVIGGMLNFMMHDQRTGPAWNVLMWTMLFLGQGIQVSLYCQEWYARRHCPLPQATFWGLVTPRSWSCHT TTAK0IN TT Literature-reported TTAK0IN FM mRNA target TTAK0IN KE hsa00100:Steroid biosynthesis TTPRO7W ID TTPRO7W TTPRO7W TN Suppressor of tumorigenicity 14 protein (ST14) TTPRO7W UP Q9Y5Y6 TTPRO7W UC ST14_HUMAN TTPRO7W BC Peptidase TTPRO7W SN Tumor-associated differentially-expressed gene 15 protein; Tumor associated differentially-expressed gene-15 protein; TADG15; Serine protease TADG-15; Serine protease 14; SNC19; Prostamin; PRSS14; Membrane-type serine protease 1; Membrane type serine protease 1; Matriptase; MT-SP1 TTPRO7W GN ST14 TTPRO7W FC Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site. Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing. Degrades extracellular matrix. TTPRO7W EC EC 3.4.21.109 TTPRO7W PD 5LYO; 4R0I; 4O9V; 4O97; 4JZI TTPRO7W SQ MGSDRARKGGGGPKDFGAGLKYNSRHEKVNGLEEGVEFLPVNNVKKVEKHGPGRWVVLAAVLIGLLLVLLGIGFLVWHLQYRDVRVQKVFNGYMRITNENFVDAYENSNSTEFVSLASKVKDALKLLYSGVPFLGPYHKESAVTAFSEGSVIAYYWSEFSIPQHLVEEAERVMAEERVVMLPPRARSLKSFVVTSVVAFPTDSKTVQRTQDNSCSFGLHARGVELMRFTTPGFPDSPYPAHARCQWALRGDADSVLSLTFRSFDLASCDERGSDLVTVYNTLSPMEPHALVQLCGTYPPSYNLTFHSSQNVLLITLITNTERRHPGFEATFFQLPRMSSCGGRLRKAQGTFNSPYYPGHYPPNIDCTWNIEVPNNQHVKVRFKFFYLLEPGVPAGTCPKDYVEINGEKYCGERSQFVVTSNSNKITVRFHSDQSYTDTGFLAEYLSYDSSDPCPGQFTCRTGRCIRKELRCDGWADCTDHSDELNCSCDAGHQFTCKNKFCKPLFWVCDSVNDCGDNSDEQGCSCPAQTFRCSNGKCLSKSQQCNGKDDCGDGSDEASCPKVNVVTCTKHTYRCLNGLCLSKGNPECDGKEDCSDGSDEKDCDCGLRSFTRQARVVGGTDADEGEWPWQVSLHALGQGHICGASLISPNWLVSAAHCYIDDRGFRYSDPTQWTAFLGLHDQSQRSAPGVQERRLKRIISHPFFNDFTFDYDIALLELEKPAEYSSMVRPICLPDASHVFPAGKAIWVTGWGHTQYGGTGALILQKGEIRVINQTTCENLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEADGRIFQAGVVSWGDGCAQRNKPGVYTRLPLFRDWIKENTGV TTPRO7W TT Patented-recorded TTPRO7W FM Peptidase TTPRO7W KE hsa05206:MicroRNAs in cancer TTGRHIB ID TTGRHIB TTGRHIB TN UDP-glucose 4-epimerase (GALE) TTGRHIB UP Q14376 TTGRHIB UC GALE_HUMAN TTGRHIB BC Racemases and epimerase TTGRHIB SN UDP-galactose4-epimerase; UDP-galactose4'-epimerase; UDP-galactose 4-epimerase; UDP-N-acetylglucosamine 4-epimerase; UDP-N-acetylgalactosamine 4-epimerase; UDP-GlcNAc 4-epimerase; UDP-GalNAc 4-epimerase; Galactowaldenase TTGRHIB GN GALE TTGRHIB FC The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6-phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids. Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. TTGRHIB EC EC 5.1.3.2 TTGRHIB PD 1I3N; 1I3M; 1I3L; 1I3K; 1HZJ TTGRHIB SQ MAEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSLPESLRRVQELTGRSVEFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMKAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKTWNAVLLRYFNPTGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRDYIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGTQA TTGRHIB TT Literature-reported TTGRHIB FM Racemases and epimerases TTGRHIB KE hsa00052:Galactose metabolism; hsa00520:Amino sugar and nucleotide sugar metabolism; hsa01100:Metabolic pathways TTSUKYD ID TTSUKYD TTSUKYD TN Virus RNA-dependent RNA polymerase (Viru RdRP) TTSUKYD UP P26662 (2420-3010) TTSUKYD UC POLG_HCVJA TTSUKYD BC Kinase TTSUKYD SN HCV NS5B; HCV p68 TTSUKYD GN Viru RdRP TTSUKYD FC Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). TTSUKYD EC EC 2.7.7.48 TTSUKYD PD 4KTC; 4JMY; 4I33; 4I32; 4I31 TTSUKYD SQ SMSYTWTGALITPCAAEESKLPINPLSNSLLRHHSMVYSTTSRSASLRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKARLLSIEEACKLTPPHSAKSKFGYGAKDVRSLSSRAVNHIRSVWEDLLEDTETPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGPSYGFQYSPGQRVEFLVNTWKSKKCPMGFSYDTRCFDSTVTENDIRTEESIYQCCDLAPEARQAIRSLTERLYVGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKATAACRAAKLQDCTMLVNGDDLVVICESAGTQEDAAALRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETVRHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQIIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRAKLLSQGGRAATCGKYLFNWAVKTKLKLTPIPAASQLDLSGWFVAGYNGGDIYHSLSRARPRWFMLCLLLLSVGVGIYLLPNR TTSUKYD TT Clinical trial TT8HGRW ID TT8HGRW TT8HGRW TN Voltage-gated potassium channel Kv7.4 (KCNQ4) TT8HGRW UP P56696 TT8HGRW UC KCNQ4_HUMAN TT8HGRW BC Voltage-gated ion channel TT8HGRW SN Voltage-gated potassium channel subunit Kv7.4; Potassium channel alpha subunit KvLQT4; KQT-like 4; KCNQ4 TT8HGRW GN KCNQ4 TT8HGRW FC Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea. KCNQ4 channels are blocked by linopirdin, XE991 and bepridil, whereas clofilium is without significant effect. Muscarinic agonist oxotremorine-M strongly suppress KCNQ4 current in CHO cells in which cloned KCNQ4 channels were coexpressed with M1muscarinic receptors. TT8HGRW PD 6N5W; 4GOW; 2OVC TT8HGRW SQ MAEAPPRRLGLGPPPGDAPRAELVALTAVQSEQGEAGGGGSPRRLGLLGSPLPPGAPLPGPGSGSGSACGQRSSAAHKRYRRLQNWVYNVLERPRGWAFVYHVFIFLLVFSCLVLSVLSTIQEHQELANECLLILEFVMIVVFGLEYIVRVWSAGCCCRYRGWQGRFRFARKPFCVIDFIVFVASVAVIAAGTQGNIFATSALRSMRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFASFLVYLAEKDANSDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRMPAANLIQAAWRLYSTDMSRAYLTATWYYYDSILPSFRELALLFEHVQRARNGGLRPLEVRRAPVPDGAPSRYPPVATCHRPGSTSFCPGESSRMGIKDRIRMGSSQRRTGPSKQHLAPPTMPTSPSSEQVGEATSPTKVQKSWSFNDRTRFRASLRLKPRTSAEDAPSEEVAEEKSYQCELTVDDIMPAVKTVIRSIRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQTRVDQIVGRGPGDRKAREKGDKGPSDAEVVDEISMMGRVVKVEKQVQSIEHKLDLLLGFYSRCLRSGTSASLGAVQVPLFDPDITSDYHSPVDHEDISVSAQTLSISRSVSTNMD TT8HGRW TT Literature-reported TT8HGRW KE hsa04725:Cholinergic synapse TT8HGRW RC R-HSA-1296072:Voltage gated Potassium channels TTIET93 ID TTIET93 TTIET93 TN Activated CDC42 kinase 1 (ACK-1) TTIET93 UP Q07912 TTIET93 UC ACK1_HUMAN TTIET93 BC Kinase TTIET93 SN Tyrosine kinase non-receptor protein 2; ACK1; ACK-1 TTIET93 GN TNK2 TTIET93 FC Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr-287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR. Phosphorylates WASP. TTIET93 EC EC 2.7.10.2 TTIET93 PD 5ZXB; 4ID7; 4HZS; 4HZR; 4EWH TTIET93 SQ MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNVTRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKALCKRKSWMSKVFSGKRLEAEFPPHHSQSTFRKTSPAPGGPAGEGPLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPDRIDELYLGNPMDPPDLLSVELSTSRPPQHLGGVKKPTYDPVSEDQDPLSSDFKRLGLRKPGLPRGLWLAKPSARVPGTKASRGSGAEVTLIDFGEEPVVPALRPCAPSLAQLAMDACSLLDETPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEICSINSTLVGAGVPAGPSQGQTNYAFVPEQARPPPPLEDNLFLPPQGGGKPPSSAQTAEIFQALQQECMRQLQAPAGSPAPSPSPGGDDKPQVPPRVPIPPRPTRPHVQLSPAPPGEEETSQWPGPASPPRVPPREPLSPQGSRTPSPLVPPGSSPLPPRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGKKVSSTHYYLLPERPSYLERYQRFLREAQSPEEPTPLPVPLLLPPPSTPAPAAPTATVRPMPQAALDPKANFSTNNSNPGARPPPPRATARLPQRGCPGDGPEAGRPADKIQMAMVHGVTTEECQAALQCHGWSVQRAAQYLKVEQLFGLGLRPRGECHKVLEMFDWNLEQAGCHLLGSWGPAHHKR TTIET93 TT Patented-recorded TTIET93 FM Kinase TTLFRKS ID TTLFRKS TTLFRKS TN Activin receptor type IIB (ACVR2B) TTLFRKS UP Q13705 TTLFRKS UC AVR2B_HUMAN TTLFRKS BC Kinase TTLFRKS SN Activin receptor type2B; Activin receptor type-2B; ACTRIIB; ACTR-IIB TTLFRKS GN ACVR2B TTLFRKS FC Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). TTLFRKS EC EC 2.7.11.30 TTLFRKS PD 5NHR; 5NGV; 4FAO; 2QLU; 2H62 TTLFRKS SQ MTAPWVALALLWGSLCAGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEAGGPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEELQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSLIRRSVNGTTSDCLVSLVTSVTNVDLPPKESSI TTLFRKS TT Literature-reported TTLFRKS FM Kinase TTLFRKS KE hsa04060:Cytokine-cytokine receptor interaction; hsa04350:TGF-beta signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells TTLFRKS RC R-HSA-1433617:Regulation of signaling by NODAL TTF5NVW ID TTF5NVW TTF5NVW TN Alanine glyoxylate aminotransferase (AGXT) TTF5NVW UP P21549 TTF5NVW UC SPYA_HUMAN TTF5NVW BC Transaminase TTF5NVW SN Serine--pyruvate aminotransferase; SPAT; Alanine--glyoxylate aminotransferase; AGT1; AGT TTF5NVW GN AGXT TTF5NVW FC Catalyzes L-alanine and glyoxylate to pyruvate and glycine. Participates in alanine and aspartate metabolism and glycine, serine and threonine metabolism. TTF5NVW EC EC 2.6.1.51 TTF5NVW PD 5OG0; 5OFY; 5LUC; 5HHY; 5F9S TTF5NVW SQ MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSFYLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLRIGLLGCNATRENVDRVTEALRAALQHCPKKKL TTF5NVW TT Literature-reported TTF5NVW KE hsa00250:Alanine, aspartate and glutamate metabolism; hsa00260:Glycine, serine and threonine metabolism; hsa00630:Glyoxylate and dicarboxylate metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa04146:Peroxisome TTURHFP ID TTURHFP TTURHFP TN Angiogenin (ANG) TTURHFP UP P03950 TTURHFP UC ANGI_HUMAN TTURHFP BC Endoribonucleases TTURHFP SN Ribonuclease 5; RNase 5; RNASE5 TTURHFP GN ANG TTURHFP FC Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA. Cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs). Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo. Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. TTURHFP EC EC 3.1.27.- TTURHFP PD 5M9V; 5M9T; 5M9S; 5M9R; 5M9Q TTURHFP SQ MVMGLGVLLLVFVLGLGLTPPTLAQDNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP TTURHFP TT Literature-reported TTURHFP FM Endoribonucleases TTURHFP RC R-HSA-418990:Adherens junctions interactions TTY8KJS ID TTY8KJS TTY8KJS TN Bacterial Deoxyuridine triphosphate nucleotidohydrolase (Bact dut) TTY8KJS UP P06968 TTY8KJS UC DUT_ECOLI TTY8KJS BC Acid anhydrides hydrolase TTY8KJS SN Deoxyuridine triphosphate nucleotidohydrolase; Deoxyuridine 5'-triphosphate nucleotidohydrolase; DUTPase; DUTP pyrophosphatase of Escherichia coli; Bact dut TTY8KJS GN Bact dut TTY8KJS FC This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. TTY8KJS PD 2HRM; 2HR6; 1SYL; 1SEH; 1RNJ TTY8KJS SQ MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ TTY8KJS TT Literature-reported TTS7LWX ID TTS7LWX TTS7LWX TN Bacterial DNA gyrase B (Bact gyrB) TTS7LWX UP P0AES6 TTS7LWX UC GYRB_ECOLI TTS7LWX BC ATP-hydrolyzing DNA topoisomerase TTS7LWX SN gyrB; DNA gyrase subunit B TTS7LWX GN Bact gyrB TTS7LWX FC DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. TTS7LWX EC EC 5.6.2.3 TTS7LWX PD 6ENG; 5Z9Q; 5Z9N; 5Z9M; 5Z9L TTS7LWX SQ MSNSYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCKEIIVTIHADNSVSVQDDGRGIPTGIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSQKLELVIQREGKIHRQIYEHGVPQAPLAVTGETEKTGTMVRFWPSLETFTNVTEFEYEILAKRLRELSFLNSGVSIRLRDKRDGKEDHFHYEGGIKAFVEYLNKNKTPIHPNIFYFSTEKDGIGVEVALQWNDGFQENIYCFTNNIPQRDGGTHLAGFRAAMTRTLNAYMDKEGYSKKAKVSATGDDAREGLIAVVSVKVPDPKFSSQTKDKLVSSEVKSAVEQQMNELLAEYLLENPTDAKIVVGKIIDAARAREAARRAREMTRRKGALDLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIVERGHVYIAQPPLYKVKKGKQEQYIKDDEAMDQYQISIALDGATLHTNASAPALAGEALEKLVSEYNATQKMINRMERRYPKAMLKELIYQPTLTEADLSDEQTVTRWVNALVSELNDKEQHGSQWKFDVHTNAEQNLFEPIVRVRTHGVDTDYPLDHEFITGGEYRRICTLGEKLRGLLEEDAFIERGERRQPVASFEQALDWLVKESRRGLSIQRYKGLGEMNPEQLWETTMDPESRRMLRVTVKDAIAADQLFTTLMGDAVEPRRAFIEENALKAANIDI TTS7LWX TT Clinical trial TTGX0HR ID TTGX0HR TTGX0HR TN Bacterial DNA ligase (Bact ligA) TTGX0HR UP P15042 TTGX0HR UC DNLJ_ECOLI TTGX0HR BC Phosphoric ester ligase TTGX0HR SN ligA; Polydeoxyribonucleotide synthase [NAD+]; NAD+-dependent DNA ligase TTGX0HR GN Bact ligA TTGX0HR FC DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. TTGX0HR EC EC 6.5.1.2 TTGX0HR PD 5TT5; 4GLX; 2OWO TTGX0HR SQ MESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLSLDNVFDEESFLAFNKRVQDRLKNNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHGENIPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELPDTHLGRLLQFKKWGLPVSDRVTLCESAEEVLAFYHKVEEDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDTREVVFPTHCPVCGSDVERVEGEAVARCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFKLTAGKLTGLERMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVHNFFAEESNRNVISELLAEGVHWPAPIVINAEEIDSPFAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDEAEMLRLLGS TTGX0HR TT Literature-reported TTFK8YB ID TTFK8YB TTFK8YB TN Bacterial DNA topoisomerase 4A (Bact parC) TTFK8YB UP P0AFI2 TTFK8YB UC PARC_ECOLI TTFK8YB BC Topoisomerase GyrA ParC TTFK8YB SN parC; Topoisomerase IV subunit A of Escherichia coli TTFK8YB GN Bact parC TTFK8YB FC Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule. MukB stimulates the relaxation activity of topoisomeraseIV and also has a modest effect on decatenation. TTFK8YB EC EC 5.6.2.3 TTFK8YB PD 4MN4; 1ZVU; 1ZVT TTFK8YB SQ MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNASAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYSELLLSELGQGTADWVPNFDGTLQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAQAAIALIDQPKTTLDQLLDIVQGPDYPTEAEIITSRAEIRKIYENGRGSVRMRAVWKKEDGAVVISALPHQVSGARVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMDQVMNHLFATTDLEKSYRINLNMIGLDGRPAVKNLLEILSEWLVFRRDTVRRRLNYRLEKVLKRLHILEGLLVAFLNIDEVIEIIRNEDEPKPALMSRFGLTETQAEAILELKLRHLAKLEEMKIRGEQSELEKERDQLQGILASERKMNNLLKKELQADAQAYGDDRRSPLQEREEAKAMSEHDMLPSEPVTIVLSQMGWVRSAKGHDIDAPGLNYKAGDSFKAAVKGKSNQPVVFVDSTGRSYAIDPITLPSARGQGEPLTGKLTLPPGATVDHMLMESDDQKLLMASDAGYGFVCTFNDLVARNRAGKALITLPENAHVMPPVVIEDASDMLLAITQAGRMLMFPVSDLPQLSKGKGNKIINIPSAEAARGEDGLAQLYVLPPQSTLTIHVGKRKIKLRPEELQKVTGERGRRGTLMRGLQRIDRVEIDSPRRASSGDSEE TTFK8YB TT Successful TTP8UCK ID TTP8UCK TTP8UCK TN Bacterial Glycosyltransferase MurG (Bact murG) TTP8UCK UP P17443 TTP8UCK UC MURG_ECOLI TTP8UCK BC Hexosyltransferase TTP8UCK SN Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase; MurG TTP8UCK GN Bact murG TTP8UCK FC Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II). TTP8UCK EC EC 2.4.1.227 TTP8UCK PD 1NLM; 1F0K TTP8UCK SQ MSGQGKRLMVMAGGTGGHVFPGLAVAHHLMAQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGIKALIAAPLRIFNAWRQARAIMKAYKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAFPNAEVVGNPVRTDVLALPLPQQRLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDSVTIWHQSGKGSQQSVEQAYAEAGQPQHKVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNALPLEKAGAAKIIEQPQLSVDAVANTLAGWSRETLLTMAERARAASIPDATERVANEVSRVARA TTP8UCK TT Literature-reported TTAZ3MN ID TTAZ3MN TTAZ3MN TN Beta-adrenergic receptor kinase 1 (ADRBK1) TTAZ3MN UP P25098 TTAZ3MN UC ARBK1_HUMAN TTAZ3MN BC Kinase TTAZ3MN SN GRK2; G-protein coupled receptor kinase 2; BetaARK1; Beta-ARK-1; Beta ARK1 TTAZ3MN GN GRK2 TTAZ3MN FC Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner. TTAZ3MN EC EC 2.7.11.15 TTAZ3MN PD 6C2Y; 5WG5; 5WG4; 5WG3; 5UVC TTAZ3MN SQ MADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFSQKLGYLLFRDFCLNHLEEARPLVEFYEEIKKYEKLETEEERVARSREIFDSYIMKELLACSHPFSKSATEHVQGHLGKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWKNVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEADMRFYAAEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCLGRGAQEVKESPFFRSLDWQMVFLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQELYRNFPLTISERWQQEVAETVFDTINAETDRLEARKKAKNKQLGHEEDYALGKDCIMHGYMSKMGNPFLTQWQRRYFYLFPNRLEWRGEGEAPQSLLTMEEIQSVEETQIKERKCLLLKIRGGKQFILQCDSDPELVQWKKELRDAYREAQQLVQRVPKMKNKPRSPVVELSKVPLVQRGSANGL TTAZ3MN TT Patented-recorded TTAZ3MN KE hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa04724:Glutamatergic synapse; hsa05032:Morphine addiction TTAZ3MN RC R-HSA-111933:Calmodulin induced events; R-HSA-416476:G alpha (q) signalling events; R-HSA-5635838:Activation of SMO TTGKF90 ID TTGKF90 TTGKF90 TN Bone morphogenetic protein receptor (BMPR2) TTGKF90 UP Q13873 TTGKF90 UC BMPR2_HUMAN TTGKF90 BC Kinase TTGKF90 SN PPH1; Bone morphogenetic protein receptor type-2; Bone morphogenetic protein receptor type II; BMPR-II; BMPR-2; BMP type-2 receptor; BMP type II receptor TTGKF90 GN BMPR2 TTGKF90 FC Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is weak but enhanced by the presence of type I receptors for BMPs. Mediates induction of adipogenesis by GDF6. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. TTGKF90 EC EC 2.7.11.30 TTGKF90 PD 3G2F; 2HLQ TTGKF90 SQ MTSSLQRPWRVPWLPWTILLVSTAAASQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSFNRDETIIIALASVSVLAVLIVALCFGYRMLTGDRKQGLHSMNMMEAAASEPSLDLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERVTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNDGTCVISDFGLSMRLTGNRLVRPGEEDNAAISEVGTIRYMAPEVLEGAVNLRDCESALKQVDMYALGLIYWEIFMRCTDLFPGESVPEYQMAFQTEVGNHPTFEDMQVLVSREKQRPKFPEAWKENSLAVRSLKETIEDCWDQDAEARLTAQCAEERMAELMMIWERNKSVSPTVNPMSTAMQNERNLSHNRRVPKIGPYPDYSSSSYIEDSIHHTDSIVKNISSEHSMSSTPLTIGEKNRNSINYERQQAQARIPSPETSVTSLSTNTTTTNTTGLTPSTGMTTISEMPYPDETNLHTTNVAQSIGPTPVCLQLTEEDLETNKLDPKEVDKNLKESSDENLMEHSLKQFSGPDPLSSTSSSLLYPLIKLAVEATGQQDFTQTANGQACLIPDVLPTQIYPLPKQQNLPKRPTSLPLNTKNSTKEPRLKFGSKHKSNLKQVETGVAKMNTINAAEPHVVTVTMNGVAGRNHSVNSHAATTQYANGTVLSGQTTNIVTHRAQEMLQNQFIGEDTRLNINSSPDEHEPLLRREQQAGHDEGVLDRLVDRRERPLEGGRTNSNNNNSNPCSEQDVLAQGVPSTAADPGPSKPRRAQRPNSLDLSATNVLDGSSIQIGESTQDGKSGSGEKIKKRVKTPYSLKRWRPSTWVISTESLDCEVNNNGSNRAVHSKSSTAVYLAEGGTATTMVSKDIGMNCL TTGKF90 TT Literature-reported TTGKF90 FM Kinase TTGKF90 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells TTES57P ID TTES57P TTES57P TN Branched-chain-amino-acid transaminase 1 (BCAT1) TTES57P UP P54687 TTES57P UC BCAT1_HUMAN TTES57P BC Transaminase TTES57P SN Protein ECA39; ECA39; Branched-chain-amino-acid aminotransferase, cytosolic; BCT1; BCAT(c) TTES57P GN BCAT1 TTES57P FC Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. TTES57P EC EC 2.6.1.42 TTES57P PD 2COJ; 2COI; 2COG; 2ABJ TTES57P SQ MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGREESDWTIVLS TTES57P TT Literature-reported TTES57P KE hsa00270:Cysteine and methionine metabolism; hsa00280:Valine, leucine and isoleucine degradation; hsa00290:Valine, leucine and isoleucine biosynthesis; hsa00770:Pantothenate and CoA biosynthesis; hsa01100:Metabolic pathways; hsa01210:2-Oxocarboxylic acid metabolism; hsa01230:Biosynthesis of amino acids TTE87WJ ID TTE87WJ TTE87WJ TN Calcium-activated potassium channel KCa1.1 (KCNMA1) TTE87WJ UP Q12791 TTE87WJ UC KCMA1_HUMAN TTE87WJ BC Voltage-gated ion channel TTE87WJ SN hSlo; Slowpoke homolog; Slo1; Slo-alpha; Slo homolog; SLO; MaxiK; Maxi K channel; KCa1.1; KCNMA; K(VCA)alpha; Calcium-activated potassium channel, subfamily M subunit alpha-1; Calcium-activated potassium channel subunit alpha-1; BKCA alpha; BK channel TTE87WJ GN KCNMA1 TTE87WJ FC Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX). TTE87WJ PD 3NAF; 3MT5; 2K44 TTE87WJ SQ MANGGGGGGGSSGGGGGGGGSSLRMSSNIHANHLSLDASSSSSSSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRPKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERAFPLSSVSVNDCSTSFRAFEDEQPSTLSPKKKQRNGGMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRQNRPKSRESRDKQKYVQEERL TTE87WJ TT Literature-reported TTE87WJ FM Ligand gated ion channel TTE87WJ KE hsa04022:cGMP-PKG signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04911:Insulin secretion; hsa04970:Salivary secretion; hsa04972:Pancreatic secretion TTE87WJ RC R-HSA-418457:cGMP effects TTNAHEX ID TTNAHEX TTNAHEX TN cAMP-dependent protein kinase A type I (PRKAR1A) TTNAHEX UP P10644 TTNAHEX UC KAP0_HUMAN TTNAHEX BC Kinase TTNAHEX SN cAMP-dependent protein kinase type I-alpha regulatory subunit; Tissue-specific extinguisher 1; TSE1; PRKAR1; PKR1 TTNAHEX GN PRKAR1A TTNAHEX FC Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. TTNAHEX PD 5KJZ; 5KJY; 5KJX TTNAHEX SQ MESGSTAASEEARSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEAKQIQNLQKAGTRTDSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFSVSFIAGETVIQQGDEGDNFYVIDQGETDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV TTNAHEX TT Literature-reported TTNAHEX FM Kinase TTNAHEX KE hsa04210:Apoptosis; hsa04910:Insulin signaling pathway TTNAHEX RC R-HSA-163615:PKA activation; R-HSA-164378:PKA activation in glucagon signalling; R-HSA-180024:DARPP-32 events; R-HSA-381676:Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-432040:Vasopressin regulates renal water homeostasis via Aquaporins; R-HSA-5610787:Hedgehog 'off' state; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTBAF05 ID TTBAF05 TTBAF05 TN Candida Peptide N-myristoyltransferase (Candi NMT1) TTBAF05 UP P30418 TTBAF05 UC NMT_CANAL TTBAF05 BC Acyltransferase TTBAF05 SN Peptide N-myristoyltransferase; NMT1; NMT; Myristoyl-CoA:protein N-myristoyltransferase TTBAF05 GN Candi NMT1 TTBAF05 FC Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N- terminal glycine in the nascent polypeptide substrates. Ser is presentat position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6. Basic residues are preferred at positions 7 and 8. TTBAF05 EC EC 2.3.1.97 TTBAF05 PD 1NMT; 1IYL; 1IYK TTBAF05 SQ MSGDNTGNKSNSAPSKSIEELLKLLAMGQELSPAQQKEMKDYKFWKTQPVPSLSETVTEEGPIDKLKTPEDVPNDPLPLISDFEWSTLDIDDNLQLDELYKLLYDNYVEDIDATFRFKYSHEFFQWALKPPGWRKDWHVGVRVKSTGKLVAFIAATPVTFKLNKSNKVIDSVEINFLCIHKKLRNKRLAPVLIKEITRRVNKQNIWQALYTGGSILPTPLTTCRYQHRPINWSKLHDVGFSHLPPNQTKSSMVASYTLPNNPKLKGLRPMTGKDVSTVLSLLYKYQERFDIVQLFTEEEFKHWMLGHDENSDSNVVKSYVVEDENGVITDYFSYYLLPFTVLDNAQHDELGIAYLFYYASDSFEKPNYKKRLNELITDALITSKKFGVDVFNCLTCQDNTYFLKDCKFGSGDGFLNYYLFNYRTFPMDGGIDKKTKEVVEDQTSGIGVVLL TTBAF05 TT Literature-reported TT3LJ6G ID TT3LJ6G TT3LJ6G TN Carboxypeptidase A1 (CPA1) TT3LJ6G UP P15085 TT3LJ6G UC CBPA1_HUMAN TT3LJ6G BC Peptidase TT3LJ6G SN CPA TT3LJ6G GN CPA1 TT3LJ6G FC Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. TT3LJ6G EC EC 3.4.17.1 TT3LJ6G PD 6I6Z; 5OM9; 4UF4; 4UEZ; 4UEF TT3LJ6G SQ MRGLLVLSVLLGAVFGKEDFVGHQVLRISVADEAQVQKVKELEDLEHLQLDFWRGPAHPGSPIDVRVPFPSIQAVKIFLESHGISYETMIEDVQSLLDEEQEQMFAFRSRARSTDTFNYATYHTLEEIYDFLDLLVAENPHLVSKIQIGNTYEGRPIYVLKFSTGGSKRPAIWIDTGIHSREWVTQASGVWFAKKITQDYGQDAAFTAILDTLDIFLEIVTNPDGFAFTHSTNRMWRKTRSHTAGSLCIGVDPNRNWDAGFGLSGASSNPCSETYHGKFANSEVEVKSIVDFVKDHGNIKAFISIHSYSQLLMYPYGYKTEPVPDQDELDQLSKAAVTALASLYGTKFNYGSIIKAIYQASGSTIDWTYSQGIKYSFTFELRDTGRYGFLLPASQIIPTAKETWLALLTIMEHTLNHPY TT3LJ6G TT Literature-reported TTBKFDV ID TTBKFDV TTBKFDV TN Cell division cycle protein 20 homolog (CDC20) TTBKFDV UP Q12834 TTBKFDV UC CDC20_HUMAN TTBKFDV SN p55CDC TTBKFDV GN CDC20 TTBKFDV FC Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation. TTBKFDV SQ MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYIPHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARRREREKASAAKSSLIHQGIR TTBKFDV TT Preclinical TTZD5QR ID TTZD5QR TTZD5QR TN Centromeric protein E (CENPE) TTZD5QR UP Q02224 TTZD5QR UC CENPE_HUMAN TTZD5QR BC TRAFAC class myosin-kinesin ATPase TTZD5QR SN Centromere-associated protein E; CENPE; CENP-E TTZD5QR GN CENPE TTZD5QR FC Essential for the maintenance of chromosomal stability through efficient stabilization of microtubule capture at kinetochores. Plays a key role in the movement of chromosomes toward the metaphase plate during mitosis. Is a slow plus end- directed motor whose activity is essential for metaphase chromosome alignment. Couples chromosome position to microtubule depolymerizing activity. The highly processive microtubule- dependent motor activity of CENPE servesto power chromosome congression and provides a flexible, motile tether linking kinetochores to dynamic spindle microtubules. Necessary for the mitotic checkpoint signal at individual kinetochores to prevent aneuploidy due to single chromosome loss. Required for the efficient recruitment of BUBR1, MAD1 and MAD2 to attached and newly unattached kinetochores. Stimulates mammalian BUBR1 kinase activity. Accumulates just before mitosis at the G2 phase of the cell cycle. TTZD5QR PD 5JVP; 1T5C TTZD5QR SQ MAEEGAVAVCVRVRPLNSREESLGETAQVYWKTDNNVIYQVDGSKSFNFDRVFHGNETTKNVYEEIAAPIIDSAIQGYNGTIFAYGQTASGKTYTMMGSEDHLGVIPRAIHDIFQKIKKFPDREFLLRVSYMEIYNETITDLLCGTQKMKPLIIREDVNRNVYVADLTEEVVYTSEMALKWITKGEKSRHYGETKMNQRSSRSHTIFRMILESREKGEPSNCEGSVKVSHLNLVDLAGSERAAQTGAAGVRLKEGCNINRSLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPVSFDETLTALQFASTAKYMKNTPYVNEVSTDEALLKRYRKEIMDLKKQLEEVSLETRAQAMEKDQLAQLLEEKDLLQKVQNEKIENLTRMLVTSSSLTLQQELKAKRKRRVTWCLGKINKMKNSNYADQFNIPTNITTKTHKLSINLLREIDESVCSESDVFSNTLDTLSEIEWNPATKLLNQENIESELNSLRADYDNLVLDYEQLRTEKEEMELKLKEKNDLDEFEALERKTKKDQEMQLIHEISNLKNLVKHAEVYNQDLENELSSKVELLREKEDQIKKLQEYIDSQKLENIKMDLSYSLESIEDPKQMKQTLFDAETVALDAKRESAFLRSENLELKEKMKELATTYKQMENDIQLYQSQLEAKKKMQVDLEKELQSAFNEITKLTSLIDGKVPKDLLCNLELEGKITDLQKELNKEVEENEALREEVILLSELKSLPSEVERLRKEIQDKSEELHIITSEKDKLFSEVVHKESRVQGLLEEIGKTKDDLATTQSNYKSTDQEFQNFKTLHMDFEQKYKMVLEENERMNQEIVNLSKEAQKFDSSLGALKTELSYKTQELQEKTREVQERLNEMEQLKEQLENRDSTLQTVEREKTLITEKLQQTLEEVKTLTQEKDDLKQLQESLQIERDQLKSDIHDTVNMNIDTQEQLRNALESLKQHQETINTLKSKISEEVSRNLHMEENTGETKDEFQQKMVGIDKKQDLEAKNTQTLTADVKDNEIIEQQRKIFSLIQEKNELQQMLESVIAEKEQLKTDLKENIEMTIENQEELRLLGDELKKQQEIVAQEKNHAIKKEGELSRTCDRLAEVEEKLKEKSQQLQEKQQQLLNVQEEMSEMQKKINEIENLKNELKNKELTLEHMETERLELAQKLNENYEEVKSITKERKVLKELQKSFETERDHLRGYIREIEATGLQTKEELKIAHIHLKEHQETIDELRRSVSEKTAQIINTQDLEKSHTKLQEEIPVLHEEQELLPNVKEVSETQETMNELELLTEQSTTKDSTTLARIEMERLRLNEKFQESQEEIKSLTKERDNLKTIKEALEVKHDQLKEHIRETLAKIQESQSKQEQSLNMKEKDNETTKIVSEMEQFKPKDSALLRIEIEMLGLSKRLQESHDEMKSVAKEKDDLQRLQEVLQSESDQLKENIKEIVAKHLETEEELKVAHCCLKEQEETINELRVNLSEKETEISTIQKQLEAINDKLQNKIQEIYEKEEQFNIKQISEVQEKVNELKQFKEHRKAKDSALQSIESKMLELTNRLQESQEEIQIMIKEKEEMKRVQEALQIERDQLKENTKEIVAKMKESQEKEYQFLKMTAVNETQEKMCEIEHLKEQFETQKLNLENIETENIRLTQILHENLEEMRSVTKERDDLRSVEETLKVERDQLKENLRETITRDLEKQEELKIVHMHLKEHQETIDKLRGIVSEKTNEISNMQKDLEHSNDALKAQDLKIQEELRIAHMHLKEQQETIDKLRGIVSEKTDKLSNMQKDLENSNAKLQEKIQELKANEHQLITLKKDVNETQKKVSEMEQLKKQIKDQSLTLSKLEIENLNLAQKLHENLEEMKSVMKERDNLRRVEETLKLERDQLKESLQETKARDLEIQQELKTARMLSKEHKETVDKLREKISEKTIQISDIQKDLDKSKDELQKKIQELQKKELQLLRVKEDVNMSHKKINEMEQLKKQFEAQNLSMQSVRMDNFQLTKKLHESLEEIRIVAKERDELRRIKESLKMERDQFIATLREMIARDRQNHQVKPEKRLLSDGQQHLTESLREKCSRIKELLKRYSEMDDHYECLNRLSLDLEKEIEFQKELSMRVKANLSLPYLQTKHIEKLFTANQRCSMEFHRIMKKLKYVLSYVTKIKEEQHESINKFEMDFIDEVEKQKELLIKIQHLQQDCDVPSRELRDLKLNQNMDLHIEEILKDFSESEFPSIKTEFQQVLSNRKEMTQFLEEWLNTRFDIEKLKNGIQKENDRICQVNNFFNNRIIAIMNESTEFEERSATISKEWEQDLKSLKEKNEKLFKNYQTLKTSLASGAQVNPTTQDNKNPHVTSRATQLTTEKIRELENSLHEAKESAMHKESKIIKMQKELEVTNDIIAKLQAKVHESNKCLEKTKETIQVLQDKVALGAKPYKEEIEDLKMKLVKIDLEKMKNAKEFEKEISATKATVEYQKEVIRLLRENLRRSQQAQDTSVISEHTDPQPSNKPLTCGGGSGIVQNTKALILKSEHIRLEKEISKLKQQNEQLIKQKNELLSNNQHLSNEVKTWKERTLKREAHKQVTCENSPKSPKVTGTASKKKQITPSQCKERNLQDPVPKESPKSCFFDSRSKSLPSPHPVRYFDNSSLGLCPEVQNAGAESVDSQPGPWHASSGKDVPECKTQ TTZD5QR TT Literature-reported TTZD5QR RC R-HSA-2132295:MHC class II antigen presentation; R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-68877:Mitotic Prometaphase; R-HSA-983189:Kinesins TTS7IR5 ID TTS7IR5 TTS7IR5 TN c-Jun messenger RNA (c-Jun mRNA) TTS7IR5 UP P05412 TTS7IR5 UC JUN_HUMAN TTS7IR5 BC mRNA target TTS7IR5 SN V-jun avian sarcoma virus 17 oncogene homolog (mRNA); Transcription factor AP-1 (mRNA); Proto-oncogene c-jun (mRNA); P39 (mRNA); C-jun proto-oncogene (mRNA); Activator protein-1 (mRNA); Activator protein 1 (mRNA); AP1 (mRNA); AP-1 transcription factor (mRNA) TTS7IR5 GN JUN TTS7IR5 FC Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells. Binds to the USP28 promoter in colorectal cancer (CRC) cells. Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. TTS7IR5 PD 5T01; 5FV8; 1T2K; 1S9K; 1JNM TTS7IR5 SQ MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF TTS7IR5 TT Literature-reported TTS7IR5 FM mRNA target TTS7IR5 KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04024:cAMP signaling pathway; hsa04310:Wnt signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04620:Toll-like receptor signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05030:Cocaine addiction; hsa05031:Amphetamine addiction; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05231:Choline metabolism in cancer; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis TTS7IR5 RC R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-450341:Activation of the AP-1 family of transcription factors; R-HSA-5687128:MAPK6/MAPK4 signaling TT6ATLX ID TT6ATLX TT6ATLX TN Complement factor I (CFI) TT6ATLX UP P05156 TT6ATLX UC CFAI_HUMAN TT6ATLX BC Peptidase TT6ATLX SN IF; Complement factor I light chain; C3B/C4B inactivator TT6ATLX GN CFI TT6ATLX FC Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins. Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces. The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization. Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. TT6ATLX EC EC 3.4.21.45 TT6ATLX PD 5O32; 2XRC TT6ATLX SQ MKLLHVFLLFLCFHLRFCKVTYTSQEDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEGIVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTQKADSPMDDFFQCVNGKYISQMKACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERRRIKSLLPKLSCGVKNRMHIRRKRIVGGKRAQLGDLPWQVAIKDASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEYVDRIIFHENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISNCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVCMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHVGRPFISQYNV TT6ATLX TT Literature-reported TT6ATLX FM Peptidase TT6ATLX KE hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection TT6ATLX RC R-HSA-977606:Regulation of Complement cascade TTAO58M ID TTAO58M TTAO58M TN Cryptochrome-2 (CRY2) TTAO58M UP Q49AN0 TTAO58M UC CRY2_HUMAN TTAO58M GN CRY2 TTAO58M FC Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. Less potent transcriptional repressor in cerebellum and liver than CRY1, though less effective in lengthening the period of the SCN oscillator. Seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY1, dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. May mediate circadian regulation of cAMP signaling and gluconeogenesis by blocking glucagon-mediated increases in intracellular cAMP concentrations and in CREB1 phosphorylation. Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1. Represses the CLOCK-ARNTL/BMAL1 induced transcription of NAMPT (By similarity). Represses PPARD and its target genes in the skeletal muscle and limits exercise capacity (By similarity). Represses the transcriptional activity of NR1I2 (By similarity). TTAO58M SQ MAATVATAAAVAPAPAPGTDSASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPWFAASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEYDSEPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQAIISRMELPKKPVGLVTSQQMESCRAEIQENHDETYGVPSLEELGFPTEGLGPAVWQGGETEALARLDKHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNSTPPLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWLSCSAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKAFPSRYIYEPWNAPESIQKAAKCIIGVDYPRPIVNHAETSRLNIERMKQIYQQLSRYRGLCLLASVPSCVEDLSHPVAEPSSSQAGSMSSAGPRPLPSGPASPKRKLEAAEEPPGEELSKRARVAELPTPELPSKDA TTAO58M TT Preclinical TTVZJ7G ID TTVZJ7G TTVZJ7G TN Cystathionine beta-synthase (CBS) TTVZJ7G UP P35520 TTVZJ7G UC CBS_HUMAN TTVZJ7G BC Alpha-carbonic anhydrase TTVZJ7G SN Serine sulfhydrase; Beta-thionase TTVZJ7G GN CBS TTVZJ7G FC Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine. Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons. TTVZJ7G EC EC 4.2.1.22 TTVZJ7G PD 5MMS; 4UUU; 4PCU; 4L3V; 4L28 TTVZJ7G SQ MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLLNFVAAQERDQK TTVZJ7G TT Clinical trial TTVZJ7G FM Carbon-oxygen lyases TTVZJ7G KE hsa00260:Glycine, serine and threonine metabolism; hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01230:Biosynthesis of amino acids TTMH124 ID TTMH124 TTMH124 TN Cytochrome P450 2B6 (CYP2B6) TTMH124 UP P20813 TTMH124 UC CP2B6_HUMAN TTMH124 BC Paired donor oxygen oxidoreductase TTMH124 SN Cytochrome P450 IIB1; CYPIIB6; 1,4-cineole 2-exo-monooxygenase TTMH124 GN CYP2B6 TTMH124 FC In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase. Cytochromes P450 are a group of heme-thiolate monooxygenases. TTMH124 EC EC 1.14.13.- TTMH124 PD 5WBG; 5UFG; 5UEC; 5UDA; 5UAP TTMH124 SQ MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRGLLKSFLRFREKYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNRWKVLRRFSVTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIICSIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKYFPGAHRQVYKNLQEINAYIGHSVEKHRETLDPSAPKDLIDTYLLHMEKEKSNAHSEFSHQNLNLNTLSLFFAGTETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTEAVIYEIQRFSDLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGALKKTEAFIPFSLGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKIPPTYQIRFLPR TTMH124 TT Literature-reported TTMH124 FM Oxidoreductases acting on paired donors TTU507L ID TTU507L TTU507L TN Cytoplasmic aspartate aminotransferase (GOT1) TTU507L UP P17174 TTU507L UC AATC_HUMAN TTU507L BC Transaminase TTU507L SN Glutamate oxaloacetate transaminase-1; GOT1 TTU507L GN GOT1 TTU507L FC Biosynthesis of L-glutamate from L-aspartate or L- cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3- mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. TTU507L EC EC 2.6.1.1 TTU507L PD 6DND; 6DNB; 6DNA; 3WZF; 3II0 TTU507L SQ MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQKIANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFLARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWAIRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPPAQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ TTU507L TT Literature-reported TTU507L KE hsa00250:Alanine, aspartate and glutamate metabolism; hsa00270:Cysteine and methionine metabolism; hsa00330:Arginine and proline metabolism; hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism; hsa00400:Phenylalanine, tyrosine and tryptophan biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa01210:2-Oxocarboxylic acid metabolism; hsa01230:Biosynthesis of amino acids TTU507L RC R-HSA-70263:Gluconeogenesis; R-HSA-70614:Amino acid synthesis and interconversion (transamination) TTJOCE4 ID TTJOCE4 TTJOCE4 TN Deoxycytidine kinase (DCK) TTJOCE4 UP P27707 TTJOCE4 UC DCK_HUMAN TTJOCE4 BC Kinase TTJOCE4 SN dCK TTJOCE4 GN DCK TTJOCE4 FC Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents. TTJOCE4 EC EC 2.7.1.74 TTJOCE4 PD 5MQT; 5MQL; 5MQJ; 4Q1F; 4Q1E TTJOCE4 SQ MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCNVQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAEKPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQATPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNEDFKDKYESLVEKVKEFLSTL TTJOCE4 TT Literature-reported TTM3B5R ID TTM3B5R TTM3B5R TN Diamine oxidase (AOC1) TTM3B5R UP P19801 TTM3B5R UC AOC1_HUMAN TTM3B5R BC CH-NH(2) donor oxidoreductase TTM3B5R SN Kidney amine oxidase; KAO; Histaminase; Amiloride-binding protein; AOC1; ABP TTM3B5R GN AOC1 TTM3B5R FC Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function. TTM3B5R EC EC 1.4.3.22 TTM3B5R PD 3MPH; 3K5T; 3HII; 3HIG; 3HI7 TTM3B5R SQ MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSSTTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLPGPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDRCLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNGKFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGPRLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYGGHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFEMPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMHATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENITNPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRTYRLQIHSMADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWHPPVVFEQFLHNNENIENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRDNGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV TTM3B5R TT Literature-reported TTM3B5R KE hsa00330:Arginine and proline metabolism; hsa00340:Histidine metabolism; hsa00380:Tryptophan metabolism TTH9WF6 ID TTH9WF6 TTH9WF6 TN Dibasic-processing enzyme (Furin) TTH9WF6 UP P09958 TTH9WF6 UC FURIN_HUMAN TTH9WF6 BC Peptidase TTH9WF6 SN Paired basic amino acid residuecleaving enzyme; Paired basic amino acid residue-cleaving enzyme; PCSK3; PACE; FUR; Dibasicprocessing enzyme TTH9WF6 GN FURIN TTH9WF6 FC Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. TTH9WF6 EC EC 3.4.21.75 TTH9WF6 PD 6HZD; 6HZC; 6HZB; 6HZA; 6HLE TTH9WF6 SQ MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL TTH9WF6 TT Preclinical TTH9WF6 FM Peptidase TTE5J6X ID TTE5J6X TTE5J6X TN Diphosphomevalonate decarboxylase (MVD) TTE5J6X UP P53602 TTE5J6X UC MVD1_HUMAN TTE5J6X BC Carbon-carbon lyase TTE5J6X SN Mevalonate pyrophosphate decarboxylase; Mevalonate (diphospho)decarboxylase; Mevalonate (diphospho)Diphosphomevalonate decarboxylasedecarboxylase; MVD TTE5J6X GN MVD TTE5J6X FC Performs the first committed step in the biosynthesis of isoprenes. TTE5J6X EC EC 4.1.1.33 TTE5J6X PD 3D4J TTE5J6X SQ MASEKPLAAVTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLHQDQLKTTTTAVISKDFTEDRIWLNGREEDVGQPRLQACLREIRCLARKRRNSRDGDPLPSSLSCKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGVESDLSEVARRGSGSACRSLYGGFVEWQMGEQADGKDSIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEMARCIRERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAHHGDTKVAYTFDAGPNAVIFTLDDTVAEFVAAVWHGFPPGSNGDTFLKGLQVRPAPLSAELQAALAMEPTPGGVKYIIVTQVGPGPQILDDPCAHLLGPDGLPKPAA TTE5J6X TT Literature-reported TTE5J6X RC R-HSA-191273:Cholesterol biosynthesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP) TTZN92A ID TTZN92A TTZN92A TN DUSP5 messenger RNA (DUSP5 mRNA) TTZN92A UP Q16690 TTZN92A UC DUS5_HUMAN TTZN92A BC mRNA target TTZN92A SN VH3 (mRNA); Dual specificity protein phosphatase hVH3 (mRNA); Dual specificity protein phosphatase 5 (mRNA) TTZN92A GN DUSP5 TTZN92A FC The highest relative activity is toward ERK1. Dual specificity protein phosphatase; active with phosphotyrosine, phosphoserine and phosphothreonine residues. TTZN92A EC EC 3.1.3.16 TTZN92A PD 2G6Z TTZN92A SQ MKVTSLDGRQLRKMLRKEAAARCVVLDCRPYLAFAASNVRGSLNVNLNSVVLRRARGGAVSARYVLPDEAARARLLQEGGGGVAAVVVLDQGSRHWQKLREESAARVVLTSLLACLPAGPRVYFLKGGYETFYSEYPECCVDVKPISQEKIESERALISQCGKPVVNVSYRPAYDQGGPVEILPFLYLGSAYHASKCEFLANLHITALLNVSRRTSEACATHLHYKWIPVEDSHTADISSHFQEAIDFIDCVREKGGKVLVHCEAGISRSPTICMAYLMKTKQFRLKEAFDYIKQRRSMVSPNFGFMGQLLQYESEILPSTPNPQPPSCQGEAAGSSLIGHLQTLSPDMQGAYCTFPASVLAPVPTHSTVSELSRSPVATATSC TTZN92A TT Literature-reported TTZN92A FM mRNA target TTZN92A KE hsa04010:MAPK signaling pathway TTZN92A RC R-HSA-112409:RAF-independent MAPK1/3 activation; R-HSA-5675221:Negative regulation of MAPK pathway TTK0TF2 ID TTK0TF2 TTK0TF2 TN DUSP8 messenger RNA (DUSP8 mRNA) TTK0TF2 UP Q13202 TTK0TF2 UC DUS8_HUMAN TTK0TF2 BC mRNA target TTK0TF2 SN VH5 (mRNA); Dual specificity protein phosphatase hVH-5 (mRNA); Dual specificity protein phosphatase 8 (mRNA); C11orf81 (mRNA) TTK0TF2 GN DUSP8 TTK0TF2 FC Expected to display protein phosphatase activity toward phosphotyrosine, phosphoserine and phosphothreonine residues. Has phosphatase activity with synthetic phosphatase substrates and negatively regulates mitogen-activated protein kinase activity, presumably by catalysing their dephosphorylation. TTK0TF2 EC EC 3.1.3.16 TTK0TF2 PD 4JMK TTK0TF2 SQ MAGDRLPRKVMDAKKLASLLRGGPGGPLVIDSRSFVEYNSWHVLSSVNICCSKLVKRRLQQGKVTIAELIQPAARSQVEATEPQDVVVYDQSTRDASVLAADSFLSILLSKLDGCFDSVAILTGGFATFSSCFPGLCEGKPAALLPMSLSQPCLPVPSVGLTRILPHLYLGSQKDVLNKDLMTQNGISYVLNASNSCPKPDFICESRFMRVPINDNYCEKLLPWLDKSIEFIDKAKLSSCQVIVHCLAGISRSATIAIAYIMKTMGMSSDDAYRFVKDRRPSISPNFNFLGQLLEYERSLKLLAALQGDPGTPSGTPEPPPSPAAGAPLPRLPPPTSESAATGNAAAREGGLSAGGEPPAPPTPPATSALQQGLRGLHLSSDRLQDTNRLKRSFSLDIKSAYAPSRRPDGPGPPDPGEAPKLCKLDSPSGAALGLSSPSPDSPDAAPEARPRPRRRPRPPAGSPARSPAHSLGLNFGDAARQTPRHGLSALSAPGLPGPGQPAGPGAWAPPLDSPGTPSPDGPWCFSPEGAQGAGGVLFAPFGRAGAPGPGGGSDLRRREAARAEPRDARTGWPEEPAPETQFKRRSCQMEFEEGMVEGRARGEELAALGKQASFSGSVEVIEVS TTK0TF2 TT Literature-reported TTK0TF2 FM mRNA target TTK0TF2 KE hsa04010:MAPK signaling pathway TTK0TF2 RC R-HSA-112409:RAF-independent MAPK1/3 activation; R-HSA-5675221:Negative regulation of MAPK pathway TT1GV6C ID TT1GV6C TT1GV6C TN DUSP9 messenger RNA (DUSP9 mRNA) TT1GV6C UP Q99956 TT1GV6C UC DUS9_HUMAN TT1GV6C BC mRNA target TT1GV6C SN Mitogen-activated protein kinase phosphatase 4 (mRNA); MKP4 (mRNA); MKP-4 (mRNA); MAP kinase phosphatase 4 (mRNA); Dual specificity protein phosphatase 9 (mRNA) TT1GV6C GN DUSP9 TT1GV6C FC Has a specificity for the ERK family. Inactivates MAP kinases. TT1GV6C EC EC 3.1.3.16 TT1GV6C PD 3LJ8; 2HXP TT1GV6C SQ MEGLGRSCLWLRRELSPPRPRLLLLDCRSRELYESARIGGALSVALPALLLRRLRRGSLSVRALLPGPPLQPPPPAPVLLYDQGGGRRRRGEAEAEAEEWEAESVLGTLLQKLREEGYLAYYLQGGFSRFQAECPHLCETSLAGRAGSSMAPVPGPVPVVGLGSLCLGSDCSDAESEADRDSMSCGLDSEGATPPPVGLRASFPVQILPNLYLGSARDSANLESLAKLGIRYILNVTPNLPNFFEKNGDFHYKQIPISDHWSQNLSRFFPEAIEFIDEALSQNCGVLVHCLAGVSRSVTVTVAYLMQKLHLSLNDAYDLVKRKKSNISPNFNFMGQLLDFERSLRLEERHSQEQGSGGQASAASNPPSFFTTPTSDGAFELAPT TT1GV6C TT Literature-reported TT1GV6C FM mRNA target TT1GV6C KE hsa04010:MAPK signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells TT1GV6C RC R-HSA-112409:RAF-independent MAPK1/3 activation; R-HSA-5675221:Negative regulation of MAPK pathway TTAMCSL ID TTAMCSL TTAMCSL TN E3 ubiquitin-protein ligase TRIM37 (TRIM37) TTAMCSL UP O94972 TTAMCSL UC TRI37_HUMAN TTAMCSL BC TRIM/RBCC family TTAMCSL SN Tripartite motif-containing protein 37; RING-type E3 ubiquitin transferase TRIM37; Mulibrey nanism protein TTAMCSL GN TRIM37 TTAMCSL FC E3 ubiquitin-protein ligase required to prevent centriole reduplication (PubMed:15885686, PubMed:23769972). Probably acts by ubiquitinating positive regulators of centriole reduplication (PubMed:23769972). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes (PubMed:25470042). Has anti-HIV activity (PubMed:24317724). TTAMCSL EC EC 2.3.2.27 TTAMCSL PD 3LRQ TTAMCSL SQ MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQLCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILRFQVRSPTFFQKSRDQHWYITQLEAAQTSYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDALETRAKKSACSDMLLEGGPTTASVREAKEDEEDEEKIQNEDYHHELSDGDLDLDLVYEDEVNQLDGSSSSASSTATSNTEENDIDEETMSGENDVEYNNMELEEGELMEDAAAAGPAGSSHGYVGSSSRISRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSIENLWGLQPRPPASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKNTLSEIKSSSAASGDMQTSLFSADQAALAACGTENSGRLQDLGMELLAKSSVANCYIRNSTNKKSNSPKPARSSVAGSLSLRRAVDPGENSRSKGDCQTLSEGSPGSSQSGSRHSSPRALIHGSIGDILPKTEDRQCKALDSDAVVVAVFSGLPAVEKRRKMVTLGANAKGGHLEGLQMTDLENNSETGELQPVLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSVGGFHDSFMVMTQPPDEDTHSSFPDGEQIGPEDLSFNTDENSGR TTAMCSL TT Literature-reported TTAMCSL KE hsa04120:Ubiquitin mediated proteolysis TTNSM2I ID TTNSM2I TTNSM2I TN Endopeptidase S1P (MBTPS1) TTNSM2I UP Q14703 TTNSM2I UC MBTP1_HUMAN TTNSM2I BC Peptidase TTNSM2I SN Subtilisin/kexin-isozyme-1; Subtilisin/kexin-isozyme 1; Site-1 protease; SKI1; SKI-1; S1P; Membrane-bound transcription factor site-1 protease; KIAA0091 TTNSM2I GN MBTPS1 TTNSM2I FC Other known substrates are BDNF, GNPTAB and ATF6. Cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4. Cleaves known substrates after Arg-Ser-Val-Leu (SERBP-2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu. Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysosomes. Serine protease that catalyzes the first step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs). TTNSM2I EC EC 3.4.21.112 TTNSM2I SQ MKLVNIWLLLLVVLLCGKKHLGDRLEKKSFEKAPCPGCSHLTLKVEFSSTVVEYEYIVAFNGYFTAKARNSFISSALKSSEVDNWRIIPRNNPSSDYPSDFEVIQIKEKQKAGLLTLEDHPNIKRVTPQRKVFRSLKYAESDPTVPCNETRWSQKWQSSRPLRRASLSLGSGFWHATGRHSSRRLLRAIPRQVAQTLQADVLWQMGYTGANVRVAVFDTGLSEKHPHFKNVKERTNWTNERTLDDGLGHGTFVAGVIASMRECQGFAPDAELHIFRVFTNNQVSYTSWFLDAFNYAILKKIDVLNLSIGGPDFMDHPFVDKVWELTANNVIMVSAIGNDGPLYGTLNNPADQMDVIGVGGIDFEDNIARFSSRGMTTWELPGGYGRMKPDIVTYGAGVRGSGVKGGCRALSGTSVASPVVAGAVTLLVSTVQKRELVNPASMKQALIASARRLPGVNMFEQGHGKLDLLRAYQILNSYKPQASLSPSYIDLTECPYMWPYCSQPIYYGGMPTVVNVTILNGMGVTGRIVDKPDWQPYLPQNGDNIEVAFSYSSVLWPWSGYLAISISVTKKAASWEGIAQGHVMITVASPAETESKNGAEQTSTVKLPIKVKIIPTPPRSKRVLWDQYHNLRYPPGYFPRDNLRMKNDPLDWNGDHIHTNFRDMYQHLRSMGYFVEVLGAPFTCFDASQYGTLLMVDSEEEYFPEEIAKLRRDVDNGLSLVIFSDWYNTSVMRKVKFYDENTRQWWMPDTGGANIPALNELLSVWNMGFSDGLYEGEFTLANHDMYYASGCSIAKFPEDGVVITQTFKDQGLEVLKQETAVVENVPILGLYQIPAEGGGRIVLYGDSNCLDDSHRQKDCFWLLDALLQYTSYGVTPPSLSHSGNRQRPPSGAGSVTPERMEGNHLHRYSKVLEAHLGDPKPRPLPACPRLSWAKPQPLNETAPSNLWKHQKLLSIDLDKVVLPNFRSNRPQVRPLSPGESGAWDIPGGIMPGRYNQEVGQTIPVFAFLGAMVVLAFFVVQINKAKSRPKRRKPRVKRPQLMQQVHPPKTPSV TTNSM2I TT Literature-reported TTNSM2I KE hsa04141:Protein processing in endoplasmic reticulum TTG84D3 ID TTG84D3 TTG84D3 TN Ephrin type-A receptor 4 (EPHA4) TTG84D3 UP P54764 TTG84D3 UC EPHA4_HUMAN TTG84D3 BC Kinase TTG84D3 SN hEK8; Tyrosineprotein kinase receptor SEK; Tyrosineprotein kinase TYRO1; Tyrosine-protein kinase receptor SEK; Tyrosine-protein kinase TYRO1; TYRO1; SEK; Ephrin typeA receptor 4; EPHlike kinase 8; EPH-like kinase 8; EK8 TTG84D3 GN EPHA4 TTG84D3 FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, plays also a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium. Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TTG84D3 EC EC 2.7.10.1 TTG84D3 PD 5JR2; 4W50; 4W4Z; 4M4R; 4M4P TTG84D3 SQ MAGIFYFALFSCLFGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEERSGECQACKIGYYKALSTDATCAKCPPHSYSVWEGATSCTCDRGFFRADNDAASMPCTRPPSAPLNLISNVNETSVNLEWSSPQNTGGRQDISYNVVCKKCGAGDPSKCRPCGSGVHYTPQQNGLKTTKVSITDLLAHTNYTFEIWAVNGVSKYNPNPDQSVSVTVTTNQAAPSSIALVQAKEVTRYSVALAWLEPDRPNGVILEYEVKYYEKDQNERSYRIVRTAARNTDIKGLNPLTSYVFHVRARTAAGYGDFSEPLEVTTNTVPSRIIGDGANSTVLLVSVSGSVVLVVILIAAFVISRRRSKYSKAKQEADEEKHLNQGVRTYVDPFTYEDPNQAVREFAKEIDASCIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRPKFGQIVNMLDKLIRNPNSLKRTGTESSRPNTALLDPSSPEFSAVVSVGDWLQAIKMDRYKDNFTAAGYTTLEAVVHVNQEDLARIGITAITHQNKILSSVQAMRTQMQQMHGRMVPV TTG84D3 TT Literature-reported TTG84D3 FM Kinase TTG84D3 KE hsa04360:Axon guidance TTG84D3 RC R-HSA-2682334:EPH-Ephrin signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-3928665:EPH-ephrin mediated repulsion of cells TTSINU2 ID TTSINU2 TTSINU2 TN ERBB3 messenger RNA (ERBB3 mRNA) TTSINU2 UP P21860 TTSINU2 UC ERBB3_HUMAN TTSINU2 BC mRNA target TTSINU2 SN Tyrosine kinase-type cell surface receptor HER3 (mRNA); Receptor tyrosine-protein kinase erbB-3 (mRNA); Proto-oncogene-like protein c-ErbB-3 (mRNA); HER3 (mRNA); C-erbB3 (mRNA); C-erbB-3 protein (mRNA) TTSINU2 GN ERBB3 TTSINU2 FC Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5. Involved in the regulation of myeloid cell differentiation. Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. TTSINU2 EC EC 2.7.10.1 TTSINU2 PD 5O7P; 5O4O; 5CUS; 4RIY; 4RIX TTSINU2 SQ MRANDALQVLGLLFSLARGSEVGNSQAVCPGTLNGLSVTGDAENQYQTLYKLYERCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNGRSCPPCHEVCKGRCWGPGSEDCQTLTKTICAPQCNGHCFGPNPNQCCHDECAGGCSGPQDTDCFACRHFNDSGACVPRCPQPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTSCVRACPPDKMEVDKNGLKMCEPCGGLCPKACEGTGSGSRFQTVDSSNIDGFVNCTKILGNLDFLITGLNGDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRIYISANRQLCYHHSLNWTKVLRGPTEERLDIKHNRPRRDCVAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSRGGVCVTHCNFLNGEPREFAHEAECFSCHPECQPMEGTATCNGSGSDTCAQCAHFRDGPHCVSSCPHGVLGAKGPIYKYPDVQNECRPCHENCTQGCKGPELQDCLGQTLVLIGKTHLTMALTVIAGLVVIFMMLGGTFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFGVADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRESGPGIAPGPEPHGLTNKKLEEVELEPELDLDLDLEAEEDNLATTTLGSALSLPVGTLNRPRGSQSLLSPSSGYMPMNQGNLGESCQESAVSGSSERCPRPVSLHPMPRGCLASESSEGHVTGSEAELQEKVSMCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDVNGYVMPDTHLKGTPSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRRRRHSPPHPPRPSSLEELGYEYMDVGSDLSASLGSTQSCPLHPVPIMPTAGTTPDEDYEYMNRQRDGGGPGGDYAAMGACPASEQGYEEMRAFQGPGHQAPHVHYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT TTSINU2 TT Literature-reported TTSINU2 FM mRNA target TTSINU2 KE hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04144:Endocytosis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer TTV3O87 ID TTV3O87 TTV3O87 TN ERK activator kinase 5 (MAP2K5) TTV3O87 UP Q13163 TTV3O87 UC MP2K5_HUMAN TTV3O87 BC Kinase TTV3O87 SN PRKMK5; Mitogen-activatedprotein kinase kinase 5; MKK5; MEK5; MEK 5; MAPKK 5; MAPK/ERK kinase 5; MAP kinase kinase5; MAP kinase kinase 5; Dual specificity mitogen-activated protein kinase kinase 5 TTV3O87 GN MAP2K5 TTV3O87 FC Activation of this pathway appears to play a critical role in protecting cells from stress-induced apoptosis, neuronal survival and cardiac development and angiogenesis. Acts as a scaffold for the formation of a ternary MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. TTV3O87 EC EC 2.7.12.2 TTV3O87 PD 4IC7; 2O2V; 2NPT TTV3O87 SQ MLWLALGPFPAMENQVLVIRIKIPNSGAVDWTVHSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYYSTVMEQQVNGQLIEPLQIFPRACKPPGERNIHGLKVNTRAGPSQHSSPAVSDSLPSNSLKKSSAELKKILANGQMNEQDIRYRDTLGHGNGGTVYKAYHVPSGKILAVKVILLDITLELQKQIMSELEILYKCDSSYIIGFYGAFFVENRISICTEFMDGGSLDVYRKMPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSLMPLQLLQCIVDEDSPVLPVGEFSEPFVHFITQCMRKQPKERPAPEELMGHPFIVQFNDGNAAVVSMWVCRALEERRSQQGPP TTV3O87 TT Literature-reported TTV3O87 FM Kinase TT405FP ID TT405FP TT405FP TN FAP-1 messenger RNA (PTPN13 mRNA) TT405FP UP Q12923 TT405FP UC PTN13_HUMAN TT405FP BC mRNA target TT405FP SN hPTPE1 (mRNA); Tyrosine-protein phosphatase non-receptor type 13 (mRNA); Protein-tyrosine phosphatase PTPL1 (mRNA); Protein-tyrosine phosphatase 1E (mRNA); PTPL1 (mRNA); PTP1E (mRNA); PTP-E1 (mRNA); PTP-BAS (mRNA); PNP1 (mRNA); Fas-associated protein-tyrosine phosphatase 1 (mRNA); FAP-1 (mRNA) TT405FP GN PTPN13 TT405FP FC May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2. Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling. TT405FP EC EC 3.1.3.48 TT405FP PD 5GLJ; 3PDZ; 3LNY; 3LNX; 2M10 TT405FP SQ MHVSLAEALEVRGGPLQEEEIWAVLNQSAESLQELFRKVSLADPAALGFIISPWSLLLLPSGSVSFTDENISNQDLRAFTAPEVLQNQSLTSLSDVEKIHIYSLGMTLYWGADYEVPQSQPIKLGDHLNSILLGMCEDVIYARVSVRTVLDACSAHIRNSNCAPSFSYVKHLVKLVLGNLSGTDQLSCNSEQKPDRSQAIRDRLRGKGLPTGRSSTSDVLDIQKPPLSHQTFLNKGLSKSMGFLSIKDTQDENYFKDILSDNSGREDSENTFSPYQFKTSGPEKKPIPGIDVLSKKKIWASSMDLLCTADRDFSSGETATYRRCHPEAVTVRTSTTPRKKEARYSDGSIALDIFGPQKMDPIYHTRELPTSSAISSALDRIRERQKKLQVLREAMNVEEPVRRYKTYHGDVFSTSSESPSIISSESDFRQVRRSEASKRFESSSGLPGVDETLSQGQSQRPSRQYETPFEGNLINQEIMLKRQEEELMQLQAKMALRQSRLSLYPGDTIKASMLDITRDPLREIALETAMTQRKLRNFFGPEFVKMTIEPFISLDLPRSILTKKGKNEDNRRKVNIMLLNGQRLELTCDTKTICKDVFDMVVAHIGLVEHHLFALATLKDNEYFFVDPDLKLTKVAPEGWKEEPKKKTKATVNFTLFFRIKFFMDDVSLIQHTLTCHQYYLQLRKDILEERMHCDDETSLLLASLALQAEYGDYQPEVHGVSYFRMEHYLPARVMEKLDLSYIKEELPKLHNTYVGASEKETELEFLKVCQRLTEYGVHFHRVHPEKKSQTGILLGVCSKGVLVFEVHNGVRTLVLRFPWRETKKISFSKKKITLQNTSDGIKHGFQTDNSKICQYLLHLCSYQHKFQLQMRARQSNQDAQDIERASFRSLNLQAESVRGFNMGRAISTGSLASSTLNKLAVRPLSVQAEILKRLSCSELSLYQPLQNSSKEKNDKASWEEKPREMSKSYHDLSQASLYPHRKNVIVNMEPPPQTVAELVGKPSHQMSRSDAESLAGVTKLNNSKSVASLNRSPERRKHESDSSSIEDPGQAYVLGMTMHSSGNSSSQVPLKENDVLHKRWSIVSSPEREITLVNLKKDAKYGLGFQIIGGEKMGRLDLGIFISSVAPGGPADLDGCLKPGDRLISVNSVSLEGVSHHAAIEILQNAPEDVTLVISQPKEKISKVPSTPVHLTNEMKNYMKKSSYMQDSAIDSSSKDHHWSRGTLRHISENSFGPSGGLREGSLSSQDSRTESASLSQSQVNGFFASHLGDQTWQESQHGSPSPSVISKATEKETFTDSNQSKTKKPGISDVTDYSDRGDSDMDEATYSSSQDHQTPKQESSSSVNTSNKMNFKTFSSSPPKPGDIFEVELAKNDNSLGISVTGGVNTSVRHGGIYVKAVIPQGAAESDGRIHKGDRVLAVNGVSLEGATHKQAVETLRNTGQVVHLLLEKGQSPTSKEHVPVTPQCTLSDQNAQGQGPEKVKKTTQVKDYSFVTEENTFEVKLFKNSSGLGFSFSREDNLIPEQINASIVRVKKLFPGQPAAESGKIDVGDVILKVNGASLKGLSQQEVISALRGTAPEVFLLLCRPPPGVLPEIDTALLTPLQSPAQVLPNSSKDSSQPSCVEQSTSSDENEMSDKSKKQCKSPSRRDSYSDSSGSGEDDLVTAPANISNSTWSSALHQTLSNMVSQAQSHHEAPKSQEDTICTMFYYPQKIPNKPEFEDSNPSPLPPDMAPGQSYQPQSESASSSSMDKYHIHHISEPTRQENWTPLKNDLENHLEDFELEVELLITLIKSEKGSLGFTVTKGNQRIGCYVHDVIQDPAKSDGRLKPGDRLIKVNDTDVTNMTHTDAVNLLRAASKTVRLVIGRVLELPRIPMLPHLLPDITLTCNKEELGFSLCGGHDSLYQVVYISDINPRSVAAIEGNLQLLDVIHYVNGVSTQGMTLEEVNRALDMSLPSLVLKATRNDLPVVPSSKRSAVSAPKSTKGNGSYSVGSCSQPALTPNDSFSTVAGEEINEISYPKGKCSTYQIKGSPNLTLPKESYIQEDDIYDDSQEAEVIQSLLDVVDEEAQNLLNENNAAGYSCGPGTLKMNGKLSEERTEDTDCDGSPLPEYFTEATKMNGCEEYCEEKVKSESLIQKPQEKKTDDDEITWGNDELPIERTNHEDSDKDHSFLTNDELAVLPVVKVLPSGKYTGANLKSVIRVLRGLLDQGIPSKELENLQELKPLDQCLIGQTKENRRKNRYKNILPYDATRVPLGDEGGYINASFIKIPVGKEEFVYIACQGPLPTTVGDFWQMIWEQKSTVIAMMTQEVEGEKIKCQRYWPNILGKTTMVSNRLRLALVRMQQLKGFVVRAMTLEDIQTREVRHISHLNFTAWPDHDTPSQPDDLLTFISYMRHIHRSGPIITHCSAGIGRSGTLICIDVVLGLISQDLDFDISDLVRCMRLQRHGMVQTEDQYIFCYQVILYVLTRLQAEEEQKQQPQLLK TT405FP TT Patented-recorded TT405FP FM mRNA target TTUX14L ID TTUX14L TTUX14L TN F-box only protein 3 (FBXO3) TTUX14L UP Q9UK99 TTUX14L UC FBX3_HUMAN TTUX14L GN FBXO3 TTUX14L FC Substrate recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. In the presence of PML, HIPK2 ubiquitination still occurs, but degradation is prevented. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. TTUX14L SQ MAAMETETAPLTLESLPTDPLLLILSFLDYRDLINCCYVSRRLSQLSSHDPLWRRHCKKYWLISEEEKTQKNQCWKSLFIDTYSDVGRYIDHYAAIKKAWDDLKKYLEPRCPRMVLSLKEGAREEDLDAVEAQIGCKLPDDYRCSYRIHNGQKLVVPGLLGSMALSNHYRSEDLLDVDTAAGGFQQRQGLKYCLPLTFCIHTGLSQYIAVEAAEGRNKNEVFYQCPDQMARNPAAIDMFIIGATFTDWFTSYVKNVVSGGFPIIRDQIFRYVHDPECVATTGDITVSVSTSFLPELSSVHPPHYFFTYRIRIEMSKDALPEKACQLDSRYWRITNAKGDVEEVQGPGVVGEFPIISPGRVYEYTSCTTFSTTSGYMEGYYTFHFLYFKDKIFNVAIPRFHMACPTFRVSIARLEMGPDEYEEMEEEEEEEEEEDEDDDSADMDESDEDDEEERRRRVFDVPIRRRRCSRLF TTUX14L TT Preclinical TTTEFBV ID TTTEFBV TTTEFBV TN Focal adhesion kinase 2 (PTK2B) TTTEFBV UP Q14289 TTTEFBV UC FAK2_HUMAN TTTEFBV BC Kinase TTTEFBV SN Related adhesion focal tyrosine kinase; RAFTK; Protein-tyrosine kinase 2-beta; Proline-rich tyrosine kinase 2; PYK2; FAK2; FADK 2; Cell adhesion kinase beta; Calcium-regulated non-receptor proline-rich tyrosine kinase; Calcium-dependent tyrosine kinase; CAKB; CAK-beta; CADTK TTTEFBV GN PTK2B TTTEFBV FC Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2. Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. TTTEFBV EC EC 2.7.10.2 TTTEFBV PD 5TOB; 5TO8; 4XEV; 4XEK; 4XEF TTTEFBV SQ MSGVSEPLSRVKLGTLRRPEGPAEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIREIITSILLSGRIGPNIRLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDAKPTCLAEFKQIRSIRCLPLEEGQAVLQLGIEGAPQALSIKTSSLAEAENMADLIDGYCRLQGEHQGSLIIHPRKDGEKRNSLPQIPMLNLEARRSHLSESCSIESDIYAEIPDETLRRPGGPQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAMEQERNARYRTPKILEPTAFQEPPPKPSRPKYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIQPSSREEAQQLWEAEKVKMRQILDKQQKQMVEDYQWLRQEEKSLDPMVYMNDKSPLTPEKEVGYLEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYLNVMELVRAVLELKNELCQLPPEGYVVVVKNVGLTLRKLIGSVDDLLPSLPSSSRTEIEGTQKLLNKDLAELINKMRLAQQNAVTSLSEECKRQMLTASHTLAVDAKNLLDAVDQAKVLANLAHPPAE TTTEFBV TT Literature-reported TTTEFBV FM Kinase TTTEFBV KE hsa04020:Calcium signaling pathway; hsa04062:Chemokine signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04670:Leukocyte transendothelial migration; hsa04912:GnRH signaling pathway; hsa05161:Hepatitis B TTTEFBV RC R-HSA-391160:Signal regulatory protein (SIRP) family interactions; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-451927:Interleukin-2 signaling TTS3H9L ID TTS3H9L TTS3H9L TN Fungal Phosphatidylinositol 4-kinase PIK1 (Fung PIK1) TTS3H9L UP P39104 TTS3H9L UC PIK1_YEAST TTS3H9L BC Kinase TTS3H9L SN PtdIns4kinase; Phosphatidylinositol 4kinase PIK1; PIK1; PI4kinase TTS3H9L GN Fung PIK1 TTS3H9L FC Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,- trisphosphate. PIK1 is part of a nuclear phosphoinositide cycle and could control cytokinesis through the actin cytoskeleton. TTS3H9L EC EC 2.7.1.67 TTS3H9L PD 2JU0 TTS3H9L SQ MHKASSSKKSFDDTIELKKNEQLLKLINSSEFTLHNCVELLCKHSENIGIHYYLCQKLATFPHSELQFYIPQLVQVLVTMETESMALEDLLLRLRAENPHFALLTFWQLQALLTDLSTDPASYGFQVARRVLNNLQTNLFNTSSGSDKNVKIHENVAPALVLSSMIMSAIAFPQLSEVTKPLVESQGRRQKAFVFKLARSAMKDFTKNMTLKNTLLNKKTSRSKRVSSNRSSTPTSPIDLIDPIKTKEDASFRKSRHSEVKLDFDIVDDIGNQVFEERISSSIKLPKRKPKYLDNSYVHRTYDGKNINRDGSISNTAKALDGNKGDYISPKGRNDENNEIGNNEDETGGETEEDADALNSDHFTSSMPDLHNIQPRTSSASSASLEGTPKLNRTNSQPLSRQAFKNSKKANSSLSQEIDLSQLSTTSKIKMLKANYFRCETQFAIALETISQRLARVPTEARLSALRAELFLLNRDLPAEVDIPTLLPPNKKGKLHKLVTITANEAQVLNSAEKVPYLLLIEYLRDEFDFDPTSETNERLLKKISGNQGGLIFDLNYMNRKENNENRNESTLTSNNTRSSVYDSNSFNNGASRNEGLSSTSRSDSASTAHVRTEVNKEEDLGDMSMVKVRNRTDDEAYRNALVIQSAANVPILPDDSQDRSPELNFGSNLDEVLIENGINSKNIHSQTDALADQMRVSAVMLAQLDKSPQQLSESTKQIRAQIISSMKEVQDKFGYHDLEALHGMAGERKLENDLMTGGIDTSYLGEDWATKKERIRKTSEYGHFENWDLCSVIAKTGDDLRQEAFAYQMIQAMANIWVKEKVDVWVKRMKILITSANTGLVETITNAMSVHSIKKALTKKMIEDAELDDKGGIASLNDHFLRAFGNPNGFKYRRAQDNFASSLAAYSVICYLLQVKDRHNGNIMIDNEGHVSHIDFGFMLSNSPGSVGFEAAPFKLTYEYIELLGGVEGEAFKKFVELTKSSFKALRKYADQIVSMCEIMQKDNMQPCFDAGEQTSVQLRQRFQLDLSEKEVDDFVENFLIGKSLGSIYTRIYDQFQLITQGIYS TTS3H9L TT Literature-reported TTS3H9L KE sce00562:Inositol phosphate metabolism; sce01100:Metabolic pathways; sce04070:Phosphatidylinositol signaling system TT64EPS ID TT64EPS TT64EPS TN Fungal Scytalone dehydratase (Fung SDH1) TT64EPS UP P56221 TT64EPS UC SCYD_MAGO7 TT64EPS BC Alpha-carbonic anhydrase TT64EPS SN SDH1 TT64EPS GN Fung SDH1 TT64EPS FC Catalyzes two steps in melanin biosynthesis. From scytalone they are two dehydration steps and one reduction step to yield melanin. TT64EPS EC EC 4.2.1.94 TT64EPS PD 7STD; 6STD; 5STD; 4STD; 3STD TT64EPS SQ MGSQVQKSDEITFSDYLGLMTCVYEWADSYDSKDWDRLRKVIAPTLRIDYRSFLDKLWEAMPAEEFVGMVSSKQVLGDPTLRTQHFIGGTRWEKVSEDEVIGYHQLRVPHQRYKDTTMKEVTMKGHAHSANLHWYKKIDGVWKFAGLKPDIRWGEFDFDRIFEDGRETFGDK TT64EPS TT Literature-reported TT40HS5 ID TT40HS5 TT40HS5 TN Gastric inhibitory polypeptide (GIP) TT40HS5 UP P09681 TT40HS5 UC GIP_HUMAN TT40HS5 BC Glucagon TT40HS5 SN Glucose-dependent insulinotropic polypeptide; GIP TT40HS5 GN GIP TT40HS5 FC Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion. TT40HS5 PD 2QKH; 2OBU; 2L71; 2L70; 2B4N TT40HS5 SQ MVATKTFALLLLSLFLAVGLGEKKEGHFSALPSLPVGSHAKVSSPQPRGPRYAEGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQREARALELASQANRKEEEAVEPQSSPAKNPSDEDLLRDLLIQELLACLLDQTNLCRLRSR TT40HS5 TT Literature-reported TT40HS5 KE hsa04911:Insulin secretion TT40HS5 RC R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors TT6Y4PN ID TT6Y4PN TT6Y4PN TN Glucagon-like peptide 1 (GLP-1:7-37) TT6Y4PN UP P01275 (92-128) TT6Y4PN UC GLUC_HUMAN TT6Y4PN BC Glucagon TT6Y4PN SN Glucagon-like peptide-1(7-36)-amide; GLP-1 (92-128); GLP; GCG TT6Y4PN GN GCG TT6Y4PN FC Glicentin may modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life. TT6Y4PN PD 6EDS; 5YQZ; 5VAI; 5OTX; 5OTW TT6Y4PN SQ HDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG TT6Y4PN TT Literature-reported TT6Y4PN KE hsa04911:Insulin secretion; hsa04922:Glucagon signaling pathway TT6Y4PN RC R-HSA-163359:Glucagon signaling in metabolic regulation; R-HSA-381676:Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-416476:G alpha (q) signalling events; R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors TTCFP0V ID TTCFP0V TTCFP0V TN Glutamine amidotransferase (GMPS) TTCFP0V UP P49915 TTCFP0V UC GUAA_HUMAN TTCFP0V BC Carbon-nitrogen ligase TTCFP0V SN GMP synthetase; GMP synthase [glutamine-hydrolyzing] TTCFP0V GN GMPS TTCFP0V FC Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division. TTCFP0V EC EC 6.3.5.2 TTCFP0V PD 2VXO; 2VPI TTCFP0V SQ MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILRESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE TTCFP0V TT Literature-reported TTCFP0V FM Carbon-nitrogen ligase TTCFP0V KE hsa00230:Purine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways TTCFP0V RC R-HSA-73817:Purine ribonucleoside monophosphate biosynthesis TTY6C71 ID TTY6C71 TTY6C71 TN G-protein coupled receptor 48 (LGR4) TTY6C71 UP Q9BXB1 TTY6C71 UC LGR4_HUMAN TTY6C71 SN G-protein coupled receptor 48 TTY6C71 GN LGR4 TTY6C71 FC Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May also act as a receptor for norrin (NDP), such results however require additional confirmation in vivo. Required during spermatogenesis to activate the Wnt signaling pathway in peritubular myoid cells. Required for the maintenance of intestinal stem cells and Paneth cell differentiation in postnatal intestinal crypts. Acts as a regulator of bone formation and remodeling. Involved in kidney development; required for maintaining the ureteric bud in an undifferentiated state. Involved in the development of the anterior segment of the eye. Required during erythropoiesis. Also acts as a negative regulator of innate immunity by inhibiting TLR2/TLR4 associated pattern-recognition and proinflammatory cytokine production. Plays an important role in regulating the circadian rhythms of plasma lipids, partially through regulating the rhythmic expression of MTTP (By similarity). TTY6C71 SQ MPGPLGLLCFLALGLLGSAGPSGAAPPLCAAPCSCDGDRRVDCSGKGLTAVPEGLSAFTQALDISMNNITQLPEDAFKNFPFLEELQLAGNDLSFIHPKALSGLKELKVLTLQNNQLKTVPSEAIRGLSALQSLRLDANHITSVPEDSFEGLVQLRHLWLDDNSLTEVPVHPLSNLPTLQALTLALNKISSIPDFAFTNLSSLVVLHLHNNKIRSLSQHCFDGLDNLETLDLNYNNLGEFPQAIKALPSLKELGFHSNSISVIPDGAFDGNPLLRTIHLYDNPLSFVGNSAFHNLSDLHSLVIRGASMVQQFPNLTGTVHLESLTLTGTKISSIPNNLCQEQKMLRTLDLSYNNIRDLPSFNGCHALEEISLQRNQIYQIKEGTFQGLISLRILDLSRNLIHEIHSRAFATLGPITNLDVSFNELTSFPTEGLNGLNQLKLVGNFKLKEALAAKDFVNLRSLSVPYAYQCCAFWGCDSYANLNTEDNSLQDHSVAQEKGTADAANVTSTLENEEHSQIIIHCTPSTGAFKPCEYLLGSWMIRLTVWFIFLVALFFNLLVILTTFASCTSLPSSKLFIGLISVSNLFMGIYTGILTFLDAVSWGRFAEFGIWWETGSGCKVAGFLAVFSSESAIFLLMLATVERSLSAKDIMKNGKSNHLKQFRVAALLAFLGATVAGCFPLFHRGEYSASPLCLPFPTGETPSLGFTVTLVLLNSLAFLLMAVIYTKLYCNLEKEDLSENSQSSMIKHVAWLIFTNCIFFCPVAFFSFAPLITAISISPEIMKSVTLIFFPLPACLNPVLYVFFNPKFKEDWKLLKRRVTKKSGSVSVSISSQGGCLEQDFYYDCGMYSHLQGNLTVCDCCESFLLTKPVSCKHLIKSHSCPALAVASCQRPEGYWSDCGTQSAHSDYADEEDSFVSDSSDQVQACGRACFYQSRGFPLVRYAYNLPRVKD TTY6C71 TT Preclinical TTKEPHX ID TTKEPHX TTKEPHX TN Granzyme B (GZMB) TTKEPHX UP P10144 TTKEPHX UC GRAB_HUMAN TTKEPHX BC Peptidase TTKEPHX SN Tcell serine protease 13E; SECT; Lymphocyte protease; Human lymphocyte protein; Granzyme2; GZMB; Fragmentin2; Cytotoxic Tlymphocyte proteinase 2; Cathepsin Glike 1; CTSGL1; CTLA1; C11 TTKEPHX GN GZMB TTKEPHX FC This enzyme is necessary for target cell lysis in cell- mediated immune responses. It cleaves after Asp. Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -7, -9and 10 to give rise to active enzymes mediating apoptosis. TTKEPHX EC EC 3.4.21.79 TTKEPHX PD 1IAU; 1FQ3 TTKEPHX SQ MQPILLLLAFLLLPRADAGEIIGGHEAKPHSRPYMAYLMIWDQKSLKRCGGFLIRDDFVLTAAHCWGSSINVTLGAHNIKEQEPTQQFIPVKRPIPHPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGKHSHTLQEVKMTVQEDRKCESDLRHYYDSTIELCVGDPEIKKTSFKGDSGGPLVCNKVAQGIVSYGRNNGMPPRACTKVSSFVHWIKKTMKRY TTKEPHX TT Literature-reported TTKEPHX KE hsa04650:Natural killer cell mediated cytotoxicity; hsa04940:Type I diabetes mellitus; hsa05202:Transcriptional misregulation in cancer; hsa05320:Autoimmune thyroid disease; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease TTKEPHX RC R-HSA-2197563:NOTCH2 intracellular domain regulates transcription TTK4JTZ ID TTK4JTZ TTK4JTZ TN Guanine deaminase (GDA) TTK4JTZ UP Q9Y2T3 TTK4JTZ UC GUAD_HUMAN TTK4JTZ BC Metallo-dependent hydrolase superfamily. ATZ/TRZ family TTK4JTZ SN p51-nedasin; KIAA1258; Guanine aminohydrolase; Guanase; GAH TTK4JTZ GN GDA TTK4JTZ FC Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. TTK4JTZ EC EC 3.5.4.3 TTK4JTZ PD 4AQL; 3E0L; 2UZ9 TTK4JTZ SQ MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV TTK4JTZ TT Literature-reported TTK4JTZ KE hsa00230:Purine metabolism; hsa01100:Metabolic pathways TTTEOPU ID TTTEOPU TTTEOPU TN Helicase-moi messenger RNA (DICER1 mRNA) TTTEOPU UP Q9UPY3 TTTEOPU UC DICER_HUMAN TTTEOPU BC mRNA target TTTEOPU SN KIAA0928 (mRNA); Helicase with RNase motif (mRNA); Helicase MOI (mRNA); HERNA (mRNA); Endoribonuclease Dicer (mRNA); DICER (mRNA) TTTEOPU GN DICER1 TTTEOPU FC Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes. Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. TTTEOPU EC EC 3.1.26.3 TTTEOPU PD 5ZAM; 5ZAL; 5ZAK; 4WYQ; 4NHA TTTEOPU SQ MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWNQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYTSQPCEIVVDCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFVTPKVIKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDIDPVMDDDDVFPPYVLRPDDGGPRVTINTAIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETVKYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRDSYPRPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFMLSLQMLELITRLHQYIFSHILRLEKPALEFKPTDADSAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPNLDFGWKKSIDSKSFISISNSSSAENDNYCKHSTIVPENAAHQGANRTSSLENHDQMSVNCRTLLSESPGKLHVEVSADLTAINGLSYNQNLANGSYDLANRDFCQGNQLNYYKQEIPVQPTTSYSIQNLYSYENQPQPSDECTLLSNKYLDGNANKSTSDGSPVMAVMPGTTDTIQVLKGRMDSEQSPSIGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNTDKWEKDEMTKDCMLANGKLDEDYEEEDEEEESLMWRAPKEEADYEDDFLEYDQEHIRFIDNMLMGSGAFVKKISLSPFSTTDSAYEWKMPKKSSLGSMPFSSDFEDFDYSSWDAMCYLDPSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTDREKALCPTRENFNSQQKNLSVSCAAASVASSRSSVLKDSEYGCLKIPPRCMFDHPDADKTLNHLISGFENFEKKINYRFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLETVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS TTTEOPU TT Literature-reported TTTEOPU FM mRNA target TTTEOPU KE hsa05206:MicroRNAs in cancer TT9ISBX ID TT9ISBX TT9ISBX TN HIF-prolyl hydroxylase 2 (HPH-2) TT9ISBX UP Q9GZT9 TT9ISBX UC EGLN1_HUMAN TT9ISBX BC Paired donor oxygen oxidoreductase TT9ISBX SN SM-20; Prolyl hydroxylase domain-containing protein 2; PHD2; Hypoxia-inducible factor prolyl hydroxylase 2; HPH-2; HIF-PH2; Egl nine homolog 1; C1orf12 TT9ISBX GN EGLN1 TT9ISBX FC Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif. TT9ISBX EC EC 1.14.11.29 TT9ISBX PD 6NMQ; 5V18; 5OX6; 5OX5; 5LBF TT9ISBX SQ MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQGSEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADPAAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF TT9ISBX TT Patented-recorded TT9ISBX FM Oxidoreductases acting on paired donors TT9ISBX KE hsa04066:HIF-1 signaling pathway; hsa05200:Pathways in cancer; hsa05211:Renal cell carcinoma TT9ISBX RC R-HSA-1234176:Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha TTVK7SB ID TTVK7SB TTVK7SB TN Histone acetyltransferase KAT2B (KAT2B) TTVK7SB UP Q92831 TTVK7SB UC KAT2B_HUMAN TTVK7SB BC Acyltransferase TTVK7SB SN Spermidine acetyltransferase KAT2B; PCAF; P300/CBP-associated factor; P/CAF; Lysine acetyltransferase 2B; Histone acetyltransferase PCAF; Histone acetylase PCAF TTVK7SB GN KAT2B TTVK7SB FC Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY, PLK4 and TBX5. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5. Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4. Also acetylates spermidine. Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. TTVK7SB EC EC 2.3.1.48 TTVK7SB PD 6J3O; 5MKX; 5LVR; 5LVQ; 5FE9 TTVK7SB SQ MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK TTVK7SB TT Literature-reported TTVK7SB FM Acyltransferase TTVK7SB RC R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-2032785:YAP1- and WWTR1 (TAZ)-stimulated gene expression; R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-3214847:HATs acetylate histones; R-HSA-350054:Notch-HLH transcription pathway; R-HSA-73762:RNA Polymerase I Transcription Initiation TTH4VJL ID TTH4VJL TTH4VJL TN Histone acetyltransferase KAT6B (KAT6B) TTH4VJL UP Q8WYB5 TTH4VJL UC KAT6B_HUMAN TTH4VJL BC Acyltransferase TTH4VJL SN KAT6B TTH4VJL GN KAT6B TTH4VJL FC Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac). Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator in the presence of CREBBP. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation ofSIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity. Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCKor NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter. Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:10733570, PubMed:11430825, PubMed:11701890, PubMed:12402037, PubMed:12586840, PubMed:12929931, PubMed:14645221, PubMed:15186775, PubMed:15890677, PubMed:16617102, PubMed:16762839, PubMed:18722353,PubMed:18995842, PubMed:23415232, PubMed:23911289, PubMed:23934153, PubMed:8945521). Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity. TTH4VJL EC EC 2.3.1.48 TTH4VJL PD 5U2J TTH4VJL SQ MVKLANPLYTEWILEAIQKIKKQKQRPSEERICHAVSTSHGLDKKTVSEQLELSVQDGSVLKVTNKGLASYKDPDNPGRFSSVKPGTFPKSAKGSRGSCNDLRNVDWNKLLRRAIEGLEEPNGSSLKNIEKYLRSQSDLTSTTNNPAFQQRLRLGAKRAVNNGRLLKDGPQYRVNYGSLDGKGAPQYPSAFPSSLPPVSLLPHEKDQPRADPIPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTTNVKALRWQCIECKTCSACRVQGRNADNMLFCDSCDRGFHMECCDPPLSRMPKGMWICQVCRPKKKGRKLLHEKAAQIKRRYAKPIGRPKNKLKQRLLSVTSDEGSMNAFTGRGSPGRGQKTKVCTTPSSGHAASGKDSSSRLAVTDPTRPGATTKITTTSTYISASTLKVNKKTKGLIDGLTKFFTPSPDGRRSRGEIIDFSKHYRPRKKVSQKQSCTSHVLATGTTQKLKPPPSSLPPPTPISGQSPSSQKSSTATSSPSPQSSSSQCSVPSLSSLTTNSQLKALFDGLSHIYTTQGQSRKKGHPSYAPPKRMRRKTELSSTAKSKAHFFGKRDIRSRFISHSSSSSWGMARGSIFKAIAHFKRTTFLKKHRMLGRLKYKVTPQMGTPSPGKGSLTDGRIKPDQDDDTEIKINIKQESADVNVIGNKDVVTEEDLDVFKQAQELSWEKIECESGVEDCGRYPSVIEFGKYEIQTWYSSPYPQEYARLPKLYLCEFCLKYMKSKNILLRHSKKCGWFHPPANEIYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLVGYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRLSYLAYWKSVILEYLYHHHERHISIKAISRATGMCPHDIATTLQHLHMIDKRDGRFVIIRREKLILSHMEKLKTCSRANELDPDSLRWTPILISNAAVSEEEREAEKEAERLMEQASCWEKEEQEILSTRANSRQSPAKVQSKNKYLHSPESRPVTGERGQLLELSKESSEEEEEEEDEEEEEEEEEEEEDEEEEEEEEEEEEEENIQSSPPRLTKPQSVAIKRKRPFVLKKKRGRKRRRINSSVTTETISETTEVLNEPFDNSDEERPMPQLEPTCEIEVEEDGRKPVLRKAFQHQPGKKRQTEEEEGKDNHCFKNADPCRNNMNDDSSNLKEGSKDNPEPLKCKQVWPKGTKRGLSKWRQNKERKTGFKLNLYTPPETPMEPDEQVTVEEQKETSEGKTSPSPIRIEEEVKETGEALLPQEENRREETCAPVSPNTSPGEKPEDDLIKPEEEEEEEEEEEEEEEEEEGEEEEGGGNVEKDPDGAKSQEKEEPEISTEKEDSARLDDHEEEEEEDEEPSHNEDHDADDEDDSHMESAEVEKEELPRESFKEVLENQETFLDLNVQPGHSNPEVLMDCGVDLTASCNSEPKELAGDPEAVPESDEEPPPGEQAQKQDQKNSKEVDTEFKEGNPATMEIDSETVQAVQSLTQESSEQDDTFQDCAETQEACRSLQNYTRADQSPQIATTLDDCQQSDHSSPVSSVHSHPGQSVRSVNSPSVPALENSYAQISPDQSAISVPSLQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNGSSQNSCSYSNLTSSSLTQSSCAVTQQMSNISGSCSMLQQTSISSPPTCSVKSPQGCVVERPPSSSQQLAQCSMAANFTPPMQLAEIPETSNANIGLYERMGQSDFGAGHYPQPSATFSLAKLQQLTNTLIDHSLPYSHSAAVTSYANSASLSTPLSNTGLVQLSQSPHSVPGGPQAQATMTPPPNLTPPPMNLPPPLLQRNMAASNIGISHSQRLQTQIASKGHISMRTKSASLSPAAATHQSQIYGRSQTVAMQGPARTLTMQRGMNMSVNLMPAPAYNVNSVNMNMNTLNAMNGYSMSQPMMNSGYHSNHGYMNQTPQYPMQMQMGMMGTQPYAQQPMQTPPHGNMMYTAPGHHGYMNTGMSKQSLNGSYMRR TTH4VJL TT Literature-reported TTH4VJL KE hsa04024:cAMP signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04310:Wnt signaling pathway; hsa04330:Notch signaling pathway; hsa04350:TGF-beta signaling pathway; hsa04520:Adherens junction; hsa04630:Jak-STAT signaling pathway; hsa04720:Long-term potentiation; hsa04916:Melanogenesis; hsa04919:Thyroid hormone signaling pathway; hsa04922:Glucagon signaling pathway; hsa05016:Huntington's disease; hsa05152:Tuberculosis; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma; hsa05215:Prostate cancer TTH4VJL RC R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-1368082:RORA activates gene expression; R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-156711:Polo-like kinase mediated events; R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-1989781:PPARA activates gene expression; R-HSA-201722:Formation of the beta-catenin:TCF transactivating complex; R-HSA-2032785:YAP1- and WWTR1 (TAZ)-stimulated gene expression; R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2197563:NOTCH2 intracellular domain regulates transcription; R-HSA-2559586:DNA Damage/Telomere Stress Induced Senescence; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-3134973:LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production; R-HSA-3214847:HATs acetylate histones; R-HSA-3371568:Attenuation phase; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-400253:Circadian Clock; R-HSA-5685938:HDR through Single Strand Annealing (SSA); R-HSA-5685942:HDR through Homologous Recombination (HRR); R-HSA-5693565:Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks; R-HSA-5693571:Nonhomologous End-Joining (NHEJ); R-HSA-5693607:Processing of DNA double-strand break ends; R-HSA-5693616:Presynaptic phase of homologous DNA pairing and strand exchange; R-HSA-6781823:Formation of TC-NER Pre-Incision Complex; R-HSA-6782135:Dual incision in TC-NER; R-HSA-6782210:Gap-filling DNA repair synthesis and ligation in TC-NER; R-HSA-69473:G2/M DNA damage checkpoint; R-HSA-73762:RNA Polymerase I Transcription Initiation; R-HSA-918233:TRAF3-dependent IRF activation pathway; R-HSA-933541:TRAF6 mediated IRF7 activation; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTJGV7F ID TTJGV7F TTJGV7F TN Histone-lysine N-methyltransferase KMT5B (KMT5B) TTJGV7F UP Q4FZB7 TTJGV7F UC KMT5B_HUMAN TTJGV7F SN Lysine N-methyltransferase 5B; Lysine-specific methyltransferase 5B; Suppressor of variegation 4-20 homolog 1; Su(var)4-20 homolog 1; Suv4-20h1; [histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B; [histone H4]-lysine20 N-methyltransferase KMT5B TTJGV7F GN KMT5B TTJGV7F FC Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity. In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes, such as EID3. Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4. May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity). TTJGV7F EC EC 2.1.1.361 TTJGV7F SQ MKWLGESKNMVVNGRRNGGKLSNDHQQNQSKLQHTGKDTLKAGKNAVERRSNRCNGNSGFEGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHFSKSDSFSHNNPVRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKEHVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEENMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGAFKSRVGLPAPAPVINSKYGLRETDKRLNRLKKLGDSSKNSDSQSVSSNTDADTTQEKNNATSNRKSSVGVKKNSKSRTLTRQSMSRIPASSNSTSSKLTHINNSRVPKKLKKPAKPLLSKIKLRNHCKRLEQKNASRKLEMGNLVLKEPKVVLYKNLPIKKDKEPEGPAQAAVASGCLTRHAAREHRQNPVRGAHSQGESSPCTYITRRSVRTRTNLKEASDIKLEPNTLNGYKSSVTEPCPDSGEQLQPAPVLQEEELAHETAQKGEAKCHKSDTGMSKKKSRQGKLVKQFAKIEESTPVHDSPGKDDAVPDLMGPHSDQGEHSGTVGVPVSYTDCAPSPVGCSVVTSDSFKTKDSFRTAKSKKKRRITRYDAQLILENNSGIPKLTLRRRHDSSSKTNDQENDGMNSSKISIKLSKDHDNDNNLYVAKLNNGFNSGSGSSSTKLKIQLKRDEENRGSYTEGLHENGVCCSDPLSLLESRMEVDDYSQYEEESTDDSSSSEGDEEEDDYDDDFEDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA TTJGV7F TT Preclinical TT7H3YM ID TT7H3YM TT7H3YM TN Histone-lysine N-methyltransferase KMT5C (KMT5C) TT7H3YM UP Q86Y97 TT7H3YM UC KMT5C_HUMAN TT7H3YM SN Lysine N-methyltransferase 5C; Lysine-specific methyltransferase 5C; Suppressor of variegation 4-20 homolog 2; Su(var)4-20 homolog 2; Suv4-20h2; [histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B; [histone H4]-lysine20 N-methyltransferase KMT5B TT7H3YM GN KMT5C TT7H3YM FC Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity. In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5C is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4. May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity). TT7H3YM EC EC 2.1.1.361 TT7H3YM SQ MGPDRVTARELCENDDLATSLVLDPYLGFRTHKMNVSPVPPLRRQQHLRSALETFLRQRDLEAAYRALTLGGWTARYFQSRGPRQEAALKTHVYRYLRAFLPESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREADEGLLRAGENDFSIMYSTRKRSAQLWLGPAAFINHDCKPNCKFVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGEGAFRTRPREPALPPRPLDKYQLRETKRRLQQGLDSGSRQGLLGPRACVHPSPLRRDPFCAACQPLRLPACSARPDTSPLWLQWLPQPQPRVRPRKRRRPRPRRAPVLSTHHAARVSLHRWGGCGPHCRLRGEALVALGQPPHARWAPQQDWHWARRYGLPYVVRVDLRRLAPAPPATPAPAGTPGPILIPKQALAFAPFSPPKRLRLVVSHGSIDLDVGGEEL TT7H3YM TT Preclinical TTKLJYX ID TTKLJYX TTKLJYX TN Histone-lysine N-methyltransferase SMYD3 (SMYD3) TTKLJYX UP Q9H7B4 TTKLJYX UC SMYD3_HUMAN TTKLJYX SN SET and MYND domain-containing protein 3; Zinc finger MYND domain-containing protein 1 TTKLJYX GN SMYD3 TTKLJYX FC Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation . Also methylates 'Lys-5' of histone H4. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences. TTKLJYX EC EC 2.1.1.354 TTKLJYX SQ MEPLKVEKFATAKRGNGLRAVTPLRPGELLFRSDPLAYTVCKGSRGVVCDRCLLGKEKLMRCSQCRVAKYCSAKCQKKAWPDHKRECKCLKSCKPRYPPDSVRLLGRVVFKLMDGAPSESEKLYSFYDLESNINKLTEDKKEGLRQLVMTFQHFMREEIQDASQLPPAFDLFEAFAKVICNSFTICNAEMQEVGVGLYPSISLLNHSCDPNCSIVFNGPHLLLRAVRDIEVGEELTICYLDMLMTSEERRKQLRDQYCFECDCFRCQTQDKDADMLTGDEQVWKEVQESLKKIEELKAHWKWEQVLAMCQAIISSNSERLPDINIYQLKVLDCAMDACINLGLLEEALFYGTRTMEPYRIFFPGSHPVRGVQVMKVGKLQLHQGMFPQAMKNLRLAFDIMRVTHGREHSLIEDLILLLEECDANIRAS TTKLJYX TT Preclinical TTBDH9A ID TTBDH9A TTBDH9A TN Human immunodeficiency virus RT messenger RNA (HIV RT mRNA) TTBDH9A UP P03366 (600-1159) TTBDH9A UC POL_HV1B1 TTBDH9A BC mRNA target TTBDH9A SN gag-pol (588-1147) (mRNA); Pr160Gag-Pol (588-1147) (mRNA); Gag-Pol polyprotein (588-1147) (mRNA) TTBDH9A GN HIV RT mRNA TTBDH9A FC Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. Gag-Pol polyprotein: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). TTBDH9A EC EC 2.7.7.49 TTBDH9A PD 6OE3; 6HAK; 6ELI; 6DUH; 6DUG TTBDH9A SQ PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKIL TTBDH9A TT Literature-reported TTBDH9A FM mRNA target TTS0EZJ ID TTS0EZJ TTS0EZJ TN Hydroxymethylglutaryl-CoA synthase 2 (HMGCS2) TTS0EZJ UP P54868 TTS0EZJ UC HMCS2_HUMAN TTS0EZJ BC Acyltransferase TTS0EZJ SN HMGCS2; HMG-CoAsynthase; 3-hydroxy-3-methylglutaryl coenzyme A synthase 2 TTS0EZJ GN HMGCS2 TTS0EZJ FC This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase. TTS0EZJ EC EC 2.3.3.10 TTS0EZJ PD 2WYA TTS0EZJ SQ MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALEVYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLPWDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYDFYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIFHTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKASQDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPGDTNSLFPGTWYLERVDEQHRRKYARRPV TTS0EZJ TT Literature-reported TTS0EZJ KE hsa00072:Synthesis and degradation of ketone bodies; hsa00280:Valine, leucine and isoleucine degradation; hsa00650:Butanoate metabolism; hsa00900:Terpenoid backbone biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa03320:PPAR signaling pathway TTS0EZJ RC R-HSA-1989781:PPARA activates gene expression TTQFBMY ID TTQFBMY TTQFBMY TN IGF1R messenger RNA (IGF1R mRNA) TTQFBMY UP P08069 TTQFBMY UC IGF1R_HUMAN TTQFBMY BC mRNA target TTQFBMY SN Type 1 insulin-like growth factor receptor (mRNA); Insulin-like growth factor 1 receptor (mRNA); IGF-IR (mRNA); IGF-I receptor (mRNA); IGF-1R (mRNA); IGF-1 receptor (mRNA); CD221 antigen (mRNA); CD221 (mRNA) TTQFBMY GN IGF1R TTQFBMY FC Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R. Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). TTQFBMY EC EC 2.7.10.1 TTQFBMY PD 5U8R; 5U8Q; 5HZN; 5FXS; 5FXR TTQFBMY SQ MKSGSGGGSPTSLWGLLFLSAALSLWPTSGEICGPGIDIRNDYQQLKRLENCTVIEGYLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTVDWSLILDAVSNNYIVGNKPPKECGDLCPGTMEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSTCGKRACTENNECCHPECLGSCSAPDNDTACVACRHYYYAGVCVPACPPNTYRFEGWRCVDRDFCANILSAESSDSEGFVIHDGECMQECPSGFIRNGSQSMYCIPCEGPCPKVCEEEKKTKTIDSVTSAQMLQGCTIFKGNLLINIRRGNNIASELENFMGLIEVVTGYVKIRHSHALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWDHRNLTIKAGKMYFAFNPKLCVSEIYRMEEVTGTKGRQSKGDINTRNNGERASCESDVLHFTSTTTSKNRIIITWHRYRPPDYRDLISFTVYYKEAPFKNVTEYDGQDACGSNSWNMVDVDLPPNKDVEPGILLHGLKPWTQYAVYVKAVTLTMVENDHIRGAKSEILYIRTNASVPSIPLDVLSASNSSSQLIVKWNPPSLPNGNLSYYIVRWQRQPQDGYLYRHNYCSKDKIPIRKYADGTIDIEEVTENPKTEVCGGEKGPCCACPKTEAEKQAEKEEAEYRKVFENFLHNSIFVPRPERKRRDVMQVANTTMSSRSRNTTAADTYNITDPEELETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTGYENFIHLIIALPVAVLLIVGGLVIMLYVFHRKRNNSRLGNGVLYASVNPEYFSAADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKEEMEPGFREVSFYYSEENKLPEPEELDLEPENMESVPLDPSASSSSLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNERALPLPQSSTC TTQFBMY TT Literature-reported TTQFBMY FM mRNA target TTQFBMY KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04114:Oocyte meiosis; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04730:Long-term depression; hsa04913:Ovarian steroidogenesis; hsa04914:Progesterone-mediated oocyte maturation; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05205:Proteoglycans in cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma TTQFBMY RC R-HSA-2428928:IRS-related events triggered by IGF1R; R-HSA-2428933:SHC-related events triggered by IGF1R TTWLVKG ID TTWLVKG TTWLVKG TN Inhibitor of nuclear factor kappa-B kinase alpha (IKKA) TTWLVKG UP O15111 TTWLVKG UC IKKA_HUMAN TTWLVKG BC Kinase TTWLVKG SN Transcription factor 16; TCF16; TCF-16; Nuclear factor NFkappaB inhibitor kinase alpha; Nuclear factor NF-kappa-B inhibitor kinase alpha; NFKBIKA; Inhibitory kappa B kinasea; Inhibitor of nuclear factor kappa-B kinase subunit alpha; IkappaB kinase A; IkBKA; IKK1; IKK-alpha; IKK-A; I-kappa-B kinase alpha; I-kappa-B kinase 1; I kappa-B kinase alpha; Conserved helix-loop-helix ubiquitous kinase TTWLVKG GN CHUK TTWLVKG FC Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Participates also in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities. Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP. Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor. Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. TTWLVKG EC EC 2.7.11.10 TTWLVKG PD 5TQY; 5TQX; 5TQW; 5EBZ; 3BRT TTWLVKG SQ MERPPGLRPGAGGPWEMRERLGTGGFGNVCLYQHRELDLKIAIKSCRLELSTKNRERWCHEIQIMKKLNHANVVKACDVPEELNILIHDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIIHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMSGEVRFSSHLPQPNSLCSLVVEPMENWLQLMLNWDPQQRGGPVDLTLKQPRCFVLMDHILNLKIVHILNMTSAKIISFLLPPDESLHSLQSRIERETGINTGSQELLSETGISLDPRKPASQCVLDGVRGCDSYMVYLFDKSKTVYEGPFASRSLSDCVNYIVQDSKIQLPIIQLRKVWAEAVHYVSGLKEDYSRLFQGQRAAMLSLLRYNANLTKMKNTLISASQQLKAKLEFFHKSIQLDLERYSEQMTYGISSEKMLKAWKEMEEKAIHYAEVGVIGYLEDQIMSLHAEIMELQKSPYGRRQGDLMESLEQRAIDLYKQLKHRPSDHSYSDSTEMVKIIVHTVQSQDRVLKELFGHLSKLLGCKQKIIDLLPKVEVALSNIKEADNTVMFMQGKRQKEIWHLLKIACTQSSARSLVGSSLEGAVTPQTSAWLPPTSAEHDHSLSCVVTPQDGETSAQMIEENLNCLGHLSTIIHEANEEQGNSMMNLDWSWLTE TTWLVKG TT Literature-reported TTWLVKG FM Kinase TTWLVKG RC R-HSA-1169091:Activation of NF-kappaB in B cells; R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-1810476:RIP-mediated NFkB activation via ZBP1; R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-446652:Interleukin-1 signaling; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5602636:IKBKB deficiency causes SCID; R-HSA-5603027:IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR); R-HSA-5603029:IkBA variant leads to EDA-ID; R-HSA-5607761:Dectin-1 mediated noncanonical NF-kB signaling; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer; R-HSA-5676590:NIK-->noncanonical NF-kB signaling; R-HSA-5684264:MAP3K8 (TPL2)-dependent MAPK1/3 activation; R-HSA-933542:TRAF6 mediated NF-kB activation; R-HSA-933543:NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10; R-HSA-937039:IRAK1 recruits IKK complex; R-HSA-937041:IKK complex recruitment mediated by RIP1; R-HSA-975144:IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation TTXWL6D ID TTXWL6D TTXWL6D TN Inositol-1(or4)-monophosphatase (IMPA2) TTXWL6D UP O14732 TTXWL6D UC IMPA2_HUMAN TTXWL6D BC Phosphoric monoester hydrolase TTXWL6D SN Myo-inositol-1-phosphate phosphohydrolase; Myo-inositol monophosphatase: IMP.18p; Lithium-sensitive myo-inositol monophosphatase A1; Inositol monophosphatase; IMPase; IMPA2; IMP TTXWL6D GN IMPA2 TTXWL6D FC Can use myo-inositol monophosphates, scylloinositol 1,4- diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'- AMP as substrates. Has been implicated as the pharmacological target for lithium Li(+) action in brain. TTXWL6D EC EC 3.1.3.25 TTXWL6D PD 2FVZ; 2DDK; 2CZK; 2CZI; 2CZH TTXWL6D SQ MKPSGEDQAALAAGPWEECFQAAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHLVEDLIISELRERFPSHRFIAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTINYGRDDEK TTXWL6D TT Literature-reported TTXWL6D KE hsa00562:Inositol phosphate metabolism; hsa01100:Metabolic pathways; hsa04070:Phosphatidylinositol signaling system TT7ALZG ID TT7ALZG TT7ALZG TN Integrin-linked protein kinase 1 (ILK) TT7ALZG UP Q13418 TT7ALZG UC ILK_HUMAN TT7ALZG BC Kinase TT7ALZG SN P59ILK; Integrin-linked protein kinase; Integrin-linked kinase; ILK2; ILK1; ILK-2; ILK-1; Beta-integrin-linked kinase; 59 kDa serine/threonine-protein kinase; 59 kDa serine/threonine protein kinase TT7ALZG GN ILK TT7ALZG FC May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B. Receptor-proximal protein kinase regulating integrin-mediated signal transduction. TT7ALZG EC EC 2.7.11.1 TT7ALZG PD 6MIB; 4HI9; 4HI8; 3REP; 3KMW TT7ALZG SQ MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLTKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQSPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK TT7ALZG TT Patented-recorded TT7ALZG FM Kinase TT7ALZG RC R-HSA-446343:Localization of the PINCH-ILK-PARVIN complex to focal adhesions TTLPF4X ID TTLPF4X TTLPF4X TN Kallikrein-6 (KLK6) TTLPF4X UP Q92876 TTLPF4X UC KLK6_HUMAN TTLPF4X BC Peptidase TTLPF4X SN Zyme; Serine protease 9; Serine protease 18; SP59; Protease M; PRSS9; PRSS18; Neurosin; MSP; K6 TTLPF4X GN KLK6 TTLPF4X FC Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralizing KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis. Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. TTLPF4X EC EC 3.4.21.- TTLPF4X PD 6QHC; 6QHB; 6QHA; 6QH9; 6QFH TTLPF4X SQ MKKLMVVLSLIAAAWAEEQNKLVHGGPCDKTSHPYQAALYTSGHLLCGGVLIHPLWVLTAAHCKKPNLQVFLGKHNLRQRESSQEQSSVVRAVIHPDYDAASHDQDIMLLRLARPAKLSELIQPLPLERDCSANTTSCHILGWGKTADGDFPDTIQCAYIHLVSREECEHAYPGQITQNMLCAGDEKYGKDSCQGDSGGPLVCGDHLRGLVSWGNIPCGSKEKPGVYTNVCRYTNWIQKTIQAK TTLPF4X TT Literature-reported TTWQM3J ID TTWQM3J TTWQM3J TN Kynureninase (KYNU) TTWQM3J UP Q16719 TTWQM3J UC KYNU_HUMAN TTWQM3J BC Carbon-carbon bonds hydrolase TTWQM3J SN L-kynurenine hydrolase; KYNU TTWQM3J GN KYNU TTWQM3J FC Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity. TTWQM3J EC EC 3.7.1.3 TTWQM3J PD 3E9K; 2HZP TTWQM3J SQ MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLSLVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLMKDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHGLNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAGQAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKPALVGWFGHELSTRFKMDNKLQLIPGVCGFRISNPPILLVCSLHASLEIFKQATMKALRKKSVLLTGYLEYLIKHNYGKDKAATKKPVVNIITPSHVEERGCQLTITFSVPNKDVFQELEKRGVVCDKRNPNGIRVAPVPLYNSFHDVYKFTNLLTSILDSAETKN TTWQM3J TT Preclinical TTWQM3J KE hsa00380:Tryptophan metabolism; hsa01100:Metabolic pathways TTWQM3J RC R-HSA-71240:Tryptophan catabolism TTPH2JB ID TTPH2JB TTPH2JB TN Large neutral amino acids transporter 1 (SLC7A5) TTPH2JB UP Q01650 TTPH2JB UC LAT1_HUMAN TTPH2JB BC Amino acid-polyamine-organocation TTPH2JB SN y+ system cationic amino acid transporter; Solute carrier family 7 member 5; MPE16; Large neutral amino acids transporter small subunit 1; LAT1; L-type amino acid transporter LAT1; L-type amino acid transporter 1; Integral membrane protein E16; HLAT1; CD98LC; CD98 light chain; 4F2LC; 4F2 light chain; 4F2 LC TTPH2JB GN SLC7A5 TTPH2JB FC Involved in cellular amino acid uptake. Acts as an amino acid exchanger. Involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Plays a role in neuronal cell proliferation (neurogenesis) in brain. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. May play an important role in high-grade gliomas. Mediates blood-to-retina L-leucine transport across the inner blood-retinal barrier which in turn may play a key role in maintaining large neutral amino acids as well as neurotransmitters in the neural retina. Acts as the major transporter of tyrosine in fibroblasts. When associated with LAPTM4B, recruits SLC3A2 and SLC7A5 to lysosomes to promote leucine uptake into these organelles and is required for mTORC1 activation. Sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. TTPH2JB PD 6IRT; 6IRS TTPH2JB SQ MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPLFPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET TTPH2JB TT Literature-reported TTPH2JB FM Amino acid-polyamine-organocation TTPH2JB KE hsa05230:Central carbon metabolism in cancer TTPH2JB RC R-HSA-210991:Basigin interactions; R-HSA-352230:Amino acid transport across the plasma membrane TTML7FG ID TTML7FG TTML7FG TN Large tumor suppressor homolog 2 (LATS2) TTML7FG UP Q9NRM7 TTML7FG UC LATS2_HUMAN TTML7FG BC Kinase TTML7FG SN Warts-like kinase; Serine/threonine-protein kinase kpm; Serine/threonine-protein kinase LATS2; Kinase phosphorylated during mitosis protein; KPM TTML7FG GN LATS2 TTML7FG FC The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in centrosome duplication, maintenance of mitotic fidelity and genomic stability. Negatively regulates G1/S transition by down-regulating cyclin E/CDK2 kinase activity. Negative regulator of the androgen receptor. Phosphorylates SNAI1 in the nucleus leading to its nuclear retention and stabilization, which enhances its epithelial-mesenchymal transition and tumor cell invasion/migration activities. This tumor-promoting activity is independent of its effects upon YAP1 or WWTR1/TAZ. Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. TTML7FG EC EC 2.7.11.1 TTML7FG PD 4ZRI TTML7FG SQ MRPKTFPATTYSGNSRQRLQEIREGLKQPSKSSVQGLPAGPNSDTSLDAKVLGSKDATRQQQQMRATPKFGPYQKALREIRYSLLPFANESGTSAAAEVNRQMLQELVNAGCDQEMAGRALKQTGSRSIEAALEYISKMGYLDPRNEQIVRVIKQTSPGKGLMPTPVTRRPSFEGTGDSFASYHQLSGTPYEGPSFGADGPTALEEMPRPYVDYLFPGVGPHGPGHQHQHPPKGYGASVEAAGAHFPLQGAHYGRPHLLVPGEPLGYGVQRSPSFQSKTPPETGGYASLPTKGQGGPPGAGLAFPPPAAGLYVPHPHHKQAGPAAHQLHVLGSRSQVFASDSPPQSLLTPSRNSLNVDLYELGSTSVQQWPAATLARRDSLQKPGLEAPPRAHVAFRPDCPVPSRTNSFNSHQPRPGPPGKAEPSLPAPNTVTAVTAAHILHPVKSVRVLRPEPQTAVGPSHPAWVPAPAPAPAPAPAPAAEGLDAKEEHALALGGAGAFPLDVEYGGPDRRCPPPPYPKHLLLRSKSEQYDLDSLCAGMEQSLRAGPNEPEGGDKSRKSAKGDKGGKDKKQIQTSPVPVRKNSRDEEKRESRIKSYSPYAFKFFMEQHVENVIKTYQQKVNRRLQLEQEMAKAGLCEAEQEQMRKILYQKESNYNRLKRAKMDKSMFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDSLYFVMDYIPGGDMMSLLIRMEVFPEHLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWTHNSKYYQKGSHVRQDSMEPSDLWDDVSNCRCGDRLKTLEQRARKQHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKVINWENTLHIPAQVKLSPEARDLITKLCCSADHRLGRNGADDLKAHPFFSAIDFSSDIRKQPAPYVPTISHPMDTSNFDPVDEESPWNDASEGSTKAWDTLTSPNNKHPEHAFYEFTFRRFFDDNGYPFRCPKPSGAEASQAESSDLESSDLVDQTEGCQPVYV TTML7FG TT Literature-reported TTML7FG FM Kinase TTSXOWE ID TTSXOWE TTSXOWE TN LDL receptor related protein-6 (LRP-6) TTSXOWE UP O75581 TTSXOWE UC LRP6_HUMAN TTSXOWE BC Low density lipoprotein receptor TTSXOWE SN Low-density lipoprotein receptor-related protein 6 TTSXOWE GN LRP6 TTSXOWE FC Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation. Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. TTSXOWE PD 6H16; 6H15; 5GJE; 5FWW; 5AIR TTSXOWE SQ MGAVLRSLLACSFCVLLRAAPLLLYANRRDLRLVDATNGKENATIVVGGLEDAAAVDFVFSHGLIYWSDVSEEAIKRTEFNKTESVQNVVVSGLLSPDGLACDWLGEKLYWTDSETNRIEVSNLDGSLRKVLFWQELDQPRAIALDPSSGFMYWTDWGEVPKIERAGMDGSSRFIIINSEIYWPNGLTLDYEEQKLYWADAKLNFIHKSNLDGTNRQAVVKGSLPHPFALTLFEDILYWTDWSTHSILACNKYTGEGLREIHSDIFSPMDIHAFSQQRQPNATNPCGIDNGGCSHLCLMSPVKPFYQCACPTGVKLLENGKTCKDGATELLLLARRTDLRRISLDTPDFTDIVLQLEDIRHAIAIDYDPVEGYIYWTDDEVRAIRRSFIDGSGSQFVVTAQIAHPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTMRKILISEDLEEPRAIVLDPMVGYMYWTDWGEIPKIERAALDGSDRVVLVNTSLGWPNGLALDYDEGKIYWGDAKTDKIEVMNTDGTGRRVLVEDKIPHIFGFTLLGDYVYWTDWQRRSIERVHKRSAEREVIIDQLPDLMGLKATNVHRVIGSNPCAEENGGCSHLCLYRPQGLRCACPIGFELISDMKTCIVPEAFLLFSRRADIRRISLETNNNNVAIPLTGVKEASALDFDVTDNRIYWTDISLKTISRAFMNGSALEHVVEFGLDYPEGMAVDWLGKNLYWADTGTNRIEVSKLDGQHRQVLVWKDLDSPRALALDPAEGFMYWTEWGGKPKIDRAAMDGSERTTLVPNVGRANGLTIDYAKRRLYWTDLDTNLIESSNMLGLNREVIADDLPHPFGLTQYQDYIYWTDWSRRSIERANKTSGQNRTIIQGHLDYVMDILVFHSSRQSGWNECASSNGHCSHLCLAVPVGGFVCGCPAHYSLNADNRTCSAPTTFLLFSQKSAINRMVIDEQQSPDIILPIHSLRNVRAIDYDPLDKQLYWIDSRQNMIRKAQEDGSQGFTVVVSSVPSQNLEIQPYDLSIDIYSRYIYWTCEATNVINVTRLDGRSVGVVLKGEQDRPRAVVVNPEKGYMYFTNLQERSPKIERAALDGTEREVLFFSGLSKPIALALDSRLGKLFWADSDLRRIESSDLSGANRIVLEDSNILQPVGLTVFENWLYWIDKQQQMIEKIDMTGREGRTKVQARIAQLSDIHAVKELNLQEYRQHPCAQDNGGCSHICLVKGDGTTRCSCPMHLVLLQDELSCGEPPTCSPQQFTCFTGEIDCIPVAWRCDGFTECEDHSDELNCPVCSESQFQCASGQCIDGALRCNGDANCQDKSDEKNCEVLCLIDQFRCANGQCIGKHKKCDHNVDCSDKSDELDCYPTEEPAPQATNTVGSVIGVIVTIFVSGTVYFICQRMLCPRMKGDGETMTNDYVVHGPASVPLGYVPHPSSLSGSLPGMSRGKSMISSLSIMGGSSGPPYDRAHVTGASSSSSSSTKGTYFPAILNPPPSPATERSHYTMEFGYSSNSPSTHRSYSYRPYSYRHFAPPTTPCSTDVCDSDYAPSRRMTSVATAKGYTSDLNYDSEPVPPPPTPRSQYLSAEENYESCPPSPYTERSYSHHLYPPPPSPCTDSS TTSXOWE TT Clinical trial TTSXOWE FM Low density lipoprotein receptor TTSXOWE KE hsa04310:Wnt signaling pathway TTSXOWE RC R-HSA-201681:TCF dependent signaling in response to WNT; R-HSA-3772470:Negative regulation of TCF-dependent signaling by WNT ligand antagonists; R-HSA-4641262:Disassembly of the destruction complex and recruitment of AXIN to the membrane; R-HSA-4641263:Regulation of FZD by ubiquitination TTMQL3K ID TTMQL3K TTMQL3K TN Lipopolysaccharide-associated protein 1 (HSPA8) TTMQL3K UP P11142 TTMQL3K UC HSP7C_HUMAN TTMQL3K BC Heat shock protein TTMQL3K SN LPS-associated protein 1; LAP-1; Heat shock protein 73; Heat shock cognate 71 kDa protein; Heat shock 70 kDa protein 8; HSPA10; HSP73; HSC70 TTMQL3K GN HSPA8 TTMQL3K FC Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21. Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. TTMQL3K PD 6B1N; 6B1M; 6B1I; 5AQV; 5AQU TTMQL3K SQ MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD TTMQL3K TT Literature-reported TTMQL3K FM Heat shock protein TTMQL3K KE hsa03040:Spliceosome; hsa04010:MAPK signaling pathway; hsa04141:Protein processing in endoplasmic reticulum; hsa04144:Endocytosis; hsa04612:Antigen processing and presentation; hsa04915:Estrogen signaling pathway; hsa05134:Legionellosis; hsa05145:Toxoplasmosis; hsa05162:Measles; hsa05164:Influenza A; hsa05169:Epstein-Barr virus infection TTMQL3K RC R-HSA-3371453:Regulation of HSF1-mediated heat shock response; R-HSA-3371568:Attenuation phase; R-HSA-3371571:HSF1-dependent transactivation; R-HSA-432720:Lysosome Vesicle Biogenesis; R-HSA-432722:Golgi Associated Vesicle Biogenesis; R-HSA-447041:CHL1 interactions; R-HSA-72163:mRNA Splicing - Major Pathway TTE7RCU ID TTE7RCU TTE7RCU TN MAPK/ERK kinase kinase 3 (MAP3K3) TTE7RCU UP Q99759 TTE7RCU UC M3K3_HUMAN TTE7RCU BC Kinase TTE7RCU SN Mitogen-activated protein kinase kinase kinase 3; MEKK3; MEKK 3; MEK kinase 3; MAPKKK3 TTE7RCU GN MAP3K3 TTE7RCU FC Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators. Component of a protein kinase signal transduction cascade. TTE7RCU EC EC 2.7.11.25 TTE7RCU PD 4YL6; 4Y5O; 2PPH; 2O2V; 2JRH TTE7RCU SQ MDEQEALNSIMNDLVALQMNRRHRMPGYETMKNKDTGHSNRQSDVRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQDRNHNSSSPHSGVSRQVRIKASQSAGDINTIYQPPEPRSRHLSVSSQNPGRSSPPPGYVPERQQHIARQGSYTSINSEGEFIPETSEQCMLDPLSSAENSLSGSCQSLDRSADSPSFRKSRMSRAQSFPDNRQEYSDRETQLYDKGVKGGTYPRRYHVSVHHKDYSDGRRTFPRIRRHQGNLFTLVPSSRSLSTNGENMGLAVQYLDPRGRLRSADSENALSVQERNVPTKSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIFVEARQRPSAEELLTHHFAQLMY TTE7RCU TT Literature-reported TTE7RCU FM Kinase TTE7RCU RC R-HSA-446652:Interleukin-1 signaling TT6NI13 ID TT6NI13 TT6NI13 TN MEK kinase kinase 4 (MAP4K4) TT6NI13 UP O95819 TT6NI13 UC M4K4_HUMAN TT6NI13 BC Kinase TT6NI13 SN Nckinteracting kinase; Nck-interacting kinase; Mitogenactivated protein kinase kinase kinase kinase 4; Mitogen-activated protein kinase kinase kinase kinase 4; MEKKK 4; MAPK/ERK kinase kinase kinase 4; KIAA0687; HPK/GCKlike kinase HGK; HPK/GCK-like kinase HGK; HGK TT6NI13 GN MAP4K4 TT6NI13 FC Appears to act upstream of the JUN N-terminal pathway. Phosphorylates SMAD1 on Thr-322. Serine/threonine kinase that may play a role in the response to environmental stress and cytokines such as TNF-alpha. TT6NI13 EC EC 2.7.11.1 TT6NI13 PD 5W5Q; 5J95; 5DI1; 4ZP5; 4ZK5 TT6NI13 SQ MANDSPAKSLVDIDLSSLRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNTKGNTLKEDWIAYISREILRGLAHLHIHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDLWSCGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRIQLKDHIDRTRKKRGEKDETEYEYSGSEEEEEEVPEQEGEPSSIVNVPGESTLRRDFLRLQQENKERSEALRRQQLLQEQQLREQEEYKRQLLAERQKRIEQQKEQRRRLEEQQRREREARRQQEREQRRREQEEKRRLEELERRRKEEEERRRAEEEKRRVEREQEYIRRQLEEEQRHLEVLQQQLLQEQAMLLECRWREMEEHRQAERLQRQLQQEQAYLLSLQHDHRRPHPQHSQQPPPPQQERSKPSFHAPEPKAHYEPADRAREVEDRFRKTNHSSPEAQSKQTGRVLEPPVPSRSESFSNGNSESVHPALQRPAEPQVPVRTTSRSPVLSRRDSPLQGSGQQNSQAGQRNSTSIEPRLLWERVEKLVPRPGSGSSSGSSNSGSQPGSHPGSQSGSGERFRVRSSSKSEGSPSQRLENAVKKPEDKKEVFRPLKPADLTALAKELRAVEDVRPPHKVTDYSSSSEESGTTDEEDDDVEQEGADESTSGPEDTRAASSLNLSNGETESVKTMIVHDDVESEPAMTPSKEGTLIVRQTQSASSTLQKHKSSSSFTPFIDPRLLQISPSSGTTVTSVVGFSCDGMRPEAIRQDPTRKGSVVNVNPTNTRPQSDTPEIRKYKKRFNSEILCAALWGVNLLVGTESGLMLLDRSGQGKVYPLINRRRFQQMDVLEGLNVLVTISGKKDKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDLEGCVHYKVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFGELVHKPLLVDLTVEEGQRLKVIYGSCAGFHAVDVDSGSVYDIYLPTHIQCSIKPHAIIILPNTDGMELLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIRSNQTMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVYFMTLGRTSLLSW TT6NI13 TT Patented-recorded TT6NI13 FM Kinase TT6NI13 RC R-HSA-2559580:Oxidative Stress Induced Senescence TTIX0ZU ID TTIX0ZU TTIX0ZU TN MEKK2 messenger RNA (MAP3K2 mRNA) TTIX0ZU UP Q9Y2U5 TTIX0ZU UC M3K2_HUMAN TTIX0ZU BC mRNA target TTIX0ZU SN Mitogen-activated protein kinase kinase kinase 2 (mRNA); MEKK2 (mRNA); MEKK 2 (mRNA); MEK kinase 2 (mRNA); MAPKKK2 (mRNA) TTIX0ZU GN MAP3K2 TTIX0ZU FC Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7. Plays a role in caveolae kiss-and-run dynamics. Component of a protein kinase signal transduction cascade. TTIX0ZU EC EC 2.7.11.25 TTIX0ZU PD 5HQ8; 5EX0; 2NPT; 2CU1 TTIX0ZU SQ MDDQQALNSIMQDLAVLHKASRPALSLQETRKAKSSSPKKQNDVRVKFEHRGEKRILQFPRPVKLEDLRSKAKIAFGQSMDLHYTNNELVIPLTTQDDLDKAVELLDRSIHMKSLKILLVINGSTQATNLEPLPSLEDLDNTVFGAERKKRLSIIGPTSRDRSSPPPGYIPDELHQVARNGSFTSINSEGEFIPESMDQMLDPLSLSSPENSGSGSCPSLDSPLDGESYPKSRMPRAQSYPDNHQEFSDYDNPIFEKFGKGGTYPRRYHVSYHHQEYNDGRKTFPRARRTQGTSLRSPVSFSPTDHSLSTSSGSSIFTPEYDDSRIRRRGSDIDNPTLTVMDISPPSRSPRAPTNWRLGKLLGQGAFGRVYLCYDVDTGRELAVKQVQFDPDSPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQEKTLSIFMEYMPGGSIKDQLKAYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSTGNVKLGDFGASKRLQTICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVACTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPKLPPHVSDYTRDFLKRIFVEAKLRPSADELLRHMFVHYH TTIX0ZU TT Literature-reported TTIX0ZU FM mRNA target TTIX0ZU KE hsa04010:MAPK signaling pathway; hsa04540:Gap junction; hsa04912:GnRH signaling pathway TTJZNIG ID TTJZNIG TTJZNIG TN MEKK3 messenger RNA (MAP3K3 mRNA) TTJZNIG UP Q99759 TTJZNIG UC M3K3_HUMAN TTJZNIG BC mRNA target TTJZNIG SN Mitogen-activated protein kinase kinase kinase 3 (mRNA); MEKK3 (mRNA); MEKK 3 (mRNA); MEK kinase 3 (mRNA); MAPKKK3 (mRNA) TTJZNIG GN MAP3K3 TTJZNIG FC Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators. Component of a protein kinase signal transduction cascade. TTJZNIG EC EC 2.7.11.25 TTJZNIG PD 4YL6; 4Y5O; 2PPH; 2O2V; 2JRH TTJZNIG SQ MDEQEALNSIMNDLVALQMNRRHRMPGYETMKNKDTGHSNRQSDVRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQDRNHNSSSPHSGVSRQVRIKASQSAGDINTIYQPPEPRSRHLSVSSQNPGRSSPPPGYVPERQQHIARQGSYTSINSEGEFIPETSEQCMLDPLSSAENSLSGSCQSLDRSADSPSFRKSRMSRAQSFPDNRQEYSDRETQLYDKGVKGGTYPRRYHVSVHHKDYSDGRRTFPRIRRHQGNLFTLVPSSRSLSTNGENMGLAVQYLDPRGRLRSADSENALSVQERNVPTKSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIFVEARQRPSAEELLTHHFAQLMY TTJZNIG TT Literature-reported TTJZNIG FM mRNA target TTJZNIG KE hsa04010:MAPK signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04912:GnRH signaling pathway; hsa05166:HTLV-I infection TTJZNIG RC R-HSA-446652:Interleukin-1 signaling TT0I76D ID TT0I76D TT0I76D TN Metabotropic glutamate receptor 7 (mGluR7) TT0I76D UP Q14831 TT0I76D UC GRM7_HUMAN TT0I76D BC GPCR glutamate TT0I76D SN mGluR7; GPRC1G TT0I76D GN GRM7 TT0I76D FC Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. G-protein coupled receptor for glutamate. TT0I76D PD 5C5C; 3MQ4 TT0I76D SQ MVQLRKLLRVLTLMKFPCCVLEVLLCALAAAARGQEMYAPHSIRIEGDVTLGGLFPVHAKGPSGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTFVQALIQKDTSDVRCTNGEPPVFVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAGGLCIAQSVRIPQERKDRTIDFDRIIKQLLDTPNSRAVVIFANDEDIKQILAAAKRADQVGHFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTSRTLENNRRNVWFAEYWEENFNCKLTISGSKKEDTDRKCTGQERIGKDSNYEQEGKVQFVIDAVYAMAHALHHMNKDLCADYRGVCPEMEQAGGKKLLKYIRNVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNTSNPGYRLIGQWTDELQLNIEDMQWGKGVREIPASVCTLPCKPGQRKKTQKGTPCCWTCEPCDGYQYQFDEMTCQHCPYDQRPNENRTGCQDIPIIKLEWHSPWAVIPVFLAMLGIIATIFVMATFIRYNDTPIVRASGRELSYVLLTGIFLCYIITFLMIAKPDVAVCSFRRVFLGLGMCISYAALLTKTNRIYRIFEQGKKSVTAPRLISPTSQLAITSSLISVQLLGVFIWFGVDPPNIIIDYDEHKTMNPEQARGVLKCDITDLQIICSLGYSILLMVTCTVYAIKTRGVPENFNEAKPIGFTMYTTCIVWLAFIPIFFGTAQSAEKLYIQTTTLTISMNLSASVALGMLYMPKVYIIIFHPELNVQKRKRSFKAVVTAATMSSRLSHKPSDRPNGEAKTELCENVDPNSPAAKKKYVSYNNLVI TT0I76D TT Literature-reported TT0I76D FM GPCR glutamate TT0I76D KE hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse TT0I76D RC R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors) TT0IFKL ID TT0IFKL TT0IFKL TN Metabotropic glutamate receptor 8 (mGluR8) TT0IFKL UP O00222 TT0IFKL UC GRM8_HUMAN TT0IFKL BC GPCR glutamate TT0IFKL SN MGluR8a; MGLUR8; Glutamate receptor mGLU8; GRM8 TT0IFKL GN GRM8 TT0IFKL FC Receptor for glutamate. The activity of this receptor is mediated by a g-protein that inhibits adenylate cyclase activity. TT0IFKL PD 6E5V; 6BT5; 6BSZ TT0IFKL SQ MVCEGKRSASCPCFFLLTAKFYWILTMMQRTHSQEYAHSIRVDGDIILGGLFPVHAKGERGVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFVQALIEKDASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTAPELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISREIGGVCIAQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQSGHFLWIGSDSWGSKIAPVYQQEEIAEGAVTILPKRASIDGFDRYFRSRTLANNRRNVWFAEFWEENFGCKLGSHGKRNSHIKKCTGLERIARDSSYEQEGKVQFVIDAVYSMAYALHNMHKDLCPGYIGLCPRMSTIDGKELLGYIRAVNFNGSAGTPVTFNENGDAPGRYDIFQYQITNKSTEYKVIGHWTNQLHLKVEDMQWAHREHTHPASVCSLPCKPGERKKTVKGVPCCWHCERCEGYNYQVDELSCELCPLDQRPNMNRTGCQLIPIIKLEWHSPWAVVPVFVAILGIIATTFVIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYSITFLMIAAPDTIICSFRRVFLGLGMCFSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFVVDPPHIIIDYGEQRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIIWLAFIPIFFGTAQSAEKMYIQTTTLTVSMSLSASVSLGMLYMPKVYIIIFHPEQNVQKRKRSFKAVVTAATMQSKLIQKGNDRPNGEVKSELCESLETNTSSTKTTYISYSNHSI TT0IFKL TT Literature-reported TT0IFKL KE hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse TT0IFKL RC R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors) TTDO3RC ID TTDO3RC TTDO3RC TN MMP2 messenger RNA (MMP2 mRNA) TTDO3RC UP P08253 TTDO3RC UC MMP2_HUMAN TTDO3RC BC mRNA target TTDO3RC SN TBE-1 (mRNA); Matrix metalloproteinase 2 (mRNA); Gelatinase A (mRNA); CLG4A (mRNA); 72 kDa type IV collagenase (mRNA); 72 kDa gelatinase (mRNA) TTDO3RC GN MMP2 TTDO3RC FC As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14. Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. TTDO3RC EC EC 3.4.24.24 TTDO3RC PD 3AYU; 1RTG; 1QIB; 1KS0; 1J7M TTDO3RC SQ MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC TTDO3RC TT Literature-reported TTDO3RC FM mRNA target TT3TWY8 ID TT3TWY8 TT3TWY8 TN MMP9 messenger RNA (MMP9 mRNA) TT3TWY8 UP P14780 TT3TWY8 UC MMP9_HUMAN TT3TWY8 BC mRNA target TT3TWY8 SN Matrix metalloproteinase 9 (mRNA); Gelatinase B (mRNA); GELB (mRNA); CLG4B (mRNA); 92 kDa type IV collagenase (mRNA); 92 kDa gelatinase (mRNA) TT3TWY8 GN MMP9 TT3TWY8 FC Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. TT3TWY8 EC EC 3.4.24.35 TT3TWY8 PD 6ESM; 5UE4; 5UE3; 5TH9; 5TH6 TT3TWY8 SQ MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED TT3TWY8 TT Literature-reported TT3TWY8 FM mRNA target TTCPLVN ID TTCPLVN TTCPLVN TN MST-1 protein kinase (STK4) TTCPLVN UP Q13043 TTCPLVN UC STK4_HUMAN TTCPLVN BC Kinase TTCPLVN SN Serine/threonine-protein kinase Krs-2; Serine/threonine-protein kinase 4 18kDa subunit; Serine/threonine-protein kinase 4; STE20-like kinase MST1; Mammalian STE20-like protein kinase 1; MST1/N; MST1/C; MST1; MST-1; KRS2 TTCPLVN GN STK4 TTCPLVN FC Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. TTCPLVN EC EC 2.7.11.1 TTCPLVN PD 5TWH; 5TWG; 4OH8; 4NR2; 3COM TTCPLVN SQ METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVRSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGANTMIEHDDTLPSQLGTMVINAEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF TTCPLVN TT Literature-reported TTCPLVN FM Kinase TTCPLVN KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04068:FoxO signaling pathway; hsa05200:Pathways in cancer; hsa05223:Non-small cell lung cancer TTQWOU1 ID TTQWOU1 TTQWOU1 TN MTHFR messenger RNA (MTHFR mRNA) TTQWOU1 UP P42898 TTQWOU1 UC MTHR_HUMAN TTQWOU1 BC mRNA target TTQWOU1 SN Methylenetetrahydrofolate reductase (mRNA) TTQWOU1 GN MTHFR TTQWOU1 FC Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co-substrate for homocysteine remethylation to methionine. TTQWOU1 EC EC 1.5.1.20 TTQWOU1 PD 6FCX TTQWOU1 SQ MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYCGLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVKHIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFVKACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIELAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREEDVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKMWGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGILTINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHLVNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYEEESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP TTQWOU1 TT Literature-reported TTQWOU1 FM mRNA target TTQWOU1 KE hsa00670:One carbon pool by folate; hsa01100:Metabolic pathways; hsa01200:Carbon metabolism TTQWOU1 RC R-HSA-196757:Metabolism of folate and pterines TTFLHJV ID TTFLHJV TTFLHJV TN Multidrug resistance-associated protein 2 (ABCC2) TTFLHJV UP Q92887 TTFLHJV UC MRP2_HUMAN TTFLHJV BC ABC transporter TTFLHJV SN MRP2; Canalicular multispecific organic anion transporter 1; Canalicular multidrug resistance protein; CMRP; CMOAT1; CMOAT; ATP-binding cassette, sub-family C, member 2; ATP-binding cassette sub-family C member 2 TTFLHJV GN ABCC2 TTFLHJV FC May function as a cellular cisplatin transporter. Mediates hepatobiliary excretion of numerous organic anions. TTFLHJV EC EC 7.6.2.2 TTFLHJV SQ MLEKFCNSTFWNSSFLDSPEADLPLCFEQTVLVWIPLGYLWLLAPWQLLHVYKSRTKRSSTTKLYLAKQVFVGFLLILAAIELALVLTEDSGQATVPAVRYTNPSLYLGTWLLVLLIQYSRQWCVQKNSWFLSLFWILSILCGTFQFQTLIRTLLQGDNSNLAYSCLFFISYGFQILILIFSAFSENNESSNNPSSIASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKTLVSKFETHMKRELQKARRALQRRQEKSSQQNSGARLPGLNKNQSQSQDALVLEDVEKKKKKSGTKKDVPKSWLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNLKTFLRHTGPEEEATVHDGSEEEDDDYGLISSVEEIPEDAASITMRRENSFRRTLSRSSRSNGRHLKSLRNSLKTRNVNSLKEDEELVKGQKLIKKEFIETGKVKFSIYLEYLQAIGLFSIFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYPASQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKEAGIENVNSTKF TTFLHJV TT Literature-reported TTFLHJV FM ABC transporter TTFLHJV KE hsa02010:ABC transporters; hsa04976:Bile secretion TTFLHJV RC R-HSA-382556:ABC-family proteins mediated transport TTPH97Y ID TTPH97Y TTPH97Y TN Mycobacterium 3-oxoacyl-[acyl-carrier-protein] synthase 1 (MycB kasA) TTPH97Y UP P9WQD9 TTPH97Y UC FAB1_MYCTU TTPH97Y BC Acyltransferase TTPH97Y SN kasA; KAS 1; Beta-ketoacyl-ACP synthase 1 TTPH97Y GN MycB kasA TTPH97Y FC Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-acp. TTPH97Y EC EC 2.3.1.41 TTPH97Y PD 5LD8; 2WGG; 2WGF; 2WGE; 2WGD TTPH97Y SQ MSQPSTANGGFPSVVVTAVTATTSISPDIESTWKGLLAGESGIHALEDEFVTKWDLAVKIGGHLKDPVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAGSPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY TTPH97Y TT Literature-reported TTMN4HY ID TTMN4HY TTMN4HY TN N-acylethanolamine-hydrolyzing acidamidase (NAAA) TTMN4HY UP Q02083 TTMN4HY UC NAAA_HUMAN TTMN4HY BC Carbon-nitrogen hydrolase TTMN4HY SN Nacylsphingosine amidohydrolaselike; Nacylethanolaminehydrolyzing acid amidase subunit beta; NAAA; Acid ceramidaselike protein; ASAHlike protein TTMN4HY GN NAAA TTMN4HY FC Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N- palmitoylethanolamine > N-myristoylethanolamine > N- lauroylethanolamine = N-stearoylethanolamine > N- arachidonoylethanolamine > N-oleoylethanolamine. Also exhibits weak hydrolytic activity against the ceramides N- lauroylsphingosine and N-palmitoylsphingosine. TTMN4HY EC EC 3.5.1.- TTMN4HY PD 6DXX; 6DXW TTMN4HY SQ MRTADREARPGLPSLLLLLLAGAGLSAASPPAAPRFNVSLDSVPELRWLPVLRHYDLDLVRAAMAQVIGDRVPKWVHVLIGKVVLELERFLPQPFTGEIRGMCDFMNLSLADCLLVNLAYESSVFCTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDERDKGWWWENAIAALFRRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPREGVVITRNRDGPADIWPLDPLNGAWFRVETNYDHWKPAPKEDDRRTSAIKALNATGQANLSLEALFQILSVVPVYNNFTIYTTVMSAGSPDKYMTRIRNPSRK TTMN4HY TT Literature-reported TTLKF5M ID TTLKF5M TTLKF5M TN NAD-dependent deacetylase sirtuin-2 (SIRT2) TTLKF5M UP Q8IXJ6 TTLKF5M UC SIR2_HUMAN TTLKF5M BC Carbon-nitrogen hydrolase TTLKF5M SN SIR2like protein 2; SIR2L2; SIR2L; SIR2-like protein 2; Regulatory protein SIR2 homolog 2; NADdependent protein deacetylase sirtuin2; NAD-dependent protein deacetylase sirtuin-2 TTLKF5M GN SIRT2 TTLKF5M FC Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis. Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response. Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition. Upon bacterium Listeria monocytogenes infection, deacetylates 'Lys-18' of histone H3 in a receptor tyrosine kinase MET- and PI3K/Akt-dependent manner, thereby inhibiting transcriptional activity and promoting late stages of listeria infection. During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis. Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha-tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity. Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells. Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy. Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation. Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions. Plays a role as tumor suppressor. NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors. TTLKF5M EC EC 3.5.1.- TTLKF5M PD 5YQO; 5YQN; 5YQM; 5YQL; 5Y5N TTLKF5M SQ MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQSGAGVPNPSTSASPKKSPPPAKDEARTTEREKPQ TTLKF5M TT Patented-recorded TTLKF5M FM Carbon-nitrogen hydrolase TTVZLIJ ID TTVZLIJ TTVZLIJ TN NAD-dependent deacetylase sirtuin-3 (SIRT3) TTVZLIJ UP Q9NTG7 TTVZLIJ UC SIR3_HUMAN TTVZLIJ BC Sirtuin family. Class I subfamily TTVZLIJ SN hSIRT3; SIR2L3; SIR2-like protein 3; Regulatory protein SIR2 homolog 3 TTVZLIJ GN SIRT3 TTVZLIJ FC NAD-dependent protein deacetylase (PubMed:12186850, PubMed:12374852, PubMed:16788062, PubMed:18680753, PubMed:18794531, PubMed:23283301, PubMed:24121500, PubMed:24252090, PubMed:19535340). Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues (PubMed:12186850, PubMed:12374852, PubMed:16788062, PubMed:18680753, PubMed:18794531, PubMed:23283301, PubMed:24121500, PubMed:24252090). Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5PO (PubMed:16788062, PubMed:18680753, PubMed:24121500, PubMed:24252090, PubMed:19535340). Contributes to the regulation of the cellular energy metabolism (PubMed:24252090). Important for regulating tissue-specific ATP levels (PubMed:18794531). In response to metabolic stress, deacetylates transcription factor FOXO3 and recruits FOXO3 and mitochondrial RNA polymerase POLRMT to mtDNA to promote mtDNA transcription (PubMed:23283301). TTVZLIJ EC EC 3.5.1.- TTVZLIJ PD 6ISO; 5ZGC; 5Z94; 5Z93; 5YTK TTVZLIJ SQ MAFWGWRAAAALRLWGRVVERVEAGGGVGPFQACGCRLVLGGRDDVSAGLRGSHGARGEPLDPARPLQRPPRPEVPRAFRRQPRAAAPSFFFSSIKGGRRSISFSVGASSVVGSGGSSDKGKLSLQDVAELIRARACQRVVVMVGAGISTPSGIPDFRSPGSGLYSNLQQYDLPYPEAIFELPFFFHNPKPFFTLAKELYPGNYKPNVTHYFLRLLHDKGLLLRLYTQNIDGLERVSGIPASKLVEAHGTFASATCTVCQRPFPGEDIRADVMADRVPRCPVCTGVVKPDIVFFGEPLPQRFLLHVVDFPMADLLLILGTSLEVEPFASLTEAVRSSVPRLLINRDLVGPLAWHPRSRDVAQLGDVVHGVESLVELLGWTEEMRDLVQRETGKLDGPDK TTVZLIJ TT Literature-reported TTVZLIJ KE hsa05230:Central carbon metabolism in cancer TTKLPHO ID TTKLPHO TTKLPHO TN Neonatal Fc receptor (FCGRT) TTKLPHO UP P55899 TTKLPHO UC FCGRN_HUMAN TTKLPHO BC Immunoglobulin TTKLPHO SN Neonatal FcR; MHC class I family-like Fc receptor; IgG Fc fragment receptor transporter, alpha chain; FcRn; FCGRT TTKLPHO GN FCGRT TTKLPHO FC Binds to the Fc region of monomericimmunoglobulins gamma. Mediates the uptake of IgG from milk. Possible role in transfer of immunoglobulin G from mother to fetus. TTKLPHO PD 6ILM; 6FGB; 6C99; 6C98; 6C97 TTKLPHO SQ MGVPRPQPWALGLLLFLLPGSLGAESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWYWEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNFDLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPPSMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSLTVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSSVLVVGIVIGVLLLTAAAVGGALLWRRMRSGLPAPWISLRGDDTGVLLPTPGEAQDADLKDVNVIPATA TTKLPHO TT Clinical trial TTED9LZ ID TTED9LZ TTED9LZ TN Neuroendocrine convertase 1 (PCSK1) TTED9LZ UP P29120 TTED9LZ UC NEC1_HUMAN TTED9LZ BC Peptidase TTED9LZ SN Proprotein convertase 1; Prohormone convertase 1; PCSK1; PC1; NEC 1 TTED9LZ GN PCSK1 TTED9LZ FC Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin and insulin. TTED9LZ EC EC 3.4.21.93 TTED9LZ SQ MERRAWSLQCTAFVLFCAWCALNSAKAKRQFVNEWAAEIPGGPEAASAIAEELGYDLLGQIGSLENHYLFKHKNHPRRSRRSAFHITKRLSDDDRVIWAEQQYEKERSKRSALRDSALNLFNDPMWNQQWYLQDTRMTAALPKLDLHVIPVWQKGITGKGVVITVLDDGLEWNHTDIYANYDPEASYDFNDNDHDPFPRYDPTNENKHGTRCAGEIAMQANNHKCGVGVAYNSKVGGIRMLDGIVTDAIEASSIGFNPGHVDIYSASWGPNDDGKTVEGPGRLAQKAFEYGVKQGRQGKGSIFVWASGNGGRQGDNCDCDGYTDSIYTISISSASQQGLSPWYAEKCSSTLATSYSSGDYTDQRITSADLHNDCTETHTGTSASAPLAAGIFALALEANPNLTWRDMQHLVVWTSEYDPLANNPGWKKNGAGLMVNSRFGFGLLNAKALVDLADPRTWRSVPEKKECVVKDNDFEPRALKANGEVIIEIPTRACEGQENAIKSLEHVQFEATIEYSRRGDLHVTLTSAAGTSTVLLAERERDTSPNGFKNWDFMSVHTWGENPIGTWTLRITDMSGRIQNEGRIVNWKLILHGTSSQPEHMKQPRVYTSYNTVQNDRRGVEKMVDPGEEQPTQENPKENTLVSKSPSSSSVGGRRDELEEGAPSQAMLRLLQSAFSKNSPPKQSPKKSPSAKLNIPYENFYEALEKLNKPSQLKDSEDSLYNDYVDVFYNTKPYKHRDDRLLQALVDILNEEN TTED9LZ TT Literature-reported TTED9LZ RC R-HSA-264876:Insulin processing TT46F0P ID TT46F0P TT46F0P TN Neuroendocrine convertase 2 (PCSK2) TT46F0P UP P16519 TT46F0P UC NEC2_HUMAN TT46F0P BC Peptidase TT46F0P SN Proprotein convertase 2; Prohormone convertase 2; PCSK2; PC2; NEC 2; KEX2-like endoprotease 2 TT46F0P GN PCSK2 TT46F0P FC Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. TT46F0P EC EC 3.4.21.94 TT46F0P SQ MKGGCVSQWKAAAGFLFCVMVFASAERPVFTNHFLVELHKGGEDKARQVAAEHGFGVRKLPFAEGLYHFYHNGLAKAKRRRSLHHKQQLERDPRVKMALQQEGFDRKKRGYRDINEIDINMNDPLFTKQWYLINTGQADGTPGLDLNVAEAWELGYTGKGVTIGIMDDGIDYLHPDLASNYNAEASYDFSSNDPYPYPRYTDDWFNSHGTRCAGEVSAAANNNICGVGVAYNSKVAGIRMLDQPFMTDIIEASSISHMPQLIDIYSASWGPTDNGKTVDGPRELTLQAMADGVNKGRGGKGSIYVWASGDGGSYDDCNCDGYASSMWTISINSAINDGRTALYDESCSSTLASTFSNGRKRNPEAGVATTDLYGNCTLRHSGTSAAAPEAAGVFALALEANLGLTWRDMQHLTVLTSKRNQLHDEVHQWRRNGVGLEFNHLFGYGVLDAGAMVKMAKDWKTVPERFHCVGGSVQDPEKIPSTGKLVLTLTTDACEGKENFVRYLEHVQAVITVNATRRGDLNINMTSPMGTKSILLSRRPRDDDSKVGFDKWPFMTTHTWGEDARGTWTLELGFVGSAPQKGVLKEWTLMLHGTQSAPYIDQVVRDYQSKLAMSKKEELEEELDEAVERSLKSILNKN TT46F0P TT Literature-reported TT46F0P RC R-HSA-264876:Insulin processing TTQACP9 ID TTQACP9 TTQACP9 TN Neuronal acetylcholine receptor alpha-9 (CHRNA9) TTQACP9 UP Q9UGM1 TTQACP9 UC ACHA9_HUMAN TTQACP9 BC Neurotransmitter receptor TTQACP9 SN Nicotinic acetylcholine receptor subunit alpha 9; NACHR alpha 9; CHRNA9 TTQACP9 GN CHRNA9 TTQACP9 FC Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding induces a conformation change that leads to the opening of an ion-conducting channel across the plasma membrane (PubMed:11752216, PubMed:25282151). The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane (PubMed:11752216, PubMed:25282151). In the ear, this may lead to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma. May also regulate keratinocyte adhesion (PubMed:11021840). TTQACP9 PD 6HY7; 4UY2; 4UXU; 4D01 TTQACP9 SQ MNWSHSCISFCWIYFAASRLRAAETADGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQIWHDAYLTWDRDQYDGLDSIRIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDAPAITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDIFNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSSFYIVNLLIPCVLISFLAPLSFYLPAASGEKVSLGVTILLAMTVFQLMVAEIMPASENVPLIGKYYIATMALITASTALTIMVMNIHFCGAEARPVPHWARVVILKYMSRVLFVYDVGESCLSPHHSRERDHLTKVYSKLPESNLKAARNKDLSRKKDMNKRLKNDLGCQGKNPQEAESYCAQYKVLTRNIEYIAKCLKDHKATNSKGSEWKKVAKVIDRFFMWIFFIMVFVMTILIIARAD TTQACP9 TT Literature-reported TTQACP9 KE hsa04080:Neuroactive ligand-receptor interaction TTQACP9 RC R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors TTTSCQ2 ID TTTSCQ2 TTTSCQ2 TN Ornithine delta-aminotransferase (OAT) TTTSCQ2 UP P04181 TTTSCQ2 UC OAT_HUMAN TTTSCQ2 BC Transaminase TTTSCQ2 SN Ornithine--oxo-acid aminotransferase; Ornithine aminotransferase, mitochondrial TTTSCQ2 GN OAT TTTSCQ2 FC Catalyzes the transfer of the delta-amino group from L-ornithine. TTTSCQ2 EC EC 2.6.1.13 TTTSCQ2 PD 5VWO; 2OAT; 2CAN; 2BYL; 2BYJ TTTSCQ2 SQ MFSKLAHLQRFAVLSRGVHSSVASATSVATKKTVQGPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHKVLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAISSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDIVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKTILSF TTTSCQ2 TT Literature-reported TTTSCQ2 KE hsa00330:Arginine and proline metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics TTTSCQ2 RC R-HSA-70614:Amino acid synthesis and interconversion (transamination) TTAFJUD ID TTAFJUD TTAFJUD TN Orotidine 5'-monophosphate decarboxylase (UMPS) TTAFJUD UP P11172 TTAFJUD UC UMPS_HUMAN TTAFJUD BC Pentosyltransferase TTAFJUD SN Uridine 5'-monophosphate synthase; UMP synthase TTAFJUD GN UMPS TTAFJUD FC Catalyses the formation of uridine monophosphate (UMP), an energy-carrying molecule in many important biosynthetic pathways. TTAFJUD PD 4HKP; 4HIB; 3MW7; 3MO7; 3MI2 TTAFJUD SQ MAVARAALGPLVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVCTLSKMLEILEQQKKVDAETVGRVKRFIQENVFVAANHNGSPLSIKEAPKELSFGARAELPRIHPVASKLLRLMQKKETNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKCHEFLIFEDRKFADIGNTVKKQYEGGIFKIASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLATGDYTRAAVRMAEEHSEFVVGFISGSRVSMKPEFLHLTPGVQLEAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMYRKAAWEAYLSRLGV TTAFJUD TT Literature-reported TTAFJUD KE hsa00240:Pyrimidine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways TTAFJUD RC R-HSA-500753:Pyrimidine biosynthesis TTECBXN ID TTECBXN TTECBXN TN Oxysterols receptor LXR-alpha (NR1H3) TTECBXN UP Q13133 TTECBXN UC NR1H3_HUMAN TTECBXN BC Nuclear hormone receptor TTECBXN SN Nuclear receptor subfamily 1 group H member 3; Nuclear receptor LXRalpha; Nuclear orphan receptor LXR-alpha; Liver X receptor alpha; LXRalpha; LXRA TTECBXN GN NR1H3 TTECBXN FC Interaction with retinoic acid receptor (RXR) shifts RXR from its role as a silent DNA-binding partner to an active ligand-binding subunit in mediating retinoid responses through target genes defined by LXRES. LXRES are DR4-type response elements characterized by direct repeats of two similar hexanuclotide half-sites spaced by four nucleotides. Plays an important role in the regulation of cholesterol homeostasis, regulating cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism. Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity. TTECBXN PD 5HJS; 5AVL; 5AVI; 3IPU; 3IPS TTECBXN SQ MSLWLGAPVPDIPPDSAVELWKPGAQDASSQAQGGSSCILREEARMPHSAGGTAGVGLEAAEPTALLTRAEPPSEPTEIRPQKRKKGPAPKMLGNELCSVCGDKASGFHYNVLSCEGCKGFFRRSVIKGAHYICHSGGHCPMDTYMRRKCQECRLRKCRQAGMREECVLSEEQIRLKKLKRQEEEQAHATSLPPRASSPPQILPQLSPEQLGMIEKLVAAQQQCNRRSFSDRLRVTPWPMAPDPHSREARQQRFAHFTELAIVSVQEIVDFAKQLPGFLQLSREDQIALLKTSAIEVMLLETSRRYNPGSESITFLKDFSYNREDFAKAGLQVEFINPIFEFSRAMNELQLNDAEFALLIAISIFSADRPNVQDQLQVERLQHTYVEALHAYVSIHHPHDRLMFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE TTECBXN TT Patented-recorded TTECBXN FM Nuclear hormone receptor family TTECBXN KE hsa03320:PPAR signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05160:Hepatitis C TTA93TL ID TTA93TL TTA93TL TN P2Y purinoceptor 1 (P2RY1) TTA93TL UP P47900 TTA93TL UC P2RY1_HUMAN TTA93TL BC GPCR rhodopsin TTA93TL SN P2Y1; P2Y(1) receptor; P2RY1; Adenosine P2Y1 receptor TTA93TL GN P2RY1 TTA93TL FC Receptor for extracellular adenine nucleotides such as ATP and ADP. In platelets binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and probably to platelet aggregation. TTA93TL PD 4XNW; 4XNV; 1Y36 TTA93TL SQ MTEVLWPAVPNGTDAAFLAGPGSSWGNSTVASTAAVSSSFKCALTKTGFQFYYLPAVYILVFIIGFLGNSVAIWMFVFHMKPWSGISVYMFNLALADFLYVLTLPALIFYYFNKTDWIFGDAMCKLQRFIFHVNLYGSILFLTCISAHRYSGVVYPLKSLGRLKKKNAICISVLVWLIVVVAISPILFYSGTGVRKNKTITCYDTTSDEYLRSYFIYSMCTTVAMFCVPLVLILGCYGLIVRALIYKDLDNSPLRRKSIYLVIIVLTVFAVSYIPFHVMKTMNLRARLDFQTPAMCAFNDRVYATYQVTRGLASLNSCVDPILYFLAGDTFRRRLSRATRKASRRSEANLQSKSEDMTLNILPEFKQNGDTSL TTA93TL TT Literature-reported TTA93TL KE hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04611:Platelet activation TTA93TL RC R-HSA-416476:G alpha (q) signalling events; R-HSA-417957:P2Y receptors; R-HSA-418592:ADP signalling through P2Y purinoceptor 1 TTEUQ4M ID TTEUQ4M TTEUQ4M TN Phosphatase and tensin homolog (PTEN) TTEUQ4M UP P60484 TTEUQ4M UC PTEN_HUMAN TTEUQ4M BC Phosphoric monoester hydrolase TTEUQ4M SN TEP1; Phosphatidylinositol 3,4,5trisphosphate 3phosphatase and dualspecificity protein phosphatase PTEN; Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN; Mutated in multiple advanced cancers 1; MMAC1 TTEUQ4M GN PTEN TTEUQ4M FC Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement. Tumor suppressor. TTEUQ4M EC EC 3.1.3.16 TTEUQ4M PD 5BZZ; 5BZX; 5BUG; 4O1V; 2KYL TTEUQ4M SQ MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV TTEUQ4M TT Literature-reported TTEUQ4M FM Phosphoric monoester hydrolases TT3ZS42 ID TT3ZS42 TT3ZS42 TN Phosphodiesterase 1B (PDE1B) TT3ZS42 UP Q01064 TT3ZS42 UC PDE1B_HUMAN TT3ZS42 BC Phosphoric diester hydrolase TT3ZS42 SN PDES1B; PDE1B1; CamPDE 1B; Cam-PDE 1B; Calcium/calmodulindependent 3',5'cyclicnucleotide phosphodiesterase 1B; Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B; 63 kDa CamPDE; 63 kDa Cam-PDE TT3ZS42 GN PDE1B TT3ZS42 FC Has a preference for cGMP as a substrate. Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. TT3ZS42 EC EC 3.1.4.17 TT3ZS42 PD 5W6E; 5UP0; 5UOY; 5B25; 4NPW TT3ZS42 SQ MELSPRSPPEMLEESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEINIEELKKNLEYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQARAKGRRAEEKPKFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTAVLNCLKNLDLWCFDVFSLNQAADDHALRTIVFELLTRHNLISRFKIPTVFLMSFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIELLAIIFAAAIHDYEHTGTTNSFHIQTKSECAIVYNDRSVLENHHISSVFRLMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKPKALSLLLHAADISHPTKQWLVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLADEDSKSKNQPSFQWRQPSLDVEVGDPNPDVVSFRSTWVKRIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD TT3ZS42 TT Patented-recorded TT3ZS42 KE hsa00230:Purine metabolism; hsa04020:Calcium signaling pathway; hsa05032:Morphine addiction TT3ZS42 RC R-HSA-418457:cGMP effects; R-HSA-418555:G alpha (s) signalling events TT9H4P3 ID TT9H4P3 TT9H4P3 TN PI3K p110 beta messenger RNA (PIK3CB mRNA) TT9H4P3 UP P42338 TT9H4P3 UC PK3CB_HUMAN TT9H4P3 BC mRNA target TT9H4P3 SN p110beta (mRNA); PtdIns3kinase subunit p110beta (mRNA); PtdIns3kinase subunit beta (mRNA); PtdIns-3-kinase subunit p110-beta (mRNA); PtdIns-3-kinase subunit beta (mRNA); Phosphatidylinositol 4,5bisphosphate 3kinase catalytic subunitbeta isoform (mRNA); Phosphatidylinositol 4,5bisphosphate 3kinase 110 kDa catalyticsubunit beta (mRNA); Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform (mRNA); Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta (mRNA); PIK3C1 (mRNA); PI3kinase subunit beta (mRNA); PI3Kbeta (mRNA); PI3K-beta (mRNA); PI3-kinase subunit beta (mRNA) TT9H4P3 GN PIK3CB TT9H4P3 FC Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Involved in the activation of AKT1 upon stimulation by G-protein coupled receptors (GPCRs) ligands such as CXCL12, sphingosine 1-phosphate, and lysophosphatidic acid. May also act downstream receptor tyrosine kinases. Required in different signaling pathways for stable platelet adhesion and aggregation. Plays a role in platelet activation signaling triggered by GPCRs, alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) and ITAM (immunoreceptor tyrosine-based activation motif)-bearing receptors such as GP6. Regulates the strength of adhesion of ITGA2B/ ITGB3 activated receptors necessary for the cellular transmission of contractile forces. Required for platelet aggregation induced by F2 (thrombin) and thromboxane A2 (TXA2). Has a role in cell survival. May have a role in cell migration. Involved in the early stage of autophagosome formation. Modulates the intracellular level of PtdIns3P (Phosphatidylinositol 3-phosphate) and activates PIK3C3 kinase activity. May act as a scaffold, independently of its lipid kinase activity to positively regulate autophagy. May have a role in insulin signaling as scaffolding protein in which the lipid kinase activity is not required. May have a kinase-independent function in regulating cell proliferation and in clathrin-mediated endocytosis. Mediator of oncogenic signal in cell lines lacking PTEN. The lipid kinase activity is necessary for its role in oncogenic transformation. Required for the growth of ERBB2 and RAS driven tumors. TT9H4P3 EC EC 2.7.1.153 TT9H4P3 SQ MCFSFIMPPAMADILDIWAVDSQIASDGSIPVDFLLPTGIYIQLEVPREATISYIKQMLWKQVHNYPMFNLLMDIDSYMFACVNQTAVYEELEDETRRLCDVRPFLPVLKLVTRSCDPGEKLDSKIGVLIGKGLHEFDSLKDPEVNEFRRKMRKFSEEKILSLVGLSWMDWLKQTYPPEHEPSIPENLEDKLYGGKLIVAVHFENCQDVFSFQVSPNMNPIKVNELAIQKRLTIHGKEDEVSPYDYVLQVSGRVEYVFGDHPLIQFQYIRNCVMNRALPHFILVECCKIKKMYEQEMIAIEAAINRNSSNLPLPLPPKKTRIISHVWENNNPFQIVLVKGNKLNTEETVKVHVRAGLFHGTELLCKTIVSSEVSGKNDHIWNEPLEFDINICDLPRMARLCFAVYAVLDKVKTKKSTKTINPSKYQTIRKAGKVHYPVAWVNTMVFDFKGQLRTGDIILHSWSSFPDELEEMLNPMGTVQTNPYTENATALHVKFPENKKQPYYYPPFDKIIEKAAEIASSDSANVSSRGGKKFLPVLKEILDRDPLSQLCENEMDLIWTLRQDCREIFPQSLPKLLLSIKWNKLEDVAQLQALLQIWPKLPPREALELLDFNYPDQYVREYAVGCLRQMSDEELSQYLLQLVQVLKYEPFLDCALSRFLLERALGNRRIGQFLFWHLRSEVHIPAVSVQFGVILEAYCRGSVGHMKVLSKQVEALNKLKTLNSLIKLNAVKLNRAKGKEAMHTCLKQSAYREALSDLQSPLNPCVILSELYVEKCKYMDSKMKPLWLVYNNKVFGEDSVGVIFKNGDDLRQDMLTLQMLRLMDLLWKEAGLDLRMLPYGCLATGDRSGLIEVVSTSETIADIQLNSSNVAAAAAFNKDALLNWLKEYNSGDDLDRAIEEFTLSCAGYCVASYVLGIGDRHSDNIMVKKTGQLFHIDFGHILGNFKSKFGIKRERVPFILTYDFIHVIQQGKTGNTEKFGRFRQCCEDAYLILRRHGNLFITLFALMLTAGLPELTSVKDIQYLKDSLALGKSEEEALKQFKQKFDEALRESWTTKVNWMAHTVRKDYRS TT9H4P3 TT Literature-reported TT9H4P3 FM mRNA target TT9H4P3 KE hsa00562:Inositol phosphate metabolism; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04070:Phosphatidylinositol signaling system; hsa04071:Sphingolipid signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04210:Apoptosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04611:Platelet activation; hsa04620:Toll-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04960:Aldosterone-regulated sodium reabsorption; hsa04973:Carbohydrate digestion and absorption; hsa05100:Bacterial invasion of epithelial cells; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TT9H4P3 RC R-HSA-109704:PI3K Cascade; R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-198203:PI3K/AKT activation; R-HSA-2029485:Role of phospholipids in phagocytosis; R-HSA-210993:Tie2 Signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-2424491:DAP12 signaling; R-HSA-2730905:Role of LAT2/NTAL/LAB on calcium mobilization; R-HSA-373753:Nephrin interactions; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-512988:Interleukin-3, 5 and GM-CSF signaling; R-HSA-912526:Interleukin receptor SHC signaling; R-HSA-912631:Regulation of signaling by CBL TT2MI95 ID TT2MI95 TT2MI95 TN PKC-alpha messenger RNA (PRKCA mRNA) TT2MI95 UP P17252 TT2MI95 UC KPCA_HUMAN TT2MI95 BC mRNA target TT2MI95 SN Protein kinase C alpha type (mRNA); Protein Kinase C alpha (mRNA); PRKACA (mRNA); PKCalpha (mRNA); PKCA (mRNA); PKC-alpha (mRNA); PKC-A (mRNA) TT2MI95 GN PRKCA TT2MI95 FC Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42. Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. TT2MI95 EC EC 2.7.11.13 TT2MI95 PD 4RA4; 4DNL; 3IW4; 2ELI TT2MI95 SQ MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV TT2MI95 TT Literature-reported TT2MI95 FM mRNA target TTBSN0L ID TTBSN0L TTBSN0L TN PKC-zeta messenger RNA (PRKCZ mRNA) TTBSN0L UP Q05513 TTBSN0L UC KPCZ_HUMAN TTBSN0L BC mRNA target TTBSN0L SN Protein kinase C zeta type (mRNA); PKC2 (mRNA); NPKC-zeta (mRNA) TTBSN0L GN PRKCZ TTBSN0L FC Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. In vein endothelial cells treated with the oxidant peroxynitrite, phosphorylates STK11 leading to nuclear export of STK11, subsequent inhibition of PI3K/Akt signaling, and increased apoptosis. Phosphorylates VAMP2 in vitro. Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). TTBSN0L EC EC 2.7.11.13 TTBSN0L SQ MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV TTBSN0L TT Literature-reported TTBSN0L FM mRNA target TTBSN0L KE hsa04015:Rap1 signaling pathway; hsa04062:Chemokine signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04390:Hippo signaling pathway; hsa04530:Tight junction; hsa04611:Platelet activation; hsa04910:Insulin signaling pathway; hsa04930:Type II diabetes mellitus TTBSN0L RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-2173791:TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition); R-HSA-5218921:VEGFR2 mediated cell proliferation TT7EASG ID TT7EASG TT7EASG TN Plasmodium Cysteine protease falcipain-2 (Malaria CPF2) TT7EASG UP Q9N6S8 TT7EASG UC Q9N6S8_PLAFA TT7EASG BC Protease TT7EASG SN Falcipain 2; Cysteine proteinase falcipain 2a TT7EASG GN Malaria CPF2 TT7EASG FC A papain family cysteine protease and important hemoglobinase of erythrocytic Plasmodium falciparum parasites. TT7EASG EC EC 3.4.22.- TT7EASG PD 3PNR; 3BPF; 2GHU; 1YVB TT7EASG SQ MDYNMDYAPHEVISQQGERFVDKYVDRKILKNKKSLLVIISLSVLSVVGFVLFYFTPNSRKSDLFKNSSVENNNDDYIINSLLKSPNGKKFIVSKIDEALSFYDSKKNDINKYNEGNNNNNADFKGLSLFKENTPSNNFIHNKDYFINFFDNKFLMNNAEHINQFYMFIKTNNKQYNSPNEMKERFQVFLQNAHKVNMHNNNKNSLYKKELNRFADLTYHEFKNKYLSLRSSKPLKNSKYLLDQMNYEEVIKKYRGEENFDHAAYDWRLHSGVTPVKDQKNCGSCWAFSSIGSVESQYAIRKNKLITLSEQELVDCSFKNYGCNGGLINNAFEDMIELGGICPDGDYPYVSDAPNLCNIDRCTEKYGIKNYLSVPDNKLKEALRFLGPISISVAVSDDFAFYKEGIFDGECGDQLNHAVMLVGFGMKEIVNPLTKKGEKHYYYIIKNSWGQQWGERGFINIETDESGLMRKCGLGTDAFIPLIE TT7EASG TT Literature-reported TTBL49X ID TTBL49X TTBL49X TN Plasmodium Hypoxanthine-guanine phosphoribosyltransferase (Malaria LACZ) TTBL49X UP P20035 TTBL49X UC HGXR_PLAFG TTBL49X BC Pentosyltransferase TTBL49X SN LACZ of Plasmodium falciparum (isolate FCR-3 / Gambia); Hypoxanthine phosphoribosyltransferase; HPRT; HGPRTase; HGPRT of Plasmodium falciparum (isolate FCR-3 / Gambia); Guanine phosphoribosyltransferase; GPRT TTBL49X GN Malaria LACZ TTBL49X FC Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5- phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway. TTBL49X PD 3OZG; 3OZF; 2VFA; 1CJB TTBL49X SQ MPIPNNPGAGENAFDPVFVNDDDGYDLDSFMIPAHYKKYLTKVLVPNGVIKNRIEKLAYDIKKVYNNEEFHILCLLKGSRGFFTALLKHLSRIHNYSAVETSKPLFGEHYVRVKSYCNDQSTGTLEIVSEDLSCLKGKHVLIVEDIIDTGKTLVKFCEYLKKFEIKTVAIACLFIKRTPLWNGFKADFVGFSIPDHFVVGYSLDYNEIFRDLDHCCLVNDEGKKKYKATSL TTBL49X TT Patented-recorded TTBL49X KE hsa00230:Purine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways TTBL49X RC R-HSA-74217:Purine salvage TT86VZE ID TT86VZE TT86VZE TN Plasmodium M1-family aminopeptidase (Malaria MFA) TT86VZE UP O96935 TT86VZE UC AMP1_PLAFQ TT86VZE BC Peptidase TT86VZE SN Pfa-M1 TT86VZE GN Malaria MFA TT86VZE FC Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC. TT86VZE EC EC 3.4.11.- TT86VZE PD 6EED; 6EE6; 6EE4; 6EE3; 6EAB TT86VZE SQ MKLTKGCAYKYIIFTVLILANILYDNKKRCMIKKNLRISSCGIISRLLKSNSNYNSFNKNYNFTSAISELQFSNFWNLDILQKDIFSNIHNNKNKPQSYIIHKRLMSEKGDNNNNNHQNNNGNDNKKRLGSVVNNEENTCSDKRMKPFEEGHGITQVDKMNNNSDHLQQNGVMNLNSNNVENNNNNNSVVVKKNEPKIHYRKDYKPSGFIINNVTLNINIHDNETIVRSVLDMDISKHNVGEDLVFDGVGLKINEISINNKKLVEGEEYTYDNEFLTIFSKFVPKSKFAFSSEVIIHPETNYALTGLYKSKNIIVSQCEATGFRRITFFIDRPDMMAKYDVTVTADKEKYPVLLSNGDKVNEFEIPGGRHGARFNDPHLKPCYLFAVVAGDLKHLSATYITKYTKKKVELYVFSEEKYVSKLQWALECLKKSMAFDEDYFGLEYDLSRLNLVAVSDFNVGAMENKGLNIFNANSLLASKKNSIDFSYARILTVVGHEYFHNYTGNRVTLRDWFQLTLKEGLTVHRENLFSEEMTKTVTTRLSHVDLLRSVQFLEDSSPLSHPIRPESYVSMENFYTTTVYDKGSEVMRMYLTILGEEYYKKGFDIYIKKNDGNTATCEDFNYAMEQAYKMKKADNSANLNQYLLWFSQSGTPHVSFKYNYDAEKKQYSIHVNQYTKPDENQKEKKPLFIPISVGLINPENGKEMISQTTLELTKESDTFVFNNIAVKPIPSLFRGFSAPVYIEDNLTDEERILLLKYDSDAFVRYNSCTNIYMKQILMNYNEFLKAKNEKLESFNLTPVNAQFIDAIKYLLEDPHADAGFKSYIVSLPQDRYIINFVSNLDTDVLADTKEYIYKQIGDKLNDVYYKMFKSLEAKADDLTYFNDESHVDFDQMNMRTLRNTLLSLLSKAQYPNILNEIIEHSKSPYPSNWLTSLSVSAYFDKYFELYDKTYKLSKDDELLLQEWLKTVSRSDRKDIYEILKKLENEVLKDSKNPNDIRAVYLPFTNNLRRFHDISGKGYKLIAEVITKTDKFNPMVATQLCEPFKLWNKLDTKRQELMLNEMNTMLQEPNISNNLKEYLLRLTNKL TT86VZE TT Literature-reported TTXMNHO ID TTXMNHO TTXMNHO TN Plasmodium Plasmepsin 2 (Malaria PLA2) TTXMNHO UP P46925 TTXMNHO UC PLM2_PLAFA TTXMNHO BC Peptidase TTXMNHO SN Plasmepsin-2; PFAPD; Aspartic hemoglobinase II TTXMNHO GN Malaria PLA2 TTXMNHO FC Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO(2))-Ser-Phe-Pro-Thr. TTXMNHO EC EC 3.4.23.39 TTXMNHO PD 5BWY; 4Z22; 4YA8; 4Y6M; 4CKU TTXMNHO SQ MDITVREHDFKHGFIKSNSTFDGLNIDNSKNKKKIQKGFQILYVLLFCSVMCGLFYYVYENVWLQRDNEMNEILKNSEHLTIGFKVENAHDRILKTIKTHKLKNYIKESVNFLNSGLTKTNYLGSSNDNIELVDFQNIMFYGDAEVGDNQQPFTFILDTGSANLWVPSVKCTTAGCLTKHLYDSSKSRTYEKDGTKVEMNYVSGTVSGFFSKDLVTVGNLSLPYKFIEVIDTNGFEPTYTASTFDGILGLGWKDLSIGSVDPIVVELKNQNKIENALFTFYLPVHDKHTGFLTIGGIEERFYEGPLTYEKLNHDLYWQITLDAHVGNIMLEKANCIVDSGTSAITVPTDFLNKMLQNLDVIKVPFLPFYVTLCNNSKLPTFEFTSENGKYTLEPEYYLQHIEDVGPGLCMLNIIGLDFPVPTFILGDPFMRKYFTVFDYDNHSVGIALAKKNL TTXMNHO TT Patented-recorded TTO8YH2 ID TTO8YH2 TTO8YH2 TN Plasmodium Serine hydroxymethyltransferase (Malaria SHMT) TTO8YH2 UP Q8I566 TTO8YH2 UC Q8I566_PLAF7 TTO8YH2 BC Methyltransferase TTO8YH2 SN Serine methylase; SHMT; Glycine hydroxymethyltransferase TTO8YH2 GN Malaria SHMT TTO8YH2 FC Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Interconversion of serine and glycine. Associates with mitochondrial DNA. TTO8YH2 EC EC 2.1.2.1 TTO8YH2 PD 4O6Z TTO8YH2 SQ MFNNDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRALEAFNVSEEEWGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDEKKKVSITSDLFESKLYKCNSEGYVDMESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILRGPRSALIFFNKKRNPGIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDLVTNGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCVSPSGIRIGTPALTTRGCKEKDMEFIADMLLKAILLTDELQQKYGKKLVDFKKGLVNNPKIDELKKEVVQWAKNLPFA TTO8YH2 TT Literature-reported TTO8YH2 KE hsa00260:Glycine, serine and threonine metabolism; hsa00460:Cyanoamino acid metabolism; hsa00630:Glyoxylate and dicarboxylate metabolism; hsa00670:One carbon pool by folate; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa01230:Biosynthesis of amino acids TTO8YH2 RC R-HSA-196757:Metabolism of folate and pterines TT976FS ID TT976FS TT976FS TN Polo-like kinase 2 (PLK2) TT976FS UP Q9NYY3 TT976FS UC PLK2_HUMAN TT976FS BC Kinase TT976FS SN hSNK; hPlk2; Serum-inducible kinase; Serine/threonine-protein kinase SNK; Serine/threonine-protein kinase PLK2; SNK; PLK-2 TT976FS GN PLK2 TT976FS FC Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress. Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. TT976FS EC EC 2.7.11.21 TT976FS PD 4XB0; 4RS6; 4I6H; 4I6F; 4I6B TT976FS SQ MELLRTITYQPAASTKMCEQALGKGCGADSKKKRPPQPPEESQPPQSQAQVPPAAPHHHHHHSHSGPEISRIIVDPTTGKRYCRGKVLGKGGFAKCYEMTDLTNNKVYAAKIIPHSRVAKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEAMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYTMPSSLLAPAKHLIASMLSKNPEDRPSLDDIIRHDFFLQGFTPDRLSSSCCHTVPDFHLSSPAKNFFKKAAAALFGGKKDKARYIDTHNRVSKEDEDIYKLRHDLKKTSITQQPSKHRTDEELQPPTTTVARSGTPAVENKQQIGDAIRMIVRGTLGSCSSSSECLEDSTMGSVADTVARVLRGCLENMPEADCIPKEQLSTSFQWVTKWVDYSNKYGFGYQLSDHTVGVLFNNGAHMSLLPDKKTVHYYAELGQCSVFPATDAPEQFISQVTVLKYFSHYMEENLMDGGDLPSVTDIRRPRLYLLQWLKSDKALMMLFNDGTFQVNFYHDHTKIIICSQNEEYLLTYINEDRISTTFRLTTLLMSGCSSELKNRMEYALNMLLQRCN TT976FS TT Patented-recorded TT976FS FM Kinase TT976FS KE hsa04068:FoxO signaling pathway TT7LCTF ID TT7LCTF TT7LCTF TN Pregnane X receptor (NR1I2) TT7LCTF UP O75469 TT7LCTF UC NR1I2_HUMAN TT7LCTF BC Nuclear hormone receptor TT7LCTF SN Steroid and xenobiotic receptor; SXR; PXR; Orphan nuclear receptor PXR; Orphan nuclear receptor PAR1; Nuclear receptor subfamily 1 group I member 2 TT7LCTF GN NR1I2 TT7LCTF FC Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, drugs and endogenous compounds. Activated by the antibiotic rifampicin and various plant metabolites, such as hyperforin, guggulipid, colupulone, and isoflavones. Response to specific ligands is species-specific. Activated by naturally occurring steroids, such as pregnenolone and progesterone. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes. Nuclear receptor that binds and is activated by variety of endogenous and xenobiotic compounds. TT7LCTF PD 6DUP; 6BNS; 5X0R; 5A86; 4XHD TT7LCTF SQ MEVRPKESWNHADFVHCEDTESVPGKPSVNADEEVGGPQICRVCGDKATGYHFNVMTCEGCKGFFRRAMKRNARLRCPFRKGACEITRKTRRQCQACRLRKCLESGMKKEMIMSDEAVEERRALIKRKKSERTGTQPLGVQGLTEEQRMMIRELMDAQMKTFDTTFSHFKNFRLPGVLSSGCELPESLQAPSREEAAKWSQVRKDLCSLKVSLQLRGEDGSVWNYKPPADSGGKEIFSLLPHMADMSTYMFKGIISFAKVISYFRDLPIEDQISLLKGAAFELCQLRFNTVFNAETGTWECGRLSYCLEDTAGGFQQLLLEPMLKFHYMLKKLQLHEEEYVLMQAISLFSPDRPGVLQHRVVDQLQEQFAITLKSYIECNRPQPAHRFLFLKIMAMLTELRSINAQHTQRLLRIQDIHPFATPLMQELFGITGS TT7LCTF TT Literature-reported TT7LCTF FM Zinc-finger TTWJTHX ID TTWJTHX TTWJTHX TN Protein kinase C iota (PRKCI) TTWJTHX UP P41743 TTWJTHX UC KPCI_HUMAN TTWJTHX BC Kinase TTWJTHX SN nPKC-iota; aPKC-lambda/iota; Protein kinase C iota type; PRKC-lambda/iota; DXS1179E; Atypical protein kinase C-lambda/iota TTWJTHX GN PRKCI TTWJTHX FC Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation. Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. TTWJTHX EC EC 2.7.11.13 TTWJTHX PD 5LIH; 5LI9; 5LI1; 3ZH8; 3A8X TTWJTHX SQ MPTQRDSSTMSHTVAGGGSGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCNEVRDMCSFDNEQLFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECGRHSLPQEPVMPMDQSSMHSDHAQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV TTWJTHX TT Literature-reported TTWJTHX FM Kinase TTWJTHX KE hsa04015:Rap1 signaling pathway; hsa04144:Endocytosis; hsa04390:Hippo signaling pathway; hsa04530:Tight junction; hsa04611:Platelet activation; hsa04910:Insulin signaling pathway TTWJTHX RC R-HSA-209543:p75NTR recruits signalling complexes; R-HSA-420029:Tight junction interactions TTD0652 ID TTD0652 TTD0652 TN Proteinase activated receptor 4 (F2RL3) TTD0652 UP Q96RI0 TTD0652 UC PAR4_HUMAN TTD0652 BC GPCR rhodopsin TTD0652 SN Thrombin receptor-like 3; Protease activated receptor 4; F2RL3; Coagulation factor II receptor-like3 TTD0652 GN F2RL3 TTD0652 FC Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation. TTD0652 PD 3QDZ; 2ZPK TTD0652 SQ MWGRLLLWPLVLGFSLSGGTQTPSVYDESGSTGGGDDSTPSILPAPRGYPGQVCANDSDTLELPDSSRALLLGWVPTRLVPALYGLVLVVGLPANGLALWVLATQAPRLPSTMLLMNLAAADLLLALALPPRIAYHLRGQRWPFGEAACRLATAALYGHMYGSVLLLAAVSLDRYLALVHPLRARALRGRRLALGLCMAAWLMAAALALPLTLQRQTFRLARSDRVLCHDALPLDAQASHWQPAFTCLALLGCFLPLLAMLLCYGATLHTLAASGRRYGHALRLTAVVLASAVAFFVPSNLLLLLHYSDPSPSAWGNLYGAYVPSLALSTLNSCVDPFIYYYVSAEFRDKVRAGLFQRSPGDTVASKASAEGGSRGMGTHSSLLQ TTD0652 TT Literature-reported TTD0652 KE hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04611:Platelet activation; hsa05200:Pathways in cancer TTD0652 RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-456926:Thrombin signalling through proteinase activated receptors (PARs) TTZILNJ ID TTZILNJ TTZILNJ TN Proto-oncogene c-Myc (MYC) TTZILNJ UP P01106 TTZILNJ UC MYC_HUMAN TTZILNJ SN Transcription factor p64; Myc proto-oncogene protein; Class E basic helix-loop-helix protein 39; BHLHE39 TTZILNJ GN MYC TTZILNJ FC Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. TTZILNJ PD 6G6L; 6G6K; 6G6J; 6C4U; 5I50 TTZILNJ SQ MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA TTZILNJ TT Literature-reported TTZILNJ KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04110:Cell cycle; hsa04151:PI3K-Akt signaling pathway; hsa04310:Wnt signaling pathway; hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04630:Jak-STAT signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05213:Endometrial cancer; hsa05216:Thyroid cancer; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05230:Central carbon metabolism in cancer TTZILNJ RC R-HSA-2122947:NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2173796:SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-4411364:Binding of TCF/LEF:CTNNB1 to target gene promoters; R-HSA-5687128:MAPK6/MAPK4 signaling; R-HSA-69202:Cyclin E associated events during G1/S transition; R-HSA-69656:Cyclin A:Cdk2-associated events at S phase entry TTKVNRF ID TTKVNRF TTKVNRF TN Pseudomonas Nicotinate-nucleotide adenylyltransferase (Pseudo nadD) TTKVNRF UP Q9HX21 TTKVNRF UC NADD_PSEAE TTKVNRF BC Kinase TTKVNRF SN nadD of Pseudomonas aeruginosa; Nicotinic acid mononucleotide adenylyltransferase of Pseudomonas aeruginosa; Nicotinatemononucleotide adenylyltransferase of Pseudomonas aeruginosa; Nicotinate-nucleotide adenylyltransferase of Pseudomonas aeruginosa; NaMN-Atase; NaMN adenylyltransferase of Pseudomonas aeruginosa; NaMN AT of Pseudomonas aeruginosa; Deamido-NAD(+) pyrophosphorylase of Pseudomonas aeruginosa; Deamido-NAD(+) diphosphorylase of Pseudomonas aeruginosa TTKVNRF GN Pseudo nadD TTKVNRF FC Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). TTKVNRF EC EC 2.7.7.18 TTKVNRF PD 1YUN; 1YUM; 1YUL TTKVNRF SQ MGKRIGLFGGTFDPVHIGHMRSAVEMAEQFALDELRLLPNARPPHRETPQVSAAQRLAMVERAVAGVERLTVDPRELQRDKPSYTIDTLESVRAELAADDQLFMLIGWDAFCGLPTWHRWEALLDHCHIVVLQRPDADSEPPESLRDLLAARSVADPQALKGPGGQITFVWQTPLAVSATQIRALLGAGRSVRFLVPDAVLNYIEAHHLYRAPH TTKVNRF TT Literature-reported TTKVNRF KE pae00760:Nicotinate and nicotinamide metabolism; pae01100:Metabolic pathways TTXI3KF ID TTXI3KF TTXI3KF TN Pyridoxal kinase (PDXK) TTXI3KF UP O00764 TTXI3KF UC PDXK_HUMAN TTXI3KF BC Kinase TTXI3KF SN Pyridoxine kinase; PDXK TTXI3KF GN PDXK TTXI3KF FC Required for synthesisof pyridoxal-5-phosphate from vitamin B6. TTXI3KF EC EC 2.7.1.35 TTXI3KF PD 4EOH; 4EN4; 3KEU; 3FHY; 3FHX TTXI3KF SQ MEEECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGSNYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL TTXI3KF TT Literature-reported TTXI3KF KE hsa00750:Vitamin B6 metabolism; hsa01100:Metabolic pathways TTJGCKM ID TTJGCKM TTJGCKM TN Pyruvate dehydrogenase kinase 2 (PDHK2) TTJGCKM UP Q15119 TTJGCKM UC PDK2_HUMAN TTJGCKM BC Kinase TTJGCKM SN PDKII; PDK2; PDH kinase 2; [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial TTJGCKM GN PDK2 TTJGCKM FC Kinase that plays a key role in the regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis. TTJGCKM EC EC 2.7.11.2 TTJGCKM PD 5M4P; 5M4N; 5M4M; 5M4K; 5J71 TTJGCKM SQ MRWVWALLKNASLAGAPKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIMEFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLIFDGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKNAMRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHYQTIQEAGDWCVPSTEPKNTSTYRVS TTJGCKM TT Literature-reported TTJGCKM RC R-HSA-204174:Regulation of pyruvate dehydrogenase (PDH) complex TTH24WI ID TTH24WI TTH24WI TN RAC-beta serine/threonine-protein kinase (AKT2) TTH24WI UP P31751 TTH24WI UC AKT2_HUMAN TTH24WI BC Kinase TTH24WI SN RAC-PK-beta; Protein kinase B beta; Protein kinase Akt-2; PKB beta TTH24WI GN AKT2 TTH24WI FC AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. TTH24WI EC EC 2.7.11.1 TTH24WI PD 3E8D; 3D0E; 3.00E+88; 3.00E+87; 2XH5 TTH24WI SQ MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIRE TTH24WI TT Literature-reported TTH24WI FM Kinase TTH24WI RC R-HSA-111447:Activation of BAD and translocation to mitochondria; R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-1445148:Translocation of GLUT4 to the plasma membrane; R-HSA-165158:Activation of AKT2; R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-198693:AKT phosphorylates targets in the nucleus; R-HSA-199418:Negative regulation of the PI3K/AKT network; R-HSA-211163:AKT-mediated inactivation of FOXO1A; R-HSA-3769402:Deactivation of the beta-catenin transactivating complex; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-5218920:VEGFR2 mediated vascular permeability; R-HSA-5628897:TP53 Regulates Metabolic Genes; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer TT2M9CG ID TT2M9CG TT2M9CG TN Ras-related C3 botulinum toxin substrate 1 (RAC1) TT2M9CG UP P63000 TT2M9CG UC RAC1_HUMAN TT2M9CG BC Small GTPase TT2M9CG SN Cell migration-inducing gene5 protein TT2M9CG GN RAC1 TT2M9CG FC In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion, migration and differentiation, and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3. Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. TT2M9CG EC EC 3.6.5.2 TT2M9CG PD 6BC1; 6AGP; 5O33; 5N6O; 5HZH TT2M9CG SQ MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL TT2M9CG TT Literature-reported TT2M9CG FM Small GTPase superfamily TT2M9CG KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04145:Phagosome; hsa04151:PI3K-Akt signaling pathway; hsa04310:Wnt signaling pathway; hsa04360:Axon guidance; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04620:Toll-like receptor signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04972:Pancreatic secretion; hsa05014:Amyotrophic lateral sclerosis (ALS); hsa05100:Bacterial invasion of epithelial cells; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05231:Choline metabolism in cancer; hsa05416:Viral myocarditis TTP2U16 ID TTP2U16 TTP2U16 TN RhoA messenger RNA (RHOA mRNA) TTP2U16 UP P61586 TTP2U16 UC RHOA_HUMAN TTP2U16 BC mRNA target TTP2U16 SN h12 (mRNA); Transforming protein RhoA (mRNA); Rho cDNA clone 12 (mRNA); RHO12 (mRNA); ARHA (mRNA); ARH12 (mRNA) TTP2U16 GN RHOA TTP2U16 FC Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. TTP2U16 EC EC 3.6.5.2 TTP2U16 PD 6R3V; 6BCB; 6BCA; 6BC0; 5ZHX TTP2U16 SQ MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKKSGCLVL TTP2U16 TT Literature-reported TTP2U16 FM mRNA target TTP2U16 KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04144:Endocytosis; hsa04270:Vascular smooth muscle contraction; hsa04310:Wnt signaling pathway; hsa04350:TGF-beta signaling pathway; hsa04360:Axon guidance; hsa04510:Focal adhesion; hsa04520:Adherens junction; hsa04530:Tight junction; hsa04611:Platelet activation; hsa04660:T cell receptor signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa04722:Neurotrophin signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa04921:Oxytocin signaling pathway; hsa04972:Pancreatic secretion; hsa05100:Bacterial invasion of epithelial cells; hsa05130:Pathogenic Escherichia coli infection; hsa05133:Pertussis; hsa05152:Tuberculosis; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer TTP2U16 RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-193634:Axonal growth inhibition (RHOA activation); R-HSA-194840:Rho GTPase cycle; R-HSA-198203:PI3K/AKT activation; R-HSA-209563:Axonal growth stimulation; R-HSA-2173791:TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition); R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-4086400:PCP/CE pathway; R-HSA-416482:G alpha (12/13) signalling events; R-HSA-416550:Sema4D mediated inhibition of cell attachment and migration; R-HSA-416572:Sema4D induced cell migration and growth-cone collapse; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5625740:RHO GTPases activate PKNs; R-HSA-5625900:RHO GTPases activate CIT; R-HSA-5627117:RHO GTPases Activate ROCKs; R-HSA-5663220:RHO GTPases Activate Formins TTH0KSX ID TTH0KSX TTH0KSX TN Rhodopsin (RHO) TTH0KSX UP P08100 TTH0KSX UC OPSD_HUMAN TTH0KSX BC GPCR rhodopsin TTH0KSX SN Opsin-2; OPN2 TTH0KSX GN RHO TTH0KSX FC Required for photoreceptor cell viability after birth. Light-induced isomerization of the chromophore 11-cis-retinal to all-trans-retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling. Photoreceptor required for image-forming vision at low light intensity. TTH0KSX PD 6CMO; 5W0P; 5DGY; 4ZWJ TTH0KSX SQ MNGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGSNFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTTICCGKNPLGDDEASATVSKTETSQVAPA TTH0KSX TT Literature-reported TTH0KSX FM GPCR rhodopsin TTH0KSX KE hsa04744:Phototransduction TTH0KSX RC R-HSA-2453902:The canonical retinoid cycle in rods (twilight vision); R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade; R-HSA-418594:G alpha (i) signalling events TT25MVL ID TT25MVL TT25MVL TN Serine protease hepsin (HPN) TT25MVL UP P05981 TT25MVL UC HEPS_HUMAN TT25MVL BC Peptidase TT25MVL SN Transmembrane protease, serine 1; HPN; HEPSIN TT25MVL GN HPN TT25MVL FC Plays an essential role in cell growth and maintenance of cell morphology. May mediate the activating cleavage of HGF and MST1/HGFL. Plays a role in the proteolytic processing of ACE2. TT25MVL EC EC 3.4.21.106 TT25MVL PD 5CE1; 3T2N; 1Z8G; 1P57; 1O5F TT25MVL SQ MAQKEGGRTVPCCSRPKVAALTAGTLLLLTAIGAASWAIVAVLLRSDQEPLYPVQVSSADARLMVFDKTEGTWRLLCSSRSNARVAGLSCEEMGFLRALTHSELDVRTAGANGTSGFFCVDEGRLPHTQRLLEVISVCDCPRGRFLAAICQDCGRRKLPVDRIVGGRDTSLGRWPWQVSLRYDGAHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVAQASPHGLQLGVQAVVYHGGYLPFRDPNSEENSNDIALVHLSSPLPLTEYIQPVCLPAAGQALVDGKICTVTGWGNTQYYGQQAGVLQEARVPIISNDVCNGADFYGNQIKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISRTPRWRLCGIVSWGTGCALAQKPGVYTKVSDFREWIFQAIKTHSEASGMVTQL TT25MVL TT Patented-recorded TT25MVL KE hsa05203:Viral carcinogenesis TT7YJFO ID TT7YJFO TT7YJFO TN SET and MYND domain-containing protein 2 (SMYD2) TT7YJFO UP Q9NRG4 TT7YJFO UC SMYD2_HUMAN TT7YJFO BC Methyltransferase TT7YJFO SN Nlysine methyltransferase SMYD2; N-lysine methyltransferase SMYD2; Lysine Nmethyltransferase 3C; Lysine N-methyltransferase 3C; KMT3C; Histone methyltransferase SMYD2; HSKMB; HSKM-B TT7YJFO GN SMYD2 TT7YJFO FC Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'. Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. TT7YJFO EC EC 2.1.1.- TT7YJFO PD 6MON; 6CBY; 6CBX; 5WCG; 5V3H TT7YJFO SQ MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIESH TT7YJFO TT Preclinical TT7YJFO FM Methyltransferase superfamily TT7YJFO RC R-HSA-3214841:PKMTs methylate histone lysines TTDBX7N ID TTDBX7N TTDBX7N TN S-methyl-5'-thioadenosine phosphorylase (MTAP) TTDBX7N UP Q13126 TTDBX7N UC MTAP_HUMAN TTDBX7N BC Glycosyltransferases TTDBX7N SN Methylthioadenosine phosphorylase; MTAPase; MTA phosphorylase; MSAP; 5'-methylthioadenosine phosphorylase TTDBX7N GN MTAP TTDBX7N FC Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. TTDBX7N EC EC 2.4.2.28 TTDBX7N PD 6DZ3; 6DZ2; 6DZ0; 6DYZ; 5TC8 TTDBX7N SQ MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH TTDBX7N TT Literature-reported TTDBX7N FM Pentosyltransferase TTDBX7N KE hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways TTLSRBZ ID TTLSRBZ TTLSRBZ TN Sorbitoldehydrogenase (SORD) TTLSRBZ UP Q00796 TTLSRBZ UC DHSO_HUMAN TTLSRBZ BC Short-chain dehydrogenases reductase TTLSRBZ SN SORD; SDH; L-iditol2-dehydrogenase TTLSRBZ GN SORD TTLSRBZ FC Convertssorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm. TTLSRBZ EC EC 1.1.1.- TTLSRBZ PD 1PL8; 1PL7; 1PL6 TTLSRBZ SQ MAAAAKPNNLSLVVHGPGDLRLENYPIPEPGPNEVLLRMHSVGICGSDVHYWEYGRIGNFIVKKPMVLGHEASGTVEKVGSSVKHLKPGDRVAIEPGAPRENDEFCKMGRYNLSPSIFFCATPPDDGNLCRFYKHNAAFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGHKVLVCGAGPIGMVTLLVAKAMGAAQVVVTDLSATRLSKAKEIGADLVLQISKESPQEIARKVEGQLGCKPEVTIECTGAEASIQAGIYATRSGGNLVLVGLGSEMTTVPLLHAAIREVDIKGVFRYCNTWPVAISMLASKSVNVKPLVTHRFPLEKALEAFETFKKGLGLKIMLKCDPSDQNP TTLSRBZ TT Literature-reported TTLSRBZ KE hsa00040:Pentose and glucuronate interconversions; hsa00051:Fructose and mannose metabolism; hsa01100:Metabolic pathways TTMFYEC ID TTMFYEC TTMFYEC TN Streptococcus Cytidylate kinase (Stre-coc cmk) TTMFYEC UP Q97PK6 TTMFYEC UC KCY_STRPN TTMFYEC BC Kinase TTMFYEC SN cmk; TIGR4; MssA protein; Cytidine monophosphate kinase; CMP kinase TTMFYEC GN Stre-coc cmk TTMFYEC FC Atp, datp, and gtp are equally effective as phosphate donors. Cmp and dcmp are the best phosphate acceptors. TTMFYEC EC EC 2.7.4.25 TTMFYEC PD 1Q3T TTMFYEC SQ MKTIQIAIDGPASSGKSTVAKIIAKDFGFTYLDTGAMYRAATYMALKNQLGVEEVEALLALLDQHPISFGRSETGDQLVFVGDVDITHPIRENEVTNHVSAIAAIPQVREKLVSLQQEIAQQGGIVMDGRDIGTVVLPQAELKIFLVASVDERAERRYKENIAKGIETDLETLKKEIAARDYKDSHRETSPLKQAEDAVYLDTTGLNIQEVVEKIKAEAEKRM TTMFYEC TT Literature-reported TTMFYEC KE spn00240:Pyrimidine metabolism; spn01100:Metabolic pathways TTJQT60 ID TTJQT60 TTJQT60 TN TGF-beta-activated kinase 1 (MAP3K7) TTJQT60 UP O43318 TTJQT60 UC M3K7_HUMAN TTJQT60 BC Kinase TTJQT60 SN Transforming growth factor-beta-activated kinase 1; TAK1; Mitogen-activated protein kinase kinase kinase 7 TTJQT60 GN MAP3K7 TTJQT60 FC Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-induced apoptosis. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity. Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. TTJQT60 EC EC 2.7.11.25 TTJQT60 PD 5V5N; 5JK3; 5JH6; 5JGD; 5JGB TTJQT60 SQ MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIAATTAYSKPKRGHRKTASFGNILDVPEIVISGNGQPRRRSIQDLTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPTRSHPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS TTJQT60 TT Literature-reported TTJQT60 FM Kinase TTJQT60 RC R-HSA-1169091:Activation of NF-kappaB in B cells; R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-4086398:Ca2+ pathway; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-446652:Interleukin-1 signaling; R-HSA-450302:activated TAK1 mediates p38 MAPK activation; R-HSA-450321:JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-937072:TRAF6 mediated induction of TAK1 complex TTEXRQD ID TTEXRQD TTEXRQD TN Thymine-DNA glycosylase (TDG) TTEXRQD UP Q13569 TTEXRQD UC TDG_HUMAN TTEXRQD BC Uracil-DNA glycosylase (UDG) superfamily. TDG/mug family TTEXRQD SN hTDG TTEXRQD GN TDG TTEXRQD FC DNA glycosylase that plays a key role in active DNA demethylation: specifically recognizes and binds 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) in the context of CpG sites and mediates their excision through base-excision repair (BER) to install an unmethylated cytosine. Cannot remove 5-hydroxymethylcytosine (5hmC). According to an alternative model, involved in DNA demethylation by mediating DNA glycolase activity toward 5-hydroxymethyluracil (5hmU) produced by deamination of 5hmC. Also involved in DNA repair by acting as a thymine-DNA glycosylase that mediates correction of G/T mispairs to G/C pairs: in the DNA of higher eukaryotes, hydrolytic deamination of 5-methylcytosine to thymine leads to the formation of G/T mismatches. Its role in the repair of canonical base damage is however minor compared to its role in DNA demethylation. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine. TTEXRQD EC EC 3.2.2.29 TTEXRQD PD 5T2W; 5JXY; 5HF7; 5FF8; 5CYS TTEXRQD SQ MEAENAGSYSLQQAQAFYTFPFQQLMAEAPNMAVVNEQQMPEEVPAPAPAQEPVQEAPKGRKRKPRTTEPKQPVEPKKPVESKKSGKSAKSKEKQEKITDTFKVKRKVDRFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIERNMDVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYGENPCSSEPCGFSSNGLIESVELRGESAFSGIPNGQWMTQSFTDQIPSFSNHCGTQEQEEESHA TTEXRQD TT Literature-reported TTEXRQD KE hsa03410:Base excision repair TT5T3P6 ID TT5T3P6 TT5T3P6 TN Tissue kallikrein (KLK1) TT5T3P6 UP P06870 TT5T3P6 UC KLK1_HUMAN TT5T3P6 BC Peptidase TT5T3P6 SN Kidney/pancreas/salivary gland kallikrein; Kallikrein1; Kallikrein-1 TT5T3P6 GN KLK1 TT5T3P6 FC Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. TT5T3P6 EC EC 3.4.21.35 TT5T3P6 PD 1SPJ TT5T3P6 SQ MWFLVLCLALSLGGTGAAPPIQSRIVGGWECEQHSQPWQAALYHFSTFQCGGILVHRQWVLTAAHCISDNYQLWLGRHNLFDDENTAQFVHVSESFPHPGFNMSLLENHTRQADEDYSHDLMLLRLTEPADTITDAVKVVELPTEEPEVGSTCLASGWGSIEPENFSFPDDLQCVDLKILPNDECKKAHVQKVTDFMLCVGHLEGGKDTCVGDSGGPLMCDGVLQGVTSWGYVPCGTPNKPSVAVRVLSYVKWIEDTIAENS TT5T3P6 TT Literature-reported TT5T3P6 KE hsa04961:Endocrine and other factor-regulated calcium reabsorption TT5T3P6 RC R-HSA-381426:Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) TT04R7I ID TT04R7I TT04R7I TN Transketolase (TK) TT04R7I UP P29401 TT04R7I UC TKT_HUMAN TT04R7I BC Transketolase TT04R7I SN TKT1; SDDHD; HEL107; HEL-S-48 TT04R7I GN TKT TT04R7I FC Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. TT04R7I EC EC 2.2.1.1 TT04R7I PD 4KXY; 4KXX; 4KXW; 4KXV; 4KXU TT04R7I SQ MESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIANIRMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLITKA TT04R7I TT Literature-reported TT04R7I FM Transferases of aldehyde or ketone residues TT04R7I KE hsa00030:Pentose phosphate pathway; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa01230:Biosynthesis of amino acids TTHQ79V ID TTHQ79V TTHQ79V TN Trypanosoma Pyrophosphate-dependent phosphofructokinase (Trypano pfk) TTHQ79V UP O15648 TTHQ79V UC PFKA_TRYBB TTHQ79V BC Kinase TTHQ79V SN Pyrophosphate-dependent 6-phosphofructose-1-kinase; Pyrophosphate--fructose 6-phosphate 1-phosphotransferase alpha subunit; PPi-PFK; PFP-ALPHA; PFP; 6-phosphofructokinase, pyrophosphate dependent TTHQ79V GN Trypano pfk TTHQ79V FC Regulatory subunit of pyrophosphate--fructose 6- phosphate 1-phosphotransferase. TTHQ79V EC EC 2.7.1.11 TTHQ79V PD 3F5M; 3CVL; 2HIG TTHQ79V SQ MAVESRSRVTSKLVKAHRAMLNSVTQEDLKVDRLPGADYPNPSKKYSSRTEFRDKTDYIMYNPRPRDEPSSENPVSVSPLLCELAAARSRIHFNPTETTIGIVTCGGICPGLNDVIRSITLTGINVYNVKRVIGFRFGYWGLSKKGSQTAIELHRGRVTNIHHYGGTILGSSRGPQDPKEMVDTLERLGVNILFTVGGDGTQRGALVISQEAKRRGVDISVFGVPKTIDNDLSFSHRTFGFQTAVEKAVQAIRAAYAEAVSANYGVGVVKLMGRDSGFIAAQAAVASAQANICLVPENPISEQEVMSLLERRFCHSRSCVIIVAEGFGQDWGRGSGGYDASGNKKLIDIGVILTEKVKAFLKANKSRYPDSTVKYIDPSYMIRACPPSANDALFCATLATLAVHEAMAGATGCIIAMRHNNYILVPIKVATSVRRVLDLRGQLWRQVREITVDLGSDVRLARKLEIRRELEAINRNRDRLHEELAKL TTHQ79V TT Literature-reported TTXEZJ4 ID TTXEZJ4 TTXEZJ4 TN Tyrosine-protein kinase EIF2AK2 (p68) TTXEZJ4 UP P19525 TTXEZJ4 UC E2AK2_HUMAN TTXEZJ4 BC Kinase TTXEZJ4 SN p68 kinase; Proteinkinase RNA-activated; Interferon-inducible RNA-dependent protein kinase p68; Interferon-induced, double-stranded RNA-activated protein kinase p68 TTXEZJ4 GN EIF2AK2 TTXEZJ4 FC Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1). Inhibits viral replication via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (EIF2S1), this phosphorylation impairs the recycling of EIF2S1 between successive rounds of initiation leading to inhibition of translation which eventually results in shutdown of cellular and viral protein synthesis. Also phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes. Can trigger apoptosis via FADD-mediated activation of CASP8. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin. IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. TTXEZJ4 EC EC 2.7.11.1 TTXEZJ4 PD 3UIU; 2A1A; 2A19; 1QU6 TTXEZJ4 SQ MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKKAVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAKRSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC TTXEZJ4 TT Patented-recorded TTXEZJ4 FM Kinase TTXEZJ4 RC R-HSA-1169408:ISG15 antiviral mechanism TTUMHT8 ID TTUMHT8 TTUMHT8 TN Tyrosine-protein kinase ZAP-70 (ZAP-70) TTUMHT8 UP P43403 TTUMHT8 UC ZAP70_HUMAN TTUMHT8 BC Kinase TTUMHT8 SN Syk-related tyrosine kinase; SRK; 70 kDa zeta-chain associated protein TTUMHT8 GN ZAP70 TTUMHT8 FC Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD247/CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. ZAP70 is also required for TCR-CD247/CD3Z internalization and degradation through interaction with the E3 ubiquitin-protein ligase CBL and adapter proteins SLA and SLA2. Thus, ZAP70 regulates both T-cell activation switch on and switch off by modulating TCR expression at the T-cell surface. During thymocyte development, ZAP70 promotes survival and cell-cycle progression of developing thymocytes before positive selection (when cells are still CD4/CD8 double negative). Additionally, ZAP70-dependent signaling pathway may also contribute to primary B-cells formation and activation through B-cell receptor (BCR). Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. TTUMHT8 EC EC 2.7.10.2 TTUMHT8 PD 5O76; 4XZ1; 4XZ0; 4K2R; 4A4C TTUMHT8 SQ MPDPAAHLPFFYGSISRAEAEEHLKLAGMADGLFLLRQCLRSLGGYVLSLVHDVRFHHFPIERQLNGTYAIAGGKAHCGPAELCEFYSRDPDGLPCNLRKPCNRPSGLEPQPGVFDCLRDAMVRDYVRQTWKLEGEALEQAIISQAPQVEKLIATTAHERMPWYHSSLTREEAERKLYSGAQTDGKFLLRPRKEQGTYALSLIYGKTVYHYLISQDKAGKYCIPEGTKFDTLWQLVEYLKLKADGLIYCLKEACPNSSASNASGAAAPTLPAHPSTLTHPQRRIDTLNSDGYTPEPARITSPDKPRPMPMDTSVYESPYSDPEELKDKKLFLKRDNLLIADIELGCGNFGSVRQGVYRMRKKQIDVAIKVLKQGTEKADTEEMMREAQIMHQLDNPYIVRLIGVCQAEALMLVMEMAGGGPLHKFLVGKREEIPVSNVAELLHQVSMGMKYLEEKNFVHRDLAARNVLLVNRHYAKISDFGLSKALGADDSYYTARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEALSYGQKPYKKMKGPEVMAFIEQGKRMECPPECPPELYALMSDCWIYKWEDRPDFLTVEQRMRACYYSLASKVEGPPGSTQKAEAACA TTUMHT8 TT Patented-recorded TTUMHT8 FM Kinase TTUMHT8 KE hsa04014:Ras signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa05340:Primary immunodeficiency TTUMHT8 RC R-HSA-202430:Translocation of ZAP-70 to Immunological synapse; R-HSA-202433:Generation of second messenger molecules TT5IH09 ID TT5IH09 TT5IH09 TN Ubiquitin carboxyl-terminal hydrolase 10 (USP10) TT5IH09 UP Q14694 TT5IH09 UC UBP10_HUMAN TT5IH09 SN Deubiquitinating enzyme 10; Ubiquitin thioesterase 10; Ubiquitin-specific-processing protease 10 TT5IH09 GN USP10 TT5IH09 FC Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. Deubiquitinates TBX21 leading to its stabilization. TT5IH09 EC EC 3.4.19.12 TT5IH09 SQ MALHSPQYIFGDFSPDEFNQFFVTPRSSVELPPYSGTVLCGTQAVDKLPDGQEYQRIEFGVDEVIEPSDTLPRTPSYSISSTLNPQAPEFILGCTASKITPDGITKEASYGSIDCQYPGSALALDGSSNVEAEVLENDGVSGGLGQRERKKKKKRPPGYYSYLKDGGDDSISTEALVNGHANSAVPNSVSAEDAEFMGDMPPSVTPRTCNSPQNSTDSVSDIVPDSPFPGALGSDTRTAGQPEGGPGADFGQSCFPAEAGRDTLSRTAGAQPCVGTDTTENLGVANGQILESSGEGTATNGVELHTTESIDLDPTKPESASPPADGTGSASGTLPVSQPKSWASLFHDSKPSSSSPVAYVETKYSPPAISPLVSEKQVEVKEGLVPVSEDPVAIKIAELLENVTLIHKPVSLQPRGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPVPPKPRQALGDKIVRDIRPGAAFEPTYIYRLLTVNKSSLSEKGRQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEKLTISNGPKNHSVNEEEQEEQGEGSEDEWEQVGPRNKTSVTRQADFVQTPITGIFGGHIRSVVYQQSSKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQGYTTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELLSPGVKNKNFKCHRTYRLFAVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVKPTAERTAYLLYYRRVDLL TT5IH09 TT Preclinical TTVJIO2 ID TTVJIO2 TTVJIO2 TN Ubiquitin carboxyl-terminal hydrolase 13 (USP13) TTVJIO2 UP Q92995 TTVJIO2 UC UBP13_HUMAN TTVJIO2 SN Deubiquitinating enzyme 13; Isopeptidase T-3; ISOT-3; Ubiquitin thioesterase 13; Ubiquitin-specific-processing protease 13 TTVJIO2 GN USP13 TTVJIO2 FC Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data. TTVJIO2 EC EC 3.4.19.12 TTVJIO2 SQ MQRRGALFGMPGGSGGRKMAAGDIGELLVPHMPTIRVPRSGDRVYKNECAFSYDSPNSEGGLYVCMNTFLAFGREHVERHFRKTGQSVYMHLKRHVREKVRGASGGALPKRRNSKIFLDLDTDDDLNSDDYEYEDEAKLVIFPDHYEIALPNIEELPALVTIACDAVLSSKSPYRKQDPDTWENELPVSKYANNLTQLDNGVRIPPSGWKCARCDLRENLWLNLTDGSVLCGKWFFDSSGGNGHALEHYRDMGYPLAVKLGTITPDGADVYSFQEEEPVLDPHLAKHLAHFGIDMLHMHGTENGLQDNDIKLRVSEWEVIQESGTKLKPMYGPGYTGLKNLGNSCYLSSVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKSELIEQVMKEEHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENPSDVFRFLVEERIQCCQTRKVRYTERVDYLMQLPVAMEAATNKDELIAYELTRREAEANRRPLPELVRAKIPFSACLQAFSEPENVDDFWSSALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPKKFDVSIDMPDLLDINHLRARGLQPGEEELPDISPPIVIPDDSKDRLMNQLIDPSDIDESSVMQLAEMGFPLEACRKAVYFTGNMGAEVAFNWIIVHMEEPDFAEPLTMPGYGGAASAGASVFGASGLDNQPPEEIVAIITSMGFQRNQAIQALRATNNNLERALDWIFSHPEFEEDSDFVIEMENNANANIISEAKPEGPRVKDGSGTYELFAFISHMGTSTMSGHYICHIKKEGRWVIYNDHKVCASERPPKDLGYMYFYRRIPS TTVJIO2 TT Preclinical TT07QDI ID TT07QDI TT07QDI TN Ubiquitin carboxyl-terminal hydrolase 20 (USP20) TT07QDI UP Q9Y2K6 TT07QDI UC UBP20_HUMAN TT07QDI SN Deubiquitinating enzyme 20; Ubiquitin thioesterase 20; Ubiquitin-specific-processing protease 20; VHL-interacting deubiquitinating enzyme 2; hVDU2 TT07QDI GN USP20 TT07QDI FC Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. TT07QDI EC EC 3.4.19.12 TT07QDI SQ MGDSRDLCPHLDSIGEVTKEDLLLKSKGTCQSCGVTGPNLWACLQVACPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRLWCYACEKEVFLEQRLAAPLLGSSSKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATVALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSQAETELLIPDEAGRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMAALDDQPAEAQPPSPRSSSPCRTPEPDNDAHLRSSSRPCSPVHHHEGHAKLSSSPPRASPVRMAPSYVLKKAQVLSAGSRRRKEQRYRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGACGDSYAAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFYRKSSEEAMRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAVNHLYVCSICQVEIEALAKRRRIEIDTFIKLNKAFQAEESPGVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHVQLKQGADYGQISEETWTYLNSLYGGGPEIAIRQSVAQPLGPENLHGEQKIEAETRAV TT07QDI TT Preclinical TTQ9EDI ID TTQ9EDI TTQ9EDI TN Ubiquitin carboxyl-terminal hydrolase 30 (USP30) TTQ9EDI UP Q70CQ3 TTQ9EDI UC UBP30_HUMAN TTQ9EDI SN Deubiquitinating enzyme 30; Ubiquitin thioesterase 30; Ubiquitin-specific-processing protease 30; Ub-specific protease 30 TTQ9EDI GN USP30 TTQ9EDI FC Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy. Preferentially cleaves 'Lys-6'- and 'Lys-11'-linked polyubiquitin chains, 2 types of linkage that participate in mitophagic signaling. Does not cleave efficiently polyubiquitin phosphorylated at 'Ser-65'. Acts as negative regulator of mitochondrial fusion by mediating deubiquitination of MFN1 and MFN2 (By similarity). TTQ9EDI EC EC 3.4.19.12 TTQ9EDI SQ MLSSRAEAAMTAADRAIQRFLRTGAAVRYKVMKNWGVIGGIAAALAAGIYVIWGPITERKKRRKGLVPGLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRQPRVTHLFDVHSLEQQSEITPKQITCRTRGSPHPTSNHWKSQHPFHGRLTSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKGTLNGEKVEHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYKYHLLGHKPSQHNPKLNKNPGPTLELQDGPGAPTPVLNQPGAPKTQIFMNGACSPSLLPTLSAPMPFPLPVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPSARNPLSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYERVLSRMQHQSQECKSEE TTQ9EDI TT Preclinical TTX9IFP ID TTX9IFP TTX9IFP TN Ubiquitin thioesterase L1 (UCHL1) TTX9IFP UP P09936 TTX9IFP UC UCHL1_HUMAN TTX9IFP BC Peptidase TTX9IFP SN Ubiquitin thiolesterase L1; Ubiquitin carboxyl-terminal hydrolase isozyme L1; Ubiquitin carboxy-terminal hydrolase L1; UCH-L1; PGP9.5; PGP 9.5; Neuron cytoplasmic protein 9.5 TTX9IFP GN UCHL1 TTX9IFP FC Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity. TTX9IFP EC EC 3.4.19.12 TTX9IFP PD 4JKJ; 4DM9; 3KW5; 3KVF; 3IRT TTX9IFP SQ MQLKPMEINPEMLNKVLSRLGVAGQWRFVDVLGLEEESLGSVPAPACALLLLFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVANNQDKLGFEDGSVLKQFLSETEKMSPEDRAKCFEKNEAIQAAHDAVAQEGQCRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDTLLKDAAKVCREFTEREQGEVRFSAVALCKAA TTX9IFP TT Preclinical TTX9IFP FM Peptidase TTO69J7 ID TTO69J7 TTO69J7 TN UDP-glucuronosyltransferase 2B7 (UGT2B7) TTO69J7 UP P16662 TTO69J7 UC UD2B7_HUMAN TTO69J7 BC Hexosyltransferase TTO69J7 SN ugt3; Uridine diphosphate glucuronosyltransferase; UDPGT TTO69J7 GN ugt3 TTO69J7 FC UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. TTO69J7 EC EC 2.4.1.17 TTO69J7 PD 2O6L TTO69J7 SQ MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSASILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFGDITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTFEKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVLGRPTTLSETMGKADVWLIRNSWNFQFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSGENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGNKPDTLGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFADQPDNIAHMKARGAAVRVDFNTMSSTDLLNALKRVINDPSYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVIGFLLVCVATVIFIVTKCCLFCFWKFARKAKKGKND TTO69J7 TT Literature-reported TTBWMKT ID TTBWMKT TTBWMKT TN WWP1 messenger RNA (WWP1 mRNA) TTBWMKT UP Q9H0M0 TTBWMKT UC WWP1_HUMAN TTBWMKT BC mRNA target TTBWMKT SN WW domain-containing protein 1 (mRNA); Tiul1 (mRNA); TGIF-interacting ubiquitin ligase 1 (mRNA); NEDD4-like E3 ubiquitin-protein ligase WWP1 (mRNA); HECT-type E3 ubiquitin transferase WWP1 (mRNA); Atrophin-1-interacting protein 5 (mRNA); AIP5 (mRNA) TTBWMKT GN WWP1 TTBWMKT FC Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1; the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF. E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. TTBWMKT EC EC 2.3.2.26 TTBWMKT PD 5HPT; 5HPS; 2OP7; 1ND7 TTBWMKT SQ MATASPRSDTSNNHSGRLQLQVTVSSAKLKRKKNWFGTAIYTEVVVDGEITKTAKSSSSSNPKWDEQLTVNVTPQTTLEFQVWSHRTLKADALLGKATIDLKQALLIHNRKLERVKEQLKLSLENKNGIAQTGELTVVLDGLVIEQENITNCSSSPTIEIQENGDALHENGEPSARTTARLAVEGTNGIDNHVPTSTLVQNSCCSYVVNGDNTPSSPSQVAARPKNTPAPKPLASEPADDTVNGESSSFAPTDNASVTGTPVVSEENALSPNCTSTTVEDPPVQEILTSSENNECIPSTSAELESEARSILEPDTSNSRSSSAFEAAKSRQPDGCMDPVRQQSGNANTETLPSGWEQRKDPHGRTYYVDHNTRTTTWERPQPLPPGWERRVDDRRRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQFNQRYLYSASMLAAENDPYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGLQNEEPLPEGWEIRYTREGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERGFRWKLAHFRYLCQSNALPSHVKINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRHYTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVGKDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFGQE TTBWMKT TT Literature-reported TTBWMKT FM mRNA target TTBWMKT KE hsa04120:Ubiquitin mediated proteolysis; hsa04144:Endocytosis TTBWMKT RC R-HSA-2672351:Stimuli-sensing channels; R-HSA-983168:Antigen processing: Ubiquitination & Proteasome degradation TT6TU05 ID TT6TU05 TT6TU05 TN WWP2 messenger RNA (WWP2 mRNA) TT6TU05 UP O00308 TT6TU05 UC WWP2_HUMAN TT6TU05 BC mRNA target TT6TU05 SN WW domaincontaining protein 2 (mRNA); WW domain-containing protein 2 (mRNA); NEDD4like E3 ubiquitinprotein ligaseWWP2 (mRNA); HECT-type E3 ubiquitin transferase WWP2 (mRNA); Atrophin1interacting protein 2 (mRNA); Atrophin-1-interacting protein 2 (mRNA); AIP2 (mRNA) TT6TU05 GN WWP2 TT6TU05 FC Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; in embryonic stem cells (ESCs) the ubiquitination is proposed to regulate POU5F1 protein level. Ubiquitinates EGR2 and promotes it to proteasomal degradation; in T-cells the ubiquitination inhibits activation-induced cell death. Ubiquitinates SLC11A2; the ubiquitination is enhanced by presence of NDFIP1 and NDFIP2. Ubiquitinates RPB1 and promotes it to proteasomal degradation. E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. TT6TU05 EC EC 2.3.2.26 TT6TU05 PD 5TJQ; 5TJ8; 5TJ7; 4Y07 TT6TU05 SQ MASASSSRAGVALPFEKSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLRNELLGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRELPNGRVYYVDHNTKTTTWERPLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQWQSQRNQLQGAMQHFSQRFLYQSSSASTDHDPLGPLPPGWEKRQDNGRVYYVNHNTRTTQWEDPRTQGMIQEPALPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNALPSHVKISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRHYTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVGKETWLPRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFGQE TT6TU05 TT Literature-reported TT6TU05 FM mRNA target TT6TU05 KE hsa04120:Ubiquitin mediated proteolysis TTWON83 ID TTWON83 TTWON83 TN 3-hydroxyanthranilate oxygenase (HAAO) TTWON83 UP P46952 TTWON83 UC 3HAO_HUMAN TTWON83 SN h3HAO; HAD; 3-hydroxyanthranilic acid dioxygenase; 3-hydroxyanthranilate 3,4-dioxygenase; 3-HAO TTWON83 GN HAAO TTWON83 FC Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate. TTWON83 EC EC 1.13.11.6 TTWON83 PD 5TKQ; 5TK5; 2QNK TTWON83 SQ MERRLGVRAWVKENRGSFQPPVCNKLMHQEQLKVMFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKPIPDQLLKEPPFPLSTRSIMEPMSLDAWLDSHHRELQAGTPLSLFGDTYETQVIAYGQGSSEGLRQNVDVWLWQLEGSSVVTMGGRRLSLAPDDSLLVLAGTSYAWERTQGSVALSVTQDPACKKPLG TTWON83 TT Literature-reported TTJB1O0 ID TTJB1O0 TTJB1O0 TN Acidic mammalian chitinase (CHIA) TTJB1O0 UP Q9BZP6 TTJB1O0 UC CHIA_HUMAN TTJB1O0 BC Glycosylase TTJB1O0 SN Lung-specific protein TSA1902; CHIA; AMCase TTJB1O0 GN CHIA TTJB1O0 FC Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding. . TTJB1O0 EC EC 3.2.1.14 TTJB1O0 PD 3RME; 3RM9; 3RM8; 3RM4; 3FY1 TTJB1O0 SQ MTKLILLTGLVLILNLQLGSAYQLTCYFTNWAQYRPGLGRFMPDNIDPCLCTHLIYAFAGRQNNEITTIEWNDVTLYQAFNGLKNKNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFITSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA TTJB1O0 TT Literature-reported TTQICM2 ID TTQICM2 TTQICM2 TN ADAM metallopeptidase 33 (ADAM33) TTQICM2 UP Q9BZ11 TTQICM2 UC ADA33_HUMAN TTQICM2 BC Peptidase TTQICM2 SN UNQ873/PRO1891; Disintegrin and metalloproteinase domain-containing protein 33; C20orf153; ADAM 33 TTQICM2 GN ADAM33 TTQICM2 FC Membrane-anchored protein structurally related to snake venom disintegrins. Invovled in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. TTQICM2 EC EC 3.4.24.- TTQICM2 PD 1R55; 1R54 TTQICM2 SQ MGWRPRRARGTPLLLLLLLLLLWPVPGAGVLQGHIPGQPVTPHWVLDGQPWRTVSLEEPVSKPDMGLVALEAEGQELLLELEKNHRLLAPGYIETHYGPDGQPVVLAPNHTDHCHYQGRVRGFPDSWVVLCTCSGMSGLITLSRNASYYLRPWPPRGSKDFSTHEIFRMEQLLTWKGTCGHRDPGNKAGMTSLPGGPQSRGRREARRTRKYLELYIVADHTLFLTRHRNLNHTKQRLLEVANYVDQLLRTLDIQVALTGLEVWTERDRSRVTQDANATLWAFLQWRRGLWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGCCVEAAAESGGCVMAAATGHPFPRVFSACSRRQLRAFFRKGGGACLSNAPDPGLPVPPALCGNGFVEAGEECDCGPGQECRDLCCFAHNCSLRPGAQCAHGDCCVRCLLKPAGALCRQAMGDCDLPEFCTGTSSHCPPDVYLLDGSPCARGSGYCWDGACPTLEQQCQQLWGPGSHPAPEACFQVVNSAGDAHGNCGQDSEGHFLPCAGRDALCGKLQCQGGKPSLLAPHMVPVDSTVHLDGQEVTCRGALALPSAQLDLLGLGLVEPGTQCGPRMVCQSRRCRKNAFQELQRCLTACHSHGVCNSNHNCHCAPGWAPPFCDKPGFGGSMDSGPVQAENHDTFLLAMLLSVLLPLLPGAGLAWCCYRLPGAHLQRCSWGCRRDPACSGPKDGPHRDHPLGGVHPMELGPTATGQPWPLDPENSHEPSSHPEKPLPAVSPDPQADQVQMPRSCLW TTQICM2 TT Patented-recorded TTS2TEI ID TTS2TEI TTS2TEI TN ADAM metallopeptidase with thrombospondin 1 (ADAMTS1) TTS2TEI UP Q9UHI8 TTS2TEI UC ATS1_HUMAN TTS2TEI BC Peptidase TTS2TEI SN METH1; METH-1; KIAA1346; ADAMTS-1; ADAM-TS1; ADAM-TS 1 TTS2TEI GN ADAMTS1 TTS2TEI FC Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture. Cleaves aggrecan, a cartilage proteoglycan, at the '1938-Glu-|-Leu-1939' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover. TTS2TEI EC EC 3.4.24.- TTS2TEI PD 3Q2H; 3Q2G; 2V4B; 2JIH TTS2TEI SQ MQRAVPEGFGRRKLGSDMGNAERAPGSRSFGPVPTLLLLAAALLAVSDALGRPSEEDEELVVPELERAPGHGTTRLRLHAFDQQLDLELRPDSSFLAPGFTLQNVGRKSGSETPLPETDLAHCFYSGTVNGDPSSAAALSLCEGVRGAFYLLGEAYFIQPLPAASERLATAAPGEKPPAPLQFHLLRRNRQGDVGGTCGVVDDEPRPTGKAETEDEDEGTEGEDEGAQWSPQDPALQGVGQPTGTGSIRKKRFVSSHRYVETMLVADQSMAEFHGSGLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIHDEQKGPEVTSNAALTLRNFCNWQKQHNPPSDRDAEHYDTAILFTRQDLCGSQTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKQCASLNGVNQDSHMMASMLSNLDHSQPWSPCSAYMITSFLDNGHGECLMDKPQNPIQLPGDLPGTSYDANRQCQFTFGEDSKHCPDAASTCSTLWCTGTSGGVLVCQTKHFPWADGTSCGEGKWCINGKCVNKTDRKHFDTPFHGSWGMWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNLEDCPDNNGKTFREEQCEAHNEFSKASFGSGPAVEWIPKYAGVSPKDRCKLICQAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKISGSVTSAKPGYHDIITIPTGATNIEVKQRNQRGSRNNGSFLAIKAADGTYILNGDYTLSTLEQDIMYKGVVLRYSGSSAALERIRSFSPLKEPLTIQVLTVGNALRPKIKYTYFVKKKKESFNAIPTFSAWVIEEWGECSKSCELGWQRRLVECRDINGQPASECAKEVKPASTRPCADHPCPQWQLGEWSSCSKTCGKGYKKRSLKCLSHDGGVLSHESCDPLKKPKHFIDFCTMAECS TTS2TEI TT Literature-reported TTBQ9IM ID TTBQ9IM TTBQ9IM TN Adenylate cyclase type 2 (ADCY2) TTBQ9IM UP Q08462 TTBQ9IM UC ADCY2_HUMAN TTBQ9IM BC Phosphorus-oxygen lyase TTBQ9IM SN ADCY2 TTBQ9IM GN ADCY2 TTBQ9IM FC This is a membrane-bound, calmodulin-insensitive adenylyl cyclase. TTBQ9IM EC EC 4.6.1.1 TTBQ9IM SQ MWQEAMRRRRYLRDRSEEAAGGGDGLPRSRDWLYESYYCMSQQHPLIVFLLLIVMGSCLALLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRLFSLVIWICLVAMGYLFMCFGGTVSPWDQVSFFLFIIFVVYTMLPFNMRDAIIASVLTSSSHTIVLSVCLSATPGGKEHLVWQILANVIIFICGNLAGAYHKHLMELALQQTYQDTCNCIKSRIKLEFEKRQQERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKMGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGAYKVEEGDGDIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPRHTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTLRTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKVLEKEYRATALPAFKYYVTCACLIFFCIFIVQILVLPKTSVLGISFGAAFLLLAFILFVCFAGQLLQCSKKASPLLMWLLKSSGIIANRPWPRISLTIITTAIILMMAVFNMFFLSDSEETIPPTANTTNTSFSASNNQVAILRAQNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHTHAHVLGDYSQVLFERPGIWKDLKTMGSVSLSIFFITLLVLGRQNEYYCRLDFLWKNKFKKEREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAVPSQEHSQEPERQYMHIGTMVEFAFALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLVLQTLGYTCTCRGIINVKGKGDLKTYFVNTEMSRSLSQSNVAS TTBQ9IM TT Literature-reported TTBQ9IM KE hsa00230:Purine metabolism; hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04114:Oocyte meiosis; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04540:Gap junction; hsa04611:Platelet activation; hsa04713:Circadian entrainment; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04727:GABAergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels; hsa04911:Insulin secretion; hsa04912:GnRH signaling pathway; hsa04913:Ovarian steroidogenesis; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04918:Thyroid hormone synthesis; hsa04921:Oxytocin signaling pathway; hsa04922:Glucagon signaling pathway; hsa04923:Regulation of lipolysis in adipocytes; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04976:Bile secretion; hsa05032:Morphine addiction; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05414:Dilated cardiomyopathy TTBQ9IM RC R-HSA-163359:Glucagon signaling in metabolic regulation; R-HSA-163615:PKA activation; R-HSA-164378:PKA activation in glucagon signalling; R-HSA-418555:G alpha (s) signalling events; R-HSA-418594:G alpha (i) signalling events; R-HSA-418597:G alpha (z) signalling events; R-HSA-432040:Vasopressin regulates renal water homeostasis via Aquaporins; R-HSA-5610787:Hedgehog 'off' state TT60XFL ID TT60XFL TT60XFL TN Adipocyte-derived leucine aminopeptidase (ERAP1) TT60XFL UP Q9NZ08 TT60XFL UC ERAP1_HUMAN TT60XFL BC Peptidase TT60XFL SN Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator; Puromycin-insensitive leucyl-specific aminopeptidase; PILS-AP; ERAP1; Aminopeptidase PILS; ARTS-1; ALAP; A-LAP TT60XFL GN ERAP1 TT60XFL FC Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulationof blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney. TT60XFL EC EC 3.4.11.- TT60XFL PD 6Q4R; 5J5E; 3RJO; 3QNF; 3MDJ TT60XFL SQ MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDGVKGMDGFCSRSQHSSSSSHWHQEGVDVKTMMNTWTLQKGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERM TT60XFL TT Literature-reported TTOQGR3 ID TTOQGR3 TTOQGR3 TN AKT1 messenger RNA (AKT1 mRNA) TTOQGR3 UP P31749 TTOQGR3 UC AKT1_HUMAN TTOQGR3 BC mRNA target TTOQGR3 SN RAC-PK-alpha (mRNA); RAC (mRNA); Proto-oncogene c-Akt (mRNA); Protein kinase B alpha (mRNA); Protein kinase B (mRNA); PKB alpha (mRNA); PKB (mRNA) TTOQGR3 GN AKT1 TTOQGR3 FC AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53. TTOQGR3 EC EC 2.7.11.1 TTOQGR3 PD 6NPZ; 6HHJ; 6HHI; 6HHH; 6HHG TTOQGR3 SQ MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA TTOQGR3 TT Literature-reported TTOQGR3 FM mRNA target TTWUHQ1 ID TTWUHQ1 TTWUHQ1 TN Alpha-tubulin N-acetyltransferase 1 (ATAT1) TTWUHQ1 UP Q5SQI0 TTWUHQ1 UC ATAT_HUMAN TTWUHQ1 BC Acetyltransferase ATAT1 family TTWUHQ1 SN MEC17; C6orf134; Alpha-TAT; Acetyltransferase mec-17 homolog TTWUHQ1 GN ATAT1 TTWUHQ1 FC Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. Required for normal sperm flagellar function. Promotes directional cell locomotion and chemotaxis, through AP2A2-dependent acetylation of alpha-tubulin at clathrin-coated pits that are concentrated at the leading edge of migrating cells. May facilitate primary cilium assembly. TTWUHQ1 EC EC 2.3.1.108 TTWUHQ1 PD 4U9Z; 4U9Y; 4PK3; 4PK2; 4IF5 TTWUHQ1 SQ MEFPFDVDALFPERITVLDQHLRPPARRPGTTTPARVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARPAGKGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPERGPLRPFVPEQELLRSLRLCPPHPTARLLLAADPGGSPAQRRRTRGTPPGLVAQSCCYSRHGGVNSSSPNTGNQDSKQGEQETKNRSASEEQALSQDGSGEKPMHTAPPQAPAPPAQSWTVGGDILNARFIRNLQERRSTRPW TTWUHQ1 TT Literature-reported TT5S8DR ID TT5S8DR TT5S8DR TN APOA1 messenger RNA (APOA1 mRNA) TT5S8DR UP P02647 TT5S8DR UC APOA1_HUMAN TT5S8DR BC mRNA target TT5S8DR SN Truncated apolipoprotein AI (mRNA); Apolipoprotein A1 (mRNA); Apolipoprotein A-I (mRNA); ApoAI (mRNA); ApoA-I (mRNA); Apo-AI (mRNA) TT5S8DR GN APOA1 TT5S8DR FC As part of the SPAP complex, activates spermatozoa motility. Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). TT5S8DR PD 6CM1; 6CLZ; 6CCX; 6CCH; 6CC9 TT5S8DR SQ MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ TT5S8DR TT Literature-reported TT5S8DR FM mRNA target TT5S8DR KE hsa03320:PPAR signaling pathway; hsa04975:Fat digestion and absorption; hsa04977:Vitamin digestion and absorption; hsa05143:African trypanosomiasis TT5S8DR RC R-HSA-114608:Platelet degranulation; R-HSA-1369062:ABC transporters in lipid homeostasis; R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-194223:HDL-mediated lipid transport; R-HSA-1989781:PPARA activates gene expression; R-HSA-2168880:Scavenging of heme from plasma; R-HSA-3000471:Scavenging by Class B Receptors; R-HSA-3000480:Scavenging by Class A Receptors; R-HSA-975634:Retinoid metabolism and transport; R-HSA-977225:Amyloid formation TT8OY02 ID TT8OY02 TT8OY02 TN ARA70 messenger RNA (NCOA4 mRNA) TT8OY02 UP Q13772 TT8OY02 UC NCOA4_HUMAN TT8OY02 BC mRNA target TT8OY02 SN Ret-activating protein ELE1 (mRNA); RFG (mRNA); Nuclear receptor coactivator 4 (mRNA); NCoA-4 (mRNA); ELE1 (mRNA); Androgen receptor-associated protein of 70 kDa (mRNA); Androgen receptor coactivator 70 kDa protein (mRNA); ARA70 (mRNA); ARA70 (dARA70N) (mRNA); 70 kDa androgen receptor coactivator (mRNA); 70 kDa AR-activator (mRNA) TT8OY02 GN NCOA4 TT8OY02 FC Ligand-independent coactivator of the peroxisome proliferator-activated receptor (PPAR) gamma. Enhances the androgen receptor transcriptional activity in prostate cancer cells. TT8OY02 PD 1T5Z TT8OY02 SQ MNTFQDQSGSSSNREPLLRCSDARRDLELAIGGVLRAEQQIKDNLREVKAQIHSCISRHLECLRSREVWLYEQVDLIYQLKEETLQQQAQQLYSLLGQFNCLTHQLECTQNKDLANQVSVCLERLGSLTLKPEDSTVLLFEADTITLRQTITTFGSLKTIQIPEHLMAHASSANIGPFLEKRGCISMPEQKSASGIVAVPFSEWLLGSKPASGYQAPYIPSTDPQDWLTQKQTLENSQTSSRACNFFNNVGGNLKGLENWLLKSEKSSYQKCNSHSTTSSFSIEMEKVGDQELPDQDEMDLSDWLVTPQESHKLRKPENGSRETSEKFKLLFQSYNVNDWLVKTDSCTNCQGNQPKGVEIENLGNLKCLNDHLEAKKPLSTPSMVTEDWLVQNHQDPCKVEEVCRANEPCTSFAECVCDENCEKEALYKWLLKKEGKDKNGMPVEPKPEPEKHKDSLNMWLCPRKEVIEQTKAPKAMTPSRIADSFQVIKNSPLSEWLIRPPYKEGSPKEVPGTEDRAGKQKFKSPMNTSWCSFNTADWVLPGKKMGNLSQLSSGEDKWLLRKKAQEVLLNSPLQEEHNFPPDHYGLPAVCDLFACMQLKVDKEKWLYRTPLQM TT8OY02 TT Literature-reported TT8OY02 FM mRNA target TT8OY02 KE hsa05200:Pathways in cancer; hsa05216:Thyroid cancer TT1K6Q4 ID TT1K6Q4 TT1K6Q4 TN Arylamine N-acetyltransferase (NAT) TT1K6Q4 UP P18440; P11245 TT1K6Q4 UC ARY1_HUMAN; ARY2_HUMAN TT1K6Q4 BC Acyltransferase TT1K6Q4 SN NAT; N-acetyltransferase; Arylamide acetylase; AAC TT1K6Q4 GN NAT1; NAT2 TT1K6Q4 FC Could have a role in acetylating, and hence inactivating, the antitubercular drug isoniazid. TT1K6Q4 SQ MDIEAYLERIGYKKSRNKLDLETLTDILQHQIRAVPFENLNIHCGDAMDLGLEAIFDQVVRRNRGGWCLQVNHLLYWALTTIGFETTMLGGYVYSTPAKKYSTGMIHLLLQVTIDGRNYIVDAGFGRSYQMWQPLELISGKDQPQVPCVFRLTEENGFWYLDQIRREQYIPNEEFLHSDLLEDSKYRKIYSFTLKPRTIEDFESMNTYLQTSPSSVFTSKSFCSLQTPDGVHCLVGFTLTHRRFNYKDNTDLIEFKTLSEEEIEKVLKNIFNISLQRKLVPKHGDRFFTI TT1K6Q4 TT Literature-reported TT2KHP7 ID TT2KHP7 TT2KHP7 TN Aspartate beta-hydroxylase (ASPH) TT2KHP7 UP Q12797 TT2KHP7 UC ASPH_HUMAN TT2KHP7 BC Paired donor oxygen oxidoreductase TT2KHP7 SN Peptideaspartate betadioxygenase; Aspartyl/asparaginyl betahydroxylase; ASPH; ASP betahydroxylase TT2KHP7 GN ASPH TT2KHP7 FC Isoform 8: membrane-bound Ca(2+)-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells. {ECO:0000269|PubMed:22586105}. TT2KHP7 EC EC 1.14.11.16 TT2KHP7 PD 6RK9; 5JZU; 5JZA; 5JZ8; 5JZ6 TT2KHP7 SQ MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARRETKHGGHKNGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHVEGEDLQQEDGPTGEPQQEDDEFLMATDVDDRFETLEPEVSHEETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQEVPPETNRKTDDPEQKAKVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI TT2KHP7 TT Literature-reported TT2YT1K ID TT2YT1K TT2YT1K TN Aspartate carbamoyltransferase (CAD) TT2YT1K UP P27708 TT2YT1K UC PYR1_HUMAN TT2YT1K BC Carbon-nitrogen ligase TT2YT1K SN CAD TT2YT1K GN CAD TT2YT1K FC This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase). TT2YT1K PD 6HG1; 6HFU; 6HFS; 6HFR; 6HFQ TT2YT1K SQ MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEATAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF TT2YT1K TT Literature-reported TT2YT1K KE hsa00240:Pyrimidine metabolism; hsa00250:Alanine, aspartate and glutamate metabolism; hsa01100:Metabolic pathways TT2YT1K RC R-HSA-500753:Pyrimidine biosynthesis TT9A0HI ID TT9A0HI TT9A0HI TN ATPase family AAA domain containing 2 (ATAD2) TT9A0HI UP Q6PL18 TT9A0HI UC ATAD2_HUMAN TT9A0HI BC Acid anhydride hydrolase TT9A0HI SN PRO2000; L16; ATPase family AAA domain-containing protein 2; ANCCA; AAA nuclear coregulator cancer-associated protein TT9A0HI GN ATAD2 TT9A0HI FC May play a role in the recruitment or occupancy of CREBBP at some ESR1 target gene promoters. May be required for histone hyperacetylation. Involved in the estrogen-induced cell proliferation and cell cycle progression of breast cancer cells. May be a transcriptional coactivator of the nuclear receptor ESR1 required to induce the expression of a subset of estradiol target genes, such as CCND1, MYC and E2F1. TT9A0HI EC EC 3.6.1.3 TT9A0HI PD 6HIE; 6HID; 6HIC; 6HIB; 6HIA TT9A0HI SQ MVVLRSSLELHNHSAASATGSLDLSSDFLSLEHIGRRRLRSAGAAQKKPAATTAKAGDGSSVKEVETYHRTRALRSLRKDAQNSSDSSFEKNVEITEQLANGRHFTRQLARQQADKKKEEHREDKVIPVTRSLRARNIVQSTEHLHEDNGDVEVRRSCRIRSRYSGVNQSMLFDKLITNTAEAVLQKMDDMKKMRRQRMRELEDLGVFNETEESNLNMYTRGKQKDIQRTDEETTDNQEGSVESSEEGEDQEHEDDGEDEDDEDDDDDDDDDDDDDDEDDEDEEDGEEENQKRYYLRQRKATVYYQAPLEKPRHQRKPNIFYSGPASPARPRYRLSSAGPRSPYCKRMNRRRHAIHSSDSTSSSSSEDEQHFERRRKRSRNRAINRCLPLNFRKDELKGIYKDRMKIGASLADVDPMQLDSSVRFDSVGGLSNHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSQGDKRVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPSIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKEARKEILKIHTRDWNPKPLDTFLEELAENCVGYCGADIKSICAEAALCALRRRYPQIYTTSEKLQLDLSSINISAKDFEVAMQKMIPASQRAVTSPGQALSTVVKPLLQNTVDKILEALQRVFPHAEFRTNKTLDSDISCPLLESDLAYSDDDVPSVYENGLSQKSSHKAKDNFNFLHLNRNACYQPMSFRPRILIVGEPGFGQGSHLAPAVIHALEKFTVYTLDIPVLFGVSTTSPEETCAQVIREAKRTAPSIVYVPHIHVWWEIVGPTLKATFTTLLQNIPSFAPVLLLATSDKPHSALPEEVQELFIRDYGEIFNVQLPDKEERTKFFEDLILKQAAKPPISKKKAVLQALEVLPVAPPPEPRSLTAEEVKRLEEQEEDTFRELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLRDIDLICSNALEYNPDRDPGDRLIRHRACALRDTAYAIIKEELDEDFEQLCEEIQESRKKRGCSSSKYAPSYYHVMPKQNSTLVGDKRSDPEQNEKLKTPSTPVACSTPAQLKRKIRKKSNWYLGTIKKRRKISQAKDDSQNAIDHKIESDTEETQDTSVDHNETGNTGESSVEENEKQQNASESKLELRNNSNTCNIENELEDSRKTTACTELRDKIACNGDASSSQIIHISDENEGKEMCVLRMTRARRSQVEQQQLITVEKALAILSQPTPSLVVDHERLKNLLKTVVKKSQNYNIFQLENLYAVISQCIYRHRKDHDKTSLIQKMEQEVENFSCSR TT9A0HI TT Literature-reported TTUXCAF ID TTUXCAF TTUXCAF TN ATP-binding cassette transporter B11 (ABCB11) TTUXCAF UP O95342 TTUXCAF UC ABCBB_HUMAN TTUXCAF BC ABC transporter TTUXCAF SN BSEP; ATP-binding cassette, sub-family B, member 11; ATP-binding cassette sub-family B member 11 TTUXCAF GN ABCB11 TTUXCAF FC Involved in the ATP-dependent secretion of bile salts into the canaliculus of hepatocytes. TTUXCAF SQ MSDSVILRSIKKFGEENDGFESDKSYNNDKKSRLQDEKKGDGVRVGFFQLFRFSSSTDIWLMFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVELQELQIPGKACVNNTIVWTNSSLNQNMTNGTRCGLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDEGEYTPGTLVQIFLSVIVGALNLGNASPCLEAFATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIKGEIEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQALNEEDIKDATEDDMLARTFSRGSYQDSLRASIRQRSKSQLSYLVHEPPLAVVDHKSTYEEDRKDKDIPVQEEVEPAPVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPISVYNTAGEKWDNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTGSPIS TTUXCAF TT Literature-reported TTUXCAF FM ABC transporter TTUXCAF KE hsa02010:ABC transporters; hsa04976:Bile secretion TTUXCAF RC R-HSA-159418:Recycling of bile acids and salts TTM1VPZ ID TTM1VPZ TTM1VPZ TN ATP-dependent protease Lon (LONP1) TTM1VPZ UP P36776 TTM1VPZ UC LONM_HUMAN TTM1VPZ BC Peptidase TTM1VPZ SN Serine protease 15; Mitochondrial ATP-dependent protease Lon; Lon protease-like protein; LONP1; LONP; LONHs TTM1VPZ GN LONP1 TTM1VPZ FC ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single- stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site- specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters. Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein. TTM1VPZ EC EC 3.4.21.53 TTM1VPZ PD 2X36 TTM1VPZ SQ MAASTGYVRLWGAARCWVLRRPMLAAAGGRVPTAAGAWLLRGQRTCDASPPWALWGRGPAIGGQWRGFWEASSRGGGAFSGGEDASEGGAEEGAGGAGGSAGAGEGPVITALTPMTIPDVFPHLPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVMGHRRVHISRQLEVEPEEPEAENKHKPRRKSKRGKKEAEDELSARHPAELAMEPTPELPAEVLMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQDKDAKGDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDEQAEALAVER TTM1VPZ TT Literature-reported TT89Z17 ID TT89Z17 TT89Z17 TN B7 translation initiation codon region messenger RNA (CD80 mRNA) TT89Z17 UP P33681 TT89Z17 UC CD80_HUMAN TT89Z17 BC mRNA target TT89Z17 SN T-lymphocyte activation antigen CD80 (mRNA); LAB7 (mRNA); CTLA-4 counter-receptor B7.1 (mRNA); CD28LG1 (mRNA); CD28LG (mRNA); BB1 (mRNA); B7 (mRNA); Activation B7-1 antigen (mRNA) TT89Z17 GN CD80 TT89Z17 FC T-cell proliferation and cytokine production is induced by the binding of CD28, binding to CTLA-4 has opposite effects and inhibits T-cell activation. Involved in the costimulatory signal essential for T-lymphocyte activation. TT89Z17 PD 1I8L; 1DR9 TT89Z17 SQ MGHTRRQGTSPSKCPYLNFFQLLVLAGLSHFCSGVIHVTKEVKEVATLSCGHNVSVEELAQTRIYWQKEKKMVLTMMSGDMNIWPEYKNRTIFDITNNLSIVILALRPSDEGTYECVVLKYEKDAFKREHLAEVTLSVKADFPTPSISDFEIPTSNIRRIICSTSGGFPEPHLSWLENGEELNAINTTVSQDPETELYAVSSKLDFNMTTNHSFMCLIKYGHLRVNQTFNWNTTKQEHFPDNLLPSWAITLISVNGIFVICCLTYCFAPRCRERRRNERLRRESVRPV TT89Z17 TT Literature-reported TT89Z17 FM mRNA target TT89Z17 KE hsa04514:Cell adhesion molecules (CAMs); hsa04620:Toll-like receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa04940:Type I diabetes mellitus; hsa05320:Autoimmune thyroid disease; hsa05322:Systemic lupus erythematosus; hsa05323:Rheumatoid arthritis; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease; hsa05416:Viral myocarditis TT89Z17 RC R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-389356:CD28 co-stimulation; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389359:CD28 dependent Vav1 pathway; R-HSA-389513:CTLA4 inhibitory signaling TTQWGU9 ID TTQWGU9 TTQWGU9 TN Bacterial Aspartate-semialdehyde dehydrogenase (Bact asd2) TTQWGU9 UP P23247 TTQWGU9 UC DHAS2_VIBCH TTQWGU9 BC Aldehyde/oxo donor oxidoreductase TTQWGU9 SN asd2; L-Aspartate-beta-semialdehyde dehydrogenase; ASADH; ASA dehydrogenase TTQWGU9 GN Bact asd2 TTQWGU9 FC Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L- aspartyl-4-phosphate. TTQWGU9 PD 2R00; 2QZ9 TTQWGU9 SQ MSQQFNVAIFGATGAVGETMLEVLQEREFPVDELFLLASERSEGKTYRFNGKTVRVQNVEEFDWSQVHIALFSAGGELSAKWAPIAAEAGVVVIDNTSHFRYDYDIPLVVPEVNPEAIAEFRNRNIIANPNCSTIQMLVALKPIYDAVGIERINVTTYQSVSGAGKAGIDELAGQTAKLLNGYPAETNTFSQQIAFNCIPQIDQFMDNGYTKEEMKMVWETQKIFNDPSIMVNPTCVRVPVFYGHAEAVHVETRAPIDAEQVMDMLEQTDGIELFRGADFPTQVRDAGGKDHVLVGRVRNDISHHSGINLWVVADNVRKGAATNAVQIAELLVRDYF TTQWGU9 TT Literature-reported TTQAOZR ID TTQAOZR TTQAOZR TN Bacterial Chorismate synthase (Bact aroC) TTQAOZR UP P12008 TTQAOZR UC AROC_ECOLI TTQAOZR BC Alpha-carbonic anhydrase TTQAOZR SN aroC; Chorismate synthase; CS; 5enolpyruvylshikimate3phosphate phospholyase; 5-enolpyruvylshikimate-3-phosphate phospholyase TTQAOZR GN Bact aroC TTQAOZR FC Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. It uses NADPH to reduce FMN. TTQAOZR EC EC 4.2.3.5 TTQAOZR SQ MAGNTIGQLFRVTTFGESHGLALGCIVDGVPPGIPLTEADLQHDLDRRRPGTSRYTTQRREPDQVKILSGVFEGVTTGTSIGLLIENTDQRSQDYSAIKDVFRPGHADYTYEQKYGLRDYRGGGRSSARETAMRVAAGAIAKKYLAEKFGIEIRGCLTQMGDIPLDIKDWSQVEQNPFFCPDPDKIDALDELMRALKKEGDSIGAKVTVVASGVPAGLGEPVFDRLDADIAHALMSINAVKGVEIGDGFDVVALRGSQNRDEITKDGFQSNHAGGILGGISSGQQIIAHMALKPTSSITVPGRTINRFGEEVEMITKGRHDPCVGIRAVPIAEAMLAIVLMDHLLRQRAQNADVKTDIPRW TTQAOZR TT Literature-reported TTZP720 ID TTZP720 TTZP720 TN Bacterial Cystathionine beta-lyase (Bact metC) TTZP720 UP P06721 TTZP720 UC METC_ECOLI TTZP720 BC Carbon-sulfur lyases TTZP720 SN Cysteine-S-conjugate beta-lyase MetC; Cysteine lyase MetC; Cysteine desulfhydrase MetC; Cystathionine beta-lyase MetC; CL; CBL; Beta-cystathionase MetC; Bacterial CD TTZP720 GN Bact metC TTZP720 FC Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis. Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine. In addition, under certain growth conditions, exhibits significant alanine racemase coactivity. TTZP720 EC EC 4.4.1.13 TTZP720 PD 4ITX; 4ITG; 2GQN; 2FQ6; 1CL2 TTZP720 SQ MADKKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGELFYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDHVLMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFLESPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFGIDVSIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAYITSRGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFWKRDFTGSSGLFSFVLKKKLNNEELANYLDNFSLFSMAYSWGGYESLILANQPEHIAAIRPQGEIDFSGTLIRLHIGLEDVDDLIADLDAGFARIV TTZP720 TT Literature-reported TTDU0HP ID TTDU0HP TTDU0HP TN Bacterial Cystathionine gamma-synthase (Bact metB) TTDU0HP UP P00935 TTDU0HP UC METB_ECOLI TTDU0HP BC Alkyl aryl transferase TTDU0HP SN metB; O-succinylhomoserine (Thiol)-lyase; CGS TTDU0HP GN Bact metB TTDU0HP FC Catalyzes the formation of L-cystathionine from O- succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma- replacement reaction. In the absence of thiol, catalyzes gamma- elimination to form 2-oxobutanoate, succinate and ammonia. TTDU0HP EC EC 2.5.1.48 TTDU0HP PD 1CS1 TTDU0HP SQ MTRKQATIAVRSGLNDDEQYGCVVPPIHLSSTYNFTGFNEPRAHDYSRRGNPTRDVVQRALAELEGGAGAVLTNTGMSAIHLVTTVFLKPGDLLVAPHDCYGGSYRLFDSLAKRGCYRVLFVDQGDEQALRAALAEKPKLVLVESPSNPLLRVVDIAKICHLAREVGAVSVVDNTFLSPALQNPLALGADLVLHSCTKYLNGHSDVVAGVVIAKDPDVVTELAWWANNIGVTGGAFDSYLLLRGLRTLVPRMELAQRNAQAIVKYLQTQPLVKKLYHPSLPENQGHEIAARQQKGFGAMLSFELDGDEQTLRRFLGGLSLFTLAESLGGVESLISHAATMTHAGMAPEARAAAGISETLLRISTGIEDGEDLIADLENGFRAANKG TTDU0HP TT Literature-reported TTTKXDL ID TTTKXDL TTTKXDL TN Bacterial Dihydroxy-2-butanone-4-phosphate synthase (Bact ribB) TTTKXDL UP P0A7J0 TTTKXDL UC RIBB_ECOLI TTTKXDL BC DHBP synthase family TTTKXDL SN RibB; DHBP synthase TTTKXDL GN Bact ribB TTTKXDL FC Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. TTTKXDL EC EC 4.1.99.12 TTTKXDL PD 1IEZ; 1G58; 1G57 TTTKXDL SQ MNQTLLSSFGTPFERVENALAALREGRGVMVLDDEDRENEGDMIFPAETMTVEQMALTIRHGSGIVCLCITEDRRKQLDLPMMVENNTSAYGTGFTVTIEAAEGVTTGVSAADRITTVRAAIADGAKPSDLNRPGHVFPLRAQAGGVLTRGGHTEATIDLMTLAGFKPAGVLCELTNDDGTMARAPECIEFANKHNMALVTIEDLVAYRQAHERKAS TTTKXDL TT Literature-reported TTW6MYZ ID TTW6MYZ TTW6MYZ TN Bacterial DNA-directed RNA polymerase beta' (Bact rpoC) TTW6MYZ UP Q2G0N5 TTW6MYZ UC RPOC_STAA8 TTW6MYZ BC Nucleotidyltransferase TTW6MYZ SN rpoC; Transcriptase subunit beta'; RNAP subunit beta'; RNA polymerasesubunit beta'; DNAdirected RNA polymerase subunit beta' TTW6MYZ GN Bact rpoC TTW6MYZ FC DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. TTW6MYZ EC EC 2.7.7.6 TTW6MYZ SQ MIDVNNFHYMKIGLASPEKIRSWSFGEVKKPETINYRTLKPEKDGLFCERIFGPTKDWECSCGKYKRVRYKGMVCDRCGVEVTKSKVRRERMGHIELAAPVSHIWYFKGIPSRMGLLLDMSPRALEEVIYFASYVVVDPGPTGLEKKTLLSEAEFRDYYDKYPGQFVAKMGAEGIKDLLEEIDLDEELKLLRDELESATGQRLTRAIKRLEVVESFRNSGNKPSWMILDVLPIIPPEIRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLLDLGAPGIIVQNEKRMLQEAVDALIDNGRRGRPVTGPGNRPLKSLSHMLKGKQGRFRQNLLGKRVDYSGRSVIAVGPSLKMYQCGLPKEMALELFKPFVMKELVQREIATNIKNAKSKIERMDDEVWDVLEEVIREHPVLLNRAPTLHRLGIQAFEPTLVEGRAIRLHPLVTTAYNADFDGDQMAVHVPLSKEAQAEARMLMLAAQNILNPKDGKPVVTPSQDMVLGNYYLTLERKDAVNTGAIFNNTNEVLKAYANGFVHLHTRIGVHASSFNNPTFTEEQNKKILATSVGKIIFNEIIPDSFAYINEPTQENLERKTPNRYFIDPTTLGEGGLKEYFENEELIEPFNKKFLGNIIAEVFNRFSITDTSMMLDRMKDLGFKFSSKAGITVGVADIVVLPDKQQILDEHEKLVDRITKQFNRGLITEEERYNAVVEIWTDAKDQIQGELMQSLDKTNPIFMMSDSGARGNASNFTQLAGMRGLMAAPSGKIIELPITSSFREGLTVLEYFISTHGARKGLADTALKTADSGYLTRRLVDVAQDVIVREEDCGTDRGLLVSDIKEGTEMIEPFIERIEGRYSKETIRHPETDEIIIRPDELITPEIAKKITDAGIEQMYIRSAFTCNARHGVCEKCYGKNLATGEKVEVGEAVGTIAAQSIGEPGTQLTMRTFHTGGVAGSDITQGLPRIQEIFEARNPKGQAVITEIEGVVEDIKLAKDRQQEIVVKGANETRSYLASGTSRIIVEIGQPVQRGEVLTEGSIEPKNYLSVAGLNATESYLLKEVQKVYRMQGVEIDDKHVEVMVRQMLRKVRIIEAGDTKLLPGSLVDIHNFTDANREAFKHRKRPATAKPVLLGITKASLETESFLSAASFQETTRVLTDAAIKGKRDDLLGLKENVIIGKLIPAGTGMRRYSDVKYEKTAKPVAEVESQTEVTE TTW6MYZ TT Literature-reported TTVL6MZ ID TTVL6MZ TTVL6MZ TN Bacterial Elongation factor Tu (Bact EFTu) TTVL6MZ UP P0CE47 TTVL6MZ UC EFTU1_ECOLI TTVL6MZ BC GTP-binding elongation factor family TTVL6MZ SN tufA; P43; Elongation factor Tu 1; EFTu 1 TTVL6MZ GN Bact EFTu TTVL6MZ FC May play an important regulatory rolein cell growth and in the bacterial response to nutrient deprivation. TTVL6MZ PD 5UYQ; 5UYP; 5UYN; 5UYM; 5UYL TTVL6MZ SQ MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG TTVL6MZ TT Literature-reported TTC21TJ ID TTC21TJ TTC21TJ TN Bacterial Endoribonuclease YbeY (Bact YbeY) TTC21TJ UP P0A898 TTC21TJ UC YBEY_ECOLI TTC21TJ BC Carboxylic ester hydrolase TTC21TJ SN ybeY; b0659; JW0656 TTC21TJ GN Bact YbeY TTC21TJ FC Acts together with the RNase R to eliminate defective 70S ribosomes, but not properly matured 70S ribosomes or individual subunits, by a process mediated specifically by the 30S ribosomal subunit. Involved in the processing of 16S, 23S and 5S rRNAs, with a particularly strong effect on maturation at both the 5'-and 3'-ends of 16S rRNA as well as maturation of the 5'-end of 23S and 5S rRNAs. Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. TTC21TJ EC EC 3.1.-.- TTC21TJ PD 1XM5 TTC21TJ SQ MSQVILDLQLACEDNSGLPEESQFQTWLNAVIPQFQEESEVTIRVVDTAESHSLNLTYRGKDKPTNVLSFPFEVPPGMEMSLLGDLVICRQVVEKEAQEQGKPLEAHWAHMVVHGSLHLLGYDHIEDDEAEEMEALETEIMLALGYEDPYIAEKE TTC21TJ TT Literature-reported TTNAW8S ID TTNAW8S TTNAW8S TN Bacterial Flavohemoglobin (Bact hmp) TTNAW8S UP P24232 TTNAW8S UC HMP_ECOLI TTNAW8S BC Paired donor oxygen oxidoreductase TTNAW8S SN Nitric oxide dioxygenase; NOD; NO oxygenase; Hemoglobin-like protein; HMP; Ferrisiderophore reductase B; Dihydropteridine reductase TTNAW8S GN Bact hmp TTNAW8S FC Various electron acceptors arealso reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if these reactions are of any biological significance in vivo. TTNAW8S EC EC 1.14.12.17 TTNAW8S PD 1GVH TTNAW8S SQ MLDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKIAQKHTSFQIKPEQYNIVGEHLLATLDEMFSPGQEVLDAWGKAYGVLANVFINREAEIYNENASKAGGWEGTRDFRIVAKTPRSALITSFELEPVDGGAVAEYRPGQYLGVWLKPEGFPHQEIRQYSLTRKPDGKGYRIAVKREEGGQVSNWLHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSLPRFTAHTWYRQPSEADRAKGQFDSEGLMDLSKLEGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECFGPHKVL TTNAW8S TT Literature-reported TTJMGDT ID TTJMGDT TTJMGDT TN Bacterial Lysyl-tRNA synthetase (Bact lysS) TTJMGDT UP P0A8N3 TTJMGDT UC SYK1_ECOLI TTJMGDT BC Carbon-oxygen ligase TTJMGDT SN Lysyl-tRNA synthetase; Lysine--tRNA ligase; LysRS TTJMGDT GN Bact lysS TTJMGDT FC Catalyses the formation of lysyl-transfer RNA, Lys-tRNA(Lys), which then is ready to insert lysine into proteins. TTJMGDT EC EC 6.1.1.6 TTJMGDT PD 1KRT; 1KRS; 1BBW; 1BBU TTJMGDT SQ MSEQHAQGADAVVDLNNELKTRREKLANLREQGIAFPNDFRRDHTSDQLHAEFDGKENEELEALNIEVAVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDDLPEGVYNEQFKKWDLGDILGAKGKLFKTKTGELSIHCTELRLLTKALRPLPDKFHGLQDQEARYRQRYLDLISNDESRNTFKVRSQILSGIRQFMVNRGFMEVETPMMQVIPGGAAARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQDILGKTEVTYGDVTLDFGKPFEKLTMREAIKKYRPETDMADLDNFDSAKAIAESIGIHVEKSWGLGRIVTEIFEEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAQRFLDQVAAKDAGDDEAMFYDEDYVTALEHGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFPAMRPVK TTJMGDT TT Literature-reported TT1NFO3 ID TT1NFO3 TT1NFO3 TN Bacterial Nicotinate-nucleotide adenylyltransferase (Bact nadD) TT1NFO3 UP P0A752 TT1NFO3 UC NADD_ECOLI TT1NFO3 BC Kinase TT1NFO3 SN nadD of Escherichia coli (strain K12); Nicotinate mononucleotide adenylyltransferase of Escherichia coli (strain K12); NaMN adenylyltransferase of Escherichia coli (strain K12); Deamido-NAD(+)Nicotinate-nucleotide adenylyltransferase pyrophosphorylase of Escherichia coli (strain K12); Deamido-NAD(+) pyrophosphorylase of Escherichia coli (strain K12); Deamido-NAD(+) diphosphorylase of Escherichia coli (strain K12) TT1NFO3 GN Bact nadD TT1NFO3 FC Catalyzes the reversible adenylation of nicotinate mononucleotide (namn) to nicotinic acid adenine dinucleotide (naad). TT1NFO3 EC EC 2.7.7.18 TT1NFO3 PD 1K4M; 1K4K TT1NFO3 SQ MKSLQALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQPEANSVQRKHMLELAIADKPLFTLDERELKRNAPSYTAQTLKEWRQEQGPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLEMAQPQYQQWLEDHLTHNPEDLHLQPAGKIYLAETPWFNISATIIRERLQNGESCEDLLPEPVLTYINQQGLYR TT1NFO3 TT Patented-recorded TTRFV0W ID TTRFV0W TTRFV0W TN Bacterial Oxoacyl-[acyl-carrier-protein] synthase II (Bact fabF) TTRFV0W UP P0AAI5 TTRFV0W UC FABF_ECOLI TTRFV0W BC Acyltransferase TTRFV0W SN KASB; KAS II; KAS 2; FabF; Condensing enzyme FabF; Beta-ketoacyl-acyl carrier protein synthase B; Beta-ketoacyl-ACP synthase II; Beta-ketoacyl-ACP synthase 2; 3-oxoacyl-[acyl-carrier-protein] synthase 2 TTRFV0W GN Bact fabF TTRFV0W FC Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis. TTRFV0W EC EC 2.3.1.179 TTRFV0W PD 3I8P; 3HO9; 3HO2; 3HNZ; 3G11 TTRFV0W SQ MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI TTRFV0W TT Literature-reported TTSEOPJ ID TTSEOPJ TTSEOPJ TN Bacterial Pantothenate kinase (Bact coaA) TTSEOPJ UP P0A6I3 TTSEOPJ UC COAA_ECOLI TTSEOPJ BC Kinase TTSEOPJ SN Rts protein; Pantothenic acid kinase; Pantothenate kinase TTSEOPJ GN Bact coaA TTSEOPJ FC Phosphorylates pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP). It is the rate-limiting step in the biosynthesis of CoA. TTSEOPJ EC EC 2.7.1.33 TTSEOPJ PD 1SQ5; 1ESN; 1ESM TTSEOPJ SQ MSIKEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK TTSEOPJ TT Literature-reported TTB30PF ID TTB30PF TTB30PF TN Bacterial Phosphoshikimate1-carboxyvinyltransferase (Bact aroA) TTB30PF UP P0A6D3 TTB30PF UC AROA_ECOLI TTB30PF BC Alkyl aryl transferase TTB30PF SN aroA of Escherichia coli; EPSPS of Escherichia coli; EPSP synthase of Escherichia coli; 5-enolpyruvylshikimate-3-phosphate synthase of Escherichia coli TTB30PF GN Bact aroA TTB30PF FC Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3- phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. TTB30PF EC EC 2.5.1.19 TTB30PF PD 3FK1; 3FK0; 3FJZ; 3FJX; 2QFU TTB30PF SQ MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTRCEIIGNGGPLHAEGALELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRLGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARISQAA TTB30PF TT Literature-reported TTM2E7C ID TTM2E7C TTM2E7C TN Bacterial Plasminogen activator (Bact pla) TTM2E7C UP P17811 TTM2E7C UC COLY_YERPE TTM2E7C BC Peptidase TTM2E7C SN pla; Coagulase/fibrinolysin TTM2E7C GN Bact pla TTM2E7C FC Seems to play an essential role in plague transmission by mediating flea blockage in a temperature-dependent fashion. Fibrinolytic activity prevails at 37 degrees Celsius whereas coagulase expression predominates at lower temperatures (<30 degrees Celsius). Activates plasminogen by cleaving it. TTM2E7C EC EC 3.4.23.48 TTM2E7C PD 4DCB; 2X56; 2X55; 2X4M TTM2E7C SQ MKKSSIVATIITILSGSANAASSQLIPNISPDSFTVAASTGMLSGKSHEMLYDAETGRKISQLDWKIKNVAILKGDISWDPYSFLTLNARGWTSLASGSGNMDDYDWMNENQSEWTDHSSHPATNVNHANEYDLNVKGWLLQDENYKAGITAGYQETRFSWTATGGSYSYNNGAYTGNFPKGVRVIGYNQRFSMPYIGLAGQYRINDFELNALFKFSDWVRAHDNDEHYMRDLTFREKTSGSRYYGTVINAGYYVTPNAKVFAEFTYSKYDEGKGGTQTIDKNSGDSVSIGGDAAGISNKNYTVTAGLQYRF TTM2E7C TT Literature-reported TTTZQOV ID TTTZQOV TTTZQOV TN Bacterial Purine nucleoside phosphorylase (Bact xapA) TTTZQOV UP P45563 TTTZQOV UC XAPA_ECOLI TTTZQOV BC Kinase TTTZQOV SN Xanthosine phosphorylase; Purine nucleoside phosphorylase II; Purine nucleoside phosphorylase 2; PNP II; Bact Inosine-guanosine phosphorylase TTTZQOV GN Bact xapA TTTZQOV FC The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. This protein can degrade all purine nucleosides including xanthosine, inosine and guanosine, but cannot cleave adenosine, deoxyadenosine or hypoxanthine arabinoside. Has a preference for the neutral over the monoanionic form of xanthosine. TTTZQOV EC EC 2.4.2.1 TTTZQOV PD 1YR3; 1YQU; 1YQQ TTTZQOV SQ MSQVQFSHNPLFCIDIIKTYKPDFTPRVAFILGSGLGALADQIENAVAISYEKLPGFPVSTVHGHAGELVLGHLQGVPVVCMKGRGHFYEGRGMTIMTDAIRTFKLLGCELLFCTNAAGSLRPEVGAGSLVALKDHINTMPGTPMVGLNDDRFGERFFSLANAYDAEYRALLQKVAKEEGFPLTEGVFVSYPGPNFETAAEIRMMQIIGGDVVGMSVVPEVISARHCDLKVVAVSAITNMAEGLSDVKLSHAQTLAAAELSKQNFINLICGFLRKIA TTTZQOV TT Literature-reported TTOYRQZ ID TTOYRQZ TTOYRQZ TN Bacterial Superoxide dismutase Mn (Bact sodA) TTOYRQZ UP P00448 TTOYRQZ UC SODM_ECOLI TTOYRQZ BC Superoxide acceptor oxidoreductase TTOYRQZ SN sodA; MnSOD; Mn-SOD; Manganese superoxide dismutase TTOYRQZ GN Bact sodA TTOYRQZ FC Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. TTOYRQZ EC EC 1.15.1.1 TTOYRQZ PD 3OT7; 3K9S; 1ZLZ; 1VEW; 1MMM TTOYRQZ SQ MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHANHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGASGFPIMGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK TTOYRQZ TT Literature-reported TT9BH7S ID TT9BH7S TT9BH7S TN Bacterial Threonine deaminase (Bact ilvA) TT9BH7S UP P04968 TT9BH7S UC ILVA_ECOLI TT9BH7S BC Carbon-nitrogen lyases TT9BH7S SN ilvA; Putative threonine dehydratase TT9BH7S GN Bact ilvA TT9BH7S FC Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form(iminobutyrate). Both intermediates are unstable and short- lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. TT9BH7S EC EC 4.3.1.19 TT9BH7S PD 1TDJ TT9BH7S SQ MADSQPLSGAPEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSGANVNFHGLRYVSERCELGEQREALLAVTIPEEKGSFLKFCQLLGGRSVTEFNYRFADAKNACIFVGVRLSRGLEERKEILQMLNDGGYSVVDLSDDEMAKLHVRYMVGGRPSHPLQERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFELGDHEPDFETRLNELGYDCHDETNNPAFRFFLAG TT9BH7S TT Literature-reported TTNS6X4 ID TTNS6X4 TTNS6X4 TN Bacterial Triosephosphate isomerase (Bact TPI) TTNS6X4 UP Q07412 TTNS6X4 UC TPIS_PLAFA TTNS6X4 BC Intramolecular oxidoreductase TTNS6X4 SN Triose-phosphate isomerase; TPI; TIM TTNS6X4 GN Bact TPI TTNS6X4 FC identical protein binding, triose-phosphate isomerase activity. TTNS6X4 EC EC 5.3.1.1 TTNS6X4 PD 5GZP; 5GV4; 5BRB; 5BNK; 5BMX TTNS6X4 SQ MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNVILAYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM TTNS6X4 TT Literature-reported TTNS6X4 FM Intramolecular oxidoreductases TT5VER7 ID TT5VER7 TT5VER7 TN Bacterial Undecaprenyl pyrophosphate synthetase (Bact ispU) TT5VER7 UP P60472 TT5VER7 UC UPPS_ECOLI TT5VER7 BC Alkyl aryl transferase TT5VER7 SN ispU; Undecaprenyl diphosphate synthase; Undecaprenyl diphosphate synthase; UPP synthetase; UPP synthase; UDS; Di-trans-poly-cis-decaprenylcistransferase TT5VER7 GN Bact ispU TT5VER7 FC Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate (FPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. TT5VER7 EC EC 2.5.1.31 TT5VER7 PD 5ZHE; 5CQJ; 5CQB; 4H3C; 4H3A TT5VER7 SQ MMLSATQPLSEKLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANNGIEALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDTSRFNSRLQERIRKSEALTAGNTGLTLNIAANYGGRWDIVQGVRQLAEKVQQGNLQPDQIDEEMLNQHVCMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALNAFANRERRFGGTEPGDETA TT5VER7 TT Literature-reported TT1AL3P ID TT1AL3P TT1AL3P TN Beta-ketoacyl-ACP synthase (OXSM) TT1AL3P UP Q9NWU1 TT1AL3P UC OXSM_HUMAN TT1AL3P BC Acyltransferase TT1AL3P SN 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial TT1AL3P GN OXSM TT1AL3P FC May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function. TT1AL3P EC EC 2.3.1.41 TT1AL3P PD 2IWZ; 2IWY; 2C9H TT1AL3P SQ MSNCLQNFLKITSTRLLCSRLCQQLRSKRKFFGTVPISRLHRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSDEGQFNEQNFVSKSDIKSMSSPTIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSDPKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEKRFIGLTNSFGFGGTNATLCIAGL TT1AL3P TT Literature-reported TT32VXH ID TT32VXH TT32VXH TN BMP-2-inducible protein kinase (BMP2K) TT32VXH UP Q9NSY1 TT32VXH UC BMP2K_HUMAN TT32VXH BC Kinase TT32VXH SN HRIHFB2017; BIKe TT32VXH GN BMP2K TT32VXH FC May be involved in osteoblast differentiation. TT32VXH EC EC 2.7.11.1 TT32VXH PD 5IKW; 5I3R; 5I3O; 4W9X; 4W9W TT32VXH SQ MKKFSRMPKSEGGSGGGAAGGGAGGAGAGAGCGSGGSSVGVRVFAVGRHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDCAVNSISDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGVNVVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQVAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFKFAKKDCPVSNINNSSIPSALPEPMTASEAAARKSQIKARITDTIGPTETSIAPRQRPKANSATTATPSVLTIQSSATPVKVLAPGEFGNHRPKGALRPGNGPEILLGQGPPQQPPQQHRVLQQLQQGDWRLQQLHLQHRHPHQQQQQQQQQQQQQQQQQQQQQQQQQQQHHHHHHHHLLQDAYMQQYQHATQQQQMLQQQFLMHSVYQPQPSASQYPTMMPQYQQAFFQQQMLAQHQPSQQQASPEYLTSPQEFSPALVSYTSSLPAQVGTIMDSSYSANRSVADKEAIANFTNQKNISNPPDMSGWNPFGEDNFSKLTEEELLDREFDLLRSNRLEERASSDKNVDSLSAPHNHPPEDPFGSVPFISHSGSPEKKAEHSSINQENGTANPIKNGKTSPASKDQRTGKKTSVQGQVQKGNDESESDFESDPPSPKSSEEEEQDDEEVLQGEQGDFNDDDTEPENLGHRPLLMDSEDEEEEEKHSSDSDYEQAKAKYSDMSSVYRDRSGSGPTQDLNTILLTSAQLSSDVAVETPKQEFDVFGAVPFFAVRAQQPQQEKNEKNLPQHRFPAAGLEQEEFDVFTKAPFSKKVNVQECHAVGPEAHTIPGYPKSVDVFGSTPFQPFLTSTSKSESNEDLFGLVPFDEITGSQQQKVKQRSLQKLSSRQRRTKQDMSKSNGKRHHGTPTSTKKTLKPTYRTPERARRHKKVGRRDSQSSNEFLTISDSKENISVALTDGKDRGNVLQPEESLLDPFGAKPFHSPDLSWHPPHQGLSDIRADHNTVLPGRPRQNSLHGSFHSADVLKMDDFGAVPFTELVVQSITPHQSQQSQPVELDPFGAAPFPSKQ TT32VXH TT Literature-reported TTY63XT ID TTY63XT TTY63XT TN B-type natriuretic peptide (BNP) TTY63XT UP P16860 TTY63XT UC ANFB_HUMAN TTY63XT BC Natriuretic peptide family TTY63XT SN Natriuretic peptides B; NPPB; Gammabrain natriuretic peptide; BNP32; BNP(529); BNP(132) TTY63XT GN NPPB TTY63XT FC Cardiac hormone which may function as a paracrine antifibrotic factor in the heart. Also plays a key role in cardiovascular homeostasis through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3. TTY63XT PD 3N56; 1YK1 TTY63XT SQ MDPQTAPSRALLLLLFLHLAFLGGRSHPLGSPGSASDLETSGLQEQRNHLQGKLSELQVEQTSLEPLQESPRPTGVWKSREVATEGIRGHRKMVLYTLRAPRSPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH TTY63XT TT Literature-reported TTY63XT KE hsa04022:cGMP-PKG signaling pathway TT78309 ID TT78309 TT78309 TN BUB1 mitotic checkpoint serine/threonine kinase (BUB1) TT78309 UP O43683 TT78309 UC BUB1_HUMAN TT78309 BC Kinase TT78309 SN hBUB1; Mitotic checkpoint serine/threonine-protein kinase BUB1; BUB1L; BUB1A TT78309 GN BUB1 TT78309 FC Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 localization and thereby affects sister chromatid cohesion. Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. TT78309 EC EC 2.7.11.1 TT78309 PD 6F7B; 5DMZ; 4R8Q; 4QPM; 4A1G TT78309 SQ MDTPENVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPENKEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGIQNQAEPREFLQQQYRLFQTRLTETHLPAQARTSEPLHNVQVLNQMITSKSNPGNNMACISKNQGSELSGVISSACDKESNMERRVITISKSEYSVHSSLASKVDVEQVVMYCKEKLIRGESEFSFEELRAQKYNQRRKHEQWVNEDRHYMKRKEANAFEEQLLKQKMDELHKKLHQVVETSHEDLPASQERSEVNPARMGPSVGSQQELRAPCLPVTYQQTPVNMEKNPREAPPVVPPLANAISAALVSPATSQSIAPPVPLKAQTVTDSMFAVASKDAGCVNKSTHEFKPQSGAEIKEGCETHKVANTSSFHTTPNTSLGMVQATPSKVQPSPTVHTKEALGFIMNMFQAPTLPDISDDKDEWQSLDQNEDAFEAQFQKNVRSSGAWGVNKIISSLSSAFHVFEDGNKENYGLPQPKNKPTGARTFGERSVSRLPSKPKEEVPHAEEFLDDSTVWGIRCNKTLAPSPKSPGDFTSAAQLASTPFHKLPVESVHILEDKENVVAKQCTQATLDSCEENMVVPSRDGKFSPIQEKSPKQALSSHMYSASLLRLSQPAAGGVLTCEAELGVEACRLTDTDAAIAEDPPDAIAGLQAEWMQMSSLGTVDAPNFIVGNPWDDKLIFKLLSGLSKPVSSYPNTFEWQCKLPAIKPKTEFQLGSKLVYVHHLLGEGAFAQVYEATQGDLNDAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGSVLVGELYSYGTLLNAINLYKNTPEKVMPQGLVISFAMRMLYMIEQVHDCEIIHGDIKPDNFILGNGFLEQDDEDDLSAGLALIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLPHLDMWNEFFHVMLNIPDCHHLPSLDLLRQKLKKVFQQHYTNKIRALRNRLIVLLLECKRSRK TT78309 TT Patented-recorded TTUI35N ID TTUI35N TTUI35N TN C/EBP beta messenger RNA (CEBPB mRNA) TTUI35N UP P17676 TTUI35N UC CEBPB_HUMAN TTUI35N BC mRNA target TTUI35N SN Transcription factor CCAAT/enhancer-binding protein beta (mRNA); Transcription factor 5 (mRNA); TCF5 (mRNA); TCF-5 (mRNA); PP9092 (mRNA); Nuclear factor NF-IL6 (mRNA); Liver-enriched inhibitory protein (mRNA); Liver activator protein (mRNA); LIP (mRNA); LAP (mRNA); CCAAT/enhancer-binding protein beta (mRNA); C/EBP beta (mRNA) TTUI35N GN CEBPB TTUI35N FC Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant functions with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Plays also a role in intracellular bacteria killing. During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation. Essential for female reproduction because of a critical role in ovarian follicle development. Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation. Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. TTUI35N PD 6MG3; 6MG2; 6MG1; 2.00E+43; 2.00E+42 TTUI35N SQ MQRLVAWDPACLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPAARPGPRPPAGELGSIGDHERAIDFSPYLEPLGAPQAPAPATATDTFEAAPPAPAPAPASSGQHHDFLSDLFSDDYGGKNCKKPAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKAPPTACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASSGHC TTUI35N TT Literature-reported TTUI35N FM mRNA target TTUI35N KE hsa04668:TNF signaling pathway; hsa05152:Tuberculosis; hsa05202:Transcriptional misregulation in cancer TTUI35N RC R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-381340:Transcriptional regulation of white adipocyte differentiation TTV298Y ID TTV298Y TTV298Y TN Calmodulin-dependent kinase II (CAMKK2) TTV298Y UP Q96RR4 TTV298Y UC KKCC2_HUMAN TTV298Y BC Kinase TTV298Y SN KIAA0787; Calcium/calmodulin-dependent protein kinase kinase beta; Calcium/calmodulin-dependent protein kinase kinase 2; CaMKK beta; CaMKK 2; CaM-kinase kinase beta; CaM-kinase kinase 2; CaM-KK beta; CaM-KK 2; CAMKKB TTV298Y GN CAMKK2 TTV298Y FC Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching. TTV298Y EC EC 2.7.11.17 TTV298Y PD 6FEL; 6EWW; 6CMJ; 6BRC; 6BQQ TTV298Y SQ MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQARPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTRECESLSELKEARQRRQPPGHRPAPRGGGGSALVRGSPCVESCWAPAPGSPARMHPLRPEEAMEPE TTV298Y TT Patented-recorded TTGLQWZ ID TTGLQWZ TTGLQWZ TN CaM-kinase IV kinase (CAMKK1) TTGLQWZ UP Q8N5S9 TTGLQWZ UC KKCC1_HUMAN TTGLQWZ BC Kinase TTGLQWZ SN Calcium/calmodulin-dependent protein kinase kinase alpha; Calcium/calmodulin-dependent protein kinase kinase 1; CaMKK alpha; CaMKK 1; CaM-kinase kinase alpha; CaM-kinase kinase 1; CaM-KK alpha; CaM-KK 1; CAMKKA TTGLQWZ GN CAMKK1 TTGLQWZ FC Calcium/calmodulin-dependent protein kinase that belongs to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4. Involved in regulating cell apoptosis. Promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-antagonist of cell death. TTGLQWZ EC EC 2.7.11.17 TTGLQWZ PD 6CD6; 6CCF TTGLQWZ SQ MEGGPAVCCQDPRAELVERVAAIDVTHLEEADGGPEPTRNGVDPPPRARAASVIPGSTSRLLPARPSLSARKLSLQERPAGSYLEAQAGPYATGPASHISPRAWRRPTIESHHVAISDAEDCVQLNQYKLQSEIGKGAYGVVRLAYNESEDRHYAMKVLSKKKLLKQYGFPRRPPPRGSQAAQGGPAKQLLPLERVYQEIAILKKLDHVNVVKLIEVLDDPAEDNLYLVFDLLRKGPVMEVPCDKPFSEEQARLYLRDVILGLEYLHCQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDAQLSSTAGTPAFMAPEAISDSGQSFSGKALDVWATGVTLYCFVYGKCPFIDDFILALHRKIKNEPVVFPEEPEISEELKDLILKMLDKNPETRIGVPDIKLHPWVTKNGEEPLPSEEEHCSVVEVTEEEVKNSVRLIPSWTTVILVKSMLRKRSFGNPFEPQARREERSMSAPGNLLVKEGFGEGGKSPELPGVQEDEAAS TTGLQWZ TT Literature-reported TTW4Y2M ID TTW4Y2M TTW4Y2M TN cAMP protein kinase type II-beta (PRKAR2B) TTW4Y2M UP P31323 TTW4Y2M UC KAP3_HUMAN TTW4Y2M BC Kinase TTW4Y2M SN cAMP-dependent protein kinase type II-beta regulatory subunit; Type RIIbeta regulatory subunit of protein kinase A; RIIbeta subunit of cAMP-dependent protein kinase; PKA RIIbeta-subunit TTW4Y2M GN PRKAR2B TTW4Y2M FC Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase. Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. TTW4Y2M SQ MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGTARFGHEGRTWGDLGAAAGGGTPSKGVNFAEEPMQSDSEDGEEEEAAPADAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEENGAVEIARCSRGQYFGELALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA TTW4Y2M TT Literature-reported TTW4Y2M FM Kinase TTW4Y2M KE hsa04210:Apoptosis; hsa04910:Insulin signaling pathway TTW4Y2M RC R-HSA-163615:PKA activation; R-HSA-164378:PKA activation in glucagon signalling; R-HSA-180024:DARPP-32 events; R-HSA-2565942:Regulation of PLK1 Activity at G2/M Transition; R-HSA-380259:Loss of Nlp from mitotic centrosomes; R-HSA-380270:Recruitment of mitotic centrosome proteins and complexes; R-HSA-380284:Loss of proteins required for interphase microtubule organization?from the centrosome; R-HSA-381676:Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-432040:Vasopressin regulates renal water homeostasis via Aquaporins; R-HSA-5610787:Hedgehog 'off' state; R-HSA-5620912:Anchoring of the basal body to the plasma membrane; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTK3CAQ ID TTK3CAQ TTK3CAQ TN Candida Chitin synthase 1 (Candi CHS1) TTK3CAQ UP P23316 TTK3CAQ UC CHS1_CANAX TTK3CAQ BC Hexosyltransferase TTK3CAQ SN Chitin-UDP acetyl-glucosaminyl transferase 1; CHS1 TTK3CAQ GN Candi CHS1 TTK3CAQ FC Formation and repair of the disk-shaped septumin yeast and the cross walls of the hyphal phase. TTK3CAQ EC EC 2.4.1.16 TTK3CAQ SQ MHNINNGYVPNREKTITKRKVRLVGGKAGNLVLENPVPTELRKVLTRTESPFGEFTNMTYTACTSQPDTFSAEGFTLRAAKYGRETEIVICITMYNEDEVAFARTMHGVMKNIAHLCSRHKSKIWGKDSWKKVQVIIVADGRNKVQQSVLELLTATGCYQENLARPYVNNSKVNAHLFEYTTQISIDENLKFKGDEKNLAPVQVLFCLKESNQKKINSHRWLFNAFCPVLDPNVIVLLDVGTKPDNHAIYNLWKAFDRDSNVAGAAGEIKAMKGKGWINLTNPLVASQNFEYKLSNILDKPLESLFGYISVLPGALSAYRYIALKNHDDGTGPLASYFKGEDLLCSHDKDKENTKANFFEANMYLAEDRILCWELVSKRNDNWVLKFVKSATGETDVPETIAEFLSQRRRWINGAFFAALYSLYHFRKIWTTDHSYARKFWLHVEEFIYQLVSLLFSFFSLSNFYLTFYFLTGSLVSYKSLGKKGGFWIFTLFNYLCIGVLTSLFIVSIGNRPHASKNIFKTLIILLTICALYALVVGFVFVINTIATFGTGGTSTYVLVSIVVSLLSTYGLYTLMSILYLDPWHMLTCSVQYFLMIPSYTCTLQIFAFCNTHDVSWGTKGDNNPKEDLSNQYIIEKNASGEFEAVIVDTNIDEDYLETLYNIRSKRSNKKVALGHSEKTPLDGDDYAKDVRTRVVLFWMIANLVFIMTMVQVYEPGDTGRNIYLAFILWAVAVLALVRAIGSLGYLIQTYARFFVESKSKWMKRGYTAPSHNPLN TTK3CAQ TT Literature-reported TT4UJX5 ID TT4UJX5 TT4UJX5 TN Carboxypeptidase B1 (CPB1) TT4UJX5 UP P15086 TT4UJX5 UC CBPB1_HUMAN TT4UJX5 BC Peptidase TT4UJX5 SN Pancreas-specific protein; PASP; Carboxypeptidase B; CPB TT4UJX5 GN CPB1 TT4UJX5 FC A carboxypeptidase that preferentially acts upon basic amino acids, such as arginine and lysine. Responsible for rapidly metabolizing the C5a protein into C5a des-Arg, with one less amino acid. TT4UJX5 EC EC 3.4.17.2 TT4UJX5 PD 1ZLI; 1KWM TT4UJX5 SQ MLALLVLVTVALASAHHGGEHFEGEKVFRVNVEDENHINIIRELASTTQIDFWKPDSVTQIKPHSTVDFRVKAEDTVTVENVLKQNELQYKVLISNLRNVVEAQFDSRVRATGHSYEKYNKWETIEAWTQQVATENPALISRSVIGTTFEGRAIYLLKVGKAGQNKPAIFMDCGFHAREWISPAFCQWFVREAVRTYGREIQVTELLDKLDFYVLPVLNIDGYIYTWTKSRFWRKTRSTHTGSSCIGTDPNRNFDAGWCEIGASRNPCDETYCGPAAESEKETKALADFIRNKLSSIKAYLTIHSYSQMMIYPYSYAYKLGENNAELNALAKATVKELASLHGTKYTYGPGATTIYPAAGGSDDWAYDQGIRYSFTFELRDTGRYGFLLPESQIRATCEETFLAIKYVASYVLEHLY TT4UJX5 TT Patented-recorded TTVOH2M ID TTVOH2M TTVOH2M TN Carboxypeptidase M (CPM) TTVOH2M UP P14384 TTVOH2M UC CBPM_HUMAN TTVOH2M BC Peptidase TTVOH2M SN Human carboxypeptidase M TTVOH2M GN CPM TTVOH2M FC It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins. Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. TTVOH2M EC EC 3.4.17.12 TTVOH2M PD 1UWY TTVOH2M SQ MDFPCLWLGLLLPLVAALDFNYHRQEGMEAFLKTVAQNYSSVTHLHSIGKSVKGRNLWVLVVGRFPKEHRIGIPEFKYVANMHGDETVGRELLLHLIDYLVTSDGKDPEITNLINSTRIHIMPSMNPDGFEAVKKPDCYYSIGRENYNQYDLNRNFPDAFEYNNVSRQPETVAVMKWLKTETFVLSANLHGGALVASYPFDNGVQATGALYSRSLTPDDDVFQYLAHTYASRNPNMKKGDECKNKMNFPNGVTNGYSWYPLQGGMQDYNYIWAQCFEITLELSCCKYPREEKLPSFWNNNKASLIEYIKQVHLGVKGQVFDQNGNPLPNVIVEVQDRKHICPYRTNKYGEYYLLLLPGSYIINVTVPGHDPHITKVIIPEKSQNFSALKKDILLPFQGQLDSIPVSNPSCPMIPLYRNLPDHSAATKPSLFLFLVSLLHIFFK TTVOH2M TT Literature-reported TTFQEMX ID TTFQEMX TTFQEMX TN Casein kinase I alpha (CSNK1A1) TTFQEMX UP P48729 TTFQEMX UC KC1A_HUMAN TTFQEMX BC Kinase TTFQEMX SN Casein kinase I isoform alpha; CKI-alpha; CK1 TTFQEMX GN CSNK1A1 TTFQEMX FC It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis. May play a role in keratin cytoskeleton disassembly and thereby, it may regulate epithelial cell migration. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. TTFQEMX EC EC 2.7.11.1 TTFQEMX PD 6GZD; 5FQD TTFQEMX SQ MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGKQTDKTKSNMKGF TTFQEMX TT Clinical trial TTH30UI ID TTH30UI TTH30UI TN Casein kinase I delta (CSNK1D) TTH30UI UP P48730 TTH30UI UC KC1D_HUMAN TTH30UI BC Kinase TTH30UI SN Tau-protein kinase CSNK1D; HCKID; Casein kinase I isoform delta; CKId; CKI-delta TTH30UI GN CSNK1D TTH30UI FC It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate. Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. TTH30UI EC EC 2.7.11.1 TTH30UI PD 6GZM; 6F26; 6F1W; 5W4W; 5OKT TTH30UI SQ MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR TTH30UI TT Preclinical TTA8PLI ID TTA8PLI TTA8PLI TN Casein kinase I epsilon (CSNK1E) TTA8PLI UP P49674 TTA8PLI UC KC1E_HUMAN TTA8PLI BC Kinase TTA8PLI SN Casein kinase I isoform epsilon; CKIe; CKI-epsilon TTA8PLI GN CSNK1E TTA8PLI FC Can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates DVL1 and DVL2. Central component of the circadian clock. In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. Inhibits cytokine-induced granuloytic differentiation. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. TTA8PLI EC EC 2.7.11.1 TTA8PLI PD 4HOK; 4HNI TTA8PLI SQ MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGAARNPEDVDRERREHEREERMGQLRGSATRALPPGPPTGATANRLRSAAEPVASTPASRIQPAGNTSPRAISRVDRERKVSMRLHRGAPANVSSSDLTGRQEVSRIPASQTSVPFDHLGK TTA8PLI TT Successful TT0UZJ9 ID TT0UZJ9 TT0UZJ9 TN Casein kinase I gamma-2 (CSNK1G2) TT0UZJ9 UP P78368 TT0UZJ9 UC KC1G2_HUMAN TT0UZJ9 BC Kinase TT0UZJ9 SN Casein kinase I isoform gamma-2; CKI-gamma 2; CK1G2 TT0UZJ9 GN CSNK1G2 TT0UZJ9 FC Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. Involved in brain development and vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. Regulates fast synaptic transmission mediated by glutamate. SMAD3 phosphorylation promotes its ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Hyperphosphorylation of the serine-repeat motif of COL4A3BP/CERT leads to its inactivation by dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis. Triggers PER1 proteasomal degradation probably through phosphorylation. Serine/threonine-protein kinase. TT0UZJ9 EC EC 2.7.11.1 TT0UZJ9 PD 2C47 TT0UZJ9 SQ MDFDKKGGKGETEEGRRMSKAGGGRSSHGIRSSGTSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLSATEGVPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLITRMEYVHTKSLIYRDVKPENFLVGRPGTKRQHAIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEEMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRSGFVFDYEYDWAGKPLPTPIGTVHTDLPSQPQLRDKTQPHSKNQALNSTNGELNADDPTAGHSNAPITAPAEVEVADETKCCCFFKRRKRKSLQRHK TT0UZJ9 TT Literature-reported TTR93NU ID TTR93NU TTR93NU TN Casein kinase II alpha prime (CSNK2A2) TTR93NU UP P19784 TTR93NU UC CSK22_HUMAN TTR93NU BC Kinase TTR93NU SN Casein kinase II subunit alpha'; CK2A2; CK II alpha' TTR93NU GN CSNK2A2 TTR93NU FC Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. TTR93NU EC EC 2.7.11.1 TTR93NU PD 6QY9; 6HMQ; 6HMD; 6HMC; 6HMB TTR93NU SQ MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCADNAVLSSGLTAAR TTR93NU TT Patented-recorded TT6KIOT ID TT6KIOT TT6KIOT TN Caspase-11 (CASP11) TT6KIOT UP P49662 TT6KIOT UC CASP4_HUMAN TT6KIOT BC Peptidase TT6KIOT SN ICH-3 protease; Casp4 of Mus musculus TT6KIOT GN Casp4 TT6KIOT FC Involved in ER-stress induced apoptosis. Cleaves caspase-1. Involved in the activation cascade of caspases responsible for apoptosis execution. Promotes IL-1 beta processing by ICE, so may also have a role in inflammatory responses. TT6KIOT EC EC 3.4.22.57 TT6KIOT SQ MAEGNHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQISPNKKAHPNMEAGPPESGESTDALKLCPHEEFLRLCKERAEEIYPIKERNNRTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFLVLMSHGILEGICGTVHDEKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGANRGELWVRDSPASLEVASSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPRAKAQMPTIERLSMTRYFYLFPGN TT6KIOT TT Literature-reported TTLXC4Q ID TTLXC4Q TTLXC4Q TN Cathepsin E (CTSE) TTLXC4Q UP P14091 TTLXC4Q UC CATE_HUMAN TTLXC4Q BC Peptidase TTLXC4Q SN Cathepsin E TTLXC4Q GN CTSE TTLXC4Q FC May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain. TTLXC4Q EC EC 3.4.23.34 TTLXC4Q PD 1TZS; 1LCG TTLXC4Q SQ MKTLLLLLLVLLELGEAQGSLHRVPLRRHPSLKKKLRARSQLSEFWKSHNLDMIQFTESCSMDQSAKEPLINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSRFQPSQSSTYSQPGQSFSIQYGTGSLSGIIGADQVSVEGLTVVGQQFGESVTEPGQTFVDAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVDLPMFSVYMSSNPEGGAGSELIFGGYDHSHFSGSLNWVPVTKQAYWQIALDNIQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDFVDGMQFCSSGFQGLDIHPPAGPLWILGDVFIRQFYSVFDRGNNRVGLAPAVP TTLXC4Q TT Literature-reported TT1ERKL ID TT1ERKL TT1ERKL TN CD40 messenger RNA (CD40 mRNA) TT1ERKL UP P25942 TT1ERKL UC TNR5_HUMAN TT1ERKL BC mRNA target TT1ERKL SN Tumor necrosis factor receptor superfamily member 5 (mRNA); TNFRSF5 (mRNA); CDw40 (mRNA); CD40L receptor (mRNA); Bp50 (mRNA); B-cell surfaceantigen CD40 (mRNA); B-cell surface antigen CD40 (mRNA) TT1ERKL GN CD40 TT1ERKL FC Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion. Receptor for TNFSF5/CD40LG. TT1ERKL PD 6FAX; 5IHL; 5DMJ; 5DMI; 3QD6 TT1ERKL SQ MVRLPLQCVLWGCLLTAVHPEPPTACREKQYLINSQCCSLCQPGQKLVSDCTEFTETECLPCGESEFLDTWNRETHCHQHKYCDPNLGLRVQQKGTSETDTICTCEEGWHCTSEACESCVLHRSCSPGFGVKQIATGVSDTICEPCPVGFFSNVSSAFEKCHPWTSCETKDLVVQQAGTNKTDVVCGPQDRLRALVVIPIIFGILFAILLVLVFIKKVAKKPTNKAPHPKQEPQEINFPDDLPGSNTAAPVQETLHGCQPVTQEDGKESRISVQERQ TT1ERKL TT Clinical trial TT1ERKL FM mRNA target TT1ERKL KE hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04514:Cell adhesion molecules (CAMs); hsa04620:Toll-like receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05144:Malaria; hsa05145:Toxoplasmosis; hsa05166:HTLV-I infection; hsa05169:Epstein-Barr virus infection; hsa05202:Transcriptional misregulation in cancer; hsa05310:Asthma; hsa05320:Autoimmune thyroid disease; hsa05322:Systemic lupus erythematosus; hsa05330:Allograft rejection; hsa05340:Primary immunodeficiency; hsa05416:Viral myocarditis TT7ORQ6 ID TT7ORQ6 TT7ORQ6 TN CD40LG messenger RNA (CD40LG mRNA) TT7ORQ6 UP P29965 TT7ORQ6 UC CD40L_HUMAN TT7ORQ6 BC mRNA target TT7ORQ6 SN Tumor necrosis factor ligand superfamily member 5 (mRNA); TRAP (mRNA); TNFSF5 (mRNA); TNF-related activation protein (mRNA); T-cell antigen Gp39 (mRNA); T cell antigen Gp39 (mRNA); CD40L (mRNA); CD40-L (mRNA); CD40 ligand (mRNA); CD154 antigen (mRNA); CD154 (mRNA) TT7ORQ6 GN CD40LG TT7ORQ6 FC Costimulates T-cell proliferation and cytokine production. Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation. Induces the activation of NF-kappa-B and kinases MAPK8 and PAK2 in T-cells. Induces tyrosine phosphorylation of isoform 3 of CD28. Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4. Involved in immunoglobulin class switching. Cytokine that binds to CD40/TNFRSF5. TT7ORQ6 PD 6BRB; 3QD6; 3LKJ; 1I9R; 1ALY TT7ORQ6 SQ MIETYNQTSPRSAATGLPISMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLHEDFVFMKTIQRCNTGERSLSLLNCEEIKSQFEGFVKDIMLNKEETKKENSFEMQKGDQNPQIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVNVTDPSQVSHGTGFTSFGLLKL TT7ORQ6 TT Literature-reported TT7ORQ6 FM mRNA target TT53XHB ID TT53XHB TT53XHB TN CD86 messenger RNA (CD86 mRNA) TT53XHB UP P42081 TT53XHB UC CD86_HUMAN TT53XHB BC mRNA target TT53XHB SN T-lymphocyte activation antigen CD86 (mRNA); FUN-1 (mRNA); CTLA-4 counter-receptor B7.2 (mRNA); CD86 (mRNA); CD28LG2 (mRNA); BU63 (mRNA); B70 (mRNA); Activation B7-2 antigen (mRNA) TT53XHB GN CD86 TT53XHB FC May play a critical role in the early events of T-cell activation and costimulation of naive T-cells, such as deciding between immunity and anergy that is made by T-cells within 24 hours after activation. Isoform 2 interferes with the formation of CD86 clusters, and thus acts as a negative regulator of T-cell activation. Receptor involved in the costimulatory signal essential for T-lymphocyte proliferation and interleukin-2 production, by binding CD28 or CTLA-4. TT53XHB PD 5YXK; 1NCN; 1I85 TT53XHB SQ MDPQCTMGLSNILFVMAFLLSGAAPLKIQAYFNETADLPCQFANSQNQSLSELVVFWQDQENLVLNEVYLGKEKFDSVHSKYMGRTSFDSDSWTLRLHNLQIKDKGLYQCIIHHKKPTGMIRIHQMNSELSVLANFSQPEIVPISNITENVYINLTCSSIHGYPEPKKMSVLLRTKNSTIEYDGVMQKSQDNVTELYDVSISLSVSFPDVTSNMTIFCILETDKTRLLSSPFSIELEDPQPPPDHIPWITAVLPTVIICVMVFCLILWKWKKKKRPRNSYKCGTNTMEREESEQTKKREKIHIPERSDEAQRVFKSSKTSSCDKSDTCF TT53XHB TT Literature-reported TT53XHB FM mRNA target TT53XHB KE hsa04514:Cell adhesion molecules (CAMs); hsa04620:Toll-like receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa04940:Type I diabetes mellitus; hsa05202:Transcriptional misregulation in cancer; hsa05320:Autoimmune thyroid disease; hsa05322:Systemic lupus erythematosus; hsa05323:Rheumatoid arthritis; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease; hsa05416:Viral myocarditis TT53XHB RC R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-389356:CD28 co-stimulation; R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-389359:CD28 dependent Vav1 pathway; R-HSA-389513:CTLA4 inhibitory signaling TTQPE1U ID TTQPE1U TTQPE1U TN CDC-like kinase 3 (CLK3) TTQPE1U UP P49761 TTQPE1U UC CLK3_HUMAN TTQPE1U BC Kinase TTQPE1U SN Dual specificity protein kinase CLK3 TTQPE1U GN CLK3 TTQPE1U FC Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. TTQPE1U EC EC 2.7.12.1 TTQPE1U PD 6RCT; 6FYR; 6FYP; 6FT7; 3RAW TTQPE1U SQ MPVLSARRRELADHAGSGRRSGPSPTARSGPHLSALRAQPARAAHLSGRGTYVRRDTAGGGPGQARPLGPPGTSLLGRGARRSGEGWCPGAFESGARAARPPSRVEPRLATAASREGAGLPRAEVAAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPSFGEDYYGPSRSRHRRRSRERGPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFFAGLTPEERSFHTSRNPSR TTQPE1U TT Literature-reported TT1RFQP ID TT1RFQP TT1RFQP TN CDC-like kinase 4 (CLK4) TT1RFQP UP Q9HAZ1 TT1RFQP UC CLK4_HUMAN TT1RFQP BC Kinase TT1RFQP SN Dual specificity protein kinase CLK4 TT1RFQP GN CLK4 TT1RFQP FC Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates SRSF1 and SRSF3. Required for the regulation of alternative splicing of MAPT/TAU. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. TT1RFQP EC EC 2.7.12.1 TT1RFQP PD 6FYV TT1RFQP SQ MRHSKRTHCPDWDSRESWGHESYRGSHKRKRRSHSSTQENRHCKPHHQFKESDCHYLEARSLNERDYRDRRYVDEYRNDYCEGYVPRHYHRDIESGYRIHCSKSSVRSRRSSPKRKRNRHCSSHQSRSKSHRRKRSRSIEDDEEGHLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHGMDGMHVAVKIVKNVGRYREAARSEIQVLEHLNSTDPNSVFRCVQMLEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFQIDHIRQMAYQICQSINFLHHNKLTHTDLKPENILFVKSDYVVKYNSKMKRDERTLKNTDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPIPQHMIQKTRKRKYFHHNQLDWDEHSSAGRYVRRRCKPLKEFMLCHDEEHEKLFDLVRRMLEYDPTQRITLDEALQHPFFDLLKKK TT1RFQP TT Literature-reported TTQWYMD ID TTQWYMD TTQWYMD TN Cell surface antigen MS2 (ADAM8) TTQWYMD UP P78325 TTQWYMD UC ADAM8_HUMAN TTQWYMD BC Peptidase TTQWYMD SN CD156a antigen; CD156; ADAM8; A disintegrin and metalloproteinase domain 8 TTQWYMD GN ADAM8 TTQWYMD FC Possible involvement in extravasation of leukocytes. TTQWYMD EC EC 3.4.24.- TTQWYMD PD 4DD8 TTQWYMD SQ MRGLGLWLLGAMMLPAIAPSRPWALMEQYEVVLPWRLPGPRVRRALPSHLGLHPERVSYVLGATGHNFTLHLRKNRDLLGSGYTETYTAANGSEVTEQPRGQDHCFYQGHVEGYPDSAASLSTCAGLRGFFQVGSDLHLIEPLDEGGEGGRHAVYQAEHLLQTAGTCGVSDDSLGSLLGPRTAAVFRPRPGDSLPSRETRYVELYVVVDNAEFQMLGSEAAVRHRVLEVVNHVDKLYQKLNFRVVLVGLEIWNSQDRFHVSPDPSVTLENLLTWQARQRTRRHLHDNVQLITGVDFTGTTVGFARVSAMCSHSSGAVNQDHSKNPVGVACTMAHEMGHNLGMDHDENVQGCRCQERFEAGRCIMAGSIGSSFPRMFSDCSQAYLESFLERPQSVCLANAPDLSHLVGGPVCGNLFVERGEQCDCGPPEDCRNRCCNSTTCQLAEGAQCAHGTCCQECKVKPAGELCRPKKDMCDLEEFCDGRHPECPEDAFQENGTPCSGGYCYNGACPTLAQQCQAFWGPGGQAAEESCFSYDILPGCKASRYRADMCGVLQCKGGQQPLGRAICIVDVCHALTTEDGTAYEPVPEGTRCGPEKVCWKGRCQDLHVYRSSNCSAQCHNHGVCNHKQECHCHAGWAPPHCAKLLTEVHAASGSLPVFVVVVLVLLAVVLVTLAGIIVYRKARSRILSRNVAPKTTMGRSNPLFHQAASRVPAKGGAPAPSRGPQELVPTTHPGQPARHPASSVALKRPPPAPPVTVSSPPFPVPVYTRQAPKQVIKPTFAPPVPPVKPGAGAANPGPAEGAVGPKVALKPPIQRKQGAGAPTAP TTQWYMD TT Literature-reported TTDYX6T ID TTDYX6T TTDYX6T TN Chitinase (CHIT1) TTDYX6T UP Q13231 TTDYX6T UC CHIT1_HUMAN TTDYX6T BC Glycosylase TTDYX6T SN Chitotriosidase1; Chitinase1; CHIT1 TTDYX6T GN CHIT1 TTDYX6T FC Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity. {ECO:0000269|PubMed:7592832, ECO:0000269|PubMed:7836450}. TTDYX6T EC EC 3.2.1.14 TTDYX6T PD 5NRF; 5NRA; 5NR8; 5HBF; 4WKH TTDYX6T SQ MVRSVAWAGFMVLLMIPWGSAAKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGMTNHQLSTTEWNDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFVNSAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQTSGKERLLLSAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAASLNVDAAVQQWLQKGTPASKLILGMPTYGRSFTLASSSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQKVPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAGFSCNQGRYPLIQTLRQELSLPYLPSGTPELEVPKPGQPSEPEHGPSPGQDTFCQGKADGLYPNPRERSSFYSCAAGRLFQQSCPTGLVFSNSCKCCTWN TTDYX6T TT Literature-reported TTMTF2P ID TTMTF2P TTMTF2P TN Citrate hydro-lyase (ACO2) TTMTF2P UP Q99798 TTMTF2P UC ACON_HUMAN TTMTF2P BC Alpha-carbonic anhydrase TTMTF2P SN Aconitase; ACO2 TTMTF2P GN ACO2 TTMTF2P FC Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. TTMTF2P EC EC 4.2.1.3 TTMTF2P SQ MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPNEYIHYDLLEKNINIVRKRLNRPLTLSEKIVYGHLDDPASQEIERGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSKVAVPSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREDIANLADEFKDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDYLTGTDGKKFRLEAPDADELPKGEFDPGQDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTPGKPLKCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ TTMTF2P TT Literature-reported TTMTF2P KE hsa00020:Citrate cycle (TCA cycle); hsa00630:Glyoxylate and dicarboxylate metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa01210:2-Oxocarboxylic acid metabolism; hsa01230:Biosynthesis of amino acids TTMTF2P RC R-HSA-1268020:Mitochondrial protein import TTZA6B3 ID TTZA6B3 TTZA6B3 TN Citrate synthase (CS) TTZA6B3 UP O75390 TTZA6B3 UC CISY_HUMAN TTZA6B3 BC Acyltransferase TTZA6B3 SN Citrate synthase, mitochondrial; Citrate (Si)-synthase TTZA6B3 GN CS TTZA6B3 FC extracellular exosome, mitochondrial matrix, mitochondrion, nucleus, citrate (Si)-synthase activity, RNA binding, carbohydrate metabolic process, tricarboxylic acid cycle. TTZA6B3 EC EC 2.3.3.1 TTZA6B3 PD 5UZR; 5UZQ; 5UZP TTZA6B3 SQ MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG TTZA6B3 TT Literature-reported TTZA6B3 FM Acyltransferase TTCSI1E ID TTCSI1E TTCSI1E TN Clostridium histolyticum Collagenase (CH colG) TTCSI1E UP Q9X721 TTCSI1E UC COLG_HATHI TTCSI1E SN Microbial collagenase; Gelatinase ColG; Collagenase ColG; Class I collagenase TTCSI1E GN CH colG TTCSI1E FC Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen. Active on soluble type I collagen, insoluble collagen, azocoll, soluble PZ-peptide (all collagenase substrates) and gelatin. The full-length protein has collagenase activity, while the in vivo derived C-terminally truncated shorter versions only act on gelatin. In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain are also synergistic with ColH, although their overall efficiency is decreased. The activator domain (residues 119-388) and catalytic subdomain (389-670) open and close around substrate using a Gly-rich hinge (387-397), allowing digestion when the protein is closed. Binding of collagen requires Ca(2+) and is inhibited by EGTA; the collagen-binding domain (CBD, S3a plus S3b) specifically recognizes the triple-helical conformation made by 3 collagen protein chains in the triple-helical region. Isolated CBD (S3a plus S3b) binds collagen fibrils and sheets of many tissues. TTCSI1E EC EC 3.4.24.3 TTCSI1E PD 5IKU; 4TN9; 4JRW; 4HPK; 4ARE TTCSI1E SQ MKKNILKILMDSYSKESKIQTVRRVTSVSLLAVYLTMNTSSLVLAKPIENTNDTSIKNVEKLRNAPNEENSKKVEDSKNDKVEHVKNIEEAKVEQVAPEVKSKSTLRSASIANTNSEKYDFEYLNGLSYTELTNLIKNIKWNQINGLFNYSTGSQKFFGDKNRVQAIINALQESGRTYTANDMKGIETFTEVLRAGFYLGYYNDGLSYLNDRNFQDKCIPAMIAIQKNPNFKLGTAVQDEVITSLGKLIGNASANAEVVNNCVPVLKQFRENLNQYAPDYVKGTAVNELIKGIEFDFSGAAYEKDVKTMPWYGKIDPFINELKALGLYGNITSATEWASDVGIYYLSKFGLYSTNRNDIVQSLEKAVDMYKYGKIAFVAMERITWDYDGIGSNGKKVDHDKFLDDAEKHYLPKTYTFDNGTFIIRAGDKVSEEKIKRLYWASREVKSQFHRVVGNDKALEVGNADDVLTMKIFNSPEEYKFNTNINGVSTDNGGLYIEPRGTFYTYERTPQQSIFSLEELFRHEYTHYLQARYLVDGLWGQGPFYEKNRLTWFDEGTAEFFAGSTRTSGVLPRKSILGYLAKDKVDHRYSLKKTLNSGYDDSDWMFYNYGFAVAHYLYEKDMPTFIKMNKAILNTDVKSYDEIIKKLSDDANKNTEYQNHIQELADKYQGAGIPLVSDDYLKDHGYKKASEVYSEISKAASLTNTSVTAEKSQYFNTFTLRGTYTGETSKGEFKDWDEMSKKLDGTLESLAKNSWSGYKTLTAYFTNYRVTSDNKVQYDVVFHGVLTDNADISNNKAPIAKVTGPSTGAVGRNIEFSGKDSKDEDGKIVSYDWDFGDGATSRGKNSVHAYKKAGTYNVTLKVTDDKGATATESFTIEIKNEDTTTPITKEMEPNDDIKEANGPIVEGVTVKGDLNGSDDADTFYFDVKEDGDVTIELPYSGSSNFTWLVYKEGDDQNHIASGIDKNNSKVGTFKSTKGRHYVFIYKHDSASNISYSLNIKGLGNEKLKEKENNDSSDKATVIPNFNTTMQGSLLGDDSRDYYSFEVKEEGEVNIELDKKDEFGVTWTLHPESNINDRITYGQVDGNKVSNKVKLRPGKYYLLVYKYSGSGNYELRVNK TTCSI1E TT Literature-reported TTCKI4P ID TTCKI4P TTCKI4P TN COP1 messenger RNA (COP1 mRNA) TTCKI4P UP Q8NHY2 TTCKI4P UC COP1_HUMAN TTCKI4P BC mRNA target TTCKI4P SN hCOP1 (mRNA); RNF200 (mRNA); RING-type E3 ubiquitin transferase RFWD2 (mRNA); RING finger protein 200 (mRNA); RING finger and WD repeat domain protein 2 (mRNA); E3 ubiquitinprotein ligase RFWD2 (mRNA); Constitutive photomorphogenesis protein 1 homolog (mRNA); COP1 (mRNA) TTCKI4P GN RFWD2 TTCKI4P FC E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif. E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. TTCKI4P EC EC 2.3.2.27 TTCKI4P PD 5IGQ; 5HQG TTCKI4P SQ MSGSRQAGSGSAGTSPGSSAASSVTSASSSLSSSPSPPSVAVSAAALVSGGVAQAAGSGGLGGPVRPVLVAPAVSGSGGGAVSTGLSRHSCAARPSAGVGGSSSSLGSGSRKRPLLAPLCNGLINSYEDKSNDFVCPICFDMIEEAYMTKCGHSFCYKCIHQSLEDNNRCPKCNYVVDNIDHLYPNFLVNELILKQKQRFEEKRFKLDHSVSSTNGHRWQIFQDWLGTDQDNLDLANVNLMLELLVQKKKQLEAESHAAQLQILMEFLKVARRNKREQLEQIQKELSVLEEDIKRVEEMSGLYSPVSEDSTVPQFEAPSPSHSSIIDSTEYSQPPGFSGSSQTKKQPWYNSTLASRRKRLTAHFEDLEQCYFSTRMSRISDDSRTASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNGSSIVSSIEFDRDCDYFAIAGVTKKIKVYEYDTVIQDAVDIHYPENEMTCNSKISCISWSSYHKNLLASSDYEGTVILWDGFTGQRSKVYQEHEKRCWSVDFNLMDPKLLASGSDDAKVKLWSTNLDNSVASIEAKANVCCVKFSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVFKGHRKAVSYAKFVSGEEIVSASTDSQLKLWNVGKPYCLRSFKGHINEKNFVGLASNGDYIACGSENNSLYLYYKGLSKTLLTFKFDTVKSVLDKDRKEDDTNEFVSAVCWRALPDGESNVLIAANSQGTIKVLELV TTCKI4P TT Literature-reported TTCKI4P FM mRNA target TTSTNJR ID TTSTNJR TTSTNJR TN COPS5 messenger RNA (COPS5 mRNA) TTSTNJR UP Q92905 TTSTNJR UC CSN5_HUMAN TTSTNJR BC mRNA target TTSTNJR SN Signalosome subunit 5 (mRNA); SGN5 (mRNA); Jun activation domain-binding protein 1 (mRNA); JAB1 (mRNA); CSN5 (mRNA); COP9 signalosome complex subunit 5 (mRNA) TTSTNJR GN COPS5 TTSTNJR FC The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. Promotes the proteasomal degradation of BRSK2. Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. TTSTNJR EC EC 3.4.-.- TTSTNJR PD 5M5Q; 5JOH; 5JOG; 4WSN; 4F7O TTSTNJR SQ MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS TTSTNJR TT Literature-reported TTSTNJR FM mRNA target TT71P0H ID TT71P0H TT71P0H TN Cyclic nucleotide phosphodiesterase (CNP) TT71P0H UP P09543 TT71P0H UC CN37_HUMAN TT71P0H BC Phosphoric diester hydrolase TT71P0H SN CNPase; CNP; 2',3'-cyclic-nucleotide 3'-phosphodiesterase TT71P0H GN CNP TT71P0H FC May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin. TT71P0H EC EC 3.1.4.37 TT71P0H PD 1WOJ TT71P0H SQ MNRGFSRKSHTFLPKIFFRKMSSSGAKDKPELQFPFLQDEDTVATLLECKTLFILRGLPGSGKSTLARVIVDKYRDGTKMVSADAYKITPGARGAFSEEYKRLDEDLAAYCRRRDIRILVLDDTNHERERLEQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSADDLKKLKPGLEKDFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRQFVPGDEPREKMDLVTYFGKRPPGVLHCTTKFCDYGKAPGAEEYAQQDVLKKSYSKAFTLTISALFVTPKTTGARVELSEQQLQLWPSDVDKLSPTDNLPRGSRAHITLGCAADVEAVQTGLDLLEILRQEKGGSRGEEVGELSRGKLYSLGNGRWMLTLAKNMEVRAIFTGYYGKGKPVPTQGSRKGGALQSCTII TT71P0H TT Literature-reported TTAMQ62 ID TTAMQ62 TTAMQ62 TN Cyclin A2 (CCNA2) TTAMQ62 UP P20248 TTAMQ62 UC CCNA2_HUMAN TTAMQ62 SN Cyclin-A2; Cyclin-A; Cyclin A; CCNA TTAMQ62 GN CCNA2 TTAMQ62 FC Functions through the formation of specific serine/threonine protein kinase holoenzyme complexes with the cyclin-dependent protein kinases CDK1 or CDK2. The cyclin subunit confers the substrate specificity of these complexes and differentially interacts with and activates CDK1 and CDK2 throughout the cell cycle. Cyclin which controls both the G1/S and the G2/M transition phases of the cell cycle. TTAMQ62 PD 6GVA; 6ATH; 5NEV; 5LMK; 5IF1 TTAMQ62 SQ MLGNSAPGPATREAGSALLALQQTALQEDQENINPEKAAPVQQPRTRAALAVLKSGNPRGLAQQQRPKTRRVAPLKDLPVNDEHVTVPPWKANSKQPAFTIHVDEAEKEAQKKPAESQKIEREDALAFNSAISLPGPRKPLVPLDYPMDGSFESPHTMDMSIILEDEKPVSVNEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNSKYHGVSLLNPPETLNL TTAMQ62 TT Literature-reported TTAMQ62 KE hsa03030:DNA replication; hsa03410:Base excision repair; hsa03420:Nucleotide excision repair; hsa03430:Mismatch repair; hsa04110:Cell cycle; hsa05161:Hepatitis B; hsa05166:HTLV-I infection TTAMQ62 RC R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-1538133:G0 and Early G1; R-HSA-174184:Cdc20:Phospho-APC/C mediated degradation of Cyclin A; R-HSA-176408:Regulation of APC/C activators between G1/S and early anaphase; R-HSA-187577:SCF(Skp2)-mediated degradation of p27/p21; R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-5358565:Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha); R-HSA-5358606:Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta); R-HSA-5685942:HDR through Homologous Recombination (HRR); R-HSA-5693607:Processing of DNA double-strand break ends; R-HSA-5696400:Dual Incision in GG-NER; R-HSA-6782135:Dual incision in TC-NER; R-HSA-6782210:Gap-filling DNA repair synthesis and ligation in TC-NER; R-HSA-68911:G2 Phase; R-HSA-68949:Orc1 removal from chromatin; R-HSA-69205:G1/S-Specific Transcription; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition; R-HSA-69656:Cyclin A:Cdk2-associated events at S phase entry TTBTI6P ID TTBTI6P TTBTI6P TN Cyclin-dependent kinase-like 1 (CDKL1) TTBTI6P UP Q00532 TTBTI6P UC CDKL1_HUMAN TTBTI6P BC Kinase TTBTI6P SN Serine/threonine-protein kinase KKIALRE; Protein kinase p42 KKIALRE TTBTI6P GN CDKL1 TTBTI6P FC Ciliary transition zone, extracellular exosome, intracellular membrane-bounded organelle, nucleoplasm, nucleus, cyclin-dependent protein serine/threonine kinase activity, protein phosphorylation, regulation of cilium assembly. TTBTI6P EC EC 2.7.11.22 TTBTI6P PD 4AGU TTBTI6P SQ MMEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKKFLESEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLHELDRYQRGVPEHLVKSITWQTLQAVNFCHKHNCIHRDVKPENILITKHSVIKLCDFGFARLLAGPSDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSTNQYFSGVKIPDPEDMEPLELKFPNISYPALGLLKGCLHMDPTQRLTCEQLLHHPYFENIREIEDLAKEHNKPTRKTLRKSRKHHCFTETSKLQYLPQLTGSSILPALDNKKYYCDTKKLNYRFPNI TTBTI6P TT Literature-reported TTMO45N ID TTMO45N TTMO45N TN Cyclin-dependent kinase-like 2 (CDKL2) TTMO45N UP Q92772 TTMO45N UC CDKL2_HUMAN TTMO45N BC Kinase TTMO45N SN Serine/threonine-protein kinase KKIAMRE; Protein kinase p56 KKIAMRE TTMO45N GN CDKL2 TTMO45N FC centrosome, nucleus, cyclin-dependent protein serine/threonine kinase activity, protein kinase activity, protein phosphorylation, sex differentiation, signal transduction. TTMO45N EC EC 2.7.11.22 TTMO45N PD 4BBM; 4AAA TTMO45N SQ MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMDGFAERFSQELQLKVQKDARNVSLSKKSQNRKKEKEKDDSLVEERKTLVVQDTNADPKIKDYKLFKIKGSKIDGEKAEKGNRASNASCLHDSRTSHNKIVPSTSLKDCSNVSVDHTRNPSVAIPPLTHNLSAVAPSINSGMGTETIPIQGYRVDEKTKKCSIPFVKPNRHSPSGIYNINVTTLVSGPPLSDDSGADLPQMEHQH TTMO45N TT Literature-reported TT7N01U ID TT7N01U TT7N01U TN Cytochrome P450 2A5 (CYP2A5) TT7N01U UP P20853 TT7N01U UC CP2A7_HUMAN TT7N01U BC Paired donor oxygen oxidoreductase TT7N01U SN Cytochrome P450-IIA3.2; Cytochrome P450-15-COH; Cyp2a5; Cyp2a-5; CYPIIA5 TT7N01U GN Cyp2a5 TT7N01U FC Exhibits a high coumarin 7-hydroxylase activity. TT7N01U EC EC 1.14.14.1 TT7N01U SQ MLASGLLLVALLACLTVMVLMSVWQQRKSRGKLPPGPTPLPFIGNYLQLNTEHICDSIMKFSECYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVAFSNGERAKQLLRFAIATLRDFGVGKRGIEERIQEESGFLIEAIRSTHGANIDPTFFLSRTVSNVISSIVFGDRFDYEDKEFLSLLSMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFKLLQGLEDFIAKKVEHNQRTLDPNSPQDFIDSFLIHMQEEEKNPNTEFYLKNLMMSTLNLFIAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRTKMPYMEAVIHEIQRFGDVIPMSLARRVKKDTKFRDFFLPKGTEVFPMLGSVLRDPSFFSNPQDFNPQHFLDDKGQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVVFATIPRNYTMSFLPR TT7N01U TT Literature-reported TTOM97J ID TTOM97J TTOM97J TN Cytohesin-2 messenger RNA (CYTH2 mRNA) TTOM97J UP Q99418 TTOM97J UC CYH2_HUMAN TTOM97J BC mRNA target TTOM97J SN Protein ARNO (mRNA); PSCD2L (mRNA); PSCD2 (mRNA); PH, SEC7 and coiled-coil domain-containing protein 2 (mRNA); Cytohesin-2 (mRNA); CYTH2 (mRNA); ARNO (mRNA); ARF nucleotide-binding site opener (mRNA); ARF exchange factor (mRNA) TTOM97J GN CYTH2 TTOM97J FC Promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Activates ARF factors through replacement of GDP with GTP. The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane. Involved in neurite growth. Acts as a guanine-nucleotide exchange factor (GEF). TTOM97J PD 4Z21; 4L5M; 4JXH; 4JWL; 4JMO TTOM97J SQ MEDGVYEPPDLTPEERMELENIRRRKQELLVEIQRLREELSEAMSEVEGLEANEGSKTLQRNRKMAMGRKKFNMDPKKGIQFLVENELLQNTPEEIARFLYKGEGLNKTAIGDYLGEREELNLAVLHAFVDLHEFTDLNLVQALRQFLWSFRLPGEAQKIDRMMEAFAQRYCLCNPGVFQSTDTCYVLSFAVIMLNTSLHNPNVRDKPGLERFVAMNRGINEGGDLPEELLRNLYDSIRNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVDDPRKPNCFELYIPNNKGQLIKACKTEADGRVVEGNHMVYRISAPTQEEKDEWIKSIQAAVSVDPFYEMLAARKKRISVKKKQEQP TTOM97J TT Literature-reported TTOM97J FM mRNA target TTOM97J KE hsa04144:Endocytosis TTERVQN ID TTERVQN TTERVQN TN Death-associated protein kinase 3 (DAPK3) TTERVQN UP O43293 TTERVQN UC DAPK3_HUMAN TTERVQN BC Kinase TTERVQN SN Zipper-interacting protein kinase; ZIPK; ZIP-kinase; MYPT1 kinase; DAP-like kinase; DAP kinase 3 TTERVQN GN DAPK3 TTERVQN FC Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in regulation of starvation-induced autophagy. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle, regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A; the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton. Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B. Overexpression leads to condensation of actin stress fibers into thick bundles. Involved in actin filament focal adhesion dynamics. The function in both reorganization of actin cytoskeleton and focal adhesion dissolution is modulated by RhoD. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Involved in regulation of cell cycle progression and cell proliferation. May be a tumor suppressor. Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. TTERVQN EC EC 2.7.11.1 TTERVQN PD 5VJA; 5A6O; 5A6N; 3BQR; 3BHY TTERVQN SQ MSTFRQEDVEDHYEMGEELGSGQFAIVRKCRQKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIRHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKAIRRRNVRGEDSGRKPERRRLKTTRLKEYTIKSHSSLPPNNSYADFERFSKVLEEAAAAEEGLRELQRSRRLCHEDVEALAAIYEEKEAWYREESDSLGQDLRRLRQELLKTEALKRQAQEEAKGALLGTSGLKRRFSRLENRYEALAKQVASEMRFVQDLVRALEQEKLQGVECGLR TTERVQN TT Literature-reported TTTK0NH ID TTTK0NH TTTK0NH TN Delta(24)-sterol reductase (DHCR24) TTTK0NH UP Q15392 TTTK0NH UC DHC24_HUMAN TTTK0NH BC CH-CH donor oxidoreductase TTTK0NH SN Seladin-1; Diminuto/dwarf1 homolog; DHCR24 TTTK0NH GN DHCR24 TTTK0NH FC Catalyzes the reduction of the delta-24 double bond of sterol intermediates. Protects cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress. Also protects against amyloid-beta peptide-induced apoptosis. TTTK0NH EC EC 1.3.1.72 TTTK0NH SQ MEPAVSLAVCALLFLLWVRLKGLEFVLIHQRWVFVCLFLLPLSLIFDIYYYVRAWVVFKLSSAPRLHEQRVRDIQKQVREWKEQGSKTFMCTGRPGWLTVSLRVGKYKKTHKNIMINLMDILEVDTKKQIVRVEPLVTMGQVTALLTSIGWTLPVLPELDDLTVGGLIMGTGIESSSHKYGLFQHICTAYELVLADGSFVRCTPSENSDLFYAVPWSCGTLGFLVAAEIRIIPAKKYVKLRFEPVRGLEAICAKFTHESQRQENHFVEGLLYSLDEAVIMTGVMTDEAEPSKLNSIGNYYKPWFFKHVENYLKTNREGLEYIPLRHYYHRHTRSIFWELQDIIPFGNNPIFRYLFGWMVPPKISLLKLTQGETLRKLYEQHHVVQDMLVPMKCLQQALHTFQNDIHVYPIWLCPFILPSQPGLVHPKGNEAELYIDIGAYGEPRVKHFEARSCMRQLEKFVRSVHGFQMLYADCYMNREEFWEMFDGSLYHKLREKLGCQDAFPEVYDKICKAARH TTTK0NH TT Literature-reported TTTK0NH KE hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways TTTK0NH RC R-HSA-191273:Cholesterol biosynthesis TTNWD8O ID TTNWD8O TTNWD8O TN Delta-tryptase (TPSD1) TTNWD8O UP Q9BZJ3 TTNWD8O UC TRYD_HUMAN TTNWD8O BC Peptidase TTNWD8O SN TPSD1; Mast cell mMCP-7-like; HmMCP-3-like tryptase III; Delta tryptase TTNWD8O GN TPSD1 TTNWD8O FC Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. TTNWD8O EC EC 3.4.21.59 TTNWD8O SQ MLLLAPQMLSLLLLALPVLASPAYVAPAPGQALQQTGIVGGQEAPRSKWPWQVSLRVRGPYWMHFCGGSLIHPQWVLTAAHCVEPDIKDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYIIQTGADIALLELEEPVNISSHIHTVTLPPASETFPPGMPCWVTGWGDVDNNVHLPPPYPLKEVEVPVVENHLCNAEYHTGLHTGHSFQIVRDDMLCAGSENHDSCQGDSGGPLVCKVNGT TTNWD8O TT Literature-reported TTMBUHI ID TTMBUHI TTMBUHI TN Deneddylase-1 (SENP8) TTMBUHI UP Q96LD8 TTMBUHI UC SENP8_HUMAN TTMBUHI BC Peptidase TTMBUHI SN Sentrin/SUMO-specific protease SENP8; Sentrin-specific protease 8; Protease, cysteine 2; PRSC2; NEDP1; NEDD8-specific protease 1; FKSG8; DEN1 TTMBUHI GN SENP8 TTMBUHI FC Protease that catalyzes two essential functions in the NEDD8 pathway: processing of full-length NEDD8 to its mature form and deconjugation of NEDD8 from targeted proteins such as cullins or p53. TTMBUHI EC EC 3.4.22.- TTMBUHI PD 2BKR; 2BKQ; 1XT9 TTMBUHI SQ MDPVVLSYMDSLLRQSDVSLLDPPSWLNDHIIGFAFEYFANSQFHDCSDHVSFISPEVTQFIKCTSNPAEIAMFLEPLDLPNKRVVFLAINDNSNQAAGGTHWSLLVYLQDKNSFFHYDSHSRSNSVHAKQVAEKLEAFLGRKGDKLAFVEEKAPAQQNSYDCGMYVICNTEALCQNFFRQQTESLLQLLTPAYITKKRGEWKDLITTLAKK TTMBUHI TT Literature-reported TTYWGOJ ID TTYWGOJ TTYWGOJ TN Deoxyribonuclease I (DNASE1) TTYWGOJ UP P24855 TTYWGOJ UC DNAS1_HUMAN TTYWGOJ BC Endodeoxyribonucleases TTYWGOJ SN Herpesvirus alkaline deoxyribonuclease; Herpesvirus alkaline DNase; Dornase alfa; DNase I; DNASE1; Alkaline deoxyribonuclease TTYWGOJ GN DNASE1 TTYWGOJ FC Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization. TTYWGOJ EC EC 3.1.21.1 TTYWGOJ PD 4AWN TTYWGOJ SQ MRGMKLLGALLALAALLQGAVSLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK TTYWGOJ TT Literature-reported TTG9MT5 ID TTG9MT5 TTG9MT5 TN Deubiquitinating enzyme 1 (USP1) TTG9MT5 UP O94782 TTG9MT5 UC UBP1_HUMAN TTG9MT5 BC Peptidase TTG9MT5 SN hUBP; Ubiquitin-specific-processing protease 1; Ubiquitin thioesterase 1; Ubiquitin carboxyl-terminal hydrolase 1 TTG9MT5 GN USP1 TTG9MT5 FC Involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2. TTG9MT5 EC EC 3.4.19.12 TTG9MT5 PD 6DO5 TTG9MT5 SQ MPGVIPSESNGLSRGSPSKKNRLSLKFFQKKETKRALDFTDSQENEEKASEYRASEIDQVVPAAQSSPINCEKRENLLPFVGLNNLGNTCYLNSILQVLYFCPGFKSGVKHLFNIISRKKEALKDEANQKDKGNCKEDSLASYELICSLQSLIISVEQLQASFLLNPEKYTDELATQPRRLLNTLRELNPMYEGYLQHDAQEVLQCILGNIQETCQLLKKEEVKNVAELPTKVEEIPHPKEEMNGINSIEMDSMRHSEDFKEKLPKGNGKRKSDTEFGNMKKKVKLSKEHQSLEENQRQTRSKRKATSDTLESPPKIIPKYISENESPRPSQKKSRVKINWLKSATKQPSILSKFCSLGKITTNQGVKGQSKENECDPEEDLGKCESDNTTNGCGLESPGNTVTPVNVNEVKPINKGEEQIGFELVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEPKTEMKTLRWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEFDCYGGGLSKINTPLLTPLKLSLEEWSTKPTNDSYGLFAVVMHSGITISSGHYTASVKVTDLNSLELDKGNFVVDQMCEIGKPEPLNEEEARGVVENYNDEEVSIRVGGNTQPSKVLNKKNVEAIGLLGGQKSKADYELYNKASNPDKVASTAFAENRNSETSDTTGTHESDRNKESSDQTGINISGFENKISYVVQSLKEYEGKWLLFDDSEVKVTEEKDFLNSLSPSTSPTSTPYLLFYKKL TTG9MT5 TT Literature-reported TT69I0C ID TT69I0C TT69I0C TN Diphosphoinositol polyphosphate phosphohydrolase 2 (NUDT3) TT69I0C UP O95989 TT69I0C UC NUDT3_HUMAN TT69I0C BC Acid anhydrides hydrolase TT69I0C SN NUDT3; Diphosphoinositol polyphosphate phosphohydrolase; DIPP2 TT69I0C GN NUDT3 TT69I0C FC Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. InsP6 (inositol hexakisphophate) is not a substrate. Acts as a negative regulator of the ERK1/2 pathway. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5- phosphoribose 1-diphosphate. TT69I0C EC EC 3.6.1.52 TT69I0C PD 2Q9P; 2FVV TT69I0C SQ MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPSVAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVNIGRKREWFKIEDAIKVLQYHKPVQASYFETLRQGYSANNGTPVVATTYSVSAQSSMSGIR TT69I0C TT Literature-reported TTU98HG ID TTU98HG TTU98HG TN Discoidin domain-containing receptor 2 (DDR2) TTU98HG UP Q16832 TTU98HG UC DDR2_HUMAN TTU98HG BC Kinase TTU98HG SN Tyrosine-protein kinase TYRO10; Receptor protein-tyrosine kinase TKT; Neurotrophic tyrosine kinase, receptor-related 3; Discoidin domain-containing receptor tyrosine kinase 2; Discoidin domain receptor 2; DDR2; CD167 antigen-like family member B TTU98HG GN DDR2 TTU98HG FC Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing. TTU98HG EC EC 2.7.10.1 TTU98HG PD 6FER; 2Z4F; 2WUH TTU98HG SQ MILIPRMLLVLFLLLPILSSAKAQVNPAICRYPLGMSGGQIPDEDITASSQWSESTAAKYGRLDSEEGDGAWCPEIPVEPDDLKEFLQIDLHTLHFITLVGTQGRHAGGHGIEFAPMYKINYSRDGTRWISWRNRHGKQVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHSMNVCMRVELYGCVWLDGLVSYNAPAGQQFVLPGGSIIYLNDSVYDGAVGYSMTEGLGQLTDGVSGLDDFTQTHEYHVWPGYDYVGWRNESATNGYIEIMFEFDRIRNFTTMKVHCNNMFAKGVKIFKEVQCYFRSEASEWEPNAISFPLVLDDVNPSARFVTVPLHHRMASAIKCQYHFADTWMMFSEITFQSDAAMYNNSEALPTSPMAPTTYDPMLKVDDSNTRILIGCLVAIIFILLAIIVIILWRQFWQKMLEKASRRMLDDEMTVSLSLPSDSSMFNNNRSSSPSEQGSNSTYDRIFPLRPDYQEPSRLIRKLPEFAPGEEESGCSGVVKPVQPSGPEGVPHYAEADIVNLQGVTGGNTYSVPAVTMDLLSGKDVAVEEFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQQGDE TTU98HG TT Patented-recorded TTQGKSD ID TTQGKSD TTQGKSD TN DNA replication licensing factor MCM6 (MCM6) TTQGKSD UP Q14566 TTQGKSD UC MCM6_HUMAN TTQGKSD BC Acid anhydride hydrolase TTQGKSD SN p105MCM; Minichromosome maintenanceprotein 6 TTQGKSD GN MCM6 TTQGKSD FC The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. TTQGKSD EC EC 3.6.4.12 TTQGKSD PD 2LE8; 2KLQ TTQGKSD SQ MDLAAAAEPGAGSQHLEVRDEVAEKCQKLFLDFLEEFQSSDGEIKYLQLAEELIRPERNTLVVSFVDLEQFNQQLSTTIQEEFYRVYPYLCRALKTFVKDRKEIPLAKDFYVAFQDLPTRHKIRELTSSRIGLLTRISGQVVRTHPVHPELVSGTFLCLDCQTVIRDVEQQFKYTQPNICRNPVCANRRRFLLDTNKSRFVDFQKVRIQETQAELPRGSIPRSLEVILRAEAVESAQAGDKCDFTGTLIVVPDVSKLSTPGARAETNSRVSGVDGYETEGIRGLRALGVRDLSYRLVFLACCVAPTNPRFGGKELRDEEQTAESIKNQMTVKEWEKVFEMSQDKNLYHNLCTSLFPTIHGNDEVKRGVLLMLFGGVPKTTGEGTSLRGDINVCIVGDPSTAKSQFLKHVEEFSPRAVYTSGKASSAAGLTAAVVRDEESHEFVIEAGALMLADNGVCCIDEFDKMDVRDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPISGHYDRSKSLKQNINLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHSRIEESIDRVYSLDDIRRYLLFARQFKPKISKESEDFIVEQYKHLRQRDGSGVTKSSWRITVRQLESMIRLSEAMARMHCCDEVQPKHVKEAFRLLNKSIIRVETPDVNLDQEEEIQMEVDEGAGGINGHADSPAPVNGINGYNEDINQESAPKASLRLGFSEYCRISNLIVLHLRKVEEEEDESALKRSELVNWYLKEIESEIDSEEELINKKRIIEKVIHRLTHYDHVLIELTQAGLKGSTEGSESYEEDPYLVVNPNYLLED TTQGKSD TT Literature-reported TTQGKSD FM Acid anhydrides hydrolase TTOHTCY ID TTOHTCY TTOHTCY TN Doublecortin-like kinase 1 (DCLK1) TTOHTCY UP O15075 TTOHTCY UC DCLK1_HUMAN TTOHTCY BC Kinase TTOHTCY SN Serine/threonine-protein kinase DCLK1; KIAA0369; Doublecortin-like and CAM kinase-like 1; Doublecortin domain-containing protein 3A; DCDC3A; DCAMKL1 TTOHTCY GN DCLK1 TTOHTCY FC May also participate in functions of the mature nervous system. Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. TTOHTCY EC EC 2.7.11.1 TTOHTCY PD 5JZN; 5JZJ; 1UF0; 1MG4; 1MFW TTOHTCY SQ MSFGRDMELEHFDERDKAQRYSRGSRVNGLPSPTHSAHCSFYRTRTLQTLSSEKKAKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRTLSDNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCGSIEPFKKLEYTKNVNPNWSVNVKTTSASRAVSSLATAKGSPSEVRENKDFIRPKLVTIIRSGVKPRKAVRILLNKKTAHSFEQVLTDITDAIKLDSGVVKRLYTLDGKQVMCLQDFFGDDDIFIACGPEKFRYQDDFLLDESECRVVKSTSYTKIASSSRRSTTKSPGPSRRSKSPASTSSVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRSSQHGGSSTSLASTKVCSSMDENDGPGEEVSEEGFQIPATITERYKVGRTIGDGNFAVVKECVERSTAREYALKIIKKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDVPTELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATIVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKELITMMLLVDVDQRFSAVQVLEHPWVNDDGLPENEHQLSVAGKIKKHFNTGPKPNSTAAGVSVIATTALDKERQVFRRRRNQDVRSRYKAQPAPPELNSESEDYSPSSSETVRSPNSPF TTOHTCY TT Literature-reported TTF3RJ0 ID TTF3RJ0 TTF3RJ0 TN Dual specificity protein phosphatase 10 (DUSP10) TTF3RJ0 UP Q9Y6W6 TTF3RJ0 UC DUS10_HUMAN TTF3RJ0 BC Phosphoric monoester hydrolase TTF3RJ0 SN Mitogen-activated protein kinase phosphatase 5; MKP5; MKP-5; MAP kinase phosphatase 5 TTF3RJ0 GN DUSP10 TTF3RJ0 FC Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38. Protein phosphatase involved in the inactivation of MAP kinases. TTF3RJ0 EC EC 3.1.3.16 TTF3RJ0 PD 3TG1; 2OUD; 2OUC; 1ZZW TTF3RJ0 SQ MPPSPLDDRVVVALSRPVRPQDLNLCLDSSYLGSANPGSNSHPPVIATTVVSLKAANLTYMPSSSGSARSLNCGCSSASCCTVATYDKDNQAQTQAIAAGTTTTAIGTSTTCPANQMVNNNENTGSLSPSSGVGSPVSGTPKQLASIKIIYPNDLAKKMTKCSKSHLPSQGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDSFKRIFSKEIIVYDENTNEPSRVMPSQPLHIVLESLKREGKEPLVLKGGLSSFKQNHENLCDNSLQLQECREVGGGASAASSLLPQPIPTTPDIENAELTPILPFLFLGNEQDAQDLDTMQRLNIGYVINVTTHLPLYHYEKGLFNYKRLPATDSNKQNLRQYFEEAFEFIEEAHQCGKGLLIHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKGKRPIISPNLNFMGQLLEFEEDLNNGVTPRILTPKLMGVETVV TTF3RJ0 TT Literature-reported TTF3RJ0 FM Phosphoric monoester hydrolases TTASI04 ID TTASI04 TTASI04 TN E2F1 messenger RNA (E2F1 mRNA) TTASI04 UP Q01094 TTASI04 UC E2F1_HUMAN TTASI04 BC mRNA target TTASI04 SN pRB-binding protein E2F-1 (mRNA); Transcription factor E2F1 (mRNA); Retinoblastoma-binding protein 3 (mRNA); Retinoblastoma-associated protein 1 (mRNA); RBBP3 (mRNA); RBBP-3 (mRNA); RBAP-1 (mRNA); PBR3 (mRNA); E2F-1 (mRNA) TTASI04 GN E2F1 TTASI04 FC The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters. Positively regulates transcription of RRP1B. Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. TTASI04 PD 6G0P; 5M9O; 5M9N; 2AZE; 1O9K TTASI04 SQ MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF TTASI04 TT Literature-reported TTASI04 FM mRNA target TTASI04 KE hsa04110:Cell cycle; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer TTASI04 RC R-HSA-111448:Activation of NOXA and translocation to mitochondria; R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-139915:Activation of PUMA and translocation to mitochondria; R-HSA-1538133:G0 and Early G1; R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559585:Oncogene Induced Senescence; R-HSA-68689:CDC6 association with the ORC:origin complex; R-HSA-68911:G2 Phase; R-HSA-69205:G1/S-Specific Transcription; R-HSA-69231:Cyclin D associated events in G1; R-HSA-69298:Association of licensing factors with the pre-replicative complex TTGT3RQ ID TTGT3RQ TTGT3RQ TN E3 ubiquitin protein ligase CBLB (CBLB) TTGT3RQ UP Q13191 TTGT3RQ UC CBLB_HUMAN TTGT3RQ BC Acyltransferase TTGT3RQ SN Signal transduction protein CBLB; Signal transduction protein CBL-B; SH3binding protein CBLB; SH3-binding protein CBL-B; RNF56; RING-type E3 ubiquitin transferase CBL-B; RING finger protein 56; Nbla00127; E3 ubiquitinprotein ligase CBLB; E3 ubiquitin-protein ligase CBL-B; Casitas Blineage lymphoma protooncogene b; Casitas B-lineage lymphoma proto-oncogene b TTGT3RQ GN CBLB TTGT3RQ FC Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBL, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA. E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. TTGT3RQ EC EC 2.3.2.27 TTGT3RQ PD 3ZNI; 3VGO; 3PFV; 2OOB; 2OOA TTGT3RQ SQ MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFGMPMLDLDDDDDREESLMMNRLANVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPPERPPPIPPDNRLSRHIHHVESVPSRDPPMPLEAWCPRDVFGTNQLVGCRLLGEGSPKPGITASSNVNGRHSRVGSDPVLMRKHRRHDLPLEGAKVFSNGHLGSEEYDVPPRLSPPPPVTTLLPSIKCTGPLANSLSEKTRDPVEEDDDEYKIPSSHPVSLNSQPSHCHNVKPPVRSCDNGHCMLNGTHGPSSEKKSNIPDLSIYLKGDVFDSASDPVPLPPARPPTRDNPKHGSSLNRTPSDYDLLIPPLGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFVDLASGQVPLPPARRLPGENVKTNRTSQDYDQLPSCSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL TTGT3RQ TT Literature-reported TTGT3RQ FM Carbon-nitrogen ligase TT5SEWD ID TT5SEWD TT5SEWD TN E3 ubiquitin protein ligase Itchy (ITCH) TT5SEWD UP Q96J02 TT5SEWD UC ITCH_HUMAN TT5SEWD BC Acyltransferase TT5SEWD SN NFE2-associated polypeptide 1; NAPP1; Itch; HECT-type E3 ubiquitin transferase Itchy homolog; E3 ubiquitin-protein ligase Itchy homolog; Atrophin-1-interacting protein 4; AIP4 TT5SEWD GN ITCH TT5SEWD FC Catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. Involved in the control of inflammatory signaling pathways. Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of the complex after TNF stimulation. Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response. Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages. Mediates JUN ubiquitination and degradation. Mediates JUNB ubiquitination and degradation. Critical regulator of type 2 helper T (Th2) cell cytokine production by inducing JUNB ubiquitination and degradation. Involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Following ligand stimulation, regulates sorting of Wnt receptor FZD4 to the degradative endocytic pathway probably by modulating PI42KA activity. Ubiquitinates PI4K2A and negatively regulates its catalytic activity. Ubiquitinates chemokine receptor CXCR4 and regulates sorting of CXCR4 to the degradative endocytic pathway following ligand stimulation by ubiquitinating endosomal sorting complex required for transport ESCRT-0 components HGS and STAM. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination. Ubiquitinates SNX9. Ubiquitinates MAP3K7 through 'Lys-48'-linked conjugation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1. Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. TT5SEWD EC EC 2.3.2.26 TT5SEWD PD 5SXP; 5DZD; 5DWS; 5CQ2; 5C7M TT5SEWD SQ MSDSGSQLGSMGSLTMKSQLQITVISAKLKENKKNWFGPSPYVEVTVDGQSKKTEKCNNTNSPKWKQPLTVIVTPVSKLHFRVWSHQTLKSDVLLGTAALDIYETLKSNNMKLEEVVVTLQLGGDKEPTETIGDLSICLDGLQLESEVVTNGETTCSENGVSLCLPRLECNSAISAHCNLCLPGLSDSPISASRVAGFTGASQNDDGSRSKDETRVSTNGSDDPEDAGAGENRRVSGNNSPSLSNGGFKPSRPPRPSRPPPPTPRRPASVNGSPSATSESDGSSTGSLPPTNTNTNTSEGATSGLIIPLTISGGSGPRPLNPVTQAPLPPGWEQRVDQHGRVYYVDHVEKRTTWDRPEPLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATSQSKEFDPLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQGQLNEKPLPEGWEMRFTVDGIPYFVDHNRRTTTYIDPRTGKSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQHIKITVTRKTLFEDSFQQIMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSVDKEILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRHYARTSKQIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVGKENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFGQE TT5SEWD TT Literature-reported TT5SEWD FM Carbon-nitrogen ligase TT1QU6G ID TT1QU6G TT1QU6G TN E3 ubiquitin-protein ligase NEDD4 (NEDD4) TT1QU6G UP P46934 TT1QU6G UC NEDD4_HUMAN TT1QU6G SN Neural precursor cell expressed developmentally down-regulated protein 4; NEDD4-1; NEDD-4; KIAA0093; HECT-type E3 ubiquitin transferase NEDD4; Cell proliferation-inducing gene 53 protein TT1QU6G GN NEDD4 TT1QU6G FC E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Specifically ubiquitinates 'Lys-63' in target proteins (PubMed:23644597). Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. Promotes ubiquitination of RAPGEF2. According to PubMed:18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed:17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD. Involved in the budding of many viruses. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). TT1QU6G EC EC 2.3.2.26 TT1QU6G PD 5C91; 5C7J; 5AHT; 4N7H; 4N7F TT1QU6G SQ MAQSLRLHFAARRSNTYPLSETSGDDLDSHVHMCFKRPTRISTSNVVQMKLTPRQTALAPLIKENVQSQERSSVPSSENVNKKSSCLQISLQPTRYSGYLQSSNVLADSDDASFTCILKDGIYSSAVVDNELNAVNDGHLVSSPAICSGSLSNFSTSDNGSYSSNGSDFGSCASITSGGSYTNSVISDSSSYTFPPSDDTFLGGNLPSDSTSNRSVPNRNTTPCEIFSRSTSTDPFVQDDLEHGLEIMKLPVSRNTKIPLKRYSSLVIFPRSPSTTRPTSPTSLCTLLSKGSYQTSHQFIISPSEIAHNEDGTSAKGFLSTAVNGLRLSKTICTPGEVRDIRPLHRKGSLQKKIVLSNNTPRQTVCEKSSEGYSCVSVHFTQRKAATLDCETTNGDCKPEMSEIKLNSDSEYIKLMHRTSACLPSSQNVDCQININGELERPHSQMNKNHGILRRSISLGGAYPNISCLSSLKHNCSKGGPSQLLIKFASGNEGKVDNLSRDSNRDCTNELSNSCKTRDDFLGQVDVPLYPLPTENPRLERPYTFKDFVLHPRSHKSRVKGYLRLKMTYLPKTSGSEDDNAEQAEELEPGWVVLDQPDAACHLQQQQEPSPLPPGWEERQDILGRTYYVNHESRRTQWKRPTPQDNLTDAENGNIQLQAQRAFTTRRQISEETESVDNRESSENWEIIREDEATMYSNQAFPSPPPSSNLDVPTHLAEELNARLTIFGNSAVSQPASSSNHSSRRGSLQAYTFEEQPTLPVLLPTSSGLPPGWEEKQDERGRSYYVDHNSRTTTWTKPTVQATVETSQLTSSQSSAGPQSQASTSDSGQQVTQPSEIEQGFLPKGWEVRHAPNGRPFFIDHNTKTTTWEDPRLKIPAHLRGKTSLDTSNDLGPLPPGWEERTHTDGRIFYINHNIKRTQWEDPRLENVAITGPAVPYSRDYKRKYEFFRRKLKKQNDIPNKFEMKLRRATVLEDSYRRIMGVKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWILENDPTELDLRFIIDEELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQSFTVEQWGTPEKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFDGVD TT1QU6G TT Literature-reported TT1QU6G KE hsa04120:Ubiquitin mediated proteolysis; hsa04144:Endocytosis; hsa04530:Tight junction; hsa05169:Epstein-Barr virus infection TTVGS1C ID TTVGS1C TTVGS1C TN Endoplasmic reticulum aminopeptidase 2 (ERAP2) TTVGS1C UP Q6P179 TTVGS1C UC ERAP2_HUMAN TTVGS1C BC Peptidase TTVGS1C SN Leukocyte-derived arginine aminopeptidase; LRAP; L-RAP TTVGS1C GN ERAP2 TTVGS1C FC Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys. Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. TTVGS1C EC EC 3.4.11.- TTVGS1C PD 5K1V; 5J6S; 5CU5; 5AB2; 5AB0 TTVGS1C SQ MFHSSAMVNSHRKPMFNIHRGFYCLTAILPQICICSQFSVPSSYHFTEDPGAFPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLKEGFAKYMELIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSCLESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT TTVGS1C TT Literature-reported TTXL0GC ID TTXL0GC TTXL0GC TN Enteropeptidase (TMPRSS15) TTXL0GC UP P98073 TTXL0GC UC ENTK_HUMAN TTXL0GC BC Peptidase TTXL0GC SN Transmembrane protease serine 15; TMPRSS15; Serine protease 7; Enterokinase TTXL0GC GN TMPRSS15 TTXL0GC FC Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. TTXL0GC EC EC 3.4.21.9 TTXL0GC PD 4DGJ TTXL0GC SQ MGSKRGISSRHHSLSSYEIMFAALFAILVVLCAGLIAVSCLTIKESQRGAALGQSHEARATFKITSGVTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFENGSIIVVFDLFFAQWVSDENVKEELIQGLEANKSSQLVTFHIDLNSVDILDKLTTTSHLATPGNVSIECLPGSSPCTDALTCIKADLFCDGEVNCPDGSDEDNKMCATVCDGRFLLTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYTDILDIYEGVGSSKILRASIWETNPGTIRIFSNQVTATFLIESDESDYVGFNATYTAFNSSELNNYEKINCNFEDGFCFWVQDLNDDNEWERIQGSTFSPFTGPNFDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSFWYHMYGENVHKLSINISNDQNMEKTVFQKEGNYGDNWNYGQVTLNETVKFKVAFNAFKNKILSDIALDDISLTYGICNGSLYPEPTLVPTPPPELPTDCGGPFELWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLENINDVVEIRDGEEADSLLLAVYTGPGPVKDVFSTTNRMTVLLITNDVLARGGFKANFTTGYHLGIPEPCKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADCVRFFNGTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKPIFPTDGGPFVKLNTAPDGHLILTPSQQCLQDSLIRLQCNHKSCGKKLAAQDITPKIVGGSNAKEGAWPWVVGLYYGGRLLCGASLVSSDWLVSAAHCVYGRNLEPSKWTAILGLHMKSNLTSPQTVPRLIDEIVINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQQMPEYNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQSFLH TTXL0GC TT Patented-recorded TTLFZVU ID TTLFZVU TTLFZVU TN Ephrin type-A receptor 1 (EPHA1) TTLFZVU UP P21709 TTLFZVU UC EPHA1_HUMAN TTLFZVU BC Kinase TTLFZVU SN hEpha1; Tyrosine-protein kinase receptor EPH; Erythropoietin-producing hepatoma receptor; EPHT1; EPHT; EPH tyrosine kinase 1; EPH tyrosine kinase; EPH TTLFZVU GN EPHA1 TTLFZVU FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Plays also a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis. Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TTLFZVU EC EC 2.7.10.1 TTLFZVU PD 3KKA; 3HIL; 2K1L; 2K1K TTLFZVU SQ MERRWPLGLGLVLLLCAPLPPGARAKEVTLMDTSKAQGELGWLLDPPKDGWSEQQQILNGTPLYMYQDCPMQGRRDTDHWLRSNWIYRGEEASRVHVELQFTVRDCKSFPGGAGPLGCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLVSGSVKLNVERCSLGRLTRRGLYLAFHNPGACVALVSVRVFYQRCPETLNGLAQFPDTLPGPAGLVEVAGTCLPHARASPRPSGAPRMHCSPDGEWLVPVGRCHCEPGYEEGGSGEACVACPSGSYRMDMDTPHCLTCPQQSTAESEGATICTCESGHYRAPGEGPQVACTGPPSAPRNLSFSASGTQLSLRWEPPADTGGRQDVRYSVRCSQCQGTAQDGGPCQPCGVGVHFSPGARGLTTPAVHVNGLEPYANYTFNVEAQNGVSGLGSSGHASTSVSISMGHAESLSGLSLRLVKKEPRQLELTWAGSRPRSPGANLTYELHVLNQDEERYQMVLEPRVLLTELQPDTTYIVRVRMLTPLGPGPFSPDHEFRTSPPVSRGLTGGEIVAVIFGLLLGAALLLGILVFRSRRAQRQRQQRQRDRATDVDREDKLWLKPYVDLQAYEDPAQGALDFTRELDPAWLMVDTVIGEGEFGEVYRGTLRLPSQDCKTVAIKTLKDTSPGGQWWNFLREATIMGQFSHPHILHLEGVVTKRKPIMIITEFMENGALDAFLREREDQLVPGQLVAMLQGIASGMNYLSNHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMSNQEVMKSIEDGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFQKLQAHLEQLLANPHSLRTIANFDPRMTLRLPSLSGSDGIPYRTVSEWLESIRMKRYILHFHSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFKD TTLFZVU TT Literature-reported TTV9KOD ID TTV9KOD TTV9KOD TN Ephrin type-A receptor 5 (EPHA5) TTV9KOD UP P54756 TTV9KOD UC EPHA5_HUMAN TTV9KOD BC Kinase TTV9KOD SN hEK7; EPH-like kinase 7; EPH homology kinase 1; EK7; EHK1; EHK-1; Brain-specific kinase; BSK TTV9KOD GN EPHA5 TTV9KOD FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Among GPI-anchored ephrin-A ligands, EFNA5 most probably constitutes the cognate/functional ligand for EPHA5. Functions as an axon guidance molecule during development and may be involved in the development of the retinotectal, entorhino-hippocampal and hippocamposeptal pathways. Together with EFNA5 plays also a role in synaptic plasticity in adult brain through regulation of synaptogenesis. In addition to its function in the nervous system, the interaction of EPHA5 with EFNA5 mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TTV9KOD EC EC 2.7.10.1 TTV9KOD PD 4ET7; 2R2P TTV9KOD SQ MRGSGPRGAGRRRPPSGGGDTPITPASLAGCYSAPRRAPLWTCLLLCAALRTLLASPSNEVNLLDSRTVMGDLGWIAFPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNSLPGGLGTCKETFNMYYFESDDQNGRNIKENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLSKKGFYLAFQDVGACIALVSVRVYYKKCPSVVRHLAVFPDTITGADSSQLLEVSGSCVNHSVTDEPPKMHCSAEGEWLVPIGKCMCKAGYEEKNGTCQVCRPGFFKASPHIQSCGKCPPHSYTHEEASTSCVCEKDYFRRESDPPTMACTRPPSAPRNAISNVNETSVFLEWIPPADTGGRKDVSYYIACKKCNSHAGVCEECGGHVRYLPRQSGLKNTSVMMVDLLAHTNYTFEIEAVNGVSDLSPGARQYVSVNVTTNQAAPSPVTNVKKGKIAKNSISLSWQEPDRPNGIILEYEIKYFEKDQETSYTIIKSKETTITAEGLKPASVYVFQIRARTAAGYGVFSRRFEFETTPVFAASSDQSQIPVIAVSVTVGVILLAVVIGVLLSGSCCECGCGRASSLCAVAHPSLIWRCGYSKAKQDPEEEKMHFHNGHIKLPGVRTYIDPHTYEDPNQAVHEFAKEIEASCITIERVIGAGEFGEVCSGRLKLPGKRELPVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIHLEGVVTKSKPVMIVTEYMENGSLDTFLKKNDGQFTVIQLVGMLRGISAGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVVSYGERPYWEMTNQDVIKAVEEGYRLPSPMDCPAALYQLMLDCWQKERNSRPKFDEIVNMLDKLIRNPSSLKTLVNASCRVSNLLAEHSPLGSGAYRSVGEWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMNSLQEMKVQLVNGMVPL TTV9KOD TT Literature-reported TTAHTVG ID TTAHTVG TTAHTVG TN Ephrin type-A receptor 7 (EPHA7) TTAHTVG UP Q15375 TTAHTVG UC EPHA7_HUMAN TTAHTVG BC Kinase TTAHTVG SN hEK11; EPH-like kinase 11; EPH homology kinase 3; EK11; EHK3; EHK-3 TTAHTVG GN EPHA7 TTAHTVG FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 AND MAPK3 which are phosphorylated upon activation of EPHA7. Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TTAHTVG EC EC 2.7.10.1 TTAHTVG PD 3NRU; 3H8M; 3DKO; 2REI TTAHTVG SQ MVFQTRYPSWIILCYIWLLRFAHTGEAQAAKEVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCWSIIENLAIFPDTVTGSEFSSLVEVRGTCVSSAEEEAENAPRMHCSAEGEWLVPIGKCICKAGYQQKGDTCEPCGRGFYKSSSQDLQCSRCPTHSFSDKEGSSRCECEDGYYRAPSDPPYVACTRPPSAPQNLIFNINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNIGYMPQQTGLEDNYVTVMDLLAHANYTFEVEAVNGVSDLSRSQRLFAAVSITTGQAAPSQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKDQRERTYSTVKTKSTSASINNLKPGTVYVFQIRAFTAAGYGNYSPRLDVATLEEATGKMFEATAVSSEQNPVIIIAVVAVAGTIILVFMVFGFIIGRRHCGYSKADQEGDEELYFHFKFPGTKTYIDPETYEDPNRAVHQFAKELDASCIKIERVIGAGEFGEVCSGRLKLPGKRDVAVAIKTLKVGYTEKQRRDFLCEASIMGQFDHPNVVHLEGVVTRGKPVMIVIEFMENGALDAFLRKHDGQFTVIQLVGMLRGIAAGMRYLADMGYVHRDLAARNILVNSNLVCKVSDFGLSRVIEDDPEAVYTTTGGKIPVRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPAPMDCPAGLHQLMLDCWQKERAERPKFEQIVGILDKMIRNPNSLKTPLGTCSRPISPLLDQNTPDFTTFCSVGEWLQAIKMERYKDNFTAAGYNSLESVARMTIEDVMSLGITLVGHQKKIMSSIQTMRAQMLHLHGTGIQV TTAHTVG TT Literature-reported TTHZ2LW ID TTHZ2LW TTHZ2LW TN Ephrin type-A receptor 8 (EPHA8) TTHZ2LW UP P29322 TTHZ2LW UC EPHA8_HUMAN TTHZ2LW BC Kinase TTHZ2LW SN hEK3; Tyrosine-protein kinase receptor EEK; KIAA1459; EPH-like kinase 3; EPH- and ELK-related kinase; EK3; EEK TTHZ2LW GN EPHA8 TTHZ2LW FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system plays also a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth. Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TTHZ2LW EC EC 2.7.10.1 TTHZ2LW PD 3KUL; 1X5L; 1UCV TTHZ2LW SQ MAPARGRLPPALWVVTAAAAAATCVSAARGEVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNSMPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGACLAILSLRIYYKKCPAMVRNLAAFSEAVTGADSSSLVEVRGQCVRHSEERDTPKMYCSAEGEWLVPIGKCVCSAGYEERRDACVACELGFYKSAPGDQLCARCPPHSHSAAPAAQACHCDLSYYRAALDPPSSACTRPPSAPVNLISSVNGTSVTLEWAPPLDPGGRSDITYNAVCRRCPWALSRCEACGSGTRFVPQQTSLVQASLLVANLLAHMNYSFWIEAVNGVSDLSPEPRRAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKDKEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSAGCGRFSQAMEVETGKPRPRYDTRTIVWICLTLITGLVVLLLLLICKKRHCGYSKAFQDSDEEKMHYQNGQAPPPVFLPLHHPPGKLPEPQFYAEPHTYEEPGRAGRSFTREIEASRIHIEKIIGSGDSGEVCYGRLRVPGQRDVPVAIKALKAGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDTFLRTHDGQFTIMQLVGMLRGVGAGMRYLSDLGYVHRDLAARNVLVDSNLVCKVSDFGLSRVLEDDPDAAYTTTGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNRDVISSVEEGYRLPAPMGCPHALHQLMLDCWHKDRAQRPRFSQIVSVLDALIRSPESLRATATVSRCPPPAFVRSCFDLRGGSGGGGGLTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLTSTQGPRRHL TTHZ2LW TT Literature-reported TT8MDAC ID TT8MDAC TT8MDAC TN Ephrin type-B receptor 1 (EPHB1) TT8MDAC UP P54762 TT8MDAC UC EPHB1_HUMAN TT8MDAC BC Kinase TT8MDAC SN hEK6; Tyrosine-protein kinase receptor EPH-2; Neuronally-expressed EPH-related tyrosine kinase; EPHT2; EPH-like kinase 6; EPH tyrosine kinase 2; ELK; EK6 TT8MDAC GN EPHB1 TT8MDAC FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation. Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TT8MDAC EC EC 2.7.10.1 TT8MDAC PD 5MJB; 5MJA; 3ZFX; 2EAO; 2DJS TT8MDAC SQ MALDYLLLLLLASAVAAMEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKPGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPAEASPICTCRTGYYRADFDPPEVACTSVPSGPRNVISIVNETSIILEWHPPRETGGRDDVTYNIICKKCRADRRSCSRCDDNVEFVPRQLGLTECRVSISSLWAHTPYTFDIQAINGVSSKSPFPPQHVSVNITTNQAAPSTVPIMHQVSATMRSITLSWPQPEQPNGIILDYEIRYYEKEHNEFNSSMARSQTNTARIDGLRPGMVYVVQVRARTVAGYGKFSGKMCFQTLTDDDYKSELREQLPLIAGSAAAGVVFVVSLVAISIVCSRKRAYSKEAVYSDKLQHYSTGRGSPGMKIYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVYKGRLKLPGKREIYVAIKTLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLAEMNYVHRDLAARNILVNSNLVCKVSDFGLSRYLQDDTSDPTYTSSLGGKIPVRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPMDCPAALHQLMLDCWQKDRNSRPRFAEIVNTLDKMIRNPASLKTVATITAVPSQPLLDRSIPDFTAFTTVDDWLSAIKMVQYRDSFLTAGFTSLQLVTQMTSEDLLRIGITLAGHQKKILNSIHSMRVQISQSPTAMA TT8MDAC TT Literature-reported TT5LM7U ID TT5LM7U TT5LM7U TN Ephrin type-B receptor 3 (EPHB3) TT5LM7U UP P54753 TT5LM7U UC EPHB3_HUMAN TT5LM7U BC Kinase TT5LM7U SN hEK2; Tyrosine-protein kinase TYRO6; TYRO6; Embryonic kinase 2; ETK2; EPH-like tyrosine kinase 2; EPH-like kinase 2; EK2 TT5LM7U GN EPHB3 TT5LM7U FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt. Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TT5LM7U EC EC 2.7.10.1 TT5LM7U PD 5L6P; 5L6O; 3ZFY; 3P1I TT5LM7U SQ MARARPPPPPSPPPGLLPLLPPLLLLPLLLLPAGCRALEETLMDTKWVTSELAWTSHPESGWEEVSGYDEAMNPIRTYQVCNVRESSQNNWLRTGFIWRRDVQRVYVELKFTVRDCNSIPNIPGSCKETFNLFYYEADSDVASASSPFWMENPYVKVDTIAPDESFSRLDAGRVNTKVRSFGPLSKAGFYLAFQDQGACMSLISVRAFYKKCASTTAGFALFPETLTGAEPTSLVIAPGTCIPNAVEVSVPLKLYCNGDGEWMVPVGACTCATGHEPAAKESQCRPCPPGSYKAKQGEGPCLPCPPNSRTTSPAASICTCHNNFYRADSDSADSACTTVPSPPRGVISNVNETSLILEWSEPRDLGGRDDLLYNVICKKCHGAGGASACSRCDDNVEFVPRQLGLTERRVHISHLLAHTRYTFEVQAVNGVSGKSPLPPRYAAVNITTNQAAPSEVPTLRLHSSSGSSLTLSWAPPERPNGVILDYEMKYFEKSEGIASTVTSQMNSVQLDGLRPDARYVVQVRARTVAGYGQYSRPAEFETTSERGSGAQQLQEQLPLIVGSATAGLVFVVAVVVIAIVCLRKQRHGSDSEYTEKLQQYIAPGMKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLKQPGRREVFVAIKTLKVGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMILTEFMENCALDSFLRLNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDPSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAVEQDYRLPPPMDCPTALHQLMLDCWVRDRNLRPKFSQIVNTLDKLIRNAASLKVIASAQSGMSQPLLDRTVPDYTTFTTVGDWLDAIKMGRYKESFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRLQMNQTLPVQV TT5LM7U TT Literature-reported TTI1FPZ ID TTI1FPZ TTI1FPZ TN Epithelial discoidin domain receptor 1 (DDR1) TTI1FPZ UP Q08345 TTI1FPZ UC DDR1_HUMAN TTI1FPZ BC Kinase TTI1FPZ SN Tyrosine-protein kinase CAK; Tyrosine kinase DDR; TRKE; TRK E; RTK6; Protein-tyrosine kinase RTK-6; Protein-tyrosine kinase 3A; PTK3A; NTRK4; NEP; Mammary carcinoma kinase 10; MCK-10; HGK2; Epithelial discoidin domain-containing receptor 1; EDDR1; Discoidin receptor tyrosine kinase; Cell adhesion kinase; CD167a; CD167 antigen-like family member A TTI1FPZ GN DDR1 TTI1FPZ FC Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing. Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11. Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. TTI1FPZ EC EC 2.7.10.1 TTI1FPZ PD 6HP9; 6GWR; 6FIQ; 6FIO; 6FIN TTI1FPZ SQ MGPEALSSLLLLLLVASGDADMKGHFDPAKCRYALGMQDRTIPDSDISASSSWSDSTAARHSRLESSDGDGAWCPAGSVFPKEEEYLQVDLQRLHLVALVGTQGRHAGGLGKEFSRSYRLRYSRDGRRWMGWKDRWGQEVISGNEDPEGVVLKDLGPPMVARLVRFYPRADRVMSVCLRVELYGCLWRDGLLSYTAPVGQTMYLSEAVYLNDSTYDGHTVGGLQYGGLGQLADGVVGLDDFRKSQELRVWPGYDYVGWSNHSFSSGYVEMEFEFDRLRAFQAMQVHCNNMHTLGARLPGGVECRFRRGPAMAWEGEPMRHNLGGNLGDPRARAVSVPLGGRVARFLQCRFLFAGPWLLFSEISFISDVVNNSSPALGGTFPPAPWWPPGPPPTNFSSLELEPRGQQPVAKAEGSPTAILIGCLVAIILLLLLIIALMLWRLHWRRLLSKAERRVLEEELTVHLSVPGDTILINNRPGPREPPPYQEPRPRGNPPHSAPCVPNGSALLLSNPAYRLLLATYARPPRGPGPPTPAWAKPTNTQAYSGDYMEPEKPGAPLLPPPPQNSVPHYAEADIVTLQGVTGGNTYAVPALPPGAVGDGPPRVDFPRSRLRFKEKLGEGQFGEVHLCEVDSPQDLVSLDFPLNVRKGHPLLVAVKILRPDATKNARNDFLKEVKIMSRLKDPNIIRLLGVCVQDDPLCMITDYMENGDLNQFLSAHQLEDKAAEGAPGDGQAAQGPTISYPMLLHVAAQIASGMRYLATLNFVHRDLATRNCLVGENFTIKIADFGMSRNLYAGDYYRVQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEVLMLCRAQPFGQLTDEQVIENAGEFFRDQGRQVYLSRPPACPQGLYELMLRCWSRESEQRPPFSQLHRFLAEDALNTV TTI1FPZ TT Patented-recorded TT6QY3J ID TT6QY3J TT6QY3J TN ERK activator kinase 7 (MAP2K7) TT6QY3J UP O14733 TT6QY3J UC MP2K7_HUMAN TT6QY3J BC Kinase TT6QY3J SN Stress-activated protein kinase kinase 4; SKK4; SAPKK4; SAPKK-4; SAPK kinase 4; PRKMK7; Mitogen-activated protein kinase kinase 7; MKK7; MEK7; MEK 7; MAPKK 7; MAPK/ERK kinase7; MAPK/ERK kinase 7; MAP kinase kinase 7; JNKK2; JNKK 2; JNK-activating kinase 2; JNK kinase 2; JNK activating kinase 2; Dual specificity mitogen-activated protein kinase kinase 7; C-Jun N-terminal kinase kinase 2 TT6QY3J GN MAP2K7 TT6QY3J FC Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by proinflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Part of a non-canonical MAPK signaling pathway, composed of the upstream MAP3K12 kinase and downstream MAP kinases MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated transcription of APP in response to APOE. Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. TT6QY3J EC EC 2.7.12.2 TT6QY3J PD 6QHR; 6QHO; 6QG7; 6QG4; 6QFT TT6QY3J SQ MAASSLEQKLSRLEAKLKQENREARRRIDLNLDISPQRPRPTLQLPLANDGGSRSPSSESSPQHPTPPARPRHMLGLPSTLFTPRSMESIEIDQKLQEIMKQTGYLTIGGQRYQAEINDLENLGEMGSGTCGQVWKMRFRKTGHVIAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVQCFGTFITNTDVFIAMELMGTCAEKLKKRMQGPIPERILGKMTVAIVKALYYLKEKHGVIHRDVKPSNILLDERGQIKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDPTKPDYDIRADVWSLGISLVELATGQFPYKNCKTDFEVLTKVLQEEPPLLPGHMGFSGDFQSFVKDCLTKDHRKRPKYNKLLEHSFIKRYETLEVDVASWFKDVMAKTESPRTSGVLSQPHLPFFR TT6QY3J TT Literature-reported TT6QY3J FM Kinase TT1PL7M ID TT1PL7M TT1PL7M TN E-selectin messenger RNA (SELE mRNA) TT1PL7M UP P16581 TT1PL7M UC LYAM2_HUMAN TT1PL7M BC mRNA target TT1PL7M SN Leukocyte-endothelial cell adhesion molecule 2 (mRNA); LECAM2 (mRNA); Endothelial leukocyte adhesion molecule 1 (mRNA); ELAM1 (mRNA); ELAM-1 (mRNA); E-selectin (mRNA); CD62E antigen (mRNA); CD62E (mRNA); CD62 antigen-like family member E (mRNA) TT1PL7M GN SELE TT1PL7M FC Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis. Cell-surface glycoprotein having a role in immunoadhesion. TT1PL7M PD 6EYK; 6EYJ; 6EYI; 4CSY; 4C16 TT1PL7M SQ MIASQFLSALTLVLLIKESGAWSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVWVWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCYTAACTNTSCSGHGECVETINNYTCKCDPGFSGLKCEQIVNCTALESPEHGSLVCSHPLGNFSYNSSCSISCDRGYLPSSMETMQCMSSGEWSAPIPACNVVECDAVTNPANGFVECFQNPGSFPWNTTCTFDCEEGFELMGAQSLQCTSSGNWDNEKPTCKAVTCRAVRQPQNGSVRCSHSPAGEFTFKSSCNFTCEEGFMLQGPAQVECTTQGQWTQQIPVCEAFQCTALSNPERGYMNCLPSASGSFRYGSSCEFSCEQGFVLKGSKRLQCGPTGEWDNEKPTCEAVRCDAVHQPPKGLVRCAHSPIGEFTYKSSCAFSCEEGFELHGSTQLECTSQGQWTEEVPSCQVVKCSSLAVPGKINMSCSGEPVFGTVCKFACPEGWTLNGSAARTCGATGHWSGLLPTCEAPTESNIPLVAGLSAAGLSLLTLAPFLLWLRKCLRKAKKFVPASSCQSLESDGSYQKPSYIL TT1PL7M TT Literature-reported TT1PL7M FM mRNA target TT1PL7M KE hsa04514:Cell adhesion molecules (CAMs); hsa04668:TNF signaling pathway; hsa05143:African trypanosomiasis; hsa05144:Malaria TT1PL7M RC R-HSA-202733:Cell surface interactions at the vascular wall TTL1WGS ID TTL1WGS TTL1WGS TN Estradiol 17 beta-dehydrogenase 4 (HSD17B4) TTL1WGS UP P51659 TTL1WGS UC DHB4_HUMAN TTL1WGS BC Short-chain dehydrogenases reductase TTL1WGS SN MFE-2; HSD17B4; DBP; D-bifunctional protein; 17-beta-hydroxysteroid dehydrogenase 4; 17-beta-HSD 4; 17 beta-hydroxysteroid dehydrogenase type 4 TTL1WGS GN HSD17B4 TTL1WGS FC Bifunctional enzymeacting on the peroxisomal beta- oxidation pathway for fatty acids. Catalyzes the formation of 3- ketoacyl-CoA intermediates from both straight-chain and 2-methyl- branched-chain fatty acids. TTL1WGS PD 1ZBQ; 1S9C; 1IKT TTL1WGS SQ MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRQKNHPMTPEAVKANWKKICDFENASKPQSIQESTGSIIEVLSKIDSEGGVSANHTSRATSTATSGFAGAIGQKLPPFSYAYTELEAIMYALGVGASIKDPKDLKFIYEGSSDFSCLPTFGVIIGQKSMMGGGLAEIPGLSINFAKVLHGEQYLELYKPLPRAGKLKCEAVVADVLDKGSGVVIIMDVYSYSEKELICHNQFSLFLVGSGGFGGKRTSDKVKVAVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNAYVDLAPTSGTSAKTPSEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNIGAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL TTL1WGS TT Literature-reported TTL1WGS KE hsa00120:Primary bile acid biosynthesis; hsa01100:Metabolic pathways; hsa04146:Peroxisome TT7LTUJ ID TT7LTUJ TT7LTUJ TN Fas messenger RNA (FAS mRNA) TT7LTUJ UP P25445 TT7LTUJ UC TNR6_HUMAN TT7LTUJ BC mRNA target TT7LTUJ SN Tumor necrosis factor receptor superfamily member 6 (mRNA); TNFRSF6 (mRNA); FASLG receptor (mRNA); FAS1 (mRNA); CD95 (mRNA); Apoptosis-mediating surface antigen FAS (mRNA); Apo-1 antigen (mRNA); APT1 (mRNA) TT7LTUJ GN FAS TT7LTUJ FC The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (in vitro). Receptor for TNFSF6/FASLG. TT7LTUJ PD 3TJE; 3THM; 3EZQ; 3EWT; 2NA7 TT7LTUJ SQ MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCRKHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKKANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV TT7LTUJ TT Literature-reported TT7LTUJ FM mRNA target TT7LTUJ KE hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04115:p53 signaling pathway; hsa04210:Apoptosis; hsa04650:Natural killer cell mediated cytotoxicity; hsa04668:TNF signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04940:Type I diabetes mellitus; hsa05010:Alzheimer's disease; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05320:Autoimmune thyroid disease; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease TT7LTUJ RC R-HSA-75157:FasL/ CD95L signaling TTO7014 ID TTO7014 TTO7014 TN FasL messenger RNA (FASLG mRNA) TTO7014 UP P48023 TTO7014 UC TNFL6_HUMAN TTO7014 BC mRNA target TTO7014 SN Tumor necrosis factor ligand superfamily member 6 (mRNA); TNFSF6 (mRNA); FasL (mRNA); Fas ligand (mRNA); FAS antigen ligand (mRNA); CD95L (mRNA); CD95-L (mRNA); CD95 ligand (mRNA); CD178 antigen (mRNA); CD178 (mRNA); Apoptosis antigen ligand (mRNA); APTL (mRNA); APT1LG1 (mRNA) TTO7014 GN FASLG TTO7014 FC Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development. Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses. TNFRSF6/FAS-mediated apoptosis has also a role in the induction of peripheral tolerance. Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis. Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells. TTO7014 PD 5L36; 5L19; 4MSV; 1BZI TTO7014 SQ MQQPFNYPYPQIYWVDSSASSPWAPPGTVLPCPTSVPRRPGQRRPPPPPPPPPLPPPPPPPPLPPLPLPPLKKRGNHSTGLCLLVMFFMVLVALVGLGLGMFQLFHLQKELAELRESTSQMHTASSLEKQIGHPSPPPEKKELRKVAHLTGKSNSRSMPLEWEDTYGIVLLSGVKYKKGGLVINETGLYFVYSKVYFRGQSCNNLPLSHKVYMRNSKYPQDLVMMEGKMMSYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESQTFFGLYKL TTO7014 TT Literature-reported TTO7014 FM mRNA target TTO7014 KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04068:FoxO signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04650:Natural killer cell mediated cytotoxicity; hsa04722:Neurotrophin signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04940:Type I diabetes mellitus; hsa05142:Chagas disease (American trypanosomiasis); hsa05143:African trypanosomiasis; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05320:Autoimmune thyroid disease; hsa05330:Allograft rejection; hsa05332:Graft-versus-host disease TTO7014 RC R-HSA-75157:FasL/ CD95L signaling TTHY0FT ID TTHY0FT TTHY0FT TN FK506-binding protein 4 (FKBP4) TTHY0FT UP Q02790 TTHY0FT UC FKBP4_HUMAN TTHY0FT BC Cis-trans-isomerase TTHY0FT SN p59; Peptidyl-prolyl cis-trans isomerase FKBP4; PPIase FKBP4; P59 protein; Immunophilin FKBP52; HSP-binding immunophilin; HSP binding immunophilin; HBI; FKBP59; FKBP52 protein; FKBP52; FKBP-52; FKBP-4; 59 kDa immunophilin; 52 kDa FKBP; 52 kDa FK506-binding protein; 52 kDa FK506 binding protein TTHY0FT GN FKBP4 TTHY0FT FC Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria. Immunophilin protein with PPIase and co-chaperone activities. TTHY0FT EC EC 5.2.1.8 TTHY0FT PD 4TW8; 4LAY; 4LAX; 4LAW; 4LAV TTHY0FT SQ MTAEEMKATESGAQSAPLPMEGVDISPKQDEGVLKVIKREGTGTEMPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAIATMKVGEVCHITCKPEYAYGSAGSPPKIPPNATLVFEVELFEFKGEDLTEEEDGGIIRRIQTRGEGYAKPNEGAIVEVALEGYYKDKLFDQRELRFEIGEGENLDLPYGLERAIQRMEKGEHSIVYLKPSYAFGSVGKEKFQIPPNAELKYELHLKSFEKAKESWEMNSEEKLEQSTIVKERGTVYFKEGKYKQALLQYKKIVSWLEYESSFSNEEAQKAQALRLASHLNLAMCHLKLQAFSAAIESCNKALELDSNNEKGLFRRGEAHLAVNDFELARADFQKVLQLYPNNKAAKTQLAVCQQRIRRQLAREKKLYANMFERLAEEENKAKAEASSGDHPTDTEMKEEQKSNTAGSQSQVETEA TTHY0FT TT Literature-reported TTHY0FT FM Cis-trans-isomerases TT0J5KQ ID TT0J5KQ TT0J5KQ TN FK506-binding protein 5 (FKBP5) TT0J5KQ UP Q13451 TT0J5KQ UC FKBP5_HUMAN TT0J5KQ BC Cis-trans-isomerase TT0J5KQ SN Peptidyl-prolyl cis-trans isomerase FKBP5; PPIase FKBP5; HSP90-binding immunophilin; FKBP54; FKBP51; FKBP-51; FKBP-5; FF1 antigen; Androgen-regulated protein 6; AIG6; 54 kDa progesterone receptor-associated immunophilin; 51 kDa FKBP; 51 kDa FK506-binding protein TT0J5KQ GN FKBP5 TT0J5KQ FC Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Immunophilin protein with PPIase and co-chaperone activities. TT0J5KQ EC EC 5.2.1.8 TT0J5KQ PD 5OMP; 5OBK; 5NJX; 5DIV; 5DIU TT0J5KQ SQ MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV TT0J5KQ TT Literature-reported TT0J5KQ FM Cis-trans-isomerases TTLRVIA ID TTLRVIA TTLRVIA TN Forkhead box O1A messenger RNA (FOXO1 mRNA) TTLRVIA UP Q12778 TTLRVIA UC FOXO1_HUMAN TTLRVIA BC mRNA target TTLRVIA SN Forkhead in rhabdomyosarcoma (mRNA); Forkhead box protein O1A (mRNA); Forkhead box protein O1 (mRNA); FOXO1A (mRNA); FKHR (mRNA) TTLRVIA GN FOXO1 TTLRVIA FC Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner. Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling. Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. TTLRVIA PD 5DUI; 4LG0; 3COA; 3CO7; 3CO6 TTLRVIA SQ MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGSAAANPDAAAGLPSASAAAVSADFMSNLSLLEESEDFPQAPGSVAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQPPPPGPLSQHPPVPPAAAGPLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRSRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGEGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPIQTLQDNKSSYGGMSQYNCAPGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVMMGPNSVMSTYGSQASHNKMMNPSSHTHPGHAQQTSAVNGRPLPHTVSTMPHTSGMNRLTQVKTPVQVPLPHPMQMSALGGYSSVSSCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG TTLRVIA TT Literature-reported TTLRVIA FM mRNA target TTLRVIA KE hsa04068:FoxO signaling pathway; hsa04152:AMPK signaling pathway; hsa04910:Insulin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04922:Glucagon signaling pathway; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05215:Prostate cancer TTLRVIA RC R-HSA-198693:AKT phosphorylates targets in the nucleus; R-HSA-210745:Regulation of gene expression in beta cells; R-HSA-211163:AKT-mediated inactivation of FOXO1A; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer; R-HSA-5687128:MAPK6/MAPK4 signaling TTWQ8IY ID TTWQ8IY TTWQ8IY TN Fungal Sterol 24-C-methyltransferase (Fung erg6) TTWQ8IY UP Q96WX4 TTWQ8IY UC ERG6_PNEC8 TTWQ8IY BC Methyltransferase TTWQ8IY SN erg6; SAM:SMT; S-adenosyl-L-methionine:sterol C-24 methyl transferase; S-adenosyl-L-methionine-C-24-delta-sterol-methyltransferase TTWQ8IY GN Fung erg6 TTWQ8IY FC Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. TTWQ8IY EC EC 2.1.1.- TTWQ8IY SQ MSFELERIDIEKDREFSEIMHGKDAAKERGLLSSFRKDKEAQKIALDSYFGFWGDKCTSEKNDIHQQERFKFYATLTRHYYNLVTDFYEYGWSTSFHFCRFAKDESFSQAIARHEHYIALHAGIREGETVLDVGCGVGGPACQISVFTGANIVGLNNNDYQIQRAKYYSEKKGLSDKLKFIKGDFMQMPFPENSFDKIYSIEATIHAPSLEGVYSEIYRVLKPGGLYASYEWVMLNKYDENDPEHQQIVYGIEIGDSIPKISKIGEAEAALIKVGFEIIHSEELSTKNSPLPWYYYLDGDLRKVRSFRDFISIARMTTIGKWLISSFIGLMEFIGLLPKGSKKVNDILLVAADSLVKAGKKEIFTPMQLWVCRKPLV TTWQ8IY TT Literature-reported TTCEJ4F ID TTCEJ4F TTCEJ4F TN G1/S-specific cyclin-E1 (CCNE1) TTCEJ4F UP P24864 TTCEJ4F UC CCNE1_HUMAN TTCEJ4F SN G1/S-specific cyclin E; Cyclin E; CCNE TTCEJ4F GN CCNE1 TTCEJ4F FC Essential for the control of the cell cycle at the G1/S (start) transition. TTCEJ4F PD 5L2W; 1W98 TTCEJ4F SQ MPRERRERDAKERDTMKEDGGAEFSARSRKRKANVTVFLQDPDEEMAKIDRTARDQCGSQPWDNNAVCADPCSLIPTPDKEDDDRVYPNSTCKPRIIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFFDRYMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVYMQVAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVPFAMVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKAMLSEQNRASPLPSGLLTPPQSGKKQSSGPEMA TTCEJ4F TT Literature-reported TTCEJ4F KE hsa04110:Cell cycle; hsa04114:Oocyte meiosis; hsa04115:p53 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa05161:Hepatitis B; hsa05162:Measles; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05206:MicroRNAs in cancer; hsa05215:Prostate cancer; hsa05222:Small cell lung cancer TTCEJ4F RC R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-1538133:G0 and Early G1; R-HSA-187577:SCF(Skp2)-mediated degradation of p27/p21; R-HSA-2559586:DNA Damage/Telomere Stress Induced Senescence; R-HSA-69202:Cyclin E associated events during G1/S transition; R-HSA-69205:G1/S-Specific Transcription; R-HSA-69563:p53-Dependent G1 DNA Damage Response TTX3HNZ ID TTX3HNZ TTX3HNZ TN Galanin receptor type 1 (GAL1-R) TTX3HNZ UP P47211 TTX3HNZ UC GALR1_HUMAN TTX3HNZ BC GPCR rhodopsin TTX3HNZ SN GALR1; GALR-1; GALNR1; GALN1R; GAL1-R TTX3HNZ GN GALR1 TTX3HNZ FC The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity. Receptor for the hormone galanin. G protein-coupled peptide receptor activity. Neuropeptide binding. Peptide hormone binding. TTX3HNZ SQ MELAVGNLSEGNASWPEPPAPEPGPLFGIGVENFVTLVVFGLIFALGVLGNSLVITVLARSKPGKPRSTTNLFILNLSIADLAYLLFCIPFQATVYALPTWVLGAFICKFIHYFFTVSMLVSIFTLAAMSVDRYVAIVHSRRSSSLRVSRNALLGVGCIWALSIAMASPVAYHQGLFHPRASNQTFCWEQWPDPRHKKAYVVCTFVFGYLLPLLLICFCYAKVLNHLHKKLKNMSKKSEASKKKTAQTVLVVVVVFGISWLPHHIIHLWAEFGVFPLTPASFLFRITAHCLAYSNSSVNPIIYAFLSENFRKAYKQVFKCHIRKDSHLSDTKESKSRIDTPPSTNCTHV TTX3HNZ TT Literature-reported TTX3HNZ KE hsa04080:Neuroactive ligand-receptor interaction TTX3HNZ RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTBPW3J ID TTBPW3J TTBPW3J TN Galanin receptor type 2 (GAL2-R) TTBPW3J UP O43603 TTBPW3J UC GALR2_HUMAN TTBPW3J BC GPCR rhodopsin TTBPW3J SN GALR2; GALR-2; GALNR2; GAL2-R TTBPW3J GN GALR2 TTBPW3J FC The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)). Receptor for the hormone galanin and GALP. Receptor for the hormone spexin-1. TTBPW3J SQ MNVSGCPGAGNASQAGGGGGWHPEAVIVPLLFALIFLVGTVGNTLVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDGWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLSLLFSGPYLSYYRQSQLANLTVCHPAWSAPRRRAMDICTFVFSYLLPVLVLGLTYARTLRYLWRAVDPVAAGSGARRAKRKVTRMILIVAALFCLCWMPHHALILCVWFGQFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRTICAGLLGRAPGRASGRVCAAARGTHSGSVLERESSDLLHMSEAAGALRPCPGASQPCILEPCPGPSWQGPKAGDSILTVDVA TTBPW3J TT Literature-reported TTBPW3J KE hsa04080:Neuroactive ligand-receptor interaction TTBPW3J RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTSRXJW ID TTSRXJW TTSRXJW TN G-alpha-11 messenger RNA (GNA11 mRNA) TTSRXJW UP P29992 TTSRXJW UC GNA11_HUMAN TTSRXJW BC mRNA target TTSRXJW SN Guanine nucleotide-binding protein subunit alpha-11 (mRNA); Guanine nucleotide-binding protein G(y) subunit alpha (mRNA); GA11 (mRNA); G-protein subunit alpha-11 (mRNA); G alpha-11 (mRNA) TTSRXJW GN GNA11 TTSRXJW FC Acts as an activator of phospholipase C. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. TTSRXJW PD 6OIJ TTSRXJW SQ MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEKVTTFEHQYVSAIKTLWEDPGIQECYDRRREYQLSDSAKYYLTDVDRIATLGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV TTSRXJW TT Literature-reported TTSRXJW FM mRNA target TTSRXJW KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04540:Gap junction; hsa04725:Cholinergic synapse; hsa04730:Long-term depression; hsa04911:Insulin secretion; hsa04912:GnRH signaling pathway; hsa05142:Chagas disease (American trypanosomiasis); hsa05146:Amoebiasis; hsa05200:Pathways in cancer TTSRXJW RC R-HSA-399997:Acetylcholine regulates insulin secretion; R-HSA-416476:G alpha (q) signalling events; R-HSA-418592:ADP signalling through P2Y purinoceptor 1; R-HSA-428930:Thromboxane signalling through TP receptor; R-HSA-434316:Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion; R-HSA-456926:Thrombin signalling through proteinase activated receptors (PARs) TTZJRL0 ID TTZJRL0 TTZJRL0 TN Gamma-glutamyl hydrolase (GGH) TTZJRL0 UP Q92820 TTZJRL0 UC GGH_HUMAN TTZJRL0 BC Peptidase TTZJRL0 SN Human glutamyl hydrolase; Gamma-Glu-X carboxypeptidase; GGH; Conjugase TTZJRL0 GN GGH TTZJRL0 FC Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha- glutamate (folic acid) and free glutamate. May play an important role in the bioavailability ofdietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. TTZJRL0 EC EC 3.4.19.9 TTZJRL0 PD 1L9X TTZJRL0 SQ MASPGCLLCVLGLLLCGAASLELSRPHGDTAKKPIIGILMQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLISGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPIYTGNISSFQQCYIFD TTZJRL0 TT Literature-reported TTG0R8Z ID TTG0R8Z TTG0R8Z TN GAP SH3 domain-binding protein 1 (G3BP1) TTG0R8Z UP Q13283 TTG0R8Z UC G3BP1_HUMAN TTG0R8Z BC Acid anhydride hydrolase TTG0R8Z SN hDH VIII; Ras GTPase-activating protein-binding protein 1; G3BP-1; G3BP; ATP-dependent DNA helicase VIII TTG0R8Z GN G3BP1 TTG0R8Z FC Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS. Enhances also DDX58-induced type I interferon production probably by helping DDX58 at sensing pathogenic RNA. In addition, plays an essential role in stress granule formation. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase that plays an essential role in innate immunity. TTG0R8Z EC EC 3.6.4.12 TTG0R8Z PD 5FW5; 4IIA; 4FCM; 4FCJ; 3Q90 TTG0R8Z SQ MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ TTG0R8Z TT Literature-reported TTG0R8Z FM Acid anhydrides hydrolase TT3LE7P ID TT3LE7P TT3LE7P TN Gastric alcohol dehydrogenase (ADH7) TT3LE7P UP P40394 TT3LE7P UC ADH7_HUMAN TT3LE7P BC Short-chain dehydrogenases reductase TT3LE7P SN Alcohol dehydrogenase class IV mu/sigma chain; Alcohol dehydrogenase class 4 mu/sigma chain; ADH7 TT3LE7P GN ADH7 TT3LE7P FC Could function in retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation. Medium-chain (octanol) and aromatic (m-nitrobenzaldehyde) compounds are the best substrates. Ethanol is not a good substrate but at the high ethanol concentrations reached in the digestive tract, it plays a role in the ethanol oxidation and contributes to the first pass ethanol metabolism. TT3LE7P EC EC 1.1.1.1 TT3LE7P PD 1D1T; 1D1S; 1AGN TT3LE7P SQ MFAEIQIQDKDRMGTAGKVIKCKAAVLWEQKQPFSIEEIEVAPPKTKEVRIKILATGICRTDDHVIKGTMVSKFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPDGNLCIRSDITGRGVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEKVCLIGCGFSTGYGAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDKFEKAMAVGATECISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGTSVVVGVPPSAKMLTYDPMLLFTGRTWKGCVFGGLKSRDDVPKLVTEFLAKKFDLDQLITHVLPFKKISEGFELLNSGQSIRTVLTF TT3LE7P TT Literature-reported TT19JIZ ID TT19JIZ TT19JIZ TN Glucose-6-phosphate isomerase (GPI) TT19JIZ UP P06744 TT19JIZ UC G6PI_HUMAN TT19JIZ BC Intramolecular oxidoreductases TT19JIZ SN Sperm antigen 36; SA-36; Phosphohexose isomerase; Phosphoglucose isomerase; PHI; PGI; Neuroleukin; NLK; GPI; Autocrine motility factor; AMF TT19JIZ GN GPI TT19JIZ FC Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. TT19JIZ EC EC 5.3.1.9 TT19JIZ PD 1NUH; 1JLH; 1JIQ; 1IRI; 1IAT TT19JIZ SQ MAALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGHILVDYSKNLVTEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLHVALRNRSNTPILVDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKTITDVINIGIGGSDLGPLMVTEALKPYSSGGPRVWYVSNIDGTHIAKTLAQLNPESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNTTKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLALLGIWYINCFGCETHAMLPYDQYLHRFAAYFQQGDMESNGKYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKMIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMRGKSTEEARKELQAAGKSPEDLERLLPHKVFEGNRPTNSIVFTKLTPFMLGALVAMYEHKIFVQGIIWDINSFDQWGVELGKQLAKKIEPELDGSAQVTSHDASTNGLINFIKQQREARVQ TT19JIZ TT Literature-reported TTUWQLT ID TTUWQLT TTUWQLT TN Glutamate carboxypeptidase III (NAALAD2) TTUWQLT UP Q9Y3Q0 TTUWQLT UC NALD2_HUMAN TTUWQLT BC Peptidase TTUWQLT SN NAALADase II; NAALAD2 TTUWQLT GN NAALAD2 TTUWQLT FC Has N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Also exhibits a dipeptidyl-peptidase IV type activity. Inactivate the peptide neurotransmitter N- acetylaspartylglutamate. TTUWQLT EC EC 3.4.17.21 TTUWQLT PD 3FF3; 3FEE; 3FED; 3FEC TTUWQLT SQ MAESRGRLYLWMCLAAALASFLMGFMVGWFIKPLKETTTSVRYHQSIRWKLVSEMKAENIKSFLRSFTKLPHLAGTEQNFLLAKKIQTQWKKFGLDSAKLVHYDVLLSYPNETNANYISIVDEHETEIFKTSYLEPPPDGYENVTNIVPPYNAFSAQGMPEGDLVYVNYARTEDFFKLEREMGINCTGKIVIARYGKIFRGNKVKNAMLAGAIGIILYSDPADYFAPEVQPYPKGWNLPGTAAQRGNVLNLNGAGDPLTPGYPAKEYTFRLDVEEGVGIPRIPVHPIGYNDAEILLRYLGGIAPPDKSWKGALNVSYSIGPGFTGSDSFRKVRMHVYNINKITRIYNVVGTIRGSVEPDRYVILGGHRDSWVFGAIDPTSGVAVLQEIARSFGKLMSKGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKILQERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEIPSPDDGFESKSLYESWLEKDPSPENKNLPRINKLGSGSDFEAYFQRLGIASGRARYTKNKKTDKYSSYPVYHTIYETFELVEKFYDPTFKKQLSVAQLRGALVYELVDSKIIPFNIQDYAEALKNYAASIYNLSKKHDQQLTDHGVSFDSLFSAVKNFSEAASDFHKRLIQVDLNNPIAVRMMNDQLMLLERAFIDPLGLPGKLFYRHIIFAPSSHNKYAGESFPGIYDAIFDIENKANSRLAWKEVKKHISIAAFTIQAAAGTLKEVL TTUWQLT TT Literature-reported TTYAHBP ID TTYAHBP TTYAHBP TN Glutathione peroxidase (GPX1) TTYAHBP UP P07203 TTYAHBP UC GPX1_HUMAN TTYAHBP BC Peroxidases TTYAHBP SN GSHPx-1; GPX1; Cellular glutathione peroxidase TTYAHBP GN GPX1 TTYAHBP FC Protects the hemoglobin in erythrocytes from oxidative breakdown. TTYAHBP EC EC 1.11.1.9 TTYAHBP PD 2F8A TTYAHBP SQ MCAARLAAAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRRFQTIDIEPDIEALLSQGPSCA TTYAHBP TT Literature-reported TTKTEAH ID TTKTEAH TTKTEAH TN Glycerol-3-phosphate dehydrogenase (GPD1) TTKTEAH UP P21695 TTKTEAH UC GPDA_HUMAN TTKTEAH BC Short-chain dehydrogenases reductase TTKTEAH SN Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic; GPDH-C; GPD-C TTKTEAH GN GPD1 TTKTEAH FC Catalyzes the reversible redox conversion of dihydroxyacetone phosphate (a.k.a. glycerone phosphate, outdated) to sn-glycerol 3-phosphate. serves as a major link between carbohydrate metabolism and lipid metabolism. A major contributor of electrons to the electron transport chain in the mitochondria. TTKTEAH EC EC 1.1.1.8 TTKTEAH PD 6E8Z; 6E8Y; 6.00E+90; 1X0X; 1X0V TTKTEAH SQ MASKKVCIVGSGNWGSAIAKIVGGNAAQLAQFDPRVTMWVFEEDIGGKKLTEIINTQHENVKYLPGHKLPPNVVAVPDVVQAAEDADILIFVVPHQFIGKICDQLKGHLKANATGISLIKGVDEGPNGLKLISEVIGERLGIPMSVLMGANIASEVADEKFCETTIGCKDPAQGQLLKELMQTPNFRITVVQEVDTVEICGALKNVVAVGAGFCDGLGFGDNTKAAVIRLGLMEMIAFAKLFCSGPVSSATFLESCGVADLITTCYGGRNRKVAEAFARTGKSIEQLEKELLNGQKLQGPETARELYSILQHKGLVDKFPLFMAVYKVCYEGQPVGEFIHCLQNHPEHM TTKTEAH TT Literature-reported TTFC29G ID TTFC29G TTFC29G TN Glycoprotein hormones alpha (CGA) TTFC29G UP P01215 TTFC29G UC GLHA_HUMAN TTFC29G BC Glycoprotein hormone TTFC29G SN Thyrotropin alpha chain; Thyroid-stimulating hormone alpha chain; TSH-alpha; Lutropin alpha chain; Luteinizing hormone alpha chain; LSH-alpha; Glycoprotein hormones alpha chain; Follitropin alpha chain; Follicle-stimulating hormone alpha chain; FSH-alpha; Chorionic gonadotrophin subunit alpha; Choriogonadotropin alpha chain; CG-alpha; Anterior pituitary glycoprotein hormones common subunit alpha TTFC29G GN CGA TTFC29G FC Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH, follitropin/follicle stimulating hormone/FSH and choriogonadotropin/CG. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways. TTFC29G PD 4MQW; 4AY9; 1XWD; 1XUL; 1QFW TTFC29G SQ MDYYRKYAAIFLVTLSVFLHVLHSAPDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS TTFC29G TT Literature-reported TTFC29G KE hsa04080:Neuroactive ligand-receptor interaction; hsa04912:GnRH signaling pathway; hsa04913:Ovarian steroidogenesis; hsa04917:Prolactin signaling pathway; hsa04918:Thyroid hormone synthesis; hsa05320:Autoimmune thyroid disease TTFC29G RC R-HSA-193048:Androgen biosynthesis; R-HSA-209968:Thyroxine biosynthesis; R-HSA-375281:Hormone ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events TTTFS8O ID TTTFS8O TTTFS8O TN GM-CSFR/IL-3R/IL-5R common beta messenger RNA (CSF2RB mRNA) TTTFS8O UP P32927 TTTFS8O UC IL3RB_HUMAN TTTFS8O BC mRNA target TTTFS8O SN IL5RB (mRNA); IL3RB (mRNA); IL-5R (mRNA); GM-CSF/IL-3/IL-5 receptor common beta subunit (mRNA); Cytokine receptor common subunit beta (mRNA); CDw131 (mRNA); CD131 (mRNA) TTTFS8O GN CSF2RB TTTFS8O FC High affinity receptor for interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor. TTTFS8O PD 5DWU; 4NKQ; 2NA9; 2NA8; 2GYS TTTFS8O SQ MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYIVSVQPRRAEKHIKSSVNIQMAPPSLNVTKDGDSYSLRWETMKMRYEHIDHTFEIQYRKDTATWKDSKTETLQNAHSMALPALEPSTRYWARVRVRTSRTGYNGIWSEWSEARSWDTESVLPMWVLALIVIFLTIAVLLALRFCGIYGYRLRRKWEEKIPNPSKSHLFQNGSAELWPPGSMSAFTSGSPPHQGPWGSRFPELEGVFPVGFGDSEVSPLTIEDPKHVCDPPSGPDTTPAASDLPTEQPPSPQPGPPAASHTPEKQASSFDFNGPYLGPPHSRSLPDILGQPEPPQEGGSQKSPPPGSLEYLCLPAGGQVQLVPLAQAMGPGQAVEVERRPSQGAAGSPSLESGGGPAPPALGPRVGGQDQKDSPVAIPMSSGDTEDPGVASGYVSSADLVFTPNSGASSVSLVPSLGLPSDQTPSLCPGLASGPPGAPGPVKSGFEGYVELPPIEGRSPRSPRNNPVPPEAKSPVLNPGERPADVSPTSPQPEGLLVLQQVGDYCFLPGLGPGPLSLRSKPSSPGPGPEIKNLDQAFQVKKPPGQAVPQVPVIQLFKALKQQDYLSLPPWEVNKPGEVC TTTFS8O TT Literature-reported TTTFS8O FM mRNA target TT42OGM ID TT42OGM TT42OGM TN Hematopoietic cell kinase (HCK) TT42OGM UP P08631 TT42OGM UC HCK_HUMAN TT42OGM BC Kinase TT42OGM SN p61Hck; p59Hck; p59-HCK/p60-HCK; Tyrosine-protein kinase HCK; Hemopoietic cell kinase TT42OGM GN HCK TT42OGM FC Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS. Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. TT42OGM EC EC 2.7.10.2 TT42OGM PD 5ZJ6; 5NUH; 5HCK; 5H0H; 5H0G TT42OGM SQ MGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIKPGPNSHNSNTPGIREAGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVPCMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP TT42OGM TT Patented-recorded TTWZRL4 ID TTWZRL4 TTWZRL4 TN Heme oxygenase 2 (HMOX2) TTWZRL4 UP P30519 TTWZRL4 UC HMOX2_HUMAN TTWZRL4 BC Paired donor oxygen oxidoreductase TTWZRL4 SN HO2; HO-2 TTWZRL4 GN HMOX2 TTWZRL4 FC Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. TTWZRL4 EC EC 1.14.14.18 TTWZRL4 PD 5UCA; 5UC9; 5UC8; 4WMH; 2RGZ TTWZRL4 SQ MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFILAAGVALAAGLLAWYYM TTWZRL4 TT Literature-reported TT8XSKJ ID TT8XSKJ TT8XSKJ TN Heparin cofactor II (SERPIND1) TT8XSKJ UP P05546 TT8XSKJ UC HEP2_HUMAN TT8XSKJ BC Serpin protein TT8XSKJ SN SERPIND1; Protease inhibitor leuserpin 2; HLS2; HC-II TT8XSKJ GN SERPIND1 TT8XSKJ FC Peptides at the N-terminal of HC-II have chemotactic activity for both monocytes and neutrophils. TT8XSKJ PD 6J12; 2NCW; 2NCV; 2NCU; 2NAT TT8XSKJ SQ MKHSLNALLIFLIITSAWGGSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDWIPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHGKSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPHKMSGMKTLEAQLTPRVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKLMGIRMLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATTVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPSRS TT8XSKJ TT Literature-reported TT8XSKJ KE hsa04610:Complement and coagulation cascades TT8XSKJ RC R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-140875:Common Pathway of Fibrin Clot Formation TTD96RW ID TTD96RW TTD96RW TN Hepatocyte growth factor activator (HGFAC) TTD96RW UP Q04756 TTD96RW UC HGFA_HUMAN TTD96RW BC Peptidase TTD96RW SN Hepatocyte growth factor activator long chain; HGFAC; HGFA; HGF activator TTD96RW GN HGFAC TTD96RW FC Activates hepatocyte growth factor (HGF) by convertingit from a single chain to a heterodimeric form. TTD96RW EC EC 3.4.21.- TTD96RW PD 3K2U; 2WUC; 2WUB; 2R0L; 2R0K TTD96RW SQ MGRWAWVPSPWPPPGLGPFLLLLLLLLLLPRGFQPQPGGNRTESPEPNATATPAIPTILVTSVTSETPATSAPEAEGPQSGGLPPPPRAVPSSSSPQAQALTEDGRPCRFPFRYGGRMLHACTSEGSAHRKWCATTHNYDRDRAWGYCVEATPPPGGPAALDPCASGPCLNGGSCSNTQDPQSYHCSCPRAFTGKDCGTEKCFDETRYEYLEGGDRWARVRQGHVEQCECFGGRTWCEGTRHTACLSSPCLNGGTCHLIVATGTTVCACPPGFAGRLCNIEPDERCFLGNGTGYRGVASTSASGLSCLAWNSDLLYQELHVDSVGAAALLGLGPHAYCRNPDNDERPWCYVVKDSALSWEYCRLEACESLTRVQLSPDLLATLPEPASPGRQACGRRHKKRTFLRPRIIGGSSSLPGSHPWLAAIYIGDSFCAGSLVHTCWVVSAAHCFSHSPPRDSVSVVLGQHFFNRTTDVTQTFGIEKYIPYTLYSVFNPSDHDLVLIRLKKKGDRCATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVADHKCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWINDRIRPPRRLVAPS TTD96RW TT Literature-reported TT2F3CD ID TT2F3CD TT2F3CD TN Hepatocyte nuclear factor 4-alpha (HNF4A) TT2F3CD UP P41235 TT2F3CD UC HNF4A_HUMAN TT2F3CD BC Nuclear hormone receptor TT2F3CD SN Transcription factor HNF-4; Transcription factor 14; TCF14; TCF-14; Nuclear receptor subfamily 2 group A member 1; NR2A1; HNF4; HNF-4-alpha TT2F3CD GN HNF4A TT2F3CD FC Activates the transcription of CYP2C38. Represses the CLOCK-ARNTL/BMAL1 transcriptional activity and is essential for circadian rhythm maintenance and period regulation in the liver and colon cells. Transcriptional regulator which controls the expression of hepatic genes during the transition of endodermal cells to hepatic progenitor cells, facilitating the recruitment of RNA pol II to the promoters of target genes. TT2F3CD PD 6CHT; 4IQR; 4B7W; 3FS1; 3CBB TT2F3CD SQ MRLSKTLVDMDMADYSAALDPAYTTLEFENVQVLTMGNDTSPSEGTNLNAPNSLGVSALCAICGDRATGKHYGASSCDGCKGFFRRSVRKNHMYSCRFSRQCVVDKDKRNQCRYCRLKKCFRAGMKKEAVQNERDRISTRRSSYEDSSLPSINALLQAEVLSRQITSPVSGINGDIRAKKIASIADVCESMKEQLLVLVEWAKYIPAFCELPLDDQVALLRAHAGEHLLLGATKRSMVFKDVLLLGNDYIVPRHCPELAEMSRVSIRILDELVLPFQELQIDDNEYAYLKAIIFFDPDAKGLSDPGKIKRLRSQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFIKLFGMAKIDNLLQEMLLGGSPSDAPHAHHPLHPHLMQEHMGTNVIVANTMPTHLSNGQMCEWPRPRGQAATPETPQPSPPGGSGSEPYKLLPGAVATIVKPLSAIPQPTITKQEVI TT2F3CD TT Literature-reported TT2F3CD FM Nuclear hormone receptor family TT2F3CD KE hsa04152:AMPK signaling pathway; hsa04950:Maturity onset diabetes of the young TT2F3CD RC R-HSA-383280:Nuclear Receptor transcription pathway TTGH73N ID TTGH73N TTGH73N TN Histone acetyltransferase p300 (EP300) TTGH73N UP Q09472 TTGH73N UC EP300_HUMAN TTGH73N BC Acyltransferase TTGH73N SN p300 HAT; Protein propionyltransferase p300; P300; Histone crotonyltransferase p300; Histone butyryltransferase p300; E1Aassociated protein p300; E1A-associated protein p300 TTGH73N GN EP300 TTGH73N FC Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1 or SIRT2. Acetylates 'Lys-131' of ALX1 and acts as its coactivator. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Acetylates FOXO1 and enhances its transcriptional activity. Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter. Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity. Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER). Acetylates MEF2D. Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degragation, this mechanism may be involved in CD4/CD8 lineage differentiation. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA) or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation or propionylation, respectively. Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (E)-but-2-enoyl-CoA (crotonyl-CoA) concentration is low. Also acts as a histone butyryltransferase; butyrylation marks active promoters. Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway. Acetylates PCK1 and promotes PCK1 anaplerotic activity. Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. TTGH73N EC EC 2.3.1.48 TTGH73N PD 6GYT; 6GYR; 6FGS; 6FGN; 6DS6 TTGH73N SQ MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMPNMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQSTLDIH TTGH73N TT Clinical trial TTGH73N FM Acyltransferase TT81PFE ID TT81PFE TT81PFE TN Histone lysine demethylase PHF8 (PHF8) TT81PFE UP Q9UPP1 TT81PFE UC PHF8_HUMAN TT81PFE BC Paired donor oxygen oxidoreductase TT81PFE SN ZNF422; PHD finger protein 8; KIAA1111 TT81PFE GN PHF8 TT81PFE FC Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Only has activity toward H4K20Me1 when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3. Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. TT81PFE EC EC 1.14.11.27 TT81PFE PD 4DO0; 3KV4; 3K3O; 3K3N; 2WWU TT81PFE SQ MNRSRAIVQRGRVLPPPAPLDTTNLAGRRTLQGRAKMASVPVYCLCRLPYDVTRFMIECDMCQDWFHGSCVGVEEEKAADIDLYHCPNCEVLHGPSIMKKRRGSSKGHDTHKGKPVKTGSPTFVRELRSRTFDSSDEVILKPTGNQLTVEFLEENSFSVPILVLKKDGLGMTLPSPSFTVRDVEHYVGSDKEIDVIDVTRQADCKMKLGDFVKYYYSGKREKVLNVISLEFSDTRLSNLVETPKIVRKLSWVENLWPEECVFERPNVQKYCLMSVRDSYTDFHIDFGGTSVWYHVLKGEKIFYLIRPTNANLTLFECWSSSSNQNEMFFGDQVDKCYKCSVKQGQTLFIPTGWIHAVLTPVDCLAFGGNFLHSLNIEMQLKAYEIEKRLSTADLFRFPNFETICWYVGKHILDIFRGLRENRRHPASYLVHGGKALNLAFRAWTRKEALPDHEDEIPETVRTVQLIKDLAREIRLVEDIFQQNVGKTSNIFGLQRIFPAGSIPLTRPAHSTSVSMSRLSLPSKNGSKKKGLKPKELFKKAERKGKESSALGPAGQLSYNLMDTYSHQALKTGSFQKAKFNITGACLNDSDDDSPDLDLDGNESPLALLMSNGSTKRVKSLSKSRRTKIAKKVDKARLMAEQVMEDEFDLDSDDELQIDERLGKEKATLIIRPKFPRKLPRAKPCSDPNRVREPGEVEFDIEEDYTTDEDMVEGVEGKLGNGSGAGGILDLLKASRQVGGPDYAALTEAPASPSTQEAIQGMLCMANLQSSSSSPATSSLQAWWTGGQDRSSGSSSSGLGTVSNSPASQRTPGKRPIKRPAYWRTESEEEEENASLDEQDSLGACFKDAEYIYPSLESDDDDPALKSRPKKKKNSDDAPWSPKARVTPTLPKQDRPVREGTRVASIETGLAAAAAKLAQQELQKAQKKKYIKKKPLLKEVEQPRPQDSNLSLTVPAPTVAATPQLVTSSSPLPPPEPKQEALSGSLADHEYTARPNAFGMAQANRSTTPMAPGVFLTQRRPSVGSQSNQAGQGKRPKKGLATAKQRLGRILKIHRNGKLLL TT81PFE TT Literature-reported TTIZQFJ ID TTIZQFJ TTIZQFJ TN Histone-arginine methyltransferase CARM1 (CARM1) TTIZQFJ UP Q86X55 TTIZQFJ UC CARM1_HUMAN TTIZQFJ BC Methyltransferase TTIZQFJ SN Protein arginine N-methyltransferase 4; PRMT4; Histonearginine methyltransferase CARM1; Coactivatorassociated arginine methyltransferase 1; Coactivator-associated arginine methyltransferase 1 TTIZQFJ GN CARM1 TTIZQFJ FC Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs. Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. TTIZQFJ EC EC 2.1.1.319 TTIZQFJ SQ MAAAAAAVGPGAGGAGSAVPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEVRAGPDSAGIALYSHEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSFYNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTTPSPPPGSHYTSPSENMWNTGSTYNLSSGMAVAGMPTAYDLSSVIASGSSVGHNNLIPLANTGIVNHTHSRMGSIMSTGIVQGSSGAQGSGGGSTSAHYAVNSQFTMGGPAISMASPMSIPTNTMHYGS TTIZQFJ TT Literature-reported TTIZQFJ FM Methyltransferase superfamily TTIZQFJ RC R-HSA-1368082:RORA activates gene expression; R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-1989781:PPARA activates gene expression; R-HSA-2032785:YAP1- and WWTR1 (TAZ)-stimulated gene expression; R-HSA-2151201:Transcriptional activation of mitochondrial biogenesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP); R-HSA-3214858:RMTs methylate histone arginines; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-400206:Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha); R-HSA-400253:Circadian Clock TTS6RZT ID TTS6RZT TTS6RZT TN Histone-lysine N-methyltransferase EHMT2 (EHMT2) TTS6RZT UP Q96KQ7 TTS6RZT UC EHMT2_HUMAN TTS6RZT BC Methyltransferase TTS6RZT SN Protein G9a; NG36; Lysine N-methyltransferase 1C; KMT1C; Histone H3-K9 methyltransferase 3; HLA-B-associated transcript 8; H3-K9-HMTase 3; G9A; Euchromatic histone-lysine N-methyltransferase 2; C6orf30; BAT8 TTS6RZT GN EHMT2 TTS6RZT FC H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself. Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. TTS6RZT EC EC 2.1.1.- TTS6RZT PD 5VSE; 5VSC; 5V9I; 5TUY; 5TTF TTS6RZT SQ MAAAAGAAAAAAAEGEAPAEMGALLLEKETRGATERVHGSLGDTPRSEETLPKATPDSLEPAGPSSPASVTVTVGDEGADTPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSPSKGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKVHRARKTMSKPGNGQPPVPEKRPPEIQHFRMSDDVHSLGKVTSDLAKRRKLNSGGGLSEELGSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEALTEQLSEEEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRRKREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGFEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGCNAAILKRETMRPSSRVALMVLCETHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDASEAQEVTIPRGDGVTPPAGTAAPAPPPLSQDVPGRADTSQPSARMRGHGEPRRPPCDPLADTIDSSGPSLTLPNGGCLSAVGLPLGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQLNRKLRLGVGNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLPELGSLPPVNT TTS6RZT TT Preclinical TTJ0FSU ID TTJ0FSU TTJ0FSU TN Histone-lysine N-methyltransferase SETD7 (SETD7) TTJ0FSU UP Q8WTS6 TTJ0FSU UC SETD7_HUMAN TTJ0FSU BC Methyltransferase TTJ0FSU SN SET9; SET7/9; SET7; SET domain-containing protein 7; Lysine N-methyltransferase 7; KMT7; KIAA1717; Histone H3-K4 methyltransferase SETD7; H3-K4-HMTase SETD7 TTJ0FSU GN SETD7 TTJ0FSU FC H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation. Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. TTJ0FSU EC EC 2.1.1.43 TTJ0FSU PD 5YLT; 5EG2; 5AYF; 4JLG; 4JDS TTJ0FSU SQ MDSDDEMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQQK TTJ0FSU TT Literature-reported TTPJ9XK ID TTPJ9XK TTPJ9XK TN hnRNP A1 messenger RNA (HNRNPA1 mRNA) TTPJ9XK UP P09651 TTPJ9XK UC ROA1_HUMAN TTPJ9XK BC mRNA target TTPJ9XK SN hnRNP core protein A1 (mRNA); hnRNP A1 (mRNA); Single-strand RNA-binding protein (mRNA); Heterogeneous nuclear ribonucleoprotein A1 (mRNA); Helix-destabilizing protein (mRNA); HNRPA1 (mRNA) TTPJ9XK GN HNRNPA1 TTPJ9XK FC May bind to specific miRNA hairpins. Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. TTPJ9XK PD 6DCL; 6BXX; 5ZGL; 5MPL; 5MPG TTPJ9XK SQ MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF TTPJ9XK TT Literature-reported TTPJ9XK FM mRNA target TTPJ9XK KE hsa03040:Spliceosome TTPJ9XK RC R-HSA-72163:mRNA Splicing - Major Pathway TTF6NLB ID TTF6NLB TTF6NLB TN Human immunodeficiency virus GAG messenger RNA (HIV gag mRNA) TTF6NLB UP P04591 TTF6NLB UC GAG_HV1H2 TTF6NLB BC mRNA target TTF6NLB SN gag (mRNA); Pr55Gag (mRNA); Gag polyprotein (mRNA) TTF6NLB GN HIV gag mRNA TTF6NLB FC Gag polyprotein: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). TTF6NLB PD 6CQR; 6CQQ; 6CQN; 6CQL; 6CQJ TTF6NLB SQ MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNFLQSRPEPTAPPEESFRSGVETTTPPQKQEPIDKELYPLTSLRSLFGNDPSSQ TTF6NLB TT Literature-reported TTF6NLB FM mRNA target TT37KAF ID TT37KAF TT37KAF TN Human immunodeficiency virus Ribonuclease H (HIV RNH) TT37KAF UP P03366 (600-1159) TT37KAF UC POL_HV1B1 TT37KAF SN Retroviral ribonuclease H; RNase H (600-1159); RNH1 TT37KAF GN HIV RNH TT37KAF FC Endonuclease that specifically degrades the RNA of RNA- DNA hybrids. TT37KAF EC EC 2.7.7.49 TT37KAF PD 6OE3; 6HAK; 6ELI; 6DUH; 6DUG TT37KAF SQ PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKIL TT37KAF TT Literature-reported TTBPJOK ID TTBPJOK TTBPJOK TN IL-1 receptor-associated kinase 3 (IRAK3) TTBPJOK UP Q9Y616 TTBPJOK UC IRAK3_HUMAN TTBPJOK BC Kinase TTBPJOK SN Interleukin-1 receptor-associated kinase 3; IRAK-M; IRAK-3; IL-1 receptor-associated kinase M TTBPJOK GN IRAK3 TTBPJOK FC Inhibits dissociation of IRAK1 and IRAK4 from the Toll-like receptor signaling complex by either inhibiting the phosphorylation of IRAK1 and IRAK4 or stabilizing the receptor complex. TTBPJOK EC EC 2.7.11.1 TTBPJOK PD 5UKE TTBPJOK SQ MAGNCGARGALSAHTLLFDLPPALLGELCAVLDSCDGALGWRGLAERLSSSWLDVRHIEKYVDQGKSGTRELLWSWAQKNKTIGDLLQVLQEMGHRRAIHLITNYGAVLSPSEKSYQEGGFPNILFKETANVTVDNVLIPEHNEKGILLKSSISFQNIIEGTRNFHKDFLIGEGEIFEVYRVEIQNLTYAVKLFKQEKKMQCKKHWKRFLSELEVLLLFHHPNILELAAYFTETEKFCLIYPYMRNGTLFDRLQCVGDTAPLPWHIRIGILIGISKAIHYLHNVQPCSVICGSISSANILLDDQFQPKLTDFAMAHFRSHLEHQSCTINMTSSSSKHLWYMPEEYIRQGKLSIKTDVYSFGIVIMEVLTGCRVVLDDPKHIQLRDLLRELMEKRGLDSCLSFLDKKVPPCPRNFSAKLFCLAGRCAATRAKLRPSMDEVLNTLESTQASLYFAEDPPTSLKSFRCPSPLFLENVPSIPVEDDESQNNNLLPSDEGLRIDRMTQKTPFECSQSEVMFLSLDKKPESKRNEEACNMPSSSCEESWFPKYIVPSQDLRPYKVNIDPSSEAPGHSCRSRPVESSCSSKFSWDEYEQYKKE TTBPJOK TT Literature-reported TT6HV2K ID TT6HV2K TT6HV2K TN Influenza PB1 messenger RNA (Influ PB1 mRNA) TT6HV2K UP Q9WLS3 TT6HV2K UC RDRP_I97A1 TT6HV2K BC mRNA target TT6HV2K SN RNA-directed RNA polymerase subunit P1 (mRNA); RNA-directed RNA polymerase catalytic subunit (mRNA); Polymerase basic protein 1 (mRNA) TT6HV2K GN Influ PB1 mRNA TT6HV2K FC The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs. RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. TT6HV2K EC EC 2.7.7.48 TT6HV2K PD 3CM8 TT6HV2K SQ MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGRWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGLFENSCLETMEVVQQTRMDKLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMDKEEMEITTHFQRKRRVRDNMTKKMVTQRTIGKKKQRLTKKSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVHFVEALARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTVTGDNTKWNENQNPRIFLAMITYITRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFESKSMKLRTQIPAEMLANIDLKYFNESTRKKIEKIRPLLVEGTASLSPGMMMGMFNMLSTVLGVSILNLGQKRYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLVGINMSKKKSYINRTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMINNDLGPATAQMALQLFIKDYRYTYRCHRGDTQIQTRRSFELKKLWEQTRSKAGLLVSDGGPNLYNIRNLHIPEVGLKWELMDEDYQGRLCNPLNPFVSHKEVESVNNAVVMPAHGPAKSMEYDAVATTHSWIPKRNRSILNTSQRGILEDEQMYQKCCTLFEKFFPSSSYRRPVGISSMMEAMVSRARIDARIDFESGRIKKEEFAEILKICSTIEELGRQGK TT6HV2K TT Literature-reported TT6HV2K FM mRNA target TTJTRMK ID TTJTRMK TTJTRMK TN Interleukin 10 receptor (IL10RB) TTJTRMK UP Q08334 TTJTRMK UC I10R2_HUMAN TTJTRMK BC Cytokine receptor TTJTRMK SN Interleukin-10 receptor subunit beta; Interleukin-10 receptor subunit 2; IL-10RB; IL-10R2; IL-10R subunit beta; IL-10R subunit 2; IL-10 receptor subunit beta; D21S66; D21S58; Cytokine receptor family 2 member 4; Cytokine receptor class-II member 4; CRFB4; CRF2-4; CDw210b TTJTRMK GN IL10RB TTJTRMK FC The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. TTJTRMK PD 5T5W; 3LQM TTJTRMK SQ MAWSLGSWLGGCLLVSALGMVPPPENVRMNSVNFKNILQWESPAFAKGNLTFTAQYLSYRIFQDKCMNTTLTECDFSSLSKYGDHTLRVRAEFADEHSDWVNITFCPVDDTIIGPPGMQVEVLADSLHMRFLAPKIENEYETWTMKNVYNSWTYNVQYWKNGTDEKFQITPQYDFEVLRNLEPWTTYCVQVRGFLPDRNKAGEWSEPVCEQTTHDETVPSWMVAVILMASVFMVCLALLGCFALLWCVYKKTKYAFSPRNSLPQHLKEFLGHPHHNTLLFFSFPLSDENDVFDKLSVIAEDSESGKQNPGDSCSLGTPPGQGPQS TTJTRMK TT Literature-reported TTJTRMK KE hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05169:Epstein-Barr virus infection TTAJSQ0 ID TTAJSQ0 TTAJSQ0 TN IRS1 messenger RNA (IRS1 mRNA) TTAJSQ0 UP P35568 TTAJSQ0 UC IRS1_HUMAN TTAJSQ0 BC mRNA target TTAJSQ0 SN Insulin receptor substrate 1 (mRNA); IRS-1 (mRNA) TTAJSQ0 GN IRS1 TTAJSQ0 FC When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit. May mediate the control of various cellular processes by insulin. TTAJSQ0 PD 6BNT; 5U1M; 2Z8C; 1QQG; 1K3A TTAJSQ0 SQ MASPPESDGFSDVRKVGYLRKPKSMHKRFFVLRAASEAGGPARLEYYENEKKWRHKSSAPKRSIPLESCFNINKRADSKNKHLVALYTRDEHFAIAADSEAEQDSWYQALLQLHNRAKGHHDGAAALGAGGGGGSCSGSSGLGEAGEDLSYGDVPPGPAFKEVWQVILKPKGLGQTKNLIGIYRLCLTSKTISFVKLNSEAAAVVLQLMNIRRCGHSENFFFIEVGRSAVTGPGEFWMQVDDSVVAQNMHETILEAMRAMSDEFRPRSKSQSSSNCSNPISVPLRRHHLNNPPPSQVGLTRRSRTESITATSPASMVGGKPGSFRVRASSDGEGTMSRPASVDGSPVSPSTNRTHAHRHRGSARLHPPLNHSRSIPMPASRCSPSATSPVSLSSSSTSGHGSTSDCLFPRRSSASVSGSPSDGGFISSDEYGSSPCDFRSSFRSVTPDSLGHTPPARGEEELSNYICMGGKGPSTLTAPNGHYILSRGGNGHRCTPGTGLGTSPALAGDEAASAADLDNRFRKRTHSAGTSPTITHQKTPSQSSVASIEEYTEMMPAYPPGGGSGGRLPGHRHSAFVPTRSYPEEGLEMHPLERRGGHHRPDSSTLHTDDGYMPMSPGVAPVPSGRKGSGDYMPMSPKSVSAPQQIINPIRRHPQRVDPNGYMMMSPSGGCSPDIGGGPSSSSSSSNAVPSGTSYGKLWTNGVGGHHSHVLPHPKPPVESSGGKLLPCTGDYMNMSPVGDSNTSSPSDCYYGPEDPQHKPVLSYYSLPRSFKHTQRPGEPEEGARHQHLRLSTSSGRLLYAATADDSSSSTSSDSLGGGYCGARLEPSLPHPHHQVLQPHLPRKVDTAAQTNSRLARPTRLSLGDPKASTLPRAREQQQQQQPLLHPPEPKSPGEYVNIEFGSDQSGYLSGPVAFHSSPSVRCPSQLQPAPREEETGTEEYMKMDLGPGRRAAWQESTGVEMGRLGPAPPGAASICRPTRAVPSSRGDYMTMQMSCPRQSYVDTSPAAPVSYADMRTGIAAEEVSLPRATMAAASSSSAASASPTGPQGAAELAAHSSLLGGPQGPGGMSAFTRVNLSPNRNQSAKVIRADPQGCRRRHSSETFSSTPSATRVGNTVPFGAGAAVGGGGGSSSSSEDVKRHSSASFENVWLRPGELGGAPKEPAKLCGAAGGLENGLNYIDLDLVKDFKQCPQECTPEPQPPPPPPPHQPLGSGESSSTRRSSEDLSAYASISFQKQPEDRQ TTAJSQ0 TT Literature-reported TTAJSQ0 FM mRNA target TTAJSQ0 KE hsa04022:cGMP-PKG signaling pathway; hsa04068:FoxO signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04910:Insulin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04930:Type II diabetes mellitus; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa04960:Aldosterone-regulated sodium reabsorption; hsa05206:MicroRNAs in cancer TTAJSQ0 RC R-HSA-109704:PI3K Cascade; R-HSA-112412:SOS-mediated signalling; R-HSA-1257604:PIP3 activates AKT signaling; R-HSA-198203:PI3K/AKT activation; R-HSA-2219530:Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-2428928:IRS-related events triggered by IGF1R; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-74713:IRS activation; R-HSA-74749:Signal attenuation; R-HSA-982772:Growth hormone receptor signaling TTYD3AN ID TTYD3AN TTYD3AN TN Isoleucyl-tRNA synthetase (IARS) TTYD3AN UP P41252 TTYD3AN UC SYIC_HUMAN TTYD3AN BC Carbon-oxygen ligase TTYD3AN SN Isoleucine--tRNA ligase, cytoplasmic; Isoleucine--tRNA ligase; IleRS; IRS TTYD3AN GN IARS TTYD3AN FC Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. TTYD3AN EC EC 6.1.1.5 TTYD3AN SQ MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHILAGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQCRAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMPFSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNPEMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCKENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTTEVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVENMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVCIGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHYPFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQKMSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAYRFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVVPRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELMYQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKTIPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMVLGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQFEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGTYLNSVIESHTEFIFTTIKAPLKPYPVSPSDKVLIQEKTQLKGSELEITLTRGSSLPGPACAYVNLNICANGSEQGGVLLLENPKGDNRLDLLKLKSVVTSIFGVKNTELAVFHDETEIQNQTDLLSLSGKTLCVTAGSAPSLINSSSTLLCQYINLQLLNAKPQECLMGTVGTLLLENPLGQNGLTHQGLLYEAAKVFGLRSRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTADF TTYD3AN TT Literature-reported TTYD3AN FM Carbon-oxygen ligase TTYD3AN KE hsa00970:Aminoacyl-tRNA biosynthesis TTGYTMA ID TTGYTMA TTGYTMA TN Isopeptidase T (USP5) TTGYTMA UP P45974 TTGYTMA UC UBP5_HUMAN TTGYTMA BC Peptidase TTGYTMA SN Ubiquitin-specific-processing protease 5; Ubiquitin thioesterase 5; Ubiquitin carboxyl-terminal hydrolase 5; ISOT; Deubiquitinating enzyme 5 TTGYTMA GN USP5 TTGYTMA FC Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition. Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. TTGYTMA EC EC 3.4.19.12 TTGYTMA PD 6NFT; 6DXT; 6DXH; 3IHP; 2G45 TTGYTMA SQ MAELSEEALLSVLPTIRVPKAGDRVHKDECAFSFDTPESEGGLYICMNTFLGFGKQYVERHFNKTGQRVYLHLRRTRRPKEEDPATGTGDPPRKKPTRLAIGVEGGFDLSEEKFELDEDVKIVILPDYLEIARDGLGGLPDIVRDRVTSAVEALLSADSASRKQEVQAWDGEVRQVSKHAFSLKQLDNPARIPPCGWKCSKCDMRENLWLNLTDGSILCGRRYFDGSGGNNHAVEHYRETGYPLAVKLGTITPDGADVYSYDEDDMVLDPSLAEHLSHFGIDMLKMQKTDKTMTELEIDMNQRIGEWELIQESGVPLKPLFGPGYTGIRNLGNSCYLNSVVQVLFSIPDFQRKYVDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPESGDGERVPEQKEVQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNCRSSENPNEVFRFLVEEKIKCLATEKVKYTQRVDYIMQLPVPMDAALNKEELLEYEEKKRQAEEEKMALPELVRAQVPFSSCLEAYGAPEQVDDFWSTALQAKSVAVKTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELDISQLRGTGLQPGEEELPDIAPPLVTPDEPKGSLGFYGNEDEDSFCSPHFSSPTSPMLDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFANPLILPGSSGPGSTSAAADPPPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDDLDAEAAMDISEGRSAADSISESVPVGPKVRDGPGKYQLFAFISHMGTSTMCGHYVCHIKKEGRWVIYNDQKVCASEKPPKDLGYIYFYQRVAS TTGYTMA TT Preclinical TTOJY1B ID TTOJY1B TTOJY1B TN Jagged2 messenger RNA (JAG2 mRNA) TTOJY1B UP Q9Y219 TTOJY1B UC JAG2_HUMAN TTOJY1B BC mRNA target TTOJY1B SN hJ2 (mRNA); Protein jagged-2 (mRNA); Jagged2 (mRNA) TTOJY1B GN JAG2 TTOJY1B FC Involved in limb development. Putative Notch ligand involved in the mediation of Notch signaling. TTOJY1B PD 5MWF; 5MW7; 5MW5 TTOJY1B SQ MRAQGRGRLPRRLLLLLALWVQAARPMGYFELQLSALRNVNGELLSGACCDGDGRTTRAGGCGHDECDTYVRVCLKEYQAKVTPTGPCSYGHGATPVLGGNSFYLPPAGAAGDRARARARAGGDQDPGLVVIPFQFAWPRSFTLIVEAWDWDNDTTPNEELLIERVSHAGMINPEDRWKSLHFSGHVAHLELQIRVRCDENYYSATCNKFCRPRNDFFGHYTCDQYGNKACMDGWMGKECKEAVCKQGCNLLHGGCTVPGECRCSYGWQGRFCDECVPYPGCVHGSCVEPWQCNCETNWGGLLCDKDLNYCGSHHPCTNGGTCINAEPDQYRCTCPDGYSGRNCEKAEHACTSNPCANGGSCHEVPSGFECHCPSGWSGPTCALDIDECASNPCAAGGTCVDQVDGFECICPEQWVGATCQLDANECEGKPCLNAFSCKNLIGGYYCDCIPGWKGINCHINVNDCRGQCQHGGTCKDLVNGYQCVCPRGFGGRHCELERDECASSPCHSGGLCEDLADGFHCHCPQGFSGPLCEVDVDLCEPSPCRNGARCYNLEGDYYCACPDDFGGKNCSVPREPCPGGACRVIDGCGSDAGPGMPGTAASGVCGPHGRCVSQPGGNFSCICDSGFTGTYCHENIDDCLGQPCRNGGTCIDEVDAFRCFCPSGWEGELCDTNPNDCLPDPCHSRGRCYDLVNDFYCACDDGWKGKTCHSREFQCDAYTCSNGGTCYDSGDTFRCACPPGWKGSTCAVAKNSSCLPNPCVNGGTCVGSGASFSCICRDGWEGRTCTHNTNDCNPLPCYNGGICVDGVNWFRCECAPGFAGPDCRINIDECQSSPCAYGATCVDEINGYRCSCPPGRAGPRCQEVIGFGRSCWSRGTPFPHGSSWVEDCNSCRCLDGRRDCSKVWCGWKPCLLAGQPEALSAQCPLGQRCLEKAPGQCLRPPCEAWGECGAEEPPSTPCLPRSGHLDNNCARLTLHFNRDHVPQGTTVGAICSGIRSLPATRAVARDRLLVLLCDRASSGASAVEVAVSFSPARDLPDSSLIQGAAHAIVAAITQRGNSSLLLAVTEVKVETVVTGGSSTGLLVPVLCGAFSVLWLACVVLCVWWTRKRRKERERSRLPREESANNQWAPLNPIRNPIERPGGHKDVLYQCKNFTPPPRRADEALPGPAGHAAVREDEEDEDLGRGEEDSLEAEKFLSHKFTKDPGRSPGRPAHWASGPKVDNRAVRSINEARYAGKE TTOJY1B TT Literature-reported TTOJY1B FM mRNA target TTOJY1B KE hsa04330:Notch signaling pathway TTOJY1B RC R-HSA-2122948:Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2644606:Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2660826:Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant; R-HSA-2691232:Constitutive Signaling by NOTCH1 HD Domain Mutants; R-HSA-2894862:Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-2979096:NOTCH2 Activation and Transmission of Signal to the Nucleus TT87E24 ID TT87E24 TT87E24 TN JUN activation domain binding protein (COPS5) TT87E24 UP Q92905 TT87E24 UC CSN5_HUMAN TT87E24 BC Peptidase TT87E24 SN Signalosome subunit 5; SGN5; Jun activation domain-binding protein 1; JAB1; CSN5; COP9 signalosome complex subunit 5 TT87E24 GN COPS5 TT87E24 FC The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. Promotes the proteasomal degradation of BRSK2. Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. TT87E24 EC EC 3.4.-.- TT87E24 PD 5M5Q; 5JOH; 5JOG; 4WSN; 4F7O TT87E24 SQ MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS TT87E24 TT Literature-reported TT87E24 FM Peptidase TTPAFR9 ID TTPAFR9 TTPAFR9 TN Ketohexokinase (KHK) TTPAFR9 UP P50053 TTPAFR9 UC KHK_HUMAN TTPAFR9 BC Kinase TTPAFR9 SN Hepatic fructokinase TTPAFR9 GN KHK TTPAFR9 FC Catalyzes the phosphorylation of the ketose sugar fructose to fructose-1-phosphate. TTPAFR9 EC EC 2.7.1.3 TTPAFR9 PD 5WBZ; 5WBR; 5WBQ; 5WBP; 5WBO TTPAFR9 SQ MEEKQILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVSQVAWQSKGDTPSSCCIINNSNGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIEGRNASEQVKMLQRIDAHNTRQPPEQKIRVSVEVEKPREELFQLFGYGDVVFVSKDVAKHLGFQSAEEALRGLYGRVRKGAVLVCAWAEEGADALGPDGKLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGLQGFDGIV TTPAFR9 TT Literature-reported TTM8FR7 ID TTM8FR7 TTM8FR7 TN KRAS messenger RNA (KRAS mRNA) TTM8FR7 UP P01116 TTM8FR7 UC RASK_HUMAN TTM8FR7 BC mRNA target TTM8FR7 SN c-Ki-ras (mRNA); c-K-ras (mRNA); RASK2 (mRNA); Ki-Ras (mRNA); KRAS2 (mRNA); K-Ras 2 (mRNA); GTPase KRas (mRNA) TTM8FR7 GN KRAS TTM8FR7 FC Plays an important role in the regulation of cell proliferation. Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. TTM8FR7 PD 6N2K; 6N2J; 6H47; 6H46; 6GQY TTM8FR7 SQ MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM TTM8FR7 TT Literature-reported TTM8FR7 FM mRNA target TTM8FR7 KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04062:Chemokine signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04320:Dorso-ventral axis formation; hsa04360:Axon guidance; hsa04370:VEGF signaling pathway; hsa04530:Tight junction; hsa04540:Gap junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa04960:Aldosterone-regulated sodium reabsorption; hsa05034:Alcoholism; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05203:Viral carcinogenesis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTM8FR7 RC R-HSA-112412:SOS-mediated signalling; R-HSA-1169092:Activation of RAS in B cells; R-HSA-1236382:Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1250196:SHC1 events in ERBB2 signaling; R-HSA-1250347:SHC1 events in ERBB4 signaling; R-HSA-171007:p38MAPK events; R-HSA-179812:GRB2 events in EGFR signaling; R-HSA-180336:SHC1 events in EGFR signaling; R-HSA-1963640:GRB2 events in ERBB2 signaling; R-HSA-210993:Tie2 Signaling; R-HSA-2179392:EGFR Transactivation by Gastrin; R-HSA-2424491:DAP12 signaling; R-HSA-2428933:SHC-related events triggered by IGF1R; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-375165:NCAM signaling for neurite out-growth; R-HSA-5218921:VEGFR2 mediated cell proliferation; R-HSA-5621575:CD209 (DC-SIGN) signaling; R-HSA-5637810:Constitutive Signaling by EGFRvIII; R-HSA-5654688:SHC-mediated cascade:FGFR1; R-HSA-5654693:FRS-mediated FGFR1 signaling; R-HSA-5654699:SHC-mediated cascade:FGFR2; R-HSA-5654700:FRS-mediated FGFR2 signaling; R-HSA-5654704:SHC-mediated cascade:FGFR3; R-HSA-5654706:FRS-mediated FGFR3 signaling; R-HSA-5654712:FRS-mediated FGFR4 signaling; R-HSA-5654719:SHC-mediated cascade:FGFR4; R-HSA-5658442:Regulation of RAS by GAPs; R-HSA-5673000:RAF activation; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5675221:Negative regulation of MAPK pathway; R-HSA-74751:Insulin receptor signalling cascade TTT3IXG ID TTT3IXG TTT3IXG TN Kynurenine oxoglutarate transaminase II (AADAT) TTT3IXG UP Q8N5Z0 TTT3IXG UC AADAT_HUMAN TTT3IXG BC Transaminase TTT3IXG SN Kynurenineoxoglutarate transaminase II; Kynurenineoxoglutarate transaminase 2; Kynurenineoxoglutarate aminotransferase II; Kynurenine/alphaaminoadipate aminotransferase, mitochondrial; Kynurenine aminotransferase II; KAT/AadAT; Alphaaminoadipate aminotransferase; AadAT; 2aminoadipate transaminase; 2aminoadipate aminotransferase TTT3IXG GN AADAT TTT3IXG FC Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino- group acceptors, with a preference for 2-oxoglutarate, 2- oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro). TTT3IXG EC EC 2.6.1.39 TTT3IXG PD 6D0A; 5TF5; 5EUN; 5EFS; 4GEB TTT3IXG SQ MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKTIQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQGLCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKPEDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNKFRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQLMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKVKGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQLIKESL TTT3IXG TT Preclinical TTA0OSE ID TTA0OSE TTA0OSE TN Lactase-phlorizin hydrolase (LCT) TTA0OSE UP P09848 TTA0OSE UC LPH_HUMAN TTA0OSE BC Glycosylase TTA0OSE SN Lactase-glycosylceramidase; LCT; Glycosyl-hydrolase TTA0OSE GN LCT TTA0OSE FC LPH splits lactose in the small intestine. TTA0OSE SQ MELSWHVVFIALLSFSCWGSDWESDRNFISTAGPLTNDLLHNLSGLLGDQSSNFVAGDKDMYVCHQPLPTFLPEYFSSLHASQITHYKVFLSWAQLLPAGSTQNPDEKTVQCYRRLLKALKTARLQPMVILHHQTLPASTLRRTEAFADLFADYATFAFHSFGDLVGIWFTFSDLEEVIKELPHQESRASQLQTLSDAHRKAYEIYHESYAFQGGKLSVVLRAEDIPELLLEPPISALAQDTVDFLSLDLSYECQNEASLRQKLSKLQTIEPKVKVFIFNLKLPDCPSTMKNPASLLFSLFEAINKDQVLTIGFDINEFLSCSSSSKKSMSCSLTGSLALQPDQQQDHETTDSSPASAYQRIWEAFANQSRAERDAFLQDTFPEGFLWGASTGAFNVEGGWAEGGRGVSIWDPRRPLNTTEGQATLEVASDSYHKVASDVALLCGLRAQVYKFSISWSRIFPMGHGSSPSLPGVAYYNKLIDRLQDAGIEPMATLFHWDLPQALQDHGGWQNESVVDAFLDYAAFCFSTFGDRVKLWVTFHEPWVMSYAGYGTGQHPPGISDPGVASFKVAHLVLKAHARTWHHYNSHHRPQQQGHVGIVLNSDWAEPLSPERPEDLRASERFLHFMLGWFAHPVFVDGDYPATLRTQIQQMNRQCSHPVAQLPEFTEAEKQLLKGSADFLGLSHYTSRLISNAPQNTCIPSYDTIGGFSQHVNHVWPQTSSSWIRVVPWGIRRLLQFVSLEYTRGKVPIYLAGNGMPIGESENLFDDSLRVDYFNQYINEVLKAIKEDSVDVRSYIARSLIDGFEGPSGYSQRFGLHHVNFSDSSKSRTPRKSAYFFTSIIEKNGFLTKGAKRLLPPNTVNLPSKVRAFTFPSEVPSKAKVVWEKFSSQPKFERDLFYHGTFRDDFLWGVSSSAYQIEGAWDADGKGPSIWDNFTHTPGSNVKDNATGDIACDSYHQLDADLNMLRALKVKAYRFSISWSRIFPTGRNSSINSHGVDYYNRLINGLVASNIFPMVTLFHWDLPQALQDIGGWENPALIDLFDSYADFCFQTFGDRVKFWMTFNEPMYLAWLGYGSGEFPPGVKDPGWAPYRIAHAVIKAHARVYHTYDEKYRQEQKGVISLSLSTHWAEPKSPGVPRDVEAADRMLQFSLGWFAHPIFRNGDYPDTMKWKVGNRSELQHLATSRLPSFTEEEKRFIRATADVFCLNTYYSRIVQHKTPRLNPPSYEDDQEMAEEEDPSWPSTAMNRAAPWGTRRLLNWIKEEYGDIPIYITENGVGLTNPNTEDTDRIFYHKTYINEALKAYRLDGIDLRGYVAWSLMDNFEWLNGYTVKFGLYHVDFNNTNRPRTARASARYYTEVITNNGMPLAREDEFLYGRFPEGFIWSAASAAYQIEGAWRADGKGLSIWDTFSHTPLRVENDAIGDVACDSYHKIAEDLVTLQNLGVSHYRFSISWSRILPDGTTRYINEAGLNYYVRLIDTLLAASIQPQVTIYHWDLPQTLQDVGGWENETIVQRFKEYADVLFQRLGDKVKFWITLNEPFVIAYQGYGYGTAAPGVSNRPGTAPYIVGHNLIKAHAEAWHLYNDVYRASQGGVISITISSDWAEPRDPSNQEDVEAARRYVQFMGGWFAHPIFKNGDYNEVMKTRIRDRSLAAGLNKSRLPEFTESEKRRINGTYDFFGFNHYTTVLAYNLNYATAISSFDADRGVASIADRSWPDSGSFWLKMTPFGFRRILNWLKEEYNDPPIYVTENGVSQREETDLNDTARIYYLRTYINEALKAVQDKVDLRGYTVWSAMDNFEWATGFSERFGLHFVNYSDPSLPRIPKASAKFYASVVRCNGFPDPATGPHACLHQPDAGPTISPVRQEEVQFLGLMLGTTEAQTALYVLFSLVLLGVCGLAFLSYKYCKRSKQGKTQRSQQELSPVSSF TTA0OSE TT Literature-reported TTA0OSE KE hsa00052:Galactose metabolism; hsa01100:Metabolic pathways; hsa04973:Carbohydrate digestion and absorption TTNFMAL ID TTNFMAL TTNFMAL TN Lactate dehydrogenase A (LDHA) TTNFMAL UP P00338 TTNFMAL UC LDHA_HUMAN TTNFMAL BC CH-OH donor oxidoreductase TTNFMAL SN Renal carcinoma antigen NYREN59; Renal carcinoma antigen NY-REN-59; PIG19; Llactate dehydrogenase A chain; LDHM; LDH-M; LDH-A; LDH muscle subunit; L-lactate dehydrogenase A chain; Cell proliferationinducing gene 19 protein; Cell proliferation-inducing gene 19 protein TTNFMAL GN LDHA TTNFMAL FC Cadherin binding, L-lactate dehydrogenase activity, glycolytic process, pyruvate metabolic process, substantia nigra development. TTNFMAL EC EC 1.1.1.27 TTNFMAL PD 6BB3; 6BB2; 6BB1; 6BB0; 6BAZ TTNFMAL SQ MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF TTNFMAL TT Literature-reported TTNFMAL FM Short-chain dehydrogenases reductases TTVF2BJ ID TTVF2BJ TTVF2BJ TN Lactosylceramide alpha-2,3-sialyltransferase (ST3GAL5) TTVF2BJ UP Q9UNP4 TTVF2BJ UC SIAT9_HUMAN TTVF2BJ BC Glycosyl transferase TTVF2BJ SN UNQ2510/PRO5998; Sialyltransferase 9; ST3Gal V; ST3GAL5; Ganglioside GM3 synthase; CMP-NeuAc:lactosylceramide alpha-2,3-sialyltransferase TTVF2BJ GN ST3GAL5 TTVF2BJ FC Catalyzes the formation of ganglioside GM3 (alpha-N- acetylneuraminyl-2,3-beta-D-galactosyl-1, 4-beta-D- glucosylceramide). TTVF2BJ EC EC 2.4.99.9 TTVF2BJ SQ MRTKAAGCAERRPLQPRTEAAAAPAGRAMPSEYTYVKLRSDCSRPSLQWYTRAQSKMRRPSLLLKDILKCTLLVFGVWILYILKLNYTTEECDMKKMHYVDPDHVKRAQKYAQQVLQKECRPKFAKTSMALLFEHRYSVDLLPFVQKAPKDSEAESKYDPPFGFRKFSSKVQTLLELLPEHDLPEHLKAKTCRRCVVIGSGGILHGLELGHTLNQFDVVIRLNSAPVEGYSEHVGNKTTIRMTYPEGAPLSDLEYYSNDLFVAVLFKSVDFNWLQAMVKKETLPFWVRLFFWKQVAEKIPLQPKHFRILNPVIIKETAFDILQYSEPQSRFWGRDKNVPTIGVIAVVLATHLCDEVSLAGFGYDLNQPRTPLHYFDSQCMAAMNFQTMHNVTTETKFLLKLVKEGVVKDLSGGIDREF TTVF2BJ TT Literature-reported TTVF2BJ KE hsa00604:Glycosphingolipid biosynthesis - ganglio series; hsa01100:Metabolic pathways TTVF2BJ RC R-HSA-4085001:Sialic acid metabolism TTTSGRH ID TTTSGRH TTTSGRH TN Leucine-rich repeat-containing GPCR 5 (LGR5) TTTSGRH UP O75473 TTTSGRH UC LGR5_HUMAN TTTSGRH BC GPCR rhodopsin TTTSGRH SN Orphan G protein-coupled receptor HG38; Leucine-rich repeat-containing G-protein coupled receptor 5; Gpr49; GPR67; G-protein coupled receptor HG38; G-protein coupled receptor 67; G-protein coupled receptor 49; G protein-coupled receptor 49 TTTSGRH GN LGR5 TTTSGRH FC Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development. Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. TTTSGRH PD 4UFS; 4UFR; 4KNG; 4BSU; 4BST TTTSGRH SQ MDTSRLGVLLSLPVLLQLATGGSSPRSGVLLRGCPTHCHCEPDGRMLLRVDCSDLGLSELPSNLSVFTSYLDLSMNNISQLLPNPLPSLRFLEELRLAGNALTYIPKGAFTGLYSLKVLMLQNNQLRHVPTEALQNLRSLQSLRLDANHISYVPPSCFSGLHSLRHLWLDDNALTEIPVQAFRSLSALQAMTLALNKIHHIPDYAFGNLSSLVVLHLHNNRIHSLGKKCFDGLHSLETLDLNYNNLDEFPTAIRTLSNLKELGFHSNNIRSIPEKAFVGNPSLITIHFYDNPIQFVGRSAFQHLPELRTLTLNGASQITEFPDLTGTANLESLTLTGAQISSLPQTVCNQLPNLQVLDLSYNLLEDLPSFSVCQKLQKIDLRHNEIYEIKVDTFQQLLSLRSLNLAWNKIAIIHPNAFSTLPSLIKLDLSSNLLSSFPITGLHGLTHLKLTGNHALQSLISSENFPELKVIEMPYAYQCCAFGVCENAYKISNQWNKGDNSSMDDLHKKDAGMFQAQDERDLEDFLLDFEEDLKALHSVQCSPSPGPFKPCEHLLDGWLIRIGVWTIAVLALTCNALVTSTVFRSPLYISPIKLLIGVIAAVNMLTGVSSAVLAGVDAFTFGSFARHGAWWENGVGCHVIGFLSIFASESSVFLLTLAALERGFSVKYSAKFETKAPFSSLKVIILLCALLALTMAAVPLLGGSKYGASPLCLPLPFGEPSTMGYMVALILLNSLCFLMMTIAYTKLYCNLDKGDLENIWDCSMVKHIALLLFTNCILNCPVAFLSFSSLINLTFISPEVIKFILLVVVPLPACLNPLLYILFNPHFKEDLVSLRKQTYVWTRSKHPSLMSINSDDVEKQSCDSTQALVTFTSSSITYDLPPSSVPSPAYPVTESCHLSSVAFVPCL TTTSGRH TT Clinical trial TTTSGRH FM GPCR rhodopsin TTTSGRH RC R-HSA-4641263:Regulation of FZD by ubiquitination TTY2KP7 ID TTY2KP7 TTY2KP7 TN Leucyl-cysteinyl aminopeptidase (LNPEP) TTY2KP7 UP Q9UIQ6 TTY2KP7 UC LCAP_HUMAN TTY2KP7 BC Peptidase TTY2KP7 SN Placental leucine aminopeptidase; P-LAP; Oxytocinase; OTase; Leucyl-cystinyl aminopeptidase; Insulin-responsive aminopeptidase; Insulin-regulated membrane aminopeptidase; IRAP; Cystinyl aminopeptidase TTY2KP7 GN LNPEP TTY2KP7 FC Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain. Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. TTY2KP7 EC EC 3.4.11.3 TTY2KP7 PD 5MJ6; 5JHQ; 5C97; 4Z7I; 4PJ6 TTY2KP7 SQ MEPFTNDRLQLPRNMIENSMFEEEPDVVDLAKEPCLHPLEPDEVEYEPRGSRLLVRGLGEHEMEEDEEDYESSAKLLGMSFMNRSSGLRNSATGYRQSPDGACSVPSARTMVVCAFVIVVAVSVIMVIYLLPRCTFTKEGCHKKNQSIGLIQPFATNGKLFPWAQIRLPTAVVPLRYELSLHPNLTSMTFRGSVTISVQALQVTWNIILHSTGHNISRVTFMSAVSSQEKQAEILEYAYHGQIAIVAPEALLAGHNYTLKIEYSANISSSYYGFYGFSYTDESNEKKYFAATQFEPLAARSAFPCFDEPAFKATFIIKIIRDEQYTALSNMPKKSSVVLDDGLVQDEFSESVKMSTYLVAFIVGEMKNLSQDVNGTLVSIYAVPEKIGQVHYALETTVKLLEFFQNYFEIQYPLKKLDLVAIPDFEAGAMENWGLLTFREETLLYDSNTSSMADRKLVTKIIAHELAHQWFGNLVTMKWWNDLWLNEGFATFMEYFSLEKIFKELSSYEDFLDARFKTMKKDSLNSSHPISSSVQSSEQIEEMFDSLSYFKGSSLLLMLKTYLSEDVFQHAVVLYLHNHSYASIQSDDLWDSFNEVTNQTLDVKRMMKTWTLQKGFPLVTVQKKGKELFIQQERFFLNMKPEIQPSDTSYLWHIPLSYVTEGRNYSKYQSVSLLDKKSGVINLTEEVLWVKVNINMNGYYIVHYADDDWEALIHQLKINPYVLSDKDRANLINNIFELAGLGKVPLKRAFDLINYLGNENHTAPITEALFQTDLIYNLLEKLGYMDLASRLVTRVFKLLQNQIQQQTWTDEGTPSMRELRSALLEFACTHNLGNCSTTAMKLFDDWMASNGTQSLPTDVMTTVFKVGAKTDKGWSFLLGKYISIGSEAEKNKILEALASSEDVRKLYWLMKSSLNGDNFRTQKLSFIIRTVGRHFPGHLLAWDFVKENWNKLVQKFPLGSYTIQNIVAGSTYLFSTKTHLSEVQAFFENQSEATFRLRCVQEALEVIQLNIQWMEKNLKSLTWWL TTY2KP7 TT Patented-recorded TTW7OTG ID TTW7OTG TTW7OTG TN Leukotriene C4 synthase (LTC4S) TTW7OTG UP Q16873 TTW7OTG UC LTC4S_HUMAN TTW7OTG BC Carbon-sulfur lyase TTW7OTG SN Leukotriene-C(4)Leukotriene C4 synthase synthase; Leukotriene-C(4) synthase; LTC4 synthase TTW7OTG GN LTC4S TTW7OTG FC Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4. TTW7OTG EC EC 4.4.1.20 TTW7OTG PD 5HV9; 4WAB; 4JRZ; 4JCZ; 4JC7 TTW7OTG SQ MKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGIFFHEGAAALCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVALAALGLLAHFLPAALRAALLGRLRTLLPWA TTW7OTG TT Patented-recorded TTW7OTG FM Carbon-sulfur lyases TTWL9TY ID TTWL9TY TTWL9TY TN LIM domain kinase-1 (LIMK-1) TTWL9TY UP P53667 TTWL9TY UC LIMK1_HUMAN TTWL9TY BC Kinase TTWL9TY SN LIMK-1; LIMK TTWL9TY GN LIMK1 TTWL9TY FC Acts downstream of several Rho family GTPase signal transduction pathways. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1). Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. TTWL9TY EC EC 2.7.11.1 TTWL9TY PD 5NXC; 5L6W; 5HVK; 5HVJ; 3S95 TTWL9TY SQ MRLTLLCCTWREERMGEEGSELPVCASCGQRIYDGQYLQALNADWHADCFRCCDCSASLSHQYYEKDGQLFCKKDYWARYGESCHGCSEQITKGLVMVAGELKYHPECFICLTCGTFIGDGDTYTLVEHSKLYCGHCYYQTVVTPVIEQILPDSPGSHLPHTVTLVSIPASSHGKRGLSVSIDPPHGPPGCGTEHSHTVRVQGVDPGCMSPDVKNSIHVGDRILEINGTPIRNVPLDEIDLLIQETSRLLQLTLEHDPHDTLGHGLGPETSPLSSPAYTPSGEAGSSARQKPVLRSCSIDRSPGAGSLGSPASQRKDLGRSESLRVVCRPHRIFRPSDLIHGEVLGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDSQYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKNVVVADFGLARLMVDEKTQPEGLRSLKKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDFGLNVRGFLDRYCPPNCPPSFFPITVRCCDLDPEKRPSFVKLEHWLETLRMHLAGHLPLGPQLEQLDRGFWETYRRGESGLPAHPEVPD TTWL9TY TT Literature-reported TTASMD8 ID TTASMD8 TTASMD8 TN LIM domain kinase-2 (LIMK-2) TTASMD8 UP P53671 TTASMD8 UC LIMK2_HUMAN TTASMD8 BC Kinase TTASMD8 SN LIMK-2; LIM domain kinase 2 TTASMD8 GN LIMK2 TTASMD8 FC Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. TTASMD8 EC EC 2.7.11.1 TTASMD8 PD 5NXD; 4TPT; 1X6A TTASMD8 SQ MSALAGEDVWRCPGCGDHIAPSQIWYRTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDYWGKFGEFCHGCSLLMTGPFMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQEQLPYSVTLISMPATTEGRRGFSVSVESACSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAISQTSQTLQLLIEHDPVSQRLDQLRLEARLAPHMQNAGHPHALSTLDTKENLEGTLRRRSLRRSNSISKSPGPSSPKEPLLFSRDISRSESLRCSSSYSQQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALSLYLGELGIPLPAELEELDHTVSMQYGLTRDSPP TTASMD8 TT Literature-reported TTIKUVC ID TTIKUVC TTIKUVC TN Linear ubiquitin chain assembly complex (RBCK1) TTIKUVC UP Q9BYM8 TTIKUVC UC HOIL1_HUMAN TTIKUVC BC Acyltransferase TTIKUVC SN XAP4; XAP3; Ubiquitin-conjugating enzyme 7-interacting protein 3; UBCE7IP3; RanBP-type and C3HC4-type zinc finger-containing protein 1; RNF54; RING-type E3 ubiquitin transferase HOIL-1; RING finger protein 54; Hepatitis B virus X-associated protein 4; Heme-oxidized IRP2 ubiquitin ligase 1; HOIL-1; HBV-associated factor 4; C20orf18 TTIKUVC GN RBCK1 TTIKUVC FC Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types. E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. TTIKUVC EC EC 2.3.2.31 TTIKUVC PD 4DBG; 2LGY; 2CRC TTIKUVC SQ MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPLSVQLKPEVSPTQDIRLWVSVEDAQMHTVTIWLTVRPDMTVASLKDMVFLDYGFPPVLQQWVIGQRLARDQETLHSHGVRQNGDSAYLYLLSARNTSLNPQELQRERQLRMLEDLGFKDLTLQPRGPLEPGPPKPGVPQEPGRGQPDAVPEPPPVGWQCPGCTFINKPTRPGCEMCCRARPEAYQVPASYQPDEEERARLAGEEEALRQYQQRKQQQQEGNYLQHVQLDQRSLVLNTEPAECPVCYSVLAPGEAVVLRECLHTFCRECLQGTIRNSQEAEVSCPFIDNTYSCSGKLLEREIKALLTPEDYQRFLDLGISIAENRSAFSYHCKTPDCKGWCFFEDDVNEFTCPVCFHVNCLLCKAIHEQMNCKEYQEDLALRAQNDVAARQTTEMLKVMLQQGEAMRCPQCQIVVQKKDGCDWIRCTVCHTEICWVTKGPRWGPGGPGDTSGGCRCRVNGIPCHPSCQNCH TTIKUVC TT Literature-reported TTIKUVC FM Carbon-nitrogen ligase TTEBMN7 ID TTEBMN7 TTEBMN7 TN Long transient receptor potential channel 2 (TRPM2) TTEBMN7 UP O94759 TTEBMN7 UC TRPM2_HUMAN TTEBMN7 BC Transient receptor potential catioin channel TTEBMN7 SN TrpC7; Transient receptor potential melastatin 2; Transient receptor potential channel 7; Transient receptor potential cation channel subfamily M member 2; LTrpC2; LTrpC-2; Estrogen-responsive element-associated gene 1 protein; EREG1 TTEBMN7 GN TRPM2 TTEBMN7 FC Isoform 1: Nonselective, voltage-independent cation channel that mediates Na(+) and Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels. Functions as ligand-gated ion channel. Binding of ADP-ribose to the cytoplasmic Nudix domain causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening. Extracellular calcium passes through the channel and increases channel activity. Contributes to Ca(2+) release from intracellular stores in response to ADP-ribose. Plays a role in numerous processes that involve signaling via intracellular Ca(2+) levels (Probable). Besides, mediates the release of lysosomal Zn(2+) stores in response to reactive oxygen species, leading to increased cytosolic Zn(2+) levels. Activated by moderate heat (35 to 40 degrees Celsius). Activated by intracellular ADP-ribose, beta-NAD (NAD(+)) and similar compounds, and by oxidative stress caused by reactive oxygen or nitrogen species. The precise physiological activators are under debate; the true, physiological activators may be ADP-ribose and ADP-ribose-2'-phosphate. Activation by ADP-ribose and beta-NAD is strongly increased by moderate heat (35 to 40 degrees Celsius). Likewise, reactive oxygen species lower the threshold for activation by moderate heat (37 degrees Celsius). Plays a role in mediating behavorial and physiological responses to moderate heat and thereby contributes to body temperature homeostasis. Plays a role in insulin secretion, a process that requires increased cytoplasmic Ca(2+) levels (By similarity). Required for normal IFNG and cytokine secretion and normal innate immune immunity in response to bacterial infection. Required for normal phagocytosis and cytokine release by macrophages exposed to zymosan (in vitro). Plays a role in dendritic cell differentiation and maturation, and in dendritic cell chemotaxis via its role in regulating cytoplasmic Ca(2+) levels (By similarity). Plays a role in the regulation of the reorganization of the actin cytoskeleton and filopodia formation in response to reactive oxygen species via its role in increasing cytoplasmic Ca(2+) and Zn(2+) levels. Confers susceptibility to cell death following oxidative stress. TTEBMN7 PD 6MJ2; 6MIZ; 6MIX TTEBMN7 SQ MEPSALRKAGSEQEEGFEGLPRRVTDLGMVSNLRRSNSSLFKSWRLQCPFGNNDKQESLSSWIPENIKKKECVYFVESSKLSDAGKVVCQCGYTHEQHLEEATKPHTFQGTQWDPKKHVQEMPTDAFGDIVFTGLSQKVKKYVRVSQDTPSSVIYHLMTQHWGLDVPNLLISVTGGAKNFNMKPRLKSIFRRGLVKVAQTTGAWIITGGSHTGVMKQVGEAVRDFSLSSSYKEGELITIGVATWGTVHRREGLIHPTGSFPAEYILDEDGQGNLTCLDSNHSHFILVDDGTHGQYGVEIPLRTRLEKFISEQTKERGGVAIKIPIVCVVLEGGPGTLHTIDNATTNGTPCVVVEGSGRVADVIAQVANLPVSDITISLIQQKLSVFFQEMFETFTESRIVEWTKKIQDIVRRRQLLTVFREGKDGQQDVDVAILQALLKASRSQDHFGHENWDHQLKLAVAWNRVDIARSEIFMDEWQWKPSDLHPTMTAALISNKPEFVKLFLENGVQLKEFVTWDTLLYLYENLDPSCLFHSKLQKVLVEDPERPACAPAAPRLQMHHVAQVLRELLGDFTQPLYPRPRHNDRLRLLLPVPHVKLNVQGVSLRSLYKRSSGHVTFTMDPIRDLLIWAIVQNRRELAGIIWAQSQDCIAAALACSKILKELSKEEEDTDSSEEMLALAEEYEHRAIGVFTECYRKDEERAQKLLTRVSEAWGKTTCLQLALEAKDMKFVSHGGIQAFLTKVWWGQLSVDNGLWRVTLCMLAFPLLLTGLISFREKRLQDVGTPAARARAFFTAPVVVFHLNILSYFAFLCLFAYVLMVDFQPVPSWCECAIYLWLFSLVCEEMRQLFYDPDECGLMKKAALYFSDFWNKLDVGAILLFVAGLTCRLIPATLYPGRVILSLDFILFCLRLMHIFTISKTLGPKIIIVKRMMKDVFFFLFLLAVWVVSFGVAKQAILIHNERRVDWLFRGAVYHSYLTIFGQIPGYIDGVNFNPEHCSPNGTDPYKPKCPESDATQQRPAFPEWLTVLLLCLYLLFTNILLLNLLIAMFNYTFQQVQEHTDQIWKFQRHDLIEEYHGRPAAPPPFILLSHLQLFIKRVVLKTPAKRHKQLKNKLEKNEEAALLSWEIYLKENYLQNRQFQQKQRPEQKIEDISNKVDAMVDLLDLDPLKRSGSMEQRLASLEEQVAQTAQALHWIVRTLRASGFSSEADVPTLASQKAAEEPDAEPGGRKKTEEPGDSYHVNARHLLYPNCPVTRFPVPNEKVPWETEFLIYDPPFYTAERKDAAAMDPMGDTLEPLSTIQYNVVDGLRDRRSFHGPYTVQAGLPLNPMGRTGLRGRGSLSCFGPNHTLYPMVTRWRRNEDGAICRKSIKKMLEVLVVKLPLSEHWALPGGSREPGEMLPRKLKRILRQEHWPSFENLLKCGMEVYKGYMDDPRNTDNAWIETVAVSVHFQDQNDVELNRLNSNLHACDSGASIRWQVVDRRIPLYANHKTLLQKAAAEFGAHY TTEBMN7 TT Literature-reported TTEBMN7 RC R-HSA-3295583:TRP channels TTUWQTK ID TTUWQTK TTUWQTK TN Lysine N-methyltransferase 1A (SUV39H1) TTUWQTK UP O43463 TTUWQTK UC SUV91_HUMAN TTUWQTK BC Methyltransferase TTUWQTK SN Suppressor of variegation 3-9 homolog 1; Su(var)3-9 homolog 1; SUV39H; Position-effect variegation 3-9 homolog; KMT1A; Histone-lysine N-methyltransferase SUV39H1; Histone H3-K9 methyltransferase 1; H3-K9-HMTase 1 TTUWQTK GN SUV39H1 TTUWQTK FC Weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. TTUWQTK EC EC 2.1.1.43 TTUWQTK PD 3MTS TTUWQTK SQ MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKGIRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF TTUWQTK TT Literature-reported TTPC3H4 ID TTPC3H4 TTPC3H4 TN Lysine N-methyltransferase 3A (SETD2) TTPC3H4 UP Q9BYW2 TTPC3H4 UC SETD2_HUMAN TTPC3H4 BC Methyltransferase TTPC3H4 SN p231HBP; hSET2; SET2; SET domain-containing protein 2; Protein-lysine N-methyltransferase SETD2; KMT3A; KIAA1732; Huntingtin-interacting protein B; Huntingtin-interacting protein 1; Huntingtin yeast partner B; Histone-lysine N-methyltransferase SETD2; HYPB; HSPC069; HIP-1; HIF1 TTPC3H4 GN SETD2 TTPC3H4 FC Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation. Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A. Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction. Required for DNA double-strand break repair in response to DNA damage: acts by mediating formation of H3K36me3, promoting recruitment of RAD51 and DNA repair via homologous recombination (HR). Acts as a tumor suppressor. H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A. H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase. Required during angiogenesis. Required for endoderm development by promoting embryonic stem cell differentiation toward endoderm: acts by mediating formation of H3K36me3 in distal promoter regions of FGFR3, leading to regulate transcription initiation of FGFR3. In addition to histones, also mediates methylation of other proteins, such as tubulins and STAT1. Trimethylates 'Lys-40' of alpha-tubulins such as TUBA1B (alpha-TubK40me3); alpha-TubK40me3 is required for normal mitosis and cytokinesis and may be a specific tag in cytoskeletal remodeling. Involved in interferon-alpha-induced antiviral defense by mediating both monomethylation of STAT1 at 'Lys-525' and catalyzing H3K36me3 on promoters of some interferon-stimulated genes (ISGs) to activate gene transcription. Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate. TTPC3H4 EC EC 2.1.1.43 TTPC3H4 PD 5V22; 5V21; 5LT8; 5LT7; 5LT6 TTPC3H4 SQ MKQLQPQPPPKMGDFYDPEHPTPEEEENEAKIENVQKTGFIKGPMFKGVASSRFLPKGTKTKVNLEEQGRQKVSFSFSLTKKTLQNRFLTALGNEKQSDTPNPPAVPLQVDSTPKMKMEIGDTLSTAEESSPPKSRVELGKIHFKKHLLHVTSRPLLATTTAVASPPTHAAPLPAVIAESTTVDSPPSSPPPPPPPAQATTLSSPAPVTEPVALPHTPITVLMAAPVPLPVDVAVRSLKEPPIIIVPESLEADTKQDTISNSLEEHVTQILNEQADISSKKEDSHIGKDEEIPDSSKISLSCKKTGSKKKSSQSEGIFLGSESDEDSVRTSSSQRSHDLKFSASIEKERDFKKSSAPLKSEDLGKPSRSKTDRDDKYFSYSKLERDTRYVSSRCRSERERRRSRSHSRSERGSRTNLSYSRSERSHYYDSDRRYHRSSPYRERTRYSRPYTDNRARESSDSEEEYKKTYSRRTSSHSSSYRDLRTSSYSKSDRDCKTETSYLEMERRGKYSSKLERESKRTSENEAIKRCCSPPNELGFRRGSSYSKHDSSASRYKSTLSKPIPKSDKFKNSFCCTELNEEIKQSHSFSLQTPCSKGSELRMINKNPEREKAGSPAPSNRLNDSPTLKKLDELPIFKSEFITHDSHDSIKELDSLSKVKNDQLRSFCPIELNINGSPGAESDLATFCTSKTDAVLMTSDDSVTGSELSPLVKACMLSSNGFQNISRCKEKDLDDTCMLHKKSESPFRETEPLVSPHQDKLMSMPVMTVDYSKTVVKEPVDTRVSCCKTKDSDIYCTLNDSNPSLCNSEAENIEPSVMKISSNSFMNVHLESKPVICDSRNLTDHSKFACEEYKQSIGSTSSASVNHFDDLYQPIGSSGIASSLQSLPPGIKVDSLTLLKCGENTSPVLDAVLKSKKSSEFLKHAGKETIVEVGSDLPDSGKGFASRENRRNNGLSGKCLQEAQEEGNSILPERRGRPEISLDERGEGGHVHTSDDSEVVFSSCDLNLTMEDSDGVTYALKCDSSGHAPEIVSTVHEDYSGSSESSNDESDSEDTDSDDSSIPRNRLQSVVVVPKNSTLPMEETSPCSSRSSQSYRHYSDHWEDERLESRRHLYEEKFESIASKACPQTDKFFLHKGTEKNPEISFTQSSRKQIDNRLPELSHPQSDGVDSTSHTDVKSDPLGHPNSEETVKAKIPSRQQEELPIYSSDFEDVPNKSWQQTTFQNRPDSRLGKTELSFSSSCEIPHVDGLHSSEELRNLGWDFSQEKPSTTYQQPDSSYGACGGHKYQQNAEQYGGTRDYWQGNGYWDPRSGRPPGTGVVYDRTQGQVPDSLTDDREEEENWDQQDGSHFSDQSDKFLLSLQKDKGSVQAPEISSNSIKDTLAVNEKKDFSKNLEKNDIKDRGPLKKRRQEIESDSESDGELQDRKKVRVEVEQGETSVPPGSALVGPSCVMDDFRDPQRWKECAKQGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCECTPLSKDERAQGEIACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGKMKKERSRKKDSVDGELEALMENGEGLSDKNQVLSLSRLMVRIETLEQKLTCLELIQNTHSQSCLKSFLERHGLSLLWIWMAELGDGRESNQKLQEEIIKTLEHLPIPTKNMLEESKVLPIIQRWSQTKTAVPPLSEGDGYSSENTSRAHTPLNTPDPSTKLSTEADTDTPKKLMFRRLKIISENSMDSAISDATSELEGKDGKEDLDQLENVPVEEEEELQSQQLLPQQLPECKVDSETNIEASKLPTSEPEADAEIEPKESNGTKLEEPINEETPSQDEEEGVSDVESERSQEQPDKTVDISDLATKLLDSWKDLKEVYRIPKKSQTEKENTTTERGRDAVGFRDQTPAPKTPNRSRERDPDKQTQNKEKRKRRSSLSPPSSAYERGTKRPDDRYDTPTSKKKVRIKDRNKLSTEERRKLFEQEVAQREAQKQQQQMQNLGMTSPLPYDSLGYNAPHHPFAGYPPGYPMQAYVDPSNPNAGKVLLPTPSMDPVCSPAPYDHAQPLVGHSTEPLSAPPPVPVVPHVAAPVEVSSSQYVAQSDGVVHQDSSVAVLPVPAPGPVQGQNYSVWDSNQQSVSVQQQYSPAQSQATIYYQGQTCPTVYGVTSPYSQTTPPIVQSYAQPSLQYIQGQQIFTAHPQGVVVQPAAAVTTIVAPGQPQPLQPSEMVVTNNLLDLPPPSPPKPKTIVLPPNWKTARDPEGKIYYYHVITRQTQWDPPTWESPGDDASLEHEAEMDLGTPTYDENPMKASKKPKTAEADTSSELAKKSKEVFRKEMSQFIVQCLNPYRKPDCKVGRITTTEDFKHLARKLTHGVMNKELKYCKNPEDLECNENVKHKTKEYIKKYMQKFGAVYKPKEDTELE TTPC3H4 TT Literature-reported TTPC3H4 FM Class V-like SAM-binding methyltransferase superfamily TTTSJ3H ID TTTSJ3H TTTSJ3H TN Lysine N-methyltransferase 3B (NSD1) TTTSJ3H UP Q96L73 TTTSJ3H UC NSD1_HUMAN TTTSJ3H BC Methyltransferase TTTSJ3H SN Nuclear receptor-binding SET domain-containing protein 1; NR-binding SET domain-containing protein; NR-binding SET domain containing protein; KMT3B; Hypothetical protein FLJ22263 similar to nuclear receptor-binding SET-domain protein 1; Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific; H4-K20-HMTase; H3-K36-HMTase; Androgen receptor-associated protein of 267 kDa; Androgen receptor-associated coregulator 267; Androgen receptor coactivator 267 kDa protein; Androgen receptor associated coregulator 267; ARA267 TTTSJ3H GN NSD1 TTTSJ3H FC Preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro). Transcriptional intermediary factor capable of both negatively or positively influencing transcription, depending on the cellular context. Histone methyltransferase. TTTSJ3H EC EC 2.1.1.43 TTTSJ3H PD 3OOI TTTSJ3H SQ MDQTCELPRRNCLLPFSNPVNLDAPEDKDSPFGNGQSNFSEPLNGCTMQLSTVSGTSQNAYGQDSPSCYIPLRRLQDLASMINVEYLNGSADGSESFQDPEKSDSRAQTPIVCTSLSPGGPTALAMKQEPSCNNSPELQVKVTKTIKNGFLHFENFTCVDDADVDSEMDPEQPVTEDESIEEIFEETQTNATCNYETKSENGVKVAMGSEQDSTPESRHGAVKSPFLPLAPQTETQKNKQRNEVDGSNEKAALLPAPFSLGDTNITIEEQLNSINLSFQDDPDSSTSTLGNMLELPGTSSSSTSQELPFCQPKKKSTPLKYEVGDLIWAKFKRRPWWPCRICSDPLINTHSKMKVSNRRPYRQYYVEAFGDPSERAWVAGKAIVMFEGRHQFEELPVLRRRGKQKEKGYRHKVPQKILSKWEASVGLAEQYDVPKGSKNRKCIPGSIKLDSEEDMPFEDCTNDPESEHDLLLNGCLKSLAFDSEHSADEKEKPCAKSRARKSSDNPKRTSVKKGHIQFEAHKDERRGKIPENLGLNFISGDISDTQASNELSRIANSLTGSNTAPGSFLFSSCGKNTAKKEFETSNGDSLLGLPEGALISKCSREKNKPQRSLVCGSKVKLCYIGAGDEEKRSDSISICTTSDDGSSDLDPIEHSSESDNSVLEIPDAFDRTENMLSMQKNEKIKYSRFAATNTRVKAKQKPLISNSHTDHLMGCTKSAEPGTETSQVNLSDLKASTLVHKPQSDFTNDALSPKFNLSSSISSENSLIKGGAANQALLHSKSKQPKFRSIKCKHKENPVMAEPPVINEECSLKCCSSDTKGSPLASISKSGKVDGLKLLNNMHEKTRDSSDIETAVVKHVLSELKELSYRSLGEDVSDSGTSKPSKPLLFSSASSQNHIPIEPDYKFSTLLMMLKDMHDSKTKEQRLMTAQNLVSYRSPGRGDCSTNSPVGVSKVLVSGGSTHNSEKKGDGTQNSANPSPSGGDSALSGELSASLPGLLSDKRDLPASGKSRSDCVTRRNCGRSKPSSKLRDAFSAQMVKNTVNRKALKTERKRKLNQLPSVTLDAVLQGDRERGGSLRGGAEDPSKEDPLQIMGHLTSEDGDHFSDVHFDSKVKQSDPGKISEKGLSFENGKGPELDSVMNSENDELNGVNQVVPKKRWQRLNQRRTKPRKRMNRFKEKENSECAFRVLLPSDPVQEGRDEFPEHRTPSASILEEPLTEQNHADCLDSAGPRLNVCDKSSASIGDMEKEPGIPSLTPQAELPEPAVRSEKKRLRKPSKWLLEYTEEYDQIFAPKKKQKKVQEQVHKVSSRCEEESLLARGRSSAQNKQVDENSLISTKEEPPVLEREAPFLEGPLAQSELGGGHAELPQLTLSVPVAPEVSPRPALESEELLVKTPGNYESKRQRKPTKKLLESNDLDPGFMPKKGDLGLSKKCYEAGHLENGITESCATSYSKDFGGGTTKIFDKPRKRKRQRHAAAKMQCKKVKNDDSSKEIPGSEGELMPHRTATSPKETVEEGVEHDPGMPASKKMQGERGGGAALKENVCQNCEKLGELLLCEAQCCGAFHLECLGLTEMPRGKFICNECRTGIHTCFVCKQSGEDVKRCLLPLCGKFYHEECVQKYPPTVMQNKGFRCSLHICITCHAANPANVSASKGRLMRCVRCPVAYHANDFCLAAGSKILASNSIICPNHFTPRRGCRNHEHVNVSWCFVCSEGGSLLCCDSCPAAFHRECLNIDIPEGNWYCNDCKAGKKPHYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTYKKALQEAAARFEELKAQKELRQLQEDRKNDKKPPPYKHIKVNRPIGRVQIFTADLSEIPRCNCKATDENPCGIDSECINRMLLYECHPTVCPAGGRCQNQCFSKRQYPEVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLGVRPKNQPIATEEKSKKFKKKQQGKRRTQGEITKEREDECFSCGDAGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWHQCDICGKEAASFCEMCPSSFCKQHREGMLFISKLDGRLSCTEHDPCGPNPLEPGEIREYVPPPVPLPPGPSTHLAEQSTGMAAQAPKMSDKPPADTNQMLSLSKKALAGTCQRPLLPERPLERTDSRPQPLDKVRDLAGSGTKSQSLVSSQRPLDRPPAVAGPRPQLSDKPSPVTSPSSSPSVRSQPLERPLGTADPRLDKSIGAASPRPQSLEKTSVPTGLRLPPPDRLLITSSPKPQTSDRPTDKPHASLSQRLPPPEKVLSAVVQTLVAKEKALRPVDQNTQSKNRAALVMDLIDLTPRQKERAASPHQVTPQADEKMPVLESSSWPASKGLGHMPRAVEKGCVSDPLQTSGKAAAPSEDPWQAVKSLTQARLLSQPPAKAFLYEPTTQASGRASAGAEQTPGPLSQSPGLVKQAKQMVGGQQLPALAAKSGQSFRSLGKAPASLPTEEKKLVTTEQSPWALGKASSRAGLWPIVAGQTLAQSCWSAGSTQTLAQTCWSLGRGQDPKPEQNTLPALNQAPSSHKCAESEQK TTTSJ3H TT Literature-reported TTTSJ3H FM Methyltransferase superfamily TTIG67W ID TTIG67W TTIG67W TN Lysine-specific demethylase 5A (KDM5A) TTIG67W UP P29375 TTIG67W UC KDM5A_HUMAN TTIG67W BC Paired donor oxygen oxidoreductase TTIG67W SN Retinoblastoma-binding protein 2; RBP2; RBBP2; RBBP-2; Jumonji/ARID domain-containing protein 1A; JARID1A; Histone demethylase JARID1A TTIG67W GN KDM5A TTIG67W FC Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Regulates specific gene transcription through DNA-binding on 5'-CCGCCC-3' motif. May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation. May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1. Seems to act as a transcriptional corepressor for some genes such as MT1F and to favor the proliferation of cancer cells. Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. TTIG67W EC EC 1.14.11.- TTIG67W PD 6DQB; 6DQA; 6DQ9; 6DQ8; 6DQ6 TTIG67W SQ MAGVGPGGYAAEFVPPPECPVFEPSWEEFTDPLSFIGRIRPLAEKTGICKIRPPKDWQPPFACEVKSFRFTPRVQRLNELEAMTRVRLDFLDQLAKFWELQGSTLKIPVVERKILDLYALSKIVASKGGFEMVTKEKKWSKVGSRLGYLPGKGTGSLLKSHYERILYPYELFQSGVSLMGVQMPNLDLKEKVEPEVLSTDTQTSPEPGTRMNILPKRTRRVKTQSESGDVSRNTELKKLQIFGAGPKVVGLAMGTKDKEDEVTRRRKVTNRSDAFNMQMRQRKGTLSVNFVDLYVCMFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCVAEECSKPREAFGFEQAVREYTLQSFGEMADNFKSDYFNMPVHMVPTELVEKEFWRLVSSIEEDVIVEYGADISSKDFGSGFPVKDGRRKILPEEEEYALSGWNLNNMPVLEQSVLAHINVDISGMKVPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPSHAAEQLEEVMRELAPELFESQPDLLHQLVTIMNPNVLMEHGVPVYRTNQCAGEFVVTFPRAYHSGFNQGYNFAEAVNFCTADWLPIGRQCVNHYRRLRRHCVFSHEELIFKMAADPECLDVGLAAMVCKELTLMTEEETRLRESVVQMGVLMSEEEVFELVPDDERQCSACRTTCFLSALTCSCNPERLVCLYHPTDLCPCPMQKKCLRYRYPLEDLPSLLYGVKVRAQSYDTWVSRVTEALSANFNHKKDLIELRVMLEDAEDRKYPENDLFRKLRDAVKEAETCASVAQLLLSKKQKHRQSPDSGRTRTKLTVEELKAFVQQLFSLPCVISQARQVKNLLDDVEEFHERAQEAMMDETPDSSKLQMLIDMGSSLYVELPELPRLKQELQQARWLDEVRLTLSDPQQVTLDVMKKLIDSGVGLAPHHAVEKAMAELQELLTVSERWEEKAKVCLQARPRHSVASLESIVNEAKNIPAFLPNVLSLKEALQKAREWTAKVEAIQSGSNYAYLEQLESLSAKGRPIPVRLEALPQVESQVAAARAWRERTGRTFLKKNSSHTLLQVLSPRTDIGVYGSGKNRRKKVKELIEKEKEKDLDLEPLSDLEEGLEETRDTAMVVAVFKEREQKEIEAMHSLRAANLAKMTMVDRIEEVKFCICRKTASGFMLQCELCKDWFHNSCVPLPKSSSQKKGSSWQAKEVKFLCPLCMRSRRPRLETILSLLVSLQKLPVRLPEGEALQCLTERAMSWQDRARQALATDELSSALAKLSVLSQRMVEQAAREKTEKIISAELQKAAANPDLQGHLPSFQQSAFNRVVSSVSSSPRQTMDYDDEETDSDEDIRETYGYDMKDTASVKSSSSLEPNLFCDEEIPIKSEEVVTHMWTAPSFCAEHAYSSASKSCSQGSSTPRKQPRKSPLVPRSLEPPVLELSPGAKAQLEELMMVGDLLEVSLDETQHIWRILQATHPPSEDRFLHIMEDDSMEEKPLKVKGKDSSEKKRKRKLEKVEQLFGEGKQKSKELKKMDKPRKKKLKLGADKSKELNKLAKKLAKEEERKKKKEKAAAAKVELVKESTEKKREKKVLDIPSKYDWSGAEESDDENAVCAAQNCQRPCKDKVDWVQCDGGCDEWFHQVCVGVSPEMAENEDYICINCAKKQGPVSPGPAPPPSFIMSYKLPMEDLKETS TTIG67W TT Patented-recorded TTIG67W FM Oxidoreductases acting on paired donors TTCLI75 ID TTCLI75 TTCLI75 TN Lysine-specific demethylase 5B (KDM5B) TTCLI75 UP Q9UGL1 TTCLI75 UC KDM5B_HUMAN TTCLI75 BC Paired donor oxygen oxidoreductase TTCLI75 SN Retinoblastomabinding protein 2 homolog 1; Retinoblastoma-binding protein 2 homolog 1; RBP2H1; RBP2-H1; RBBP2H1; PLU1; PLU-1; Lysinespecific demethylase 5B; Jumonji/ARID domaincontaining protein 1B; Jumonji/ARID domain-containing protein 1B; JARID1B; Histone demethylase JARID1B; Cancer/testis antigen 31; CT31 TTCLI75 GN KDM5B TTCLI75 FC Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2. Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. TTCLI75 EC EC 1.14.11.- TTCLI75 PD 6EK6; 6EJ1; 6EJ0; 6EIY; 6EIU TTCLI75 SQ MEAATTLHPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKLVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTPKKKKIKLSHPKDMNNFKLERERSYELVRSAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVDWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTVKDAPSRK TTCLI75 TT Literature-reported TTCLI75 FM Oxidoreductases acting on paired donors TT94UCF ID TT94UCF TT94UCF TN Lysine-specific demethylase 5C (KDM5C) TT94UCF UP P41229 TT94UCF UC KDM5C_HUMAN TT94UCF BC Paired donor oxygen oxidoreductase TT94UCF SN XE169; SMCX; Protein Xe169; Protein SmcX; Jumonji/ARID domain-containing protein 1C; JARID1C; Histone demethylase JARID1C; DXS1272E TT94UCF GN KDM5C TT94UCF FC Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2. Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. TT94UCF EC EC 1.14.11.- TT94UCF PD 5FWJ; 2JRZ TT94UCF SQ MEPGSDDFLPPPECPVFEPSWAEFRDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEVDNFRFTPRIQRLNELEAQTRVKLNYLDQIAKFWEIQGSSLKIPNVERRILDLYSLSKIVVEEGGYEAICKDRRWARVAQRLNYPPGKNIGSLLRSHYERIVYPYEMYQSGANLVQCNTRPFDNEEKDKEYKPHSIPLRQSVQPSKFNSYGRRAKRLQPDPEPTEEDIEKNPELKKLQIYGAGPKMMGLGLMAKDKTLRKKDKEGPECPPTVVVKEELGGDVKVESTSPKTFLESKEELSHSPEPCTKMTMRLRRNHSNAQFIESYVCRMCSRGDEDDKLLLCDGCDDNYHIFCLLPPLPEIPKGVWRCPKCVMAECKRPPEAFGFEQATREYTLQSFGEMADSFKADYFNMPVHMVPTELVEKEFWRLVNSIEEDVTVEYGADIHSKEFGSGFPVSDSKRHLTPEEEEYATSGWNLNVMPVLEQSVLCHINADISGMKVPWLYVGMVFSAFCWHIEDHWSYSINYLHWGEPKTWYGVPSLAAEHLEEVMKKLTPELFDSQPDLLHQLVTLMNPNTLMSHGVPVVRTNQCAGEFVITFPRAYHSGFNQGYNFAEAVNFCTADWLPAGRQCIEHYRRLRRYCVFSHEELICKMAACPEKLDLNLAAAVHKEMFIMVQEERRLRKALLEKGITEAEREAFELLPDDERQCIKCKTTCFLSALACYDCPDGLVCLSHINDLCKCSSSRQYLRYRYTLDELPAMLHKLKVRAESFDTWANKVRVALEVEDGRKRSLEELRALESEARERRFPNSELLQQLKNCLSEAEACVSRALGLVSGQEAGPHRVAGLQMTLTELRAFLDQMNNLPCAMHQIGDVKGVLEQVEAYQAEAREALASLPSSPGLLQSLLERGRQLGVEVPEAQQLQRQVEQARWLDEVKRTLAPSARRGTLAVMRGLLVAGASVAPSPAVDKAQAELQELLTIAERWEEKAHLCLEARQKHPPATLEAIIREAENIPVHLPNIQALKEALAKARAWIADVDEIQNGDHYPCLDDLEGLVAVGRDLPVGLEELRQLELQVLTAHSWREKASKTFLKKNSCYTLLEVLCPCADAGSDSTKRSRWMEKELGLYKSDTELLGLSAQDLRDPGSVIVAFKEGEQKEKEGILQLRRTNSAKPSPLASSSTASSTTSICVCGQVLAGAGALQCDLCQDWFHGRCVSVPRLLSSPRPNPTSSPLLAWWEWDTKFLCPLCMRSRRPRLETILALLVALQRLPVRLPEGEALQCLTERAISWQGRARQALASEDVTALLGRLAELRQRLQAEPRPEEPPNYPAAPASDPLREGSGKDMPKVQGLLENGDSVTSPEKVAPEEGSGKRDLELLSSLLPQLTGPVLELPEATRAPLEELMMEGDLLEVTLDENHSIWQLLQAGQPPDLERIRTLLELEKAERHGSRARGRALERRRRRKVDRGGEGDDPAREELEPKRVRSSGPEAEEVQEEEELEEETGGEGPPAPIPTTGSPSTQENQNGLEPAEGTTSGPSAPFSTLTPRLHLPCPQQPPQQQL TT94UCF TT Literature-reported TTAOZBW ID TTAOZBW TTAOZBW TN Lysozyme (LYZ) TTAOZBW UP P61626 TTAOZBW UC LYSC_HUMAN TTAOZBW BC Glycosylase TTAOZBW SN Lysozyme C; LYZ; 1,4betaNacetylmuramidase C TTAOZBW GN LYZ TTAOZBW FC Lysozymes have primarily a bacteriolytic function; those intissues and body fluids are associated with the monocyte- macrophage system and enhance the activity of immunoagents. TTAOZBW EC EC 3.2.1.17 TTAOZBW PD 5LVK; 5LSH; 4R0P; 4ML7; 4I0C TTAOZBW SQ MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV TTAOZBW TT Literature-reported TT1KW50 ID TT1KW50 TT1KW50 TN Maspin (SERPINB5) TT1KW50 UP P36952 TT1KW50 UC SPB5_HUMAN TT1KW50 BC Serpin protein TT1KW50 SN Serpin B5; Protease inhibitor 5; Peptidase inhibitor 5; PI5; PI-5 TT1KW50 GN SERPINB5 TT1KW50 FC It blocks the growth, invasion, and metastatic properties of mammary tumors. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. Tumor suppressor. TT1KW50 PD 1XU8; 1XQJ; 1XQG; 1WZ9 TT1KW50 SQ MDALQLANSAFAVDLFKQLCEKEPLGNVLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDVPFGFQTVTSDVNKLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINNSIKDLTDGHFENILADNSVNDQTKILVVNAAYFVGKWMKKFSESETKECPFRVNKTDTKPVQMMNMEATFCMGNIDSINCKIIELPFQNKHLSMFILLPKDVEDESTGLEKIEKQLNSESLSQWTNPSTMANAKVKLSIPKFKVEKMIDPKACLENLGLKHIFSEDTSDFSGMSETKGVALSNVIHKVCLEITEDGGDSIEVPGARILQHKDELNADHPFIYIIRHNKTRNIIFFGKFCSP TT1KW50 TT Literature-reported TT1KW50 FM Serpin family TT1KW50 KE hsa04115:p53 signaling pathway; hsa05206:MicroRNAs in cancer TTXLEG7 ID TTXLEG7 TTXLEG7 TN Matrix metalloproteinase-10 (MMP-10) TTXLEG7 UP P09238 TTXLEG7 UC MMP10_HUMAN TTXLEG7 BC Peptidase TTXLEG7 SN Transin-2; Stromelysin-2; STMY2; SL-2 TTXLEG7 GN MMP10 TTXLEG7 FC Activates procollagenase. Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. TTXLEG7 EC EC 3.4.24.22 TTXLEG7 PD 4ILW; 3V96; 1Q3A TTXLEG7 SQ MMHLAFLVLLCLPVCSAYPLSGAAKEEDSNKDLAQQYLEKYYNLEKDVKQFRRKDSNLIVKKIQGMQKFLGLEVTGKLDTDTLEVMRKPRCGVPDVGHFSSFPGMPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYPPGPGLYGDIHFDDDEKWTEDASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSFTELAQFRLSQDDVNGIQSLYGPPPASTEEPLVPTKSVPSGSEMPAKCDPALSFDAISTLRGEYLFFKDRYFWRRSHWNPEPEFHLISAFWPSLPSYLDAAYEVNSRDTVFIFKGNEFWAIRGNEVQAGYPRGIHTLGFPPTIRKIDAAVSDKEKKKTYFFAADKYWRFDENSQSMEQGFPRLIADDFPGVEPKVDAVLQAFGFFYFFSGSSQFEFDPNARMVTHILKSNSWLHC TTXLEG7 TT Patented-recorded TTZW4MV ID TTZW4MV TTZW4MV TN Matrix metalloproteinase-11 (MMP-11) TTZW4MV UP P24347 TTZW4MV UC MMP11_HUMAN TTZW4MV BC Peptidase TTZW4MV SN Stromelysin-3 (ST3) gene; Stromelysin-3; STR-3; STMY3; ST3/MMP11; ST3; SL-3 TTZW4MV GN MMP11 TTZW4MV FC May play an important role in the progression of epithelial malignancies. TTZW4MV EC EC 3.4.24.- TTZW4MV SQ MAPAAWLRSAAARALLPPMLLLLLQPPPLLARALPPDAHHLHAERRGPQPWHAALPSSPAPAPATQEAPRPASSLRPPRCGVPDPSDGLSARNRQKRFVLSGGRWEKTDLTYRILRFPWQLVQEQVRQTMAEALKVWSDVTPLTFTEVHEGRADIMIDFARYWHGDDLPFDGPGGILAHAFFPKTHREGDVHFDYDETWTIGDDQGTDLLQVAAHEFGHVLGLQHTTAAKALMSAFYTFRYPLSLSPDDCRGVQHLYGQPWPTVTSRTPALGPQAGIDTNEIAPLEPDAPPDACEASFDAVSTIRGELFFFKAGFVWRLRGGQLQPGYPALASRHWQGLPSPVDAAFEDAQGHIWFFQGAQYWVYDGEKPVLGPAPLTELGLVRFPVHAALVWGPEKNKIYFFRGRDYWRFHPSTRRVDSPVPRRATDWRGVPSEIDAAFQDADGYAYFLRGRLYWKFDPVKVKALEGFPRLVGPDFFGCAEPANTFL TTZW4MV TT Literature-reported TTZW4MV FM Peptidase TTZW4MV RC R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases TTNP4CU ID TTNP4CU TTNP4CU TN Matrix metalloproteinase-16 (MMP-16) TTNP4CU UP P51512 TTNP4CU UC MMP16_HUMAN TTNP4CU BC Peptidase TTNP4CU SN Membrane-type-3 matrix metalloproteinase; Membrane-type matrix metalloproteinase 3; MTMMP3; MT3MMP; MT3-MMP; MT-MMP 3; MMPX2; MMP-X2; C8orf57 TTNP4CU GN MMP16 TTNP4CU FC Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells. Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. TTNP4CU EC EC 3.4.24.- TTNP4CU PD 1RM8 TTNP4CU SQ MILLTFSTGRRLDFVHHSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFHIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSIPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITVWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRVKEGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV TTNP4CU TT Literature-reported TTYRF5E ID TTYRF5E TTYRF5E TN Matrix metalloproteinase-21 (MMP-21) TTYRF5E UP Q8N119 TTYRF5E UC MMP21_HUMAN TTYRF5E BC Peptidase TTYRF5E SN MMP TTYRF5E GN MMP21 TTYRF5E FC May act as a negative regulator of the NOTCH-signaling pathway. Cleaves alpha-1-antitrypsin. Plays a specialized role in the generation of left-right asymmetry during embryogenesis. TTYRF5E EC EC 3.4.24.- TTYRF5E SQ MLAASIFRPTLLLCWLAAPWPTQPESLFHSRDRSDLEPSPLRQAKPIADLHAAQRFLSRYGWSGVWAAWGPSPEGPPETPKGAALAEAVRRFQRANALPASGELDAATLAAMNRPRCGVPDMRPPPPSAPPSPPGPPPRARSRRSPRAPLSLSRRGWQPRGYPDGGAAQAFSKRTLSWRLLGEALSSQLSVADQRRIVALAFRMWSEVTPLDFREDLAAPGAAVDIKLGFGRGRHLGCPRAFDGSGQEFAHAWRLGDIHFDDDEHFTPPTSDTGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPAFELDWSDRKAIQKLYGSCEGSFDTAFDWIRKERNQYGEVMVRFSTYFFRNSWYWLYENRNNRTRYGDPIQILTGWPGIPTHNIDAFVHIWTWKRDERYFFQGNQYWRYDSDKDQALTEDEQGKSYPKLISEGFPGIPSPLDTAFYDRRQKLIYFFKESLVFAFDVNRNRVLNSYPKRITEVFPAVIPQNHPFRNIDSAYYSYAYNSIFFFKGNAYWKVVNDKDKQQNSWLPANGLFPKKFISEKWFDVCDVHISTLNM TTYRF5E TT Literature-reported TTSHWUP ID TTSHWUP TTSHWUP TN MEK kinase kinase 1 (MAP4K1) TTSHWUP UP Q92918 TTSHWUP UC M4K1_HUMAN TTSHWUP BC Kinase TTSHWUP SN Mitogen-activated protein kinase kinase kinase kinase 1; MEKKK 1; MAPK/ERK kinase kinase kinase 1; Hematopoietic progenitor kinase; HPK1 TTSHWUP GN MAP4K1 TTSHWUP FC Appears to act upstream of the JUN N-terminal pathway. May play a role in hematopoietic lineage decisions and growth regulation. Able to autophosphorylate. Serine/threonine-protein kinase, which may play a role in the response to environmental stress. TTSHWUP EC EC 2.7.11.1 TTSHWUP PD 6NG0; 6NFZ; 6NFY; 6CQF; 6CQE TTSHWUP SQ MDVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILILKTCRHANIVAYHGSYLWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGISAQIGATLARRLSFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLFLMTKSGYQPPRLKEKGKWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKNPGKGPSIGDIEDEEPELPPAIPRRIRSTHRSSSLGIPDADCCRRHMEFRKLRGMETRPPANTARLQPPRDLRSSSPRKQLSESSDDDYDDVDIPTPAEDTPPPLPPKPKFRSPSDEGPGSMGDDGQLSPGVLVRCASGPPPNSPRPGPPPSTSSPHLTAHSEPSLWNPPSRELDKPPLLPPKKEKMKRKGCALLVKLFNGCPLRIHSTAAWTHPSTKDQHLLLGAEEGIFILNRNDQEATLEMLFPSRTTWVYSINNVLMSLSGKTPHLYSHSILGLLERKETRAGNPIAHISPHRLLARKNMVSTKIQDTKGCRACCVAEGASSGGPFLCGALETSVVLLQWYQPMNKFLLVRQVLFPLPTPLSVFALLTGPGSELPAVCIGVSPGRPGKSVLFHTVRFGALSCWLGEMSTEHRGPVQVTQVEEDMVMVLMDGSVKLVTPEGSPVRGLRTPEIPMTEAVEAVAMVGGQLQAFWKHGVQVWALGSDQLLQELRDPTLTFRLLGSPRLECSGTISPHCNLLLPGSSNSPASASRVAGITGL TTSHWUP TT Clinical trial TTSHWUP FM Kinase TTI0AHJ ID TTI0AHJ TTI0AHJ TN MEK kinase kinase 3 (MAP4K3) TTI0AHJ UP Q8IVH8 TTI0AHJ UC M4K3_HUMAN TTI0AHJ BC Kinase TTI0AHJ SN RAB8IPL1; Mitogen-activated protein kinase kinase kinase kinase 3; MEKKK 3; MAPK/ERK kinase kinase kinase 3; Germinal center kinase-related protein kinase; GLK TTI0AHJ GN MAP4K3 TTI0AHJ FC Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. TTI0AHJ EC EC 2.7.11.1 TTI0AHJ PD 5J5T TTI0AHJ SQ MNPGFDLSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHPNIVAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGPLSELQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAPEVAAVERKGGYNQLCDLWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQHLTRSLAIELLDKVNNPDHSTYHDFDDDDPEPLVAVPHRIHSTSRNVREEKTRSEITFGQVKFDPPLRKETEPHHELPDSDGFLDSSEEIYYTARSNLDLQLEYGQGHQGGYFLGANKSLLKSVEEELHQRGHVAHLEDDEGDDDESKHSTLKAKIPPPLPPKPKSIFIPQEMHSTEDENQGTIKRCPMSGSPAKPSQVPPRPPPPRLPPHKPVALGNGMSSFQLNGERDGSLCQQQNEHRGTNLSRKEKKDVPKPISNGLPPTPKVHMGACFSKVFNGCPLKIHCASSWINPDTRDQYLIFGAEEGIYTLNLNELHETSMEQLFPRRCTWLYVMNNCLLSISGKASQLYSHNLPGLFDYARQMQKLPVAIPAHKLPDRILPRKFSVSAKIPETKWCQKCCVVRNPYTGHKYLCGALQTSIVLLEWVEPMQKFMLIKHIDFPIPCPLRMFEMLVVPEQEYPLVCVGVSRGRDFNQVVRFETVNPNSTSSWFTESDTPQTNVTHVTQLERDTILVCLDCCIKIVNLQGRLKSSRKLSSELTFDFQIESIVCLQDSVLAFWKHGMQGRSFRSNEVTQEISDSTRIFRLLGSDRVVVLESRPTDNPTANSNLYILAGHENSY TTI0AHJ TT Literature-reported TTW8TJI ID TTW8TJI TTW8TJI TN MEKK1 messenger RNA (MAP3K1 mRNA) TTW8TJI UP Q13233 TTW8TJI UC M3K1_HUMAN TTW8TJI BC mRNA target TTW8TJI SN Mitogenactivated protein kinase kinase kinase 1 (mRNA); Mitogen-activated protein kinase kinase kinase 1 (mRNA); MEKK1 (mRNA); MEKK 1 (mRNA); MEKK (mRNA); MEK kinase 1 (mRNA); MAPKKK1 (mRNA) TTW8TJI GN MAP3K1 TTW8TJI FC Activates the ERK and JNK kinase pathways by phosphorylation of MAP2K1 and MAP2K4. May phosphorylate the MAPK8/JNK1 kinase. Activates CHUK and IKBKB, the central protein kinases of the NF-kappa-B pathway. Component of a protein kinase signal transduction cascade. TTW8TJI EC EC 2.7.11.25 TTW8TJI SQ MAAAAGNRASSSGFPGARATSPEAGGGGGALKASSAPAAAAGLLREAGSGGRERADWRRRQLRKVRSVELDQLPEQPLFLAASPPASSTSPSPEPADAAGSGTGFQPVAVPPPHGAASRGGAHLTESVAAPDSGASSPAAAEPGEKRAPAAEPSPAAAPAGREMENKETLKGLHKMDDRPEERMIREKLKATCMPAWKHEWLERRNRRGPVVVKPIPVKGDGSEMNHLAAESPGEVQASAASPASKGRRSPSPGNSPSGRTVKSESPGVRRKRVSPVPFQSGRITPPRRAPSPDGFSPYSPEETNRRVNKVMRARLYLLQQIGPNSFLIGGDSPDNKYRVFIGPQNCSCARGTFCIHLLFVMLRVFQLEPSDPMLWRKTLKNFEVESLFQKYHSRRSSRIKAPSRNTIQKFVSRMSNSHTLSSSSTSTSSSENSIKDEEEQMCPICLLGMLDEESLTVCEDGCRNKLHHHCMSIWAEECRRNREPLICPLCRSKWRSHDFYSHELSSPVDSPSSLRAAQQQTVQQQPLAGSRRNQESNFNLTHYGTQQIPPAYKDLAEPWIQVFGMELVGCLFSRNWNVREMALRRLSHDVSGALLLANGESTGNSGGSSGSSPSGGATSGSSQTSISGDVVEACCSVLSMVCADPVYKVYVAALKTLRAMLVYTPCHSLAERIKLQRLLQPVVDTILVKCADANSRTSQLSISTLLELCKGQAGELAVGREILKAGSIGIGGVDYVLNCILGNQTESNNWQELLGRLCLIDRLLLEFPAEFYPHIVSTDVSQAEPVEIRYKKLLSLLTFALQSIDNSHSMVGKLSRRIYLSSARMVTTVPHVFSKLLEMLSVSSSTHFTRMRRRLMAIADEVEIAEAIQLGVEDTLDGQQDSFLQASVPNNYLETTENSSPECTVHLEKTGKGLCATKLSASSEDISERLASISVGPSSSTTTTTTTTEQPKPMVQTKGRPHSQCLNSSPLSHHSQLMFPALSTPSSSTPSVPAGTATDVSKHRLQGFIPCRIPSASPQTQRKFSLQFHRNCPENKDSDKLSPVFTQSRPLPSSNIHRPKPSRPTPGNTSKQGDPSKNSMTLDLNSSSKCDDSFGCSSNSSNAVIPSDETVFTPVEEKCRLDVNTELNSSIEDLLEASMPSSDTTVTFKSEVAVLSPEKAENDDTYKDDVNHNQKCKEKMEAEEEEALAIAMAMSASQDALPIVPQLQVENGEDIIIIQQDTPETLPGHTKAKQPYREDTEWLKGQQIGLGAFSSCYQAQDVGTGTLMAVKQVTYVRNTSSEQEEVVEALREEIRMMSHLNHPNIIRMLGATCEKSNYNLFIEWMAGGSVAHLLSKYGAFKESVVINYTEQLLRGLSYLHENQIIHRDVKGANLLIDSTGQRLRIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVLRGQQYGRSCDVWSVGCAIIEMACAKPPWNAEKHSNHLALIFKIASATTAPSIPSHLSPGLRDVALRCLELQPQDRPPSRELLKHPVFRTTW TTW8TJI TT Literature-reported TTW8TJI FM mRNA target TTW8TJI KE hsa04010:MAPK signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa04622:RIG-I-like receptor signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04912:GnRH signaling pathway; hsa05161:Hepatitis B; hsa05166:HTLV-I infection TTW8TJI RC R-HSA-166058:MyD88:Mal cascade initiated on plasma membrane; R-HSA-2871796:FCERI mediated MAPK activation; R-HSA-933542:TRAF6 mediated NF-kB activation; R-HSA-975138:TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation; R-HSA-975871:MyD88 cascade initiated on plasma membrane TTNI91K ID TTNI91K TTNI91K TN Melanocortin receptor 3 (MC3R) TTNI91K UP P41968 TTNI91K UC MC3R_HUMAN TTNI91K BC GPCR rhodopsin TTNI91K SN MC3-R TTNI91K GN MC3R TTNI91K FC Receptor for MSH (alpha, beta and gamma) and ACTH. This receptor is mediated by G proteins which activate adenylate cyclase. Required for expression of anticipatory patterns of activity and wakefulness during periods of limited nutrient availability and for the normal regulation of circadian clock activity in the brain. TTNI91K SQ MNASCCLPSVQPTLPNGSEHLQAPFFSNQSSSAFCEQVFIKPEVFLSLGIVSLLENILVILAVVRNGNLHSPMYFFLCSLAVADMLVSVSNALETIMIAIVHSDYLTFEDQFIQHMDNIFDSMICISLVASICNLLAIAVDRYVTIFYALRYHSIMTVRKALTLIVAIWVCCGVCGVVFIVYSESKMVIVCLITMFFAMMLLMGTLYVHMFLFARLHVKRIAALPPADGVAPQQHSCMKGAVTITILLGVFIFCWAPFFLHLVLIITCPTNPYCICYTAHFNTYLVLIMCNSVIDPLIYAFRSLELRNTFREILCGCNGMNLG TTNI91K TT Literature-reported TTNI91K KE hsa04080:Neuroactive ligand-receptor interaction TTNI91K RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events TTB4PAZ ID TTB4PAZ TTB4PAZ TN Membrane-associated kinase (PKMYT1) TTB4PAZ UP O14731 TTB4PAZ UC PMYT1_HUMAN TTB4PAZ BC Kinase TTB4PAZ SN Myt1 kinase; Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase; MYT1 TTB4PAZ GN PKMYT1 TTB4PAZ FC Mediates phosphorylation of CDK1 predominantly on 'Thr-14'. Also involved in Golgi fragmentation. May be involved in phosphorylation of CDK1 on 'Tyr-15' to a lesser degree, however tyrosine kinase activity is unclear and may be indirect. May be a downstream target of Notch signaling pathway during eye development. Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase specifically when CDK1 is complexed to cyclins. TTB4PAZ EC EC 2.7.11.1 TTB4PAZ PD 5VD3; 5VD1; 5VD0; 5VCZ; 5VCY TTB4PAZ SQ MLERPPALAMPMPTEGTPPPLSGTPIPVPAYFRHAEPGFSLKRPRGLSRSLPPPPPAKGSIPISRLFPPRTPGWHQLQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARKLAEVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDVKPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQLRQGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQPRAWGVLWCMAAEALSRGWALWQALLALLCWLWHGLAHPASWLQPLGPPATPPGSPPCSLLLDSSLSSNWDDDSLGPSLSPEAVLARTVGSTSTPRSRCTPRDALDLSDINSEPPRGSFPSFEPRNLLSLFEDTLDPT TTB4PAZ TT Literature-reported TTICZ1O ID TTICZ1O TTICZ1O TN Metabotropic glutamate receptor 4 (mGluR4) TTICZ1O UP Q14833 TTICZ1O UC GRM4_HUMAN TTICZ1O BC GPCR glutamate TTICZ1O SN mGluR4; Group III metabotropic glutamate receptor 4; GPRC1D TTICZ1O GN GRM4 TTICZ1O FC Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. G-protein coupled receptor for glutamate. TTICZ1O SQ MPGKRGLGWWWARLPLCLLLSLYGPWMPSSLGKPKGHPHMNSIRIDGDITLGGLFPVHGRGSEGKPCGELKKEKGIHRLEAMLFALDRINNDPDLLPNITLGARILDTCSRDTHALEQSLTFVQALIEKDGTEVRCGSGGPPIITKPERVVGVIGASGSSVSIMVANILRLFKIPQISYASTAPDLSDNSRYDFFSRVVPSDTYQAQAMVDIVRALKWNYVSTVASEGSYGESGVEAFIQKSREDGGVCIAQSVKIPREPKAGEFDKIIRRLLETSNARAVIIFANEDDIRRVLEAARRANQTGHFFWMGSDSWGSKIAPVLHLEEVAEGAVTILPKRMSVRGFDRYFSSRTLDNNRRNIWFAEFWEDNFHCKLSRHALKKGSHVKKCTNRERIGQDSAYEQEGKVQFVIDAVYAMGHALHAMHRDLCPGRVGLCPRMDPVDGTQLLKYIRNVNFSGIAGNPVTFNENGDAPGRYDIYQYQLRNDSAEYKVIGSWTDHLHLRIERMHWPGSGQQLPRSICSLPCQPGERKKTVKGMPCCWHCEPCTGYQYQVDRYTCKTCPYDMRPTENRTGCRPIPIIKLEWGSPWAVLPLFLAVVGIAATLFVVITFVRYNDTPIVKASGRELSYVLLAGIFLCYATTFLMIAEPDLGTCSLRRIFLGLGMSISYAALLTKTNRIYRIFEQGKRSVSAPRFISPASQLAITFSLISLQLLGICVWFVVDPSHSVVDFQDQRTLDPRFARGVLKCDISDLSLICLLGYSMLLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIVWLAFIPIFFGTSQSADKLYIQTTTLTVSVSLSASVSLGMLYMPKVYIILFHPEQNVPKRKRSLKAVVTAATMSNKFTQKGNFRPNGEAKSELCENLEAPALATKQTYVTYTNHAI TTICZ1O TT Literature-reported TTICZ1O FM GPCR glutamate TTICZ1O KE hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse; hsa04742:Taste transduction TTICZ1O RC R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors) TTUTO39 ID TTUTO39 TTUTO39 TN Methionine synthase (MTR) TTUTO39 UP Q99707 TTUTO39 UC METH_HUMAN TTUTO39 BC Methyltransferase TTUTO39 SN Methionine synthase, vitamin-B12dependent; MTR; MS; Cobalamin-dependent methionine synthase; B12 dependent methionine synthetase; 5-methyltetrahydrofolate:homocysteine methyltransferase; 5-methyltetrahydrofolate-homocysteine methyltransferase; 5-methyltetrahydrofolate homocysteine methyltransferase TTUTO39 GN MTR TTUTO39 FC Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. TTUTO39 EC EC 2.1.1.13 TTUTO39 PD 4CCZ; 2O2K TTUTO39 SQ MSPALQDLSQPEGLKKTLRDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHARPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNMCSAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQTGEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDETPSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPATAFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDGMLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGMEAIREAMHGVFLYHAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQGTGGKKVIQTDEWRNGPVEERLEYALVKGIEKHIIEDTEEARLNQKKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREETRVLNGTVEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQVFEDYDLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKTVGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVPQAAEPIATFYGLRQQAEKDSASTEPYYCLSDFIAPLHSGIRDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTGIRLTESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPILGYDTD TTUTO39 TT Literature-reported TT1QUZV ID TT1QUZV TT1QUZV TN Methionine-R-sulfoxide reductase B1 (MSRB1) TT1QUZV UP Q9NZV6 TT1QUZV UC MSRB1_HUMAN TT1QUZV BC MsrB Met sulfoxide reductase family TT1QUZV SN Selenoprotein X; SelX; SEPX1; MsrB1 TT1QUZV GN MSRB1 TT1QUZV FC Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to actin repolymerization in macrophages. TT1QUZV EC EC 1.8.4.12 TT1QUZV PD 3MAO TT1QUZV SQ MSFCSFFGGEVFQNHFEPGVYVCAKCGYELFSSRSKYAHSSPWPAFTETIHADSVAKRPEHNRSEALKVSCGKCGNGLGHEFLNDGPKPGQSRFUIFSSSLKFVPKGKETSASQGH TT1QUZV TT Literature-reported TT5DFHW ID TT5DFHW TT5DFHW TN Mevalonate kinase (MVK) TT5DFHW UP Q03426 TT5DFHW UC KIME_HUMAN TT5DFHW BC Kinase TT5DFHW SN POROK3; MVLK; LRBP TT5DFHW GN MVK TT5DFHW FC Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis. TT5DFHW EC EC 2.7.1.36 TT5DFHW PD 2R3V TT5DFHW SQ MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKRAWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSICRKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKEDLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVPRNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDMNQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQALTSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL TT5DFHW TT Literature-reported TTVQEZS ID TTVQEZS TTVQEZS TN Mitotic growth and transcription activator (BAF190A) TTVQEZS UP P51532 TTVQEZS UC SMCA4_HUMAN TTVQEZS BC Acid anhydride hydrolase TTVQEZS SN Transcription activator BRG1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4; SNF2L4; SNF2B; SNF2-beta; Protein brahma homolog 1; Protein BRG-1; BRG1-associated factor 190A; BRG1; ATP-dependent helicase SMARCA4 TTVQEZS GN SMARCA4 TTVQEZS FC Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating the calcium-dependent release of a repressor complex and the recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by SMARCA4-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves the release of HDAC1 and recruitment of CREBBP. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development, a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues. Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1. Binds via DLX1 to enhancers located in the intergenic region between DLX5 and DLX6 and this binding is stabilized by the long non-coding RNA (lncRNA) Evf2. Binds to RNA in a promiscuous manner. Binding to RNAs including lncRNA Evf2 leads to inhibition of SMARCA4 ATPase and chromatin remodeling activities. Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). TTVQEZS EC EC 3.6.4.- TTVQEZS PD 6BGH; 5EA1; 5DKD; 3UVD; 2H60 TTVQEZS SQ MSTPDPPLGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSMMGPSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYNQMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQQQMPTLPPPSVSATGPGPGPGPGPGPGPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPMVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDESRHCSTGSGSASFAHTAPPPAGVNPDLEEPPLKEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED TTVQEZS TT Literature-reported TTSW9YL ID TTSW9YL TTSW9YL TN Mixed lineage kinase 4 (MAP3K21) TTSW9YL UP Q5TCX8 TTSW9YL UC M3K21_HUMAN TTSW9YL BC Protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily TTSW9YL SN Mitogen-activated protein kinase kinase kinase MLK4; MLK4beta TTSW9YL GN MAP3K21 TTSW9YL FC Negative regulator of TLR4 signaling. Does not activate JNK1/MAPK8 pathway, p38/MAPK14, nor ERK2/MAPK1 pathways. TTSW9YL EC EC 2.7.11.25 TTSW9YL PD 4UYA TTSW9YL SQ MALRGAAGATDTPVSSAGGAPGGSASSSSTSSGGSASAGAGLWAALYDYEARGEDELSLRRGQLVEVLSQDAAVSGDEGWWAGQVQRRLGIFPANYVAPCRPAASPAPPPSRPSSPVHVAFERLELKELIGAGGFGQVYRATWQGQEVAVKAARQDPEQDAAAAAESVRREARLFAMLRHPNIIELRGVCLQQPHLCLVLEFARGGALNRALAAANAAPDPRAPGPRRARRIPPHVLVNWAVQIARGMLYLHEEAFVPILHRDLKSSNILLLEKIEHDDICNKTLKITDFGLAREWHRTTKMSTAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTLPIPSTCPEPFAKLMKECWQQDPHIRPSFALILEQLTAIEGAVMTEMPQESFHSMQDDWKLEIQQMFDELRTKEKELRSREEELTRAALQQKSQEELLKRREQQLAEREIDVLERELNILIFQLNQEKPKVKKRKGKFKRSRLKLKDGHRISLPSDFQHKITVQASPNLDKRRSLNSSSSSPPSSPTMMPRLRAIQLTSDESNKTWGRNTVFRQEEFEDVKRNFKKKGCTWGPNSIQMKDRTDCKERIRPLSDGNSPWSTILIKNQKTMPLASLFVDQPGSCEEPKLSPDGLEHRKPKQIKLPSQAYIDLPLGKDAQRENPAEAESWEEAASANAATVSIEMTPTNSLSRSPQRKKTESALYGCTVLLASVALGLDLRELHKAQAAEEPLPKEEKKKREGIFQRASKSRRSASPPTSLPSTCGEASSPPSLPLSSALGILSTPSFSTKCLLQMDSEDPLVDSAPVTCDSEMLTPDFCPTAPGSGREPALMPRLDTDCSVSRNLPSSFLQQTCGNVPYCASSKHRPSHHRRTMSDGNPTPTGATIISATGASALPLCPSPAPHSHLPREVSPKKHSTVHIVPQRRPASLRSRSDLPQAYPQTAVSQLAQTACVVGRPGPHPTQFLAAKERTKSHVPSLLDADVEGQSRDYTVPLCRMRSKTSRPSIYELEKEFLS TTSW9YL TT Literature-reported TT1GNDM ID TT1GNDM TT1GNDM TN Mixed-lineage leukemia protein (MLL) TT1GNDM UP Q03164 TT1GNDM UC KMT2A_HUMAN TT1GNDM BC Methyltransferase TT1GNDM SN p320; p180; Zinc finger protein HRX; Trithoraxlike protein; Trithorax-like protein; Myeloid/lymphoid or mixed-lineage leukemia protein 1; Myeloid/lymphoid or mixed-lineage leukemia; MLL1; MLL cleavage product C180; Lysine Nmethyltransferase 2A; Lysine N-methyltransferase 2A; Histonelysine Nmethyltransferase MLL; Histone-lysine N-methyltransferase 2A; HTRX; HRX; CXXCtype zinc finger protein 7; CXXC7; CXXC-type zinc finger protein 7; ALL1; ALL-1 TT1GNDM GN KMT2A TT1GNDM FC Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state. Required for transcriptional activation of HOXA9. Promotes PPP1R15A-induced apoptosis. Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-ARNTL/BMAL1 heterodimer. Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-ARNTL/BMAL1 to chromatin. Histone methyltransferase that plays an essential role in early development and hematopoiesis. TT1GNDM EC EC 2.1.1.43 TT1GNDM PD 6EMQ; 5SVH; 5F6L; 5F5E; 4NW3 TT1GNDM SQ MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAVAAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPRSGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKDISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIVRRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRIIPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSRIIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSSSPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGSRTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPASTAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPEDVGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSNRTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSLSISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFTPGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQSSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKILIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTDKRVASLLKKAKAQLCKIEKSKSLKQTDQPKAQGQESDSSETSVRGPRIKHVCRRAAVALGRKRAVFPDDMPTLSALPWEEREKILSSMGNDDKSSIAGSEDAEPLAPPIKPIKPVTRNKAPQEPPVKKGRRSRRCGQCPGCQVPEDCGVCTNCLDKPKFGGRNIKKQCCKMRKCQNLQWMPSKAYLQKQAKAVKKKEKKSKTSEKKDSKESSVVKNVVDSSQKPTPSAREDPAPKKSSSEPPPRKPVEEKSEEGNVSAPGPESKQATTPASRKSSKQVSQPALVIPPQPPTTGPPRKEVPKTTPSEPKKKQPPPPESGPEQSKQKKVAPRPSIPVKQKPKEKEKPPPVNKQENAGTLNILSTLSNGNSSKQKIPADGVHRIRVDFKEDCEAENVWEMGGLGILTSVPITPRVVCFLCASSGHVEFVYCQVCCEPFHKFCLEENERPLEDQLENWCCRRCKFCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKKVWICTKCVRCKSCGSTTPGKGWDAQWSHDFSLCHDCAKLFAKGNFCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCVNCTERHPAEWRLALEKELQISLKQVLTALLNSRTTSHLLRYRQAAKPPDLNPETEESIPSRSSPEGPDPPVLTEVSKQDDQQPLDLEGVKRKMDQGNYTSVLEFSDDIVKIIQAAINSDGGQPEIKKANSMVKSFFIRQMERVFPWFSVKKSRFWEPNKVSSNSGMLPNAVLPPSLDHNYAQWQEREENSHTEQPPLMKKIIPAPKPKGPGEPDSPTPLHPPTPPILSTDRSREDSPELNPPPGIEDNRQCALCLTYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLDDKKVYCQRHRDLIKGEVVPENGFEVFRRVFVDFEGISLRRKFLNGLEPENIHMMIGSMTIDCLGILNDLSDCEDKLFPIGYQCSRVYWSTTDARKRCVYTCKIVECRPPVVEPDINSTVEHDENRTIAHSPTSFTESSSKESQNTAEIISPPSPDRPPHSQTSGSCYYHVISKVPRIRTPSYSPTQRSPGCRPLPSAGSPTPTTHEIVTVGDPLLSSGLRSIGSRRHSTSSLSPQRSKLRIMSPMRTGNTYSRNNVSSVSTTGTATDLESSAKVVDHVLGPLNSSTSLGQNTSTSSNLQRTVVTVGNKNSHLDGSSSSEMKQSSASDLVSKSSSLKGEKTKVLSSKSSEGSAHNVAYPGIPKLAPQVHNTTSRELNVSKIGSFAEPSSVSFSSKEALSFPHLHLRGQRNDRDQHTDSTQSANSSPDEDTEVKTLKLSGMSNRSSIINEHMGSSSRDRRQKGKKSCKETFKEKHSSKSFLEPGQVTTGEEGNLKPEFMDEVLTPEYMGQRPCNNVSSDKIGDKGLSMPGVPKAPPMQVEGSAKELQAPRKRTVKVTLTPLKMENESQSKNALKESSPASPLQIESTSPTEPISASENPGDGPVAQPSPNNTSCQDSQSNNYQNLPVQDRNLMLPDGPKPQEDGSFKRRYPRRSARARSNMFFGLTPLYGVRSYGEEDIPFYSSSTGKKRGKRSAEGQVDGADDLSTSDEDDLYYYNFTRTVISSGGEERLASHNLFREEEQCDLPKISQLDGVDDGTESDTSVTATTRKSSQIPKRNGKENGTENLKIDRPEDAGEKEHVTKSSVGHKNEPKMDNCHSVSRVKTQGQDSLEAQLSSLESSRRVHTSTPSDKNLLDTYNTELLKSDSDNNNSDDCGNILPSDIMDFVLKNTPSMQALGESPESSSSELLNLGEGLGLDSNREKDMGLFEVFSQQLPTTEPVDSSVSSSISAEEQFELPLELPSDLSVLTTRSPTVPSQNPSRLAVISDSGEKRVTITEKSVASSESDPALLSPGVDPTPEGHMTPDHFIQGHMDADHISSPPCGSVEQGHGNNQDLTRNSSTPGLQVPVSPTVPIQNQKYVPNSTDSPGPSQISNAAVQTTPPHLKPATEKLIVVNQNMQPLYVLQTLPNGVTQKIQLTSSVSSTPSVMETNTSVLGPMGGGLTLTTGLNPSLPTSQSLFPSASKGLLPMSHHQHLHSFPAATQSSFPPNISNPPSGLLIGVQPPPDPQLLVSESSQRTDLSTTVATPSSGLKKRPISRLQTRKNKKLAPSSTPSNIAPSDVVSNMTLINFTPSQLPNHPSLLDLGSLNTSSHRTVPNIIKRSKSSIMYFEPAPLLPQSVGGTAATAAGTSTISQDTSHLTSGSVSGLASSSSVLNVVSMQTTTTPTSSASVPGHVTLTNPRLLGTPDIGSISNLLIKASQQSLGIQDQPVALPPSSGMFPQLGTSQTPSTAAITAASSICVLPSTQTTGITAASPSGEADEHYQLQHVNQLLASKTGIHSSQRDLDSASGPQVSNFTQTVDAPNSMGLEQNKALSSAVQASPTSPGGSPSSPSSGQRSASPSVPGPTKPKPKTKRFQLPLDKGNGKKHKVSHLRTSSSEAHIPDQETTSLTSGTGTPGAEAEQQDTASVEQSSQKECGQPAGQVAVLPEVQVTQNPANEQESAEPKTVEEEESNFSSPLMLWLQQEQKRKESITEKKPKKGLVFEISSDDGFQICAESIEDAWKSLTDKVQEARSNARLKQLSFAGVNGLRMLGILHDAVVFLIEQLSGAKHCRNYKFRFHKPEEANEPPLNPHGSARAEVHLRKSAFDMFNFLASKHRQPPEYNPNDEEEEEVQLKSARRATSMDLPMPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGNVIRSIQTDKREKYYDSKGIGCYMFRIDDSEVVDATMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN TT1GNDM TT Literature-reported TT1GNDM FM Methyltransferase superfamily TTG45HY ID TTG45HY TTG45HY TN mRNA cap guanine-N7 methyltransferase (RNMT) TTG45HY UP O43148 TTG45HY UC MCES_HUMAN TTG45HY BC Methyltransferase TTG45HY SN hcm1p; hMet; hCMT1; RG7MT1; KIAA0398 TTG45HY GN RNMT TTG45HY FC Binds RNA containing 5'-terminal GpppC. Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. TTG45HY EC EC 2.1.1.56 TTG45HY PD 5E9W; 5E9J; 5E8J; 3EPP; 3BGV TTG45HY SQ MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRKEFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTGDGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEPYPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ TTG45HY TT Literature-reported TTUCT4J ID TTUCT4J TTUCT4J TN Mycobacterium Aminoglycoside 2'-N-acetyltransferase (MycB aac) TTUCT4J UP P0A5N0 TTUCT4J UC AAC2_MYCTU TTUCT4J BC Acyltransferase TTUCT4J SN Aminoglycoside 2'-N-acetyltransferase; AAC(2')-Ic TTUCT4J GN MycB aac TTUCT4J FC May catalyze the coenzyme A-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides and confer resistance to aminoglycosides (By similarity). In vitro assays show no significant increase of resistance to aminoglycosides, possibly due to low expression in a heterologous system. TTUCT4J EC EC 2.3.1.- TTUCT4J PD 1M4I; 1M4G; 1M4D; 1M44 TTUCT4J SQ MHTQVHTARLVHTADLDSETRQDIRQMVTGAFAGDFTETDWEHTLGGMHALIWHHGAIIAHAAVIQRRLIYRGNALRCGYVEGVAVRADWRGQRLVSALLDAVEQVMRGAYQLGALSSSARARRLYASRGWLPWHGPTSVLAPTGPVRTPDDDGTVFVLPIDISLDTSAELMCDWRAGDVW TTUCT4J TT Literature-reported TTBK0PU ID TTBK0PU TTBK0PU TN Mycobacterium Cytochrome p450 121 (MycB cyp121) TTBK0PU UP P0A515 TTBK0PU UC CP121_MYCBO TTBK0PU BC Paired donor oxygen oxidoreductase TTBK0PU SN Cytochrome P450 MT2; Cytochrome P450 121 TTBK0PU GN MycB cyp121 TTBK0PU FC Catalyzes the formation of an intramolecular C-C bond between two tyrosyl carbon atoms of Cyy. TTBK0PU EC EC 1.14.-.- TTBK0PU PD 5EDT TTBK0PU SQ MTATVLLEVPFSARGDRIPDAVAELRTREPIRKVRTITGAEAWLVSSYALCTQVLEDRRFSMKETAAAGAPRLNALTVPPEVVNNMGNIADAGLRKAVMKAITPKAPGLEQFLRDTANSLLDNLITEGAPADLRNDFADPLATALHCKVLGIPQEDGPKLFRSLSIAFMSSADPIPAAKINWDRDIEYMAGILENPNITTGLMGELSRLRKDPAYSHVSDELFATIGVTFFGAGVISTGSFLTTALISLIQRPQLRNLLHEKPELIPAGVEELLRINLSFADGLPRLATADIQVGDVLVRKGELVLVLLEGANFDPEHFPNPGSIELDRPNPTSHLAFGRGQHFCPGSALGRRHAQIGIEALLKKMPGVDLAVPIDQLVWRTRFQRRIPERLPVLW TTBK0PU TT Literature-reported TTKGY3F ID TTKGY3F TTKGY3F TN Mycobacterium DTDP-dehydrorhamnose epimerase rmlC (MycB rmlC) TTKGY3F UP P9WH11 TTKGY3F UC RMLC_MYCTU TTKGY3F BC Racemases and epimerases TTKGY3F SN dTDP-L-rhamnose synthase; dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase; dTDP-4-keto-6-deoxyglucose 3,5-epimerase; dTDP-4-dehydrorhamnose 3,5-epimerase; Thymidine diphospho-4-keto-rhamnose 3,5-epimerase TTKGY3F GN MycB rmlC TTKGY3F FC Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage. TTKGY3F EC EC 5.1.3.13 TTKGY3F PD 2IXC; 1UPI; 1PM7 TTKGY3F SQ MKARELDVPGAWEITPTIHVDSRGLFFEWLTDHGFRAFAGHSLDVRQVNCSVSSAGVLRGLHFAQLPPSQAKYVTCVSGSVFDVVVDIREGSPTFGRWDSVLLDDQDRRTIYVSEGLAHGFLALQDNSTVMYLCSAEYNPQREHTICATDPTLAVDWPLVDGAAPSLSDRDAAAPSFEDVRASGLLPRWEQTQRFIGEMRGT TTKGY3F TT Literature-reported TTV7Y40 ID TTV7Y40 TTV7Y40 TN Mycobacterium Orotidine phosphate decarboxylase (MycB pyrF) TTV7Y40 UP P9WIU2 TTV7Y40 UC PYRF_MYCTO TTV7Y40 BC Carbon-carbon lyase TTV7Y40 SN Orotidine 5'-phosphate decarboxylase; OMPdecase; OMPDCase; OMP decarboxylase TTV7Y40 GN MycB pyrF TTV7Y40 FC Catalyzes the decarboxylation of orotidine monophosphate (OMP), producing uridine monophosphate (UMP). TTV7Y40 EC EC 4.1.1.23 TTV7Y40 SQ MTGFGLRLAEAKARRGPLCLGIDPHPELLRGWDLATTADGLAAFCDICVRAFADFAVVKPQVAFFESYGAAGFAVLERTIAELRAADVLVLADAKRGDIGATMSAYATAWVGDSPLAADAVTASPYLGFGSLRPLLEVAAAHGRGVFVLAATSNPEGAAVQNAAADGRSVAQLVVDQVGAANEAAGPGPGSIGVVVGATAPQAPDLSAFTGPVLVPGVGVQGGRPEALGGLGGAASSQLLPAVAREVLRAGPGVPELRAAGERMRDAVAYLAAV TTV7Y40 TT Literature-reported TTHDERA ID TTHDERA TTHDERA TN Myotubularin-related protein 1 (MTMR1) TTHDERA UP Q13613 TTHDERA UC MTMR1_HUMAN TTHDERA BC Phosphoric monoester hydrolase TTHDERA SN MTMR1 TTHDERA GN MTMR1 TTHDERA FC Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol (3,5)-bisphosphate. TTHDERA EC EC 3.1.3.95 TTHDERA PD 5C16 TTHDERA SQ MDRPAAAAAAGCEGGGGPNPGPAGGRRPPRAAGGATAGSRQPSVETLDSPTGSHVEWCKQLIAATISSQISGSVTSENVSRDYKALRDGNKLAQMEEAPLFPGESIKAIVKDVMYICPFMGAVSGTLTVTDFKLYFKNVERDPHFILDVPLGVISRVEKIGAQSHGDNSCGIEIVCKDMRNLRLAYKQEEQSKLGIFENLNKHAFPLSNGQALFAFSYKEKFPINGWKVYDPVSEYKRQGLPNESWKISKINSNYEFCDTYPAIIVVPTSVKDDDLSKVAAFRAKGRVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYPNAELVFLEIHNIHVMRESLRKLKEIVYPSIDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFETLVEKEWISFGHRFALRVGHGNDNHADADRSPIFLQFVDCVWQMTRQFPSAFEFNELFLITILDHLYSCLFGTFLCNCEQQRFKEDVYTKTISLWSYINSQLDEFSNPFFVNYENHVLYPVASLSHLELWVNYYVRWNPRMRPQMPIHQNLKELLAVRAELQKRVEGLQREVATRAVSSSSERGSSPSHSATSVHTSV TTHDERA TT Literature-reported TTH0IOD ID TTH0IOD TTH0IOD TN NAD-dependent deacetylase sirtuin-5 (SIRT5) TTH0IOD UP Q9NXA8 TTH0IOD UC SIR5_HUMAN TTH0IOD BC Sirtuin family. Class III subfamily TTH0IOD SN SIR2L5; SIR2-like protein 5; Regulatory protein SIR2 homolog 5 TTH0IOD GN SIRT5 TTH0IOD FC NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693, PubMed:29180469). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (PubMed:24140062). Activates SHMT2 by mediating its desuccinylation (PubMed:29180469). Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX. TTH0IOD EC EC 3.5.1.- TTH0IOD PD 6EQS; 5XHS; 5BWL; 4HDA; 4G1C TTH0IOD SQ MRPLQIVPSRLISQLYCGLKPPASTRNQICLKMARPSSSMADFRKFFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPLAFAHNPSRVWEFYHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKAGTKNLLEIHGSLFKTRCTSCGVVAENYKSPICPALSGKGAPEPGTQDASIPVEKLPRCEEAGCGGLLRPHVVWFGENLDPAILEEVDRELAHCDLCLVVGTSSVVYPAAMFAPQVAARGVPVAEFNTETTPATNRFRFHFQGPCGTTLPEALACHENETVS TTH0IOD TT Literature-reported TT5T8MR ID TT5T8MR TT5T8MR TN NADPH oxidase 2 (CYBB) TT5T8MR UP P04839 TT5T8MR UC CY24B_HUMAN TT5T8MR BC Phagocyte NADPH oxidase TT5T8MR SN p22 phagocyte Bcytochrome; p22 phagocyte B-cytochrome; gp91phox; gp911; gp91-phox; gp91-1; Superoxidegenerating NADPH oxidase heavy chain subunit; Superoxide-generating NADPH oxidase heavy chain subunit; Neutrophil cytochrome b 91 kDa polypeptide; NOX2; Hemebinding membrane glycoprotein gp91phox; Heme-binding membrane glycoprotein gp91phox; Cytochrome b558 subunit beta; Cytochrome b245 heavy chain; Cytochrome b-245 heavy chain; Cytochrome b(558) subunit beta; CGD91phox; CGD91-phox TT5T8MR GN CYBB TT5T8MR FC It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc. Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. TT5T8MR EC EC 1.-.-.- TT5T8MR PD 3A1F TT5T8MR SQ MGNWAVNEGLSIFVILVWLGLNVFLFVWYYRVYDIPPKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRVRRQLDRNLTFHKMVAWMIALHSAIHTIAHLFNVEWCVNARVNNSDPYSVALSELGDRQNESYLNFARKRIKNPEGGLYLAVTLLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTAESLAVHNITVCEQKISEWGKIKECPIPQFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNNATNLKLKKIYFYWLCRDTHAFEWFADLLQLLESQMQERNNAGFLSYNIYLTGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASQHPNTRIGVFLCGPEALAETLSKQSISNSESGPRGVHFIFNKENF TT5T8MR TT Literature-reported TT3W4IX ID TT3W4IX TT3W4IX TN NADPH:adrenodoxin oxidoreductase (FDXR) TT3W4IX UP P22570 TT3W4IX UC ADRO_HUMAN TT3W4IX BC Ferredoxin--NADP reductase type 1 TT3W4IX SN NADPH:adrenodoxin oxidoreductase, mitochondrial; FerredoxinNADP(+) reductase; Ferredoxin reductase; FDXR; Adrenodoxin reductase TT3W4IX GN FDXR TT3W4IX FC Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitaminD3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver. TT3W4IX EC EC 1.18.1.6 TT3W4IX SQ MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAGFYTAQHLLKHPQAHVDIYEKQPVPFGLVRFGVAPDHPEVKNVINTFTQTAHSGRCAFWGNVEVGRDVTVPELREAYHAVVLSYGAEDHRALEIPGEELPGVCSARAFVGWYNGLPENQELEPDLSCDTAVILGQGNVALDVARILLTPPEHLERTDITKAALGVLRQSRVKTVWLVGRRGPLQVAFTIKELREMIQLPGARPILDPVDFLGLQDKIKEVPRPRKRLTELLLRTATEKPGPAEAARQASASRAWGLRFFRSPQQVLPSPDGRRAAGVRLAVTRLEGVDEATRAVPTGDMEDLPCGLVLSSIGYKSRPVDPSVPFDSKLGVIPNVEGRVMDVPGLYCSGWVKRGPTGVIATTMTDSFLTGQMLLQDLKAGLLPSGPRPGYAAIQALLSSRGVRPVSFSDWEKLDAEEVARGQGTGKPREKLVDPQEMLRLLGH TT3W4IX TT Literature-reported TT27XFN ID TT27XFN TT27XFN TN NDR1 protein kinase (STK38) TT27XFN UP Q15208 TT27XFN UC STK38_HUMAN TT27XFN BC Kinase TT27XFN SN Serine/threonine-protein kinase 38; Nuclear Dbf2-related kinase 1; NDR1 TT27XFN GN STK38 TT27XFN FC Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2. Negative regulator of MAP3K1/2 signaling. TT27XFN EC EC 2.7.11.1 TT27XFN PD 6BXI; 1PSB TT27XFN SQ MAMTGSTPCSSMSNHTKERVTMTKVTLENFYSNLIAQHEEREMRQKKLEKVMEEEGLKDEEKRLRRSAHARKETEFLRLKRTRLGLEDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYRNLNHSLPSDFTFQNMNSKRKAETWKRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNWKETLTFPPEVPISEKAKDLILRFCCEWEHRIGAPGVEEIKSNSFFEGVDWEHIRERPAAISIEIKSIDDTSNFDEFPESDILKPTVATSNHPETDYKNKDWVFINYTYKRFEGLTARGAIPSYMKAAK TT27XFN TT Literature-reported TTNM4ZH ID TTNM4ZH TTNM4ZH TN NDR2 protein kinase (STK38L) TTNM4ZH UP Q9Y2H1 TTNM4ZH UC ST38L_HUMAN TTNM4ZH BC Kinase TTNM4ZH SN Serine/threonine-protein kinase 38-like; Nuclear Dbf2-related kinase 2; NDR2; KIAA0965 TTNM4ZH GN STK38L TTNM4ZH FC Involved in the regulation of structural processes in differentiating and mature neuronal cells. TTNM4ZH EC EC 2.7.11.1 TTNM4ZH PD 5XQZ TTNM4ZH SQ MAMTAGTTTTFPMSNHTRERVTVAKLTLENFYSNLILQHEERETRQKKLEVAMEEEGLADEEKKLRRSQHARKETEFLRLKRTRLGLDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKSDMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYISETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEFYRNLTHNPPSDFSFQNMNSKRKAETWKKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFCIDSENRIGNSGVEEIKGHPFFEGVDWEHIRERPAAIPIEIKSIDDTSNFDDFPESDILQPVPNTTEPDYKSKDWVFLNYTYKRFEGLTQRGSIPTYMKAGKL TTNM4ZH TT Literature-reported TTO0DKT ID TTO0DKT TTO0DKT TN NEDD4-like E3 ubiquitin-protein ligase WWP2 (WWP2) TTO0DKT UP O00308 TTO0DKT UC WWP2_HUMAN TTO0DKT BC Acyltransferase TTO0DKT SN WW domaincontaining protein 2; WW domain-containing protein 2; NEDD4like E3 ubiquitinprotein ligaseWWP2; HECT-type E3 ubiquitin transferase WWP2; Atrophin1interacting protein 2; Atrophin-1-interacting protein 2; AIP2 TTO0DKT GN WWP2 TTO0DKT FC Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; in embryonic stem cells (ESCs) the ubiquitination is proposed to regulate POU5F1 protein level. Ubiquitinates EGR2 and promotes it to proteasomal degradation; in T-cells the ubiquitination inhibits activation-induced cell death. Ubiquitinates SLC11A2; the ubiquitination is enhanced by presence of NDFIP1 and NDFIP2. Ubiquitinates RPB1 and promotes it to proteasomal degradation. E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. TTO0DKT EC EC 2.3.2.26 TTO0DKT PD 5TJQ; 5TJ8; 5TJ7; 4Y07 TTO0DKT SQ MASASSSRAGVALPFEKSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLRNELLGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRELPNGRVYYVDHNTKTTTWERPLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQWQSQRNQLQGAMQHFSQRFLYQSSSASTDHDPLGPLPPGWEKRQDNGRVYYVNHNTRTTQWEDPRTQGMIQEPALPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNALPSHVKISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRHYTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVGKETWLPRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFGQE TTO0DKT TT Literature-reported TTO0DKT FM Carbon-nitrogen ligase TT0AH4L ID TT0AH4L TT0AH4L TN Netrin-1 (NTN1) TT0AH4L UP O95631 TT0AH4L UC NET1_HUMAN TT0AH4L SN NTN1; Epididymis tissue protein Li 131P TT0AH4L GN NTN1 TT0AH4L FC Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either Dor some UNC5 receptors will lead to axon attraction or repulsion, respectively. It also serve as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in tumorigenesis by regulating apoptosis. TT0AH4L PD 6FKQ; 4URT TT0AH4L SQ MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYFYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGYYRDMGKPITHRKACKACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPVAPPTTAASSVEEPEDCDSYCKASKGKLKINMKKYCKKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPDQSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKCKKA TT0AH4L TT Literature-reported TT0AH4L KE hsa04360:Axon guidance TT0AH4L RC R-HSA-376172:DSCAM interactions; R-HSA-418885:DCC mediated attractive signaling; R-HSA-418886:Netrin mediated repulsion signals; R-HSA-418890:Role of second messengers in netrin-1 signaling TTH5MRS ID TTH5MRS TTH5MRS TN Neuropsin (KLK8) TTH5MRS UP O60259 TTH5MRS UC KLK8_HUMAN TTH5MRS BC Peptidase TTH5MRS SN hK8; UNQ283/PRO322; Tumor-associated differentially expressed gene-14 protein; Tumor-associated differentially expressed gene 14 protein; TADG14; Serine protease TADG-14; Serine protease 19; PRSS19; Ovasin; Neuropsin (M(r) 25032); NRPN; NP; Kallikrein-8; Kallikrein 8; KLK8 (neuropsin/ovasin) TTH5MRS GN KLK8 TTH5MRS FC Cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte proliferation. Plays a role in the secondary phase of pathogenesis following spinal cord injury. Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. TTH5MRS EC EC 3.4.21.118 TTH5MRS PD 5MS4; 5MS3 TTH5MRS SQ MGRPRPRAAKTWMFLLLLGGAWAGHSRAQEDKVLGGHECQPHSQPWQAALFQGQQLLCGGVLVGGNWVLTAAHCKKPKYTVRLGDHSLQNKDGPEQEIPVVQSIPHPCYNSSDVEDHNHDLMLLQLRDQASLGSKVKPISLADHCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKIFPQKKCEDAYPGQITDGMVCAGSSKGADTCQGDSGGPLVCDGALQGITSWGSDPCGRSDKPGVYTNICRYLDWIKKIIGSKG TTH5MRS TT Literature-reported TTIM2WO ID TTIM2WO TTIM2WO TN Neurotrophin-4 (NTF4) TTIM2WO UP P34130 TTIM2WO UC NTF4_HUMAN TTIM2WO BC Growth factor TTIM2WO SN Neutrophic factor 4; Neurotrophin5; Neurotrophin4; Neurotrophin-5; NTF5; NT4; NT-5; NT-4 TTIM2WO GN NTF4 TTIM2WO FC Target-derived survival factor for peripheral sensory sympathetic neurons. TTIM2WO PD 1HCF; 1B98; 1B8M TTIM2WO SQ MLPLPSCSLPILLLFLLPSVPIESQPPPSTLPPFLAPEWDLLSPRVVLSRGAPAGPPLLFLLEAGAFRESAGAPANRSRRGVSETAPASRRGELAVCDAVSGWVTDRRTAVDLRGREVEVLGEVPAAGGSPLRQYFFETRCKADNAEEGGPGAGGGGCRGVDRRHWVSECKAKQSYVRALTADAQGRVGWRWIRIDTACVCTLLSRTGRA TTIM2WO TT Literature-reported TTIM2WO FM NGF-beta family TTIM2WO KE hsa04010:MAPK signaling pathway; hsa04722:Neurotrophin signaling pathway TTRU01G ID TTRU01G TTRU01G TN N-glycosylase/DNA lyase (OGG1) TTRU01G UP O15527 TTRU01G UC OGG1_HUMAN TTRU01G BC Type-1 OGG1 family TTRU01G SN OGH1; MUTM; MMH TTRU01G GN OGG1 TTRU01G FC DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion. TTRU01G PD 5AN4; 3KTU; 3IH7; 2XHI; 2NOZ TTRU01G SQ MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQSRHAQEPPAKRRKGSKGPEG TTRU01G TT Literature-reported TTRU01G KE hsa03410:Base excision repair TT3VZ24 ID TT3VZ24 TT3VZ24 TN NIMA-related kinase 2 (NEK2) TT3VZ24 UP P51955 TT3VZ24 UC NEK2_HUMAN TT3VZ24 BC Kinase TT3VZ24 SN Serine/threonine-protein kinase Nek2; NimA-related protein kinase 2; NimA-like protein kinase 1; Never in mitosis A-related kinase 2; NLK1; NEK2A; HSPK 21 TT3VZ24 GN NEK2 TT3VZ24 FC Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly. NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis. Involved in the regulation of centrosome disjunction. Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. TT3VZ24 EC EC 2.7.11.1 TT3VZ24 PD 6H0O; 5M57; 5M55; 5M53; 5M51 TT3VZ24 SQ MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLIADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNPELLNLPSSVIKKKVHFSGESKENIMRSENSESQLTSKSKCKDLKKRLHAAQLRAQALSDIEKNYQLKSRQILGMR TT3VZ24 TT Literature-reported TT1TYN7 ID TT1TYN7 TT1TYN7 TN Nuclear receptor ROR-alpha (RORA) TT1TYN7 UP P35398 TT1TYN7 UC RORA_HUMAN TT1TYN7 BC Nuclear hormone receptor TT1TYN7 SN Retinoid-related orphan receptor-alpha; Retinoic acid-related orphan receptor alpha; RZRA; RAR-related orphan receptor A; Nuclear receptor subfamily 1 group F member 1; Nuclear receptor RZR-alpha; NR1F1 TT1TYN7 GN RORA TT1TYN7 FC Key regulator of embryonic development, cellular differentiation, immunity, circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively. Recruits distinct combinations of cofactors to target genes regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates genes involved in photoreceptor development including OPN1SW, OPN1SM and ARR3 and skeletal muscle development with MYOD1. Required for proper cerebellum development. Regulates SHH gene expression, among others, to induce granule cells proliferation as well as expression of genes involved in calcium-mediated signal transduction. Regulates the circadian expression of several clock genes, including CLOCK, ARNTL/BMAL1, NPAS2 and CRY1. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as ARNTL/BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORA-mediated activation of clock genes expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Regulates genes involved in lipid metabolism such as apolipoproteins APOA1, APOA5, APOC3 and PPARG. In liver, has specific and redundant functions with RORC as positive or negative modulator of expression of genes encoding phase I and phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as CYP7B1 and SULT2A1. Induces a rhythmic expression of some of these genes. In addition, interplays functionally with NR1H2 and NR1H3 for the regulation of genes involved in cholesterol metabolism. Also involved in the regulation of hepatic glucose metabolism through the modulation of G6PC and PCK1. In adipose tissue, plays a role as negative regulator of adipocyte differentiation, probably acting through dual mechanisms. May suppress CEBPB-dependent adipogenesis through direct interaction and PPARG-dependent adipogenesis through competition for DNA-binding. Downstream of IL6 and TGFB and synergistically with RORC isoform 2, is implicated in the lineage specification of uncommitted CD4(+) T-helper (T(H)) cells into T(H)17 cells, antagonizing the T(H)1 program. Probably regulates IL17 and IL17F expression on T(H) by binding to the essential enhancer conserved non-coding sequence 2 (CNS2) in the IL17-IL17F locus. Involved in hypoxia signaling by interacting with and activating the transcriptional activity of HIF1A. May inhibit cell growth in response to cellular stress. May exert an anti-inflammatory role by inducing CHUK expression and inhibiting NF-kappa-B signaling. Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. TT1TYN7 PD 4S15; 1S0X; 1N83 TT1TYN7 SQ MESAPAAPDPAASEPGSSGADAAAGSRETPLNQESARKSEPPAPVRRQSYSSTSRGISVTKKTHTSQIEIIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQSNATYSCPRQKNCLIDRTSRNRCQHCRLQKCLAVGMSRDAVKFGRMSKKQRDSLYAEVQKHRMQQQQRDHQQQPGEAEPLTPTYNISANGLTELHDDLSNYIDGHTPEGSKADSAVSSFYLDIQPSPDQSGLDINGIKPEPICDYTPASGFFPYCSFTNGETSPTVSMAELEHLAQNISKSHLETCQYLREELQQITWQTFLQEEIENYQNKQREVMWQLCAIKITEAIQYVVEFAKRIDGFMELCQNDQIVLLKAGSLEVVFIRMCRAFDSQNNTVYFDGKYASPDVFKSLGCEDFISFVFEFGKSLCSMHLTEDEIALFSAFVLMSADRSWLQEKVKIEKLQQKIQLALQHVLQKNHREDGILTKLICKVSTLRALCGRHTEKLMAFKAIYPDIVRLHFPPLYKELFTSEFEPAMQIDG TT1TYN7 TT Preclinical TT1TYN7 FM Nuclear hormone receptor family TT1TYN7 KE hsa04710:Circadian rhythm; hsa05321:Inflammatory bowel disease (IBD) TT1TYN7 RC R-HSA-1368082:RORA activates gene expression; R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-1989781:PPARA activates gene expression; R-HSA-383280:Nuclear Receptor transcription pathway; R-HSA-400253:Circadian Clock TTK1V5Q ID TTK1V5Q TTK1V5Q TN Nucleolin messenger RNA (NCL mRNA) TTK1V5Q UP P19338 TTK1V5Q UC NUCL_HUMAN TTK1V5Q BC mRNA target TTK1V5Q SN Protein C23 (mRNA); Nucleolin (mRNA) TTK1V5Q GN NCL TTK1V5Q FC It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Nucleolin is the major nucleolar protein of growing eukaryotic cells. TTK1V5Q PD 2KRR; 2FC9; 2FC8 TTK1V5Q SQ MVKLAKAGKNQGDPKKMAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDDDDDEEDDSEEEAMETTPAKGKKAAKVVPVKAKNVAEDEDEEEDDEDEDDDDDEDDEDDDDEDDEEEEEEEEEEPVKEAPGKRKKEMAKQKAAPEAKKQKVEGTEPTTAFNLFVGNLNFNKSAPELKTGISDVFAKNDLAVVDVRIGMTRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGKDSKKERDARTLLAKNLPYKVTQDELKEVFEDAAEIRLVSKDGKSKGIAYIEFKTEADAEKTFEEKQGTEIDGRSISLYYTGEKGQNQDYRGGKNSTWSGESKTLVLSNLSYSATEETLQEVFEKATFIKVPQNQNGKSKGYAFIEFASFEDAKEALNSCNKREIEGRAIRLELQGPRGSPNARSQPSKTLFVKGLSEDTTEETLKESFDGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDHKPQGKKTKFE TTK1V5Q TT Literature-reported TTK1V5Q FM mRNA target TTK1V5Q KE hsa05130:Pathogenic Escherichia coli infection TTDY8JH ID TTDY8JH TTDY8JH TN Nucleoside diphosphate kinase A (NM23-H1) TTDY8JH UP P15531 TTDY8JH UC NDKA_HUMAN TTDY8JH BC Kinase TTDY8JH SN nm23H1; Tumor metastatic processassociated protein; Tumor metastatic process-associated protein; NM23; NDPKA; NDP kinase A; NDK A; Metastasis inhibition factor nm23; Granzyme Aactivated DNase; Granzyme A-activated DNase; GAAD TTDY8JH GN NME1 TTDY8JH FC The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair. Major role in the synthesis of nucleoside triphosphates other than ATP. TTDY8JH EC EC 2.7.4.6 TTDY8JH PD 5UI4; 4ENO; 3L7U; 2HVE; 2HVD TTDY8JH SQ MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEIGLWFHPEELVDYTSCAQNWIYE TTDY8JH TT Literature-reported TTDY8JH FM Kinase TTBLG3H ID TTBLG3H TTBLG3H TN P120 messenger RNA (NOP2 mRNA) TTBLG3H UP P46087 TTBLG3H UC NOP2_HUMAN TTBLG3H BC mRNA target TTBLG3H SN Proliferation-associated nucleolar protein p120 (mRNA); Proliferating-cell nucleolar antigen p120 (mRNA); Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferase (mRNA); Nucleolar protein 2 homolog (mRNA); Nucleolar protein 1 (mRNA); NSUN1 (mRNA); NOL1 (mRNA) TTBLG3H GN NOP2 TTBLG3H FC S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 4447 in 28S rRNA. May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation. Involved in ribosomal large subunit assembly. TTBLG3H EC EC 2.1.1.- TTBLG3H SQ MGRKLDPTKEKRGPGRKARKQKGAETELVRFLPAVSDENSKRLSSRARKRAAKRRLGSVEAPKTNKSPEAKPLPGKLPKGISAGAVQTAGKKGPQSLFNAPRGKKRPAPGSDEEEEEEDSEEDGMVNHGDLWGSEDDADTVDDYGADSNSEDEEEGEALLPIERAARKQKAREAAAGIQWSEEETEDEEEEKEVTPESGPPKVEEADGGLQINVDEEPFVLPPAGEMEQDAQAPDLQRVHKRIQDIVGILRDFGAQREEGRSRSEYLNRLKKDLAIYYSYGDFLLGKLMDLFPLSELVEFLEANEVPRPVTLRTNTLKTRRRDLAQALINRGVNLDPLGKWSKTGLVVYDSSVPIGATPEYLAGHYMLQGASSMLPVMALAPQEHERILDMCCAPGGKTSYMAQLMKNTGVILANDANAERLKSVVGNLHRLGVTNTIISHYDGRQFPKVVGGFDRVLLDAPCSGTGVISKDPAVKTNKDEKDILRCAHLQKELLLSAIDSVNATSKTGGYLVYCTCSITVEENEWVVDYALKKRNVRLVPTGLDFGQEGFTRFRERRFHPSLRSTRRFYPHTHNMDGFFIAKFKKFSNSIPQSQTGNSETATPTNVDLPQVIPKSENSSQPAKKAKGAAKTKQQLQKQQHPKKASFQKLNGISKGADSELSTVPSVTKTQASSSFQDSSQPAGKAEGIREPKVTGKLKQRSPKLQSSKKVAFLRQNAPPKGTDTQTPAVLSPSKTQATLKPKDHHQPLGRAKGVEKQQLPEQPFEKAAFQKQNDTPKGPQPPTVSPIRSSRPPPAKRKKSQSRGNSQLLLS TTBLG3H TT Literature-reported TTBLG3H FM mRNA target TTFN95D ID TTFN95D TTFN95D TN PAK-1 protein kinase (PAK1) TTFN95D UP Q13153 TTFN95D UC PAK1_HUMAN TTFN95D BC Kinase TTFN95D SN p65-PAK; p21-activated kinase 1; Serine/threonine-protein kinase PAK 1; PAK-1; Alpha-PAK TTFN95D GN PAK1 TTFN95D FC Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion. In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling. Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. TTFN95D EC EC 2.7.11.1 TTFN95D PD 6B16; 5KBR; 5KBQ; 5IME; 5DFP TTFN95D SQ MSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVSEDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNH TTFN95D TT Literature-reported TT279WO ID TT279WO TT279WO TN PAK-2 protein kinase (PAK2) TT279WO UP Q13177 TT279WO UC PAK2_HUMAN TT279WO BC Kinase TT279WO SN p21-activated kinase 2; Serine/threonine-protein kinase PAK 2; S6/H4 kinase; PAK65; PAK-2; Gamma-PAK TT279WO GN PAK2 TT279WO FC Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3. 3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation. Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. TT279WO EC EC 2.7.11.1 TT279WO PD 3PCS TT279WO SQ MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAKGTEAPAVVTEEEDDDEETAPPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR TT279WO TT Literature-reported TT317EC ID TT317EC TT317EC TN PDGFR beta messenger RNA (PDGFRB mRNA) TT317EC UP P09619 TT317EC UC PGFRB_HUMAN TT317EC BC mRNA target TT317EC SN Platelet-derived growth factor receptor 1 (mRNA); PDGFR1 (mRNA); PDGFR-beta (mRNA); PDGFR-1 (mRNA); PDGFR (mRNA); PDGF-R-beta (mRNA); CD140b antigen (mRNA); CD140b (mRNA); CD140 antigen-like family member B (mRNA); Beta-type platelet-derived growth factor receptor (mRNA); Beta-PDGFR (mRNA); Beta platelet-derived growth factor receptor (mRNA) TT317EC GN PDGFRB TT317EC FC Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. TT317EC EC EC 2.7.10.1 TT317EC PD 3MJG; 2PLE; 2PLD; 2L6W; 2IUI TT317EC SQ MRLPGAMPALALKGELLLLSLLLLLEPQISQGLVVTPPGPELVLNVSSTFVLTCSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFVPDPTVGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLGEVGTLQFAELHRSRTLQVVFEAYPPPTVLWFKDNRTLGDSSAGEIALSTRNVSETRYVSELTLVRVKVAEAGHYTMRAFHEDAEVQLSFQLQINVPVRVLELSESHPDSGEQTVRCRGRGMPQPNIIWSACRDLKRCPRELPPTLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRCTLRNAVGQDTQEVIVVPHSLPFKVVVISAILALVVLTIISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPMQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQHHSDKRRPPSAELYSNALPVGLPLPSHVSLTGESDGGYMDMSKDESVDYVPMLDMKGDVKYADIESSNYMAPYDNYVPSAPERTCRATLINESPVLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGFHGLRSPLDTSSVLYTAVQPNEGDNDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQDEPEPEPQLELQVEPEPELEQLPDSGCPAPRAEAEDSFL TT317EC TT Literature-reported TT317EC FM mRNA target TTMY6BZ ID TTMY6BZ TTMY6BZ TN PDZ binding kinase (PBK) TTMY6BZ UP Q96KB5 TTMY6BZ UC TOPK_HUMAN TTMY6BZ BC Kinase TTMY6BZ SN TOPK; T-LAK cell-originated protein kinase; Spermatogenesis-related protein kinase; SPK protein; PDZ-binding kinase; Nori-3; MAPKK-like protein kinase; Lymphokine-activated killer T-cell-originated protein kinase; Cancer/testis antigen 84; CT84 TTMY6BZ GN PBK TTMY6BZ FC Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage. Phosphorylates MAP kinase p38. TTMY6BZ EC EC 2.7.12.2 TTMY6BZ PD 5J0A TTMY6BZ SQ MEGISNFKTPSKLSEKKKSVLCSTPTINIPASPFMQKLGFGTGVNVYLMKRSPRGLSHSPWAVKKINPICNDHYRSVYQKRLMDEAKILKSLHHPNIVGYRAFTEANDGSLCLAMEYGGEKSLNDLIEERYKASQDPFPAAIILKVALNMARGLKYLHQEKKLLHGDIKSSNVVIKGDFETIKICDVGVSLPLDENMTVTDPEACYIGTEPWKPKEAVEENGVITDKADIFAFGLTLWEMMTLSIPHINLSNDDDDEDKTFDESDFDDEAYYAALGTRPPINMEELDESYQKVIELFSVCTNEDPKDRPSAAHIVEALETDV TTMY6BZ TT Literature-reported TTQHAXM ID TTQHAXM TTQHAXM TN Peptidyl arginine deiminase type IV (PADI4) TTQHAXM UP Q9UM07 TTQHAXM UC PADI4_HUMAN TTQHAXM BC Carbon-nitrogen hydrolase TTQHAXM SN Protein-arginine deiminase type-4; Protein-arginine deiminase type IV; Peptidylarginine deiminase IV; PDI5; PADI5; PAD4; HL-60 PAD TTQHAXM GN PADI4 TTQHAXM FC Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg-54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci. Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription. Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1. Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance. TTQHAXM EC EC 3.5.3.15 TTQHAXM PD 5N1B; 5N0Z; 5N0Y; 5N0M; 4X8G TTQHAXM SQ MAQGTLIRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVVDIAHGPPAKKKSTGSSTWPLDPGVEVTLTMKVASGSTGDQKVQISYYGPKTPPVKALLYLTGVEISLCADITRTGKVKPTRAVKDQRTWTWGPCGQGAILLVNCDRDNLESSAMDCEDDEVLDSEDLQDMSLMTLSTKTPKDFFTNHTLVLHVARSEMDKVRVFQATRGKLSSKCSVVLGPKWPSHYLMVPGGKHNMDFYVEALAFPDTDFPGLITLTISLLDTSNLELPEAVVFQDSVVFRVAPWIMTPNTQPPQEVYACSIFENEDFLKSVTTLAMKAKCKLTICPEEENMDDQWMQDEMEIGYIQAPHKTLPVVFDSPRNRGLKEFPIKRVMGPDFGYVTRGPQTGGISGLDSFGNLEVSPPVTVRGKEYPLGRILFGDSCYPSNDSRQMHQALQDFLSAQQVQAPVKLYSDWLSVGHVDEFLSFVPAPDRKGFRLLLASPRSCYKLFQEQQNEGHGEALLFEGIKKKKQQKIKNILSNKTLREHNSFVERCIDWNRELLKRELGLAESDIIDIPQLFKLKEFSKAEAFFPNMVNMLVLGKHLGIPKPFGPVINGRCCLEEKVCSLLEPLGLQCTFINDFFTYHIRHGEVHCGTNVRRKPFSFKWWNMVP TTQHAXM TT Literature-reported TTPBL9I ID TTPBL9I TTPBL9I TN Peroxiredoxin-4 (PRDX4) TTPBL9I UP Q13162 TTPBL9I UC PRDX4_HUMAN TTPBL9I BC Peroxidases TTPBL9I SN Thioredoxindependent peroxide reductase A0372; Thioredoxin peroxidase AO372; PrxIV; Peroxiredoxin4; Peroxiredoxin IV; PRDX4; Antioxidant enzyme AOE372; AOE372 TTPBL9I GN PRDX4 TTPBL9I FC Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. TTPBL9I EC EC 1.11.1.15 TTPBL9I PD 5HQP; 4RQX; 3TKS; 3TKR; 3TKQ TTPBL9I SQ MEALPLLAATTPDHGRHRRLLLLPLLLFLLPAGAVQGWETEERPRTREEECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN TTPBL9I TT Literature-reported TT73TEJ ID TT73TEJ TT73TEJ TN Phosphodiesterase 1A (PDE1A) TT73TEJ UP P54750 TT73TEJ UC PDE1A_HUMAN TT73TEJ BC Phosphoric diester hydrolase TT73TEJ SN hCam-1; Cam-PDE 1A; Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A; 61 kDa Cam-PDE TT73TEJ GN PDE1A TT73TEJ FC Has a higher affinity for cGMP than for cAMP. Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. TT73TEJ EC EC 3.1.4.17 TT73TEJ PD 1LXQ TT73TEJ SQ MGSSATEIEELENTTFKYLTGEQTEKMWQRLKGILRCLVKQLERGDVNVVDLKKNIEYAASVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRSIVHAVQAGIFVERMYRKTYHMVGLAYPAAVIVTLKDVDKWSFDVFALNEASGEHSLKFMIYELFTRYDLINRFKIPVSCLITFAEALEVGYSKYKNPYHNLIHAADVTQTVHYIMLHTGIMHWLTELEILAMVFAAAIHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLMQEEEMNILINLSKDDWRDLRNLVIEMVLSTDMSGHFQQIKNIRNSLQQPEGIDRAKTMSLILHAADISHPAKSWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGFIDFIVEPTFSLLTDSTEKIVIPLIEEASKAETSSYVASSSTTIVGLHIADALRRSNTKGSMSDGSYSPDYSLAAVDLKSFKNNLVDIIQQNKERWKELAAQEARTSSQKCEFIHQ TT73TEJ TT Literature-reported TTW2HRK ID TTW2HRK TTW2HRK TN Phosphodiesterase 1C (PDE1C) TTW2HRK UP Q14123 TTW2HRK UC PDE1C_HUMAN TTW2HRK BC Phosphoric diester hydrolase TTW2HRK SN Hcam3; Cam-PDE 1C; Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C; 3',5'-cyclic-GMP phosphodiesterase; 3',5'-cyclic-AMP phosphodiesterase TTW2HRK GN PDE1C TTW2HRK FC Has a high affinity for both cAMP and cGMP. Modulates the amplitude and duration of the cAMP signal in sensory cilia in response to odorant stimulation, hence contributing to the generation of action potentials. Regulates smooth muscle cell proliferation. Regulates the stability of growth factor receptors, including PDGFRB. Calmodulin-dependent cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. TTW2HRK EC EC 3.1.4.- TTW2HRK PD 1LXS TTW2HRK SQ MESPTKEIEEFESNSLKYLQPEQIEKIWLRLRGLRKYKKTSQRLRSLVKQLERGEASVVDLKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRRSDEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIEALKDVDKWSFDVFSLNEASGDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTVHYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENHHLSAAYRLLQDDEEMNILINLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPEAIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKSTMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDETSQTGGTGQRRSSLNSISSSDAKRSGVKTSGSEGSAPINNSVISVDYKSFKATWTEVVHINRERWRAKVPKEEKAKKEAEEKARLAAEEQQKEMEAKSQAEEGASGKAEKKTSGETKNQVNGTRANKSDNPRGKNSKAEKSSGEQQQNGDFKDGKNKTDKKDHSNIGNDSKKTDGTKQRSHGSPAPSTSSTCRLTLPVIKPPLRHFKRPAYASSSYAPSVSKKTDEHPARYKMLDQRIKMKKIQNISHNWNRK TTW2HRK TT Literature-reported TT6A59G ID TT6A59G TT6A59G TN Phosphodiesterase 4C (PDE4C) TT6A59G UP Q08493 TT6A59G UC PDE4C_HUMAN TT6A59G BC Phosphoric diester hydrolase TT6A59G SN cAMP-specific 3',5'-cyclic phosphodiesterase 4C; PDE21; DPDE1 TT6A59G GN PDE4C TT6A59G FC Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. TT6A59G EC EC 3.1.4.53 TT6A59G PD 2QYM; 1LXU TT6A59G SQ MENLGVGEGAEACSRLSRSRGRHSMTRAPKHLWRQPRRPIRIQQRFYSDPDKSAGCRERDLSPRPELRKSRLSWPVSSCRRFDLENGLSCGRRALDPQSSPGLGRIMQAPVPHSQRRESFLYRSDSDYELSPKAMSRNSSVASDLHGEDMIVTPFAQVLASLRTVRSNVAALARQQCLGAAKQGPVGNPSSSNQLPPAEDTGQKLALETLDELDWCLDQLETLQTRHSVGEMASNKFKRILNRELTHLSETSRSGNQVSEYISRTFLDQQTEVELPKVTAEEAPQPMSRISGLHGLCHSASLSSATVPRFGVQTDQEEQLAKELEDTNKWGLDVFKVAELSGNRPLTAIIFSIFQERDLLKTFQIPADTLATYLLMLEGHYHANVAYHNSLHAADVAQSTHVLLATPALEAVFTDLEILAALFASAIHDVDHPGVSNQFLINTNSELALMYNDASVLENHHLAVGFKLLQAENCDIFQNLSAKQRLSLRRMVIDMVLATDMSKHMNLLADLKTMVETKKVTSLGVLLLDNYSDRIQVLQNLVHCADLSNPTKPLPLYRQWTDRIMAEFFQQGDRERESGLDISPMCDKHTASVEKSQVGFIDYIAHPLWETWADLVHPDAQDLLDTLEDNREWYQSKIPRSPSDLTNPERDGPDRFQFELTLEEAEEEDEEEEEEGEETALAKEALELPDTELLSPEAGPDPGDLPLDNQRT TT6A59G TT Patented-recorded TTIS4OW ID TTIS4OW TTIS4OW TN Phosphodiesterase 8 (PDE8) TTIS4OW UP O60658 TTIS4OW UC PDE8A_HUMAN TTIS4OW BC Phosphoric diester hydrolase TTIS4OW SN High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A TTIS4OW GN PDE8A TTIS4OW FC May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development. Binding to RAF1 reduces RAF1 'Ser-259' inhibitory-phosphorylation and stimulates RAF1-dependent EGF-activated ERK-signaling. Protects against cell death induced by hydrogen peroxide and staurosporine. Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. TTIS4OW EC EC 3.1.4.53 TTIS4OW PD 3ECN; 3ECM; 1LXX; 1LHQ TTIS4OW SQ MGCAPSIHISERLVAEDAPSPAAPPLSSGGPRLPQGQKTAALPRTRGAGLLESELRDGSGKKVAVADVQFGPMRFHQDQLQVLLVFTKEDNQCNGFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRQLDAEALCRSIRSSKLSENTVIVGVVRRVDREELSVMPFISAGFTRRYVENPNIMACYNELLQLEFGEVRSQLKLRACNSVFTALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKAEKISECVQSDTHTDNQTGKHKDRRKGSLDVKAVASRATEVSSQRRHSSMARIHSMTIEAPITKVINIINAAQESSPMPVTEALDRVLEILRTTELYSPQFGAKDDDPHANDLVGGLMSDGLRRLSGNEYVLSTKNTQMVSSNIITPISLDDVPPRIARAMENEEYWDFDIFELEAATHNRPLIYLGLKMFARFGICEFLHCSESTLRSWLQIIEANYHSSNPYHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNAGSELAILYNDTAVLESHHAALAFQLTTGDDKCNIFKNMERNDYRTLRQGIIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKNQEVINTMLRTPENRTLIKRMLIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFVDLPDLMQHLDNNFKYWKGLDEMKLRNLRPPPE TTIS4OW TT Patented-recorded TT8DRCK ID TT8DRCK TT8DRCK TN Phosphoglycerate dehydrogenase (PHGDH) TT8DRCK UP O43175 TT8DRCK UC SERA_HUMAN TT8DRCK BC Short-chain dehydrogenases reductase TT8DRCK SN PGDH3; Malate dehydrogenase; D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase TT8DRCK GN PHGDH TT8DRCK FC Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate. TT8DRCK EC EC 1.1.1.95 TT8DRCK PD 5OFW; 5OFV; 5OFM; 5NZQ; 5NZP TT8DRCK SQ MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQGTSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGECLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPTMIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHF TT8DRCK TT Literature-reported TT4YO0Z ID TT4YO0Z TT4YO0Z TN Phosphopantetheine adenylyltransferase (PPAT) TT4YO0Z UP Q13057 (180-358) TT4YO0Z UC COASY_HUMAN TT4YO0Z BC Kinase TT4YO0Z SN Pantetheine-phosphate adenylyltransferase; Dephospho-CoA pyrophosphorylase; COASY TT4YO0Z GN COASY TT4YO0Z FC Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation. TT4YO0Z EC EC 2.7.7.3 TT4YO0Z SQ VAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDLRHTENEEDKVSSSSFRQRMLGNLLRPPYERPELPTCL TT4YO0Z TT Literature-reported TT4YO0Z KE hsa00770:Pantothenate and CoA biosynthesis; hsa01100:Metabolic pathways TT9NVXQ ID TT9NVXQ TT9NVXQ TN Phosphoribosylaminoimidazolecarboxamide formyltransferase (ATIC) TT9NVXQ UP P31939 TT9NVXQ UC PUR9_HUMAN TT9NVXQ BC Methyltransferase TT9NVXQ SN PURH; OK/SW-cl.86; Bifunctional purine biosynthesis protein PURH TT9NVXQ GN ATIC TT9NVXQ FC Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis. TT9NVXQ PD 5UZ0; 5UY8; 1PL0; 1PKX; 1P4R TT9NVXQ SQ MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLYPFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVVSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKELKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTILSKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVVTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHCTRLAGDKANYWWLRHHPQVLSMKFKTGVKRAEISNAIDQYVTGTIGEDEDLIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRSGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH TT9NVXQ TT Literature-reported TTCGOIN ID TTCGOIN TTCGOIN TN PIM-3 protein kinase (PIM3) TTCGOIN UP Q86V86 TTCGOIN UC PIM3_HUMAN TTCGOIN BC Kinase TTCGOIN SN Serine/threonine-protein kinase pim-3 TTCGOIN GN PIM3 TTCGOIN FC May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression, protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth. Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis, promote cell survival and protein translation. TTCGOIN EC EC 2.7.11.1 TTCGOIN SQ MLLSKFGSLAHLCGPGGVDHLPVKILQPAKADKESFEKAYQVGAVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGSLGGATVPLEVVLLRKVGAAGGARGVIRLLDWFERPDGFLLVLERPEPAQDLFDFITERGALDEPLARRFFAQVLAAVRHCHSCGVVHRDIKDENLLVDLRSGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLLFRRRVSPECQQLIRWCLSLRPSERPSLDQIAAHPWMLGADGGVPESCDLRLCTLDPDDVASTTSSSESL TTCGOIN TT Patented-recorded TTCGOIN FM Kinase TTYAWV0 ID TTYAWV0 TTYAWV0 TN Plasmodium Acetyl-CoA carboxylase 1 (Malaria ACC1) TTYAWV0 UP Q9U752 TTYAWV0 UC Q9U752_PLAFA TTYAWV0 BC Carbon-carbon ligase TTYAWV0 SN Acetyl-CoA carboxylase; ACC1; ACC-alpha TTYAWV0 GN Malaria ACC1 TTYAWV0 FC Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. This protein carries three functions: biotin carboxyl carrier protein, biotin carboxylase, and carboxyltransferase. TTYAWV0 SQ SQGGGGKGIRKVENEYEIKKAYEQVQNELPNSPIFLMKVCNNVRHIEIQVVGDMYGNVCSLSGRDCTTQRRFQKIFEEGPPSVVPYPIFREMEKSSIRLTKMIKYRGAGTIEYLYDQINKKYFFLELNPRL TTYAWV0 TT Literature-reported TTYAWV0 KE hsa00061:Fatty acid biosynthesis; hsa00620:Pyruvate metabolism; hsa00640:Propanoate metabolism; hsa01100:Metabolic pathways; hsa01212:Fatty acid metabolism; hsa04152:AMPK signaling pathway; hsa04910:Insulin signaling pathway; hsa04922:Glucagon signaling pathway TTYAWV0 RC R-HSA-163765:ChREBP activates metabolic gene expression; R-HSA-200425:Import of palmitoyl-CoA into the mitochondrial matrix; R-HSA-2426168:Activation of gene expression by SREBF (SREBP); R-HSA-75105:Fatty Acyl-CoA Biosynthesis TTRAMF0 ID TTRAMF0 TTRAMF0 TN Plasmodium Cytochrome B (Malaria MT-CYB) TTRAMF0 UP Q02768 TTRAMF0 UC CYB_PLAFA TTRAMF0 BC Cytochrome b family TTRAMF0 SN MT-CYB; Cyb TTRAMF0 GN Malaria MT-CYB TTRAMF0 FC Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. TTRAMF0 SQ MNFYSINLVKAHLINYPCPLNINFLWNYGFLLGIIFFIQIITGVFLASRYTPDVSYAYYSIQHILRELWSGWCFRYMHATGASLVFLLTYLHILRGLNYSYMYLPLSWISGLILFMIFIVTAFVGYVLPWGQMSYWGATVITNLLSSIPVAVIWICGGYTVSDPTIKRFFVLHFILPFIGLCIVFIHIFFLHLHGSTNPLGYDTALKIPFYPNLLSLDVKGFNNVIILFLIQSLFGIIPLSHPDNAIVVNTYVTPSQIVPEWYFLPFYAMLKTVPSKPAGLVIVLLSLQLLFLLAEQRSLTTIIQFKMIFGARDYSVPIIWFMCAFYALLWIGCQLPQDIFILYGRLFIVLFFCSGLFVLVHYRRTHYDYSSQANI TTRAMF0 TT Literature-reported TTRAMF0 KE pfa00190:Oxidative phosphorylation; pfa01100:Metabolic pathways TT1FL6V ID TT1FL6V TT1FL6V TN Plasmodium Fructose-bisphosphate aldolase (Malaria FBA) TT1FL6V UP P14223 TT1FL6V UC ALF_PLAFA TT1FL6V BC Carbon-carbon lyase TT1FL6V SN Fructose-bisphosphate aldolase; 41 kDa antigen TT1FL6V GN Malaria FBA TT1FL6V FC Catalyzes carboncarbon bond formation (or cleavage). Participate in the metabolically important pathways of gluconeogenesis and glycolysis. TT1FL6V PD 2PC4; 2EPH; 1A5C TT1FL6V SQ MAHCTEYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRTVLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALTFSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGGAGGENAGASLYEKKYVY TT1FL6V TT Literature-reported TTH9VL3 ID TTH9VL3 TTH9VL3 TN Plasmodium Plasmepsin 1 (Malaria PLA1) TTH9VL3 UP P39898 TTH9VL3 UC PLM1_PLAFA TTH9VL3 BC Peptidase TTH9VL3 SN Plasmepsin I; PFAPG; Aspartic hemoglobinase I TTH9VL3 GN Malaria PLA1 TTH9VL3 FC Participates in the digestion of the host hemoglobin. Initial cleavage at the hinge region of hemoglobin, than cleaves at other sites, leading to denaturation of the molecule and to further degradation. TTH9VL3 PD 3QS1; 3QRV; 1LDU; 1LCR TTH9VL3 SQ MALSIKEDFSSAFAKNESAVNSSTFNNNMKTWKIQKRFQILYVFFFLLITGALFYYLIDNVLFPKNKKINEIMNTSKHVIIGFSIENSHDRIMKTVKQHRLKNYIKESLKFFKTGLTQKPHLGNAGDSVTLNDVANVMYYGEAQIGDNKQKFAFIFDTGSANLWVPSAQCNTIGCKTKNLYDSNKSKTYEKDGTKVEMNYVSGTVSGFFSKDIVTIANLSFPYKFIEVTDTNGFEPAYTLGQFDGIVGLGWKDLSIGSVDPVVVELKNQNKIEQAVFTFYLPFDDKHKGYLTIGGIEDRFYEGQLTYEKLNHDLYWQVDLDLHFGNLTVEKATAIVDSGTSSITAPTEFLNKFFEGLDVVKIPFLPLYITTCNNPKLPTLEFRSATNVYTLEPEYYLQQIFDFGISLCMVSIIPVDLNKNTFILGDPFMRKYFTVFDYDNHTVGFALAKKKL TTH9VL3 TT Literature-reported TTGPNZQ ID TTGPNZQ TTGPNZQ TN Polo-like kinase 4 (PLK4) TTGPNZQ UP O00444 TTGPNZQ UC PLK4_HUMAN TTGPNZQ BC Kinase TTGPNZQ SN Serine/threonine-protein kinase Sak; Serine/threonine-protein kinase PLK4; Serine/threonine-protein kinase 18; STK18; SAK; PLK-4 TTGPNZQ GN PLK4 TTGPNZQ FC Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification. Serine/threonine-protein kinase that plays a central role in centriole duplication. TTGPNZQ EC EC 2.7.11.21 TTGPNZQ PD 5LHZ; 5LHY; 4YYP; 4YUR; 4N9J TTGPNZQ SQ MATCIGEKIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEMNRYLKNRVKPFSENEARHFMHQIITGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPSFLSIEAKDLIHQLLRRNPADRLSLSSVLDHPFMSRNSSTKSKDLGTVEDSIDSGHATISTAITASSSTSISGSLFDKRRLLIGQPLPNKMTVFPKNKSSTDFSSSGDGNSFYTQWGNQETSNSGRGRVIQDAEERPHSRYLRRAYSSDRSGTSNSQSQAKTYTMERCHSAEMLSVSKRSGGGENEERYSPTDNNANIFNFFKEKTSSSSGSFERPDNNQALSNHLCPGKTPFPFADPTPQTETVQQWFGNLQINAHLRKTTEYDSISPNRDFQGHPDLQKDTSKNAWTDTKVKKNSDASDNAHSVKQQNTMKYMTALHSKPEIIQQECVFGSDPLSEQSKTRGMEPPWGYQNRTLRSITSPLVAHRLKPIRQKTKKAVVSILDSEEVCVELVKEYASQEYVKEVLQISSDGNTITIYYPNGGRGFPLADRPPSPTDNISRYSFDNLPEKYWRKYQYASRFVQLVRSKSPKITYFTRYAKCILMENSPGADFEVWFYDGVKIHKTEDFIQVIEKTGKSYTLKSESEVNSLKEEIKMYMDHANEGHRICLALESIISEEERKTRSAPFFPIIIGRKPGSTSSPKALSPPPSVDSNYPTRERASFNRMVMHSAASPTQAPILNPSMVTNEGLGLTTTASGTDISSNSLKDCLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPNGQTTRYGENEKLPDYIKQKLQCLSSILLMFSNPTPNFH TTGPNZQ TT Literature-reported TT39J16 ID TT39J16 TT39J16 TN Poly [ADP-ribose] glycohydrolase (PARG) TT39J16 UP Q9Y4W7 TT39J16 UC PARG_HUMAN TT39J16 BC Glycosylase TT39J16 SN Poly(ADP-ribose) glycohydrolase TT39J16 GN PARG TT39J16 FC Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming. TT39J16 EC EC 3.2.1.143 TT39J16 PD 6HMN; 6HMM; 6HML; 6HMK; 6HH6 TT39J16 SQ MNAGPGCEPCTKRPRWGAATTSPAASDARSFPSRQRRVLDPKDAHVQFRVPPSSPACVPGRAGQHRGSATSLVFKQKTITSWMDTKGIKTAESESLDSKENNNTRIESMMSSVQKDNFYQHNVEKLENVSQLSLDKSPTEKSTQYLNQHQTAAMCKWQNEGKHTEQLLESEPQTVTLVPEQFSNANIDRSPQNDDHSDTDSEENRDNQQFLTTVKLANAKQTTEDEQAREAKSHQKCSKSCDPGEDCASCQQDEIDVVPESPLSDVGSEDVGTGPKNDNKLTRQESCLGNSPPFEKESEPESPMDVDNSKNSCQDSEADEETSPGFDEQEDGSSSQTANKPSRFQARDADIEFRKRYSTKGGEVRLHFQFEGGESRTGMNDLNAKLPGNISSLNVECRNSKQHGKKDSKITDHFMRLPKAEDRRKEQWETKHQRTERKIPKYVPPHLSPDKKWLGTPIEEMRRMPRCGIRLPLLRPSANHTVTIRVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDENGERTAGSRWELIQTALLNKFTRPQNLKDAILKYNVAYSKKWDFTALIDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSITMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKPLTRLHVTYEGTIEENGQGMLQVDFANRFVGGGVTSAGLVQEEIRFLINPELIISRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWSRSHEDGSERDDWQRRCTEIVAIDALHFRRYLDQFVPEKMRRELNKAYCGFLRPGVSSENLSAVATGNWGCGAFGGDARLKALIQILAAAAAERDVVYFTFGDSELMRDIYSMHIFLTERKLTVGDVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHAVESCAETADHSGQRTGT TT39J16 TT Literature-reported TTPFWHU ID TTPFWHU TTPFWHU TN Proprotein convertase subtilisin/kexin type 5 (PCSK5) TTPFWHU UP Q92824 TTPFWHU UC PCSK5_HUMAN TTPFWHU BC Peptidase TTPFWHU SN hPC6; Subtilisin/kexin-like protease PC5; Proprotein convertase 6; Proprotein convertase 5; PCSK5; PC6; PC5 TTPFWHU GN PCSK5 TTPFWHU FC Likely to represent a widespread endoprotease activity within the constitutive and regulated secretory pathway. Capable of cleavage at the RX(K/R)R consensus motif. Plays an essential role in pregnancy establishment by proteolytic activation of a number of important factors such as BMP2, CALD1 and alpha- integrins. TTPFWHU EC EC 3.4.21.- TTPFWHU SQ MGWGSRCCCPGRLDLLCVLALLGGCLLPVCRTRVYTNHWAVKIAGGFPEANRIASKYGFINIGQIGALKDYYHFYHSRTIKRSVISSRGTHSFISMEPKVEWIQQQVVKKRTKRDYDFSRAQSTYFNDPKWPSMWYMHCSDNTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRYDASNENKHGTRCAGEVAAAANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSFNPQHVHIYSASWGPDDDGKTVDGPAPLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGESYDKKIITTDLRQRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRAGHLNANDWKTNAAGFKVSHLYGFGLMDAEAMVMEAEKWTTVPRQHVCVESTDRQIKTIRPNSAVRSIYKASGCSDNPNRHVNYLEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTPSQLRNFKTPGKLKEWSLVLYGTSVQPYSPTNEFPKVERFRYSRVEDPTDDYGTEDYAGPCDPECSEVGCDGPGPDHCNDCLHYYYKLKNNTRICVSSCPPGHYHADKKRCRKCAPNCESCFGSHGDQCMSCKYGYFLNEETNSCVTHCPDGSYQDTKKNLCRKCSENCKTCTEFHNCTECRDGLSLQGSRCSVSCEDGRYFNGQDCQPCHRFCATCAGAGADGCINCTEGYFMEDGRCVQSCSISYYFDHSSENGYKSCKKCDISCLTCNGPGFKNCTSCPSGYLLDLGMCQMGAICKDGEYVDEHGHCQTCEASCAKCQGPTQEDCTTCPMTRIFDDGRCVSNCPSWKFEFENQCHPCHHTCQRCQGSGPTHCTSCGADNYGREHFLYQGECGDSCPEGHYATEGNTCLPCPDNCELCHSVHVCTRCMKGYFIAPTNHTCQKLECGQGEVQDPDYEECVPCEEGCLGCSLDDPGTCTSCAMGYYRFDHHCYKTCPEKTYSEEVECKACDSNCGSCDQNGCYWCEEGFFLLGGSCVRKCGPGFYGDQEMGECESCHRACETCTGPGHDECSSCQEGLQLLRGMCVHATKTQEEGKFWNDILRKLQPCHSSCKTCNGSATLCTSCPKGAYLLAQACVSSCPQGTWPSVRSGSCENCTEACAICSGADLCKKCQMQPGHPLFLHEGRCYSKCPEGSYAEDGICERCSSPCRTCEGNATNCHSCEGGHVLHHGVCQENCPERHVAVKGVCKHCPEMCQDCIHEKTCKECTPEFFLHDDMCHQSCPRGFYADSRHCVPCHKDCLECSGPKADDCELCLESSWVLYDGLCLEECPAGTYYEKETKECRDCHKSCLTCSSSGTCTTCQKGLIMNPRGSCMANEKCSPSEYWDEDAPGCKPCHVKCFHCMGPAEDQCQTCPMNSLLLNTTCVKDCPEGYYADEDSNRCAHCHSSCRTCEGRHSRQCHSCRPGWFQLGKECLLQCREGYYADNSTGRCERCNRSCKGCQGPRPTDCLSCDRFFFLLRSKGECHRSCPDHYYVEQSTQTCERCHPTCDQCKGKGALNCLSCVWSYHLMGGICTSDCLVGEYRVGEGEKFNCEKCHESCMECKGPGAKNCTLCPANLVLHMDDSHCLHCCNTSDPPSAQECCDCQDTTDECILRTSKVRPATEHFKTALFITSSMMLVLLLGAAVVVWKKSRGRVQPAAKAGYEKLADPNKSYSSYKSSYRESTSFEEDQVIEYRDRDYDEDDDDDIVYMGQDGTVYRKFKYGLLDDDDIDELEYDDESYSYYQ TTPFWHU TT Literature-reported TTLXKZR ID TTLXKZR TTLXKZR TN Prostacyclin synthase (PTGIS) TTLXKZR UP Q16647 TTLXKZR UC PTGIS_HUMAN TTLXKZR BC Intramolecular oxidoreductases TTLXKZR SN Prostaglandin I2 synthase; PTGIS TTLXKZR GN PTGIS TTLXKZR FC Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2). TTLXKZR EC EC 5.3.99.4 TTLXKZR PD 3B6H; 2IAG TTLXKZR SQ MAWAALLGLLAALLLLLLLSRRRTRRPGEPPLDLGSIPWLGYALDFGKDAASFLTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQLPHYSPSDEKARMKLTLLHRELQALTEAMYTNLHAVLLGDATEAGSGWHEMGLLDFSYSFLLRAGYLTLYGIEALPRTHESQAQDRVHSADVFHTFRQLDRLLPKLARGSLSVGDKDHMCSVKSRLWKLLSPARLARRAHRSKWLESYLLHLEEMGVSEEMQARALVLQLWATQGNMGPAAFWLLLFLLKNPEALAAVRGELESILWQAEQPVSQTTTLPQKVLDSTPVLDSVLSESLRLTAAPFITREVVVDLAMPMADGREFNLRRGDRLLLFPFLSPQRDPEIYTDPEVFKYNRFLNPDGSEKKDFYKDGKRLKNYNMPWGAGHNHCLGRSYAVNSIKQFVFLVLVHLDLELINADVEIPEFDLSRYGFGLMQPEHDVPVRYRIRP TTLXKZR TT Literature-reported TTSLUMT ID TTSLUMT TTSLUMT TN Protein kinase D (PRKD1) TTSLUMT UP Q15139 TTSLUMT UC KPCD1_HUMAN TTSLUMT BC Kinase TTSLUMT SN nPKC-mu; nPKC-D1; Serine/threonine-protein kinase D1; Protein kinase C mu type; PRKCM; PKD1; PKD TTSLUMT GN PRKD1 TTSLUMT FC Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenetic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor. Plays a role in activated KRAS-mediated stabilization of ZNF304 in colorectal cancer (CRC) cells. Regulates nuclear translocation of transcription factor TFEB in macrophages upon live S. enterica infection. Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. TTSLUMT EC EC 2.7.11.13 TTSLUMT SQ MSAPPVLRPPSPLLPVAAAAAAAAAALVPGSGPGPAPFLAPVAAPVGGISFHLQIGLSREPVLLLQDSSGDYSLAHVREMACSIVDQKFPECGFYGMYDKILLFRHDPTSENILQLVKAASDIQEGDLIEVVLSASATFEDFQIRPHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRRRRLSNVSLTGVSTIRTSSAELSTSAPDEPLLQKSPSESFIGREKRSNSQSYIGRPIHLDKILMSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLGEVTINGDLLSPGAESDVVMEEGSDDNDSERNSGLMDDMEEAMVQDAEMAMAECQNDSGEMQDPDPDHEDANRTISPSTSNNIPLMRVVQSVKHTKRKSSTVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILSLEPVKTSALIPNGANPHCFEITTANVVYYVGENVVNPSSPSPNNSVLTSGVGADVARMWEIAIQHALMPVIPKGSSVGTGTNLHRDISVSISVSNCQIQENVDISTVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQTWLDLRELECKIGERYITHESDDLRWEKYAGEQGLQYPTHLINPSASHSDTPETEETEMKALGERVSIL TTSLUMT TT Literature-reported TTSLUMT FM Kinase TTSLUMT RC R-HSA-1660661:Sphingolipid de novo biosynthesis TT7IZSA ID TT7IZSA TT7IZSA TN Protein kinase G1 (PRKG1) TT7IZSA UP Q13976 TT7IZSA UC KGP1_HUMAN TT7IZSA BC Kinase TT7IZSA SN cGMP-dependent protein kinase I; cGMP-dependent protein kinase 1; cGKI; cGK1; cGK 1; PRKGR1B; PRKGR1A; PRKG1B TT7IZSA GN PRKG1 TT7IZSA FC GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle. Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. TT7IZSA EC EC 2.7.11.12 TT7IZSA PD 6C0T; 6BG2; 6BDL; 5L0N; 5JD7 TT7IZSA SQ MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDSPSEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDSFPEDNDEPPPDDNSGWDIDF TT7IZSA TT Literature-reported TTSL41O ID TTSL41O TTSL41O TN Protein kinase N1 (PKN1) TTSL41O UP Q16512 TTSL41O UC PKN1_HUMAN TTSL41O BC Kinase TTSL41O SN Serine/threonine-protein kinase N1; Serine-threonine protein kinase N; Protein-kinase C-related kinase 1; Protein kinase PKN-alpha; Protein kinase C-like PKN; Protein kinase C-like 1; Protease-activated kinase 1; PRKCL1; PRK1; PKN; PAK1 TTSL41O GN PKN1 TTSL41O FC Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. TTSL41O EC EC 2.7.11.13 TTSL41O PD 4OTI; 4OTH; 4OTG; 4OTD; 4NKG TTSL41O SQ MASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRSLGPVELLLRGSSRRLDLLHQQLQELHAHVVLPDPAATHDGPQSPGAGGPTCSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQAGQLENQAAPDDTQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAASSAAFSTRLAGPFPATHYSTLCKPAPLTGTLEVRVVGCRDLPETIPWNPTPSMGGPGTPDSRPPFLSRPARGLYSRSGSLSGRSSLKAEAENTSEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPVIERIPRLRRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPNATGTGTFSPGASPGSEARTTGDISVEKLNLGTDSDSSPQKSSRDPPSSPSSLSSPIQESTAPELPSETQETPGPALCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLDFDFVAGGC TTSL41O TT Literature-reported TTTHO0M ID TTTHO0M TTTHO0M TN Protein kinase N2 (PKN2) TTTHO0M UP Q16513 TTTHO0M UC PKN2_HUMAN TTTHO0M BC Kinase TTTHO0M SN Serine/threonine-protein kinase N2; Protein-kinase C-related kinase 2; Protein kinase C-like 2; PRKCL2; PRK2; PKN gamma TTTHO0M GN PKN2 TTTHO0M FC Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis. PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. TTTHO0M EC EC 2.7.11.13 TTTHO0M PD 6GBE; 6CCY; 4RRV; 4CRS TTTHO0M SQ MASNPERGEILLTELQGDSRSLPFSENVSAVQKLDFSDTMVQQKLDDIKDRIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDITDCPRTPDTPNNDPRCSTSNNRLKALQKQLDIELKVKQGAENMIQMYSNGSSKDRKLHGTAQQLLQDSKTKIEVIRMQILQAVQTNELAFDNAKPVISPLELRMEELRHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNEVPKNHPKSRIIIEELSLVAASPTLSPRQSMISTQNQYSTLSKPAALTGTLEVRLMGCQDILENVPGRSKATSVALPGWSPSETRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTSWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQAPVPTTVPVVDVRIPQLAPPASDSTVTKLDFDLEPEPPPAPPRASSLGEIDESSELRVLDIPGQDSETVFDIQNDRNSILPKSQSEYKPDTPQSGLEYSGIQELEDRRSQQRFQFNLQDFRCCAVLGRGHFGKVLLAEYKNTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEGFVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGASEKDAEDVKKHPFFRLIDWSALMDKKVKPPFIPTIRGREDVSNFDDEFTSEAPILTPPREPRILSEEEQEMFRDFDYIADWC TTTHO0M TT Literature-reported TTA8GFO ID TTA8GFO TTA8GFO TN Protein tyrosine phosphatase IVA 1 (PRL-1) TTA8GFO UP Q93096 TTA8GFO UC TP4A1_HUMAN TTA8GFO BC Phosphoric monoester hydrolase TTA8GFO SN Protein-tyrosine phosphatase of regenerating liver 1; Protein-tyrosine phosphatase 4a1; Protein tyrosine phosphatase type IVA 1; PTPCAAX1; PTP(CAAXI); PRL1 TTA8GFO GN PTP4A1 TTA8GFO FC May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. TTA8GFO EC EC 3.1.3.48 TTA8GFO PD 5BX1; 1XM2; 1RXD TTA8GFO SQ MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHRNNCCIQ TTA8GFO TT Literature-reported TTA8GFO FM Phosphoric monoester hydrolases TT1MHKD ID TT1MHKD TT1MHKD TN Protein tyrosine phosphatase IVA 2 (PRL-2) TT1MHKD UP Q12974 TT1MHKD UC TP4A2_HUMAN TT1MHKD BC Phosphoric monoester hydrolase TT1MHKD SN Protein-tyrosine phosphatase of regenerating liver 2; Protein-tyrosine phosphatase 4a2; Protein tyrosine phosphatase type IVA 2; PTPCAAX2; PTP(CAAXII); PRL2; OV-1; HU-PP-1; BM-008 TT1MHKD GN PTP4A2 TT1MHKD FC Promotes tumors. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB. Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. TT1MHKD EC EC 3.1.3.48 TT1MHKD PD 5K25; 5K23; 5K22 TT1MHKD SQ MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFRDTNGHCCVQ TT1MHKD TT Literature-reported TT1MHKD FM Phosphoric monoester hydrolases TT7YM8D ID TT7YM8D TT7YM8D TN Protein tyrosine phosphatase IVA 3 (PRL-3) TT7YM8D UP O75365 TT7YM8D UC TP4A3_HUMAN TT7YM8D BC Phosphoric monoester hydrolase TT7YM8D SN Protein-tyrosine phosphatase of regenerating liver 3; Protein-tyrosine phosphatase 4a3; Protein tyrosine phosphatase type IVA 3; PRL3; PRL-3 TT7YM8D GN PTP4A3 TT7YM8D FC Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II. TT7YM8D EC EC 3.1.3.48 TT7YM8D PD 5TSR; 2MBC; 1V3A; 1R6H TT7YM8D SQ MARMNRPAPVEVSYKHMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLVKAKFCEAPGSCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHKTRCCVM TT7YM8D TT Literature-reported TT7YM8D FM Phosphoric monoester hydrolases TTWMKXP ID TTWMKXP TTWMKXP TN Protein-tyrosine phosphatase eta (HPTP) TTWMKXP UP Q12913 TTWMKXP UC PTPRJ_HUMAN TTWMKXP BC Phosphoric monoester hydrolase TTWMKXP SN Receptor-type tyrosine-protein phosphatase eta; R-PTP-eta; R-PTP-J; Protein-tyrosine phosphatase receptor type J; HPTP eta; Density-enhanced phosphatase 1; DEP1; DEP-1; CD148 TTWMKXP GN PTPRJ TTWMKXP FC Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling. Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. TTWMKXP EC EC 3.1.3.48 TTWMKXP PD 2NZ6; 2DLE; 2CFV TTWMKXP SQ MKPAAREARLPPRSPGLRWALPLLLLLLRLGQILCAGGTPSPIPDPSVATVATGENGITQISSTAESFHKQNGTGTPQVETNTSEDGESSGANDSLRTPEQGSNGTDGASQKTPSSTGPSPVFDIKAVSISPTNVILTWKSNDTAASEYKYVVKHKMENEKTITVVHQPWCNITGLRPATSYVFSITPGIGNETWGDPRVIKVITEPIPVSDLRVALTGVRKAALSWSNGNGTASCRVLLESIGSHEELTQDSRLQVNISGLKPGVQYNINPYLLQSNKTKGDPLGTEGGLDASNTERSRAGSPTAPVHDESLVGPVDPSSGQQSRDTEVLLVGLEPGTRYNATVYSQAANGTEGQPQAIEFRTNAIQVFDVTAVNISATSLTLIWKVSDNESSSNYTYKIHVAGETDSSNLNVSEPRAVIPGLRSSTFYNITVCPVLGDIEGTPGFLQVHTPPVPVSDFRVTVVSTTEIGLAWSSHDAESFQMHITQEGAGNSRVEITTNQSIIIGGLFPGTKYCFEIVPKGPNGTEGASRTVCNRTVPSAVFDIHVVYVTTTEMWLDWKSPDGASEYVYHLVIESKHGSNHTSTYDKAITLQGLIPGTLYNITISPEVDHVWGDPNSTAQYTRPSNVSNIDVSTNTTAATLSWQNFDDASPTYSYCLLIEKAGNSSNATQVVTDIGITDATVTELIPGSSYTVEIFAQVGDGIKSLEPGRKSFCTDPASMASFDCEVVPKEPALVLKWTCPPGANAGFELEVSSGAWNNATHLESCSSENGTEYRTEVTYLNFSTSYNISITTVSCGKMAAPTRNTCTTGITDPPPPDGSPNITSVSHNSVKVKFSGFEASHGPIKAYAVILTTGEAGHPSADVLKYTYEDFKKGASDTYVTYLIRTEEKGRSQSLSEVLKYEIDVGNESTTLGYYNGKLEPLGSYRACVAGFTNITFHPQNKGLIDGAESYVSFSRYSDAVSLPQDPGVICGAVFGCIFGALVIVTVGGFIFWRKKRKDAKNNEVSFSQIKPKKSKLIRVENFEAYFKKQQADSNCGFAEEYEDLKLVGISQPKYAAELAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIVRSQKDSKVDLIYQNTTAMTIYENLAPVTTFGKTNGYIA TTWMKXP TT Patented-recorded TTWMKXP FM Phosphoric monoester hydrolases TTNIR6C ID TTNIR6C TTNIR6C TN Protein-tyrosine phosphatase pez (PTPN14) TTNIR6C UP Q15678 TTNIR6C UC PTN14_HUMAN TTNIR6C BC Phosphoric monoester hydrolase TTNIR6C SN Tyrosine-protein phosphatase non-receptor type 14; PTPD2; PEZ TTNIR6C GN PTPN14 TTNIR6C FC Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor. Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial-mesenchymal transition. TTNIR6C EC EC 3.1.3.48 TTNIR6C PD 2BZL TTNIR6C SQ MPFGLKLRRTRRYNVLSKNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFFGVMFYVPNVSWLQQEATRYQYYLQVKKDVLEGRLRCTLDQVIRLAGLAVQADFGDYNQFDSQDFLREYVLFPMDLALEEAVLEELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIFPVKDNHGNCVHLGIFFMGIFVRNRIGRQAVIYRWNDMGNITHNKSTILVELINKEETALFHTDDIENAKYISRLFATRHKFYKQNKICTEQSNSPPPIRRQPTWSRSSLPRQQPYILPPVHVQCGEHYSETHTSQDSIFHGNEEALYCNSHNSLDLNYLNGTVTNGSVCSVHSVNSLNCSQSFIQASPVSSNLSIPGSDIMRADYIPSHRHSAIIVPSYRPTPDYETVMRQMKRGILHTDSQSQSLRNLNIINTHAYNQPEDLVYSQPEMRERHPYTVPYGPQGVYSNKLVSPSDQRNPKNNVVPSKPGASAISHTVSTPELANMQLQGSHNYSTAHMLKNYLFRPPPPYPRPRPATSTPDLASHRHKYVSGSSPDLVTRKVQLSVKTFQEDSSPVVHQSLQEVSEPLTATKHHGTVNKRHSLEVMNSMVRGMEAMTLKSLHLPMARRNTLREQGPPEEGSGSHEVPQLPQYHHKKTFSDATMLIHSSESEEEEEEAPESVPQIPMLREKMEYSAQLQAALARIPNKPPPEYPGPRKSVSNGALRQDQASLPPAMARARVLRHGPAKAISMSRTDPPAVNGASLGPSISEPDLTSVKERVKKEPVKERPVSEMFSLEDSIIEREMMIRNLEKQKMAGLEAQKRPLMLAALNGLSVARVSGREENRVDATRVPMDERFRTLKKKLEEGMVFTEYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMLEGTKNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFLQNSRLI TTNIR6C TT Literature-reported TTNIR6C FM Phosphoric monoester hydrolases TTFEUYR ID TTFEUYR TTFEUYR TN Proto-oncogene c-Crk (c-Crk) TTFEUYR UP P46108 TTFEUYR UC CRK_HUMAN TTFEUYR SN P38; Adapter molecule crk TTFEUYR GN CRK TTFEUYR FC Mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling. Isoform Crk-II: Regulates cell adhesion, spreading and migration. TTFEUYR PD 6ATV; 5UL6; 2MS4; 2EYZ; 2EYY TTFEUYR SQ MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVSRSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS TTFEUYR TT Literature-reported TTFEUYR FM Transmembrane protein TTFEUYR KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04015:Rap1 signaling pathway; hsa04062:Chemokine signaling pathway; hsa04510:Focal adhesion; hsa04666:Fc gamma R-mediated phagocytosis; hsa04722:Neurotrophin signaling pathway; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa05100:Bacterial invasion of epithelial cells; hsa05131:Shigellosis; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma; hsa05220:Chronic myeloid leukemia TTFEUYR RC R-HSA-170984:ARMS-mediated activation; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-372708:p130Cas linkage to MAPK signaling for integrins; R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-912631:Regulation of signaling by CBL TTRA9G0 ID TTRA9G0 TTRA9G0 TN Proto-oncogene c-Fer (FER) TTRA9G0 UP P16591 TTRA9G0 UC FER_HUMAN TTRA9G0 BC Kinase TTRA9G0 SN p94-Fer; Tyrosine-protein kinase Fer; Tyrosine kinase 3; TYK3; Fujinami poultry sarcoma/Feline sarcoma-related protein Fer; Feline encephalitis virus-related kinase FER TTRA9G0 GN FER TTRA9G0 FC Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission. Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this depends on cell type and stimulus. Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. TTRA9G0 EC EC 2.7.10.2 TTRA9G0 PD 2KK6 TTRA9G0 SQ MGFGSDLKNSHEAVLKLQDWELRLLETVKKFMALRIKSDKEYASTLQNLCNQVDKESTVQMNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYIGVHQQIEAEMIKVTKTELEKLKCSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQNQYYDITLPLLLDSLQKMQEEMIKALKGIFDEYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTAESLQVMLKTLAEELMQTQQMLLNKEEAVLELEKRIEESSETCEKKSDIVLLLSQKQALEELKQSVQQLRCTEAKFSAQKELLEQKVQENDGKEPPPVVNYEEDARSVTSMERKERLSKFESIRHSIAGIIRSPKSALGSSALSDMISISEKPLAEQDWYHGAIPRIEAQELLKKQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQYVDNMYRFEGTGFSNIPQLIDHHYTTKQVITKKSGVVLLNPIPKDKKWILSHEDVILGELLGKGNFGEVYKGTLKDKTSVAVKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVSGGDFLTFLRRKKDELKLKQLVKFSLDAAAGMLYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQHCPEDISKIMMKCWDYKPENRPKFSELQKELTIIKRKLT TTRA9G0 TT Literature-reported TTLBY21 ID TTLBY21 TTLBY21 TN Proto-oncogene c-Fes (FES) TTLBY21 UP P07332 TTLBY21 UC FES_HUMAN TTLBY21 BC Kinase TTLBY21 SN p93c-fes; Tyrosine-protein kinase Fes/Fps; Proto-oncogene c-Fps; Feline sarcoma/Fujinami avian sarcoma oncogene homolog; FPS TTLBY21 GN FES TTLBY21 FC Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28. Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. TTLBY21 EC EC 2.7.10.2 TTLBY21 PD 4DYL; 4.00E+93; 3CD3; 3CBL; 3BKB TTLBY21 SQ MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVATEMVFRRQEMVTQLQQELRNEEENTHPRERVQLLGKRQVLQEALQGLQVALCSQAKLQAQQELLQTKLEHLGPGEPPPVLLLQDDRHSTSSSEQEREGGRTPTLEILKSHISGIFRPKFSLPPPLQLIPEVQKPLHEQLWYHGAIPRAEVAELLVHSGDFLVRESQGKQEYVLSVLWDGLPRHFIIQSLDNLYRLEGEGFPSIPLLIDHLLSTQQPLTKKSGVVLHRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGVYAASGGLRQVPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGASPYPNLSNQQTREFVEKGGRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTIYQELQSIRKRHR TTLBY21 TT Literature-reported TT1HEMJ ID TT1HEMJ TT1HEMJ TN Pseudomonas Arginine deiminase (Pseudo arcA) TT1HEMJ UP P13981 TT1HEMJ UC ARCA_PSEAE TT1HEMJ BC Carbon-nitrogen hydrolase TT1HEMJ SN Arginine dihydrolase; Arginine deiminase; ADI; AD TT1HEMJ GN Pseudo arcA TT1HEMJ FC Catalyzes the irreversible hydrolysis of arginine to citrulline and ammonia. Involved in the first step of the most widespread anaerobic route of arginine degradation TT1HEMJ EC EC 3.5.3.6 TT1HEMJ PD 2ACI; 2ABR; 2AAF; 2A9G; 1RXX TT1HEMJ SQ MSTEKTKLGVHSEAGKLRKVMVCSPGLAHQRLTPSNCDELLFDDVIWVNQAKRDHFDFVTKMRERGIDVLEMHNLLTETIQNPEALKWILDRKITADSVGLGLTSELRSWLESLEPRKLAEYLIGGVAADDLPASEGANILKMYREYLGHSSFLLPPLPNTQFTRDTTCWIYGGVTLNPMYWPARRQETLLTTAIYKFHPEFANAEFEIWYGDPDKDHGSSTLEGGDVMPIGNGVVLIGMGERSSRQAIGQVAQSLFAKGAAERVIVAGLPKSRAAMHLDTVFSFCDRDLVTVFPEVVKEIVPFSLRPDPSSPYGMNIRREEKTFLEVVAESLGLKKLRVVETGGNSFAAEREQWDDGNNVVCLEPGVVVGYDRNTYTNTLLRKAGVEVITISASELGRGRGGGHCMTCPIVRDPIDY TT1HEMJ TT Literature-reported TT1UY5C ID TT1UY5C TT1UY5C TN Pseudomonas Methionine gamma-lyase (Pseudo mdeA) TT1UY5C UP P13254 TT1UY5C UC MEGL_PSEPU TT1UY5C BC Carbon-sulfur lyases TT1UY5C SN Pseudo MGL; L-methionine gamma-lyase; L-methioninase; Homocysteine desulfhydrase TT1UY5C GN Pseudo mdeA TT1UY5C FC Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia. Is involved in L-methionine catabolism. In fact, shows a multicatalytic function since it also catalyzes gamma-replacement of L-methionine with thiol compounds, alpha,gamma-elimination and gamma-replacement reactions of L-homocysteine and its S-substituted derivatives, O-substituted-L-homoserines and DL-selenomethionine, and, to a lesser extent, alpha,beta-elimination and beta-replacement reactions of L-cysteine, S-methyl-L-cysteine, and O-acetyl-L-serine. Also catalyzes deamination and gamma-addition reactions of L-vinylglycine. Thus, the enzyme is able to cleave C-S, C-Se, and C-O bonds of sulfur, selenium, and oxygen amino acids, respectively. TT1UY5C EC EC 4.4.1.11 TT1UY5C PD 5X30; 5X2Z; 5X2Y; 5X2X; 5X2W TT1UY5C SQ MHGSNKLPGFATRAIHHGYDPQDHGGALVPPVYQTATFTFPTVEYGAACFAGEQAGHFYSRISNPTLNLLEARMASLEGGEAGLALASGMGAITSTLWTLLRPGDEVLLGNTLYGCTFAFLHHGIGEFGVKLRHVDMADLQALEAAMTPATRVIYFESPANPNMHMADIAGVAKIARKHGATVVVDNTYCTPYLQRPLELGADLVVHSATKYLSGHGDITAGIVVGSQALVDRIRLQGLKDMTGAVLSPHDAALLMRGIKTLNLRMDRHCANAQVLAEFLARQPQVELIHYPGLASFPQYTLARQQMSQPGGMIAFELKGGIGAGRRFMNALQLFSRAVSLGDAESLAQHPASMTHSSYTPEERAHYGISEGLVRLSVGLEDIDDLLADVQQALKASA TT1UY5C TT Literature-reported TTDRIAZ ID TTDRIAZ TTDRIAZ TN Pseudomonas Omega-amino acid:pyruvate aminotransferase (Pseudo Omega-APT) TTDRIAZ UP P28269 TTDRIAZ UC OAPT_PSEPU TTDRIAZ BC Transaminase TTDRIAZ SN Omega-APT; Beta-alanine--pyruvate aminotransferase TTDRIAZ GN Pseudo Omega-APT TTDRIAZ FC Catalyzes transamination between a variety of omega- amino acids, mono and diamines, and pyruvate. Plays a pivotal role in the metabolism of the omega amino acids. TTDRIAZ EC EC 2.6.1.18 TTDRIAZ PD 3A8U TTDRIAZ SQ NMPEHAGASLASQLKLDAHWMPYTANRNFLRDPRLIVAAEGSWLVDDKGRKVYDSLSGLWTCGAGHTRKEIQEAVAKQLSTLDYSPGFQYGHPLSFQLAEKITDLTPGNLNHVFFTDSGSECALTAVKMVRAYWRLKGQATKTKMIGRARGYHGVNIAGTSLGGVNGNRKLFGQPMQDVDHLPHTLLASNAYSRGMPKEGGIALADELLKLIELHDASNIAAVFVEPLAGSAGVLVPPEGYLKRNREICNQHNILLVFDEVITGFGRTGSMFGADSFGVTPDLMCIAKQVTNGAIPMGAVIASTEIYQTFMNQPTPEYAVEFPHGYTYSAHPVACAAGLAALCLLQKENLVQSVAEVAPHFEKALHGIKGAKNVIDIRNFGLAGAIQIAPRDGDAIVRPFEAGMALWKAGFYVRFGGDTLQFGPTFNSKPQDLDRLFDAVGEVLNKLLD TTDRIAZ TT Literature-reported TTXJ3W7 ID TTXJ3W7 TTXJ3W7 TN PTEN messenger RNA (PTEN mRNA) TTXJ3W7 UP P60484 TTXJ3W7 UC PTEN_HUMAN TTXJ3W7 BC mRNA target TTXJ3W7 SN TEP1 (mRNA); Phosphatidylinositol 3,4,5trisphosphate 3phosphatase and dualspecificity protein phosphatase PTEN (mRNA); Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (mRNA); Mutated in multiple advanced cancers 1 (mRNA); MMAC1 (mRNA) TTXJ3W7 GN PTEN TTXJ3W7 FC Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement. Tumor suppressor. TTXJ3W7 EC EC 3.1.3.16 TTXJ3W7 PD 5BZZ; 5BZX; 5BUG; 4O1V; 2KYL TTXJ3W7 SQ MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV TTXJ3W7 TT Literature-reported TTXJ3W7 FM mRNA target TT9UYG4 ID TT9UYG4 TT9UYG4 TN Pyridoxal phosphate phosphatase (PDXP) TT9UYG4 UP Q96GD0 TT9UYG4 UC PLPP_HUMAN TT9UYG4 BC Phosphoric monoester hydrolase TT9UYG4 SN PLPP; PLP phosphatase; PDXP TT9UYG4 GN PDXP TT9UYG4 FC Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho- tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP. TT9UYG4 EC EC 3.1.3.3 TT9UYG4 PD 5GYN; 2P69; 2P27; 2OYC; 2CFT TT9UYG4 SQ MARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADLTEGLED TT9UYG4 TT Literature-reported TTDEQIP ID TTDEQIP TTDEQIP TN Pyruvate dehydrogenase kinase 3 (PDHK3) TTDEQIP UP Q15120 TTDEQIP UC PDK3_HUMAN TTDEQIP BC Kinase TTDEQIP SN Pyruvate dehydrogenase kinase isoform 3; PDK3 TTDEQIP GN PDK3 TTDEQIP FC Inhibits pyruvatedehydrogenase activity by phosphorylation of the E1 subunit PDHA1, and thereby regulates glucose metabolism and aerobic respiration. Can also phosphorylate PDHA2. Decreases glucose utilization and increases fat metabolism in response to prolonged fasting, and as adaptation to a high-fat diet. Plays a role in glucose homeostasis and in maintaining normal blood glucose levels in function of nutrient levels and under starvation. Plays a role in the generation of reactive oxygen species. TTDEQIP EC EC 2.7.11.2 TTDEQIP PD 2Q8I; 2PNR; 1Y8P; 1Y8O; 1Y8N TTDEQIP SQ MRLFRWLLKQPVPKQIERYSRFSPSPLSIKQFLDFGRDNACEKTSYMFLRKELPVRLANTMREVNLLPDNLLNRPSVGLVQSWYMQSFLELLEYENKSPEDPQVLDNFLQVLIKVRNRHNDVVPTMAQGVIEYKEKFGFDPFISTNIQYFLDRFYTNRISFRMLINQHTLLFGGDTNPVHPKHIGSIDPTCNVADVVKDAYETAKMLCEQYYLVAPELEVEEFNAKAPDKPIQVVYVPSHLFHMLFELFKNSMRATVELYEDRKEGYPAVKTLVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRPSLEPTRAAPLAGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVIYLKALSSESFERLPVFNKSAWRHYKTTPEADDWSNPSSEPRDASKYKAKQ TTDEQIP TT Literature-reported TTP6UO8 ID TTP6UO8 TTP6UO8 TN Quinone oxidoreductase (CRYZ) TTP6UO8 UP Q08257 TTP6UO8 UC QOR_HUMAN TTP6UO8 SN Zeta-crystallin; NADPH:quinone reductase; CRYZ TTP6UO8 GN CRYZ TTP6UO8 FC Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding. TTP6UO8 EC EC 1.6.5.5 TTP6UO8 PD 1YB5 TTP6UO8 SQ MATGQKLMRAVRVFEFGGPEVLKLRSDIAVPIPKDHQVLIKVHACGVNPVETYIRSGTYSRKPLLPYTPGSDVAGVIEAVGDNASAFKKGDRVFTSSTISGGYAEYALAADHTVYKLPEKLDFKQGAAIGIPYFTAYRALIHSACVKAGESVLVHGASGGVGLAACQIARAYGLKILGTAGTEEGQKIVLQNGAHEVFNHREVNYIDKIKKYVGEKGIDIIIEMLANVNLSKDLSLLSHGGRVIVVGSRGTIEINPRDTMAKESSIIGVTLFSSTKEEFQQYAAALQAGMEIGWLKPVIGSQYPLEKVAEAHENIIHGSGATGKMILLL TTP6UO8 TT Literature-reported TT3K9S2 ID TT3K9S2 TT3K9S2 TN RANK messenger RNA (RANK mRNA) TT3K9S2 UP Q9Y6Q6 TT3K9S2 UC TNR11_HUMAN TT3K9S2 BC mRNA target TT3K9S2 SN Tumor necrosis factor receptor superfamily member 11A (mRNA); Receptor activator of NF-KB (mRNA); RANK (mRNA); Osteoclast differentiation factor receptor (mRNA); ODFR (mRNA); CD265 (mRNA) TT3K9S2 GN TNFRSF11A TT3K9S2 FC Involved in the regulation of interactions between T-cells and dendritic cells. Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis. TT3K9S2 PD 1LB5 TT3K9S2 SQ MAPRARRRRPLFALLLLCALLARLQVALQIAPPCTSEKHYEHLGRCCNKCEPGKYMSSKCTTTSDSVCLPCGPDEYLDSWNEEDKCLLHKVCDTGKALVAVVAGNSTTPRRCACTAGYHWSQDCECCRRNTECAPGLGAQHPLQLNKDTVCKPCLAGYFSDAFSSTDKCRPWTNCTFLGKRVEHHGTEKSDAVCSSSLPARKPPNEPHVYLPGLIILLLFASVALVAAIIFGVCYRKKGKALTANLWHWINEACGRLSGDKESSGDSCVSTHTANFGQQGACEGVLLLTLEEKTFPEDMCYPDQGGVCQGTCVGGGPYAQGEDARMLSLVSKTEIEEDSFRQMPTEDEYMDRPSQPTDQLLFLTEPGSKSTPPFSEPLEVGENDSLSQCFTGTQSTVGSESCNCTEPLCRTDWTPMSSENYLQKEVDSGHCPHWAASPSPNWADVCTGCRNPPGEDCEPLVGSPKRGPLPQCAYGMGLPPEEEASRTEARDQPEDGADGRLPSSARAGAGSGSSPGGQSPASGNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGAAAAAEPMGRPVQEETLARRDSFAGNGPRFPDPCGGPEGLREPEKASRPVQEQGGAKA TT3K9S2 TT Literature-reported TT3K9S2 FM mRNA target TT3K9S2 KE hsa04060:Cytokine-cytokine receptor interaction; hsa04064:NF-kappa B signaling pathway; hsa04380:Osteoclast differentiation; hsa04917:Prolactin signaling pathway; hsa05323:Rheumatoid arthritis TT3K9S2 RC R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway TTJ10AL ID TTJ10AL TTJ10AL TN Receptor of activated protein C kinase 1 (RACK1) TTJ10AL UP P63244 TTJ10AL UC RACK1_HUMAN TTJ10AL BC WD repeat G protein beta family. Ribosomal protein RACK1 subfamily TTJ10AL SN Small ribosomal subunit protein RACK1; Receptor of activated protein C kinase 1, N-terminally processed; Receptor for activated C kinase; Human lung cancer oncogene 7 protein; HLC-7; Guanine nucleotide-binding protein subunit beta-like protein 12.3; Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed; Guanine nucleotide-binding protein subunit beta-2-like 1; GNB2L1; Cell proliferation-inducing gene 21 protein TTJ10AL GN RACK1 TTJ10AL FC Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158). TTJ10AL PD 6QZP; 6G5I; 6G5H; 6G53; 6G51 TTJ10AL SQ MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR TTJ10AL TT Literature-reported TTJ10AL KE hsa05162:Measles TT4SEA8 ID TT4SEA8 TT4SEA8 TN Receptor-type protein-tyrosine phosphatase zeta (PTPRZ1) TT4SEA8 UP P23471 TT4SEA8 UC PTPRZ_HUMAN TT4SEA8 BC Phosphoric monoester hydrolase TT4SEA8 SN Receptor protein tyrosine phosphatase zeta; R-PTP-zeta; PTPRZ1 TT4SEA8 GN PTPRZ1 TT4SEA8 FC Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades. TT4SEA8 EC EC 3.1.3.48 TT4SEA8 PD 5H08; 5AWX; 3S97; 3JXF TT4SEA8 SQ MRILKRFLACIQLLCVCRLDWANGYYRQQRKLVEEIGWSYTGALNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNTGKTVEINLTNDYRVSGGVSEMVFKASKITFHWGKCNMSSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMDYLQNNFREQQYKFSRQVFSSYTGKEEIHEAVCSSEPENVQADPENYTSLLVTWERPRVVYDTMIEKFAVLYQQLDGEDQTKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAICTNGLYGKYSDQLIVDMPTDNPELDLFPELIGTEEIIKEEEEGKDIEEGAIVNPGRDSATNQIRKKEPQISTTTHYNRIGTKYNEAKTNRSPTRGSEFSGKGDVPNTSLNSTSQPVTKLATEKDISLTSQTVTELPPHTVEGTSASLNDGSKTVLRSPHMNLSGTAESLNTVSITEYEEESLLTSFKLDTGAEDSSGSSPATSAIPFISENISQGYIFSSENPETITYDVLIPESARNASEDSTSSGSEESLKDPSMEGNVWFPSSTDITAQPDVGSGRESFLQTNYTEIRVDESEKTTKSFSAGPVMSQGPSVTDLEMPHYSTFAYFPTEVTPHAFTPSSRQQDLVSTVNVVYSQTTQPVYNGETPLQPSYSSEVFPLVTPLLLDNQILNTTPAASSSDSALHATPVFPSVDVSFESILSSYDGAPLLPFSSASFSSELFRHLHTVSQILPQVTSATESDKVPLHASLPVAGGDLLLEPSLAQYSDVLSTTHAASETLEFGSESGVLYKTLMFSQVEPPSSDAMMHARSSGPEPSYALSDNEGSQHIFTVSYSSAIPVHDSVGVTYQGSLFSGPSHIPIPKSSLITPTASLLQPTHALSGDGEWSGASSDSEFLLPDTDGLTALNISSPVSVAEFTYTTSVFGDDNKALSKSEIIYGNETELQIPSFNEMVYPSESTVMPNMYDNVNKLNASLQETSVSISSTKGMFPGSLAHTTTKVFDHEISQVPENNFSVQPTHTVSQASGDTSLKPVLSANSEPASSDPASSEMLSPSTQLLFYETSASFSTEVLLQPSFQASDVDTLLKTVLPAVPSDPILVETPKVDKISSTMLHLIVSNSASSENMLHSTSVPVFDVSPTSHMHSASLQGLTISYASEKYEPVLLKSESSHQVVPSLYSNDELFQTANLEINQAHPPKGRHVFATPVLSIDEPLNTLINKLIHSDEILTSTKSSVTGKVFAGIPTVASDTFVSTDHSVPIGNGHVAITAVSPHRDGSVTSTKLLFPSKATSELSHSAKSDAGLVGGGEDGDTDDDGDDDDDDRGSDGLSIHKCMSCSSYRESQEKVMNDSDTHENSLMDQNNPISYSLSENSEEDNRVTSVSSDSQTGMDRSPGKSPSANGLSQKHNDGKEENDIQTGSALLPLSPESKAWAVLTSDEESGSGQGTSDSLNENETSTDFSFADTNEKDADGILAAGDSEITPGFPQSPTSSVTSENSEVFHVSEAEASNSSHESRIGLAEGLESEKKAVIPLVIVSALTFICLVVLVGILIYWRKCFQTAHFYLEDSTSPRVISTPPTPIFPISDDVGAIPIKHFPKHVADLHASSGFTEEFETLKEFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEVLDSHIHAYVNALLIPGPAGKTKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILSLVSTRQEENPSTSLDSNGAALPDGNIAESLESLV TT4SEA8 TT Literature-reported TTDQTEY ID TTDQTEY TTDQTEY TN Recoverin (RCVRN) TTDQTEY UP P35243 TTDQTEY UC RECO_HUMAN TTDQTEY BC Recoverin family TTDQTEY SN RCVRN; Cancer associated retinopathy protein; CAR protein TTDQTEY GN RCVRN TTDQTEY FC Seems to be implicated in the pathway from retinal rod guanylatecyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse. TTDQTEY PD 2D8N TTDQTEY SQ MGNSKSGALSKEILEELQLNTKFSEEELCSWYQSFLKDCPTGRITQQQFQSIYAKFFPDTDPKAYAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMITPEDVKLLPDDENTPEKRAEKIWKYFGKNDDDKLTEKEFIEGTLANKEILRLIQFEPQKVKEKMKNA TTDQTEY TT Literature-reported TTDQTEY KE hsa04744:Phototransduction TTDQTEY RC R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade TTUZX6V ID TTUZX6V TTUZX6V TN Renal carcinoma antigen NY-REN-54 (UBE3A) TTUZX6V UP Q05086 TTUZX6V UC UBE3A_HUMAN TTUZX6V BC Acyltransferase TTUZX6V SN Ubiquitin-protein ligase E3A; Oncogenic protein-associated protein E6-AP; Human papillomavirus E6-associated protein; HPVE6A; HECT-type ubiquitin transferase E3A; EPVE6AP; E6AP ubiquitin-protein ligase; E6AP TTUZX6V GN UBE3A TTUZX6V FC Several substrates have been identified including the ARNTL/BMAL1, ARC, RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B. Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo. Plays an important role in the regulation of the circadian clock: involved in the ubiquitination of the core clock component ARNTL/BMAL1, leading to its proteasomal degradation. Acts as transcriptional coactivator of progesterone receptor PGR upon progesterone hormone activation. Acts as a regulator of synaptic development by mediating ubiquitination and degradation of ARC. Synergizes with WBP2 in enhancing PGR activity. E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. TTUZX6V EC EC 2.3.2.26 TTUZX6V PD 4XR8; 4GIZ; 2KR1; 1EQX; 1D5F TTUZX6V SQ MEKLHQCYWKSGEPQSDDIEASRMKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGAPNNSCSEIKMNKKGARIDFKDVTYLTEEKVYEILELCREREDYSPLIRVIGRVFSSAEALVQSFRKVKQHTKEELKSLQAKDEDKDEDEKEKAACSAAAMEEDSEASSSRIGDSSQGDNNLQKLGPDDVSVDIDAIRRVYTRLLSNEKIETAFLNALVYLSPNVECDLTYHNVYSRDPNYLNLFIIVMENRNLHSPEYLEMALPLFCKAMSKLPLAAQGKLIRLWSKYNADQIRRMMETFQQLITYKVISNEFNSRNLVNDDDAIVAASKCLKMVYYANVVGGEVDTNHNEEDDEEPIPESSELTLQELLGEERRNKKGPRVDPLETELGVKTLDCRKPLIPFEEFINEPLNEVLEMDKDYTFFKVETENKFSFMTCPFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGML TTUZX6V TT Literature-reported TTUZX6V FM Carbon-nitrogen ligase TT7V0K4 ID TT7V0K4 TT7V0K4 TN Ribonuclease L (RNASEL) TT7V0K4 UP Q05823 TT7V0K4 UC RN5A_HUMAN TT7V0K4 BC Endoribonucleases TT7V0K4 SN Ribonuclease 4; RNase L; RNS4; 25Adependent ribonuclease; 25Adependent RNase; 2-5A-dependent ribonuclease; 2-5A-dependent RNase TT7V0K4 GN RNASEL TT7V0K4 FC In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis. Might play a central role in the regulation of mRNA turnover. Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length. Endoribonuclease that functions in the interferon (IFN) antiviral response. TT7V0K4 EC EC 3.1.26.- TT7V0K4 PD 4OAV; 4OAU; 4G8L; 4G8K; 1WDY TT7V0K4 SQ MESRDHNNPQEGPTSSSGRRAAVEDNHLLIKAVQNEDVDLVQQLLEGGANVNFQEEEGGWTPLHNAVQMSREDIVELLLRHGADPVLRKKNGATPFILAAIAGSVKLLKLFLSKGADVNECDFYGFTAFMEAAVYGKVKALKFLYKRGANVNLRRKTKEDQERLRKGGATALMDAAEKGHVEVLKILLDEMGADVNACDNMGRNALIHALLSSDDSDVEAITHLLLDHGADVNVRGERGKTPLILAVEKKHLGLVQRLLEQEHIEINDTDSDGKTALLLAVELKLKKIAELLCKRGASTDCGDLVMTARRNYDHSLVKVLLSHGAKEDFHPPAEDWKPQSSHWGAALKDLHRIYRPMIGKLKFFIDEKYKIADTSEGGIYLGFYEKQEVAVKTFCEGSPRAQREVSCLQSSRENSHLVTFYGSESHRGHLFVCVTLCEQTLEACLDVHRGEDVENEEDEFARNVLSSIFKAVQELHLSCGYTHQDLQPQNILIDSKKAAHLADFDKSIKWAGDPQEVKRDLEDLGRLVLYVVKKGSISFEDLKAQSNEEVVQLSPDEETKDLIHRLFHPGEHVRDCLSDLLGHPFFWTWESRYRTLRNVGNESDIKTRKSESEILRLLQPGPSEHSKSFDKWTTKINECVMKKMNKFYEKRGNFYQNTVGDLLKFIRNLGEHIDEEKHKKMKLKIGDPSLYFQKTFPDLVIYVYTKLQNTEYRKHFPQTHSPNKPQCDGAGGASGLASPGC TT7V0K4 TT Literature-reported TT7V0K4 FM Endoribonucleases TTYXEPL ID TTYXEPL TTYXEPL TN Ribosomal protein S6 kinase alpha-5 (RSK5) TTYXEPL UP O75582 TTYXEPL UC KS6A5_HUMAN TTYXEPL BC Kinase TTYXEPL SN S6K-alpha-5; RSKL; RSK-like protein kinase; Nuclear mitogen- and stress-activated protein kinase 1; MSK1; 90 kDa ribosomal protein S6 kinase 5 TTYXEPL GN RPS6KA5 TTYXEPL FC Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury. Phosphorylates TRIM7 at 'Ser-107' in response to growth factor signaling via the MEK/ERK pathway, thereby stimulating its ubiquitin ligase activity. Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. TTYXEPL EC EC 2.7.11.1 TTYXEPL PD 3KN6; 3KN5; 1VZO TTYXEPL SQ MEEEGGSSGGAAGTSADGGDGGEQLLTVKHELRTANLTGHAEKVGIENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAALPQSSEKLFQGYSFVAPSILFKRNAAVIDPLQFHMGVERPGVTNVARSAMMKDSPFYQHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDENDNLEIKIIDFGFARLKPPDNQPLKTPCFTLHYAAPELLNQNGYDESCDLWSLGVILYTMLSGQVPFQSHDRSLTCTSAVEIMKKIKKGDFSFEGEAWKNVSQEAKDLIQGLLTVDPNKRLKMSGLRYNEWLQDGSQLSSNPLMTPDILGSSGAAVHTCVKATFHAFNKYKREGFCLQNVDKAPLAKRRKMKKTSTSTETRSSSSESSHSSSSHSHGKTTPTKTLQPSNPADSNNPETLFQFSDSVA TTYXEPL TT Patented-recorded TTEWDK1 ID TTEWDK1 TTEWDK1 TN RING finger protein RIFF (RNF34) TTEWDK1 UP Q969K3 TTEWDK1 UC RNF34_HUMAN TTEWDK1 BC Carbon-nitrogen ligase TTEWDK1 SN hRFI; RNF34; RING finger protein 34; Human RING finger homologous to inhibitor of apoptosis protein; FYVERING finger protein Momo; E3 ubiquitinprotein ligase RNF34; Caspases8 and 10associated RING finger protein 1; Caspase regulator CARP1; CARP1 TTEWDK1 GN RNF34 TTEWDK1 FC E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis (PubMed:15069192). May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation (PubMed:17121812). Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN (PubMed:18382127). Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells (PubMed:22064484). Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1and its subsequent proteasomal degradation (PubMed:25012219). TTEWDK1 EC EC 2.3.2.27 TTEWDK1 SQ MKAGATSMWASCCGLLNEVMGTGAVRGQQSAFAGATGPFRFTPNPEFSTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLILRNIPIDTCREKEDLVDLVLCHHGLGSEDDMDTSSLNSSRSQTSSFFTRSFFSNYTAPSATMSSFQGELMDGDQTSRSGVPAQVQSEITSANTEDDDDDDDEDDDDEEENAEDRNPGLSKERVRASLSDLSSLDDVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERLQLQDEEDDSLCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAVHVFKS TTEWDK1 TT Literature-reported TTEWDK1 RC R-HSA-983168:Antigen processing: Ubiquitination & Proteasome degradation TTRFQTB ID TTRFQTB TTRFQTB TN Rotamase F (PPIF) TTRFQTB UP P30405 TTRFQTB UC PPIF_HUMAN TTRFQTB BC Cis-trans-isomerase TTRFQTB SN Peptidylprolyl cistrans isomerase F, mitochondrial; Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIase F; Mitochondrial cyclophilin; Cyclophilin F; CyPM; CyP-M; CyP-D; CYP3 TTRFQTB GN PPIF TTRFQTB FC Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis. PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. TTRFQTB EC EC 5.2.1.8 TTRFQTB PD 5NWO; 5CCS; 5CCR; 5CCQ; 5CCN TTRFQTB SQ MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCGQLS TTRFQTB TT Literature-reported TTRFQTB FM Cis-trans-isomerases TTPR5SX ID TTPR5SX TTPR5SX TN S100 calcium-binding protein A4 (S100A4) TTPR5SX UP P26447 TTPR5SX UC S10A4_HUMAN TTPR5SX BC S100 calcium-binding protein TTPR5SX SN Protein S100-A4; Protein Mts1; Placental calcium-binding protein; Metastasin; MTS1; Calvasculin; CAPL TTPR5SX GN S100A4 TTPR5SX FC collagen-containing extracellular matrix, extracellular exosome, extracellular region, extracellular space, nucleus, perinuclear region of cytoplasm, calcium ion binding, identical protein binding, RAGE receptor binding, RNA binding TTPR5SX PD 5LPU; 4HSZ; 4ETO; 4CFR; 4CFQ TTPR5SX SQ MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK TTPR5SX TT Literature-reported TTW9HY5 ID TTW9HY5 TTW9HY5 TN Sentrin specific protease-1 (SENP1) TTW9HY5 UP Q9P0U3 TTW9HY5 UC SENP1_HUMAN TTW9HY5 BC Peptidase TTW9HY5 SN Sentrin/SUMO-specific protease SENP1; Sentrin-specific protease 1 TTW9HY5 GN SENP1 TTW9HY5 FC The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity. Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity. Deconjugates SUMO2 from MTA1. Deconjugates SUMO1 from METTL3. Desumoylates CCAR2 which decreases its interaction with SIRT1. Deconjugates SUMO1 from GPS2. Protease that catalyzes two essential functions in the SUMO pathway. TTW9HY5 EC EC 3.4.22.- TTW9HY5 PD 6NNQ; 2XRE; 2XPH; 2IYD; 2IYC TTW9HY5 SQ MDDIADRMRMDAGEVTLVNHNSVFKTHLLPQTGFPEDQLSLSDQQILSSRQGHLDRSFTCSTRSAAYNPSYYSDNPSSDSFLGSGDLRTFGQSANGQWRNSTPSSSSSLQKSRNSRSLYLETRKTSSGLSNSFAGKSNHHCHVSAYEKSFPIKPVPSPSWSGSCRRSLLSPKKTQRRHVSTAEETVQEEEREIYRQLLQMVTGKQFTIAKPTTHFPLHLSRCLSSSKNTLKDSLFKNGNSCASQIIGSDTSSSGSASILTNQEQLSHSVYSLSSYTPDVAFGSKDSGTLHHPHHHHSVPHQPDNLAASNTQSEGSDSVILLKVKDSQTPTPSSTFFQAELWIKELTSVYDSRARERLRQIEEQKALALQLQNQRLQEREHSVHDSVELHLRVPLEKEIPVTVVQETQKKGHKLTDSEDEFPEITEEMEKEIKNVFRNGNQDEVLSEAFRLTITRKDIQTLNHLNWLNDEIINFYMNMLMERSKEKGLPSVHAFNTFFFTKLKTAGYQAVKRWTKKVDVFSVDILLVPIHLGVHWCLAVVDFRKKNITYYDSMGGINNEACRILLQYLKQESIDKKRKEFDTNGWQLFSKKSQEIPQQMNGSDCGMFACKYADCITKDRPINFTQQHMPYFRKRMVWEILHRKLL TTW9HY5 TT Literature-reported TTW9HY5 FM Peptidase TTOT2RY ID TTOT2RY TTOT2RY TN Sequestosome-1 p62 (SQSTM1) TTOT2RY UP Q13501 TTOT2RY UC SQSTM_HUMAN TTOT2RY BC Zinc-finger TTOT2RY SN Ubiquitin-binding protein p62; Sequestosome-1; Phosphotyrosine-independent ligand for the Lck SH2 domain of 62kDa; Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa; OSIL; ORCA; EBIAP; EBI3-associated protein of 60 kDa TTOT2RY GN SQSTM1 TTOT2RY FC Functions as a bridge between polyubiquitinated cargo and autophagosomes. Interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. Along with WDFY3, involved in the formation and autophagic degradation of cytoplasmic ubiquitin-containing inclusions (p62 bodies, ALIS/aggresome-like induced structures). Along with WDFY3, required to recruit ubiquitinated proteins to PML bodies in the nucleus. May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD. May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport. Promotes relocalization of 'Lys-63'-linked ubiquitinated TMEM173/STING to autophagosomes. Autophagy receptor required for selective macroautophagy (aggrephagy). TTOT2RY PD 6MJ7; 5YPH; 5YPG; 5YPF; 5YPE TTOT2RY SQ MASLTVKAYLLGKEDAAREIRRFSFCCSPEPEAEAEAAAGPGPCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVKDDIFRIYIKEKKECRRDHRPPCAQEAPRNMVHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHRGHTKLAFPSPFGHLSEGFSHSRWLRKVKHGHFGWPGWEMGPPGNWSPRPPRAGEARPGPTAESASGPSEDPSVNFLKNVGESVAAALSPLGIEVDIDVEHGGKRSRLTPVSPESSSTEEKSSSQPSSCCSDPSKPGGNVEGATQSLAEQMRKIALESEGRPEEQMESDNCSGGDDDWTHLSSKEVDPSTGELQSLQMPESEGPSSLDPSQEGPTGLKEAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL TTOT2RY TT Literature-reported TTOT2RY FM Zinc-finger TTOT2RY KE hsa04380:Osteoclast differentiation TTOT2RY RC R-HSA-205043:NRIF signals cell death from the nucleus; R-HSA-209543:p75NTR recruits signalling complexes; R-HSA-209560:NF-kB is activated and signals survival; R-HSA-446652:Interleukin-1 signaling TT8POQR ID TT8POQR TT8POQR TN Serine protease HTRA1 (HTRA1) TT8POQR UP Q92743 TT8POQR UC HTRA1_HUMAN TT8POQR BC Peptidase TT8POQR SN Serine protease 11; L56; High-temperature requirement A serine peptidase 1; HTRA1 TT8POQR GN HTRA1 TT8POQR FC Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. TT8POQR EC EC 3.4.21.- TT8POQR PD 3TJQ; 3TJO; 3TJN; 3NZI; 3NWU TT8POQR SQ MQIPRAALLPLLLLLLAAPASAQLSRAGRSAPLAAGCPDRCEPARCPPQPEHCEGGRARDACGCCEVCGAPEGAACGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDANTYANLCQLRAASRRSERLHRPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELFRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKHRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDKIKKFLTESHDRQAKGKAITKKKYIGIRMMSLTSSKAKELKDRHRDFPDVISGAYIIEVIPDTPAEAGGLKENDVIISINGQSVVSANDVSDVIKRESTLNMVVRRGNEDIMITVIPEEIDP TT8POQR TT Literature-reported TTZFUY6 ID TTZFUY6 TTZFUY6 TN Serine Racemase (SRR) TTZFUY6 UP Q9GZT4 TTZFUY6 UC SRR_HUMAN TTZFUY6 BC Racemases and epimerase TTZFUY6 SN L-serine dehydratase; L-serine ammonia-lyase; D-serine dehydratase; D-serine ammonia-lyase TTZFUY6 GN SRR TTZFUY6 FC D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine. Catalyzes the synthesis of D-serine from L-serine. TTZFUY6 EC EC 5.1.1.18 TTZFUY6 PD 5X2L; 3L6R; 3L6B TTZFUY6 SQ MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV TTZFUY6 TT Literature-reported TT4LIAC ID TT4LIAC TT4LIAC TN Serine/threonine-protein kinase NIK (MAP3K14) TT4LIAC UP Q99558 TT4LIAC UC M3K14_HUMAN TT4LIAC BC Kinase TT4LIAC SN NIK; NF-kappa-beta-inducing kinase; Mitogen-activated protein kinase kinase kinase 14; HsNIK TT4LIAC GN MAP3K14 TT4LIAC FC Promotes proteolytic processing of NFKB2/P100, which leads to activation of NF-kappa-B via the non-canonical pathway. Could act in a receptor-selective manner. Lymphotoxin beta-activated kinase which seems to be exclusively involved in the activation of NF-kappa-B and its transcriptional activity. TT4LIAC EC EC 2.7.11.25 TT4LIAC PD 4IDV; 4IDT; 4G3D; 4DN5 TT4LIAC SQ MAVMEMACPGAPGSAVGQQKELPKAKEKTPPLGKKQSSVYKLEAVEKSPVFCGKWEILNDVITKGTAKEGSEAGPAAISIIAQAECENSQEFSPTFSERIFIAGSKQYSQSESLDQIPNNVAHATEGKMARVCWKGKRRSKARKKRKKKSSKSLAHAGVALAKPLPRTPEQESCTIPVQEDESPLGAPYVRNTPQFTKPLKEPGLGQLCFKQLGEGLRPALPRSELHKLISPLQCLNHVWKLHHPQDGGPLPLPTHPFPYSRLPHPFPFHPLQPWKPHPLESFLGKLACVDSQKPLPDPHLSKLACVDSPKPLPGPHLEPSCLSRGAHEKFSVEEYLVHALQGSVSSGQAHSLTSLAKTWAARGSRSREPSPKTEDNEGVLLTEKLKPVDYEYREEVHWATHQLRLGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACAGLTSPRIVPLYGAVREGPWVNIFMELLEGGSLGQLVKEQGCLPEDRALYYLGQALEGLEYLHSRRILHGDVKADNVLLSSDGSHAALCDFGHAVCLQPDGLGKSLLTGDYIPGTETHMAPEVVLGRSCDAKVDVWSSCCMMLHMLNGCHPWTQFFRGPLCLKIASEPPPVREIPPSCAPLTAQAIQEGLRKEPIHRVSAAELGGKVNRALQQVGGLKSPWRGEYKEPRHPPPNQANYHQTLHAQPRELSPRAPGPRPAEETTGRAPKLQPPLPPEPPEPNKSPPLTLSKEESGMWEPLPLSSLEPAPARNPSSPERKATVPEQELQQLEIELFLNSLSQPFSLEEQEQILSCLSIDSLSLSDDSEKNPSKASQSSRDTLSSGVHSWSSQAEARSSSWNMVLARGRPTDTPSYFNGVKVQIQSLNGEHLHIREFHRVKVGDIATGISSQIPAAAFSLVTKDGQPVRYDMEVPDSGIDLQCTLAPDGSFAWSWRVKHGQLENRP TT4LIAC TT Literature-reported TT4D7MJ ID TT4D7MJ TT4D7MJ TN Serine/threonine-protein kinase ULK1 (ULK1) TT4D7MJ UP O75385 TT4D7MJ UC ULK1_HUMAN TT4D7MJ BC Kinase TT4D7MJ SN hATG1; Unc-51-like kinase 1; KIAA0722; Autophagy-related protein 1 homolog; ATG1 TT4D7MJ GN ULK1 TT4D7MJ FC Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity. May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences. Plays a role early in neuronal differentiation and is required for granule cell axon formation. May also phosphorylate SESN2 and SQSTM1 to regulate autophagy. Serine/threonine-protein kinase involved in autophagy in response to starvation. TT4D7MJ EC EC 2.7.11.1 TT4D7MJ PD 6QAS; 6MNH; 6HYO; 5CI7; 4WNP TT4D7MJ SQ MEPGRGGTETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHAMRTLSEDTIRLFLQQIAGAMRLLHSKGIIHRDLKPQNILLSNPAGRRANPNSIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPTIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASPSVRKSPPVPVPSYPSSGSGSSSSSSSTSHLASPPSLGEMQQLQKTLASPADTAGFLHSSRDSGGSKDSSCDTDDFVMVPAQFPGDLVAEAPSAKPPPDSLMCSGSSLVASAGLESHGRTPSPSPPCSSSPSPSGRAGPFSSSRCGASVPIPVPTQVQNYQRIERNLQSPTQFQTPRSSAIRRSGSTSPLGFARASPSPPAHAEHGGVLARKMSLGGGRPYTPSPQVGTIPERPGWSGTPSPQGAEMRGGRSPRPGSSAPEHSPRTSGLGCRLHSAPNLSDLHVVRPKLPKPPTDPLGAVFSPPQASPPQPSHGLQSCRNLRGSPKLPDFLQRNPLPPILGSPTKAVPSFDFPKTPSSQNLLALLARQGVVMTPPRNRTLPDLSEVGPFHGQPLGPGLRPGEDPKGPFGRSFSTSRLTDLLLKAAFGTQAPDPGSTESLQEKPMEIAPSAGFGGSLHPGARAGGTSSPSPVVFTVGSPPSGSTPPQGPRTRMFSAGPTGSASSSARHLVPGPCSEAPAPELPAPGHGCSFADPITANLEGAVTFEAPDLPEETLMEQEHTEILRGLRFTLLFVQHVLEIAALKGSASEAAGGPEYQLQESVVADQISLLSREWGFAEQLVLYLKVAELLSSGLQSAIDQIRAGKLCLSSTVKQVVRRLNELYKASVVSCQGLSLRLQRFFLDKQRLLDRIHSITAERLIFSHAVQMVQSAALDEMFQHREGCVPRYHKALLLLEGLQHMLSDQADIENVTKCKLCIERRLSALLTGICA TT4D7MJ TT Literature-reported TT9LX82 ID TT9LX82 TT9LX82 TN Serum paraoxonase/arylesterase 1 (PON1) TT9LX82 UP P27169 TT9LX82 UC PON1_HUMAN TT9LX82 BC Carboxylic ester hydrolase TT9LX82 SN Serum paraoxonase; Serum aryldialkylphosphatase 1; Serum aryldiakylphosphatase 1; PON 1; PON; K-45; Aromatic esterase 1; A-esterase 1 TT9LX82 GN PON1 TT9LX82 FC Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation. Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. TT9LX82 EC EC 3.1.1.2 TT9LX82 PD 1XHR; 1V04 TT9LX82 SQ MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL TT9LX82 TT Literature-reported TT9LX82 FM Carboxylic ester hydrolase TTGC95K ID TTGC95K TTGC95K TN SET domain containing 8 (KMT5A) TTGC95K UP Q9NQR1 TTGC95K UC KMT5A_HUMAN TTGC95K BC Methyltransferase TTGC95K SN SETD8; SET8; SET07; SET domain-containing protein 8; PRSET7; PR/SET07; PR/SET domain-containing protein 07; PR-Set7; N-lysine methyltransferase KMT5A; Lysine-specific methylase 5A; Lysine N-methyltransferase 5A; Histone-lysine N-methyltransferase KMT5A; H4-K20-HMTase KMT5A TTGC95K GN KMT5A TTGC95K FC Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration. Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. TTGC95K EC EC 2.1.1.- TTGC95K PD 6BOZ; 5W1Y; 5V2N; 5TH7; 5TEG TTGC95K SQ MGEGGAAAALVAAAAAAAAAAAAVVAGQRRRRLGRRARCHGPGRAAGGKMSKPCAVEAAAAAVAATAPGPEMVERRGPGRPRTDGENVFTGQSKIYSYMSPNKCSGMRFPLQEENSVTHHEVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDARKGPLVPFPNQKSEAAEPPKTPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRKLTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQTKLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASIEAHPWLKH TTGC95K TT Preclinical TTNVC34 ID TTNVC34 TTNVC34 TN Short transient receptor potential channel 3 (TRPC3) TTNVC34 UP Q13507 TTNVC34 UC TRPC3_HUMAN TTNVC34 BC Transient receptor potential catioin channel TTNVC34 SN TrpC3; Htrp3; Htrp-3 TTNVC34 GN TRPC3 TTNVC34 FC Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5- triphosphate receptors (ITPR) with bound IP3. May also be activated by internalcalcium store depletion. TTNVC34 PD 6DJS; 6D7L; 6CUD; 5ZBG TTNVC34 SQ MREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAAEYGNIPVVRKMLEESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYVRIVEAILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILAAHCQKYEVVHMLLMKGARIERPHDYFCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYLSLSSEDPVLTALELSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESAEPLEVHRHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIAIKCLVVLVVALGLPFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDRFEGITTLPNITVTDYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQLWNVLDFGMLSIFIAAFTARFLAFLQATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARDKWLPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVLFIMVFFAFMIGMFILYSYYLGAKVNAAFTTVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIGYVLYGIYNVTMVVVLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPFSLVPSPKSFVYFIMRIVNFPKCRRRRLQKDIEMGMGNSKSRLNLFTQSNSRVFESHSFNSILNQPTRYQQIMKRLIKRYVLKAQVDKENDEVNEGELKEIKQDISSLRYELLEDKSQATEELAILIHKLSEKLNPSMLRCE TTNVC34 TT Literature-reported TTNVC34 RC R-HSA-114508:Effects of PIP2 hydrolysis; R-HSA-3295583:TRP channels; R-HSA-418890:Role of second messengers in netrin-1 signaling TTRBT3W ID TTRBT3W TTRBT3W TN Short transient receptor potential channel 6 (TRPC6) TTRBT3W UP Q9Y210 TTRBT3W UC TRPC6_HUMAN TTRBT3W BC Transient receptor potential catioin channel TTRBT3W SN TRPC6; TRP6; STrpC6 TTRBT3W GN TRPC6 TTRBT3W FC Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C. Seems not to be activated by intracellular calcium store depletion. TTRBT3W PD 5YX9 TTRBT3W SQ MSQSPAFGPRRGSSPRGAAGAAARRNESQDYLLMDSELGEDGCPQAPLPCYGYYPCFRGSDNRLAHRRQTVLREKGRRLANRGPAYMFSDRSTSLSIEEERFLDAAEYGNIPVVRKMLEECHSLNVNCVDYMGQNALQLAVANEHLEITELLLKKENLSRVGDALLLAISKGYVRIVEAILSHPAFAEGKRLATSPSQSELQQDDFYAYDEDGTRFSHDVTPIILAAHCQEYEIVHTLLRKGARIERPHDYFCKCNDCNQKQKHDSFSHSRSRINAYKGLASPAYLSLSSEDPVMTALELSNELAVLANIEKEFKNDYKKLSMQCKDFVVGLLDLCRNTEEVEAILNGDVETLQSGDHGRPNLSRLKLAIKYEVKKFVAHPNCQQQLLSIWYENLSGLRQQTMAVKFLVVLAVAIGLPFLALIYWFAPCSKMGKIMRGPFMKFVAHAASFTIFLGLLVMNAADRFEGTKLLPNETSTDNAKQLFRMKTSCFSWMEMLIISWVIGMIWAECKEIWTQGPKEYLFELWNMLDFGMLAIFAASFIARFMAFWHASKAQSIIDANDTLKDLTKVTLGDNVKYYNLARIKWDPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYIGAKQNEAFTTVEESFKTLFWAIFGLSEVKSVVINYNHKFIENIGYVLYGVYNVTMVIVLLNMLIAMINSSFQEIEDDADVEWKFARAKLWFSYFEEGRTLPVPFNLVPSPKSLFYLLLKLKKWISELFQGHKKGFQEDAEMNKINEEKKLGILGSHEDLSKLSLDKKQVGHNKQPSIRSSEDFHLNSFNNPPRQYQKIMKRLIKRYVLQAQIDKESDEVNEGELKEIKQDISSLRYELLEEKSQNTEDLAELIRELGEKLSMEPNQEETNR TTRBT3W TT Literature-reported TTRBT3W RC R-HSA-114508:Effects of PIP2 hydrolysis; R-HSA-3295583:TRP channels; R-HSA-418890:Role of second messengers in netrin-1 signaling TTDP8YM ID TTDP8YM TTDP8YM TN Sialyltransferase 8D (ST8SIA4) TTDP8YM UP Q92187 TTDP8YM UC SIA8D_HUMAN TTDP8YM BC Glycosyltransferases TTDP8YM SN Sialyltransferase St8Sia IV; ST8SiaIV; SIAT8D; SIAT8-D; Polysialyltransferase-1; PST1; PST; CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase; Alpha-2,8-sialyltransferase 8D TTDP8YM GN ST8SIA4 TTDP8YM FC Catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA), which is present on the embryonic neural cell adhesion molecule (N-CAM), necessary for plasticity of neural cells. TTDP8YM EC EC 2.4.99.- TTDP8YM PD 6AHZ; 5Y3U; 5Y22 TTDP8YM SQ MRSIRKRWTICTISLLLIFYKTKEIARTEEHQETQLIGDGELSLSRSLVNSSDKIIRKAGSSIFQHNVEGWKINSSLVLEIRKNILRFLDAERDVSVVKSSFKPGDVIHYVLDRRRTLNISHDLHSLLPEVSPMKNRRFKTCAVVGNSGILLDSECGKEIDSHNFVIRCNLAPVVEFAADVGTKSDFITMNPSVVQRAFGGFRNESDREKFVHRLSMLNDSVLWIPAFMVKGGEKHVEWVNALILKNKLKVRTAYPSLRLIHAVRGYWLTNKVPIKRPSTGLLMYTLATRFCDEIHLYGFWPFPKDLNGKAVKYHYYDDLKYRYFSNASPHRMPLEFKTLNVLHNRGALKLTTGKCVKQ TTDP8YM TT Literature-reported TTDP8YM FM Transferases of glycosyl groups TT7QT13 ID TT7QT13 TT7QT13 TN Signal transduction protein CBL (CBL) TT7QT13 UP P22681 TT7QT13 UC CBL_HUMAN TT7QT13 BC Acyltransferase TT7QT13 SN RNF55; RING-type E3 ubiquitin transferase CBL; RING finger protein 55; Proto-oncogene c-CBL; E3 ubiquitin-protein ligase CBL; Casitas B-lineage lymphoma proto-oncogene; CBL2; C-Cbl TT7QT13 GN CBL TT7QT13 FC Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA. Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. TT7QT13 EC EC 2.3.2.27 TT7QT13 PD 5O76; 5J3X; 5HL0; 5HKZ; 5HKY TT7QT13 SQ MAGNVKKSSGAGGGSGSGGSGSGGLIGLMKDAFQPHHHHHHHLSPHPPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFDPRGSGSLLRQGAEGAPSPNYDDDDDERADDTLFMMKELAGAKVERPPSPFSMAPQASLPPVPPRLDLLPQRVCVPSSASALGTASKAASGSLHKDKPLPVPPTLRDLPPPPPPDRPYSVGAESRPQRRPLPCTPGDCPSRDKLPPVPSSRLGDSWLPRPIPKVPVSAPSSSDPWTGRELTNRHSLPFSLPSQMEPRPDVPRLGSTFSLDTSMSMNSSPLVGPECDHPKIKPSSSANAIYSLAARPLPVPKLPPGEQCEGEEDTEYMTPSSRPLRPLDTSQSSRACDCDQQIDSCTYEAMYNIQSQAPSITESSTFGEGNLAAAHANTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGDPTTNVTEGSQVPERPPKPFPRRINSERKAGSCQQGSGPAASAATASPQLSSEIENLMSQGYSYQDIQKALVIAQNNIEMAKNILREFVSISSPAHVAT TT7QT13 TT Literature-reported TT7QT13 FM Carbon-nitrogen ligase TT9GR53 ID TT9GR53 TT9GR53 TN Smad1 messenger RNA (SMAD1 mRNA) TT9GR53 UP Q15797 TT9GR53 UC SMAD1_HUMAN TT9GR53 BC mRNA target TT9GR53 SN Transforming growth factor-beta-signaling protein 1 (mRNA); Smad1 (mRNA); SMAD family member 1 (mRNA); SMAD 1 (mRNA); Mothers against decapentaplegic homolog 1 (mRNA); Mothers against DPP homolog 1 (mRNA); Mad-related protein 1 (mRNA); MADR1 (mRNA); MADH1 (mRNA); MAD homolog 1 (mRNA); JV4-1 (mRNA); BSP1 (mRNA); BSP-1 (mRNA) TT9GR53 GN SMAD1 TT9GR53 FC SMAD1 is a receptor-regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. TT9GR53 PD 5ZOK; 3Q4A; 3Q47; 2LB1; 2LB0 TT9GR53 SQ MNVTSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSCPGQPSNCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEYNPQHSLLAQFRNLGQNEPHMPLNATFPDSFQQPNSHPFPHSPNSSYPNSPGSSSSTYPHSPTSSDPGSPFQMPADTPPPAYLPPEDPMTQDGSQPMDTNMMAPPLPSEINRGDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS TT9GR53 TT Literature-reported TT9GR53 FM mRNA target TT9GR53 KE hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa05202:Transcriptional misregulation in cancer TTVSMOH ID TTVSMOH TTVSMOH TN Sphingosine-1-phosphate receptor 2 (S1PR2) TTVSMOH UP O95136 TTVSMOH UC S1PR2_HUMAN TTVSMOH BC GPCR rhodopsin TTVSMOH SN Sphingosine 1-phosphate receptor Edg-5; S1PR2; S1P2; S1P receptor Edg-5; S1P receptor 2; Endothelial differentiation G-protein coupled receptor 5 TTVSMOH GN S1PR2 TTVSMOH FC Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis. TTVSMOH PD 1ZTI TTVSMOH SQ MGSLYSEYLNPNKVQEHYNYTKETLETQETTSRQVASAFIVILCCAIVVENLLVLIAVARNSKFHSAMYLFLGNLAASDLLAGVAFVANTLLSGSVTLRLTPVQWFAREGSAFITLSASVFSLLAIAIERHVAIAKVKLYGSDKSCRMLLLIGASWLISLVLGGLPILGWNCLGHLEACSTVLPLYAKHYVLCVVTIFSIILLAIVALYVRIYCVVRSSHADMAAPQTLALLKTVTIVLGVFIVCWLPAFSILLLDYACPVHSCPILYKAHYFFAVSTLNSLLNPVIYTWRSRDLRREVLRPLQCWRPGVGVQGRRRGGTPGHHLLPLRSSSSLERGMHMPTSPTFLEGNTVV TTVSMOH TT Patented-recorded TTVSMOH KE hsa04071:Sphingolipid signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTVSMOH RC R-HSA-418594:G alpha (i) signalling events; R-HSA-419408:Lysosphingolipid and LPA receptors TTL2WUI ID TTL2WUI TTL2WUI TN Spliceosome-associated protein 155 (SF3B1) TTL2WUI UP O75533 TTL2WUI UC SF3B1_HUMAN TTL2WUI BC SF3B1 family TTL2WUI SN Splicing factor 3B subunit 1; SF3b155; SAP155; SAP 155; Pre-mRNA-splicing factor SF3b 155 kDa subunit TTL2WUI GN SF3B1 TTL2WUI FC Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron. TTL2WUI PD 6QX9; 6N3E; 6FF7; 6FF4; 6EN4 TTL2WUI SQ MAKIAKTHEDIEAQIREIQGKKAALDEAQGVGLDSTGYYDQEIYGGSDSRFAGYVTSIAATELEDDDDDYSSSTSLLGQKKPGYHAPVALLNDIPQSTEQYDPFAEHRPPKIADREDEYKKHRRTMIISPERLDPFADGGKTPDPKMNARTYMDVMREQHLTKEEREIRQQLAEKAKAGELKVVNGAAASQPPSKRKRRWDQTADQTPGATPKKLSSWDQAETPGHTPSLRWDETPGRAKGSETPGATPGSKIWDPTPSHTPAGAATPGRGDTPGHATPGHGGATSSARKNRWDETPKTERDTPGHGSGWAETPRTDRGGDSIGETPTPGASKRKSRWDETPASQMGGSTPVLTPGKTPIGTPAMNMATPTPGHIMSMTPEQLQAWRWEREIDERNRPLSDEELDAMFPEGYKVLPPPAGYVPIRTPARKLTATPTPLGGMTGFHMQTEDRTMKSVNDQPSGNLPFLKPDDIQYFDKLLVDVDESTLSPEEQKERKIMKLLLKIKNGTPPMRKAALRQITDKAREFGAGPLFNQILPLLMSPTLEDQERHLLVKVIDRILYKLDDLVRPYVHKILVVIEPLLIDEDYYARVEGREIISNLAKAAGLATMISTMRPDIDNMDEYVRNTTARAFAVVASALGIPSLLPFLKAVCKSKKSWQARHTGIKIVQQIAILMGCAILPHLRSLVEIIEHGLVDEQQKVRTISALAIAALAEAATPYGIESFDSVLKPLWKGIRQHRGKGLAAFLKAIGYLIPLMDAEYANYYTREVMLILIREFQSPDEEMKKIVLKVVKQCCGTDGVEANYIKTEILPPFFKHFWQHRMALDRRNYRQLVDTTVELANKVGAAEIISRIVDDLKDEAEQYRKMVMETIEKIMGNLGAADIDHKLEEQLIDGILYAFQEQTTEDSVMLNGFGTVVNALGKRVKPYLPQICGTVLWRLNNKSAKVRQQAADLISRTAVVMKTCQEEKLMGHLGVVLYEYLGEEYPEVLGSILGALKAIVNVIGMHKMTPPIKDLLPRLTPILKNRHEKVQENCIDLVGRIADRGAEYVSAREWMRICFELLELLKAHKKAIRRATVNTFGYIAKAIGPHDVLATLLNNLKVQERQNRVCTTVAIAIVAETCSPFTVLPALMNEYRVPELNVQNGVLKSLSFLFEYIGEMGKDYIYAVTPLLEDALMDRDLVHRQTASAVVQHMSLGVYGFGCEDSLNHLLNYVWPNVFETSPHVIQAVMGALEGLRVAIGPCRMLQYCLQGLFHPARKVRDVYWKIYNSIYIGSQDALIAHYPRIYNDDKNTYIRYELDYIL TTL2WUI TT Literature-reported TTL2WUI KE hsa03040:Spliceosome TTU3WV6 ID TTU3WV6 TTU3WV6 TN SRSF protein kinase 1 (SRPK1) TTU3WV6 UP Q96SB4 TTU3WV6 UC SRPK1_HUMAN TTU3WV6 BC Kinase TTU3WV6 SN Serine/arginine-rich protein-specific kinase 1; SR-protein-specific kinase 1; SFRS protein kinase 1 TTU3WV6 GN SRPK1 TTU3WV6 FC Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation. Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. TTU3WV6 EC EC 2.7.11.1 TTU3WV6 PD 5XV7; 5NNG; 5MY8; 5MXX; 4WUA TTU3WV6 SQ MERKVLALQARKKRTKAKKDKAQRKSETQHRGSAPHSESDLPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNREMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVERPLKENPPNKMTQEKLEESSTIGQDQTLMERDTEGGAAEINCNGVIEVINYTQNSNNETLRHKEDLHNANDCDVQNLNQESSFLSSQNGDSSTSQETDSCTPITSEVSDTMVCQSSSTVGQSFSEQHISQLQESIRAEIPCEDEQEQEHNGPLDNKGKSTAGNFLVNPLEPKNAEKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEEYTRDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLFEVLVEKYEWSQEEAAGFTDFLLPMLELIPEKRATAAECLRHPWLNS TTU3WV6 TT Preclinical TTCZEJ9 ID TTCZEJ9 TTCZEJ9 TN SRSF protein kinase 2 (SRPK2) TTCZEJ9 UP P78362 TTCZEJ9 UC SRPK2_HUMAN TTCZEJ9 BC Kinase TTCZEJ9 SN Serine/arginine-rich protein-specific kinase 2; SR-protein-specific kinase 2; SFRS protein kinase 2 TTCZEJ9 GN SRPK2 TTCZEJ9 FC Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation. Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28. Can mediate hepatitis B virus (HBV) core protein phosphorylation. Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. TTCZEJ9 EC EC 2.7.11.1 TTCZEJ9 PD 5MYV; 2X7G TTCZEJ9 SQ MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPPPLPDPTPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKIIEENITSAAPSNDQDGEYCPEVKLKTTGLEEAAEAETAKDNGEAEDQEEKEDAEKENIEKDEDDVDQELANIDPTWIESPKTNGHIENGPFSLEQQLDDEDDDEEDCPNPEEYNLDEPNAESDYTYSSSYEQFNGELPNGRHKIPESQFPEFSTSLFSGSLEPVACGSVLSEGSPLTEQEESSPSHDRSRTVSASSTGDLPKAKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS TTCZEJ9 TT Literature-reported TTIYAUP ID TTIYAUP TTIYAUP TN Streptococcus Pyrroline carboxylate reductase (Stre-coc proC) TTIYAUP UP Q9A1S9 TTIYAUP UC Q9A1S9_STRP1 TTIYAUP BC CH-NH donor oxidoreductase TTIYAUP SN Pyrroline-5-carboxylate reductase; PCA reductase; P5CR; P5C reductase TTIYAUP GN Stre-coc proC TTIYAUP FC Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. TTIYAUP EC EC 1.5.1.2 TTIYAUP PD 2AMF; 2AHR TTIYAUP SQ MKIGIIGVGKMASAIIKGLKQTPHELIISGSSLERSKEIAEQLALPYAMSHQDLIDQVDLVILGIKPQLFETVLKPLHFKQPIISMAAGISLQRLATFVGQDLPLLRIMPNMNAQILQSSTALTGNALVSQELQARVRDLTDSFGSTFDISEKDFDTFTALAGSSPAYIYLFIEALAKAGVKNGIPKAKALEIVTQTVLASASNLKTSSQSPHDFIDAICSPGGTTIAGLMELERLGLTATVSSAIDKTIDKAKSL TTIYAUP TT Literature-reported TTKS60G ID TTKS60G TTKS60G TN STXBP4 messenger RNA (STXBP4 mRNA) TTKS60G UP Q6ZWJ1 TTKS60G UC STXB4_HUMAN TTKS60G BC mRNA target TTKS60G SN Syntaxin-binding protein 4 (mRNA); Syntaxin 4-interacting protein (mRNA); Synip (mRNA); STX4-interacting protein (mRNA) TTKS60G GN STXBP4 TTKS60G FC Inhibits the translocation of SLC2A4 from intracellular vesicles to the plasma membrane by STX4A binding and preventing the interaction between STX4A and VAMP2. Stimulation with insulin disrupts the interaction with STX4A, leading to increased levels of SLC2A4 at the plasma membrane. May also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose. Plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane. TTKS60G PD 2YSG TTKS60G SQ MNKNTSTVVSPSLLEKDPAFQMITIAKETGLGLKVLGGINRNEGPLVYIQEIIPGGDCYKDGRLKPGDQLVSVNKESMIGVSFEEAKSIITGAKLRLESAWEIAFIRQKSDNIQPENLSCTSLIEASGEYGPQASTLSLFSSPPEILIPKTSSTPKTNNDILSSCEIKTGYNKTVQIPITSENSTVGLSNTDVASAWTENYGLQEKISLNPSVRFKAEKLEMALNYLGIQPTKEQHQALRQQVQADSKGTVSFGDFVQVARNLFCLQLDEVNVGAHEISNILDSQLLPCDSSEADEMERLKCERDDALKEVNTLKEKLLESDKQRKQLTEELQNVKQEAKAVVEETRALRSRIHLAEAAQRQAHGMEMDYEEVIRLLEAKITELKAQLADYSDQNKESVQDLKKRIMVLDCQLRKSEMARKTFEASTEKLLHFVEAIQEVFSDNSTPLSNLSERRAVLASQTSLTPLGRNGRSIPATLALESKELVKSVRALLDMDCLPYGWEEAYTADGIKYFINHVTQTTSWIHPVMSVLNLSRSEENEEDCSRELPNQKS TTKS60G TT Literature-reported TTKS60G FM mRNA target TTEWOHV ID TTEWOHV TTEWOHV TN Survivin messenger RNA (Survivin mRNA) TTEWOHV UP O15392 TTEWOHV UC BIRC5_HUMAN TTEWOHV BC mRNA target TTEWOHV SN Survivin (mRNA); IAP4 (mRNA); Baculoviral IAP repeat-containing protein 5 (mRNA); Apoptosis inhibitor survivin (mRNA); Apoptosis inhibitor 4 (mRNA); API4 (mRNA) TTEWOHV GN BIRC5 TTEWOHV FC Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform. Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. TTEWOHV PD 4A0N; 4A0J; 4A0I; 3UIK; 3UIJ TTEWOHV SQ MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD TTEWOHV TT Literature-reported TTEWOHV FM mRNA target TTQSMFG ID TTQSMFG TTQSMFG TN Talin messenger RNA (TLN1 mRNA) TTQSMFG UP Q9Y490 TTQSMFG UC TLN1_HUMAN TTQSMFG BC mRNA target TTQSMFG SN Talin-1 (mRNA); TLN (mRNA); KIAA1027 (mRNA) TTQSMFG GN TLN1 TTQSMFG FC High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. Probably involved in connections of major cytoskeletal structures to the plasma membrane. TTQSMFG PD 4DJ9; 2MWN; 1SYQ TTQSMFG SQ MVALSLKISIGNVVKTMQFEPSTMVYDACRIIRERIPEAPAGPPSDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEYRKKQRPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKEEITGTLRKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTLREQGVEEHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWNLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDIILKKKKSKDHFGLEGDEESTMLEDSVSPKKSTVLQQQYNRVGKVEHGSVALPAIMRSGASGPENFQVGSMPPAQQQITSGQMHRGHMPPLTSAQQALTGTINSSMQAVQAAQATLDDFDTLPPLGQDAASKAWRKNKMDESKHEIHSQVDAITAGTASVVNLTAGDPAETDYTAVGCAVTTISSNLTEMSRGVKLLAALLEDEGGSGRPLLQAAKGLAGAVSELLRSAQPASAEPRQNLLQAAGNVGQASGELLQQIGESDTDPHFQDALMQLAKAVASAAAALVLKAKSVAQRTEDSGLQTQVIAAATQCALSTSQLVACTKVVAPTISSPVCQEQLVEAGRLVAKAVEGCVSASQAATEDGQLLRGVGAAATAVTQALNELLQHVKAHATGAGPAGRYDQATDTILTVTENIFSSMGDAGEMVRQARILAQATSDLVNAIKADAEGESDLENSRKLLSAAKILADATAKMVEAAKGAAAHPDSEEQQQRLREAAEGLRMATNAAAQNAIKKKLVQRLEHAAKQAAASATQTIAAAQHAASTPKASAGPQPLLVQSCKAVAEQIPLLVQGVRGSQAQPDSPSAQLALIAASQSFLQPGGKMVAAAKASVPTIQDQASAMQLSQCAKNLGTALAELRTAAQKAQEACGPLEMDSALSVVQNLEKDLQEVKAAARDGKLKPLPGETMEKCTQDLGNSTKAVSSAIAQLLGEVAQGNENYAGIAARDVAGGLRSLAQAARGVAALTSDPAVQAIVLDTASDVLDKASSLIEEAKKAAGHPGDPESQQRLAQVAKAVTQALNRCVSCLPGQRDVDNALRAVGDASKRLLSDSLPPSTGTFQEAQSRLNEAAAGLNQAATELVQASRGTPQDLARASGRFGQDFSTFLEAGVEMAGQAPSQEDRAQVVSNLKGISMSSSKLLLAAKALSTDPAAPNLKSQLAAAARAVTDSINQLITMCTQQAPGQKECDNALRELETVRELLENPVQPINDMSYFGCLDSVMENSKVLGEAMTGISQNAKNGNLPEFGDAISTASKALCGFTEAAAQAAYLVGVSDPNSQAGQQGLVEPTQFARANQAIQMACQSLGEPGCTQAQVLSAATIVAKHTSALCNSCRLASARTTNPTAKRQFVQSAKEVANSTANLVKTIKALDGAFTEENRAQCRAATAPLLEAVDNLSAFASNPEFSSIPAQISPEGRAAMEPIVISAKTMLESAGGLIQTARALAVNPRDPPSWSVLAGHSRTVSDSIKKLITSMRDKAPGQLECETAIAALNSCLRDLDQASLAAVSQQLAPREGISQEALHTQMLTAVQEISHLIEPLANAARAEASQLGHKVSQMAQYFEPLTLAAVGAASKTLSHPQQMALLDQTKTLAESALQLLYTAKEAGGNPKQAAHTQEALEEAVQMMTEAVEDLTTTLNEAASAAGVVGGMVDSITQAINQLDEGPMGEPEGSFVDYQTTMVRTAKAIAVTVQEMVTKSNTSPEELGPLANQLTSDYGRLASEAKPAAVAAENEEIGSHIKHRVQELGHGCAALVTKAGALQCSPSDAYTKKELIECARRVSEKVSHVLAALQAGNRGTQACITAASAVSGIIADLDTTIMFATAGTLNREGTETFADHREGILKTAKVLVEDTKVLVQNAAGSQEKLAQAAQSSVATITRLADVVKLGAASLGAEDPETQVVLINAVKDVAKALGDLISATKAAAGKVGDDPAVWQLKNSAKVMVTNVTSLLKTVKAVEDEATKGTRALEATTEHIRQELAVFCSPEPPAKTSTPEDFIRMTKGITMATAKAVAAGNSCRQEDVIATANLSRRAIADMLRACKEAAYHPEVAPDVRLRALHYGRECANGYLELLDHVLLTLQKPSPELKQQLTGHSKRVAGSVTELIQAAEAMKGTEWVDPEDPTVIAENELLGAAAAIEAAAKKLEQLKPRAKPKEADESLNFEEQILEAAKSIAAATSALVKAASAAQRELVAQGKVGAIPANALDDGQWSQGLISAARMVAAATNNLCEAANAAVQGHASQEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAGNAVKRASDNLVKAAQKAAAFEEQENETVVVKEKMVGGIAQIIAAQEEMLRKERELEEARKKLAQIRQQQYKFLPSELRDEH TTQSMFG TT Literature-reported TTQSMFG FM mRNA target TTQSMFG KE hsa04015:Rap1 signaling pathway; hsa04510:Focal adhesion; hsa04611:Platelet activation; hsa05166:HTLV-I infection TTQSMFG RC R-HSA-114608:Platelet degranulation; R-HSA-354192:Integrin alphaIIb beta3 signaling; R-HSA-354194:GRB2:SOS provides linkage to MAPK signaling for Integrins; R-HSA-372708:p130Cas linkage to MAPK signaling for integrins; R-HSA-381038:XBP1(S) activates chaperone genes; R-HSA-445355:Smooth Muscle Contraction; R-HSA-5674135:MAP2K and MAPK activation TTYFAM9 ID TTYFAM9 TTYFAM9 TN Tau-tubulin kinase (TTBK1) TTYFAM9 UP Q5TCY1 TTYFAM9 UC TTBK1_HUMAN TTYFAM9 BC Kinase TTYFAM9 SN Tau-tubulin kinase 1; KIAA1855; Brain-derived tau kinase; BDTK TTYFAM9 GN TTBK1 TTYFAM9 FC Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Induces aggregation of TAU. TTYFAM9 EC EC 2.7.11.1 TTYFAM9 PD 4NFN; 4NFM; 4BTM; 4BTK; 4BTJ TTYFAM9 SQ MQCLAAALKDETNMSGGGEQADILPANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFENSMKERGIAENEAFDWEKAGTDALLSTSTSTPPQQNTRQTAAMFGVVNVTPVPGDLLRENTEDVLQGEHLSDQENAPPILPGRPSEGLGPSPHLVPHPGGPEAEVWEETDVNRNKLRINIGKSPCVEEEQSRGMGVPSSPVRAPPDSPTTPVRSLRYRRVNSPESERLSTADGRVELPERRSRMDLPGSPSRQACSSQPAQMLSVDTGHADRQASGRMDVSASVEQEALSNAFRSVPLAEEEDFDSKEWVIIDKETELKDFPPGAEPSTSGTTDEEPEELRPLPEEGEERRRLGAEPTVRPRGRSMQALAEEDLQHLPPQPLPPQLSQGDGRSETSQPPTPGSPSHSPLHSGPRPRRRESDPTGPQRQVFSVAPPFEVNGLPRAVPLSLPYQDFKRDLSDYRERARLLNRVRRVGFSHMLLTTPQVPLAPVQPQANGKEEEEEEEEDEEEEEEDEEEEEEEEEEEEEEEEEEEEEEEAAAAVALGEVLGPRSGSSSEGSERSTDRSQEGAPSTLLADDQKESRGRASMADGDLEPEEGSKTLVLVSPGDMKKSPVTAELAPDPDLGTLAALTPQHERPQPTGSQLDVSEPGTLSSVLKSEPKPPGPGAGLGAGTVTTGVGGVAVTSSPFTKVERTFVHIAEKTHLNVMSSGGQALRSEEFSAGGELGLELASDGGAVEEGARAPLENGLALSGLNGAEIEGSALSGAPRETPSEMATNSLPNGPALADGPAPVSPLEPSPEKVATISPRRHAMPGSRPRSRIPVLLSEEDTGSEPSGSLSAKERWSKRARPQQDLARLVMEKRQGRLLLRLASGASSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRKSGRAAATRSRIPRPIGLRMPMPVAAQQPASRSHGAAPALDTAITSRLQLQTPPGSATAADLRPKQPPGRGLGPGRAQAGARPPAPRSPRLPASTSAARNASASPRSQSLSRRESPSPSHQARPGVPPPRGVPPARAQPDGTPSPGGSKKGPRGKLQAQRATTKGRAGGAEGRAGAR TTYFAM9 TT Literature-reported TT3A6MT ID TT3A6MT TT3A6MT TN TGFB1 messenger RNA (TGFB1 mRNA) TT3A6MT UP P01137 TT3A6MT UC TGFB1_HUMAN TT3A6MT BC mRNA target TT3A6MT SN Transforming growth factor beta-1 proprotein (mRNA); Transforming growth factor beta-1 (mRNA); TGFB (mRNA); TGF-beta1 (mRNA); TGF-beta 1 (mRNA) TT3A6MT GN TGFB1 TT3A6MT FC Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. TT3A6MT PD 5VQP; 5FFO; 4KV5; 3KFD; 1KLD TT3A6MT SQ MPPSGLRLLLLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS TT3A6MT TT Literature-reported TT3A6MT FM mRNA target TTDYFVB ID TTDYFVB TTDYFVB TN Thioredoxin glutathione reductase (TGR) TTDYFVB UP Q86VQ6 TTDYFVB UC TRXR3_HUMAN TTDYFVB BC Sulfur donor oxidoreductase TTDYFVB SN Thioredoxin reductase TR2; Thioredoxin reductase 3; Thioredoxin and glutathione reductase; TGR TTDYFVB GN TXNRD3 TTDYFVB FC Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components (By similarity). TTDYFVB EC EC 1.8.1.9 TTDYFVB PD 3H8Q TTDYFVB SQ MERSPPQSPGPGKAGDAPNRRSGHVRGARVLSPPGRRARLSSPGPSRSSEAREELRRHLVGLIERSRVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQKLLQEDLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGIQGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEKGSPGKLKVLAKSTEGTETIEGVYNTVLLAIGRDSCTRKIGLEKIGVKINEKSGKIPVNDVEQTNVPYVYAVGDILEDKPELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLEIYHTLFWPLEWTVAGRENNTCYAKIICNKFDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSGLDITQKGCUG TTDYFVB TT Literature-reported TT7KNZQ ID TT7KNZQ TT7KNZQ TN Thymidine kinase 2 (Mt-TK2) TT7KNZQ UP O00142 TT7KNZQ UC KITM_HUMAN TT7KNZQ BC Kinase TT7KNZQ SN dnk; Multispecific deoxynucleoside kinase; Dm-Dnk; Deoxyribonucleoside kinase TT7KNZQ GN dnk TT7KNZQ FC Deoxyribonucleoside kinase that has a broad specificity phosphorylating thymidine, deoxyadenosine, deoxycytidine and deoxyguanosine. Specificity is higher for pyrimidine nucleosides. Several anti-viral and anti-cancer nucleoside analogs are also efficiently phosphorylated. TT7KNZQ EC EC 2.7.1.21 TT7KNZQ SQ MLLWPLRGWAARALRCFGPGSRGSPASGPGPRRVQRRAWPPDKEQEKEKKSVICVEGNIASGKTTCLEFFSNATDVEVLTEPVSKWRNVRGHNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRPQVSSVRLMERSIHSARYIFVENLYRSGKMPEVDYVVLSEWFDWILRNMDVSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEYLEAIHHLHEEWLIKGSLFPMAAPVLVIEADHHMERMLELFEQNRDRILTPENRKHCP TT7KNZQ TT Clinical trial TT5FOMZ ID TT5FOMZ TT5FOMZ TN Thymidylate synthase (TYMS) TT5FOMZ UP P04818 TT5FOMZ UC TYSY_HUMAN TT5FOMZ BC Methyltransferase TT5FOMZ SN TSase; TS TT5FOMZ GN TYMS TT5FOMZ FC Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. TT5FOMZ EC EC 2.1.1.45 TT5FOMZ PD 6R2E; 6QYQ; 6QXH; 6QXG; 5X69 TT5FOMZ SQ MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV TT5FOMZ TT Clinical trial TT5FOMZ FM Methyltransferase superfamily TTT4236 ID TTT4236 TTT4236 TN Tie-1 tyrosine kinase receptor (TIE1) TTT4236 UP P35590 TTT4236 UC TIE1_HUMAN TTT4236 BC Kinase TTT4236 SN Tyrosine-protein kinase receptor Tie-1; TIE1 TTT4236 GN TIE1 TTT4236 FC Transmembrane tyrosine-protein kinase that may modulate TEK/TIE2 activity and contribute to the regulation of angiogenesis. TTT4236 EC EC 2.7.10.1 TTT4236 PD 5N06 TTT4236 SQ MVWRVPPFLLPILFLASHVGAAVDLTLLANLRLTDPQRFFLTCVSGEAGAGRGSDAWGPPLLLEKDDRIVRTPPGPPLRLARNGSHQVTLRGFSKPSDLVGVFSCVGGAGARRTRVIYVHNSPGAHLLPDKVTHTVNKGDTAVLSARVHKEKQTDVIWKSNGSYFYTLDWHEAQDGRFLLQLPNVQPPSSGIYSATYLEASPLGSAFFRLIVRGCGAGRWGPGCTKECPGCLHGGVCHDHDGECVCPPGFTGTRCEQACREGRFGQSCQEQCPGISGCRGLTFCLPDPYGCSCGSGWRGSQCQEACAPGHFGADCRLQCQCQNGGTCDRFSGCVCPSGWHGVHCEKSDRIPQILNMASELEFNLETMPRINCAAAGNPFPVRGSIELRKPDGTVLLSTKAIVEPEKTTAEFEVPRLVLADSGFWECRVSTSGGQDSRRFKVNVKVPPVPLAAPRLLTKQSRQLVVSPLVSFSGDGPISTVRLHYRPQDSTMDWSTIVVDPSENVTLMNLRPKTGYSVRVQLSRPGEGGEGAWGPPTLMTTDCPEPLLQPWLEGWHVEGTDRLRVSWSLPLVPGPLVGDGFLLRLWDGTRGQERRENVSSPQARTALLTGLTPGTHYQLDVQLYHCTLLGPASPPAHVLLPPSGPPAPRHLHAQALSDSEIQLTWKHPEALPGPISKYVVEVQVAGGAGDPLWIDVDRPEETSTIIRGLNASTRYLFRMRASIQGLGDWSNTVEESTLGNGLQAEGPVQESRAAEEGLDQQLILAVVGSVSATCLTILAALLTLVCIRRSCLHRRRTFTYQSGSGEETILQFSSGTLTLTRRPKLQPEPLSYPVLEWEDITFEDLIGEGNFGQVIRAMIKKDGLKMNAAIKMLKEYASENDHRDFAGELEVLCKLGHHPNIINLLGACKNRGYLYIAIEYAPYGNLLDFLRKSRVLETDPAFAREHGTASTLSSRQLLRFASDAANGMQYLSEKQFIHRDLAARNVLVGENLASKIADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEQPRNCDDEVYELMRQCWRDRPYERPPFAQIALQLGRMLEARKAYVNMSLFENFTYAGIDATAEEA TTT4236 TT Literature-reported TTCDR6M ID TTCDR6M TTCDR6M TN TNF receptor-associated factor 6 (TRAF6) TTCDR6M UP Q9Y4K3 TTCDR6M UC TRAF6_HUMAN TTCDR6M BC Acyltransferase TTCDR6M SN RNF85; RING-type E3 ubiquitin transferase TRAF6; RING finger protein 85; Interleukin-1 signal transducer; E3 ubiquitin-protein ligase TRAF6 TTCDR6M GN TRAF6 TTCDR6M FC Mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN. May be essential for the formation of functional osteoclasts. Seems to also play a role in dendritic cells (DCs) maturation and/or activation. Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. TTCDR6M EC EC 2.3.2.27 TTCDR6M PD 6A33; 5ZUJ; 4Z8M; 3HCU; 3HCT TTCDR6M SQ MSLLNCENSCGSSQSESDCCVAMASSCSAVTKDDSVGGTASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLMVKCPNEGCLHKMELRHLEDHQAHCEFALMDCPQCQRPFQKFHINIHILKDCPRRQVSCDNCAASMAFEDKEIHDQNCPLANVICEYCNTILIREQMPNHYDLDCPTAPIPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMLAQAVHSLSVIPDSGYISEVRNFQETIHQLEGRLVRQDHQIRELTAKMETQSMYVSELKRTIRTLEDKVAEIEAQQCNGIYIWKIGNFGMHLKCQEEEKPVVIHSPGFYTGKPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEAPVRQNHEEIMDAKPELLAFQRPTIPRNPKGFGYVTFMHLEALRQRTFIKDDTLLVRCEVSTRFDMGSLRREGFQPRSTDAGV TTCDR6M TT Literature-reported TTCDR6M FM Carbon-nitrogen ligase TTF85KW ID TTF85KW TTF85KW TN Torsin-1A (TOR1A) TTF85KW UP O14656 TTF85KW UC TOR1A_HUMAN TTF85KW BC Acid anhydride hydrolase TTF85KW SN Torsin family 1 member A; Torsin ATPase-1A; TORA; TA; Dystonia 1 protein; DYT1; DQ2 TTF85KW GN TOR1A TTF85KW FC Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non-neural tissues. Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. TTF85KW EC EC 3.6.4.- TTF85KW PD 5J1T; 5J1S TTF85KW SQ MKLGRAVLGLLLLAPSVVQAVEPISLGLALAGVLTGYIYPRLYCLFAECCGQKRSLSREALQKDLDDNLFGQHLAKKIILNAVFGFINNPKPKKPLTLSLHGWTGTGKNFVSKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQLWIRGNVSACARSIFIFDEMDKMHAGLIDAIKPFLDYYDLVDGVSYQKAMFIFLSNAGAERITDVALDFWRSGKQREDIKLKDIEHALSVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYEIDEDIVSRVAEEMTFFPKEERVFSDKGCKTVFTKLDYYYDD TTF85KW TT Literature-reported TTQ2BKV ID TTQ2BKV TTQ2BKV TN Transcription intermediary factor 1-beta (TRIM28) TTQ2BKV UP Q13263 TTQ2BKV UC TIF1B_HUMAN TTQ2BKV BC TRIM/RBCC family TTQ2BKV SN Tripartite motif-containing protein 28; TIF1B; TIF1-beta; RNF96; RING-type E3 ubiquitin transferase TIF1-beta; RING finger protein 96; Nuclear corepressor KAP-1; KRIP-1; KRAB-interacting protein 1; KRAB-associated protein 1; KAP1; KAP-1; E3 SUMO-protein ligase TRIM28 TTQ2BKV GN TRIM28 TTQ2BKV FC Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg) (PubMed:23543754). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway. Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (PubMed:27029610). Acts as a corepressor for ZFP568. TTQ2BKV EC EC 2.3.2.27 TTQ2BKV PD 6I9H; 2YVR; 2RO1; 1FP0 TTQ2BKV SQ MAASAAAASAAAASAASGSPGPGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPAPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGSGDDPYSSAEPHVSGVKRSRSGEGEVSGLMRKVPRVSLERLDLDLTADSQPPVFKVFPGSTTEDYNLIVIERGAAAAATGQPGTAPAGTPGAPPLAGMAIVKEEETEAAIGAPPTATEGPETKPVLMALAEGPGAEGPRLASPSGSTSSGLEVVAPEGTSAPGGGPGTLDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSLDQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNEAFGDTKFSAVLVEPPPMSLPGAGLSSQELSGGPGDGP TTQ2BKV TT Literature-reported TT8WXAV ID TT8WXAV TT8WXAV TN Transferrin messenger RNA (TF mRNA) TT8WXAV UP P02787 TT8WXAV UC TRFE_HUMAN TT8WXAV BC mRNA target TT8WXAV SN Transferrin (mRNA); Siderophilin (mRNA); Serotransferrin (mRNA); PRO1400 (mRNA); Beta-1 metal-binding globulin (mRNA) TT8WXAV GN TF TT8WXAV FC It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. TT8WXAV PD 6D05; 6D04; 6D03; 6CTC; 5Y6K TT8WXAV SQ MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKSDNCEDTPEAGYFAIAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP TT8WXAV TT Literature-reported TT8WXAV FM mRNA target TT8WXAV KE hsa04066:HIF-1 signaling pathway; hsa04978:Mineral absorption TT8WXAV RC R-HSA-114608:Platelet degranulation; R-HSA-917937:Iron uptake and transport; R-HSA-917977:Transferrin endocytosis and recycling TTNQ1J3 ID TTNQ1J3 TTNQ1J3 TN Transketolase-like protein 1 (TKTL1) TTNQ1J3 UP P51854 TTNQ1J3 UC TKTL1_HUMAN TTNQ1J3 BC Transketolase family TTNQ1J3 SN Transketolase-related protein; Transketolase 2; TKT2; TKR; TK 2 TTNQ1J3 GN TKTL1 TTNQ1J3 FC Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. TTNQ1J3 EC EC 2.2.1.1 TTNQ1J3 SQ MADAEARAEFPEEARPDRGTLQVLQDMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAKRLSFVDVATGWLGQGLGVACGMAYTGKYFDRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKLIESQIQTSRNLDPQPPIEDSPEVNITDVRMTSPPDYRVGDKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTRPETMVIYTPQERFEIGQAKVLRHCVSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVPQSGKSEELLDMYGISARHIIVAVKCMLLN TTNQ1J3 TT Literature-reported TTNQ1J3 KE hsa00030:Pentose phosphate pathway; hsa01100:Metabolic pathways; hsa01200:Carbon metabolism; hsa01230:Biosynthesis of amino acids TT1GM2Z ID TT1GM2Z TT1GM2Z TN Transmembrane protease serine 2 (TMPRSS2) TT1GM2Z UP O15393 TT1GM2Z UC TMPS2_HUMAN TT1GM2Z BC Peptidase TT1GM2Z SN TMPRSS2 protease; TMPRSS2 TT1GM2Z GN TMPRSS2 TT1GM2Z FC Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus- cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike glycoprotein which activates the glycoprotein for cathepsin L- independent host cell entry. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity. TT1GM2Z EC EC 3.4.21.- TT1GM2Z SQ MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG TT1GM2Z TT Literature-reported TT9Q7AE ID TT9Q7AE TT9Q7AE TN Tripartite motif-containing 24 (TRIM24) TT9Q7AE UP O15164 TT9Q7AE UC TIF1A_HUMAN TT9Q7AE BC Acyltransferase TT9Q7AE SN Tripartite motif-containing protein 24; Transcription intermediary factor 1-alpha; TIF1A; TIF1-alpha; TIF1; RNF82; RING-type E3 ubiquitin transferase TIF1-alpha; RING finger protein 82; E3 ubiquitin-protein ligase TRIM24 TT9Q7AE GN TRIM24 TT9Q7AE FC Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes. Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. TT9Q7AE EC EC 2.3.2.27 TT9Q7AE PD 5H1V; 5H1U; 5H1T; 4ZQL; 4YC9 TT9Q7AE SQ MEVAVEKAVAAAAAASAAASGGPSAAPSGENEAESRQGPDSERGGEAARLNLLDTCAVCHQNIQSRAPKLLPCLHSFCQRCLPAPQRYLMLPAPMLGSAETPPPVPAPGSPVSGSSPFATQVGVIRCPVCSQECAERHIIDNFFVKDTTEVPSSTVEKSNQVCTSCEDNAEANGFCVECVEWLCKTCIRAHQRVKFTKDHTVRQKEEVSPEAVGVTSQRPVFCPFHKKEQLKLYCETCDKLTCRDCQLLEHKEHRYQFIEEAFQNQKVIIDTLITKLMEKTKYIKFTGNQIQNRIIEVNQNQKQVEQDIKVAIFTLMVEINKKGKALLHQLESLAKDHRMKLMQQQQEVAGLSKQLEHVMHFSKWAVSSGSSTALLYSKRLITYRLRHLLRARCDASPVTNNTIQFHCDPSFWAQNIINLGSLVIEDKESQPQMPKQNPVVEQNSQPPSGLSSNQLSKFPTQISLAQLRLQHMQQQVMAQRQQVQRRPAPVGLPNPRMQGPIQQPSISHQQPPPRLINFQNHSPKPNGPVLPPHPQQLRYPPNQNIPRQAIKPNPLQMAFLAQQAIKQWQISSGQGTPSTTNSTSSTPSSPTITSAAGYDGKAFGSPMIDLSSPVGGSYNLPSLPDIDCSSTIMLDNIVRKDTNIDHGQPRPPSNRTVQSPNSSVPSPGLAGPVTMTSVHPPIRSPSASSVGSRGSSGSSSKPAGADSTHKVPVVMLEPIRIKQENSGPPENYDFPVVIVKQESDEESRPQNANYPRSILTSLLLNSSQSSTSEETVLRSDAPDSTGDQPGLHQDNSSNGKSEWLDPSQKSPLHVGETRKEDDPNEDWCAVCQNGGELLCCEKCPKVFHLSCHVPTLTNFPSGEWICTFCRDLSKPEVEYDCDAPSHNSEKKKTEGLVKLTPIDKRKCERLLLFLYCHEMSLAFQDPVPLTVPDYYKIIKNPMDLSTIKKRLQEDYSMYSKPEDFVADFRLIFQNCAEFNEPDSEVANAGIKLENYFEELLKNLYPEKRFPKPEFRNESEDNKFSDDSDDDFVQPRKKRLKSIEERQLLK TT9Q7AE TT Literature-reported TT1A6HL ID TT1A6HL TT1A6HL TN Tyrosine-protein kinase ABL2 (ABL2) TT1A6HL UP P42684 TT1A6HL UC ABL2_HUMAN TT1A6HL BC Kinase TT1A6HL SN Tyrosine-protein kinase ARG; Abelson-related gene protein; Abelson tyrosine-protein kinase 2; Abelson murine leukemia viral oncogene homolog 2; ARG; ABLL TT1A6HL GN ABL2 TT1A6HL FC Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. ABL2 acts also as a regulator of multiple pathological signaling cascades during infection. Pathogens can highjack ABL2 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion and receptor endocytosis. TT1A6HL EC EC 2.7.10.2 TT1A6HL PD 5NP5; 5NP3; 4EIH; 3ULR; 3HMI TT1A6HL SQ MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTTETGFNIFTQHDHFASCVEDGFEGDKTGGSSPEALHRPYGCDVEPQALNEAIRWSSKENLLGATESDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNQNGEWSEVRSKNGQGWVPSNYITPVNSLEKHSWYHGPVSRSAAEYLLSSLINGSFLVRESESSPGQLSISLRYEGRVYHYRINTTADGKVYVTAESRFSTLAELVHHHSTVADGLVTTLHYPAPKCNKPTVYGVSPIHDKWEMERTDITMKHKLGGGQYGEVYVGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTLEPPFYIVTEYMPYGNLLDYLRECNREEVTAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHVVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNTFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYDLLEKGYRMEQPEGCPPKVYELMRACWKWSPADRPSFAETHQAFETMFHDSSISEEVAEELGRAASSSSVVPYLPRLPILPSKTRTLKKQVENKENIEGAQDATENSASSLAPGFIRGAQASSGSPALPRKQRDKSPSSLLEDAKETCFTRDRKGGFFSSFMKKRNAPTPPKRSSSFREMENQPHKKYELTGNFSSVASLQHADGFSFTPAQQEANLVPPKCYGGSFAQRNLCNDDGGGGGGSGTAGGGWSGITGFFTPRLIKKTLGLRAGKPTASDDTSKPFPRSNSTSSMSSGLPEQDRMAMTLPRNCQRSKLQLERTVSTSSQPEENVDRANDMLPKKSEESAAPSRERPKAKLLPRGATALPLRTPSGDLAITEKDPPGVGVAGVAAAPKGKEKNGGARLGMAGVPEDGEQPGWPSPAKAAPVLPTTHNHKVPVLISPTLKHTPADVQLIGTDSQGNKFKLLSEHQVTSSGDKDRPRRVKPKCAPPPPPVMRLLQHPSICSDPTEEPTALTAGQSTSETQEGGKKAALGAVPISGKAGRPVMPPPQVPLPTSSISPAKMANGTAGTKVALRKTKQAAEKISADKISKEALLECADLLSSALTEPVPNSQLVDTGHQLLDYCSGYVDCIPQTRNKFAFREAVSKLELSLQELQVSSAAAGVPGTNPVLNNLLSCVQEISDVVQR TT1A6HL TT Literature-reported TTN2I9E ID TTN2I9E TTN2I9E TN Tyrosine-protein kinase BMX (BMX) TTN2I9E UP P51813 TTN2I9E UC BMX_HUMAN TTN2I9E BC Kinase TTN2I9E SN NTK38; Epithelial and endothelial tyrosine kinase; ETK; Cytoplasmic tyrosine-protein kinase BMX; Bone marrow tyrosine kinase gene in chromosome X protein TTN2I9E GN BMX TTN2I9E FC Non-receptor tyrosine kinase that plays central but diverse modulatory roles in various signaling processes involved in the regulation of actin reorganization, cell migration, cell proliferation and survival, cell adhesion, and apoptosis. Participates in signal transduction stimulated by growth factor receptors, cytokine receptors, G-protein coupled receptors, antigen receptors and integrins. Induces tyrosine phosphorylation of BCAR1 in response to integrin regulation. Activation of BMX by integrins is mediated by PTK2/FAK1, a key mediator of integrin signaling events leading to the regulation of actin cytoskeleton and cell motility. Plays a critical role in TNF-induced angiogenesis, and implicated in the signaling of TEK and FLT1 receptors, 2 important receptor families essential for angiogenesis. Required for the phosphorylation and activation of STAT3, a transcription factor involved in cell differentiation. Also involved in interleukin-6 (IL6) induced differentiation. Plays also a role in programming adaptive cytoprotection against extracellular stress in different cell systems, salivary epithelial cells, brain endothelial cells, and dermal fibroblasts. May be involved in regulation of endocytosis through its interaction with an endosomal protein RUFY1. May also play a role in the growth and differentiation of hematopoietic cells; as well as in signal transduction in endocardial and arterial endothelial cells. TTN2I9E EC EC 2.7.10.2 TTN2I9E PD 3SXS; 3SXR; 2YS2; 2EKX TTN2I9E SQ MDTKSILEELLLKRSQQKKKMSPNNYKERLFVLTKTNLSYYEYDKMKRGSRKGSIEIKKIRCVEKVNLEEQTPVERQYPFQIVYKDGLLYVYASNEESRSQWLKALQKEIRGNPHLLVKYHSGFFVDGKFLCCQQSCKAAPGCTLWEAYANLHTAVNEEKHRVPTFPDRVLKIPRAVPVLKMDAPSSSTTLAQYDNESKKNYGSQPPSSSTSLAQYDSNSKKIYGSQPNFNMQYIPREDFPDWWQVRKLKSSSSSEDVASSNQKERNVNHTTSKISWEFPESSSSEEEENLDDYDWFAGNISRSQSEQLLRQKGKEGAFMVRNSSQVGMYTVSLFSKAVNDKKGTVKHYHVHTNAENKLYLAENYCFDSIPKLIHYHQHNSAGMITRLRHPVSTKANKVPDSVSLGNGIWELKREEITLLKELGSGQFGVVQLGKWKGQYDVAVKMIKEGSMSEDEFFQEAQTMMKLSHPKLVKFYGVCSKEYPIYIVTEYISNGCLLNYLRSHGKGLEPSQLLEMCYDVCEGMAFLESHQFIHRDLAARNCLVDRDLCVKVSDFGMTRYVLDDQYVSSVGTKFPVKWSAPEVFHYFKYSSKSDVWAFGILMWEVFSLGKQPYDLYDNSQVVLKVSQGHRLYRPHLASDTIYQIMYSCWHELPEKRPTFQQLLSSIEPLREKDKH TTN2I9E TT Patented-recorded TTX6F0Q ID TTX6F0Q TTX6F0Q TN Tyrosine-protein kinase CSK (CSK) TTX6F0Q UP P41240 TTX6F0Q UC CSK_HUMAN TTX6F0Q BC Kinase TTX6F0Q SN Protein-tyrosine kinase CYL; C-Src kinase TTX6F0Q GN CSK TTX6F0Q FC Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN, CSK or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK. Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. TTX6F0Q EC EC 2.7.10.2 TTX6F0Q PD 3EAZ; 3EAC; 3D7U; 3D7T; 1CSK TTX6F0Q SQ MSAIQAAWPSGTECIAKYNFHGTAEQDLPFCKGDVLTIVAVTKDPNWYKAKNKVGREGIIPANYVQKREGVKAGTKLSLMPWFHGKITREQAERLLYPPETGLFLVRESTNYPGDYTLCVSCDGKVEHYRIMYHASKLSIDEEVYFENLMQLVEHYTSDADGLCTRLIKPKVMEGTVAAQDEFYRSGWALNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYEVMKNCWHLDAAMRPSFLQLREQLEHIKTHELHL TTX6F0Q TT Patented-recorded TTYF26D ID TTYF26D TTYF26D TN Tyrosyl-DNA phosphodiesterase 2 (TDP2) TTYF26D UP O95551 TTYF26D UC TYDP2_HUMAN TTYF26D BC Phosphoric diester hydrolase TTYF26D SN hTDP2; VPg unlinkase; Tyrosyl-RNA phosphodiesterase; Tyr-DNA phosphodiesterase 2; TRAF and TNF receptor-associated protein; TDP2; ETS1-associated protein II; ETS1-associated protein 2; EAPII; 5'-tyrosyl-DNA phosphodiesterase; 5'-Tyr-DNA phosphodiesterase TTYF26D GN TDP2 TTYF26D FC DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. Hydrolyzes 5'- phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Has also 3'- tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'- tyrosyl-DNA phosphodiesterase in cells. Also acts as a 5'-tyrosyl- RNA phosphodiesterase following picornavirus infection: its activity is hijacked by picornavirus and acts by specifically cleaving the protein-RNA covalent linkage generated during the viral genomic RNA replication steps of a picornavirus infection, without impairing the integrity of viral RNA. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta: associates with components of the TGF- beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non- canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation. Acts as a regulator of ribosome biogenesis following stress. TTYF26D EC EC 3.1.4.- TTYF26D PD 5J3S; 5J3P; 5INO TTYF26D SQ MELGSCLEGGREAAEEEGEPEVKKRRLLCVEFASVASCDAAVAQCFLAENDWEMERALNSYFEPPVEESALERRPETISEPKTYVDLTNEETTDSTTSKISPSEDTQQENGSMFSLITWNIDGLDLNNLSERARGVCSYLALYSPDVIFLQEVIPPYYSYLKKRSSNYEIITGHEEGYFTAIMLKKSRVKLKSQEIIPFPSTKMMRNLLCVHVNVSGNELCLMTSHLESTRGHAAERMNQLKMVLKKMQEAPESATVIFAGDTNLRDREVTRCGGLPNNIVDVWEFLGKPKHCQYTWDTQMNSNLGITAACKLRFDRIFFRAAAEEGHIIPRSLDLLGLEKLDCGRFPSDHWGLLCNLDIIL TTYF26D TT Literature-reported TTUEQ1W ID TTUEQ1W TTUEQ1W TN Ubiquitin carboxyl-terminal hydrolase 2 (USP2) TTUEQ1W UP O75604 TTUEQ1W UC UBP2_HUMAN TTUEQ1W BC Peptidase TTUEQ1W SN Ubiquitin-specific-processing protease 2; Ubiquitin thioesterase 2; UBP41; Deubiquitinating enzyme 2; 41 kDa ubiquitin-specific protease TTUEQ1W GN USP2 TTUEQ1W FC Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues. Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability. Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells. Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. TTUEQ1W EC EC 3.4.19.12 TTUEQ1W PD 6DGF; 5XVE; 5XU8; 3V6E; 3V6C TTUEQ1W SQ MSQLSSTLKRYTESARYTDAHYAKSGYGAYTPSSYGANLAASLLEKEKLGFKPVPTSSFLTRPRTYGPSSLLDYDRGRPLLRPDITGGGKRAESQTRGTERPLGSGLSGGSGFPYGVTNNCLSYLPINAYDQGVTLTQKLDSQSDLARDFSSLRTSDSYRIDPRNLGRSPMLARTRKELCTLQGLYQTASCPEYLVDYLENYGRKGSASQVPSQAPPSRVPEIISPTYRPIGRYTLWETGKGQAPGPSRSSSPGRDGMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM TTUEQ1W TT Preclinical TTUEQ1W FM Peptidase TTJDELN ID TTJDELN TTJDELN TN Ubiquitin carboxyl-terminal hydrolase 37 (USP37) TTJDELN UP Q86T82 TTJDELN UC UBP37_HUMAN TTJDELN BC Peptidase TTJDELN SN Ubiquitin-specific-processing protease 37; Ubiquitin thioesterase 37; KIAA1594; Deubiquitinating enzyme 37 TTJDELN GN USP37 TTJDELN FC Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). Plays an important role in the regulation of DNA replication by stabilizing the licensing factor CDT1. Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. TTJDELN EC EC 3.4.19.12 TTJDELN PD 3U12 TTJDELN SQ MSPLKIHGPIRIRSMQTGITKWKEGSFEIVEKENKVSLVVHYNTGGIPRIFQLSHNIKNVVLRPSGAKQSRLMLTLQDNSFLSIDKVPSKDAEEMRLFLDAVHQNRLPAAMKPSQGSGSFGAILGSRTSQKETSRQLSYSDNQASAKRGSLETKDDIPFRKVLGNPGRGSIKTVAGSGIARTIPSLTSTSTPLRSGLLENRTEKRKRMISTGSELNEDYPKENDSSSNNKAMTDPSRKYLTSSREKQLSLKQSEENRTSGLLPLQSSSFYGSRAGSKEHSSGGTNLDRTNVSSQTPSAKRSLGFLPQPVPLSVKKLRCNQDYTGWNKPRVPLSSHQQQQLQGFSNLGNTCYMNAILQSLFSLQSFANDLLKQGIPWKKIPLNALIRRFAHLLVKKDICNSETKKDLLKKVKNAISATAERFSGYMQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVSGEENSPDISATRAYTCPVITNLEFEVQHSIICKACGEIIPKREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSLNNKIGQQVIIPRYLTLSSHCTENTKPPFTLGWSAHMAISRPLKASQMVNSCITSPSTPSKKFTFKSKSSLALCLDSDSEDELKRSVALSQRLCEMLGNEQQQEDLEKDSKLCPIEPDKSELENSGFDRMSEEELLAAVLEISKRDASPSLSHEDDDKPTSSPDTGFAEDDIQEMPENPDTMETEKPKTITELDPASFTEITKDCDENKENKTPEGSQGEVDWLQQYDMEREREEQELQQALAQSLQEQEAWEQKEDDDLKRATELSLQEFNNSFVDALGSDEDSGNEDVFDMEYTEAEAEELKRNAETGNLPHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRSGYIFFYMHKEIFDELLETEKNSQSLSTEVGKTTRQAL TTJDELN TT Literature-reported TTJDELN FM Peptidase TT1J07C ID TT1J07C TT1J07C TN Ubiquitin isopeptidase Y (USP8) TT1J07C UP P40818 TT1J07C UC UBP8_HUMAN TT1J07C BC Peptidase TT1J07C SN hUBPy; Ubiquitin-specific-processing protease 8; Ubiquitin thioesterase 8; Ubiquitin carboxyl-terminal hydrolase 8; UBPY; KIAA0055; Deubiquitinating enzyme 8 TT1J07C GN USP8 TT1J07C FC Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-medaited APP cleavage and amyloid-beta formation. Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. TT1J07C EC EC 3.4.19.12 TT1J07C PD 6F09; 3N3K; 2GWF; 2GFO; 2A9U TT1J07C SQ MPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAKGSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSIKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLGPRVTDVAT TT1J07C TT Preclinical TT1J07C FM Peptidase TT23UD6 ID TT23UD6 TT23UD6 TN Ubiquitin thioesterase L3 (UCHL3) TT23UD6 UP P15374 TT23UD6 UC UCHL3_HUMAN TT23UD6 BC Peptidase TT23UD6 SN Ubiquitin carboxyl-terminal hydrolase isozyme L3; UCH-L3 TT23UD6 GN UCHL3 TT23UD6 FC Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders. Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. TT23UD6 EC EC 3.4.19.12 TT23UD6 PD 6ISU; 1XD3; 1UCH TT23UD6 SQ MEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFLEESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA TT23UD6 TT Literature-reported TTFSH0K ID TTFSH0K TTFSH0K TN Ubiquitin thioesterase OTU1 (YOD1) TTFSH0K UP Q5VVQ6 TTFSH0K UC OTU1_HUMAN TTFSH0K BC Peptidase TTFSH0K SN PRO0907; OTUD2; OTU domain-containing protein 2; HsHIN7; HIV-1-induced protease 7; HIN7; HIN-7; DUBA8; DUBA-8 TTFSH0K GN YOD1 TTFSH0K FC May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin. May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes. May recruit PLAA, UBXN6 and VCP to damaged lysosome membranes decorated with K48-linked ubiquitin chains and remove these chains allowing autophagosome formation. Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. TTFSH0K EC EC 3.4.19.12 TTFSH0K PD 4BOZ; 4BOS; 4BOQ TTFSH0K SQ MFGPAKGRHFGVHPAPGFPGGVSQQAAGTKAGPAGAWPVGSRTDTMWRLRCKAKDGTHVLQGLSSRTRVRELQGQIAAITGIAPGGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIIEEDQTRPRSSPAFTKRGASSYVRETLPVLTRTVVPADNSCLFTSVYYVVEGGVLNPACAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEISILSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDGIHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEARRRRQFTDVNRFTLRCMVCQKGLTGQAEAREHAKETGHTNFGEV TTFSH0K TT Literature-reported TTFSH0K FM Peptidase TTXJEOF ID TTXJEOF TTXJEOF TN Ubiquitin-protein ligase E2 (UBE2E2) TTXJEOF UP Q96LR5 TTXJEOF UC UB2E2_HUMAN TTXJEOF BC Ubiquitin-conjugating enzyme TTXJEOF SN Ubiquitin-conjugating enzyme E2 E2; Ubiquitin carrier protein E2; UbcH8; E2 ubiquitin-conjugating enzyme E2 TTXJEOF GN UBE2E2 TTXJEOF FC In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Catalyzes the ISGylation of influenza A virus NS1 protein. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. TTXJEOF EC EC 2.3.2.23 TTXJEOF PD 1Y6L TTXJEOF SQ MSTEAQRVDDSPSTSGGSSDGDQRESVQQEPEREQVQPKKKEGKISSKTAAKLSTSAKRIQKELAEITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFSPDYPFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYMTNRAEHDRMARQWTKRYAT TTXJEOF TT Literature-reported TTXJEOF FM Carbon-nitrogen ligase TTL2PXZ ID TTL2PXZ TTL2PXZ TN Vacuolar-type proton ATPase catalytic A (v-ATPase-A) TTL2PXZ UP P38606 TTL2PXZ UC VATA_HUMAN TTL2PXZ BC Acid anhydrides hydrolase TTL2PXZ SN Vacuolar proton pump subunit alpha; Vacuolar ATPase isoform VA68; VPP2; V-ATPase subunit A; V-ATPase 69 kDa subunit; ATP6V1A1; ATP6V1A; ATP6A1 TTL2PXZ GN ATP6V1A TTL2PXZ FC Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. TTL2PXZ EC EC 7.1.2.2 TTL2PXZ SQ MDFSKLPKILDEDKESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWDFTPCKNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTYIAPPGNYDTSDVVLELEFEGVKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDNKITWSIIREHMGDILYKLSSMKFKDPLKDGEAKIKSDYAQLLEDMQNAFRSLED TTL2PXZ TT Literature-reported TTL2PXZ KE hsa00190:Oxidative phosphorylation; hsa01100:Metabolic pathways; hsa04145:Phagosome; hsa04721:Synaptic vesicle cycle; hsa04966:Collecting duct acid secretion; hsa05110:Vibrio cholerae infection; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05323:Rheumatoid arthritis TTL2PXZ RC R-HSA-1222556:ROS production in response to bacteria; R-HSA-77387:Insulin receptor recycling; R-HSA-917977:Transferrin endocytosis and recycling TTTZ3EU ID TTTZ3EU TTTZ3EU TN Valacyclovir hydrolase (BPHL) TTTZ3EU UP Q86WA6 TTTZ3EU UC BPHL_HUMAN TTTZ3EU BC Carboxylic ester hydrolase TTTZ3EU SN VACVase; MCNAA; DJ40E16.6.1; Breast epithelial mucin-associated antigen; Bph-rp; Biphenyl hydrolase-like protein (Serine hydrolase) (Breast epithelial mucin-associated antigen, MCNAA, Bph-rp), variant 1; Biphenyl hydrolase-like protein; BPHL TTTZ3EU GN BPHL TTTZ3EU FC Serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. Activates valacyclovir to acyclovir. May play a role in detoxification processes. It is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring aprimary alcohol. TTTZ3EU EC EC 3.1.-.- TTTZ3EU PD 2OCL; 2OCK; 2OCI; 2OCG TTTZ3EU SQ MVAVLGGRGVLRLRLLLSALKPGIHVPRAGPAAAFGTSVTSAKVAVNGVQLHYQQTGEGDHAVLLLPGMLGSGETDFGPQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFPADFFERDAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYFARTCEKWVDGIRQFKHLPDGNICRHLLPRVQCPALIVHGEKDPLVPRFHADFIHKHVKGSRLHLMPEGKHNLHLRFADEFNKLAEDFLQ TTTZ3EU TT Literature-reported TTHCEF6 ID TTHCEF6 TTHCEF6 TN VCAM-1 messenger RNA (VCAM1 mRNA) TTHCEF6 UP P19320 TTHCEF6 UC VCAM1_HUMAN TTHCEF6 BC mRNA target TTHCEF6 SN Vascular cell adhesion protein 1 (mRNA); Vascular cell adhesion molecule 1 (mRNA); VCAM-1 (mRNA); V-CAM 1 (mRNA); INCAM-100 (mRNA); CD106 antigen (mRNA); CD106 (mRNA) TTHCEF6 GN VCAM1 TTHCEF6 FC Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation. Important in cell-cell recognition. TTHCEF6 PD 1VSC; 1VCA; 1IJ9 TTHCEF6 SQ MPGKMVVILGASNILWIMFAASQAFKIETTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGIQVEIYSFPKDPEIHLSGPLEAGKPITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGKVLVCRAKLHIDEMDSVPTVRQAVKELQVYISPKNTVISVNPSTKLQEGGSVTMTCSSEGLPAPEIFWSKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIVQEKPFTVEISPGPRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGKVRSEGTNSTLTLSPVSFENEHSYLCTVTCGHKKLEKGIQVELYSFPRDPEIEMSGGLVNGSSVTVSCKVPSVYPLDRLEIELLKGETILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGKALVCQAKLHIDDMEFEPKQRQSTQTLYVNVAPRDTTVLVSPSSILEEGSSVNMTCLSQGFPAPKILWSRQLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVELIIQVTPKDIKLTAFPSESVKEGDTVIISCTCGNVPETWIILKKKAETGDTVLKSIDGAYTIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQGRENNKDYFSPELLVLYFASSLIIPAIGMIIYFARKANMKGSYSLVEAQKSKV TTHCEF6 TT Literature-reported TTHCEF6 FM mRNA target TTHCEF6 KE hsa04064:NF-kappa B signaling pathway; hsa04514:Cell adhesion molecules (CAMs); hsa04668:TNF signaling pathway; hsa04670:Leukocyte transendothelial migration; hsa05143:African trypanosomiasis; hsa05144:Malaria; hsa05166:HTLV-I infection TTHCEF6 RC R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-216083:Integrin cell surface interactions; R-HSA-877300:Interferon gamma signaling TTGIKO3 ID TTGIKO3 TTGIKO3 TN VEGF A165 messenger RNA (VEGF A165 mRNA) TTGIKO3 UP P15692 TTGIKO3 UC VEGFA_HUMAN TTGIKO3 BC mRNA target TTGIKO3 SN Vascular permeability factor A165 (mRNA); Vascular endothelial growth factor A A165 (mRNA); VPF A165 (mRNA); VEGF-A A165 (mRNA); VEGF A165 (mRNA) TTGIKO3 GN VEGFA A165 TTGIKO3 FC Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development. Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. TTGIKO3 PD 6D3O; 6BFT; 5T89; 5O4E; 5HHD TTGIKO3 SQ MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPHPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR TTGIKO3 TT Literature-reported TTGIKO3 FM mRNA target TT3LJ9K ID TT3LJ9K TT3LJ9K TN VEGF messenger RNA (VEGF mRNA) TT3LJ9K UP P15692 TT3LJ9K UC VEGFA_HUMAN TT3LJ9K BC mRNA target TT3LJ9K SN Vascular permeability factor (mRNA); Vascular endothelial growth factor A (mRNA); VPF (mRNA); VEGF-A (mRNA); VEGF (mRNA) TT3LJ9K GN VEGFA TT3LJ9K FC Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development. Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. TT3LJ9K PD 6D3O; 6BFT; 5T89; 5O4E; 5HHD TT3LJ9K SQ MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPHPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR TT3LJ9K TT Literature-reported TT3LJ9K FM mRNA target TT3LJ9K KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04370:VEGF signaling pathway; hsa04510:Focal adhesion; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05219:Bladder cancer; hsa05323:Rheumatoid arthritis TT3LJ9K RC R-HSA-114608:Platelet degranulation; R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-194313:VEGF ligand-receptor interactions; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization TTH52YN ID TTH52YN TTH52YN TN VLA-4 messenger RNA (VLA-4 mRNA) TTH52YN UP P13612-P05556 TTH52YN UC ITA4_HUMAN-ITB1_HUMAN TTH52YN BC mRNA target TTH52YN SN VLA-4 (mRNA); Integrin alpha-4/beta-1 (mRNA) TTH52YN GN ITGA4-ITGB1 TTH52YN FC Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha- 4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha- 4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. TTH52YN SQ MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGKMAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD TTH52YN TT Literature-reported TTH52YN FM mRNA target TTH52YN KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04514:Cell adhesion molecules (CAMs); hsa04640:Hematopoietic cell lineage; hsa04670:Leukocyte transendothelial migration; hsa04672:Intestinal immune network for IgA production; hsa04810:Regulation of actin cytoskeleton; hsa05140:Leishmaniasis; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTH52YN RC R-HSA-1566948:Elastic fibre formation; R-HSA-1566977:Fibronectin matrix formation; R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-202733:Cell surface interactions at the vascular wall; R-HSA-210991:Basigin interactions; R-HSA-2129379:Molecules associated with elastic fibres; R-HSA-216083:Integrin cell surface interactions; R-HSA-3000157:Laminin interactions; R-HSA-3000170:Syndecan interactions; R-HSA-3000178:ECM proteoglycans; R-HSA-416700:Other semaphorin interactions; R-HSA-446343:Localization of the PINCH-ILK-PARVIN complex to focal adhesions; R-HSA-447041:CHL1 interactions; R-HSA-5663220:RHO GTPases Activate Formins TTM1I7L ID TTM1I7L TTM1I7L TN Voltage-dependent anion-selective channel 2 (VDAC2) TTM1I7L UP P45880 TTM1I7L UC VDAC2_HUMAN TTM1I7L BC Eukaryotic mitochondrial porin TTM1I7L SN hVDAC2; VDAC2; VDAC-2; Outer mitochondrial membrane protein porin 2 TTM1I7L GN VDAC2 TTM1I7L FC Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation- selective. TTM1I7L SQ MATHGQTCARPMCIPPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRNNFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSINAGGHKVGLALELEA TTM1I7L TT Literature-reported TTM1I7L KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa05012:Parkinson's disease; hsa05016:Huntington's disease; hsa05166:HTLV-I infection TTYRP0M ID TTYRP0M TTYRP0M TN Voltage-gated calcium channel alpha Cav2.3 (CACNA1E) TTYRP0M UP Q15878 TTYRP0M UC CAC1E_HUMAN TTYRP0M BC Voltage-gated ion channel TTYRP0M SN Voltage-gated calcium channel subunit alpha Cav2.3; Voltage-gated calcium channel alpha subunit Cav2.3; Voltage-dependent R-type calcium channel subunit alpha-1E; Voltage-dependent R-type calcium channel; R-type voltage-gated calcium channel; Class E voltage-gated calcium channel; Calcium channel, Ltype, alpha-1 polypeptide, isoform 6; Calcium channel, L type, alpha-1 polypeptide, isoform 6; CACNL1A6; CACH6; Brain calcium channel II; BII TTYRP0M GN CACNA1E TTYRP0M FC The isoform alpha-1E gives rise to R-type calcium currents. R-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by nickel. They are however insensitive to dihydropyridines (DHP). Calcium channels containing alpha-1E subunit could be involved in the modulation of firing patterns of neurons which is important for information processing. Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. TTYRP0M PD 3BXL TTYRP0M SQ MARFGEAVVARPGSGDGDSDQSRNRQGTPVPASGQAAAYKQTKAQRARTMALYNPIPVRQNCFTVNRSLFIFGEDNIVRKYAKKLIDWPPFEYMILATIIANCIVLALEQHLPEDDKTPMSRRLEKTEPYFIGIFCFEAGIKIVALGFIFHKGSYLRNGWNVMDFIVVLSGILATAGTHFNTHVDLRTLRAVRVLRPLKLVSGIPSLQIVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYSGKLHRACFMNNSGILEGFDPPHPCGVQGCPAGYECKDWIGPNDGITQFDNILFAVLTVFQCITMEGWTTVLYNTNDALGATWNWLYFIPLIIIGSFFVLNLVLGVLSGEFAKERERVENRRAFMKLRRQQQIERELNGYRAWIDKAEEVMLAEENKNAGTSALEVLRRATIKRSRTEAMTRDSSDEHCVDISSVGTPLARASIKSAKVDGVSYFRHKERLLRISIRHMVKSQVFYWIVLSLVALNTACVAIVHHNQPQWLTHLLYYAEFLFLGLFLLEMSLKMYGMGPRLYFHSSFNCFDFGVTVGSIFEVVWAIFRPGTSFGISVLRALRLLRIFKITKYWASLRNLVVSLMSSMKSIISLLFLLFLFIVVFALLGMQLFGGRFNFNDGTPSANFDTFPAAIMTVFQILTGEDWNEVMYNGIRSQGGVSSGMWSAIYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEQEEEEAFNQKHALQKAKEVSPMSAPNMPSIERDRRRRHHMSMWEPRSSHLRERRRRHHMSVWEQRTSQLRKHMQMSSQEALNREEAPTMNPLNPLNPLSSLNPLNAHPSLYRRPRAIEGLALGLALEKFEEERISRGGSLKGDGGDRSSALDNQRTPLSLGQREPPWLARPCHGNCDPTQQEAGGGEAVVTFEDRARHRQSQRRSRHRRVRTEGKESSSASRSRSASQERSLDEAMPTEGEKDHELRGNHGAKEPTIQEERAQDLRRTNSLMVSRGSGLAGGLDEADTPLVLPHPELEVGKHVVLTEQEPEGSSEQALLGNVQLDMGRVISQSEPDLSCITANTDKATTESTSVTVAIPDVDPLVDSTVVHISNKTDGEASPLKEAEIREDEEEVEKKKQKKEKRETGKAMVPHSSMFIFSTTNPIRRACHYIVNLRYFEMCILLVIAASSIALAAEDPVLTNSERNKVLRYFDYVFTGVFTFEMVIKMIDQGLILQDGSYFRDLWNILDFVVVVGALVAFALANALGTNKGRDIKTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVTSLKNVFNILIVYKLFMFIFAVIAVQLFKGKFFYCTDSSKDTEKECIGNYVDHEKNKMEVKGREWKRHEFHYDNIIWALLTLFTVSTGEGWPQVLQHSVDVTEEDRGPSRSNRMEMSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKMMEECSLEKNERACIDFAISAKPLTRYMPQNRHTFQYRVWHFVVSPSFEYTIMAMIALNTVVLMMKYYSAPCTYELALKYLNIAFTMVFSLECVLKVIAFGFLNYFRDTWNIFDFITVIGSITEIILTDSKLVNTSGFNMSFLKLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIKLDEESHINRHNNFRSFFGSLMLLFRSATGEAWQEIMLSCLGEKGCEPDTTAPSGQNENERCGTDLAYVYFVSFIFFCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFVRVWAEYDRAACGRIHYTEMYEMLTLMSPPLGLGKRCPSKVAYKRLVLMNMPVAEDMTVHFTSTLMALIRTALDIKIAKGGADRQQLDSELQKETLAIWPHLSQKMLDLLVPMPKASDLTVGKIYAAMMIMDYYKQSKVKKQRQQLEEQKNAPMFQRMEPSSLPQEIIANAKALPYLQQDPVSGLSGRSGYPSMSPLSPQDIFQLACMDPADDGQFQERQSLEPEVSELKSVQPSNHGIYLPSDTQEHAGSGRASSMPRLTVDPQVVTDPSSMRRSFSTIRDKRSNSSWLEEFSMERSSENTYKSRRRSYHSSLRLSAHRLNSDSGHKSDTHRSGGRERGRSKERKHLLSPDVSRCNSEERGTQADWESPERRQSRSPSEGRSQTPNRQGTGSLSESSIPSVSDTSTPRRSRRQLPPVPPKPRPLLSYSSLIRHAGSISPPADGSEEGSPLTSQALESNNACLTESSNSPHPQQSQHASPQRYISEPYLALHEDSHASDCGEEETLTFEAAVATSLGRSNTIGSAPPLRHSWQMPNGHYRRRRRGGPGPGMMCGAVNNLLSDTEEDDKC TTYRP0M TT Literature-reported TTYRP0M FM Calcium channel TTYRP0M KE hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04930:Type II diabetes mellitus TTQZFTH ID TTQZFTH TTQZFTH TN Voltage-gated calcium channel alpha Cav3.3 (CACNA1I) TTQZFTH UP Q9P0X4 TTQZFTH UC CAC1I_HUMAN TTQZFTH BC Voltage-gated ion channel TTQZFTH SN Voltage-gated calcium channel subunit alpha Cav3.3; Voltage-dependent T-type calcium channel subunit alpha-1I; KIAA1120; Ca(v)3.3 TTQZFTH GN CACNA1I TTQZFTH FC Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. This channel gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group and are strongly blocked by nickel and mibefradil. A particularity of this type of channels is an opening at quite negative potentials, and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes. Gates in voltage ranges similar to, but higher than alpha 1G or alpha 1H (By similarity). TTQZFTH SQ MAESASPPSSSAAAPAAEPGVTTEQPGPRSPPSSPPGLEEPLDGADPHVPHPDLAPIAFFCLRQTTSPRNWCIKMVCNPWFECVSMLVILLNCVTLGMYQPCDDMDCLSDRCKILQVFDDFIFIFFAMEMVLKMVALGIFGKKCYLGDTWNRLDFFIVMAGMVEYSLDLQNINLSAIRTVRVLRPLKAINRVPSMRILVNLLLDTLPMLGNVLLLCFFVFFIFGIIGVQLWAGLLRNRCFLEENFTIQGDVALPPYYQPEEDDEMPFICSLSGDNGIMGCHEIPPLKEQGRECCLSKDDVYDFGAGRQDLNASGLCVNWNRYYNVCRTGSANPHKGAINFDNIGYAWIVIFQVITLEGWVEIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQREHRLMLEQRQRYLSSSTVASYAEPGDCYEEIFQYVCHILRKAKRRALGLYQALQSRRQALGPEAPAPAKPGPHAKEPRHYHGKTKGQGDEGRHLGSRHCQTLHGPASPGNDHSGRELCPQHSPLDATPHTLVQPIPATLASDPASCPCCQHEDGRRPSGLGSTDSGQEGSGSGSSAGGEDEADGDGARSSEDGASSELGKEEEEEEQADGAVWLCGDVWRETRAKLRGIVDSKYFNRGIMMAILVNTVSMGIEHHEQPEELTNILEICNVVFTSMFALEMILKLAAFGLFDYLRNPYNIFDSIIVIISIWEIVGQADGGLSVLRTFRLLRVLKLVRFMPALRRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHIFGCKFSLRTDTGDTVPDRKNFDSLLWAIVTVFQILTQEDWNVVLYNGMASTSPWASLYFVALMTFGNYVLFNLLVAILVEGFQAEGDANRSYSDEDQSSSNIEEFDKLQEGLDSSGDPKLCPIPMTPNGHLDPSLPLGGHLGPAGAAGPAPRLSLQPDPMLVALGSRKSSVMSLGRMSYDQRSLSSSRSSYYGPWGRSAAWASRRSSWNSLKHKPPSAEHESLLSAERGGGARVCEVAADEGPPRAAPLHTPHAHHIHHGPHLAHRHRHHRRTLSLDNRDSVDLAELVPAVGAHPRAAWRAAGPAPGHEDCNGRMPSIAKDVFTKMGDRGDRGEDEEEIDYTLCFRVRKMIDVYKPDWCEVREDWSVYLFSPENRFRVLCQTIIAHKLFDYVVLAFIFLNCITIALERPQIEAGSTERIFLTVSNYIFTAIFVGEMTLKVVSLGLYFGEQAYLRSSWNVLDGFLVFVSIIDIVVSLASAGGAKILGVLRVLRLLRTLRPLRVISRAPGLKLVVETLISSLKPIGNIVLICCAFFIIFGILGVQLFKGKFYHCLGVDTRNITNRSDCMAANYRWVHHKYNFDNLGQALMSLFVLASKDGWVNIMYNGLDAVAVDQQPVTNHNPWMLLYFISFLLIVSFFVLNMFVGVVVENFHKCRQHQEAEEARRREEKRLRRLEKKRRKAQRLPYYATYCHTRLLIHSMCTSHYLDIFITFIICLNVVTMSLEHYNQPTSLETALKYCNYMFTTVFVLEAVLKLVAFGLRRFFKDRWNQLDLAIVLLSVMGITLEEIEINAALPINPTIIRIMRVLRIARVLKLLKMATGMRALLDTVVQALPQVGNLGLLFMLLFFIYAALGVELFGKLVCNDENPCEGMSRHATFENFGMAFLTLFQVSTGDNWNGIMKDTLRDCTHDERSCLSSLQFVSPLYFVSFVLTAQFVLINVVVAVLMKHLDDSNKEAQEDAEMDAELELEMAHGLGPGPRLPTGSPGAPGRGPGGAGGGGDTEGGLCRRCYSPAQENLWLDSVSLIIKDSLEGELTIIDNLSGSIFHHYSSPAGCKKCHHDKQEVQLAETEAFSLNSDRSSSILLGDDLSLEDPTACPPGRKDSKGELDPPEPMRVGDLGECFFPLSSTAVSPDPENFLCEMEEIPFNPVRSWLKHDSSQAPPSPFSPDASSPLLPMPAEFFHPAVSASQKGPEKGTGTGTLPKIALQGSWASLRSPRVNCTLLRQATGSDTSLDASPSSSAGSLQTTLEDSLTLSDSPRRALGPPAPAPGPRAGLSPAARRRLSLRGRGLFSLRGLRAHQRSHSSGGSTSPGCTHHDSMDPSDEEGRGGAGGGGAGSEHSETLSSLSLTSLFCPPPPPPAPGLTPARKFSSTSSLAAPGRPHAAALAHGLARSPSWAADRSKDPPGRAPLPMGLGPLAPPPQPLPGELEPGDAASKRKR TTQZFTH TT Literature-reported TTQZFTH KE rno04010:MAPK signaling pathway; rno04020:Calcium signaling pathway; rno04713:Circadian entrainment TTU8P3M ID TTU8P3M TTU8P3M TN Voltage-gated calcium channel alpha-2/delta-2 (CACNA2D2) TTU8P3M UP Q9NY47 TTU8P3M UC CA2D2_HUMAN TTU8P3M BC Voltage-gated ion channel TTU8P3M SN Voltage-gated calcium channel subunit alpha-2/delta-2; Voltage-dependent calcium channel subunit delta-2; Voltage-dependent calcium channel subunit alpha-2-2; CACNA2D2 TTU8P3M GN CACNA2D2 TTU8P3M FC The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) and possibly T-type (CACNA1G). Overexpression induces apoptosis. TTU8P3M SQ MAVPARTCGASRPGPARTARPWPGCGPHPGPGTRRPTSGPPRPLWLLLPLLPLLAAPGASAYSFPQQHTMQHWARRLEQEVDGVMRIFGGVQQLREIYKDNRNLFEVQENEPQKLVEKVAGDIESLLDRKVQALKRLADAAENFQKAHRWQDNIKEEDIVYYDAKADAELDDPESEDVERGSKASTLRLDFIEDPNFKNKVNYSYAAVQIPTDIYKGSTVILNELNWTEALENVFMENRRQDPTLLWQVFGSATGVTRYYPATPWRAPKKIDLYDVRRRPWYIQGASSPKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPVSCFTHLVQANVRNKKVFKEAVQGMVAKGTTGYKAGFEYAFDQLQNSNITRANCNKMIMMFTDGGEDRVQDVFEKYNWPNRTVRVFTFSVGQHNYDVTPLQWMACANKGYYFEIPSIGAIRINTQEYLDVLGRPMVLAGKEAKQVQWTNVYEDALGLGLVVTGTLPVFNLTQDGPGEKKNQLILGVMGIDVALNDIKRLTPNYTLGANGYVFAIDLNGYVLLHPNLKPQTTNFREPVTLDFLDAELEDENKEEIRRSMIDGNKGHKQIRTLVKSLDERYIDEVTRNYTWVPIRSTNYSLGLVLPPYSTFYLQANLSDQILQVKLPISKLKDFEFLLPSSFESEGHVFIAPREYCKDLNASDNNTEFLKNFIELMEKVTPDSKQCNNFLLHNLILDTGITQQLVERVWRDQDLNTYSLLAVFAATDGGITRVFPNKAAEDWTENPEPFNASFYRRSLDNHGYVFKPPHQDALLRPLELENDTVGILVSTAVELSLGRRTLRPAVVGVKLDLEAWAEKFKVLASNRTHQDQPQKCGPNSHCEMDCEVNNEDLLCVLIDDGGFLVLSNQNHQWDQVGRFFSEVDANLMLALYNNSFYTRKESYDYQAACAPQPPGNLGAAPRGVFVPTVADFLNLAWWTSAAAWSLFQQLLYGLIYHSWFQADPAEAEGSPETRESSCVMKQTQYYFGSVNASYNAIIDCGNCSRLFHAQRLTNTNLLFVVAEKPLCSQCEAGRLLQKETHSDGPEQCELVQRPRYRRGPHICFDYNATEDTSDCGRGASFPPSLGVLVSLQLLLLLGLPPRPQPQVLVHASRRL TTU8P3M TT Literature-reported TTU8P3M KE hsa04010:MAPK signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04921:Oxytocin signaling pathway; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTU8P3M RC R-HSA-112308:Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels; R-HSA-400042:Adrenaline,noradrenaline inhibits insulin secretion; R-HSA-422356:Regulation of insulin secretion TTN7T29 ID TTN7T29 TTN7T29 TN Voltage-gated calcium channel alpha-2/delta-3 (CACNA2D3) TTN7T29 UP Q8IZS8 TTN7T29 UC CA2D3_HUMAN TTN7T29 BC Voltage-gated ion channel TTN7T29 SN Voltage-gated calcium channel subunit alpha-2/delta-3; Voltage-dependent calcium channel subunit delta-3; Voltage-dependent calcium channel subunit alpha-2-3; CACNA2D3 TTN7T29 GN CACNA2D3 TTN7T29 FC The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) but not T-type (CACNA1G). TTN7T29 SQ MAGPGSPRRASRGASALLAAALLYAALGDVVRSEQQIPLSVVKLWASAFGGEIKSIAAKYSGSQLLQKKYKEYEKDVAIEEIDGLQLVKKLAKNMEEMFHKKSEAVRRLVEAAEEAHLKHEFDADLQYEYFNAVLINERDKDGNFLELGKEFILAPNDHFNNLPVNISLSDVQVPTNMYNKDPAIVNGVYWSESLNKVFVDNFDRDPSLIWQYFGSAKGFFRQYPGIKWEPDENGVIAFDCRNRKWYIQAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNEELHYVEPCLNGTLVQADRTNKEHFREHLDKLFAKGIGMLDIALNEAFNILSDFNHTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTYLIGREAAFADNLKWMACANKGFFTQISTLADVQENVMEYLHVLSRPKVIDQEHDVVWTEAYIDSTLPQAQKLTDDQGPVLMTTVAMPVFSKQNETRSKGILLGVVGTDVPVKELLKTIPKYKLGIHGYAFAITNNGYILTHPELRLLYEEGKKRRKPNYSSVDLSEVEWEDRDDVLRNAMVNRKTGKFSMEVKKTVDKGKRVLVMTNDYYYTDIKGTPFSLGVALSRGHGKYFFRGNVTIEEGLHDLEHPDVSLADEWSYCNTDLHPEHRHLSQLEAIKLYLKGKEPLLQCDKELIQEVLFDAVVSAPIEAYWTSLALNKSENSDKGVEVAFLGTRTGLSRINLFVGAEQLTNQDFLKAGDKENIFNADHFPLWYRRAAEQIPGSFVYSIPFSTGPVNKSNVVTASTSIQLLDERKSPVVAAVGIQMKLEFFQRKFWTASRQCASLDGKCSISCDDETVNCYLIDNNGFILVSEDYTQTGDFFGEIEGAVMNKLLTMGSFKRITLYDYQAMCRANKESSDGAHGLLDPYNAFLSAVKWIMTELVLFLVEFNLCSWWHSDMTAKAQKLKQTLEPCDTEYPAFVSERTIKETTGNIACEDCSKSFVIQQIPSSNLFMVVVDSSCLCESVAPITMAPIEIRYNESLKCERLKAQKIRRRPESCHGFHPEENARECGGAPSLQAQTVLLLLPLLLMLFSR TTN7T29 TT Literature-reported TTN7T29 KE hsa04010:MAPK signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04921:Oxytocin signaling pathway; hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy TTN7T29 RC R-HSA-112308:Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels TTS3DIK ID TTS3DIK TTS3DIK TN Voltage-gated potassium channel Kv1.1 (KCNA1) TTS3DIK UP Q09470 TTS3DIK UC KCNA1_HUMAN TTS3DIK BC Voltage-gated ion channel TTS3DIK SN Voltagegated potassium channel subunit Kv1.1; Voltagegated potassium channel HBK1; Voltagegated K(+) channel HuKI; Potassium voltagegated channel subfamily A member 1; KCNA1 TTS3DIK GN KCNA1 TTS3DIK FC Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the kidney (PubMed:19903818). Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability (PubMed:17156368). Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:19912772). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:12077175, PubMed:17156368). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels (PubMed:12077175, PubMed:17156368). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA1 forms a delayed-rectifier potassium channel that opens inresponse to membrane depolarization, followed by slow spontaneous channel closure (PubMed:19912772, PubMed:19968958, PubMed:19307729, PubMed:19903818). In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (PubMed:17156368). Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability. Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacemaking and regulate the output of deep cerebellar nuclear neurons. May function as down- stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons. May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) release. Plays a role in regulating the generation of action potentials and preventing hyperexcitability in myelinated axons of the vagus nerve, and thereby contributes to the regulation of heart contraction. Required for normal neuromuscular responses (PubMed:11026449, PubMed:17136396). Regulates the frequency of neuronal action potential firing in response to mechanical stimuli, and plays a role in the perception of pain caused by mechanical stimuli,but does not play a role in the perception of pain due to heat stimuli. Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception. The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine. Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain. Plays a role in the reabsorption of Mg(2+) in the distal convoluted tubules in the kidney and in magnesium ion homeostasis, probably via its effect on the membrane potential (PubMed:23903368, PubMed:19307729). TTS3DIK PD 2AFL TTS3DIK SQ MTVMSGENVDEASAAPGHPQDGSYPRQADHDDHECCERVVINISGLRFETQLKTLAQFPNTLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDMFSEEIKFYELGEEAMEKFREDEGFIKEEERPLPEKEYQRQVWLLFEYPESSGPARVIAIVSVMVILISIVIFCLETLPELKDDKDFTGTVHRIDNTTVIYNSNIFTDPFFIVETLCIIWFSFELVVRFFACPSKTDFFKNIMNFIDIVAIIPYFITLGTEIAEQEGNQKGEQATSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEAEEAESHFSSIPDAFWWAVVSMTTVGYGDMYPVTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQLLHVSSPNLASDSDLSRRSSSTMSKSEYMEIEEDMNNSIAHYRQVNIRTANCTTANQNCVNKSKLLTDV TTS3DIK TT Literature-reported TTS3DIK RC R-HSA-1296072:Voltage gated Potassium channels TTPXI3S ID TTPXI3S TTPXI3S TN Voltage-gated potassium channel Kv7.2 (KCNQ2) TTPXI3S UP O43526 TTPXI3S UC KCNQ2_HUMAN TTPXI3S BC Voltage-gated ion channel TTPXI3S SN Voltage-gated potassium channel subunit Kv7.2; Neuroblastoma-specific potassium channel alpha subunit KvLQT2; Neuroblastoma-specific potassium channel KQT-like 2; KQT-like 2; KCNQ2; K+ channel KCNQ2 TTPXI3S GN KCNQ2 TTPXI3S FC Probably importantin the regulation of neuronal excitability. Associates with kcnq3 to form a potassium channel with essentially identical properties to the channel underlying the native m-current. TTPXI3S PD 6FEH; 6FEG; 5J03 TTPXI3S SQ MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCRGPLCGCCPGRSSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGSLVRIPPPPAHERSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGESDTDSDLCTPCGPPPRSATGEGPFGDVGWAGPRK TTPXI3S TT Literature-reported TTPXI3S KE hsa04725:Cholinergic synapse TTPXI3S RC R-HSA-1296072:Voltage gated Potassium channels; R-HSA-445095:Interaction between L1 and Ankyrins TTRP74I ID TTRP74I TTRP74I TN WEE1 messenger RNA (WEE1 mRNA) TTRP74I UP P30291 TTRP74I UC WEE1_HUMAN TTRP74I BC mRNA target TTRP74I SN Wee1A kinase (mRNA); WEE1hu (mRNA) TTRP74I GN WEE1 TTRP74I FC Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation. Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. TTRP74I EC EC 2.7.10.2 TTRP74I PD 5VDA; 5VD9; 5VD8; 5VD7; 5VD5 TTRP74I SQ MSFLSRQQPPPPRRAGAACTLRQKLIFSPCSDCEEEEEEEEEEGSGHSTGEDSAFQEPDSPLPPARSPTEPGPERRRSPGPAPGSPGELEEDLLLPGACPGADEAGGGAEGDSWEEEGFGSSSPVKSPAAPYFLGSSFSPVRCGGPGDASPRGCGARRAGEGRRSPRPDHPGTPPHKTFRKLRLFDTPHTPKSLLSKARGIDSSSVKLRGSSLFMDTEKSGKREFDVRQTPQVNINPFTPDSLLLHSSGQCRRRKRTYWNDSCGEDMEASDYELEDETRPAKRITITESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYFSAWAEDDHMLIQNEYCNGGSLADAISENYRIMSYFKEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDDWASNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIPQVLSQEFTELLKVMIHPDPERRPSAMALVKHSVLLSASRKSAEQLRIELNAEKFKNSLLQKELKKAQMAKAAAEERALFTDRMATRSTTQSNRTSRLIGKKMNRSVSLTIY TTRP74I TT Literature-reported TTRP74I FM mRNA target TTLZXI0 ID TTLZXI0 TTLZXI0 TN Xaa-Pro dipeptidase (PEPD) TTLZXI0 UP P12955 TTLZXI0 UC PEPD_HUMAN TTLZXI0 BC Peptidase TTLZXI0 SN X-Pro dipeptidase; Proline dipeptidase; Prolidase; PEPD; Imidodipeptidase TTLZXI0 GN PEPD TTLZXI0 FC Splits dipeptides with a prolyl or hydroxyprolyl residuein the carboxyl terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen. TTLZXI0 EC EC 3.4.13.9 TTLZXI0 PD 6H2Q; 6H2P; 5MC5; 5MC4; 5MC3 TTLZXI0 SQ MAAATGPSFWLGNETLKVPLALFALNRQRLCERLRKNPAVQAGSIVVLQGGEETQRYCTDTGVLFRQESFFHWAFGVTEPGCYGVIDVDTGKSTLFVPRLPASHATWMGKIHSKEHFKEKYAVDDVQYVDEIASVLTSQKPSVLLTLRGVNTDSGSVCREASFDGISKFEVNNTILHPEIVECRVFKTDMELEVLRYTNKISSEAHREVMKAVKVGMKEYELESLFEHYCYSRGGMRHSSYTCICGSGENSAVLHYGHAGAPNDRTIQNGDMCLFDMGGEYYCFASDITCSFPANGKFTADQKAVYEAVLRSSRAVMGAMKPGVWWPDMHRLADRIHLEELAHMGILSGSVDAMVQAHLGAVFMPHGLGHFLGIDVHDVGGYPEGVERIDEPGLRSLRTARHLQPGMVLTVEPGIYFIDHLLDEALADPARASFLNREVLQRFRGFGGVRIEEDVVVTDSGIELLTCVPRTVEEIEACMAGCDKAFTPFSGPK TTLZXI0 TT Literature-reported TTCB9KW ID TTCB9KW TTCB9KW TN X-ray repair cross-complementing 5 (Ku80) TTCB9KW UP P13010 TTCB9KW UC XRCC5_HUMAN TTCB9KW BC Acid anhydride hydrolase TTCB9KW SN X-ray repair cross-complementing protein 5; X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining); Thyroid-lupus autoantigen; TLAA; Nuclear factor IV; Lupus Ku autoantigen protein p86; Ku86; G22P2; DNA repair protein XRCC5; CTCBF; CTC85; CTC box-binding factor 85 kDa subunit; ATP-dependent DNA helicase II 80 kDa subunit; ATP-dependent DNA helicase 2 subunit 2; 86 kDa subunit of Ku antigen TTCB9KW GN XRCC5 TTCB9KW FC Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. Single-stranded DNA-dependent ATP-dependent helicase. TTCB9KW EC EC 3.6.4.- TTCB9KW PD 6ERH; 6ERG; 6ERF; 5Y3R; 3RZ9 TTCB9KW SQ MVRSGNKAAVVLCMDVGFTMSNSIPGIESPFEQAKKVITMFVQRQVFAENKDEIALVLFGTDGTDNPLSGGDQYQNITVHRHLMLPDFDLLEDIESKIQPGSQQADFLDALIVSMDVIQHETIGKKFEKRHIEIFTDLSSRFSKSQLDIIIHSLKKCDISLQFFLPFSLGKEDGSGDRGDGPFRLGGHGPSFPLKGITEQQKEGLEIVKMVMISLEGEDGLDEIYSFSESLRKLCVFKKIERHSIHWPCRLTIGSNLSIRIAAYKSILQERVKKTWTVVDAKTLKKEDIQKETVYCLNDDDETEVLKEDIIQGFRYGSDIVPFSKVDEEQMKYKSEGKCFSVLGFCKSSQVQRRFFMGNQVLKVFAARDDEAAAVALSSLIHALDDLDMVAIVRYAYDKRANPQVGVAFPHIKHNYECLVYVQLPFMEDLRQYMFSSLKNSKKYAPTEAQLNAVDALIDSMSLAKKDEKTDTLEDLFPTTKIPNPRFQRLFQCLLHRALHPREPLPPIQQHIWNMLNPPAEVTTKSQIPLSKIKTLFPLIEAKKKDQVTAQEIFQDNHEDGPTAKKLKTEQGGAHFSVSSLAEGSVTSVGSVNPAENFRVLVKQKKASFEEASNQLINHIEQFLDTNETPYFMKSIDCIRAFREEAIKFSEEQRFNNFLKALQEKVEIKQLNHFWEIVVQDGITLITKEEASGSSVTAEEAKKFLAPKDKPSGDTAAVFEEGGDVDDLLDMI TTCB9KW TT Literature-reported TTCB9KW FM Acid anhydrides hydrolase TT5W0IO ID TT5W0IO TT5W0IO TN Zinc finger protein A20 (TNFAIP3) TT5W0IO UP P21580 TT5W0IO UC TNAP3_HUMAN TT5W0IO BC Acyltransferase TT5W0IO SN Tumor necrosis factor, alpha-induced protein3; Tumor necrosis factor alpha-induced protein 3; TNF alpha-induced protein 3; Putative DNA-binding protein A20; Putative DNA binding protein A20; OTUD7C; OTU domain-containing protein 7C; A20 TT5W0IO GN TNFAIP3 TT5W0IO FC Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS-induced production of proinflammatory cytokines and IFN beta in LPS-tolerized macrophages. Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. TT5W0IO EC EC 2.3.2.- TT5W0IO PD 5V3P; 5V3B; 5LRX; 3ZJG; 3ZJF TT5W0IO SQ MAEQVLPQALYLSNMRKAVKIRERTPEDIFKPTNGIIHHFKTMHRYTLEMFRTCQFCPQFREIIHKALIDRNIQATLESQKKLNWCREVRKLVALKTNGDGNCLMHATSQYMWGVQDTDLVLRKALFSTLKETDTRNFKFRWQLESLKSQEFVETGLCYDTRNWNDEWDNLIKMASTDTPMARSGLQYNSLEEIHIFVLCNILRRPIIVISDKMLRSLESGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSHHFVPLVTLKDSGPEIRAVPLVNRDRGRFEDLKVHFLTDPENEMKEKLLKEYLMVIEIPVQGWDHGTTHLINAAKLDEANLPKEINLVDDYFELVQHEYKKWQENSEQGRREGHAQNPMEPSVPQLSLMDVKCETPNCPFFMSVNTQPLCHECSERRQKNQNKLPKLNSKPGPEGLPGMALGASRGEAYEPLAWNPEESTGGPHSAPPTAPSPFLFSETTAMKCRSPGCPFTLNVQHNGFCERCHNARQLHASHAPDHTRHLDPGKCQACLQDVTRTFNGICSTCFKRTTAEASSSLSTSLPPSCHQRSKSDPSRLVRSPSPHSCHRAGNDAPAGCLSQAARTPGDRTGTSKCRKAGCVYFGTPENKGFCTLCFIEYRENKHFAAASGKVSPTASRFQNTIPCLGRECGTLGSTMFEGYCQKCFIEAQNQRFHEAKRTEEQLRSSQRRDVPRTTQSTSRPKCARASCKNILACRSEELCMECQHPNQRMGPGAHRGEPAPEDPPKQRCRAPACDHFGNAKCNGYCNECFQFKQMYG TT5W0IO TT Literature-reported TT5W0IO FM Peptidase TTVMWLP ID TTVMWLP TTVMWLP TN Acid-sensing ion channel 2 (ASIC2) TTVMWLP UP Q16515 TTVMWLP UC ASIC2_HUMAN TTVMWLP BC Amiloride-sensitive sodium channel TTVMWLP SN Mammalian degenerin homolog; Brain sodium channel 1; BNaC1; BNC1; Amiloridesensitive cation channelneuronal 1; Amiloridesensitive cation channel1, neuronal; Amiloridesensitive brain sodium channel; Acidsensing ion channel 2; ASIC2 TTVMWLP GN ASIC2 TTVMWLP FC Cation channel with high affinityfor sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Li(+) and K(+). Generates a biphasic current with a fast inactivating and a slow sustained phase. Heteromeric channel assembly seems to modulate. TTVMWLP SQ MDLKESPSEGSLQPSSIQIFANTSTLHGIRHIFVYGPLTIRRVLWAVAFVGSLGLLLVESSERVSYYFSYQHVTKVDEVVAQSLVFPAVTLCNLNGFRFSRLTTNDLYHAGELLALLDVNLQIPDPHLADPSVLEALRQKANFKHYKPKQFSMLEFLHRVGHDLKDMMLYCKFKGQECGHQDFTTVFTKYGKCYMFNSGEDGKPLLTTVKGGTGNGLEIMLDIQQDEYLPIWGETEETTFEAGVKVQIHSQSEPPFIQELGFGVAPGFQTFVATQEQRLTYLPPPWGECRSSEMGLDFFPVYSITACRIDCETRYIVENCNCRMVHMPGDAPFCTPEQHKECAEPALGLLAEKDSNYCLCRTPCNLTRYNKELSMVKIPSKTSAKYLEKKFNKSEKYISENILVLDIFFEALNYETIEQKKAYEVAALLGDIGGQMGLFIGASILTILELFDYIYELIKEKLLDLLGKEEDEGSHDENVSTCDTMPNHSETISHTVNVPLQTTLGTLEEIAC TTVMWLP TT Literature-reported TTVMWLP KE hsa04742:Taste transduction; hsa04750:Inflammatory mediator regulation of TRP channels TTVMWLP RC R-HSA-2672351:Stimuli-sensing channels TTLGDIS ID TTLGDIS TTLGDIS TN Acid-sensing ion channel 3 (ASIC3) TTLGDIS UP Q9UHC3 TTLGDIS UC ASIC3_HUMAN TTLGDIS BC Amiloride-sensitive sodium channel TTLGDIS SN hTNaC1; hASIC3; Testis sodium channel 1; TNAC1; SLNAC1; Neuronal amiloride-sensitive cation channel 3; Amiloride-sensitive cation channel 3; ASIC3; ACCN3 TTLGDIS GN ASIC3 TTLGDIS FC Cation channel with high affinity for sodium, whichis gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties. TTLGDIS SQ MKPTSGPEEARRPASDIRVFASNCSMHGLGHVFGPGSLSLRRGMWAAAVVLSVATFLYQVAERVRYYREFHHQTALDERESHRLIFPAVTLCNINPLRRSRLTPNDLHWAGSALLGLDPAEHAAFLRALGRPPAPPGFMPSPTFDMAQLYARAGHSLDDMLLDCRFRGQPCGPENFTTIFTRMGKCYTFNSGADGAELLTTTRGGMGNGLDIMLDVQQEEYLPVWRDNEETPFEVGIRVQIHSQEEPPIIDQLGLGVSPGYQTFVSCQQQQLSFLPPPWGDCSSASLNPNYEPEPSDPLGSPSPSPSPPYTLMGCRLACETRYVARKCGCRMVYMPGDVPVCSPQQYKNCAHPAIDAMLRKDSCACPNPCASTRYAKELSMVRIPSRAAARFLARKLNRSEAYIAENVLALDIFFEALNYETVEQKKAYEMSELLGDIGGQMGLFIGASLLTILEILDYLCEVFRDKVLGYFWNRQHSQRHSSTNLLQEGLGSHRTQVPHLSLGPRPPTPPCAVTKTLSASHRTCYLVTQL TTLGDIS TT Literature-reported TTLGDIS KE hsa04750:Inflammatory mediator regulation of TRP channels TTLGDIS RC R-HSA-2672351:Stimuli-sensing channels TT2AFT6 ID TT2AFT6 TT2AFT6 TN Activated leukocyte cell adhesionmolecule (ALCAM) TT2AFT6 UP Q13740 TT2AFT6 UC CD166_HUMAN TT2AFT6 BC Basigin protein TT2AFT6 SN MEMD; CD166 antigen; CD166; Activated leukocyte cell adhesion molecule TT2AFT6 GN ALCAM TT2AFT6 FC Promotes T-cell activation and proliferation via its interactions with CD6. Contributes to the formation and maturation of the immunological synapse via its interactions with CD6. Mediates homotypic interactions with cells that express ALCAM. Required for normal hematopoietic stem cell engraftment in the bone marrow. Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction. Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions. Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation. Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM. Mediates outgrowth and pathfinding for retinal ganglion cell axons. Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts. TT2AFT6 PD 5A2F; 1KJC TT2AFT6 SQ MESKGASSCRLLFCLLISATVFRPGLGWYTVNSAYGDTIIIPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLNLSENYTLSISNARISDEKRFVCMLVTEDNVFEAPTIVKVFKQPSKPEIVSKALFLETEQLKKLGDCISEDSYPDGNITWYRNGKVLHPLEGAVVIIFKKEMDPVTQLYTMTSTLEYKTTKADIQMPFTCSVTYYGPSGQKTIHSEQAVFDIYYPTEQVTIQVLPPKNAIKEGDNITLKCLGNGNPPPEEFLFYLPGQPEGIRSSNTYTLTDVRRNATGDYKCSLIDKKSMIASTAITVHYLDLSLNPSGEVTRQIGDALPVSCTISASRNATVVWMKDNIRLRSSPSFSSLHYQDAGNYVCETALQEVEGLKKRESLTLIVEGKPQIKMTKKTDPSGLSKTIICHVEGFPKPAIQWTITGSGSVINQTEESPYINGRYYSKIIISPEENVTLTCTAENQLERTVNSLNVSAISIPEHDEADEISDENREKVNDQAKLIVGIVVGLLLAALVAGVVYWLYMKKSKTASKHVNKDLGNMEENKKLEENNHKTEA TT2AFT6 TT Clinical trial TTQCKWT ID TTQCKWT TTQCKWT TN Activating transcription factor 4 (ATF-4) TTQCKWT UP P18848 TTQCKWT UC ATF4_HUMAN TTQCKWT BC Basic leucine zipper bZIP TTQCKWT SN cAMPresponsive elementbinding protein 2; cAMPdependent transcription factor ATF4; cAMP-responsive element-binding protein 2; cAMP-dependent transcription factor ATF-4; Taxresponsive enhancer elementbinding protein 67; TaxREB67; Tax-responsive enhancer element-binding protein 67; TXREB; DNAbinding protein TAXREB67; DNA-binding protein TAXREB67; Cyclic AMPresponsive elementbinding protein 2; Cyclic AMPdependent transcription factor ATF4; Cyclic AMP-responsive element-binding protein 2; Cyclic AMP-dependent transcription factor ATF-4; CREB2; CREB-2 TTQCKWT GN ATF4 TTQCKWT FC Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production. It binds to a Tax-responsive enhancer element in the long terminal repeat of HTLV-I. Regulates the induction of DDIT3/CHOP and asparagine synthetase (ASNS) in response to endoplasmic reticulum (ER) stress. In concert with DDIT3/CHOP, activates the transcription of TRIB3 and promotes ER stress-induced neuronal apoptosis by regulating the transcriptional induction of BBC3/PUMA. Activates transcription of SIRT4. Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4. Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes. During ER stress response, activates the transcription of NLRP1, possibly in concert with other factors. Transcriptional activator. TTQCKWT PD 1CI6 TTQCKWT SQ MTEMSFLSSEVLVGDLMSPFDQSGLGAEESLGLLDDYLEVAKHFKPHGFSSDKAKAGSSEWLAVDGLVSPSNNSKEDAFSGTDWMLEKMDLKEFDLDALLGIDDLETMPDDLLTTLDDTCDLFAPLVQETNKQPPQTVNPIGHLPESLTKPDQVAPFTFLQPLPLSPGVLSSTPDHSFSLELGSEVDITEGDRKPDYTAYVAMIPQCIKEEDTPSDNDSGICMSPESYLGSPQHSPSTRGSPNRSLPSPGVLCGSARPKPYDPPGEKMVAAKVKGEKLDKKLKKMEQNKTAATRYRQKKRAEQEALTGECKELEKKNEALKERADSLAKEIQYLKDLIEEVRKARGKKRVP TTQCKWT TT Literature-reported TTPKHTZ ID TTPKHTZ TTPKHTZ TN Activin receptor type IB (ACVR1B) TTPKHTZ UP P36896 TTPKHTZ UC ACV1B_HUMAN TTPKHTZ BC Kinase TTPKHTZ SN Serine/threonine-protein kinase receptor R2; SKR2; Activin receptor-like kinase 4; Activin receptor type-1B; ALK4; ALK-4; ACVRLK4; ACTR-IB TTPKHTZ GN ACVR1B TTPKHTZ FC Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. ACVR1B also phosphorylates TDP2. Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). TTPKHTZ EC EC 2.7.11.30 TTPKHTZ SQ MAESAGASSFFPLVVLLLAGSGGSGPRGVQALLCACTSCLQANYTCETDGACMVSIFNLDGMEHHVRTCIPKVELVPAGKPFYCLSSEDLRNTHCCYTDYCNRIDLRVPSGHLKEPEHPSMWGPVELVGIIAGPVFLLFLIIIIVFLVINYHQRVYHNRQRLDMEDPSCEMCLSKDKTLQDLVYDLSTSGSGSGLPLFVQRTVARTIVLQEIIGKGRFGEVWRGRWRGGDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTIEGMIKLALSAASGLAHLHMEIVGTQGKPGIAHRDLKSKNILVKKNGMCAIADLGLAVRHDAVTDTIDIAPNQRVGTKRYMAPEVLDETINMKHFDSFKCADIYALGLVYWEIARRCNSGGVHEEYQLPYYDLVPSDPSIEEMRKVVCDQKLRPNIPNWWQSYEALRVMGKMMRECWYANGAARLTALRIKKTLSQLSVQEDVKI TTPKHTZ TT Patented-recorded TTYWEDQ ID TTYWEDQ TTYWEDQ TN Acylamino-acid-releasing enzyme (APEH) TTYWEDQ UP P13798 TTYWEDQ UC ACPH_HUMAN TTYWEDQ BC Peptidase TTYWEDQ SN Oxidized protein hydrolase; OPH; DNF15S2 protein; Acylpeptide hydrolase; Acylaminoacyl-peptidase; Acyl-peptide hydrolase; APH; APEH; AARE TTYWEDQ GN APEH TTYWEDQ FC This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N- acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser. TTYWEDQ EC EC 3.4.19.1 TTYWEDQ SQ MERQVLLSEPEEAAALYRGLSRQPALSAACLGPEVTTQYGGQYRTVHTEWTQRDLERMENIRFCRQYLVFHDGDSVVFAGPAGNSVETRGELLSRESPSGTMKAVLRKAGGTGPGEEKQFLEVWEKNRKLKSFNLSALEKHGPVYEDDCFGCLSWSHSETHLLYVAEKKRPKAESFFQTKALDVSASDDEIARLKKPDQAIKGDQFVFYEDWGENMVSKSIPVLCVLDVESGNISVLEGVPENVSPGQAFWAPGDAGVVFVGWWHEPFRLGIRFCTNRRSALYYVDLIGGKCELLSDDSLAVSSPRLSPDQCRIVYLQYPSLIPHHQCSQLCLYDWYTKVTSVVVDVVPRQLGENFSGIYCSLLPLGCWSADSQRVVFDSAQRSRQDLFAVDTQVGTVTSLTAGGSGGSWKLLTIDQDLMVAQFSTPSLPPTLKVGFLPSAGKEQSVLWVSLEEAEPIPDIHWGIRVLQPPPEQENVQYAGLDFEAILLQPGSPPDKTQVPMVVMPHGGPHSSFVTAWMLFPAMLCKMGFAVLLVNYRGSTGFGQDSILSLPGNVGHQDVKDVQFAVEQVLQEEHFDASHVALMGGSHGGFISCHLIGQYPETYRACVARNPVINIASMLGSTDIPDWCVVEAGFPFSSDCLPDLSVWAEMLDKSPIRYIPQVKTPLLLMLGQEDRRVPFKQGMEYYRALKTRNVPVRLLLYPKSTHALSEVEVESDSFMNAVLWLRTHLGS TTYWEDQ TT Literature-reported TTJETQC ID TTJETQC TTJETQC TN Acylglycerol kinase (AGK) TTJETQC UP Q53H12 TTJETQC UC AGK_HUMAN TTJETQC BC Kinase TTJETQC SN hAGK; Multisubstrate lipid kinase; Multiple substrate lipid kinase; MuLK; HsMuLK; Acylglycerol kinase, mitochondrial; AGK TTJETQC GN AGK TTJETQC FC Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Does not phosphorylate sphingosine. Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth. TTJETQC EC EC 2.7.1.107 TTJETQC SQ MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPTQ TTJETQC TT Literature-reported TT2EJXQ ID TT2EJXQ TT2EJXQ TN Acyloxyacyl hydrolase (neutrophil) TT2EJXQ UP P28039 TT2EJXQ UC AOAH_HUMAN TT2EJXQ SN Acyloxyacyl hydrolase TT2EJXQ GN AOAH TT2EJXQ FC Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides. By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (By similarity). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (By similarity). TT2EJXQ EC EC 3.1.1.77 TT2EJXQ PD 5W7C; 5W78 TT2EJXQ SQ MQSPWKILTVAPLFLLLSLQSSASPANDDQSRPSLSNGHTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEKLFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFCKQNTGQPLCHLYPLPKETWKFTLQKARQIVKKSPILKYSRSGSDICSLPVLAKICQKIKLAMEQSVPFKDVDSDKYSVFPTLRGYHWRGRDCNDSDESVYPGRRPNNWDVHQDSNCNGIWGVDPKDGVPYEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDSTVGIKEKSIYLRLWKRNHCNHRDYQNISRNGASSRNLKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPVPAMTTPEKLYSNVMQTLKHLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQLSNTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNEVALLLLADHFWKKVQLQWPQILGKENPFNPQIKQVFGDQGGH TT2EJXQ TT Literature-reported TTAJDQY ID TTAJDQY TTAJDQY TN ADAM metallopeptidase 30 (ADAM30) TTAJDQY UP Q9UKF2 TTAJDQY UC ADA30_HUMAN TTAJDQY BC Peptidase TTAJDQY SN Disintegrin and metalloproteinase domaincontaining protein 30; ADAM30 TTAJDQY GN ADAM30 TTAJDQY FC May be involved in spermatogenesis and fertilization. TTAJDQY EC EC 3.4.24.- TTAJDQY SQ MRSVQIFLSQCRLLLLLVPTMLLKSLGEDVIFHPEGEFDSYEVTIPEKLSFRGEVQGVVSPVSYLLQLKGKKHVLHLWPKRLLLPRHLRVFSFTEHGELLEDHPYIPKDCNYMGSVKESLDSKATISTCMGGLRGVFNIDAKHYQIEPLKASPSFEHVVYLLKKEQFGNQVCGLSDDEIEWQMAPYENKARLRDFPGSYKHPKYLELILLFDQSRYRFVNNNLSQVIHDAILLTGIMDTYFQDVRMRIHLKALEVWTDFNKIRVGYPELAEVLGRFVIYKKSVLNARLSSDWAHLYLQRKYNDALAWSFGKVCSLEYAGSVSTLLDTNILAPATWSAHELGHAVGMSHDEQYCQCRGRLNCIMGSGRTGFSNCSYISFFKHISSGATCLNNIPGLGYVLKRCGNKIVEDNEECDCGSTEECQKDRCCQSNCKLQPGANCSIGLCCHDCRFRPSGYVCRQEGNECDLAEYCDGNSSSCPNDVYKQDGTPCKYEGRCFRKGCRSRYMQCQSIFGPDAMEAPSECYDAVNLIGDQFGNCEITGIRNFKKCESANSICGRLQCINVETIPDLPEHTTIISTHLQAENLMCWGTGYHLSMKPMGIPDLGMINDGTSCGEGRVCFKKNCVNSSVLQFDCLPEKCNTRGVCNNRKNCHCMYGWAPPFCEEVGYGGSIDSGPPGLLRGAIPSSIWVVSIIMFRLILLILSVVFVFFRQVIGNHLKPKQEKMPLSKAKTEQEESKTKTVQEESKTKTGQEESEAKTGQEESKAKTGQEESKANIESKRPKAKSVKKQKK TTAJDQY TT Literature-reported TTNB0ZK ID TTNB0ZK TTNB0ZK TN Adenine DNA glycosylase (MUTYH) TTNB0ZK UP Q9UIF7 TTNB0ZK UC MUTYH_HUMAN TTNB0ZK SN hMYH; MutY homolog; MYH TTNB0ZK GN MUTYH TTNB0ZK FC Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase activities. TTNB0ZK EC EC 3.2.2.31 TTNB0ZK PD 3N5N; 1X51 TTNB0ZK SQ MTPLVSRLSRLWAIMRKPRAAVGSGHRKQAASQEGRQKHAKNNSQAKPSACDGMIAECPGAPAGLARQPEEVVLQASVSSYHLFRDVAEVTAFRGSLLSWYDQEKRDLPWRRRAEDEMDLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLLASGSLSGSPDVEECAPNTGQCHLCLPPSEPWDQTLGVVNFPRKASRKPPREESSATCVLEQPGALGAQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKALLQELQRWAGPLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFRVYQGQQPGTCMGSKRSQVSSPCSRKKPRMGQQVLDNFFRSHISTDAHSLNSAAQ TTNB0ZK TT Literature-reported TTN64VU ID TTN64VU TTN64VU TN Adenylate cyclase type 5 (AC5) TTN64VU UP O95622 TTN64VU UC ADCY5_HUMAN TTN64VU BC Phosphorus-oxygen lyase TTN64VU SN Adenylyl cyclase 5; Adenylate cyclase type V; ATP pyrophosphate-lyase 5; AC5 TTN64VU GN ADCY5 TTN64VU FC Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion. TTN64VU EC EC 4.6.1.1 TTN64VU SQ MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGAVTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRRGAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEGGEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVFTITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSPWPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADLLVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS TTN64VU TT Literature-reported TTXKA7D ID TTXKA7D TTXKA7D TN Adiponectin (ADIPOQ) TTXKA7D UP Q15848 TTXKA7D UC ADIPO_HUMAN TTXKA7D BC Adiponectin protein TTXKA7D SN Gelatin-binding protein; GBP28; ApM-1; Adipose most abundant gene transcript 1 protein; Adipose most abundant gene transcript 1; Adipocyte, C1q and collagen domain-containing protein; Adipocyte, C1q and collagen domain containingprotein; Adipocyte complement-related 30 kDa protein; APM1; ACRP30; ACDC; 30 kDa adipocyte complement-related protein TTXKA7D GN ADIPOQ TTXKA7D FC Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW. Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. TTXKA7D PD 4DOU TTXKA7D SQ MLLLGAVLLLLALPGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLYHDTN TTXKA7D TT Literature-reported TT70KXY ID TT70KXY TT70KXY TN ADP-ribosylation factor 1 (ARF1) TT70KXY UP P84077 TT70KXY UC ARF1_HUMAN TT70KXY BC Small GTPase TT70KXY SN PVNH8 TT70KXY GN ARF1 TT70KXY FC Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD). GTP-binding protein involved in protein trafficking among different compartments. TT70KXY PD 6FAE; 6DFF; 6D84; 6D83; 6CRI TT70KXY SQ MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK TT70KXY TT Literature-reported TT70KXY FM Small GTPase superfamily TTIDSFT ID TTIDSFT TTIDSFT TN ADP-ribosylation factor-like protein 2 (ARL2) TTIDSFT UP P36404 TTIDSFT UC ARL2_HUMAN TTIDSFT BC Small GTPase TTIDSFT SN ARFL2 TTIDSFT GN ARL2 TTIDSFT FC GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle. Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). TTIDSFT PD 3DOF; 3DOE TTIDSFT SQ MGLLTILKKMKQKERELRLLMLGLDNAGKTTILKKFNGEDIDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATLLIFANKQDLPGALSSNAIREVLELDSIRSHHWCIQGCSAVTGENLLPGIDWLLDDISSRIFTAD TTIDSFT TT Literature-reported TTIDSFT FM Small GTPase superfamily TTV14YH ID TTV14YH TTV14YH TN Adrenomedullin (ADM) TTV14YH UP P35318 TTV14YH UC ADML_HUMAN TTV14YH BC Adrenomedullin TTV14YH SN AM; ADM TTV14YH GN ADM TTV14YH FC AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels. TTV14YH PD 5V6Y; 4RWF; 2L7S; 2FLY TTV14YH SQ MKLVSVALMYLGSLAFLGADTARLDVASEFRKKWNKWALSRGKRELRMSSSYPTGLADVKAGPAQTLIRPQDMKGASRSPEDSSPDAARIRVKRYRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGYGRRRRRSLPEAGPGRTLVSSKPQAHGAPAPPSGSAPHFL TTV14YH TT Literature-reported TTM642F ID TTM642F TTM642F TN Adrenomedullin 2 (ADM2) TTM642F UP Q7Z4H4 TTM642F UC ADM2_HUMAN TTM642F BC Adrenomedullin TTM642F SN Intermedin; ADM2 TTM642F GN ADM2 TTM642F FC IMDL and IMDS may play a role as physiological regulators of gastrointestinal, cardiovascular bioactivities mediated by the CALCRL/RAMPs receptor complexes. Activates the cAMP-dependent pathway. TTM642F PD 6D1U TTM642F SQ MARIPTAALGCISLLCLQLPGSLSRSLGGDPRPVKPREPPARSPSSSLQPRHPAPRPVVWKLHRALQAQRGAGLAPVMGQPLRDGGRQHSGPRRHSGPRRTQAQLLRVGCVLGTCQVQNLSHRLWQLMGPAGRQDSAPVDPSSPHSYG TTM642F TT Literature-reported TTWHYC8 ID TTWHYC8 TTWHYC8 TN Airway trypsin-like protease (TMPRSS11D) TTWHYC8 UP O60235 TTWHYC8 UC TM11D_HUMAN TTWHYC8 BC Peptidase TTWHYC8 SN TMPRSS11D; Human airway trypsin-like protease; HAT TTWHYC8 GN TMPRSS11D TTWHYC8 FC May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Proteolytically cleaves and activates the human coronavirus 229E (HCoV-229E) spike glycoprotein which facilitate virus-cell membrane fusions; spike proteins are synthesized andmaintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. TTWHYC8 EC EC 3.4.21.- TTWHYC8 SQ MYRPARVTSTSRFLNPYVVCFIVVAGVVILAVTIALLVYFLAFDQKSYFYRSSFQLLNVEYNSQLNSPATQEYRTLSGRIESLITKTFKESNLRNQFIRAHVAKLRQDGSGVRADVVMKFQFTRNNNGASMKSRIESVLRQMLNNSGNLEINPSTEITSLTDQAAANWLINECGAGPDLITLSEQRILGGTEAEEGSWPWQVSLRLNNAHHCGGSLINNMWILTAAHCFRSNSNPRDWIATSGISTTFPKLRMRVRNILIHNNYKSATHENDIALVRLENSVTFTKDIHSVCLPAATQNIPPGSTAYVTGWGAQEYAGHTVPELRQGQVRIISNDVCNAPHSYNGAILSGMLCAGVPQGGVDACQGDSGGPLVQEDSRRLWFIVGIVSWGDQCGLPDKPGVYTRVTAYLDWIRQQTGI TTWHYC8 TT Literature-reported TTH2W9Y ID TTH2W9Y TTH2W9Y TN Aldosterone receptor (NR3C2) TTH2W9Y UP P08235 TTH2W9Y UC MCR_HUMAN TTH2W9Y SN MR TTH2W9Y GN NR3C2 TTH2W9Y FC Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels. TTH2W9Y PD 6GGG; 6GG8; 6GEV; 5MWY; 5MWP TTH2W9Y SQ METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNSTQGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYEQQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAVVKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPNVENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSPANINNSRCSVSSPSNTNNRSTLSSPAASTVGSICSPVNNAFSYTASGTSAGSSTLRDVVPSPDTQEKGAQEVPFPKTEEVESAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNSKINSDSSFSVPIKQESTKHSCSGTSFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGFDGNCEGSGFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSARDQSFQHLSSFPPVNTLVESWKSHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPSKICLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRLQKCLQAGMNLGARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEEGTTYIAPAKEPSVNTALVPQLSTISRALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKCPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAMLVEIISDQLPKVESGNAKPLYFHRK TTH2W9Y TT Literature-reported TTPQNAZ ID TTPQNAZ TTPQNAZ TN Alkaline phosphatase (ALPPL2) TTPQNAZ UP P10696 TTPQNAZ UC PPBN_HUMAN TTPQNAZ BC Phosphoric monoester hydrolase TTPQNAZ SN Placental alkaline phosphatase-like; PLAP-like; Germ cell alkaline phosphatase; GCAP; Alkaline phosphatase, placental-like; Alkaline phosphatase, germ cell type; Alkaline phosphatase Nagao isozyme; ALPPL; ALPG; ALP-1 TTPQNAZ GN ALPPL2 TTPQNAZ FC extracellular region, plasma membrane, alkaline phosphatase activity. TTPQNAZ EC EC 3.1.3.1 TTPQNAZ SQ MQGPWVLLLLGLRLQLSLGIIPVEEENPDFWNRQAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPETFLAMDRFPYVALSKTYSVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGAYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAKHQGARYVWNRTELLQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALLLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVLKDGARPDVTESESGSPEYRQQSAVPLDGETHAGEDVAVFARGPQAHLVHGVQEQTFIAHVMAFAACLEPYTACDLAPRAGTTDAAHPGPSVVPALLPLLAGTLLLLGTATAP TTPQNAZ TT Literature-reported TTPQNAZ FM Phosphoric monoester hydrolases TTLN1AP ID TTLN1AP TTLN1AP TN Alpha-methylacyl-CoA racemase (AMACR) TTLN1AP UP Q9UHK6 TTLN1AP UC AMACR_HUMAN TTLN1AP BC CaiB/BaiF CoA-transferase family TTLN1AP SN IBLi; 2-methylacyl-CoA racemase TTLN1AP GN AMACR TTLN1AP FC Racemization of 2-methyl-branched fatty acid CoA esters. Responsible for the conversion of pristanoyl-CoA and C27-bile acyl-CoAs to their (S)-stereoisomers. TTLN1AP EC EC 5.1.99.4 TTLN1AP SQ MALQGISVVELSGLAPGPFCAMVLADFGARVVRVDRPGSRYDVSRLGRGKRSLVLDLKQPRGAAVLRRLCKRSDVLLEPFRRGVMEKLQLGPEILQRENPRLIYARLSGFGQSGSFCRLAGHDINYLALSGVLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVIDANMVEGTAYLSSFLWKTQKLSLWEAPRGQNMLDGGAPFYTTYRTADGEFMAVGAIEPQFYELLIKGLGLKSDELPNQMSMDDWPEMKKKFADVFAEKTKAEWCQIFDGTDACVTPVLTFEEVVHHDHNKERGSFITSEEQDVSPRPAPLLLNTPAIPSFKRDPFIGEHTEEILEEFGFSREEIYQLNSDKIIESNKVKASL TTLN1AP TT Literature-reported TTWALY5 ID TTWALY5 TTWALY5 TN Angiopoietin-related protein 4 (ANGPTL4) TTWALY5 UP Q9BY76 TTWALY5 UC ANGL4_HUMAN TTWALY5 BC Fibrinogen protein TTWALY5 SN UNQ171/PRO197; PSEC0166; PP1158; PGAR; Hepatic fibrinogen/angiopoietin-related protein; HFARP; Angiopoietin-like protein PP1158; Angiopoietin-like protein 4; Angiopoietin-like 4; ARP4 TTWALY5 GN ANGPTL4 TTWALY5 FC May also play a role in regulating glucose homeostasis and insulin sensitivity. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro). Depending on context, may modulate tumor-related angiogenesis. Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. TTWALY5 PD 6EUB TTWALY5 SQ MSGAPTAGAALMLCAATAVLLSAQGGPVQSKSPRFASWDEMNVLAHGLLQLGQGLREHAERTRSQLSALERRLSACGSACQGTEGSTDLPLAPESRVDPEVLHSLQTQLKAQNSRIQQLFHKVAQQQRHLEKQHLRIQHLQSQFGLLDHKHLDHEVAKPARRKRLPEMAQPVDPAHNVSRLHRLPRDCQELFQVGERQSGLFEIQPQGSPPFLVNCKMTSDGGWTVIQRRHDGSVDFNRPWEAYKAGFGDPHGEFWLGLEKVHSITGDRNSRLAVQLRDWDGNAELLQFSVHLGGEDTAYSLQLTAPVAGQLGATTVPPSGLSVPFSTWDQDHDLRRDKNCAKSLSGGWWFGTCSHSNLNGQYFRSIPQQRQKLKKGIFWKTWRGRYYPLQATTMLIQPMAAEAAS TTWALY5 TT Literature-reported TTWALY5 FM Fibrinogen TT5C0UB ID TT5C0UB TT5C0UB TN Angiotensinogen (AGT) TT5C0UB UP P01019 TT5C0UB UC ANGT_HUMAN TT5C0UB BC Serpin protein TT5C0UB SN Serpin A8; SERPINA8 TT5C0UB GN AGT TT5C0UB FC Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. TT5C0UB PD 6I3I; 6I3F; 5XJM; 5M3Y; 5M3X TT5C0UB SQ MRKRAPQSEMAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVANPLSTA TT5C0UB TT Literature-reported TT5C0UB FM Serpin family TT4YANI ID TT4YANI TT4YANI TN Annexin A2 (ANXA2) TT4YANI UP P07355 TT4YANI UC ANXA2_HUMAN TT4YANI BC Annexin protein TT4YANI SN p36; Protein I; Placental anticoagulant protein IV; PAP-IV; Lipocortin II; LPC2D; Chromobindin-8; Calpactin-1 heavy chain; Calpactin I heavy chain; CAL1H; Annexin-2; Annexin II; ANX2L4; ANX2 TT4YANI GN ANXA2 TT4YANI FC It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9. Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. TT4YANI PD 5N7G; 5N7F; 5N7D; 5LQ2; 5LQ0 TT4YANI SQ MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD TT4YANI TT Literature-reported TT4YANI FM Annexin family TTSW16P ID TTSW16P TTSW16P TN Annexin A8 (ANXA8) TTSW16P UP P13928 TTSW16P UC ANXA8_HUMAN TTSW16P BC Annexin protein TTSW16P SN Vascular anticoagulant-beta; VAC-beta; Annexin-8; Annexin VIII; ANX8 TTSW16P GN ANXA8 TTSW16P FC This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. TTSW16P PD 1W45; 1W3W TTSW16P SQ MAWWKSWIEQEGVTVKSSSHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNTQRQQIAKSFKAQFGKDLTETLKSELSGKFERLIVALMYPPYRYEAKELHDAMKGLGTKEGVIIEILASRTKNQLREIMKAYEEDYGSSLEEDIQADTSGYLERILVCLLQGSRDDVSSFVDPGLALQDAQDLYAAGEKIRGTDEMKFITILCTRSATHLLRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTVVKCTQNLHSYFAERLYYAMKGAGTRDGTLIRNIVSRSEIDLNLIKCHFKKMYGKTLSSMIMEDTSGDYKNALLSLVGSDP TTSW16P TT Literature-reported TTB4UNG ID TTB4UNG TTB4UNG TN Antigen KI-67 messenger RNA (MKI67 mRNA) TTB4UNG UP P46013 TTB4UNG UC KI67_HUMAN TTB4UNG BC mRNA target TTB4UNG SN Proliferation marker protein Ki-67 (mRNA); Antigen identified by monoclonal antibody Ki-67 (mRNA); Antigen Ki67 (mRNA); Antigen KI-67 (mRNA) TTB4UNG GN MKI67 TTB4UNG FC Associates with the surface of the mitotic chromosome, the perichromosomal layer, and covers a substantial fraction of the chromosome surface. Prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility. Binds DNA, with a preference for supercoiled DNA and AT-rich DNA. Does not contribute to the internal structure of mitotic chromosomes. May play a role in chromatin organization. It is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in maintaining mitotic chromosomes dispersed. Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. TTB4UNG PD 5J28; 2AFF; 1R21 TTB4UNG SQ MWPTRRLVTIKRSGVDGPHFPLSLSTCLFGRGIECDIRIQLPVVSKQHCKIEIHEQEAILHNFSSTNPTQVNGSVIDEPVRLKHGDVITIIDRSFRYENESLQNGRKSTEFPRKIREQEPARRVSRSSFSSDPDEKAQDSKAYSKITEGKVSGNPQVHIKNVKEDSTADDSKDSVAQGTTNVHSSEHAGRNGRNAADPISGDFKEISSVKLVSRYGELKSVPTTQCLDNSKKNESPFWKLYESVKKELDVKSQKENVLQYCRKSGLQTDYATEKESADGLQGETQLLVSRKSRPKSGGSGHAVAEPASPEQELDQNKGKGRDVESVQTPSKAVGASFPLYEPAKMKTPVQYSQQQNSPQKHKNKDLYTTGRRESVNLGKSEGFKAGDKTLTPRKLSTRNRTPAKVEDAADSATKPENLSSKTRGSIPTDVEVLPTETEIHNEPFLTLWLTQVERKIQKDSLSKPEKLGTTAGQMCSGLPGLSSVDINNFGDSINESEGIPLKRRRVSFGGHLRPELFDENLPPNTPLKRGEAPTKRKSLVMHTPPVLKKIIKEQPQPSGKQESGSEIHVEVKAQSLVISPPAPSPRKTPVASDQRRRSCKTAPASSSKSQTEVPKRGGRKSGNLPSKRVSISRSQHDILQMICSKRRSGASEANLIVAKSWADVVKLGAKQTQTKVIKHGPQRSMNKRQRRPATPKKPVGEVHSQFSTGHANSPCTIIIGKAHTEKVHVPARPYRVLNNFISNQKMDFKEDLSGIAEMFKTPVKEQPQLTSTCHIAISNSENLLGKQFQGTDSGEEPLLPTSESFGGNVFFSAQNAAKQPSDKCSASPPLRRQCIRENGNVAKTPRNTYKMTSLETKTSDTETEPSKTVSTANRSGRSTEFRNIQKLPVESKSEETNTEIVECILKRGQKATLLQQRREGEMKEIERPFETYKENIELKENDEKMKAMKRSRTWGQKCAPMSDLTDLKSLPDTELMKDTARGQNLLQTQDHAKAPKSEKGKITKMPCQSLQPEPINTPTHTKQQLKASLGKVGVKEELLAVGKFTRTSGETTHTHREPAGDGKSIRTFKESPKQILDPAARVTGMKKWPRTPKEEAQSLEDLAGFKELFQTPGPSEESMTDEKTTKIACKSPPPESVDTPTSTKQWPKRSLRKADVEEEFLALRKLTPSAGKAMLTPKPAGGDEKDIKAFMGTPVQKLDLAGTLPGSKRQLQTPKEKAQALEDLAGFKELFQTPGHTEELVAAGKTTKIPCDSPQSDPVDTPTSTKQRPKRSIRKADVEGELLACRNLMPSAGKAMHTPKPSVGEEKDIIIFVGTPVQKLDLTENLTGSKRRPQTPKEEAQALEDLTGFKELFQTPGHTEEAVAAGKTTKMPCESSPPESADTPTSTRRQPKTPLEKRDVQKELSALKKLTQTSGETTHTDKVPGGEDKSINAFRETAKQKLDPAASVTGSKRHPKTKEKAQPLEDLAGLKELFQTPVCTDKPTTHEKTTKIACRSQPDPVDTPTSSKPQSKRSLRKVDVEEEFFALRKRTPSAGKAMHTPKPAVSGEKNIYAFMGTPVQKLDLTENLTGSKRRLQTPKEKAQALEDLAGFKELFQTRGHTEESMTNDKTAKVACKSSQPDPDKNPASSKRRLKTSLGKVGVKEELLAVGKLTQTSGETTHTHTEPTGDGKSMKAFMESPKQILDSAASLTGSKRQLRTPKGKSEVPEDLAGFIELFQTPSHTKESMTNEKTTKVSYRASQPDLVDTPTSSKPQPKRSLRKADTEEEFLAFRKQTPSAGKAMHTPKPAVGEEKDINTFLGTPVQKLDQPGNLPGSNRRLQTRKEKAQALEELTGFRELFQTPCTDNPTTDEKTTKKILCKSPQSDPADTPTNTKQRPKRSLKKADVEEEFLAFRKLTPSAGKAMHTPKAAVGEEKDINTFVGTPVEKLDLLGNLPGSKRRPQTPKEKAKALEDLAGFKELFQTPGHTEESMTDDKITEVSCKSPQPDPVKTPTSSKQRLKISLGKVGVKEEVLPVGKLTQTSGKTTQTHRETAGDGKSIKAFKESAKQMLDPANYGTGMERWPRTPKEEAQSLEDLAGFKELFQTPDHTEESTTDDKTTKIACKSPPPESMDTPTSTRRRPKTPLGKRDIVEELSALKQLTQTTHTDKVPGDEDKGINVFRETAKQKLDPAASVTGSKRQPRTPKGKAQPLEDLAGLKELFQTPICTDKPTTHEKTTKIACRSPQPDPVGTPTIFKPQSKRSLRKADVEEESLALRKRTPSVGKAMDTPKPAGGDEKDMKAFMGTPVQKLDLPGNLPGSKRWPQTPKEKAQALEDLAGFKELFQTPGTDKPTTDEKTTKIACKSPQPDPVDTPASTKQRPKRNLRKADVEEEFLALRKRTPSAGKAMDTPKPAVSDEKNINTFVETPVQKLDLLGNLPGSKRQPQTPKEKAEALEDLVGFKELFQTPGHTEESMTDDKITEVSCKSPQPESFKTSRSSKQRLKIPLVKVDMKEEPLAVSKLTRTSGETTQTHTEPTGDSKSIKAFKESPKQILDPAASVTGSRRQLRTRKEKARALEDLVDFKELFSAPGHTEESMTIDKNTKIPCKSPPPELTDTATSTKRCPKTRPRKEVKEELSAVERLTQTSGQSTHTHKEPASGDEGIKVLKQRAKKKPNPVEEEPSRRRPRAPKEKAQPLEDLAGFTELSETSGHTQESLTAGKATKIPCESPPLEVVDTTASTKRHLRTRVQKVQVKEEPSAVKFTQTSGETTDADKEPAGEDKGIKALKESAKQTPAPAASVTGSRRRPRAPRESAQAIEDLAGFKDPAAGHTEESMTDDKTTKIPCKSSPELEDTATSSKRRPRTRAQKVEVKEELLAVGKLTQTSGETTHTDKEPVGEGKGTKAFKQPAKRKLDAEDVIGSRRQPRAPKEKAQPLEDLASFQELSQTPGHTEELANGAADSFTSAPKQTPDSGKPLKISRRVLRAPKVEPVGDVVSTRDPVKSQSKSNTSLPPLPFKRGGGKDGSVTGTKRLRCMPAPEEIVEELPASKKQRVAPRARGKSSEPVVIMKRSLRTSAKRIEPAEELNSNDMKTNKEEHKLQDSVPENKGISLRSRRQNKTEAEQQITEVFVLAERIEINRNEKKPMKTSPEMDIQNPDDGARKPIPRDKVTENKRCLRSARQNESSQPKVAEESGGQKSAKVLMQNQKGKGEAGNSDSMCLRSRKTKSQPAASTLESKSVQRVTRSVKRCAENPKKAEDNVCVKKIRTRSHRDSEDI TTB4UNG TT Literature-reported TTB4UNG FM mRNA target TTGQA9W ID TTGQA9W TTGQA9W TN Apolipoprotein A-II (APOA2) TTGQA9W UP P02652 TTGQA9W UC APOA2_HUMAN TTGQA9W BC Apolipoprotein TTGQA9W SN Apolipoprotein A2; ApoA-II; Apo-AII TTGQA9W GN APOA2 TTGQA9W FC May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. TTGQA9W SQ MKLLAATVLLLTICSLEGALVRRQAKEPCVESLVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLSYFVELGTQPATQ TTGQA9W TT Literature-reported TTGQA9W FM Apolipoprotein TTGQA9W KE hsa03320:PPAR signaling pathway TTGQA9W RC R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-1989781:PPARA activates gene expression; R-HSA-975634:Retinoid metabolism and transport TTNC3WS ID TTNC3WS TTNC3WS TN Apolipoprotein A-IV (APOA4) TTNC3WS UP P06727 TTNC3WS UC APOA4_HUMAN TTNC3WS BC Apolipoprotein TTNC3WS SN Apolipoprotein A4; ApoAIV; APOA4 TTNC3WS GN APOA4 TTNC3WS FC May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons. TTNC3WS PD 3S84 TTNC3WS SQ MFLKAVVLTLALVAVAGARAEVSADQVATVMWDYFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYADQLRTQVSTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVEGHLSFLEKDLRDKVNSFFSTFKEKESQDKTLSLPELEQQQEQQQEQQQEQVQMLAPLES TTNC3WS TT Literature-reported TTTNMUF ID TTTNMUF TTTNMUF TN Apoptosis antigen ligand (CD178) TTTNMUF UP P48023 TTTNMUF UC TNFL6_HUMAN TTTNMUF BC Cytokine: tumor necrosis factor TTTNMUF SN Tumor necrosis factor ligand superfamily member 6; TNFSF6; FasL; Fas ligand; FAS antigen ligand; CD95L; CD95-L; CD95 ligand; CD178 antigen; CD178; APTL; APT1LG1 TTTNMUF GN FASLG TTTNMUF FC Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development. Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses. TNFRSF6/FAS-mediated apoptosis has also a role in the induction of peripheral tolerance. Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis. Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells. TTTNMUF PD 5L36; 5L19; 4MSV; 1BZI TTTNMUF SQ MQQPFNYPYPQIYWVDSSASSPWAPPGTVLPCPTSVPRRPGQRRPPPPPPPPPLPPPPPPPPLPPLPLPPLKKRGNHSTGLCLLVMFFMVLVALVGLGLGMFQLFHLQKELAELRESTSQMHTASSLEKQIGHPSPPPEKKELRKVAHLTGKSNSRSMPLEWEDTYGIVLLSGVKYKKGGLVINETGLYFVYSKVYFRGQSCNNLPLSHKVYMRNSKYPQDLVMMEGKMMSYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESQTFFGLYKL TTTNMUF TT Literature-reported TTTNMUF FM Cytokine: tumor necrosis factor TTFM7V0 ID TTFM7V0 TTFM7V0 TN Apoptosis regulator BAK (BAK) TTFM7V0 UP Q16611 TTFM7V0 UC BAK_HUMAN TTFM7V0 BC B-cell lymphoma Bcl-2 TTFM7V0 SN CDN1; Bcl2like protein 7; Bcl2L7; Bcl2-L-7; Bcl2 homologous antagonist/killer; Bcl-2-like protein 7; Bcl-2 homologous antagonist/killer TTFM7V0 GN BAK1 TTFM7V0 FC Upon arrival of cell death signals, promotes mitochondrial outer membrane (MOM) permeabilization by oligomerizing to form pores within the MOM. This releases apoptogenic factors into the cytosol, including cytochrome c, promoting the activation of caspase 9 which in turn processes and activates the effector caspases. Plays a role in the mitochondrial apoptosic process. TTFM7V0 PD 5VX1; 5VX0; 5VWZ; 5VWY; 5VWX TTFM7V0 SQ MASGQGPGPPRQECGEPALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNGPILNVLVVLGVVLLGQFVVRRFFKS TTFM7V0 TT Literature-reported TTFM7V0 FM Bcl-2 family TTG51ON ID TTG51ON TTG51ON TN APP messenger RNA (APP mRNA) TTG51ON UP P05067 TTG51ON UC A4_HUMAN TTG51ON BC mRNA target TTG51ON SN Vascular beta-amyloid (mRNA); Protease nexin-II (mRNA); PreA4 (mRNA); PN-II (mRNA); Cerebral vascular amyloidpeptide (mRNA); Cerebral vascular amyloid peptide (mRNA); CVAP (mRNA); Beta-amyloid peptide (mRNA); Amyloid-beta precursor protein (mRNA); Amyloid-beta A4 protein (mRNA); Amyloid precursor protein (mRNA); Amyloid beta precursor protein (mRNA); Alzheimer's disease amyloid protein (mRNA); Alzheimer disease amyloid protein (mRNA); APPI (mRNA); AD1 (mRNA); ABPP (mRNA); A4 (mRNA) TTG51ON GN APP TTG51ON FC Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. TTG51ON PD 6IYC; 6GFI; 6CO3; 5W3P; 5VZY TTG51ON SQ MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN TTG51ON TT Literature-reported TTG51ON FM mRNA target TTSF1KH ID TTSF1KH TTSF1KH TN Aquaporin-1 (AQP1) TTSF1KH UP P29972 TTSF1KH UC AQP1_HUMAN TTSF1KH BC Major intrinsic protein TTSF1KH SN Water channel protein for red blood cells and kidney proximal tubule; Urine water channel; CHIP28; Aquaporin-CHIP; AQP-1 TTSF1KH GN AQP1 TTSF1KH FC Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. TTSF1KH PD 4CSK; 1IH5; 1H6I; 1FQY TTSF1KH SQ MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK TTSF1KH TT Clinical trial TTNGCRK ID TTNGCRK TTNGCRK TN Aquaporin-7 (AQP7) TTNGCRK UP O14520 TTNGCRK UC AQP7_HUMAN TTNGCRK BC Major intrinsic protein TTNGCRK SN Aquaporin-7-like; Aquaporin adipose; Aquaglyceroporin-7; AQPap; AQP7L; AQP-7 TTNGCRK GN AQP7 TTNGCRK FC Forms a channel for water and glycerol. TTNGCRK SQ MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF TTNGCRK TT Literature-reported TTNGCRK KE hsa03320:PPAR signaling pathway; hsa04923:Regulation of lipolysis in adipocytes TT8V2KD ID TT8V2KD TT8V2KD TN Arginine carboxypeptidase (CPN1) TT8V2KD UP P15169 TT8V2KD UC CBPN_HUMAN TT8V2KD SN Serum carboxypeptidase N; SCPN; Plasma carboxypeptidase N; Lysine carboxypeptidase; Kininase-1; Carboxypeptidase N small subunit; Carboxypeptidase N polypeptide 1; Carboxypeptidase N catalytic chain; CPN; Anaphylatoxin inactivator; ACBP TT8V2KD GN CPN1 TT8V2KD FC Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation. TT8V2KD EC EC 3.4.17.3 TT8V2KD PD 2NSM TT8V2KD SQ MSDLLSVFLHLLLLFKLVAPVTFRHHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLPLPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTASTPTPDDKLFQKLAKVYSYAHGWMFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQVHQGIKGMVLDENYNNLANAVISVSGINHDVTSGDHGDYFRLLLPGIYTVSATAPGYDPETVTVTVGPAEPTLVNFHLKRSIPQVSPVRRAPSRRHGVRAKVQPQARKKEMEMRQLQRGPA TT8V2KD TT Literature-reported TT2BJ1X ID TT2BJ1X TT2BJ1X TN Astrocyte glutamine synthetase (GLUL) TT2BJ1X UP P15104 TT2BJ1X UC GLNA_HUMAN TT2BJ1X SN Palmitoyltransferase GLUL; Glutamine synthetase; Glutamate--ammonia ligase; GS; GLNS TT2BJ1X GN GLUL TT2BJ1X FC Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine. Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia (By similarity). Essential for proliferation of fetal skin fibroblasts. Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ. Plays a role in ribosomal 40S subunit biogenesis. TT2BJ1X EC EC 6.3.1.2 TT2BJ1X PD 2QC8; 2OJW TT2BJ1X SQ MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETGDEPFQYKN TT2BJ1X TT Literature-reported TTKZ7WY ID TTKZ7WY TTKZ7WY TN ATP-binding cassette transporter G5 (ABCG5) TTKZ7WY UP Q9H222 TTKZ7WY UC ABCG5_HUMAN TTKZ7WY BC ABC transporter TTKZ7WY SN Sterolin1; ATPbinding cassette subfamily G member 5; ABCG5 TTKZ7WY GN ABCG5 TTKZ7WY FC Transporter that appears to play an indispensable role in the selective transportof the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile. TTKZ7WY PD 5DO7 TTKZ7WY SQ MGDLSSLTPGGSMGLQVNRGSQSSLEGAPATAPEPHSLGILHASYSVSHRVRPWWDITSCRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTSVDTQSKEREIETSKRVQMIESAYKKSAICHKTLKNIERMKHLKTLPMVPFKTKDSPGVFSKLGVLLRRVTRNLVRNKLAVITRLLQNLIMGLFLLFFVLRVRSNVLKGAIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSVVALLSIAGVLVGSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEFYGLNFTCGSSNVSVTTNPMCAFTQGIQFIEKTCPGATSRFTMNFLILYSFIPALVILGIVVFKIRDHLISR TTKZ7WY TT Literature-reported TTTRNH6 ID TTTRNH6 TTTRNH6 TN Bacterial ATP-dependent Clp proteolytic protease (Bact clpP) TTTRNH6 UP Q5GS83 TTTRNH6 UC CLPP_WOLTR TTTRNH6 BC Peptidase TTTRNH6 SN clpP; Bact Endopeptidase Clp TTTRNH6 GN Bact clpP TTTRNH6 FC Cleaves peptides in various proteins ina process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. TTTRNH6 EC EC 3.4.21.92 TTTRNH6 SQ MTLIPIVIEQTSRGERAYDIYSRLVKERIIFVTGPVEDNMASVIVAQLLFLESENPDKDIYMYINSPGGVVTAGLSIYDTMQYIKPDVSTLCIGQAASMGSLLLAAGTEGKRYSLPHSRIMIHQPSGGYQGQATDIEIHANEILRVKRKLNQIYEKHTGNSLKKIEGMMERDKFMDPEEARRIGLIDRVIAERKDIKVENIKVEQKVG TTTRNH6 TT Literature-reported TTQ5J3T ID TTQ5J3T TTQ5J3T TN Bacterial Betaine aldehyde dehydrogenase (Bact betB) TTQ5J3T UP P17445 TTQ5J3T UC BETB_ECOLI TTQ5J3T BC Aldehyde/oxo donor oxidoreductase TTQ5J3T SN betB; BADH TTQ5J3T GN Bact betB TTQ5J3T FC Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid. It is highly specific for betaine and has a significantly higher affinity for NAD than for NADP. TTQ5J3T EC EC 1.2.1.8 TTQ5J3T SQ MSRMAEQQLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWASMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGVGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFGPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCSDDMTIVREEIFGPVMSILTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQVEMAKFQSIF TTQ5J3T TT Literature-reported TT0O4QL ID TT0O4QL TT0O4QL TN Bacterial Beta-ketoacyl-ACP synthase I (Bact fabB) TT0O4QL UP P0A954 TT0O4QL UC FABB_ECOL6 TT0O4QL BC Acyltransferase TT0O4QL SN fabB; KAS I; Condensing enzyme FabB; 3-oxoacyl-[acyl-carrier-protein] synthase I TT0O4QL GN Bact fabB TT0O4QL FC Catalyzes the condensation reactionof fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-acp. Specific for elongation from c-10 to unsaturated c-16 and c-18 fatty acids. TT0O4QL EC EC 2.3.1.41 TT0O4QL SQ MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAMRGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVMRKLKD TT0O4QL TT Literature-reported TTPL9SG ID TTPL9SG TTPL9SG TN Bacterial Botulinum toxin B (Bact botB) TTPL9SG UP P10844 TTPL9SG UC BXB_CLOBO TTPL9SG BC Peptidase TTPL9SG SN botB; Botulinum neurotoxin type B; Botulinum neurotoxin B heavy chain; BontoxilysinB; BoNT/B TTPL9SG GN Bact botB TTPL9SG FC Botulinum toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that cleaves the '76-Gln-|-Phe-77' bond of synaptobrevin-2. TTPL9SG PD 6G5K; 6G5G; 6G5F; 5VMR; 5VID TTPL9SG SQ MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNIAENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVKAPGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNYIENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVYEKQPAIKKIFTDENTIFQYLYSQTFPLDIRDISLTSSFDDALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDFVIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFENAFEIAGASILLEFIPELLIPVVGAFLLESYIDNKNKIIKTIDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYKALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLNEGINQAIDNINNFINGCSVSYLMKKMIPLAVEKLLDFDNTLKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLSIYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKLTSSANSKIRVTQNQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGWKISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGKLESNTDIKDIREVIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSEYLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYIGEKFIIRRKSNSQSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDSDEFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISKWYLKEVKRKPYNLKLGCNWQFIPKDEGWTE TTPL9SG TT Literature-reported TTSI0C6 ID TTSI0C6 TTSI0C6 TN Bacterial Class 1 lysyl-tRNA synthetase (Bact lysK) TTSI0C6 UP Q937U6 TTSI0C6 UC Q937U6_BORHE TTSI0C6 BC Carbon-oxygen ligase TTSI0C6 SN Class 1 lysyl-tRNA synthetase TTSI0C6 GN Bact lysK TTSI0C6 FC Catalyses the formation of lysyl-transfer RNA, Lys-tRNA(Lys), which then is ready to insert lysine into proteins. Only found in a few bacteria such as -proteobacteria. Functionally equivalent but structurally unrelated compared with class II LysRS. Requires tRNALys binding prior to aminoacyl-adenylate synthesis. TTSI0C6 EC EC 6.1.1.6 TTSI0C6 SQ DFYAKKIIEEKGEKEQYTVASGITPSGTVHIGNFREVISVDLVARALKDAGRNVRFIYSWDNYDVFRKVPKNMPNQELLTTHLRQAITRVPDTQTNQSSYARANEVEFEKYLPIVGIKPEFIDQSLKYMSSDYSSQIKFALDHKDEIEKVLNKYRTTKLADNWYPISIFCTKCNRDTTTIKNYNHCYSIEYCCECGNKESLDLRKTWAVKLPWRIDWPMRWKYENVDFEPAGKDHHSSGGSFDTSIEIVKIFGGTPPITFQYDFISIKGRGGKISSSSGDVGSLKDVLEIYTPEVTRFLFASTKPNTEFSISFDLDVIKIYEDYDKFERVYYGIDDIKENKKEAFKRIYELSQPKLPDKEIPYQIGFRHLSTICQIFEGDKDKIFKLLNDVKESQKAKLINKIECAINWIKKFAPEDFKFSLRYTFDNIEPLKDNNKQGVTQLLDFLKKDFNNITEKEIQDEIYNIARNNNIEPPLFFKQLYNILINKDKGPKLAGFIKIIGIKKFEEIVKHYI TTSI0C6 TT Literature-reported TTPS7KA ID TTPS7KA TTPS7KA TN Bacterial Dehydroquinate synthase (Bact aroB) TTPS7KA UP P07639 TTPS7KA UC AROB_ECOLI TTPS7KA BC Alpha-carbonic anhydrase TTPS7KA SN DHQS; 3-dehydroquinate synthase TTPS7KA GN Bact aroB TTPS7KA FC Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). TTPS7KA SQ MERIVVTLGERSYPITIASGLFNEPASFLPLKSGEQVMLVTNETLAPLYLDKVRGVLEQAGVNVDSVILPDGEQYKSLAVLDTVFTALLQKPHGRDTTLVALGGGVVGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVVDLDCLKTLPPRELASGLAEVIKYGIILDGAFFNWLEENLDALLRLDGPAMAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFSSAETQRIITLLKRAGLPVNGPREMSAQAYLPHMLRDKKVLAGEMRLILPLAIGKSEVRSGVSHELVLNAIADCQSA TTPS7KA TT Literature-reported TTVNA43 ID TTVNA43 TTVNA43 TN Bacterial Deoxy-D-manno-octulosonate 8-phosphate synthase (Bact kdsA) TTVNA43 UP P0A715 TTVNA43 UC KDSA_ECOLI TTVNA43 BC Alkyl aryl transferase TTVNA43 SN kdsA; Phospho-2-dehydro-3-deoxyoctonate aldolase; KDOPS; KDOP synthase; KDO8PS; KDO8P synthase; KDO8-P synthase; KDO-8-phosphate synthetase; 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase; 3-Deoxy-d-manno-2-octulosonate-8-phosphate synthase; 2-dehydro-3-deoxyphosphooctonate aldolase TTVNA43 GN Bact kdsA TTVNA43 FC Synthesis of KDO 8-P which is required for lipid A maturation and cellular growth. TTVNA43 PD 1X8F; 1X6U; 1Q3N; 1PL9; 1PHW TTVNA43 SQ MKQKVVSIGDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDRGANFGYDNLVVDMLGFSIMKKVSGNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPLAKLEPFLKQMKAIDDLVKGFEELDTSK TTVNA43 TT Literature-reported TTGERMY ID TTGERMY TTGERMY TN Bacterial Dihydroneopterin aldolase (Bact folB) TTGERMY UP O84620 TTGERMY UC FOLB_CHLTR TTGERMY BC Carbon-carbon lyase TTGERMY SN folB of Chlamydia trachomatis; DhnA-type aldolase; DHNA of Chlamydia trachomatis TTGERMY GN Bact folB TTGERMY FC Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin. TTGERMY EC EC 4.1.2.25 TTGERMY SQ MLLYRLDIADFRVWVSIGVSEQERHYPQPVLVSLSLFFKEEPKACSTDKVSDSVCYAELVSLIEEVATNNPCALIERLAKVLLEKIEKALAGQVSRIDLRVSKERPPIPDLLSPVSFSISREVP TTGERMY TT Literature-reported TT6LDTK ID TT6LDTK TT6LDTK TN Bacterial Glutamate-1-semialdehyde aminomutase (Bact hemL) TT6LDTK UP P23893 TT6LDTK UC GSA_ECOLI TT6LDTK BC Intramolecular transferases TT6LDTK SN Glutamate-1-semialdehyde aminotransferase; Glutamate-1-semialdehyde 2,1-aminomutase; GSA-AT; GSA TT6LDTK GN Bact hemL TT6LDTK FC Catalyses the formation of this key precursor of tetrapyrroles. TT6LDTK SQ MSKSENLYSAARELIPGGVNSPVRAFTGVGGTPLFIEKADGAYLYDVDGKAYIDYVGSWGPMVLGHNHPAIRNAVIEAAERGLSFGAPTEMEVKMAQLVTELVPTMDMVRMVNSGTEATMSAIRLARGFTGRDKIIKFEGCYHGHADCLLVKAGSGALTLGQPNSPGVPADFAKYTLTCTYNDLASVRAAFEQYPQEIACIIVEPVAGNMNCVPPLPEFLPGLRALCDEFGALLIIDEVMTGFRVALAGAQDYYGVVPDLTCLGKIIGGGMPVGAFGGRRDVMDALAPTGPVYQAGTLSGNPIAMAAGFACLNEVAQPGVHETLDELTTRLAEGLLEAAEEAGIPLVVNHVGGMFGIFFTDAESVTCYQDVMACDVERFKRFFHMMLDEGVYLAPSAFEAGFMSVAHSMEDINNTIDAARRVFAKL TT6LDTK TT Literature-reported TTOR5EH ID TTOR5EH TTOR5EH TN Bacterial Holo-ACP synthase (Bact acpS) TTOR5EH UP P24224 TTOR5EH UC ACPS_ECOLI TTOR5EH BC Kinase TTOR5EH SN acpS; Holo-[acyl-carrier protein] synthase; 4'-phosphopantetheinyl transferase acpS TTOR5EH GN Bact acpS TTOR5EH FC Transfers the 4'-phosphopantetheine moiety from coenzyme A to the 'Ser-36' of acyl-carrier-protein. TTOR5EH PD 5XUH; 5XU7; 5VCB; 5VBX TTOR5EH SQ MAILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWKTHHQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFNDELGKPRLRLWGEALKLAEKLGVANMHVTLADERHYACATVIIES TTOR5EH TT Literature-reported TTDTNEF ID TTDTNEF TTDTNEF TN Bacterial Homoserine dehydrogenase (Bact hom) TTDTNEF UP P19582 TTDTNEF UC DHOM_BACSU TTDTNEF BC Short-chain dehydrogenases reductase TTDTNEF SN Homoserine dehydrogenase; HDH TTDTNEF GN Bact hom TTDTNEF FC A dimer enzyme, with each monomer composed of three regions, the nucleotide-binding region, the dimerization region and the catalytic region. Required for the biosynthesis of the three essential amino acids, methionine, isoleucine and threonine from aspartate. Participates in this aspartate pathway of the NAD(P)H-dependent reduction of L-aspartate semialdehyde (L-ASA) to L-homoserine (L-Hse). TTDTNEF EC EC 1.1.1.3 TTDTNEF SQ MKAIRVGLLGLGTVGSGVVKIIQDHQDKLMHQVGCPVTIKKVLVKDLEKKREVDLPKEVLTTEVYDVIDDPDVDVVIEVIGGVEQTKQYLVDALRSKKHVVTANKDLMAVYGSELLAEAKENGCDIYFEASVAGGIPILRTLEEGLSSDRITKMMGIVNGTTNFILTKMIKEKSPYEEVLKEAQDLGFAEADPTSDVEGLDAARKMAILARLGFSMNVDLEDVKVKGISQITDEDISFSKRLGYTMKLIGIAQRDGSKIEVSVQPTLLPDHHPLSAVHNEFNAVYVYGEAVGETMFYGPGAGSMPTATSVVSDLVAVMKNMRLGVTGNSFVGPQYEKNMKSPSDIYAQQFLRIHVKDEVGSFSKITSVFSERGVSFEKILQLPIKGHDELAEIVIVTHHTSEADFSDILQNLNDLEVVQEVKSTYRVEGNGWS TTDTNEF TT Literature-reported TT38ECI ID TT38ECI TT38ECI TN Bacterial Hydroxymethyl-dihydropterin pyrophosphokinase (Bact folK) TT38ECI UP P26281 TT38ECI UC HPPK_ECOLI TT38ECI BC Kinase TT38ECI SN PPPK; HPPK; 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase TT38ECI GN Bact folK TT38ECI FC 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity, magnesium ion binding TT38ECI PD 6AN6; 6AN4; 5ETP; 5ETO; 5ETN TT38ECI SQ MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW TT38ECI TT Literature-reported TT04KI2 ID TT04KI2 TT04KI2 TN Bacterial Ketol-acid reductoisomerase (Bact ilvC) TT04KI2 UP P05793 TT04KI2 UC ILVC_ECOLI TT04KI2 BC Short-chain dehydrogenases reductase TT04KI2 SN Ketol-acid reductoisomerase type II; Ketol-acid reductoisomerase type 2; Ketol-acid reductoisomerase (NADP(+)); KARI; Alpha-keto-beta-hydroxylacyl reductoisomerase; Acetohydroxy-acid isomeroreductase; AHIR TT04KI2 GN Bact ilvC TT04KI2 FC Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. Also able to use 2-ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate, 3-hydroxypyruvate, 3-hydroxy-2-ketobutyrate and pyruvate. TT04KI2 PD 3ULK; 1YRL TT04KI2 SQ MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRTVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFSYACVPLLKPFMAELQPGDLGKAIPEGAVDNGQLRDVNEAIRSHAIEQVGKKLRGYMTDMKRIAVAG TT04KI2 TT Literature-reported TTFSX6G ID TTFSX6G TTFSX6G TN Bacterial MTA/SAH nucleosidase (Bact mtnN) TTFSX6G UP P0AF12 TTFSX6G UC MTNN_ECOLI TTFSX6G BC Glycosylase TTFSX6G SN mtnN; S-adenosylhomocysteine nucleosidase; P46; 5'-methylthioadenosine nucleosidase; 5'-Methylthioadenosine/S-adenosylhomocysteine (MTA/AdoHcy) nucleosidase TTFSX6G GN Bact mtnN TTFSX6G FC Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S- adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Can also use 5'-isobutylthioadenosine, 5'-n- butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza- adenosylhomocysteine as substrates. TTFSX6G PD 4YML; 4WKC; 3O4V; 1Z5P; 1Z5O TTFSX6G SQ MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG TTFSX6G TT Literature-reported TTFKXOM ID TTFKXOM TTFKXOM TN Bacterial NADH-dependent enoyl-ACP reductase (Bact fabI) TTFKXOM UP P0AEK4 TTFKXOM UC FABI_ECOLI TTFKXOM BC Short-chain dehydrogenases reductase TTFKXOM SN Enoyl[acylcarrierprotein] reductase [NADH] FabI; ENR of Mycobacterium tuberculosis TTFKXOM GN Bact fabI TTFKXOM FC Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis. TTFKXOM PD 5CG2; 5CG1; 5CFZ; 4JX8; 4JQC TTFKXOM SQ MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK TTFKXOM TT Literature-reported TTCH81V ID TTCH81V TTCH81V TN Bacterial NADH-dependent enoyl-ACP reductase 1 (Bact fabI1) TTCH81V UP P58380 TTCH81V UC FABI1_RHIME TTCH81V BC CH-CH donor oxidoreductase TTCH81V SN NADH-dependent enoyl-ACP reductase 1; Enoyl-[acyl-carrier-protein] reductase [NADH] 1 TTCH81V GN Bact fabI1 TTCH81V FC A key enzyme of the type II fatty acid synthesis (FAS) system. Essential for bacterial metabolism and its sequence conservation across many bacterial species but distinctly different from those of mammalian fatty acid biosynthesis enzymes. TTCH81V SQ MAQASGLMNGKRGVIMGVANNRSIAWGIAKALAEAGAEIALTWQGDALKKRVEPLAQELGAFMAGHCDVTDLATIDAVFSALEEKWGKIDFVVHAIAFSDKDELTGRYLDTSRDNFARTMDISVYSFTAVAARADRVMNDGGSILTLTYYGAEKVMPHYNVMGVAKAALEASVRYLAVDLGNRGIRVNAISAGPIKTLAASGIGDFRYILKWNEYNAPLKRTVSIEEVGNSALYLLSDLSSGVTGEVHHVDSGYHTVGMKAVDAPDISVLKD TTCH81V TT Literature-reported TTCH81V KE sme00061:Fatty acid biosynthesis; sme00780:Biotin metabolism; sme01100:Metabolic pathways; sme01212:Fatty acid metabolism TT283NK ID TT283NK TT283NK TN Bacterial NADH-dependent enoyl-ACP reductase 2 (Bact fabI2) TT283NK UP P58381 TT283NK UC FABI2_RHIME TT283NK BC CH-CH donor oxidoreductase TT283NK SN NADH-dependent enoyl-ACP reductase 2; Enoyl-[acyl-carrier-protein] reductase [NADH] 2 TT283NK GN Bact fabI2 TT283NK FC Identified as the FabI protein, which is the target of a group of antibacterial compounds, the diazaborines. TT283NK SQ MNGLMNGKRGLIMGVANSHSIAWGIAKSLAAQGAELAFTYQGEALGKRVKPLAAEVNSDFLLPCDVEDIGSVDAVVDAIKERWGKLDFVVHAIGFSDKNELKGLYADTTRDNFSRTMVISCFSFTEIAKRAAELMSEGGTMLTLTYGGSMRVMPNYNVMGVAKAALEASVRYLAADYGSRGIRVNAISAGPIRTLAGAGISDARAMLSWQQKNSPLRRTVTIEDVGSSALYLLSDLSRGVTGEIHYVDSGYNITSMPTLEALRVADAD TT283NK TT Literature-reported TT283NK KE sme00061:Fatty acid biosynthesis; sme00780:Biotin metabolism; sme01100:Metabolic pathways; sme01212:Fatty acid metabolism TT8WCXO ID TT8WCXO TT8WCXO TN Bacterial NH(3)-dependent NAD(+) synthetase (Bact nadE) TT8WCXO UP P18843 TT8WCXO UC NADE_ECOLI TT8WCXO BC Carbon-nitrogen ligase TT8WCXO SN efg; Nitrogen-regulatory protein; Nicotinamide adenine dinucleotide synthetase; NadE; NAD+ synthetase; NAD+ synthase; NAD(+)-synthetase; NAD synthetase; NAD synthase; Diphosphopyridine nucleotide synthetase TT8WCXO GN Bact nadE TT8WCXO FC Catalyzes a keystep in NAD biosynthesis, transforming deamido-NAD into NAD by a two-step reaction. TT8WCXO PD 1WXI; 1WXH; 1WXG; 1WXF; 1WXE TT8WCXO SQ MTLQQQIIKALGAKPQINAEEEIRRSVDFLKSYLQTYPFIKSLVLGISGGQDSTLAGKLCQMAINELRLETGNESLQFIAVRLPYGVQADEQDCQDAIAFIQPDRVLTVNIKGAVLASEQALREAGIELSDFVRGNEKARERMKAQYSIAGMTSGVVVGTDHAAEAITGFFTKYGDGGTDINPLYRLNKRQGKQLLAALACPEHLYKKAPTADLEDDRPSLPDEVALGVTYDNIDDYLEGKNVPQQVARTIENWYLKTEHKRRPPITVFDDFWKK TT8WCXO TT Literature-reported TTBE0LS ID TTBE0LS TTBE0LS TN Bacterial O-acetylserine sulfhydrylase A (Bact cysK) TTBE0LS UP P0ABK5 TTBE0LS UC CYSK_ECOLI TTBE0LS BC Alkyl aryl transferase TTBE0LS SN Sulfate starvation-induced protein 5; SSI5; S-carboxymethylcysteine synthase; OAS-TL A; O-acetylserine sulfhydrylase A; O-acetylserine (thiol)-lyase A; Cysteine synthase A; CSase A TTBE0LS GN Bact cysK TTBE0LS FC In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC in microbial infection; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 and X90, both K12 derivatives). This protein is not required for CDI of strain EC93, whose toxin may function by forming inner cell membrane pores. CysK stabilizes CdiA-CT, allowing it to bind tRNA substrate; neither CdiA-CT nor CysK bind tRNA alone in vitro. TTBE0LS PD 5J5V; 5J43 TTBE0LS SQ MSKIFEDNSLTIGHTPLVRLNRIGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASNPEKYLLLQQFSNPANPEIHEKTTGPEIWEDTDGQVDVFIAGVGTGGTLTGVSRYIKGTKGKTDLISVAVEPTDSPVIAQALAGEEIKPGPHKIQGIGAGFIPANLDLKLVDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDESFTNKNIVVILPSSGERYLSTALFADLFTEKELQQ TTBE0LS TT Literature-reported TTTP8L7 ID TTTP8L7 TTTP8L7 TN Bacterial O-acetylserine sulfhydrylase B (Bact cysM) TTTP8L7 UP P16703 TTTP8L7 UC CYSM_ECOLI TTTP8L7 BC Alkyl aryl transferase TTTP8L7 SN OAS-TL B; O-acetylserine sulfhydrylase B; O-acetylserine (thiol)-lyase B; Cysteine synthase B; CSase B TTTP8L7 GN Bact cysM TTTP8L7 FC Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. TTTP8L7 PD 2V03; 2BHT; 2BHS TTTP8L7 SQ MSTLEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMANRGEGKLLDQFNNPDNPYAHYTTTGPEIWQQTGGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPGIRRWPTEYLPGIFNASLVDEVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAKANPDAVVVAIICDRGDRYLSTGVFGEEHFSQGAGI TTTP8L7 TT Literature-reported TT329FH ID TT329FH TT329FH TN Bacterial Penicillin-binding protein 1B (Bact mrcB) TT329FH UP P02919 TT329FH UC PBPB_ECOLI TT329FH BC Acyltransferase TT329FH SN mrcB; PBP1b; PBP-1b; PBP 1b; Murein polymerase TT329FH GN Bact mrcB TT329FH FC Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). TT329FH PD 6G5R; 6FZK; 5HLD; 5HLB; 5HLA TT329FH SQ MAGNDREPIGRKGKPTRPVKQKVSRRRYEDDDDYDDYDDYEDEEPMPRKGKGKGKGRKPRGKRGWLWLLLKLAIVFAVLIAIYGVYLDQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTISKNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHLATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDARYSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASIYNPWRNPKLALERRNLVLRLLQQQQIIDQELYDMLSARPLGVQPRGGVISPQPAFMQLVRQELQAKLGDKVKDLSGVKIFTTFDSVAQDAAEKAAVEGIPALKKQRKLSDLETAIVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIALRQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPKDQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAERAVPAQAAYLTLWTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTNNNVDTWFAGIDGSTVTITWVGRDNNQPTKLYGASGAMSIYQRYLANQTPTPLNLVPPEDIADMGVDYDGNFVCSGGMRILPVWTSDPQSLCQQSEMQQQPSGNPFDQSSQPQQQPQQQPAQQEQKDSDGVAGWIKDMFGSN TT329FH TT Literature-reported TTFGVKC ID TTFGVKC TTFGVKC TN Bacterial Phosphoenolpyruvate transferase (Bact ptsI) TTFGVKC UP P08839 TTFGVKC UC PT1_ECOLI TTFGVKC BC Kinase TTFGVKC SN ptsI; Phosphotransferase system, enzyme I; Phosphoenolpyruvate-protein phosphotransferase TTFGVKC GN Bact ptsI TTFGVKC FC General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). TTFGVKC PD 3EZE; 3EZB; 3EZA; 2XDF; 2N5T TTFGVKC SQ MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAIRIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC TTFGVKC TT Literature-reported TTJW9OF ID TTJW9OF TTJW9OF TN Bacterial Protease II (Bact ptrB) TTJW9OF UP P24555 TTJW9OF UC PTRB_ECOLI TTJW9OF BC Peptidase TTJW9OF SN ptrB; Oligopeptidase B TTJW9OF GN Bact ptrB TTJW9OF FC Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues. TTJW9OF EC EC 3.4.21.83 TTJW9OF SQ MLPKAARIPHAMTLHGDTRIDNYYWLRDDTRSQPEVLDYLQQENSYGHRVMASQQALQDRILKEIIDRIPQREVSAPYIKNGYRYRHIYEPGCEYAIYQRQSAFSEEWDEWETLLDANKRAAHSEFYSMGGMAITPDNTIMALAEDFLSRRQYGIRFRNLETGNWYPELLDNVEPSFVWANDSWIFYYVRKHPVTLLPYQVWRHAIGTPASQDKLIYEEKDDTYYVSLHKTTSKHYVVIHLASATTSEVRLLDAEMADAEPFVFLPRRKDHEYSLDHYQHRFYLRSNRHGKNFGLYRTRMRDEQQWEELIPPRENIMLEGFTLFTDWLVVEERQRGLTSLRQINRKTREVIGIAFDDPAYVTWIAYNPEPETARLRYGYSSMTTPDTLFELDMDTGERRVLKQTEVPGFYAANYRSEHLWIVARDGVEVPVSLVYHRKHFRKGHNPLLVYGYGSYGASIDADFSFSRLSLLDRGFVYAIVHVRGGGELGQQWYEDGKFLKKKNTFNDYLDACDALLKLGYGSPSLCYAMGGSAGGMLMGVAINQRPELFHGVIAQVPFVDVVTTMLDESIPLTTGEFEEWGNPQDPQYYEYMKSYSPYDNVTAQAYPHLLVTTGLHDSQVQYWEPAKWVAKLRELKTDDHLLLLCTDMDSGHGGKSGRFKSYEGVAMEYAFLVALAQGTLPATPAD TTJW9OF TT Literature-reported TTHB48R ID TTHB48R TTHB48R TN Bacterial Pyridoxal phosphate biosynthetic pdxJ (Bact pdxJ) TTHB48R UP P0A794 TTHB48R UC PDXJ_ECOLI TTHB48R SN pdxJ; Pyridoxine 5'-phosphate synthase; PNP synthase TTHB48R GN Bact pdxJ TTHB48R FC Catalyzes the condensation of 1-deoxy-d-xylulose-5- phosphate (dxp) and 1-amino-3-(phosphohydroxy)propan-2-one to form pyridoxine 5'-phosphate (pnp). TTHB48R EC EC 2.6.99.2 TTHB48R PD 1M5W; 1IXQ; 1IXP; 1IXO; 1IXN TTHB48R SQ MAELLLGVNIDHIATLRNARGTAYPDPVQAAFIAEQAGADGITVHLREDRRHITDRDVRILRQTLDTRMNLEMAVTEEMLAIAVETKPHFCCLVPEKRQEVTTEGGLDVAGQRDKMRDACKRLADAGIQVSLFIDADEEQIKAAAEVGAPFIEIHTGCYADAKTDAEQAQELARIAKAATFAASLGLKVNAGHGLTYHNVKAIAAIPEMHELNIGHAIIGRAVMTGLKDAVAEMKRLMLEARG TTHB48R TT Literature-reported TTLUBN0 ID TTLUBN0 TTLUBN0 TN Bacterial RNA endonuclease (Bact endA) TTLUBN0 UP P25736 TTLUBN0 UC END1_ECOLI TTLUBN0 BC Endodeoxyribonucleases TTLUBN0 SN endA; Endonuclease I; Endo I TTLUBN0 GN Bact endA TTLUBN0 FC Has double-strand break activity. TTLUBN0 EC EC 3.1.21.1 TTLUBN0 SQ MYRYLSIAAVVLSAAFSGPALAEGINSFSQAKAAAVKVHADAPGTFYCGCKINWQGKKGVVDLQSCGYQVRKNENRASRVEWEHVVPAWQFGHQRQCWQDGGRKNCAKDPVYRKMESDMHNLQPSVGEVNGDRGNFMYSQWNGGEGQYGQCAMKVDFKEKAAEPPARARGAIARTYFYMRDQYNLTLSRQQTQLFNAWNKMYPVTDWECERDERIAKVQGNHNPYVQRACQARKS TTLUBN0 TT Literature-reported TTES76Y ID TTES76Y TTES76Y TN Bacterial Sensor protein QseC (Bact QseC) TTES76Y UP P40719 TTES76Y UC QSEC_ECOLI TTES76Y SN Sensor protein QseC TTES76Y GN Bact QseC TTES76Y FC Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. May activate QseB by phosphorylation. TTES76Y EC EC 2.7.13.3 TTES76Y PD 3JZ3; 2KSE TTES76Y SQ MKFTQRLSLRVRLTLIFLILASVTWLLSSFVAWKQTTDNVDELFDTQLMLFAKRLSTLDLNEINAADRMAQTPNRLKHGHVDDDALTFAIFTHDGRMVLNDGDNGEDIPYSYQREGFADGQLVGEDDPWRFVWMTSPDGKYRIVVGQEWEYREDMALAIVAGQLIPWLVALPIMLIIMMVLLGRELAPLNKLALALRMRDPDSEKPLNATGVPSEVRPLVESLNQLFARTHAMMVRERRFTSDAAHELRSPLTALKVQTEVAQLSDDDPQARKKALLQLHSGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSSVMDIYHTAQQAKIDVRLTLNAHSIKRTGQPLLLSLLVRNLLDNAVRYSPQGSVVDVTLNADNFIVRDNGPGVTPEALARIGERFYRPPGQTATGSGLGLSIVQRIAKLHGMNVEFGNAEQGGFEAKVSW TTES76Y TT Literature-reported TTJVCG0 ID TTJVCG0 TTJVCG0 TN Bacterial Sporulation kinase A (Bact kinA) TTJVCG0 UP P16497 TTJVCG0 UC KINA_BACSU TTJVCG0 SN Stage II sporulation protein J; Stage II sporulation protein F; Sporulation kinase A TTJVCG0 GN Bact kinA TTJVCG0 FC Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. It also autophosphorylates in the presence of ATP. TTJVCG0 EC EC 2.7.13.3 TTJVCG0 PD 2VLG TTJVCG0 SQ MEQDTQHVKPLQTKTDIHAVLASNGRIIYISANSKLHLGYLQGEMIGSFLKTFLHEEDQFLVESYFYNEHHLMPCTFRFIKKDHTIVWVEAAVEIVTTRAERTEREIILKMKVLEEETGHQSLNCEKHEIEPASPESTTYITDDYERLVENLPSPLCISVKGKIVYVNSAMLSMLGAKSKDAIIGKSSYEFIEEEYHDIVKNRIIRMQKGMEVGMIEQTWKRLDGTPVHLEVKASPTVYKNQQAELLLLIDISSRKKFQTILQKSRERYQLLIQNSIDTIAVIHNGKWVFMNESGISLFEAATYEDLIGKNIYDQLHPCDHEDVKERIQNIAEQKTESEIVKQSWFTFQNRVIYTEMVCIPTTFFGEAAVQVILRDISERKQTEELMLKSEKLSIAGQLAAGIAHEIRNPLTAIKGFLQLMKPTMEGNEHYFDIVFSELSRIELILSELLMLAKPQQNAVKEYLNLKKLIGEVSALLETQANLNGIFIRTSYEKDSIYINGDQNQLKQVFINLIKNAVESMPDGGTVDIIITEDEHSVHVTVKDEGEGIPEKVLNRIGEPFLTTKEKGTGLGLMVTFNIIENHQGVIHVDSHPEKGTAFKISFPKK TTJVCG0 TT Literature-reported TTAEOJ4 ID TTAEOJ4 TTAEOJ4 TN Bacterial UDP-N-acetylenolpyruvylglucosamine reductase (Bact murB) TTAEOJ4 UP P08373 TTAEOJ4 UC MURB_ECOLI TTAEOJ4 BC Short-chain dehydrogenases reductase TTAEOJ4 SN UDP-N-acetylmuramate dehydrogenase; MurB TTAEOJ4 GN Bact murB TTAEOJ4 FC Cell wall formation. TTAEOJ4 PD 2Q85; 2MBR; 1UXY; 1MBT; 1MBB TTAEOJ4 SQ MNHSLKPWNTFGIDHNAQHIVCAEDEQQLLNAWQYATAEGQPVLILGEGSNVLFLEDYRGTVIINRIKGIEIHDEPDAWYLHVGAGENWHRLVKYTLQEGMPGLENLALIPGCVGSSPIQNIGAYGVELQRVCAYVDSVELATGKQVRLTAKECRFGYRDSIFKHEYQDRFAIVAVGLRLPKEWQPVLTYGDLTRLDPTTVTPQQVFNAVCHMRTTKLPDPKVNGNAGSFFKNPVVSAETAKALLSQFPTAPNYPQADGSVKLAAGWLIDQCQLKGMQIGGAAVHRQQALVLINEDNAKSEDVVQLAHHVRQKVGEKFNVWLEPEVRFIGASGEVSAVETIS TTAEOJ4 TT Literature-reported TT7JUKC ID TT7JUKC TT7JUKC TN Bcl-2-binding component 3 (BBC3) TT7JUKC UP Q9BXH1 TT7JUKC UC BBC3_HUMAN TT7JUKC BC B-cell lymphoma Bcl-2 TT7JUKC SN p53 upregulated modulator of apoptosis; p53 up-regulated modulator of apoptosis; PUMA; JFY1; JFY-1; Bcl2binding component 3 TT7JUKC GN BBC3 TT7JUKC FC Functions by promoting partial unfolding of BCL2L1 and dissociation of BCL2L1 from p53/TP53. Regulates ER stress-induced neuronal apoptosis. Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis. TT7JUKC PD 5UUL; 4HNJ; 4BPK; 4BPJ; 4BPI TT7JUKC SQ MARARQEGSSPEPVEGLARDGPRPFPLGRLVPSAVSCGLCEPGLAAAPAAPTLLPAAYLCAPTAPPAVTAALGGSRWPGGPRSRPRGPRPDGPQPSLSLAEQHLESPVPSAPGALAGGPTQAAPGVRGEEEQWAREIGAQLRRMADDLNAQYERRRQEEQQRHRPSPWRVLYNLIMGLLPLPRGHRAPEMEPN TT7JUKC TT Literature-reported TT0UMTJ ID TT0UMTJ TT0UMTJ TN Beta-1,2-xylosyltransferase (RXYLT1) TT0UMTJ UP Q9Y2B1 TT0UMTJ UC RXLT1_HUMAN TT0UMTJ BC Pentosyltransferase TT0UMTJ SN XYLT; Beta-(1,2)-xylosyltransferase TT0UMTJ GN XYLT TT0UMTJ FC Catalyzes beta-1,2 glycosidic linkages. TT0UMTJ EC EC 2.4.2.- TT0UMTJ SQ MRLTRKRLCSFLIALYCLFSLYAAYHVFFGRRRQAPAGSPRGLRKGAAPARERRGREQSTLESEEWNPWEGDEKNEQQHRFKTSLQILDKSTKGKTDLSVQIWGKAAIGLYLWEHIFEGLLDPSDVTAQWREGKSIVGRTQYSFITGPAVIPGYFSVDVNNVVLILNGREKAKIFYATQWLLYAQNLVQIQKLQHLAVVLLGNEHCDNEWINPFLKRNGGFVELLFIIYDSPWINDVDVFQWPLGVATYRNFPVVEASWSMLHDERPYLCNFLGTIYENSSRQALMNILKKDGNDKLCWVSAREHWQPQETNESLKNYQDALLQSDLTLCPVGVNTECYRIYEACSYGSIPVVEDVMTAGNCGNTSVHHGAPLQLLKSMGAPFIFIKNWKELPAVLEKEKTIILQEKIERRKMLLQWYQHFKTELKMKFTNILESSFLMNNKS TT0UMTJ TT Literature-reported TTMVD4A ID TTMVD4A TTMVD4A TN Beta-arrestin-1 (ARRB1) TTMVD4A UP P49407 TTMVD4A UC ARRB1_HUMAN TTMVD4A BC Arrestin protein TTMVD4A SN Non-visual arrestin-2; Betaarrestin1; Arrestin beta1; Arrestin beta-1; ARR1 TTMVD4A GN ARRB1 TTMVD4A FC During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6). Involved in IL8-mediated granule release in neutrophils. Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3. Negatively regulates the NOTCH signaling pathway by mediating the ubiquitination and degradation of NOTCH1 by ITCH. Participates to the recruitment of the ubiquitin-protein ligase to the receptor. Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. TTMVD4A PD 2IV8 TTMVD4A SQ MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTCAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPPNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEPPHREVPENETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKEEEEDGTGSPQLNNR TTMVD4A TT Literature-reported TT39YVO ID TT39YVO TT39YVO TN Beta-chimaerin (CHN2) TT39YVO UP P52757 TT39YVO UC CHIO_HUMAN TT39YVO BC Zinc-finger TT39YVO SN Rho-GTPase-activating protein 3; CHN2; Beta2-chimaerin; Beta-chimerin TT39YVO GN CHN2 TT39YVO FC Gtpase activating protein for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher rac activity and could therefore play a role in the progression from low-grade to high-grade tumors. TT39YVO PD 1XA6 TT39YVO SQ MAASSNSSLSGSSVSSDAEEYQPPIWKSYLYQLQQEAPRPKRIICPREVENRPKYYGREFHGIISREQADELLGGVEGAYILRESQRQPGCYTLALRFGNQTLNYRLFHDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYISKMTTNPIYEHIGYATLLREKVSRRLSRSKNEPRKTNVTHEEHTAVEKISSLVRRAALTHNDNHFNYEKTHNFKVHTFRGPHWCEYCANFMWGLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLKRIKKVYCCDLTTLVKAHNTQRPMVVDICIREIEARGLKSEGLYRVSGFTEHIEDVKMAFDRDGEKADISANVYPDINIITGALKLYFRDLPIPVITYDTYSKFIDAAKISNADERLEAVHEVLMLLPPAHYETLRYLMIHLKKVTMNEKDNFMNAENLGIVFGPTLMRPPEDSTLTTLHDMRYQKLIVQILIENEDVLF TT39YVO TT Literature-reported TTNGJPH ID TTNGJPH TTNGJPH TN Beta-galactosidase (GLB1) TTNGJPH UP P16278 TTNGJPH UC BGAL_HUMAN TTNGJPH SN Lactase; Elastin receptor 1; ELNR1; Acid beta-galactosidase TTNGJPH GN GLB1 TTNGJPH FC Isoform 1: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. TTNGJPH EC EC 3.2.1.23 TTNGJPH PD 3WF4; 3WF3; 3WF2; 3WF1; 3WF0 TTNGJPH SQ MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV TTNGJPH TT Preclinical TT90BJT ID TT90BJT TT90BJT TN Bone marrow stromal antigen 2 (BST2) TT90BJT UP Q10589 TT90BJT UC BST2_HUMAN TT90BJT BC Tetherin family TT90BJT SN Tetherin; HM1.24 antigen; CD317; BST2 TT90BJT GN BST2 TT90BJT FC IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), human immunodeficiency virus type 2 (HIV-2), simian immunodeficiency viruses (SIVs), equine infectious anemia virus (EIAV), feline immunodeficiency virus (FIV), prototype foamy virus (PFV), Mason- Pfizer monkey virus (MPMV), human T-cell leukemia virus type 1 (HTLV-1), Rous sarcoma virus (RSV) and murine leukemia virus (MLV), flavivirideae: hepatitis C virus (HCV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), arenaviridae: lassa virus (LASV) and machupo virus (MACV), herpesviridae: kaposis sarcoma- associated herpesvirus (KSHV), rhabdoviridae: vesicular stomatitis virus (VSV), orthomyxoviridae: influenza A virus, and paramyxoviridae: nipah virus. Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells. Isoform 1 and isoform 2 are both effective viral restriction factors but have differing antiviral and signaling activities. Isoform 2 is resistant to HIV-1 Vpu-mediated degradation and restricts HIV-1 viral budding in the presence of Vpu. Isoform 1 acts as an activator of NF-kappa-B and this activity is inhibited by isoform 2. TT90BJT PD 6DFF; 6D84; 6D83; 6CRI; 6CM9 TT90BJT SQ MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ TT90BJT TT Literature-reported TTZV7LJ ID TTZV7LJ TTZV7LJ TN BRCA1-associated C-terminal helicase 1 (FANCJ) TTZV7LJ UP Q9BX63 TTZV7LJ UC FANCJ_HUMAN TTZV7LJ SN Protein FACJ; Fanconi anemia group J protein; FANCJ; BRCA1-interacting protein C-terminal helicase 1; BRCA1-interacting protein 1; BACH1; ATP-dependent RNA helicase BRIP1 TTZV7LJ GN BRIP1 TTZV7LJ FC DNA-dependent ATPase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Acts late in the Fanconi anemia pathway, after FANCD2 ubiquitination. Involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1. TTZV7LJ EC EC 3.6.4.13 TTZV7LJ PD 3AL3; 1T29; 1T15 TTZV7LJ SQ MSSMWSEYTIGGVKIYFPYKAYPSQLAMMNSILRGLNSKQHCLLESPTGSGKSLALLCSALAWQQSLSGKPADEGVSEKAEVQLSCCCACHSKDFTNNDMNQGTSRHFNYPSTPPSERNGTSSTCQDSPEKTTLAAKLSAKKQASIYRDENDDFQVEKKRIRPLETTQQIRKRHCFGTEVHNLDAKVDSGKTVKLNSPLEKINSFSPQKPPGHCSRCCCSTKQGNSQESSNTIKKDHTGKSKIPKIYFGTRTHKQIAQITRELRRTAYSGVPMTILSSRDHTCVHPEVVGNFNRNEKCMELLDGKNGKSCYFYHGVHKISDQHTLQTFQGMCKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIEDCARESASYSVTEVQLRFARDELDSMVNNNIRKKDHEPLRAVCCSLINWLEANAEYLVERDYESACKIWSGNEMLLTLHKMGITTATFPILQGHFSAVLQKEEKISPIYGKEEAREVPVISASTQIMLKGLFMVLDYLFRQNSRFADDYKIAIQQTYSWTNQIDISDKNGLLVLPKNKKRSRQKTAVHVLNFWCLNPAVAFSDINGKVQTIVLTSGTLSPMKSFSSELGVTFTIQLEANHIIKNSQVWVGTIGSGPKGRNLCATFQNTETFEFQDEVGALLLSVCQTVSQGILCFLPSYKLLEKLKERWLSTGLWHNLELVKTVIVEPQGGEKTNFDELLQVYYDAIKYKGEKDGALLVAVCRGKVSEGLDFSDDNARAVITIGIPFPNVKDLQVELKRQYNDHHSKLRGLLPGRQWYEIQAYRALNQALGRCIRHRNDWGALILVDDRFRNNPSRYISGLSKWVRQQIQHHSTFESALESLAEFSKKHQKVLNVSIKDRTNIQDNESTLEVTSLKYSTSPYLLEAASHLSPENFVEDEAKICVQELQCPKIITKNSPLPSSIISRKEKNDPVFLEEAGKAEKIVISRSTSPTFNKQTKRVSWSSFNSLGQYFTGKIPKATPELGSSENSASSPPRFKTEKMESKTVLPFTDKCESSNLTVNTSFGSCPQSETIISSLKIDATLTRKNHSEHPLCSEEALDPDIELSLVSEEDKQSTSNRDFETEAEDESIYFTPELYDPEDTDEEKNDLAETDRGNRLANNSDCILAKDLFEIRTIKEVDSAREVKAEDCIDTKLNGILHIEESKIDDIDGNVKTTWINELELGKTHEIEIKNFKPSPSKNKGMFPGFK TTZV7LJ TT Literature-reported TTUARD6 ID TTUARD6 TTUARD6 TN Breast cancer type 2 susceptibility protein (BRCA2) TTUARD6 UP P51587 TTUARD6 UC BRCA2_HUMAN TTUARD6 SN Fanconi anemia group D1 protein; FANCD1; FACD TTUARD6 GN BRCA2 TTUARD6 FC Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination. Involved in double-strand break repair and/or homologous recombination. TTUARD6 PD 3EU7; 1N0W TTUARD6 SQ MPIGSKERPTFFEIFKTRCNKADLGPISLNWFEELSSEAPPYNSEPAEESEHKNNNYEPNLFKTPQRKPSYNQLASTPIIFKEQGLTLPLYQSPVKELDKFKLDLGRNVPNSRHKSLRTVKTKMDQADDVSCPLLNSCLSESPVVLQCTHVTPQRDKSVVCGSLFHTPKFVKGRQTPKHISESLGAEVDPDMSWSSSLATPPTLSSTVLIVRNEEASETVFPHDTTANVKSYFSNHDESLKKNDRFIASVTDSENTNQREAASHGFGKTSGNSFKVNSCKDHIGKSMPNVLEDEVYETVVDTSEEDSFSLCFSKCRTKNLQKVRTSKTRKKIFHEANADECEKSKNQVKEKYSFVSEVEPNDTDPLDSNVANQKPFESGSDKISKEVVPSLACEWSQLTLSGLNGAQMEKIPLLHISSCDQNISEKDLLDTENKRKKDFLTSENSLPRISSLPKSEKPLNEETVVNKRDEEQHLESHTDCILAVKQAISGTSPVASSFQGIKKSIFRIRESPKETFNASFSGHMTDPNFKKETEASESGLEIHTVCSQKEDSLCPNLIDNGSWPATTTQNSVALKNAGLISTLKKKTNKFIYAIHDETSYKGKKIPKDQKSELINCSAQFEANAFEAPLTFANADSGLLHSSVKRSCSQNDSEEPTLSLTSSFGTILRKCSRNETCSNNTVISQDLDYKEAKCNKEKLQLFITPEADSLSCLQEGQCENDPKSKKVSDIKEEVLAAACHPVQHSKVEYSDTDFQSQKSLLYDHENASTLILTPTSKDVLSNLVMISRGKESYKMSDKLKGNNYESDVELTKNIPMEKNQDVCALNENYKNVELLPPEKYMRVASPSRKVQFNQNTNLRVIQKNQEETTSISKITVNPDSEELFSDNENNFVFQVANERNNLALGNTKELHETDLTCVNEPIFKNSTMVLYGDTGDKQATQVSIKKDLVYVLAEENKNSVKQHIKMTLGQDLKSDISLNIDKIPEKNNDYMNKWAGLLGPISNHSFGGSFRTASNKEIKLSEHNIKKSKMFFKDIEEQYPTSLACVEIVNTLALDNQKKLSKPQSINTVSAHLQSSVVVSDCKNSHITPQMLFSKQDFNSNHNLTPSQKAEITELSTILEESGSQFEFTQFRKPSYILQKSTFEVPENQMTILKTTSEECRDADLHVIMNAPSIGQVDSSKQFEGTVEIKRKFAGLLKNDCNKSASGYLTDENEVGFRGFYSAHGTKLNVSTEALQKAVKLFSDIENISEETSAEVHPISLSSSKCHDSVVSMFKIENHNDKTVSEKNNKCQLILQNNIEMTTGTFVEEITENYKRNTENEDNKYTAASRNSHNLEFDGSDSSKNDTVCIHKDETDLLFTDQHNICLKLSGQFMKEGNTQIKEDLSDLTFLEVAKAQEACHGNTSNKEQLTATKTEQNIKDFETSDTFFQTASGKNISVAKESFNKIVNFFDQKPEELHNFSLNSELHSDIRKNKMDILSYEETDIVKHKILKESVPVGTGNQLVTFQGQPERDEKIKEPTLLGFHTASGKKVKIAKESLDKVKNLFDEKEQGTSEITSFSHQWAKTLKYREACKDLELACETIEITAAPKCKEMQNSLNNDKNLVSIETVVPPKLLSDNLCRQTENLKTSKSIFLKVKVHENVEKETAKSPATCYTNQSPYSVIENSALAFYTSCSRKTSVSQTSLLEAKKWLREGIFDGQPERINTADYVGNYLYENNSNSTIAENDKNHLSEKQDTYLSNSSMSNSYSYHSDEVYNDSGYLSKNKLDSGIEPVLKNVEDQKNTSFSKVISNVKDANAYPQTVNEDICVEELVTSSSPCKNKNAAIKLSISNSNNFEVGPPAFRIASGKIVCVSHETIKKVKDIFTDSFSKVIKENNENKSKICQTKIMAGCYEALDDSEDILHNSLDNDECSTHSHKVFADIQSEEILQHNQNMSGLEKVSKISPCDVSLETSDICKCSIGKLHKSVSSANTCGIFSTASGKSVQVSDASLQNARQVFSEIEDSTKQVFSKVLFKSNEHSDQLTREENTAIRTPEHLISQKGFSYNVVNSSAFSGFSTASGKQVSILESSLHKVKGVLEEFDLIRTEHSLHYSPTSRQNVSKILPRVDKRNPEHCVNSEMEKTCSKEFKLSNNLNVEGGSSENNHSIKVSPYLSQFQQDKQQLVLGTKVSLVENIHVLGKEQASPKNVKMEIGKTETFSDVPVKTNIEVCSTYSKDSENYFETEAVEIAKAFMEDDELTDSKLPSHATHSLFTCPENEEMVLSNSRIGKRRGEPLILVGEPSIKRNLLNEFDRIIENQEKSLKASKSTPDGTIKDRRLFMHHVSLEPITCVPFRTTKERQEIQNPNFTAPGQEFLSKSHLYEHLTLEKSSSNLAVSGHPFYQVSATRNEKMRHLITTGRPTKVFVPPFKTKSHFHRVEQCVRNINLEENRQKQNIDGHGSDDSKNKINDNEIHQFNKNNSNQAAAVTFTKCEEEPLDLITSLQNARDIQDMRIKKKQRQRVFPQPGSLYLAKTSTLPRISLKAAVGGQVPSACSHKQLYTYGVSKHCIKINSKNAESFQFHTEDYFGKESLWTGKGIQLADGGWLIPSNDGKAGKEEFYRALCDTPGVDPKLISRIWVYNHYRWIIWKLAAMECAFPKEFANRCLSPERVLLQLKYRYDTEIDRSRRSAIKKIMERDDTAAKTLVLCVSDIISLSANISETSSNKTSSADTQKVAIIELTDGWYAVKAQLDPPLLAVLKNGRLTVGQKIILHGAELVGSPDACTPLEAPESLMLKISANSTRPARWYTKLGFFPDPRPFPLPLSSLFSDGGNVGCVDVIIQRAYPIQWMEKTSSGLYIFRNEREEEKEAAKYVEAQQKRLEALFTKIQEEFEEHEENTTKPYLPSRALTRQQVRALQDGAELYEAVKNAADPAYLEGYFSEEQLRALNNHRQMLNDKKQAQIQLEIRKAMESAEQKEQGLSRDVTTVWKLRIVSYSKKEKDSVILSIWRPSSDLYSLLTEGKRYRIYHLATSKSKSKSERANIQLAATKKTQYQQLPVSDEILFQIYQPREPLHFSKFLDPDFQPSCSEVDLIGFVVSVVKKTGLAPFVYLSDECYNLLAIKFWIDLNEDIIKPHMLIAASNLQWRPESKSGLLTLFAGDFSVFSASPKEGHFQETFNKMKNTVENIDILCNEAENKLMHILHANDPKWSTPTKDCTSGPYTAQIIPGTGNKLLMSSPNCEIYYQSPLSLCMAKRKSVSTPVSAQMTSKSCKGEKEIDDQKNCKKRRALDFLSRLPLPPPVSPICTFVSPAAQKAFQPPRSCGTKYETPIKKKELNSPQMTPFKKFNEISLLESNSIADEELALINTQALLSGSTGEKQFISVSESTRTAPTSSEDYLRLKRRCTTSLIKEQESSQASTEECEKNKQDTITTKKYI TTUARD6 TT Literature-reported TTUARD6 FM DNA repair TTT09OB ID TTT09OB TTT09OB TN Bromodomain-containing protein 1 (BRD1) TTT09OB UP O95696 TTT09OB UC BRD1_HUMAN TTT09OB BC Bromodomain TTT09OB SN Bromodomain and PHD finger-containing protein 2; BRPF2; BRL; BR140-like protein TTT09OB GN BRD1 TTT09OB FC Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. TTT09OB PD 5PWB; 5PWA; 5PW9; 5PW8; 5PW7 TTT09OB SQ MRRKGRCHRGSAARHPSSPCSVKHSPTRETLTYAQAQRMVEIEIEGRLHRISIFDPLEIILEDDLTAQEMSECNSNKENSERPPVCLRTKRHKNNRVKKKNEALPSAHGTPASASALPEPKVRIVEYSPPSAPRRPPVYYKFIEKSAEELDNEVEYDMDEEDYAWLEIVNEKRKGDCVPAVSQSMFEFLMDRFEKESHCENQKQGEQQSLIDEDAVCCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRHCLQSRARPADCVLCPNKGGAFKKTDDDRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGVGACIQCHKANCYTAFHVTCAQKAGLYMKMEPVKELTGGGTTFSVRKTAYCDVHTPPGCTRRPLNIYGDVEMKNGVCRKESSVKTVRSTSKVRKKAKKAKKALAEPCAVLPTVCAPYIPPQRLNRIANQVAIQRKKQFVERAHSYWLLKRLSRNGAPLLRRLQSSLQSQRSSQQRENDEEMKAAKEKLKYWQRLRHDLERARLLIELLRKREKLKREQVKVEQVAMELRLTPLTVLLRSVLDQLQDKDPARIFAQPVSLKEVPDYLDHIKHPMDFATMRKRLEAQGYKNLHEFEEDFDLIIDNCMKYNARDTVFYRAAVRLRDQGGVVLRQARREVDSIGLEEASGMHLPERPAAAPRRPFSWEDVDRLLDPANRAHLGLEEQLRELLDMLDLTCAMKSSGSRSKRAKLLKKEIALLRNKLSQQHSQPLPTGPGLEGFEEDGAALGPEAGEEVLPRLETLLQPRKRSRSTCGDSEVEEESPGKRLDAGLTNGFGGARSEQEPGGGLGRKATPRRRCASESSISSSNSPLCDSSFNAPKCGRGKPALVRRHTLEDRSELISCIENGNYAKAARIAAEVGQSSMWISTDAAASVLEPLKVVWAKCSGYPSYPALIIDPKMPRVPGHHNGVTIPAPPLDVLKIGEHMQTKSDEKLFLVLFFDNKRSWQWLPKSKMVPLGIDETIDKLKMMEGRNSSIRKAVRIAFDRAMNHLSRVHGEPTSDLSDID TTT09OB TT Literature-reported TT07ZS1 ID TT07ZS1 TT07ZS1 TN Bromodomain-containing protein 7 (BRD7) TT07ZS1 UP Q9NPI1 TT07ZS1 UC BRD7_HUMAN TT07ZS1 BC Bromodomain TT07ZS1 SN Protein CELTIX-1; CELTIX1; BP75; 75 kDa bromodomain protein TT07ZS1 GN BRD7 TT07ZS1 FC May play a role in chromatin remodeling. Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR. Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase. Acts both as coactivator and as corepressor. TT07ZS1 PD 5MQ1; 2I7K TT07ZS1 SQ MGKKHKKHKSDKHLYEEYVEKPLKLVLKVGGNEVTELSTGSSGHDSSLFEDKNDHDKHKDRKRKKRKKGEKQIPGEEKGRKRRRVKEDKKKRDRDRVENEAEKDLQCHAPVRLDLPPEKPLTSSLAKQEEVEQTPLQEALNQLMRQLQRKDPSAFFSFPVTDFIAPGYSMIIKHPMDFSTMKEKIKNNDYQSIEELKDNFKLMCTNAMIYNKPETIYYKAAKKLLHSGMKILSQERIQSLKQSIDFMADLQKTRKQKDGTDTSQSGEDGGCWQREREDSGDAEAHAFKSPSKENKKKDKDMLEDKFKSNNLEREQEQLDRIVKESGGKLTRRLVNSQCEFERRKPDGTTTLGLLHPVDPIVGEPGYCPVRLGMTTGRLQSGVNTLQGFKEDKRNKVTPVLYLNYGPYSSYAPHYDSTFANISKDDSDLIYSTYGEDSDLPSDFSIHEFLATCQDYPYVMADSLLDVLTKGGHSRTLQEMEMSLPEDEGHTRTLDTAKEMEITEVEPPGRLDSSTQDRLIALKAVTNFGVPVEVFDSEEAEIFQKKLDETTRLLRELQEAQNERLSTRPPPNMICLLGPSYREMHLAEQVTNNLKELAQQVTPGDIVSTYGVRKAMGISIPSPVMENNFVDLTEDTEEPKKTDVAECGPGGS TT07ZS1 TT Literature-reported TTR7L5Y ID TTR7L5Y TTR7L5Y TN Bromodomain-containing protein 9 (BRD9) TTR7L5Y UP Q9H8M2 TTR7L5Y UC BRD9_HUMAN TTR7L5Y BC Bromodomain TTR7L5Y SN Rhabdomyosarcoma antigen MU-RMS-40.8 TTR7L5Y GN BRD9 TTR7L5Y FC Plays a role in chromatin remodeling and regulation of transcription. Acts as a chromatin reader that recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated. Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. TTR7L5Y PD 6HM0; 6BQA; 5TWX; 5MKY; 5JI8 TTR7L5Y SQ MGKKHKKHKAEWRSSYEDYADKPLEKPLKLVLKVGGSEVTELSGSGHDSSYYDDRSDHERERHKEKKKKKKKKSEKEKHLDDEERRKRKEEKKRKREREHCDTEGEADDFDPGKKVEVEPPPDRPVRACRTQPAENESTPIQQLLEHFLRQLQRKDPHGFFAFPVTDAIAPGYSMIIKHPMDFGTMKDKIVANEYKSVTEFKADFKLMCDNAMTYNRPDTVYYKLAKKILHAGFKMMSKQAALLGNEDTAVEEPVPEVVPVQVETAKKSKKPSREVISCMFEPEGNACSLTDSTAEEHVLALVEHAADEARDRINRFLPGGKMGYLKRNGDGSLLYSVVNTAEPDADEEETHPVDLSSLSSKLLPGFTTLGFKDERRNKVTFLSSATTALSMQNNSVFGDLKSDEMELLYSAYGDETGVQCALSLQEFVKDAGSYSKKVVDDLLDQITGGDHSRTLFQLKQRRNVPMKPPDEAKVGDTLGDSSSSVLEFMSMKSYPDVSVDISMLSSLGKVKKELDPDDSHLNLDETTKLLQDLHEAQAERGGSRPSSNLSSLSNASERDQHHLGSPSRLSVGEQPDVTHDPYEFLQSPEPAASAKT TTR7L5Y TT Literature-reported TT3AF4R ID TT3AF4R TT3AF4R TN Calcium-activated chloride channel protein 1 (CaCC-1) TT3AF4R UP A8K7I4 TT3AF4R UC CLCA1_HUMAN TT3AF4R BC Voltage-gated ion channel TT3AF4R SN hCaCC-1; hCLCA1; Calcium-activated chloride channel regulator 1; Calcium-activated chloride channel family member 1; CaCC-1; CACC1 TT3AF4R GN CLCA1 TT3AF4R FC May be involved in mediating calcium-activated chloride conductance. May play critical roles in goblet cell metaplasia, mucus hypersecretion, cystic fibrosis and AHR. May be involved in the regulation of mucus production and/or secretion by goblet cells. Involved in the regulation of tissue inflammation in the innate immune response. May play a role as a tumor suppressor. Induces MUC5AC. TT3AF4R EC EC 3.4.-.- TT3AF4R SQ MGPFKSSVFILILHLLEGALSNSLIQLNNNGYEGIVVAIDPNVPEDETLIQQIKDMVTQASLYLLEATGKRFYFKNVAILIPETWKTKADYVRPKLETYKNADVLVAESTPPGNDEPYTEQMGNCGEKGERIHLTPDFIAGKKLAEYGPQGRAFVHEWAHLRWGVFDEYNNDEKFYLSNGRIQAVRCSAGITGTNVVKKCQGGSCYTKRCTFNKVTGLYEKGCEFVLQSRQTEKASIMFAQHVDSIVEFCTEQNHNKEAPNKQNQKCNLRSTWEVIRDSEDFKKTTPMTTQPPNPTFSLLQIGQRIVCLVLDKSGSMATGNRLNRLNQAGQLFLLQTVELGSWVGMVTFDSAAHVQNELIQINSGSDRDTLAKRLPAAASGGTSICSGLRSAFTVIRKKYPTDGSEIVLLTDGEDNTISGCFNEVKQSGAIIHTVALGPSAAQELEELSKMTGGLQTYASDQVQNNGLIDAFGALSSGNGAVSQRSIQLESKGLTLQNSQWMNGTVIVDSTVGKDTLFLITWTMQPPQILLWDPSGQKQGGFVVDKNTKMAYLQIPGIAKVGTWKYSLQASSQTLTLTVTSRASNATLPPITVTSKTNKDTSKFPSPLVVYANIRQGASPILRASVTALIESVNGKTVTLELLDNGAGADATKDDGVYSRYFTTYDTNGRYSVKVRALGGVNAARRRVIPQQSGALYIPGWIENDEIQWNPPRPEINKDDVQHKQVCFSRTSSGGSFVASDVPNAPIPDLFPPGQITDLKAEIHGGSLINLTWTAPGDDYDHGTAHKYIIRISTSILDLRDKFNESLQVNTTALIPKEANSEEVFLFKPENITFENGTDLFIAIQAVDKVDLKSEISNIARVSLFIPPQTPPETPSPDETSAPCPNIHINSTIPGIHILKIMWKWIGELQLSIA TT3AF4R TT Literature-reported TTI9XK6 ID TTI9XK6 TTI9XK6 TN Calcium-activated potassium channel KCa5.1 (KCNU1) TTI9XK6 UP A8MYU2 TTI9XK6 UC KCNU1_HUMAN TTI9XK6 BC Voltage-gated ion channel TTI9XK6 SN Slowpoke homolog 3; SLO3; Potassium channel subfamily U member 1; KCa5; KCNMC1; KCNMA3; Calcium-activated potassium channel, subfamily M subunit alpha-3; Calcium-activated potassium channel subunit alpha-3 TTI9XK6 GN KCNU1 TTI9XK6 FC Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K(+). May represent the primary spermatozoan K(+) current. In contrast to KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for fertility. May play an important role in sperm osmoregulation required for the acquisition of normal morphology and motility when faced with osmotic challenges, such as those experienced after mixing with seminal fluid and entry into the vagina. TTI9XK6 PD 4HPF TTI9XK6 SQ MFQTKLRNETWEDLPKMSCTTEIQAAFILSSFVTFFSGLIILLIFRLIWRSVKKWQIIKGTGIILELFTSGTIARSHVRSLHFQGQFRDHIEMLLSAQTFVGQVLVILVFVLSIGSLIIYFINSADPVGSCSSYEDKTIPIDLVFNAFFSFYFGLRFMAADDKIKFWLEMNSIVDIFTIPPTFISYYLKSNWLGLRFLRALRLLELPQILQILRAIKTSNSVKFSKLLSIILSTWFTAAGFIHLVENSGDPWLKGRNSQNISYFESIYLVMATTSTVGFGDVVAKTSLGRTFIMFFTLGSLILFANYIPEMVELFANKRKYTSSYEALKGKKFIVVCGNITVDSVTAFLRNFLRDKSGEINTEIVFLGETPPSLELETIFKCYLAYTTFISGSAMKWEDLRRVAVESAEACLIIANPLCSDSHAEDISNIMRVLSIKNYDSTTRIIIQILQSHNKVYLPKIPSWNWDTGDNIICFAELKLGFIAQGCLVPGLCTFLTSLFVEQNKKVMPKQTWKKHFLNSMKNKILTQRLSDDFAGMSFPEVARLCFLKMHLLLIAIEYKSLFTDGFCGLILNPPPQVRIRKNTLGFFIAETPKDVRRALFYCSVCHDDVFIPELITNCGCKSRSRQHITVPSVKRMKKCLKGISSRISGQDSPPRVSASTSSISNFTTRTLQHDVEQDSDQLDSSGMFHWCKPTSLDKVTLKRTGKSKYKFRNHIVACVFGDAHSAPMGLRNFVMPLRASNYTRKELKDIVFIGSLDYLQREWRFLWNFPQIYILPGCALYSGDLHAANIEQCSMCAVLSPPPQPSSNQTLVDTEAIMATLTIGSLQIDSSSDPSPSVSEETPGYTNGHNEKSNCRKVPILTELKNPSNIHFIEQLGGLEGSLQETNLHLSTAFSTGTVFSGSFLDSLLATAFYNYHVLELLQMLVTGGVSSQLEQHLDKDKVYGVADSCTSLLSGRNRCKLGLLSLHETILSDVNPRNTFGQLFCGSLDLFGILCVGLYRIIDEEELNPENKRFVITRPANEFKLLPSDLVFCAIPFSTACYKRNEEFSLQKSYEIVNKASQTTETHSDTNCPPTIDSVTETLYSPVYSYQPRTNSLSFPKQIAWNQSRTNSIISSQIPLGDNAKENERKTSDEVYDEDPFAYSEPL TTI9XK6 TT Literature-reported TT4AF6N ID TT4AF6N TT4AF6N TN Calgranulin A (S100A8) TT4AF6N UP P05109 TT4AF6N UC S10A8_HUMAN TT4AF6N BC S100 calcium-binding protein TT4AF6N SN Urinary stone protein band A; S100 calcium-binding protein A8; Protein S100-A8; P8; Myeloid-related protein 8; Migration inhibitory factor-related protein 8; MRP8; MRP-8; Leukocyte L1 complex light chain; Cystic fibrosis antigen; Calprotectin L1L subunit; Calgranulin-A; CFAG; CAGA TT4AF6N GN S100A8 TT4AF6N FC It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. The iNOS-S100A8/A9 transnitrosylase complex directs selective inflammatory stimulus-dependent S-nitrosylation of GAPDH and probably multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity. S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. TT4AF6N PD 6DS2; 5W1F; 5HLV; 5HLO; 4XJK TT4AF6N SQ MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE TT4AF6N TT Literature-reported TT1YHKR ID TT1YHKR TT1YHKR TN Candida AIR carboxylase (Candi ADE2) TT1YHKR UP Q92210 TT1YHKR UC PUR6_CANAL TT1YHKR BC Carbon-carbon lyase TT1YHKR SN Phosphoribosylaminoimidazole carboxylase; AIRC; AIR carboxylase TT1YHKR GN Candi ADE2 TT1YHKR FC Catalyzes the sixth step of the de novo purine biosynthesis pathway. TT1YHKR EC EC 4.1.1.21 TT1YHKR SQ MDSKTVGILGGGQLGRMIVEAAHRLNIKTVILDAAKSPAKQINALDDHVDGSFTNYDSIVKLAEKADVLTVEIEHVDVDALIKVQEKFPKVEIYPLPETIRLIQDKYLQKNHLIKHDVAVTESVAVETNTVDDLLHIGEKFGYPYMLKSRTLAYDGRGNFVVKDKSYCEKALEFLKDRPLYAEKWCPFTKELAVMVVRSLEGEVFAYPTVETIHENNICHLVYAPARIPDTLAKKASILAKNAVKSFLGCGIFGVEMFLLENNELLINEIAPRPHNSGHYTIDACVTSQFEAHVRAVTGLPMPKGFTEFSTSITNAIMLNVLGDKATPNKELEICRRALETPHASVYLYGKTTRPERKMGHINVVTSSMQDAESRLSYILGDTTEIPKSLATDKESPLVGIIMGSDSDLPVMAVGARILKQFGVPFELTIVSAHRTPHRMSEYAIEAPKRGLKCIIAGAGGAAHLPGMVAAMTPLPVIGVPVKGSTLDGVDSLHSIVQMPRGIPVATVAINNSTNAALLAIRILGAYDSKWLTEMNQYMLNMETEVLGKAETLEEIGYEDYLTDKLKK TT1YHKR TT Literature-reported TT6TDPW ID TT6TDPW TT6TDPW TN Candida PtdIns-3-kinase VPS34 (Candi VPS34) TT6TDPW UP Q92213 TT6TDPW UC VPS34_CANAX TT6TDPW BC Kinase TT6TDPW SN Vacuolar sorting protein 34; VPS34; PtdIns-3-kinase; Phosphatidylinositol 3-kinase VPS34 TT6TDPW GN Candi VPS34 TT6TDPW FC Phosphatidylinositol 3-kinase homolog required for vacuolar sorting and segregation. TT6TDPW EC EC 2.7.1.137 TT6TDPW SQ MATLSQPQSALPKTKIATTFGLSKDLKSPISVKVCYLECTRNNVSLVPLSTKFEDPTVFKKLSQIYKNSDLFVEIRVYDGKNNNLISTPVRTSYKAFNNKGRTWNQQLKLNIDYNQISIDAYLKFSICEIIDTKPSVFGVSYLSLFSHDSSTLRSGSHKIPVFMEDDPQYSKNIQYGTLIGLTDLEKRLIDYENGKYPRLNWLDKMVLPKVDATFLKTNNKDHDYYLYIELPQFEFPIVYSDIIYQIPTIEPITETTSKIPPDDTLNSNIIINSIDIPMATSHDPSIMKVYDPDFHITANNHLNPNATTFDPVELKYRKLERNIDNNTILDKELKPTPQLRDELLRIMIKPSNAESTDNEKNLIWKFRYYFSKNNSGNDPSNKSVKSFLPKFLRSINWENDYELDHTFKEIIPFYWNVDKLQIGDALELLGDYFNPYTLGKPTYQDDSMTSKSSKMKSDEKRFIKIYNNVCFLRKLAVERLKLANSEELLLYLLQLVQALKYEALIYEKSPPFCERSDQIEDNASSTLKSPLADFLIERAVENEKLGNFFYWYVKVENEDQLNNPHIDGPIKIYMDILNRYIELLKAHCHENRLPYYKHLKHQIWFIKKLTSLVELLRASFKKNEATAKKVEYLREYLANSGNELLKFPEPFPLPLDPSVMICGCYPEESSVFKSSLAPLKITLKTIEKKKHGHATSQLFGKRSRYGKYPLMFKIGDDLRQDQLVIQIIDLMDQLLKNENLDLKLTPYKILATSPISGLIQFVPNETLDSILSKTYPTSVTYSGGGETSDGPPSVSNNGILNYLRLHSQEQQSEEPISKSILSTNTSQSNTEIPVLPRQPKPTITSDLGVSPILMDNYVKSCAGYCVITYILGVGDRHLDNLLLSPNGKFWHADFGYILGRDPKPFPPLMKLPIQVIDGMGGLHHENYNVFKSYCFITYTTLRKNSNLILNLFQLMLDANIPDIQFDPSRVIEKVQEKFCLQMTEEEAILHFQNLINDSVNAFLPVVIDRLHSLAQYWRA TT6TDPW TT Literature-reported TTXPWO6 ID TTXPWO6 TTXPWO6 TN Carboxypeptidase E (CPE) TTXPWO6 UP P16870 TTXPWO6 UC CBPE_HUMAN TTXPWO6 BC Peptidase TTXPWO6 SN Prohormone processing carboxypeptidase; Enkephalin convertase; CPH; CPE TTXPWO6 GN CPE TTXPWO6 FC Removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing. Processes proinsulin. TTXPWO6 EC EC 3.4.17.10 TTXPWO6 SQ MAGRGGSALLALCGALAACGWLLGAEAQEPGAPAAGMRRRRRLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQKGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNMKKIVDQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGSAHEYSSSPDDAIFQSLARAYSSFNPAMSDPNRPPCRKNDDDSSFVDGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKFPPEETLKTYWEDNKNSLISYLEQIHRGVKGFVRDLQGNPIANATISVEGIDHDVTSAKDGDYWRLLIPGNYKLTASAPGYLAITKKVAVPYSPAAGVDFELESFSERKEEEKEELMEWWKMMSETLNF TTXPWO6 TT Literature-reported TTWAS18 ID TTWAS18 TTWAS18 TN Cardiac muscle troponin T (TNNT2) TTWAS18 UP P45379 TTWAS18 UC TNNT2_HUMAN TTWAS18 BC Troponin TTWAS18 SN TnTC; TNNT2; Cardiac troponin C (cTnC); CTnT TTWAS18 GN TNNT2 TTWAS18 FC Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. TTWAS18 PD 4Y99; 1J1E; 1J1D TTWAS18 SQ MSDIEEVVEEYEEEEQEEAAVEEEEDWREDEDEQEEAAEEDAEAEAETEETRAEEDEEEEEAKEAEDGPMEESKPKPRSFMPNLVPPKIPDGERVDFDDIHRKRMEKDLNELQALIEAHFENRKKEEEELVSLKDRIERRRAERAEQQRIRNEREKERQNRLAEERARREEEENRRKAEDEARKKKALSNMMHFGGYIQKQAQTERKSGKRQTEREKKKKILAERRKVLAIDHLNEDQLREKAKELWQSIYNLEAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK TTWAS18 TT Literature-reported TTNLDK6 ID TTNLDK6 TTNLDK6 TN Cardiac troponin I (TNNI3) TTNLDK6 UP P19429 TTNLDK6 UC TNNI3_HUMAN TTNLDK6 BC Troponin TTNLDK6 SN TNNI3 TTNLDK6 GN TNNI3 TTNLDK6 FC Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. TTNLDK6 PD 6MV3; 5WCL; 5W88; 5VLN; 4Y99 TTNLDK6 SQ MADGSSDAAREPRPAPAPIRRRSSNYRAYATEPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES TTNLDK6 TT Literature-reported TTQR5YD ID TTQR5YD TTQR5YD TN Casein kinase I gamma-1 (CSNK1G1) TTQR5YD UP Q9HCP0 TTQR5YD UC KC1G1_HUMAN TTQR5YD SN Casein kinase I isoform gamma-1; CKI-gamma 1 TTQR5YD GN CSNK1G1 TTQR5YD FC Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate (By similarity). Phosphorylates CLSPN. TTQR5YD EC EC 2.7.11.1 TTQR5YD PD 2CMW TTQR5YD SQ MDHPSREKDERQRTTKPMAQRSAHCSRPSGSSSSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLGSAGEGLPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLLSRMEYVHSKNLIYRDVKPENFLIGRQGNKKEHVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRNTPIEALCENFPEEMATYLRYVRRLDFFEKPDYEYLRTLFTDLFEKKGYTFDYAYDWVGRPIPTPVGSVHVDSGASAITRESHTHRDRPSQQQPLRNQVVSSTNGELNVDDPTGAHSNAPITAHAEVEVVEEAKCCCFFKRKRKKTAQRHK TTQR5YD TT Literature-reported TT34L5N ID TT34L5N TT34L5N TN Casein kinase I gamma-3 (CSNK1G3) TT34L5N UP Q9Y6M4 TT34L5N UC KC1G3_HUMAN TT34L5N SN Casein kinase I isoform gamma-3; CKI-gamma 3 TT34L5N GN CSNK1G3 TT34L5N FC Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate (By similarity). TT34L5N EC EC 2.7.11.1 TT34L5N PD 6GRO; 4HGS; 4HGL; 4G17; 4G16 TT34L5N SQ MENKKKDKDKSDDRMARPSGRSGHNTRGTGSSSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGKQLPTPVGAVQQDPALSSNREAHQHRDKMQQSKNQSADHRAAWDSQQANPHHLRAHLAADRHGGSVQVVSSTNGELNTDDPTAGRSNAPITAPTEVEVMDETKCCCFFKRRKRKTIQRHK TT34L5N TT Literature-reported TTJZQYH ID TTJZQYH TTJZQYH TN CASP8-FADD-like regulator (CFLAR) TTJZQYH UP O15519 TTJZQYH UC CFLAR_HUMAN TTJZQYH BC Peptidase TTJZQYH SN cFLIP; c-FLIP; Usurpin; MRIT; MACHrelated inducer of toxicity; MACH-related inducer of toxicity; Inhibitor of FLICE; IFLICE; I-FLICE; FLAME1; FLAME-1; FADDlike antiapoptotic molecule 1; FADD-like antiapoptotic molecule 1; Cellular FLICElike inhibitory protein; Cellular FLICE-like inhibitory protein; Casper; Caspaselike apoptosis regulatory protein; Caspaseeightrelated protein; Caspase-like apoptosis regulatory protein; Caspase-eight-related protein; Caspase homolog; CLARP; CASP8AP1; CASP8 and FADDlike apoptosis regulator subunit p12; CASP8 and FADDlike apoptosis regulator; CASP8 and FADD-like apoptosis regulator; CASH TTJZQYH GN CFLAR TTJZQYH FC Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity. Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. TTJZQYH PD 3H13; 3H11; 2N5R TTJZQYH SQ MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVETHLLRNPHLVSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYKQSVQGAGTSYRNVLQAAIQKSLKDPSNNFRLHNGRSKEQRLKEQLGAQQEPVKKSIQESEAFLPQSIPEERYKMKSKPLGICLIIDCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVSRGGSQSVYGVDQTHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYVVSEGQLEDSSLLEVDGPAMKNVEFKAQKRGLCTVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQERKRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTLRKKLILSYT TTJZQYH TT Literature-reported TT2SRE0 ID TT2SRE0 TT2SRE0 TN Caspase-activated deoxyribonuclease (DFFB) TT2SRE0 UP O76075 TT2SRE0 UC DFFB_HUMAN TT2SRE0 SN DFFB; DFF-40; Caspase-activated nuclease; Caspase-activated DNase; CPAN TT2SRE0 GN DFFB TT2SRE0 FC Nuclease that induces DNA fragmentation andchromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology. TT2SRE0 EC EC 3.-.-.- TT2SRE0 PD 1IBX TT2SRE0 SQ MLQKPKSVKLRALRSPRKFGVAGRSCQEVLRKGCLRFQLPERGSRLCLYEDGTELTEDYFPSVPDNAELVLLTLGQAWQGYVSDIRRFLSAFHEPQVGLIQAAQQLLCDEQAPQRQRLLADLLHNVSQNIAAETRAEDPPWFEGLESRFQSKSGYLRYSCESRIRSYLREVSSYPSTVGAEAQEEFLRVLGSMCQRLRSMQYNGSYFDRGAKGGSRLCTPEGWFSCQGPFDMDSCLSRHSINPYSNRESRILFSTWNLDHIIEKKRTIIPTLVEAIKEQDGREVDWEYFYGLLFTSENLKLVHIVCHKKTTHKLNCDPSRIYKPQTRLKRKQPVRKRQ TT2SRE0 TT Literature-reported TT3G406 ID TT3G406 TT3G406 TN Cathepsin H (CTSH) TT3G406 UP P09668 TT3G406 UC CATH_HUMAN TT3G406 BC Peptidase TT3G406 SN Pro-cathepsin H TT3G406 GN CTSH TT3G406 FC Important for the overall degradation of proteins in lysosomes. TT3G406 PD 6CZS; 6CZK; 1BZN TT3G406 SQ MWATLPLLCAGAWLLGVPVCGAAELCVNSLEKFHFKSWMSKHRKTYSTEEYHHRLQTFASNWRKINAHNNGNHTFKMALNQFSDMSFAEIKHKYLWSEPQNCSATKSNYLRGTGPYPPSVDWRKKGNFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSCHKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYPIPLV TT3G406 TT Literature-reported TTHAPJK ID TTHAPJK TTHAPJK TN C-C motif chemokine 23 (CCL23) TTHAPJK UP P55773 TTHAPJK UC CCL23_HUMAN TTHAPJK BC Cytokine: CC chemokine TTHAPJK SN Small-inducible cytokine A23; SCYA23; Myeloid progenitor inhibitory factor 1; Macrophage inflammatory protein 3; MPIF1; MPIF-1; MIP3; MIP-3; CKB-8; CK-beta-8 TTHAPJK GN CCL23 TTHAPJK FC Inhibits proliferation of myeloid progenitor cells in colony formation assays. This protein can bind heparin. Binds CCR1. CCL23(19-99), CCL23(22-99), CCL23(27-99), CCL23(30-99) are more potent chemoattractants than the small-inducible cytokine A23. Shows chemotactic activity for monocytes, resting T-lymphocytes, and neutrophils, but not for activated lymphocytes. TTHAPJK PD 1G91 TTHAPJK SQ MKVSVAALSCLMLVTALGSQARVTKDAETEFMMSKLPLENPVLLDRFHATSADCCISYTPRSIPCSLLESYFETNSECSKPGVIFLTKKGRRFCANPSDKQVQVCVRMLKLDTRIKTRKN TTHAPJK TT Literature-reported TTRSJH4 ID TTRSJH4 TTRSJH4 TN CCAAT/enhancer binding protein beta (CEBPB) TTRSJH4 UP P17676 TTRSJH4 UC CEBPB_HUMAN TTRSJH4 BC Basic leucine zipper bZIP TTRSJH4 SN Transcription factor CCAAT/enhancer-binding protein beta; Transcription factor 5; TCF5; TCF-5; PP9092; Nuclear factor NF-IL6; Liver-enriched inhibitory protein; Liver activator protein; LIP; LAP; CCAAT/enhancer-binding protein beta; C/EBP beta TTRSJH4 GN CEBPB TTRSJH4 FC Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant functions with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Plays also a role in intracellular bacteria killing. During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation. Essential for female reproduction because of a critical role in ovarian follicle development. Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation. Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. TTRSJH4 PD 6MG3; 6MG2; 6MG1; 2.00E+43; 2.00E+42 TTRSJH4 SQ MQRLVAWDPACLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPAARPGPRPPAGELGSIGDHERAIDFSPYLEPLGAPQAPAPATATDTFEAAPPAPAPAPASSGQHHDFLSDLFSDDYGGKNCKKPAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKAPPTACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASSGHC TTRSJH4 TT Literature-reported TTI6LBU ID TTI6LBU TTI6LBU TN CD74 messenger RNA (CD74 mRNA) TTI6LBU UP P04233 TTI6LBU UC HG2A_HUMAN TTI6LBU BC mRNA target TTI6LBU SN p33 (mRNA); Ii (mRNA); Ia antigenassociated invariant chain (mRNA); Ia antigen-associated invariant chain (mRNA); HLADR antigensassociated invariant chain (mRNA); HLA-DR antigens-associated invariant chain (mRNA); HLA class II histocompatibility antigen gamma chain (mRNA); DHLAG (mRNA) TTI6LBU GN CD74 TTI6LBU FC Serves as cell surface receptor for the cytokine MIF. Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to the endosomal/lysosomal system where the antigen processing and binding of antigenic peptides to MHC class II takes place. TTI6LBU PD 5KSV; 5KSU; 4X5W; 4AH2; 4AEN TTI6LBU SQ MHRRRSRSCREDQKPVMDDQRDLISNNEQLPMLGRRPGAPESKCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKPPKPVSKMRMATPLLMQALPMGALPQGPMQNATKYGNMTEDHVMHLLQNADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPTDAPPKVLTKCQEEVSHIPAVHPGSFRPKCDENGNYLPLQCYGSIGYCWCVFPNGTEVPNTRSRGHHNCSESLELEDPSSGLGVTKQDLGPVPM TTI6LBU TT Literature-reported TTI6LBU FM mRNA target TT5Z0EF ID TT5Z0EF TT5Z0EF TN CDC42 binding protein kinase alpha (DMPK-like alpha) TT5Z0EF UP Q5VT25 TT5Z0EF UC MRCKA_HUMAN TT5Z0EF BC Kinase TT5Z0EF SN Serine/threonine-protein kinase MRCK alpha; Myotonic dystrophy protein kinase-like alpha; Myotonic dystrophy kinase-related CDC42-binding kinase alpha; MRCK alpha; KIAA0451; CDC42-binding protein kinase alpha TT5Z0EF GN CDC42BPA TT5Z0EF FC Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2. In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates: PPP1R12A, LIMK1 and LIMK2. May play a role in TFRC-mediated iron uptake. In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation. Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. TT5Z0EF EC EC 2.7.11.1 TT5Z0EF SQ MSGEVRLRQLEQFILDGPAQTNGQCFSVETLLDILICLYDECNNSPLRREKNILEYLEWAKPFTSKVKQMRLHREDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDNKWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVIAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPAQVTDVSENAKDLIRRLICSREHRLGQNGIEDFKKHPFFSGIDWDNIRNCEAPYIPEVSSPTDTSNFDVDDDCLKNSETMPPPTHTAFSGHHLPFVGFTYTSSCVLSDRSCLRVTAGPTSLDLDVNVQRTLDNNLATEAYERRIKRLEQEKLELSRKLQESTQTVQALQYSTVDGPLTASKDLEIKNLKEEIEKLRKQVTESSHLEQQLEEANAVRQELDDAFRQIKAYEKQIKTLQQEREDLNKELVQASERLKNQSKELKDAHCQRKLAMQEFMEINERLTELHTQKQKLARHVRDKEEEVDLVMQKVESLRQELRRTERAKKELEVHTEALAAEASKDRKLREQSEHYSKQLENELEGLKQKQISYSPGVCSIEHQQEITKLKTDLEKKSIFYEEELSKREGIHANEIKNLKKELHDSEGQQLALNKEIMILKDKLEKTRRESQSEREEFESEFKQQYEREKVLLTEENKKLTSELDKLTTLYENLSIHNQQLEEEVKDLADKKESVAHWEAQITEIIQWVSDEKDARGYLQALASKMTEELEALRNSSLGTRATDMPWKMRRFAKLDMSARLELQSALDAEIRAKQAIQEELNKVKASNIITECKLKDSEKKNLELLSEIEQLIKDTEELRSEKGIEHQDSQHSFLAFLNTPTDALDQFERSPSCTPASKGRRTVDSTPLSVHTPTLRKKGCPGSTGFPPKRKTHQFFVKSFTTPTKCHQCTSLMVGLIRQGCSCEVCGFSCHITCVNKAPTTCPVPPEQTKGPLGIDPQKGIGTAYEGHVRIPKPAGVKKGWQRALAIVCDFKLFLYDIAEGKASQPSVVISQVIDMRDEEFSVSSVLASDVIHASRKDIPCIFRVTASQLSASNNKCSILMLADTENEKNKWVGVLSELHKILKKNKFRDRSVYVPKEAYDSTLPLIKTTQAAAIIDHERIALGNEEGLFVVHVTKDEIIRVGDNKKIHQIELIPNDQLVAVISGRNRHVRLFPMSALDGRETDFYKLSETKGCQTVTSGKVRHGALTCLCVAMKRQVLCYELFQSKTRHRKFKEIQVPYNVQWMAIFSEQLCVGFQSGFLRYPLNGEGNPYSMLHSNDHTLSFIAHQPMDAICAVEISSKEYLLCFNSIGIYTDCQGRRSRQQELMWPANPSSCCYNAPYLSVYSENAVDIFDVNSMEWIQTLPLKKVRPLNNEGSLNLLGLETIRLIYFKNKMAEGDELVVPETSDNSRKQMVRNINNKRRYSFRVPEEERMQQRREMLRDPEMRNKLISNPTNFNHIAHMGPGDGIQILKDLPMNPRPQESRTVFSGSVSIPSITKSRPEPGRSMSASSGLSARSSAQNGSALKREFSGGSYSAKRQPMPSPSEGSLSSGGMDQGSDAPARDFDGEDSDSPRHSTASNSSNLSSPPSPASPRKTKSLSLESTDRGSWDP TT5Z0EF TT Literature-reported TTT9MRQ ID TTT9MRQ TTT9MRQ TN Cell surface protein HB15 (CD83) TTT9MRQ UP Q01151 TTT9MRQ UC CD83_HUMAN TTT9MRQ BC Immunoglobulin TTT9MRQ SN hCD83; CD83 antigen; Bcell activation protein; B-cell activation protein TTT9MRQ GN CD83 TTT9MRQ FC May play a significant role in antigen presentation or the cellular interactions that follow lymphocyte activation. TTT9MRQ PD 5MJ2; 5MJ1; 5MJ0; 5MIX TTT9MRQ SQ MSRGLQLLLLSCAYSLAPATPEVKVACSEDVDLPCTAPWDPQVPYTVSWVKLLEGGEERMETPQEDHLRGQHYHQKGQNGSFDAPNERPYSLKIRNTTSCNSGTYRCTLQDPDGQRNLSGKVILRVTGCPAQRKEETFKKYRAEIVLLLALVIFYLTLIIFTCKFARLQSIFPDFSKAGMERAFLPVTSPNKHLGLVTPHKTELV TTT9MRQ TT Literature-reported TTT9MRQ FM Immunoglobulin superfamily TTV2DON ID TTV2DON TTV2DON TN Cellular retinol binding protein III (RBP5) TTV2DON UP P82980 TTV2DON UC RET5_HUMAN TTV2DON BC Calycin family TTV2DON SN Retinol-binding protein 5; RBP5; HRBPiso; CRBP-III TTV2DON GN RBP5 TTV2DON FC Intracellular transport of retinol. TTV2DON PD 6E5W; 1GGL TTV2DON SQ MPPNLTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSVDGRKCQTIVTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQVFRKVR TTV2DON TT Literature-reported TTOM5AU ID TTOM5AU TTOM5AU TN c-Fos messenger RNA (c-Fos mRNA) TTOM5AU UP P01100 TTOM5AU UC FOS_HUMAN TTOM5AU BC mRNA target TTOM5AU SN Proto-oncogene c-Fos (mRNA); G0S7 (mRNA); G0/G1 switch regulatory protein 7 (mRNA); Cellular oncogene fos (mRNA); C-fos (mRNA) TTOM5AU GN FOS TTOM5AU FC In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum. Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. TTOM5AU PD 1S9K; 1FOS; 1A02 TTOM5AU SQ MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL TTOM5AU TT Literature-reported TTOM5AU FM mRNA target TTZC6DR ID TTZC6DR TTZC6DR TN cGMP-dependent protein kinase (cGK) TTZC6DR UP Q13976; Q13237 TTZC6DR UC KGP1_HUMAN; KGP2_HUMAN TTZC6DR BC Kinase TTZC6DR SN cGK; PRKGR TTZC6DR GN PRKG1; PRKG2 TTZC6DR FC Activated by cGMP. Phosphorylates a number of biologically important targets and is implicated in the regulation of smooth muscle relaxation, platelet function, sperm metabolism, cell division, and nucleic acid synthesis. TTZC6DR SQ MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDSPSEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDSFPEDNDEPPPDDNSGWDIDF TTZC6DR TT Literature-reported TTT4N0Q ID TTT4N0Q TTT4N0Q TN Channel-activating protease 1 (CAP1) TTT4N0Q UP Q16651 TTT4N0Q UC PRSS8_HUMAN TTT4N0Q SN Serine protease 8; Prostasin; CAP1 TTT4N0Q GN PRSS8 TTT4N0Q FC Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates. Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G). TTT4N0Q EC EC 3.4.21.- TTT4N0Q PD 3GYM; 3GYL; 3FVF; 3E1X; 3E0P TTT4N0Q SQ MAQKGVLGPGQLGAVAILLYLGLLRSGTGAEGAEAPCGVAPQARITGGSSAVAGQWPWQVSITYEGVHVCGGSLVSEQWVLSAAHCFPSEHHKEAYEVKLGAHQLDSYSEDAKVSTLKDIIPHPSYLQEGSQGDIALLQLSRPITFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLLTPKPLQQLEVPLISRETCNCLYNIDAKPEEPHFVQEDMVCAGYVEGGKDACQGDSGGPLSCPVEGLWYLTGIVSWGDACGARNRPGVYTLASSYASWIQSKVTELQPRVVPQTQESQPDSNLCGSHLAFSSAPAQGLLRPILFLPLGLALGLLSPWLSEH TTT4N0Q TT Literature-reported TTUYAF3 ID TTUYAF3 TTUYAF3 TN Chloride channel protein 1 (ClC-1) TTUYAF3 UP P35523 TTUYAF3 UC CLCN1_HUMAN TTUYAF3 BC Chloride channel TTUYAF3 SN ClC-1; Chloride channel protein, skeletal muscle; CLC1 TTUYAF3 GN CLCN1 TTUYAF3 FC Voltage-gated chloride channel. Plays an important role in membrane repolarization in skeletal muscle cells after muscle contraction. TTUYAF3 PD 6QVU; 6QVD; 6QVC; 6QVB; 6QV6 TTUYAF3 SQ MEQSRSQQRGGEQSWWGSDPQYQYMPFEHCTSYGLPSENGGLQHRLRKDAGPRHNVHPTQIYGHHKEQFSDREQDIGMPKKTGSSSTVDSKDEDHYSKCQDCIHRLGQVVRRKLGEDGIFLVLLGLLMALVSWSMDYVSAKSLQAYKWSYAQMQPSLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSVFCGVYEQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHRQVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASFTFPPGMGQFMAGELMPREAISTLFDNNTWVKHAGDPESLGQSAVWIHPRVNVVIIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGILFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPDLGWNQLSKYTIFVEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDSMILLGSVERSELQALLQRHLCPERRLRAAQEMARKLSELPYDGKARLAGEGLPGAPPGRPESFAFVDEDEDEDLSGKSELPPSLALHPSTTAPLSPEEPNGPLPGHKQQPEAPEPAGQRPSIFQSLLHCLLGRARPTKKKTTQDSTDLVDNMSPEEIEAWEQEQLSQPVCFDSCCIDQSPFQLVEQTTLHKTHTLFSLLGLHLAYVTSMGKLRGVLALEELQKAIEGHTKSGVQLRPPLASFRNTTSTRKSTGAPPSSAENWNLPEDRPGATGTGDVIAASPETPVPSPSPEPPLSLAPGKVEGELEELELVESPGLEEELADILQGPSLRSTDEEDEDELIL TTUYAF3 TT Literature-reported TT823N1 ID TT823N1 TT823N1 TN Chloride channel protein ClC-Ka (ClC-K1) TT823N1 UP P51800 TT823N1 UC CLCKA_HUMAN TT823N1 BC Chloride channel TT823N1 SN ClC-K1; Chloride channel Ka TT823N1 GN CLCNKA TT823N1 FC Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. May be important in urinary concentrating mechanisms. TT823N1 PD 2PFI TT823N1 SQ MEELVGLREGFSGDPVTLQELWGPCPHIRRAIQGGLEWLKQKVFRLGEDWYFLMTLGVLMALVSYAMNFAIGCVVRAHQWLYREIGDSHLLRYLSWTVYPVALVSFSSGFSQSITPSSGGSGIPELKTMLAGVILEDYLDIKNFGAKVVGLSCTLATGSTLFLGKVGPFVHLSVMIAAYLGRVRTTTIGEPENKSKQNEMLVAAAAVGVATVFAAPFSGVLFSIEVMSSHFSVRDYWRGFFAATCGAFIFRLLAVFNSEQETITSLYKTSFRVDVPFDLPEIFFFVALGGICGVLSCAYLFCQRTFLSFIKTNRYSSKLLATSKPVYSALATLLLASITYPPGVGHFLASRLSMKQHLDSLFDNHSWALMTQNSSPPWPEELDPQHLWWEWYHPRFTIFGTLAFFLVMKFWMLILATTIPMPAGYFMPIFILGAAIGRLLGEALAVAFPEGIVTGGVTNPIMPGGYALAGAAAFSGAVTHTISTALLAFELTGQIVHALPVLMAVLAANAIAQSCQPSFYDGTIIVKKLPYLPRILGRNIGSHHVRVEHFMNHSITTLAKDTPLEEVVKVVTSTDVTEYPLVESTESQILVGIVQRAQLVQALQAEPPSRAPGHQQCLQDILARGCPTEPVTLTLFSETTLHQAQNLFKLLNLQSLFVTSRGRAVGCVSWVEMKKAISNLTNPPAPK TT823N1 TT Literature-reported TT3RMNA ID TT3RMNA TT3RMNA TN Chymotrypsin-C (CLCR) TT3RMNA UP Q99895 TT3RMNA UC CTRC_HUMAN TT3RMNA SN Caldecrin; CLCR TT3RMNA GN CTRC TT3RMNA FC Regulates activation and degradation of trypsinogens and procarboxypeptidases by targeting specific cleavage sites within their zymogen precursors. Has chymotrypsin-type protease activity and hypocalcemic activity. TT3RMNA EC EC 3.4.21.2 TT3RMNA PD 4H4F TT3RMNA SQ MLGITVLAALLACASSCGVPSFPPNLSARVVGGEDARPHSWPWQISLQYLKNDTWRHTCGGTLIASNFVLTAAHCISNTRTYRVAVGKNNLEVEDEEGSLFVGVDTIHVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWTNGPIADKLQQGLQPVVDHATCSRIDWWGFRVKKTMVCAGGDGVISACNGDSGGPLNCQLENGSWEVFGIVSFGSRRGCNTRKKPVVYTRVSAYIDWINEKMQL TT3RMNA TT Patented-recorded TTQST3U ID TTQST3U TTQST3U TN CIRL-3 messenger RNA (CIRL-3 mRNA) TTQST3U UP Q9HAR2 TTQST3U UC AGRL3_HUMAN TTQST3U BC mRNA target TTQST3U SN Lectomedin-3 (mRNA); Latrophilin-3 (mRNA); LPHN3 (mRNA); LEC3 (mRNA); KIAA0768 (mRNA); Calcium-independent alpha-latrotoxin receptor 3 (mRNA); CIRL-3 (mRNA); Adhesion G protein-coupled receptor L3 (mRNA) TTQST3U GN ADGRL3 TTQST3U FC Plays a role in the development of glutamatergic synapses in the cortex. Important in determining the connectivity rates between the principal neurons in the cortex. Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells. TTQST3U PD 5CMN TTQST3U SQ MWPSQLLIFMMLLAPIIHAFSRAPIPMAVVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCPGTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDTSPYRWGGKSDIDLAVDENGLWVIYATEQNNGKIVISQLNPYTLRIEGTWDTAYDKRSASNAFMICGILYVVKSVYEDDDNEATGNKIDYIYNTDQSKDSLVDVPFPNSYQYIAAVDYNPRDNLLYVWNNYHVVKYSLDFGPLDSRSGQAHHGQVSYISPPIHLDSELERPSVKDISTTGPLGMGSTTTSTTLRTTTLSPGRSTTPSVSGRRNRSTSTPSPAVEVLDDMTTHLPSASSQIPALEESCEAVEAREIMWFKTRQGQIAKQPCPAGTIGVSTYLCLAPDGIWDPQGPDLSNCSSPWVNHITQKLKSGETAANIARELAEQTRNHLNAGDITYSVRAMDQLVGLLDVQLRNLTPGGKDSAARSLNKAMVETVNNLLQPQALNAWRDLTTSDQLRAATMLLHTVEESAFVLADNLLKTDIVRENTDNIKLEVARLSTEGNLEDLKFPENMGHGSTIQLSANTLKQNGRNGEIRVAFVLYNNLGPYLSTENASMKLGTEALSTNHSVIVNSPVITAAINKEFSNKVYLADPVVFTVKHIKQSEENFNPNCSFWSYSKRTMTGYWSTQGCRLLTTNKTHTTCSCNHLTNFAVLMAHVEVKHSDAVHDLLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFTWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLNVIFLGIALYKMFHHTAILKPESGCLDNIKSWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIFIFHCVLQKKVRKEYGKCLRTHCCSGKSTESSIGSGKTSGSRTPGRYSTGSQSRIRRMWNDTVRKQSESSFITGDINSSASLNREGLLNNARDTSVMDTLPLNGNHGNSYSIASGEYLSNCVQIIDRGYNHNETALEKKILKELTSNYIPSYLNNHERSSEQNRNLMNKLVNNLGSGREDDAIVLDDATSFNHEESLGLELIHEESDAPLLPPRVYSTENHQPHHYTRRRIPQDHSESFFPLLTNEHTEDLQSPHRDSLYTSMPTLAGVAATESVTTSTQTEPPPAKCGDAEDVYYKSMPNLGSRNHVHQLHTYYQLGRGSSDGFIVPPNKDGTPPEGSSKGPAHLVTSL TTQST3U TT Literature-reported TTQST3U FM mRNA target TTSJIRP ID TTSJIRP TTSJIRP TN Connexin 32 messenger RNA (GJB1 mRNA) TTSJIRP UP P08034 TTSJIRP UC CXB1_HUMAN TTSJIRP BC mRNA target TTSJIRP SN Gap junction beta-1 protein (mRNA); GAP junction 28 kDa liver protein (mRNA); CX32 (mRNA) TTSJIRP GN GJB1 TTSJIRP FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTSJIRP PD 5KK9; 1TXH TTSJIRP SQ MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGCNSVCYDQFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHGDPLHLEEVKRHKVHISGTLWWTYVISVVFRLLFEAVFMYVFYLLYPGYAMVRLVKCDVYPCPNTVDCFVSRPTEKTVFTVFMLAASGICIILNVAEVVYLIIRACARRAQRRSNPPSRKGSGFGHRLSPEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC TTSJIRP TT Literature-reported TTSJIRP FM mRNA target TTHWA40 ID TTHWA40 TTHWA40 TN Connexin-32 (Cx32) TTHWA40 UP P08034 TTHWA40 UC CXB1_HUMAN TTHWA40 BC Gap junction-forming connexin TTHWA40 SN Gap junction beta-1 protein; GAP junction 28 kDa liver protein; CX32 TTHWA40 GN GJB1 TTHWA40 FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTHWA40 PD 5KK9; 1TXH TTHWA40 SQ MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGCNSVCYDQFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHGDPLHLEEVKRHKVHISGTLWWTYVISVVFRLLFEAVFMYVFYLLYPGYAMVRLVKCDVYPCPNTVDCFVSRPTEKTVFTVFMLAASGICIILNVAEVVYLIIRACARRAQRRSNPPSRKGSGFGHRLSPEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC TTHWA40 TT Literature-reported TTEP7OC ID TTEP7OC TTEP7OC TN Connexin-45 (Cx45) TTEP7OC UP P36383 TTEP7OC UC CXG1_HUMAN TTEP7OC BC Gap junction-forming connexin TTEP7OC SN Gap junction gamma-1 protein; Gap junction alpha-7 protein; GJA7 TTEP7OC GN GJC1 TTEP7OC FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTEP7OC PD 3SHW TTEP7OC SQ MSWSFLTRLLEEIHNHSTFVGKIWLTVLIVFRIVLTAVGGESIYYDEQSKFVCNTEQPGCENVCYDAFAPLSHVRFWVFQIILVATPSVMYLGYAIHKIAKMEHGEADKKAARSKPYAMRWKQHRALEETEEDNEEDPMMYPEMELESDKENKEQSQPKPKHDGRRRIREDGLMKIYVLQLLARTVFEVGFLIGQYFLYGFQVHPFYVCSRLPCPHKIDCFISRPTEKTIFLLIMYGVTGLCLLLNIWEMLHLGFGTIRDSLNSKRRELEDPGAYNYPFTWNTPSAPPGYNIAVKPDQIQYTELSNAKIAYKQNKANTAQEQQYGSHEENLPADLEALQREIRMAQERLDLAVQAYSHQNNPHGPREKKAKVGSKAGSNKSTASSKSGDGKTSVWI TTEP7OC TT Literature-reported TTPR8FK ID TTPR8FK TTPR8FK TN Contactin-1 (CNTN1) TTPR8FK UP Q12860 TTPR8FK UC CNTN1_HUMAN TTPR8FK BC Immunoglobulin TTPR8FK SN Neural cell surface protein F3; Glycoprotein gp135; CNTN1 TTPR8FK GN CNTN1 TTPR8FK FC Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth. TTPR8FK PD 3S97; 2EE2 TTPR8FK SQ MKMWLLVSHLVIISITTCLAEFTWYRRYGHGVSEEDKGFGPIFEEQPINTIYPEESLEGKVSLNCRARASPFPVYKWRMNNGDVDLTSDRYSMVGGNLVINNPDKQKDAGIYYCLASNNYGMVRSTEATLSFGYLDPFPPEERPEVRVKEGKGMVLLCDPPYHFPDDLSYRWLLNEFPVFITMDKRRFVSQTNGNLYIANVEASDKGNYSCFVSSPSITKSVFSKFIPLIPIPERTTKPYPADIVVQFKDVYALMGQNVTLECFALGNPVPDIRWRKVLEPMPSTAEISTSGAVLKIFNIQLEDEGIYECEAENIRGKDKHQARIYVQAFPEWVEHINDTEVDIGSDLYWPCVATGKPIPTIRWLKNGYAYHKGELRLYDVTFENAGMYQCIAENTYGAIYANAELKILALAPTFEMNPMKKKILAAKGGRVIIECKPKAAPKPKFSWSKGTEWLVNSSRILIWEDGSLEINNITRNDGGIYTCFAENNRGKANSTGTLVITDPTRIILAPINADITVGENATMQCAASFDPALDLTFVWSFNGYVIDFNKENIHYQRNFMLDSNGELLIRNAQLKHAGRYTCTAQTIVDNSSASADLVVRGPPGPPGGLRIEDIRATSVALTWSRGSDNHSPISKYTIQTKTILSDDWKDAKTDPPIIEGNMEAARAVDLIPWMEYEFRVVATNTLGRGEPSIPSNRIKTDGAAPNVAPSDVGGGGGRNRELTITWAPLSREYHYGNNFGYIVAFKPFDGEEWKKVTVTNPDTGRYVHKDETMSPSTAFQVKVKAFNNKGDGPYSLVAVINSAQDAPSEAPTEVGVKVLSSSEISVHWEHVLEKIVESYQIRYWAAHDKEEAANRVQVTSQEYSARLENLLPDTQYFIEVGACNSAGCGPPSDMIEAFTKKAPPSQPPRIISSVRSGSRYIITWDHVVALSNESTVTGYKVLYRPDGQHDGKLYSTHKHSIEVPIPRDGEYVVEVRAHSDGGDGVVSQVKISGAPTLSPSLLGLLLPAFGILVYLEF TTPR8FK TT Literature-reported TT2Z1WB ID TT2Z1WB TT2Z1WB TN Contactin-2 (CNTN2) TT2Z1WB UP Q02246 TT2Z1WB UC CNTN2_HUMAN TT2Z1WB BC Basigin family TT2Z1WB SN Transient axonal glycoprotein 1; TAX-1 gene; TAX-1; CNTN2; Axonin-1; Axonal glycoprotein TAG-1 TT2Z1WB GN CNTN2 TT2Z1WB FC In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region. May be involved in cell adhesion. TT2Z1WB PD 2OM5 TT2Z1WB SQ MGTATRRKPHLLLVAAVALVSSSAWSSALGSQTTFGPVFEDQPLSVLFPEESTEEQVLLACRARASPPATYRWKMNGTEMKLEPGSRHQLVGGNLVIMNPTKAQDAGVYQCLASNPVGTVVSREAILRFGFLQEFSKEERDPVKAHEGWGVMLPCNPPAHYPGLSYRWLLNEFPNFIPTDGRHFVSQTTGNLYIARTNASDLGNYSCLATSHMDFSTKSVFSKFAQLNLAAEDTRLFAPSIKARFPAETYALVGQQVTLECFAFGNPVPRIKWRKVDGSLSPQWTTAEPTLQIPSVSFEDEGTYECEAENSKGRDTVQGRIIVQAQPEWLKVISDTEADIGSNLRWGCAAAGKPRPTVRWLRNGEPLASQNRVEVLAGDLRFSKLSLEDSGMYQCVAENKHGTIYASAELAVQALAPDFRLNPVRRLIPAARGGEILIPCQPRAAPKAVVLWSKGTEILVNSSRVTVTPDGTLIIRNISRSDEGKYTCFAENFMGKANSTGILSVRDATKITLAPSSADINLGDNLTLQCHASHDPTMDLTFTWTLDDFPIDFDKPGGHYRRTNVKETIGDLTILNAQLRHGGKYTCMAQTVVDSASKEATVLVRGPPGPPGGVVVRDIGDTTIQLSWSRGFDNHSPIAKYTLQARTPPAGKWKQVRTNPANIEGNAETAQVLGLTPWMDYEFRVIASNILGTGEPSGPSSKIRTREAAPSVAPSGLSGGGGAPGELIVNWTPMSREYQNGDGFGYLLSFRRQGSTHWQTARVPGADAQYFVYSNESVRPYTPFEVKIRSYNRRGDGPESLTALVYSAEEEPRVAPTKVWAKGVSSSEMNVTWEPVQQDMNGILLGYEIRYWKAGDKEAAADRVRTAGLDTSARVSGLHPNTKYHVTVRAYNRAGTGPASPSANATTMKPPPRRPPGNISWTFSSSSLSIKWDPVVPFRNESAVTGYKMLYQNDLHLTPTLHLTGKNWIEIPVPEDIGHALVQIRTTGPGGDGIPAEVHIVRNGGTSMMVENMAVRPAPHPGTVISHSVAMLILIGSLEL TT2Z1WB TT Literature-reported TT7LJGM ID TT7LJGM TT7LJGM TN Coronavirus Nucleocapsid messenger RNA (HCoV Nucleoprotein mRNA) TT7LJGM UP P15130 TT7LJGM UC NCAP_CVH22 TT7LJGM BC mRNA target TT7LJGM SN Nc of HCoV (mRNA); N of HCoV (mRNA) TT7LJGM GN HCoV Nucleoprotein mRNA TT7LJGM FC Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. TT7LJGM SQ MATVKWADASEPQRGRQGRIPYSLYSPLLVDSEQPWKVIPRNLVPINKKDKNKLIGYWNVQKRFRTRKGKRVDLSPKLHFYYLGTGPHKDAKFRERVEGVVWVAVDGAKTEPTGYGVRRKNSEPEIPHFNQKLPNGVTVVEEPDSRAPSRSQSRSQSRGRGESKPQSRNPSSDRNHNSQDDIMKAVAAALKSLGFDKPQEKDKKSAKTGTPKPSRNQSPASSQTSAKSLARSQSSETKEQKHEMQKPRWKRQPNDDVTSNVTQCFGPRDLDHNFGSAGVVANGVKAKGYPQFAELVPSTAAMLFDSHIVSKESGNTVVLTFTTRVTVPKDHPHLGKFLEELNAFTREMQQHPLLNPSALEFNPSQTSPATAEPVRDEVSIETDIIDEVN TT7LJGM TT Literature-reported TT7LJGM FM mRNA target TTA7YIZ ID TTA7YIZ TTA7YIZ TN Corticoliberin (CRH) TTA7YIZ UP P06850 TTA7YIZ UC CRF_HUMAN TTA7YIZ SN Corticotropin-releasing hormone; Corticotropin-releasing factor; Corticotropin releasing hormone; Corticotropin; CRF; Adrenocorticotropic hormone TTA7YIZ GN CRH TTA7YIZ FC Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile. Hormone regulating the release of corticotropin from pituitary gland. TTA7YIZ PD 3EHU; 3EHT; 1GOE; 1GO9 TTA7YIZ SQ MRLPLLVSAGVLLVALLPCPPCRALLSRGPVPGARQAPQHPQPLDFFQPPPQSEQPQQPQARPVLLRMGEEYFLRLGNLNKSPAAPLSPASSLLAGGSGSRPSPEQATANFFRVLLQQLLLPRRSLDSPAALAERGARNALGGHQEAPERERRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEIIGK TTA7YIZ TT Literature-reported TTA7YIZ KE hsa04730:Long-term depression; hsa05034:Alcoholism TTA7YIZ RC R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-418555:G alpha (s) signalling events TT21AKM ID TT21AKM TT21AKM TN Corticotropin-lipotropin (POMC) TT21AKM UP P01189 TT21AKM UC COLI_HUMAN TT21AKM SN Pro-opiomelanocortin TT21AKM GN POMC TT21AKM FC Corticotropin: Stimulates the adrenal glands to release cortisol. TT21AKM PD 4Y49; 4XPD; 4XNH TT21AKM SQ MPRSCCSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLECIRACKPDLSAETPMFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNSSSSGSSGAGQKREDVSAGEDCGPLPEGGPEPRSDGAKPGPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAEAFPLEFKRELTGQRLREGDGPDGPADDGAGAQADLEHSLLVAAEKKDEGPYRMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE TT21AKM TT Literature-reported TT21AKM KE hsa04916:Melanogenesis; hsa04920:Adipocytokine signaling pathway TT21AKM RC R-HSA-193048:Androgen biosynthesis; R-HSA-194002:Glucocorticoid biosynthesis; R-HSA-211976:Endogenous sterols; R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events; R-HSA-418594:G alpha (i) signalling events TTFWETR ID TTFWETR TTFWETR TN CREB-regulated transcription coactivator 2 (TORC2) TTFWETR UP Q53ET0 TTFWETR UC CRTC2_HUMAN TTFWETR BC Transducer of regulated CREB TTFWETR SN Transducer of regulated cAMP response elementbinding protein 2; Transducer of CREB protein 2; CRTC2; CREBregulated transcription coactivator 2 TTFWETR GN CRTC2 TTFWETR FC Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133'phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific genes such as thesteroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). TTFWETR PD 4HTM TTFWETR SQ MATSGANGPGSATASASNPRKFSEKIALQKQRQAEETAAFEEVMMDIGSTRLQAQKLRLAYTRSSHYGGSLPNVNQIGSGLAEFQSPLHSPLDSSRSTRHHGLVERVQRDPRRMVSPLRRYTRHIDSSPYSPAYLSPPPESSWRRTMAWGNFPAEKGQLFRLPSALNRTSSDSALHTSVMNPSPQDTYPGPTPPSILPSRRGGILDGEMDPKVPAIEENLLDDKHLLKPWDAKKLSSSSSRPRSCEVPGINIFPSPDQPANVPVLPPAMNTGGSLPDLTNLHFPPPLPTPLDPEETAYPSLSGGNSTSNLTHTMTHLGISRGMGLGPGYDAPGLHSPLSHPSLQSSLSNPNLQASLSSPQPQLQGSHSHPSLPASSLARHVLPTTSLGHPSLSAPALSSSSSSSSTSSPVLGAPSYPASTPGASPHHRRVPLSPLSLLAGPADARRSQQQLPKQFSPTMSPTLSSITQGVPLDTSKLSTDQRLPPYPYSSPSLVLPTQPHTPKSLQQPGLPSQSCSVQSSGGQPPGRQSHYGTPYPPGPSGHGQQSYHRPMSDFNLGNLEQFSMESPSASLVLDPPGFSEGPGFLGGEGPMGGPQDPHTFNHQNLTHCSRHGSGPNIILTGDSSPGFSKEIAAALAGVPGFEVSAAGLELGLGLEDELRMEPLGLEGLNMLSDPCALLPDPAVEESFRSDRLQ TTFWETR TT Literature-reported TT2BVUA ID TT2BVUA TT2BVUA TN C-X-C chemokine receptor type 6 (CXCR6) TT2BVUA UP O00574 TT2BVUA UC CXCR6_HUMAN TT2BVUA BC GPCR rhodopsin TT2BVUA SN TYMSTR; STRL33; G-protein coupled receptor bonzo; G-protein coupled receptor STRL33; G protein-coupled receptor bonzo; G protein-coupled receptor STRL33; Chemokine receptor CXCR6; CXCR-6; CXC-R6; CDw186; CD186; BONZO TT2BVUA GN CXCR6 TT2BVUA FC Used as a coreceptor by SIVs and by strains of HIV-2 and m-tropic HIV-1. Receptor for the C-X-C chemokine CXCL16. TT2BVUA SQ MAEHDYHEDYGFSSFNDSSQEEHQDFLQFSKVFLPCMYLVVFVCGLVGNSLVLVISIFYHKLQSLTDVFLVNLPLADLVFVCTLPFWAYAGIHEWVFGQVMCKSLLGIYTINFYTSMLILTCITVDRFIVVVKATKAYNQQAKRMTWGKVTSLLIWVISLLVSLPQIIYGNVFNLDKLICGYHDEAISTVVLATQMTLGFFLPLLTMIVCYSVIIKTLLHAGGFQKHRSLKIIFLVMAVFLLTQMPFNLMKFIRSTHWEYYAMTSFHYTIMVTEAIAYLRACLNPVLYAFVSLKFRKNFWKLVKDIGCLPYLGVSHQWKSSEDNSKTFSASHNVEATSMFQL TT2BVUA TT Literature-reported TT2BVUA FM GPCR rhodopsin TT2BVUA KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway TT2BVUA RC R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTLK1RW ID TTLK1RW TTLK1RW TN C-X-C motif chemokine 1 (CXCL1) TTLK1RW UP P09341 TTLK1RW UC GROA_HUMAN TTLK1RW BC Cytokine: CXC chemokine TTLK1RW SN SCYB1; Neutrophil-activating protein 3; NAP-3; Melanoma growth stimulatory activity; MGSA; Growth-regulated alpha protein; Growth regulated protein; GROA; GRO1; GRO-alpha(1-73); GRO-alpha; GRO-a protein; GRO TTLK1RW GN CXCL1 TTLK1RW FC May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity. Has chemotactic activity for neutrophils. TTLK1RW PD 1ROD; 1MSH; 1MSG; 1MGS TTLK1RW SQ MARAALSAAPSNPRLLRVALLLLLLVAAGRRAAGASVATELRCQCLQTLQGIHPKNIQSVNVKSPGPHCAQTEVIATLKNGRKACLNPASPIVKKIIEKMLNSDKSN TTLK1RW TT Literature-reported TTLK1RW FM Intercrine-alpha family TTWG0RE ID TTWG0RE TTWG0RE TN C-X-C motif chemokine 11 (CXCL11) TTWG0RE UP O14625 TTWG0RE UC CXL11_HUMAN TTWG0RE BC Cytokine: CXC chemokine TTWG0RE SN Small-inducible cytokine B11; SCYB9B; SCYB11; Interferon-inducible T-cell alpha chemoattractant; Interferon gamma-inducible protein 9; ITAC; IP-9; I-TAC; H174; Beta-R1 TTWG0RE GN CXCL11 TTWG0RE FC Induces calcium release in activated T-cells. Binds to CXCR3. May play an important role in CNS diseases which involve T-cell recruitment. May play a role in skin immune responses. Chemotactic for interleukin-activated T-cells but not unstimulated T-cells, neutrophils or monocytes. TTWG0RE PD 1RJT TTWG0RE SQ MSVKGMAIALAVILCATVVQGFPMFKRGRCLCIGPGVKAVKVADIEKASIMYPSNNCDKIEVIITLKENKGQRCLNPKSKQARLIIKKVERKNF TTWG0RE TT Literature-reported TT0NIZ1 ID TT0NIZ1 TT0NIZ1 TN C-X-C motif chemokine 13 (CXCL13) TT0NIZ1 UP O43927 TT0NIZ1 UC CXL13_HUMAN TT0NIZ1 BC Cytokine: CXC chemokine TT0NIZ1 SN Smallinducible cytokine B13; Small-inducible cytokine B13; SCYB13; CXC chemokine BLC; BLC; BCA1; BCA-1; B lymphocyte chemoattractant; B cellattracting chemokine 1; B cell-attracting chemokine 1; Angie TT0NIZ1 GN CXCL13 TT0NIZ1 FC Does not induce calcium release in B-lymphocytes. Binds to BLR1/CXCR5. Chemotactic for B-lymphocytes but not for T-lymphocytes, monocytes and neutrophils. TT0NIZ1 PD 5CBE; 5CBA; 4ZAI TT0NIZ1 SQ MKFISTSLLLMLLVSSLSPVQGVLEVYYTSLRCRCVQESSVFIPRRFIDRIQILPRGNGCPRKEIIVWKKNKSIVCVDPQAEWIQRMMEVLRKRSSSTLPVPVFKRKIP TT0NIZ1 TT Literature-reported TTH4AN3 ID TTH4AN3 TTH4AN3 TN Cyclic AMP-responsive element-binding protein (CREB1) TTH4AN3 UP P16220 TTH4AN3 UC CREB1_HUMAN TTH4AN3 BC Basic leucine zipper bZIP TTH4AN3 SN cAMP-responsive element-binding protein 1; Cyclic AMP-responsive element-binding protein 1; Cyclic AMP responseelement-binding protein; CREB-1; CREB; CAMP-response element binding protein TTH4AN3 GN CREB1 TTH4AN3 FC Transcription activation is enhanced by the TORC coactivators which act independently of Ser-133 phosphorylation. Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells. Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters. TTH4AN3 PD 5ZKO; 5ZK1; 2LXT TTH4AN3 SQ MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD TTH4AN3 TT Literature-reported TT5Q79O ID TT5Q79O TT5Q79O TN Cyclin-dependent kinase 11B (CDK11B) TT5Q79O UP P21127 TT5Q79O UC CD11B_HUMAN TT5Q79O BC Kinase TT5Q79O SN p58 CLK1; p58 CLK-1; PK58; PITSLREA; PITSLRE serine/threonineprotein kinase CDC2L1; PITSLRE serine/threonine-protein kinase CDC2L1; Galactosyltransferaseassociated protein kinase p58/GTA; Galactosyltransferase-associated protein kinase p58/GTA; Cyclindependent kinase 11B; Cell division protein kinase 11B; Cell division cycle 2-like protein kinase 1; CLK-1; CDK11; CDC2L1 TT5Q79O GN CDK11B TT5Q79O FC Involved in pre-mRNA splicing in a kinase activity-dependent manner. Isoform 7 may act as a negative regulator of normal cell cycle progression. Plays multiple roles in cell cycle progression, cytokinesis and apoptosis. TT5Q79O EC EC 2.7.11.22 TT5Q79O SQ MGDEKDSWKVKTLDEILQEKKRRKEQEEKAEIKRLKNSDDRDSKRDSLEEGELRDHRMEITIRNSPYRREDSMEDRGEEDDSLAIKPPQQMSRKEKAHHRKDEKRKEKRRHRSHSAEGGKHARVKEKEREHERRKRHREEQDKARREWERQKRREMAREHSRRERDRLEQLERKRERERKMREQQKEQREQKERERRAEERRKEREARREVSAHHRTMREDYSDKVKASHWSRSPPRPPRERFELGDGRKPGEARPAPAQKPAQLKEEKMEERDLLSDLQDISDSERKTSSAESSSAESGSGSEEEEEEEEEEEEEGSTSEESEEEEEEEEEEEEETGSNSEEASEQSAEEVSEEEMSEDEERENENHLLVVPESRFDRDSGESEEAEEEVGEGTPQSSALTEGDYVPDSPALSPIELKQELPKYLPALQGCRSVEEFQCLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPITSLREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYVEHDLKSLMETMKQPFLPGEVKTLMIQLLRGVKHLHDNWILHRDLKTSNLLLSHAGILKVGDFGLAREYGSPLKAYTPVVVTLWYRAPELLLGAKEYSTAVDMWSVGCIFGELLTQKPLFPGKSEIDQINKVFKDLGTPSEKIWPGYSELPAVKKMTFSEHPYNNLRKRFGALLSDQGFDLMNKFLTYFPGRRISAEDGLKHEYFRETPLPIDPSMFPTWPAKSEQQRVKRGTSPRPPEGGLGYSQLGDDDLKETGFHLTTTNQGASAAGPGFSLKF TT5Q79O TT Literature-reported TT5Q79O FM Kinase TTUMFAR ID TTUMFAR TTUMFAR TN Cyclin-dependent kinase 18 (CDK18) TTUMFAR UP Q07002 TTUMFAR UC CDK18_HUMAN TTUMFAR BC Kinase TTUMFAR SN Serine/threonine-protein kinase PCTAIRE-3; PCTK3; PCTAIRE3; PCTAIRE-motif protein kinase 3; Cell division protein kinase 18 TTUMFAR GN CDK18 TTUMFAR FC May play a role in signal transduction cascades in terminally differentiated cells. TTUMFAR EC EC 2.7.11.22 TTUMFAR SQ MIMNKMKNFKRRFSLSVPRTETIEESLAEFTEQFNQLHNRRNENLQLGPLGRDPPQECSTFSPTDSGEEPGQLSPGVQFQRRQNQRRFSMEDVSKRLSLPMDIRLPQEFLQKLQMESPDLPKPLSRMSRRASLSDIGFGKLETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDLIHTDRSLTLVFEYLDSDLKQYLDHCGNLMSMHNVKIFMFQLLRGLAYCHHRKILHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCIHYEMATGRPLFPGSTVKEELHLIFRLLGTPTEETWPGVTAFSEFRTYSFPCYLPQPLINHAPRLDTDGIHLLSSLLLYESKSRMSAEAALSHSYFRSLGERVHQLEDTASIFSLKEIQLQKDPGYRGLAFQQPGRGKNRRQSIF TTUMFAR TT Literature-reported TTLQUZS ID TTLQUZS TTLQUZS TN Cystathionine gamma-lyase (CTH) TTLQUZS UP P32929 TTLQUZS UC CGL_HUMAN TTLQUZS SN Gamma-cystathionase; Cysteine-protein sulfhydrase TTLQUZS GN CTH TTLQUZS FC Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function. TTLQUZS EC EC 4.4.1.1 TTLQUZS PD 5TT2; 5TSU; 5EIG; 3ELP; 3COG TTLQUZS SQ MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEYSRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRYFRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHGDIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQNSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQHELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVLKNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS TTLQUZS TT Patented-recorded TTUX6KI ID TTUX6KI TTUX6KI TN Cytomegalovirus Glycoprotein coupled receptor (CMV US28) TTUX6KI UP P69333 TTUX6KI UC US28_HCMVT TTUX6KI BC GPCR rhodopsin TTUX6KI SN HHRF3; G-protein coupled receptor homolog US28 TTUX6KI GN CMV US28 TTUX6KI FC Receptor for a C-C type chemokine. Binds to MIP-1 alpha, RANTES, and MCP-1 and subsequently transduces a signal by increasing the intracellular calcium ions level. May regulate viral latency or reactivation; potential pathway for virally transformed cell proliferation. TTUX6KI PD 5WB2; 5WB1 TTUX6KI SQ MTPTTTTAELTTEFDYDEDATPCVFTDVLNQSKPVTLFLYGVVFLFGSIGNFLVIFTITWRRRIQCSGDVYFINLAAADLLFVCTLPLWMQYLLDHNSLASVPCTLLTACFYVAMFASLCFITEIALDRYYAIVYMRYRPVKQACLFSIFWWIFAVIIAIPHFMVVTKKDNQCMTDYDYLEVSYPIILNVELMLGAFVIPLSVISYCYYRISRIVAVSQSRHKGRIVRVLIAVVLVFIIFWLPYHLTLFVDTLKLLKWISSSCEFERSLKRALILTESLAFCHCCLNPLLYVFVGTKFRQELHCLLAEFRQRLFSRDVSWYHSMSFSRRSSPSRRETSSDTLSDEVCRVSQIIP TTUX6KI TT Literature-reported TT5DOVB ID TT5DOVB TT5DOVB TN Cytomegalovirus Protease (CMV UL80) TT5DOVB UP P16753 TT5DOVB UC SCAF_HCMVA TT5DOVB BC Peptidase TT5DOVB SN UL80; Capsid protein P40; Assemblin TT5DOVB GN CMV UL80 TT5DOVB FC Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging. TT5DOVB PD 2WPO; 1WPO; 1NKM; 1NKK; 1NJU TT5DOVB SQ MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEAATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDGLRAQWQRCGSTAVDASGDPFRSDSYGLLGNSVDALYIRERLPKLRYDKQLVGVTERESYVKASVSPEAACDIKAASAERSGDSRSQAATPAAGARVPSSSPSPPVEPPSPVQPPALPASPSVLPAESPPSLSPSEPAEAASMSHPLSAAVPAATAPPGATVAGASPAVSSLAWPHDGVYLPKDAFFSLLGASRSAVPVMYPGAVAAPPSASPAPLPLPSYPASYGAPVVGYDQLAARHFADYVDPHYPGWGRRYEPAPSLHPSYPVPPPPSPAYYRRRDSPGGMDEPPSGWERYDGGHRGQSQKQHRHGGSGGHNKRRKETAAASSSSSDEDLSFPGEAEHGRARKRLKSHVNSDGGSGGHAGSNQQQQQRYDELRDAIHELKRDLFAARQSSTLLSAALPSAASSSPTTTTVCTPTGELTSGGGETPTALLSGGAKVAERAQAGVVNASCRLATASGSEAATAGPSTAGSSSCPASVVLAAAAAQAAAASQSPPKDMVDLNRRIFVAALNKLE TT5DOVB TT Patented-recorded TTEYF03 ID TTEYF03 TTEYF03 TN Cytoplasmic DRAK1 (STK17A) TTEYF03 UP Q9UEE5 TTEYF03 UC ST17A_HUMAN TTEYF03 BC Kinase TTEYF03 SN Serine/threonine-protein kinase 17A; STK17A; DAP kinase-related apoptosis-inducing protein kinase 1 TTEYF03 GN STK17A TTEYF03 FC Acts as a positive regulator of apoptosis. Also acts as a regulator of cellular reactive oxygen species. TTEYF03 EC EC 2.7.11.1 TTEYF03 SQ MIPLEKPGSGGSSPGATSGSGRAGRGLSGPCRPPPPPQARGLLTEIRAVVRTEPFQDGYSLCPGRELGRGKFAVVRKCIKKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQDNPWVINLHEVYETASEMILVLEYAAGGEIFDQCVADREEAFKEKDVQRLMRQILEGVHFLHTRDVVHLDLKPQNILLTSESPLGDIKIVDFGLSRILKNSEELREIMGTPEYVAPEILSYDPISMATDMWSIGVLTYVMLTGISPFLGNDKQETFLNISQMNLSYSEEEFDVLSESAVDFIRTLLVKKPEDRATAEECLKHPWLTQSSIQEPSFRMEKALEEANALQEGHSVPEINSDTDKSETKESIVTEELIVVTSYTLGQCRQSEKEKMEQKAISKRFKFEEPLLQEIPGEFIY TTEYF03 TT Literature-reported TTE47YC ID TTE47YC TTE47YC TN Cytovillin (EZR) TTE47YC UP P15311 TTE47YC UC EZRI_HUMAN TTE47YC SN p81; Villin-2; VIL2 TTE47YC GN EZR TTE47YC FC Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis. TTE47YC PD 4RMA; 4RM9; 4RM8; 1NI2 TTE47YC SQ MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL TTE47YC TT Literature-reported TTE47YC KE hsa04530:Tight junction; hsa04670:Leukocyte transendothelial migration; hsa04810:Regulation of actin cytoskeleton; hsa04971:Gastric acid secretion; hsa05130:Pathogenic Escherichia coli infection; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer TTOYT5L ID TTOYT5L TTOYT5L TN Dipeptidyl-peptidase 7 (DPP7) TTOYT5L UP Q9UHL4 TTOYT5L UC DPP2_HUMAN TTOYT5L SN Quiescent cell proline dipeptidase; QPP; Dipeptidyl peptidase II; Dipeptidyl peptidase 7; Dipeptidyl peptidase 2; Dipeptidyl aminopeptidase II; DPP2; DPP II TTOYT5L GN DPP7 TTOYT5L FC Plays an important role in the degradation of some oligopeptides. TTOYT5L EC EC 3.4.14.2 TTOYT5L PD 4EBB; 3N0T; 3JYH TTOYT5L SQ MGSAPWAPVLLLALGLRGLQAGARRAPDPGFQERFFQQRLDHFNFERFGNKTFPQRFLVSDRFWVRGEGPIFFYTGNEGDVWAFANNSAFVAELAAERGALLVFAEHRYYGKSLPFGAQSTQRGHTELLTVEQALADFAELLRALRRDLGAQDAPAIAFGGSYGGMLSAYLRMKYPHLVAGALAASAPVLAVAGLGDSNQFFRDVTADFEGQSPKCTQGVREAFRQIKDLFLQGAYDTVRWEFGTCQPLSDEKDLTQLFMFARNAFTVLAMMDYPYPTDFLGPLPANPVKVGCDRLLSEAQRITGLRALAGLVYNASGSEHCYDIYRLYHSCADPTGCGTGPDARAWDYQACTEINLTFASNNVTDMFPDLPFTDELRQRYCLDTWGVWPRPDWLLTSFWGGDLRAASNIIFSNGNLDPWAGGGIRRNLSASVIAVTIQGGAHHLDLRASHPEDPASVVEARKLEATIIGEWVKAARREQQPALRGGPRLSL TTOYT5L TT Patented-recorded TT2IS7P ID TT2IS7P TT2IS7P TN Divalent metal transporter 1 (SLC11A2) TT2IS7P UP P49281 TT2IS7P UC NRAM2_HUMAN TT2IS7P BC Natural resistance-associated macrophage protein TT2IS7P SN Solute carrier family 11 member 2; OK/SW-cl.20; Natural resistanceassociated macrophage protein 2; Natural resistance-associated macrophage protein 2; NRAMP2; NRAMP 2; Divalent cation transporter 1; DMT1; DMT-1; DCT1 TT2IS7P GN SLC11A2 TT2IS7P FC Can also transport manganese, cobalt, cadmium, nickel, vanadium and lead. Involved in apical iron uptake into duodenal enterocytes. Involved in iron transport from acidified endosomes into the cytoplasm of erythroid precursor cells. May play an important role in hepatic iron accumulation and tissue iron distribution. May serve to import iron into the mitochondria. Important in metal transport, in particular iron. TT2IS7P PD 5F0P; 5F0M; 5F0L TT2IS7P SQ MVLGPEQKMSDDSVSGDHGESASLGNINPAYSNPSLSQSPGDSEEYFATYFNEKISIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWILLLATLVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRVILWLMVELAIIGSDMQEVIGSAIAINLLSVGRIPLWGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVKPSQSQVLKGMFVPSCSGCRTPQIEQAVGIVGAVIMPHNMYLHSALVKSRQVNRNNKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFGKTNEQVVEVCTNTSSPHAGLFPKDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVVLTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSDFANGLGWRIAGGILVLIICSINMYFVVVYVRDLGHVALYVVAAVVSVAYLGFVFYLGWQCLIALGMSFLDCGHTCHLGLTAQPELYLLNTMDADSLVSR TT2IS7P TT Literature-reported TTC0G1L ID TTC0G1L TTC0G1L TN DNA repair protein RAD51 homolog 1 (RAD51) TTC0G1L UP Q06609 TTC0G1L UC RAD51_HUMAN TTC0G1L SN hRAD51; RECA; RAD51A; RAD51 homolog A; HsRAD51 TTC0G1L GN RAD51 TTC0G1L FC Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair. TTC0G1L PD 5NWL; 5NP7; 5JZC; 5H1C; 5H1B TTC0G1L SQ MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD TTC0G1L TT Clinical trial TTC0G1L FM DNA repair TTC0G1L KE hsa03440:Homologous recombination; hsa03460:Fanconi anemia pathway; hsa05200:Pathways in cancer; hsa05212:Pancreatic cancer TTC0G1L RC R-HSA-5685938:HDR through Single Strand Annealing (SSA); R-HSA-5685942:HDR through Homologous Recombination (HRR); R-HSA-5693616:Presynaptic phase of homologous DNA pairing and strand exchange; R-HSA-912446:Meiotic recombination TT1RM3F ID TT1RM3F TT1RM3F TN DNA replication licensing factor MCM7 (MCM7) TT1RM3F UP P33993 TT1RM3F UC MCM7_HUMAN TT1RM3F BC Acid anhydride hydrolase TT1RM3F SN P1.1-MCM3; Minichromosome maintenanceprotein 7; MCM2; CDC47 homolog; CDC47 TT1RM3F GN MCM7 TT1RM3F FC The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for S-phase checkpoint activation upon UV-induced damage. Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. TT1RM3F EC EC 3.6.4.12 TT1RM3F SQ MALKDYALEKEKVKKFLQEFYQDDELGKKQFKYGNQLVRLAHREQVALYVDLDDVAEDDPELVDSICENARRYAKLFADAVQELLPQYKEREVVNKDVLDVYIEHRLMMEQRSRDPGMVRSPQNQYPAELMRRFELYFQGPSSNKPRVIREVRADSVGKLVTVRGIVTRVSEVKPKMVVATYTCDQCGAETYQPIQSPTFMPLIMCPSQECQTNRSGGRLYLQTRGSRFIKFQEMKMQEHSDQVPVGNIPRSITVLVEGENTRIAQPGDHVSVTGIFLPILRTGFRQVVQGLLSETYLEAHRIVKMNKSEDDESGAGELTREELRQIAEEDFYEKLAASIAPEIYGHEDVKKALLLLLVGGVDQSPRGMKIRGNINICLMGDPGVAKSQLLSYIDRLAPRSQYTTGRGSSGVGLTAAVLRDSVSGELTLEGGALVLADQGVCCIDEFDKMAEADRTAIHEVMEQQTISIAKAGILTTLNARCSILAAANPAYGRYNPRRSLEQNIQLPAALLSRFDLLWLIQDRPDRDNDLRLAQHITYVHQHSRQPPSQFEPLDMKLMRRYIAMCREKQPMVPESLADYITAAYVEMRREAWASKDATYTSARTLLAILRLSTALARLRMVDVVEKEDVNEAIRLMEMSKDSLLGDKGQTARTQRPADVIFATVRELVSGGRSVRFSEAEQRCVSRGFTPAQFQAALDEYEELNVWQVNASRTRITFV TT1RM3F TT Literature-reported TT1RM3F FM Acid anhydrides hydrolase TTLFRIC ID TTLFRIC TTLFRIC TN DNA-binding protein SATB1 (SATB1) TTLFRIC UP Q01826 TTLFRIC UC SATB1_HUMAN TTLFRIC BC CUT homeobox family TTLFRIC SN Special AT-rich sequence-binding protein 1 TTLFRIC GN SATB1 TTLFRIC FC Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma. Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes (e.g. PML at the MHC-I locus) and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis. Interacts with the unique region (UR) of cytomegalovirus (CMV). Alu-like motifs and SATB1-binding sites provide a unique chromatin context which seems preferentially targeted by the HIV-1 integration machinery. Moreover, HIV-1 Tat may overcome SATB1-mediated repression of IL2 and IL2RA (interleukin) in T-cells by binding to the same domain than HDAC1. Delineates specific epigenetic modifications at target gene loci, directly up-regulating metastasis-associated genes while down-regulating tumor-suppressor genes. Reprograms chromatin organization and the transcription profiles of breast tumors to promote growth and metastasis. TTLFRIC PD 3TUO; 3NZL; 2O4A; 2O49; 2MW8 TTLFRIC SQ MDHLNEATQGKEHSEMSNNVSDPKGPPAKIARLEQNGSPLGRGRLGSTGAKMQGVPLKHSGHLMKTNLRKGTMLPVFCVVEHYENAIEYDCKEEHAEFVLVRKDMLFNQLIEMALLSLGYSHSSAAQAKGLIQVGKWNPVPLSYVTDAPDATVADMLQDVYHVVTLKIQLHSCPKLEDLPPEQWSHTTVRNALKDLLKDMNQSSLAKECPLSQSMISSIVNSTYYANVSAAKCQEFGRWYKHFKKTKDMMVEMDSLSELSQQGANHVNFGQQPVPGNTAEQPPSPAQLSHGSQPSVRTPLPNLHPGLVSTPISPQLVNQQLVMAQLLNQQYAVNRLLAQQSLNQQYLNHPPPVSRSMNKPLEQQVSTNTEVSSEIYQWVRDELKRAGISQAVFARVAFNRTQGLLSEILRKEEDPKTASQSLLVNLRAMQNFLQLPEAERDRIYQDERERSLNAASAMGPAPLISTPPSRPPQVKTATIATERNGKPENNTMNINASIYDEIQQEMKRAKVSQALFAKVAATKSQGWLCELLRWKEDPSPENRTLWENLSMIRRFLSLPQPERDAIYEQESNAVHHHGDRPPHIIHVPAEQIQQQQQQQQQQQQQQQAPPPPQPQQQPQTGPRLPPRQPTVASPAESDEENRQKTRPRTKISVEALGILQSFIQDVGLYPDEEAIQTLSAQLDLPKYTIIKFFQNQRYYLKHHGKLKDNSGLEVDVAEYKEEELLKDLEESVQDKNTNTLFSVKLEEELSVEGNTDINTDLKD TTLFRIC TT Literature-reported TTD4YFP ID TTD4YFP TTD4YFP TN DNA-directed RNA polymerase II RPB7 (hsRPB7) TTD4YFP UP P62487 TTD4YFP UC RPB7_HUMAN TTD4YFP BC Kinase TTD4YFP SN RPB7; Human RNA polymerase II seventh subunit; HsRPB7 TTD4YFP GN POLR2G TTD4YFP FC Dna-dependent rna polymerase catalyzes the transcription of dna into rna using the four ribonucleoside triphosphates as substrates. It is suggested that rpb7 contributes to the function of rna polymerase ii in the absence of rpb4. TTD4YFP PD 5IYD; 5IYC; 5IYB; 5IYA; 5IY9 TTD4YFP SQ MFYHISLEHEILLHPRYFGPNLLNTVKQKLFTEVEGTCTGKYGFVIAVTTIDNIGAGVIQPGRGFVLYPVKYKAIVFRPFKGEVVDAVVTQVNKVGLFTEIGPMSCFISRHSIPSEMEFDPNSNPPCYKTMDEDIVIQQDDEIRLKIVGTRVDKNDIFAIGSLMDDYLGLVS TTD4YFP TT Literature-reported TTHK3MO ID TTHK3MO TTHK3MO TN Doublecortin-like kinase 2 (DCLK2) TTHK3MO UP Q8N568 TTHK3MO UC DCLK2_HUMAN TTHK3MO BC Kinase TTHK3MO SN Serine/threonine-protein kinase DCLK2; Doublecortin-like and CAM kinase-like 2; Doublecortin domain-containing protein 3B; DCK2; DCDC3B; DCAMKL2; CaMK-like CREB regulatory kinase 2; CLICK2; CLICK-II; CL2 TTHK3MO GN DCLK2 TTHK3MO FC May play a role in the down-regulation of CRE-dependent gene activation probably by phosphorylation of the CREB coactivator CRTC2/TORC2 and the resulting retention of TORC2 in the cytoplasm. Protein kinase with a significantly reduced C(a2+)/CAM affinity and dependence compared to other members of the CaMK family. TTHK3MO EC EC 2.7.11.1 TTHK3MO SQ MASTRSIELEHFEERDKRPRPGSRRGAPSSSGGSSSSGPKGNGLIPSPAHSAHCSFYRTRTLQALSSEKKAKKARFYRNGDRYFKGLVFAISSDRFRSFDALLIELTRSLSDNVNLPQGVRTIYTIDGSRKVTSLDELLEGESYVCASNEPFRKVDYTKNINPNWSVNIKGGTSRALAAASSVKSEVKESKDFIKPKLVTVIRSGVKPRKAVRILLNKKTAHSFEQVLTDITEAIKLDSGVVKRLCTLDGKQVTCLQDFFGDDDVFIACGPEKFRYAQDDFVLDHSECRVLKSSYSRSSAVKYSGSKSPGPSRRSKSPASVNGTPSSQLSTPKSTKSSSSSPTSPGSFRGLKQISAHGRSSSNVNGGPELDRCISPEGVNGNRCSESSTLLEKYKIGKVIGDGNFAVVKECIDRSTGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLVEEMETATELFLVMELVKGGDLFDAITSSTKYTERDGSAMVYNLANALRYLHGLSIVHRDIKPENLLVCEYPDGTKSLKLGDFGLATVVEGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILAGKLEFPAPYWDNITDSAKELISQMLQVNVEARCTAGQILSHPWVSDDASQENNMQAEVTGKLKQHFNNALPKQNSTTTGVSVIMNTALDKEGQIFCSKHCQDSGRPGMEPISPVPPSVEEIPVPGEAVPAPTPPESPTPHPPPAAPGGERAGTWRRHRD TTHK3MO TT Literature-reported TTMYK4Z ID TTMYK4Z TTMYK4Z TN Doublecortin-like kinase 3 (DCLK3) TTMYK4Z UP Q9C098 TTMYK4Z UC DCLK3_HUMAN TTMYK4Z BC Kinase TTMYK4Z SN Serine/threonine-protein kinase DCLK3; KIAA1765; Doublecortin-like and CAM kinase-like 3; Doublecortin domain-containing protein 3C; DCDC3C; DCAMKL3 TTMYK4Z GN DCLK3 TTMYK4Z FC Protein kinase activity, peptidyl-serine phosphorylation. TTMYK4Z EC EC 2.7.11.1 TTMYK4Z SQ MGKEPLTLKSIQVAVEELYPNKARALTLAQHSRAPSPRLRSRLFSKALKGDHRCGETETPKSCSEVAGCKAAMRHQGKIPEELSLDDRARTQKKWGRGKWEPEPSSKPPREATLEERHARGEKHLGVEIEKTSGEIIRCEKCKRERELQQSLERERLSLGTSELDMGKGPMYDVEKLVRTRSCRRSPEANPASGEEGWKGDSHRSSPRNPTQELRRPSKSMDKKEDRGPEDQESHAQGAAKAKKDLVEVLPVTEEGLREVKKDTRPMSRSKHGGWLLREHQAGFEKLRRTRGEEKEAEKEKKPCMSGGRRMTLRDDQPAKLEKEPKTRPEENKPERPSGRKPRPMGIIAANVEKHYETGRVIGDGNFAVVKECRHRETRQAYAMKIIDKSRLKGKEDMVDSEILIIQSLSHPNIVKLHEVYETDMEIYLILEYVQGGDLFDAIIESVKFPEPDAALMIMDLCKALVHMHDKSIVHRDLKPENLLVQRNEDKSTTLKLADFGLAKHVVRPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDQDELFNIIQLGHFEFLPPYWDNISDAAKDLVSRLLVVDPKKRYTAHQVLQHPWIETAGKTNTVKRQKQVSPSSEGHFRSQHKRVVEQVS TTMYK4Z TT Literature-reported TTCLIHJ ID TTCLIHJ TTCLIHJ TN Dual-specificity tyrosine-phosphorylation regulated kinase 4 (DYRK4) TTCLIHJ UP Q9NR20 TTCLIHJ UC DYRK4_HUMAN TTCLIHJ BC Kinase TTCLIHJ SN Dual specificity tyrosine-phosphorylation-regulated kinase 4 TTCLIHJ GN DYRK4 TTCLIHJ FC Possible non-essential role in spermiogenesis. TTCLIHJ EC EC 2.7.12.1 TTCLIHJ SQ MPASELKASEIPFHPSIKTQDPKAEEKSPKKQKVTLTAAEALKLFKNQLSPYEQSEILGYAELWFLGLEAKKLDTAPEKFSKTSFDDEHGFYLKVLHDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQPRPQTLRKSNSFFPSETRKDKVQGCHHSSRKADEITKETTEKTKDSPTKHVQHSGDQQDCLQHGADTVQLPQLVDAPKKSEAAVGAEVSMTSPGQSKNFSLKNTNVLPPIV TTCLIHJ TT Literature-reported TTA7MXQ ID TTA7MXQ TTA7MXQ TN Dysferlin (DYSF) TTA7MXQ UP O75923 TTA7MXQ UC DYSF_HUMAN TTA7MXQ BC Synaptosomal vesicle fusion pore TTA7MXQ SN Fer1like protein 1; Dystrophyassociated fer1like protein; DYSF TTA7MXQ GN DYSF TTA7MXQ FC Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress.{ECO:0000250}. TTA7MXQ PD 4IQH; 4IHB; 4CAI; 4CAH TTA7MXQ SQ MLRVFILYAENVHTPDTDISDAYCSAVFAGVKKRTKVIKNSVNPVWNEGFEWDLKGIPLDQGSELHVVVKDHETMGRNRFLGEAKVPLREVLATPSLSASFNAPLLDTKKQPTGASLVLQVSYTPLPGAVPLFPPPTPLEPSPTLPDLDVVADTGGEEDTEDQGLTGDEAEPFLDQSGGPGAPTTPRKLPSRPPPHYPGIKRKRSAPTSRKLLSDKPQDFQIRVQVIEGRQLPGVNIKPVVKVTAAGQTKRTRIHKGNSPLFNETLFFNLFDSPGELFDEPIFITVVDSRSLRTDALLGEFRMDVGTIYREPRHAYLRKWLLLSDPDDFSAGARGYLKTSLCVLGPGDEAPLERKDPSEDKEDIESNLLRPTGVALRGAHFCLKVFRAEDLPQMDDAVMDNVKQIFGFESNKKNLVDPFVEVSFAGKMLCSKILEKTANPQWNQNITLPAMFPSMCEKMRIRIIDWDRLTHNDIVATTYLSMSKISAPGGEIEEEPAGAVKPSKASDLDDYLGFLPTFGPCYINLYGSPREFTGFPDPYTELNTGKGEGVAYRGRLLLSLETKLVEHSEQKVEDLPADDILRVEKYLRRRKYSLFAAFYSATMLQDVDDAIQFEVSIGNYGNKFDMTCLPLASTTQYSRAVFDGCHYYYLPWGNVKPVVVLSSYWEDISHRIETQNQLLGIADRLEAGLEQVHLALKAQCSTEDVDSLVAQLTDELIAGCSQPLGDIHETPSATHLDQYLYQLRTHHLSQITEAALALKLGHSELPAALEQAEDWLLRLRALAEEPQNSLPDIVIWMLQGDKRVAYQRVPAHQVLFSRRGANYCGKNCGKLQTIFLKYPMEKVPGARMPVQIRVKLWFGLSVDEKEFNQFAEGKLSVFAETYENETKLALVGNWGTTGLTYPKFSDVTGKIKLPKDSFRPSAGWTWAGDWFVCPEKTLLHDMDAGHLSFVEEVFENQTRLPGGQWIYMSDNYTDVNGEKVLPKDDIECPLGWKWEDEEWSTDLNRAVDEQGWEYSITIPPERKPKHWVPAEKMYYTHRRRRWVRLRRRDLSQMEALKRHRQAEAEGEGWEYASLFGWKFHLEYRKTDAFRRRRWRRRMEPLEKTGPAAVFALEGALGGVMDDKSEDSMSVSTLSFGVNRPTISCIFDYGNRYHLRCYMYQARDLAAMDKDSFSDPYAIVSFLHQSQKTVVVKNTLNPTWDQTLIFYEIEIFGEPATVAEQPPSIVVELYDHDTYGADEFMGRCICQPSLERMPRLAWFPLTRGSQPSGELLASFELIQREKPAIHHIPGFEVQETSRILDESEDTDLPYPPPQREANIYMVPQNIKPALQRTAIEILAWGLRNMKSYQLANISSPSLVVECGGQTVQSCVIRNLRKNPNFDICTLFMEVMLPREELYCPPITVKVIDNRQFGRRPVVGQCTIRSLESFLCDPYSAESPSPQGGPDDVSLLSPGEDVLIDIDDKEPLIPIQEEEFIDWWSKFFASIGEREKCGSYLEKDFDTLKVYDTQLENVEAFEGLSDFCNTFKLYRGKTQEETEDPSVIGEFKGLFKIYPLPEDPAIPMPPRQFHQLAAQGPQECLVRIYIVRAFGLQPKDPNGKCDPYIKISIGKKSVSDQDNYIPCTLEPVFGKMFELTCTLPLEKDLKITLYDYDLLSKDEKIGETVVDLENRLLSKFGARCGLPQTYCVSGPNQWRDQLRPSQLLHLFCQQHRVKAPVYRTDRVMFQDKEYSIEEIEAGRIPNPHLGPVEERLALHVLQQQGLVPEHVESRPLYSPLQPDIEQGKLQMWVDLFPKALGRPGPPFNITPRRARRFFLRCIIWNTRDVILDDLSLTGEKMSDIYVKGWMIGFEEHKQKTDVHYRSLGGEGNFNWRFIFPFDYLPAEQVCTIAKKDAFWRLDKTESKIPARVVFQIWDNDKFSFDDFLGSLQLDLNRMPKPAKTAKKCSLDQLDDAFHPEWFVSLFEQKTVKGWWPCVAEEGEKKILAGKLEMTLEIVAESEHEERPAGQGRDEPNMNPKLEDPRRPDTSFLWFTSPYKTMKFILWRRFRWAIILFIILFILLLFLAIFIYAFPNYAAMKLVKPFS TTA7MXQ TT Literature-reported TT4X7PG ID TT4X7PG TT4X7PG TN Dystroglycan (DAG1) TT4X7PG UP Q14118 TT4X7PG UC DAG1_HUMAN TT4X7PG BC Dystroglycan protein TT4X7PG SN Dystrophin-associated glycoprotein 1; Alpha-dystroglycan TT4X7PG GN DAG1 TT4X7PG FC The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. TT4X7PG PD 5LLK; 5GGP; 2MK7; 1EG4 TT4X7PG SQ MRMSVGLSLLLPLSGRTFLLLLSVVMAQSHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRTASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTMTIPGYVEPTAVATPPTTTTKKPRVSTPKPATPSTDSTTTTTRRPTKKPRTPRPVPRVTTKVSITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDRAPARFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDDGKPRPAFSNALEPDFKATSITVTGSGSCRHLQFIPVVPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQDTMGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP TT4X7PG TT Literature-reported TT4X7PG FM Transmembrane protein TTWIJYH ID TTWIJYH TTWIJYH TN E2F3 messenger RNA (E2F3 mRNA) TTWIJYH UP O00716 TTWIJYH UC E2F3_HUMAN TTWIJYH BC mRNA target TTWIJYH SN Transcription factor E2F3 (mRNA); KIAA0075 (mRNA); E2F-3 (mRNA) TTWIJYH GN E2F3 TTWIJYH FC The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters. Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. TTWIJYH SQ MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAAAAAPGAYIQILTTNTSTTSCSSSLQSGAVAAGPLLPSAPGAEQTAGSLLYTTPHGPSSRAGLLQQPPALGRGGSGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEVPDSIESLQIHLASTQGPIEVYLCPEETETHSPMKTNNQDHNGNIPKPASKDLASTNSGHSDCSVSMGNLSPLASPANLLQQTEDQIPSNLEGPFVNLLPPLLQEDYLLSLGEEEGISDLFDAYDLEKLPLVEDFMCS TTWIJYH TT Literature-reported TTWIJYH FM mRNA target TTWIJYH KE hsa04110:Cell cycle; hsa05161:Hepatitis B; hsa05166:HTLV-I infection; hsa05200:Pathways in cancer; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05222:Small cell lung cancer; hsa05223:Non-small cell lung cancer TTWIJYH RC R-HSA-1912408:Pre-NOTCH Transcription and Translation; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-2559585:Oncogene Induced Senescence; R-HSA-68689:CDC6 association with the ORC:origin complex; R-HSA-68911:G2 Phase; R-HSA-69231:Cyclin D associated events in G1; R-HSA-69298:Association of licensing factors with the pre-replicative complex TTITER7 ID TTITER7 TTITER7 TN E3 ubiquitin-protein ligase makorin-1 (MKRN1) TTITER7 UP Q9UHC7 TTITER7 UC MKRN1_HUMAN TTITER7 BC Carbon-nitrogen ligase TTITER7 SN RNF61; RING-type E3 ubiquitin transferase makorin-1; RING finger protein 61 TTITER7 GN MKRN1 TTITER7 FC E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing p53/TP53 under normal conditions, but stimulates apoptosis by repressing CDKN1A under stress conditions. Acts as a negative regulator of telomerase. Has negative and positive effects on RNA polymerase II-dependent transcription. TTITER7 EC EC 2.3.2.27 TTITER7 SQ MAEAATPGTTATTSGAGAAAATAAAASPTPIPTVTAPSLGAGGGGGGSDGSGGGWTKQVTCRYFMHGVCKEGDNCRYSHDLSDSPYSVVCKYFQRGYCIYGDRCRYEHSKPLKQEEATATELTTKSSLAASSSLSSIVGPLVEMNTGEAESRNSNFATVGAGSEDWVNAIEFVPGQPYCGRTAPSCTEAPLQGSVTKEESEKEQTAVETKKQLCPYAAVGECRYGENCVYLHGDSCDMCGLQVLHPMDAAQRSQHIKSCIEAHEKDMELSFAVQRSKDMVCGICMEVVYEKANPSERRFGILSNCNHTYCLKCIRKWRSAKQFESKIIKSCPECRITSNFVIPSEYWVEEKEEKQKLILKYKEAMSNKACRYFDEGRGSCPFGGNCFYKHAYPDGRREEPQRQKVGTSSRYRAQRRNHFWELIEERENSNPFDNDEEEVVTFELGEMLLMLLAAGGDDELTDSEDEWDLFHDELEDFYDLDL TTITER7 TT Literature-reported TT4S09X ID TT4S09X TT4S09X TN E3 ubiquitin-protein ligase RNF6 (RNF6) TT4S09X UP Q9Y252 TT4S09X UC RNF6_HUMAN TT4S09X BC RNF12 family TT4S09X SN SPG2; RING-type E3 ubiquitin transferase RNF6 TT4S09X GN RNF6 TT4S09X FC E3 ubiquitin-protein ligase mediating 'Lys-48'-linked polyubiquitination of LIMK1 and its subsequent targeting to the proteasome for degradation. Negatively regulates axonal outgrowth through regulation of the LIMK1 turnover. Mediates 'Lys-6' and 'Lys-27'-linked polyubiquitination of AR/androgen receptor thereby modulating its transcriptional activity. May also bind DNA and function as a transcriptional regulator. TT4S09X EC EC 2.3.2.27 TT4S09X SQ MNQSRSRSDGGSEETLPQDHNHHENERRWQQERLHREEAYYQFINELNDEDYRLMRDHNLLGTPGEITSEELQQRLDGVKEQLASQPDLRDGTNYRDSEVPRESSHEDSLLEWLNTFRRTGNATRSGQNGNQTWRAVSRTNPNNGEFRFSLEIHVNHENRGFEIHGEDYTDIPLSDSNRDHTANRQQRSTSPVARRTRSQTSVNFNGSSSNIPRTRLASRGQNPAEGSFSTLGRLRNGIGGAAGIPRANASRTNFSSHTNQSGGSELRQREGQRFGAAHVWENGARSNVTVRNTNQRLEPIRLRSTSNSRSRSPIQRQSGTVYHNSQRESRPVQQTTRRSVRRRGRTRVFLEQDRERERRGTAYTPFSNSRLVSRITVEEGEESSRSSTAVRRHPTITLDLQVRRIRPGENRDRDSIANRTRSRVGLAENTVTIESNSGGFRRTISRLERSGIRTYVSTITVPLRRISENELVEPSSVALRSILRQIMTGFGELSSLMEADSESELQRNGQHLPDMHSELSNLGTDNNRSQHREGSSQDRQAQGDSTEMHGENETTQPHTRNSDSRGGRQLRNPNNLVETGTLPILRLAHFFLLNESDDDDRIRGLTKEQIDNLSTRHYEHNSIDSELGKICSVCISDYVTGNKLRQLPCMHEFHIHCIDRWLSENCTCPICRQPVLGSNIANNG TT4S09X TT Literature-reported TTG2CRH ID TTG2CRH TTG2CRH TN E3 ubiquitin-protein ligase TRIP12 (TRIP12) TTG2CRH UP Q14669 TTG2CRH UC TRIPC_HUMAN TTG2CRH BC Carbon-nitrogen ligase TTG2CRH SN ULF; Thyroid receptorinteracting protein 12; TRinteracting protein 12; TRIP12; E3 ubiquitinprotein ligase for Arf; E3 ubiquitinprotein ligase TRIP12 TTG2CRH GN TRIP12 TTG2CRH FC E3 ubiquitin-protein ligase involved inubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus,regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. TTG2CRH EC EC 2.3.2.26 TTG2CRH SQ MSNRPNNNPGGSLRRSQRNTAGAQPQDDSIGGRSCSSSSAVIVPQPEDPDRANTSERQKTGQVPKKDNSRGVKRSASPDYNRTNSPSSAKKPKALQHTESPSETNKPHSKSKKRHLDQEQQLKSAQSPSTSKAHTRKSGATGGSRSQKRKRTESSCVKSGSGSESTGAEERSAKPTKLASKSATSAKAGCSTITDSSSAASTSSSSSAVASASSTVPPGARVKQGKDQNKARRSRSASSPSPRRSSREKEQSKTGGSSKFDWAARFSPKVSLPKTKLSLPGSSKSETSKPGPSGLQAKLASLRKSTKKRSESPPAELPSLRRSTRQKTTGSCASTSRRGSGLGKRGAAEARRQEKMADPESNQEAVNSSAARTDEAPQGAAGAVGMTTSGESESDDSEMGRLQALLEARGLPPHLFGPLGPRMSQLFHRTIGSGASSKAQQLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQMEHNFDIMNHACRALTYMMEALPRSSAVVVDAIPVFLEKLQVIQCIDVAEQALTALEMLSRRHSKAILQAGGLADCLLYLEFFSINAQRNALAIAANCCQSITPDEFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASKDLLTNVQQLLVVTPPILSSGMFIMVVRMFSLMCSNCPTLAVQLMKQNIAETLHFLLCGASNGSCQEQIDLVPRSPQELYELTSLICELMPCLPKEGIFAVDTMLKKGNAQNTDGAIWQWRDDRGLWHPYNRIDSRIIEQINEDTGTARAIQRKPNPLANSNTSGYSESKKDDARAQLMKEDPELAKSFIKTLFGVLYEVYSSSAGPAVRHKCLRAILRIIYFADAELLKDVLKNHAVSSHIASMLSSQDLKIVVGALQMAEILMQKLPDIFSVYFRREGVMHQVKHLAESESLLTSPPKACTNGSGSMGSTTSVSSGTATAATHAAADLGSPSLQHSRDDSLDLSPQGRLSDVLKRKRLPKRGPRRPKYSPPRDDDKVDNQAKSPTTTQSPKSSFLASLNPKTWGRLSTQSNSNNIEPARTAGGSGLARAASKDTISNNREKIKGWIKEQAHKFVERYFSSENMDGSNPALNVLQRLCAATEQLNLQVDGGAECLVEIRSIVSESDVSSFEIQHSGFVKQLLLYLTSKSEKDAVSREIRLKRFLHVFFSSPLPGEEPIGRVEPVGNAPLLALVHKMNNCLSQMEQFPVKVHDFPSGNGTGGSFSLNRGSQALKFFNTHQLKCQLQRHPDCANVKQWKGGPVKIDPLALVQAIERYLVVRGYGRVREDDEDSDDDGSDEEIDESLAAQFLNSGNVRHRLQFYIGEHLLPYNMTVYQAVRQFSIQAEDERESTDDESNPLGRAGIWTKTHTIWYKPVREDEESNKDCVGGKRGRAQTAPTKTSPRNAKKHDELWHDGVCPSVSNPLEVYLIPTPPENITFEDPSLDVILLLRVLHAISRYWYYLYDNAMCKEIIPTSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGKTCPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPEINQSDSQDSRVAPRLDRKKRTVNREELLKQAESVMQDLGSSRAMLEIQYENEVGTGLGPTLEFYALVSQELQRADLGLWRGEEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQETSLTSHDLFDIDPVVARSVYHLEDIVRQKKRLEQDKSQTKESLQYALETLTMNGCSVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSKADTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQQSFHLS TTG2CRH TT Literature-reported TTMXE2Q ID TTMXE2Q TTMXE2Q TN Early response protein NAK1 (NR4A1) TTMXE2Q UP P22736 TTMXE2Q UC NR4A1_HUMAN TTMXE2Q BC Nuclear hormone receptor TTMXE2Q SN Testicular receptor 3; ST-59; Orphan nuclear receptor TR3; Orphan nuclear receptor HMR; Nur77; Nuclear receptor subfamily 4 group A member 1; Nuclear hormone receptor NUR/77; NAK1; GFRP1 TTMXE2Q GN NR4A1 TTMXE2Q FC May act concomitantly with NURR1 in regulating the expression of delayed-early genes during liver regeneration. Binds the NGFI-B response element (NBRE) 5'-AAAAGGTCA-3'. May inhibit NF-kappa-B transactivation of IL2. Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation. Plays a role in the vascular response to injury. Orphan nuclear receptor. TTMXE2Q PD 4WHG; 4WHF; 4RZG; 4RZF; 4RZE TTMXE2Q SQ MPCIQAQYGTPAPSPGPRDHLASDPLTPEFIKPTMDLASPEAAPAAPTALPSFSTFMDGYTGEFDTFLYQLPGTVQPCSSASSSASSTSSSSATSPASASFKFEDFQVYGCYPGPLSGPVDEALSSSGSDYYGSPCSAPSPSTPSFQPPQLSPWDGSFGHFSPSQTYEGLRAWTEQLPKASGPPQPPAFFSFSPPTGPSPSLAQSPLKLFPSQATHQLGEGESYSMPTAFPGLAPTSPHLEGSGILDTPVTSTKARSGAPGGSEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKNAKYICLANKDCPVDKRRRNRCQFCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKQPPDASPANLLTSLVRAHLDSGPSTAKLDYSKFQELVLPHFGKEDAGDVQQFYDLLSGSLEVIRKWAEKIPGFAELSPADQDLLLESAFLELFILRLAYRSKPGEGKLIFCSGLVLHRLQCARGFGDWIDSILAFSRSLHSLLVDVPAFACLSALVLITDRHGLQEPRRVEELQNRIASCLKEHVAAVAGEPQPASCLSRLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPPIIDKIFMDTLPF TTMXE2Q TT Literature-reported TTMXE2Q FM Zinc-finger TT0VH8G ID TT0VH8G TT0VH8G TN Elegans Endoprotease bli-4 (Elegans bli-4) TT0VH8G UP P51559 TT0VH8G UC BLI4_CAEEL TT0VH8G BC Peptidase TT0VH8G SN kpc-4; bli-4; K04F10.4; Endoprotease bli-4; Blistered cuticle protein 4; Blisterase TT0VH8G GN Elegans bli-4 TT0VH8G FC Involved in cuticle biosynthesis probably by cleaving pro-collagen into its mature form. Acts in ASEL sensory neurons to regulate high salt chemotaxis responses probably by cleaving insulin-like protein ins-6 into its mature and active form. Essential for embryonic and larval development. isoform a, isoform e, isoform f, isoform g and isoform h are involved in cuticle biosynthesis but are dispensable for larval development. Serine endoprotease which cleaves proproteins at paired basic amino acids. TT0VH8G EC EC 3.4.21.- TT0VH8G SQ MRISIGRIAWQILAVLIAVAFTIEHDSICDESIGACGEPIHTVIRLAKRDDELARRIAADHDMHVKGDPFLDTHYFLYHSETTRTRRHKRAIVERLDSHPAVEWVEEQRPKKRVKRDYILLDNDVHHSNPFRRSVLNRDGTRRAQRQQPQSPREIPSLPFPDPLYKDQWYLHGGAVGGYDMNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPQNNGDNKHGTRCAGEVAALAGNNQCGVGVAFKAKIGGVRMLDGAVSDSVEAASLSLNQDHIDIYSASWGPEDDGKTFDGPGPLAREAFYRGIKNGRGGKGNIFVWASGNGGSRQDSCSADGYTTSVYTLSISSATYDNHRPWYLEECPSSIATTYSSADFRQPAIVTVDVPGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWKPLENNPGWSRNGVGRMVSNKFGYGLIDGGALVNMAKTWKTVPEQHICTYEYRLANPNPRPIVGRFQLNFTLDVNGCESGTPVLYLEHVQVHATVRYLKRGDLKLTLFSPSGTRSVLLPPRPQDFNANGFHKWPFLSVQQWGEDPRGTWLLMVESVTTNPAATGTFHDWTLLLYGTADPAQSGDPVYSATPATSQGVLSRVHQLTSQVEESAPISFPDLTSAGNCHDECNGGCTESSSATSCFACKHLTQTLRNKGGSGFKCVQKCDDTYYLDGDKCKMCSSHCHTCTKAEVCETCPGSLLLIDVDNMPHYDHGKCVESCPPGLVADYESNLVQAKCIWRKDLCGDGYYINAVGKCDLCDSSCETCTAPGPMSCEKCSKGYGKGSIGYCRPCCPEGSTKSWQCEDCSKPDPTLLIDSNKSSGFGLMFWIVVSLIAACGICACKKCASETKSSNVEYAPLAQYNATNGAINLGAHTDDEDDDEDEVFVNPQIV TT0VH8G TT Literature-reported TTTYNAM ID TTTYNAM TTTYNAM TN Endophilin-A2 (SH3GL1) TTTYNAM UP Q99961 TTTYNAM UC SH3G1_HUMAN TTTYNAM BC Endophilin family TTTYNAM SN SH3D2B; SH3 domain-containing GRB2-like protein 1; SH3 domain protein 2B; Extra eleven-nineteen leukemia fusion gene protein; Endophilin-2; EEN fusion partner of MLL; EEN; CNSA1 TTTYNAM GN SH3GL1 TTTYNAM FC Implicated in endocytosis. May recruit other proteins to membranes with high curvature. TTTYNAM SQ MSVAGLKKQFYKASQLVSEKVGGAEGTKLDDDFKEMEKKVDVTSKAVTEVLARTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGECMIRHGKELGGESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCEKDLKEIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILDELAEKLKRRMREASSRPKREYKPKPREPFDLGEPEQSNGGFPCTTAPKIAASSSFRSSDKPIRTPSRSMPPLDQPSCKALYDFEPENDGELGFHEGDVITLTNQIDENWYEGMLDGQSGFFPLSYVEVLVPLPQ TTTYNAM TT Literature-reported TTTYNAM KE hsa04144:Endocytosis TTOJ9QL ID TTOJ9QL TTOJ9QL TN Endoplasmic reticulum to nucleus signaling 1 (ERN1) TTOJ9QL UP O75460 TTOJ9QL UC ERN1_HUMAN TTOJ9QL BC Kinase TTOJ9QL SN Serine/threonine-protein kinase/endoribonuclease IRE1; Ire1-alpha; IRE1a; IRE1; Inositol-requiring protein 1; hIRE1p; Endoplasmic reticulum-to-nucleus signaling 1 TTOJ9QL GN ERN1 TTOJ9QL FC In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity. The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA. The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes. Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A. Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR). TTOJ9QL PD 6HX1; 6HV0; 5HGI; 4Z7H; 4Z7G TTOJ9QL SQ MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL TTOJ9QL TT Clinical trial TTJR60Z ID TTJR60Z TTJR60Z TN Endothelin-1 (EDN1) TTJR60Z UP P05305 TTJR60Z UC EDN1_HUMAN TTJR60Z BC Endothelin/sarafotoxin TTJR60Z SN Preproendothelin-1; PPET1 TTJR60Z GN EDN1 TTJR60Z FC Endothelins are endothelium-derived vasoconstrictor peptides. TTJR60Z PD 6DK5; 5GLH; 1V6R; 1T7H; 1EDP TTJR60Z SQ MDYLLMIFSLLFVACQGAPETAVLGAELSAVGENGGEKPTPSPPWRLRRSKRCSCSSLMDKECVYFCHLDIIWVNTPEHVVPYGLGSPRSKRALENLLPTKATDRENRCQCASQKDKKCWNFCQAGKELRAEDIMEKDWNNHKKGKDCSKLGKKCIYQQLVRGRKIRRSSEEHLRQTRSETMRNSVKSSFHDPKLKGKPSRERYVTHNRAHW TTJR60Z TT Literature-reported TTJR60Z FM Endothelin family TT5U914 ID TT5U914 TT5U914 TN Endothelin-converting enzyme 2 (ECE2) TT5U914 UP O60344 TT5U914 UC ECE2_HUMAN TT5U914 SN UNQ403/PRO740; KIAA0604; ECE-2 TT5U914 GN ECE2 TT5U914 FC Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides. May limit beta- amyloid peptide accumulation in brain. May also have methyltransferase activity. TT5U914 EC EC 3.4.24.71 TT5U914 SQ MNVALQELGAGSNMVEYKRATLRDEDAPETPVEGGASPDAMEVGKGASPFSPGPSPGMTPGTPRSSGLFWRVTCPHLRSISGLCSRTMVGFQKGTRQLLGSRTQLELVLAGASLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAEQKTQRFYLSCLQVERIEELGAQPLRDLIEKIGGWNITGPWDQDNFMEVLKAVAGTYRATPFFTVYISADSKSSNSNVIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGRPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPSMDWLEFLSFLLSPLELSDSEPVVVYGMDYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDRRFESAQEKLLETLYGTKKSCVPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRTAFEEALGQLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEISEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYARNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACMEEQYNQYQVNGERLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW TT5U914 TT Literature-reported TTJS7O4 ID TTJS7O4 TTJS7O4 TN Entamoeba Alcohol dehydrogenase 2 (Entamo ADH2) TTJS7O4 UP Q24803 TTJS7O4 UC ADH2_ENTHI TTJS7O4 BC CH-OH donor oxidoreductase TTJS7O4 SN Aldehydealcohol dehydrogenase 2; Aldehyde-alcohol dehydrogenase 2; Alcohol dehydrogenase; ADH; ACDH TTJS7O4 GN Entamo ADH2 TTJS7O4 FC May be a critical enzyme in the fermentative pathway. This enzyme has two NAD(+)-dependent activities: ADH and ACDH. TTJS7O4 SQ MSTQQTMTVDEHINQLVRKAQVALKEYLKPEYTQEKIDYIVKKASVAALDQHCALAAAAVEETGRGIFEDKATKNIFACEHVTHEMRHAKTVGIINVDPLYGITEIAEPVGVVCGVTPVTNPTSTAIFKSLISIKTRNPIVFSFHPSALKCSIMAAKIVRDAAIAAGAPENCIQWIEFGGIEASNKLMNHPGVATILATGGNAMVKAAYSSGKPALGVGAGNVPTYIEKTCNIKQAANDVVMSKSFDNGMICASEQAAIIDKEIYDQVVEEMKTLGAYFINEEEKAKLEKFMFGVNAYSADVNNARLNPKCPGMSPQWFAEQVGIKVPEDCNIICAVCKEVGPNEPLTREKLSPVLAILKAENTQDGIDKAEAMVEFNGRGHSAAIHSNDKAVVEKYALTMKACRILHNTPSSQGGIGSIYNYIWPSFTLGCGSYGGNSVSANVTYHNLLNIKRLADRRNNLQWFRVPPKIFFEPHSIRYLAELKELSKIFIVSDRMMYKLGYVDRVMDVLKRRSNEVEIEIFIDVEPDPSIQTVQKGLAVMNTFGPDNIIAIGGGSAMDAAKIMWLLYEHPEADFFAMKQKFIDLRKRAFKFPTMGKKARLICIPTTSGTGSEVTPFAVISDHETGKKYPLADYSLTPSVAIVDPMFTMSLPKRAIADTGLDVLVHATEAYVSVMANEYTDGLAREAVKLVFENLLKSYNGDLEAREKMHNAATIAGMAFASAFLGMDHSMAHKVGAAFHLPHGRCVAVLLPHVIRYNGQKPRKLAMWPKYNFYKADQRYMELAQMVGLKCNTPAEGVEAFAKACEELMKATETITGFKKANIDEAAWMSKVPEMALLAFEDQCSPANPRVPMVKDMEKILKAAYYPIA TTJS7O4 TT Literature-reported TTJS7O4 FM Short-chain dehydrogenases reductases TTJS7O4 KE hsa00010:Glycolysis / Gluconeogenesis; hsa00040:Pentose and glucuronate interconversions; hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01220:Degradation of aromatic compounds TTCIO0M ID TTCIO0M TTCIO0M TN Eosinophil peroxidase (EPX) TTCIO0M UP P11678 TTCIO0M UC PERE_HUMAN TTCIO0M BC Peroxidases TTCIO0M SN EPX TTCIO0M GN EPX TTCIO0M FC Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis. TTCIO0M EC EC 1.11.1.7 TTCIO0M SQ MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQRLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTEPQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLSLPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPESPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRNQINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARKIMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPFMFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDELRDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLARKFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTKRQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT TTCIO0M TT Literature-reported TTFAHWI ID TTFAHWI TTFAHWI TN Ephrin type-A receptor 6 (EPHA6) TTFAHWI UP Q9UF33 TTFAHWI UC EPHA6_HUMAN TTFAHWI BC Kinase TTFAHWI SN HEK12; EPH-like kinase 12; EPH homology kinase 2; EK12; EHK2; EHK-2 TTFAHWI GN EPHA6 TTFAHWI FC The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. TTFAHWI EC EC 2.7.10.1 TTFAHWI SQ MGGCEVREFLLQFGFFLPLLTAWPGDCSHVSNNQVVLLDTTTVLGELGWKTYPLNGWDAITEMDEHNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVEMKFTLRDCNSIPWVLGTCKETFNLFYMESDESHGIKFKPNQYTKIDTIAADESFTQMDLGDRILKLNTEIREVGPIERKGFYLAFQDIGACIALVSVRVFYKKCPFTVRNLAMFPDTIPRVDSSSLVEVRGSCVKSAEERDTPKLYCGADGDWLVPLGRCICSTGYEEIEGSCHACRPGFYKAFAGNTKCSKCPPHSLTYMEATSVCQCEKGYFRAEKDPPSMACTRPPSAPRNVVFNINETALILEWSPPSDTGGRKDLTYSVICKKCGLDTSQCEDCGGGLRFIPRHTGLINNSVIVLDFVSHVNYTFEIEAMNGVSELSFSPKPFTAITVTTDQDAPSLIGVVRKDWASQNSIALSWQAPAFSNGAILDYEIKYYEKEHEQLTYSSTRSKAPSVIITGLKPATKYVFHIRVRTATGYSGYSQKFEFETGDETSDMAAEQGQILVIATAAVGGFTLLVILTLFFLITGRCQWYIKAKMKSEEKRRNHLQNGHLRFPGIKTYIDPDTYEDPSLAVHEFAKEIDPSRIRIERVIGAGEFGEVCSGRLKTPGKREIPVAIKTLKGGHMDRQRRDFLREASIMGQFDHPNIIRLEGVVTKRSFPAIGVEAFCPSFLRAGFLNSIQAPHPVPGGGSLPPRIPAGRPVMIVVEYMENGSLDSFLRKHDGHFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTTTGGKIPIRWTAPEAIAYRKFSSASDAWSYGIVMWEVMSYGERPYWEMSNQDVILSIEEGYRLPAPMGCPASLHQLMLHCWQKERNHRPKFTDIVSFLDKLIRNPSALHTLVEDILVMPESPGEVPEYPLFVTVGDWLDSIKMGQYKNNFVAAGFTTFDLISRMSIDDIRRIGVILIGHQRRIVSSIQTLRLHMMHIQEKGFHV TTFAHWI TT Literature-reported TTKF0XS ID TTKF0XS TTKF0XS TN Estrogen-related receptor-beta (ESRRB) TTKF0XS UP O95718 TTKF0XS UC ERR2_HUMAN TTKF0XS BC Nuclear hormone receptor TTKF0XS SN Steroid hormone receptor ERR2; Nuclear receptor subfamily 3 group B member 2; NR3B2; Estrogen-related receptor beta; Estrogen receptor-like 2; ESRL2; ERRB2; ERR-beta; ERR beta-2 TTKF0XS GN ESRRB TTKF0XS FC Isoform 3: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcription activity. Plays a role, in a LIF-independent manner, in maintainance of self-renewal and pluripotency of embryonic and trophoblast stem cells through different signaling pathways including FGF signaling pathway and Wnt signaling pathways. Upon FGF signaling pathway activation, interacts with KDM1A by directly binding to enhancer site of ELF5 and EOMES and activating their transcription leading to self-renewal of trophoblast stem cells. Also regulates expression of multiple rod-specific genes and is required for survival of this cell type (By similarity). Plays a role as transcription factor activator of GATA6, NR0B1, POU5F1 and PERM1. Plays a role as transcription factor repressor of NFE2L2 transcriptional activity and ESR1 transcriptional activity. During mitosis remains bound to a subset of interphase target genes, including pluripotency regulators, through the canonical ESRRB recognition (ERRE) sequence, leading to their transcriptional activation in early G1 phase. Can coassemble on structured DNA elements with other transcription factors like SOX2, POU5F1, KDM1A and NCOA3 to trigger ESRRB-dependent gene activation. This mechanism, in the case of SOX2 corecruitment prevents the embryonic stem cells (ESCs) to epiblast stem cells (EpiSC) transition through positive regulation of NR0B1 that inhibits the EpiSC transcriptional program. Also plays a role inner ear development by controlling expression of ion channels and transporters and in early placentation (By similarity). TTKF0XS PD 1LO1 TTKF0XS SQ MSSDDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGLALGTHANGLDSPPMFAGAGLGGTPCRKSYEDCASGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSESSPYLSLQISPPAKKPLTKIVSYLLVAEPDKLYAMPPPGMPEGDIKALTTLCDLADRELVVIIGWAKHIPGFSSLSLGDQMSLLQSAWMEILILGIVYRSLPYDDKLVYAEDYIMDEEHSRLAGLLELYRAILQLVRRYKKLKVEKEEFVTLKALALANSDSMYIEDLEAVQKLQDLLHEALQDYELSQRHEEPWRTGKLLLTLPLLRQTAAKAVQHFYSVKLQGKVPMHKLFLEMLEAKV TTKF0XS TT Literature-reported TT9ZRHB ID TT9ZRHB TT9ZRHB TN Estrogen-related receptor-gamma (ESRRG) TT9ZRHB UP P62508 TT9ZRHB UC ERR3_HUMAN TT9ZRHB BC Nuclear hormone receptor TT9ZRHB SN Nuclear receptor subfamily 3 group B member 3; NR3B3; KIAA0832; Estrogen-related receptor gamma; Estrogen receptor-related protein 3; ERRG2; ERR3; ERR gamma-2 TT9ZRHB GN ESRRG TT9ZRHB FC Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements. Induces the expression of PERM1 in the skeletal muscle. Orphan receptor that acts as transcription activator in the absence of bound ligand. TT9ZRHB PD 6A6K; 5YSO; 2ZKC; 2ZBS; 2ZAS TT9ZRHB SQ MDSVELCLPESFSLHYEEELLCRMSNKDRHIDSSCSSFIKTEPSSPASLTDSVNHHSPGGSSDASGSYSSTMNGHQNGLDSPPLYPSAPILGGSGPVRKLYDDCSSTIVEDPQTKCEYMLNSMPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRIDAENSPYLNPQLVQPAKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVIIGWAKHIPGFSTLSLADQMSLLQSAWMEILILGVVYRSLSFEDELVYADDYIMDEDQSKLAGLLDLNNAILQLVKKYKSMKLEKEEFVTLKAIALANSDSMHIEDVEAVQKLQDVLHEALQDYEAGQHMEDPRRAGKMLMTLPLLRQTSTKAVQHFYNIKLEGKVPMHKLFLEMLEAKV TT9ZRHB TT Literature-reported TTOFXD7 ID TTOFXD7 TTOFXD7 TN Euchromatic histone-lysine N-methyltransferase 1 (EHMT1) TTOFXD7 UP Q9H9B1 TTOFXD7 UC EHMT1_HUMAN TTOFXD7 SN EHMT1 TTOFXD7 GN EHMT1 TTOFXD7 FC Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. TTOFXD7 EC EC 2.1.1.- TTOFXD7 PD 6MBP; 6MBO; 6BY9; 5VSF; 5VSD TTOFXD7 SQ MAAADAEAVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESSKAKEVTIAKADTTSTVTPVPGQEKGSALEGRADTTTGSAAGPPLSEDDKLQGAASHVPEGFDPTGPAGLGRPTPGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDRPSPVERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQEDGLPDTSSAAAADPL TTOFXD7 TT Literature-reported TT2F078 ID TT2F078 TT2F078 TN Excitatory amino acid transporter 2 (SLC1A2) TT2F078 UP P43004 TT2F078 UC EAA2_HUMAN TT2F078 BC Dicarboxylate/amino acid:cation symporter TT2F078 SN Solute carrier family 1 member 2; Sodium-dependent glutamate/aspartate transporter 2; Glutamate/aspartatetransporter II; Glutamate/aspartate transporter II; GLT1; EAAT2 TT2F078 GN SLC1A2 TT2F078 FC Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Essential for the rapid removal of released glutamate from the synaptic cleft, and for terminating the postsynaptic action of glutamate. Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. TT2F078 SQ MASTEGANNMPKQVEVRMHDSHLGSEEPKHRHLGLRLCDKLGKNLLLTLTVFGVILGAVCGGLLRLASPIHPDVVMLIAFPGDILMRMLKMLILPLIISSLITGLSGLDAKASGRLGTRAMVYYMSTTIIAAVLGVILVLAIHPGNPKLKKQLGPGKKNDEVSSLDAFLDLIRNLFPENLVQACFQQIQTVTKKVLVAPPPDEEANATSAVVSLLNETVTEVPEETKMVIKKGLEFKDGMNVLGLIGFFIAFGIAMGKMGDQAKLMVDFFNILNEIVMKLVIMIMWYSPLGIACLICGKIIAIKDLEVVARQLGMYMVTVIIGLIIHGGIFLPLIYFVVTRKNPFSFFAGIFQAWITALGTASSAGTLPVTFRCLEENLGIDKRVTRFVLPVGATINMDGTALYEAVAAIFIAQMNGVVLDGGQIVTVSLTATLASVGAASIPSAGLVTMLLILTAVGLPTEDISLLVAVDWLLDRMRTSVNVVGDSFGAGIVYHLSKSELDTIDSQHRVHEDIEMTKTQSIYDDMKNHRESNSNQCVYAAHNSVIVDECKVTLAANGKSADCSVEEEPWKREK TT2F078 TT Literature-reported TT2F078 FM Dicarboxylate amino acid:cation symporter TTT2VDU ID TTT2VDU TTT2VDU TN Fatty acid desaturase 2 (FADS2) TTT2VDU UP O95864 TTT2VDU UC FADS2_HUMAN TTT2VDU BC Paired donor oxygen oxidoreductase TTT2VDU SN FADS2; Delta-6 desaturase; Delta(6) fatty acid desaturase; Delta(6) desaturase; D6D TTT2VDU GN FADS2 TTT2VDU FC Component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the first andrate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma- linoleic acid (GLA) (18:3n-6) and stearidonic acid (18:4n-3) respectively and other desaturation steps. Highly unsaturated fatty acids (HUFA) play pivotal roles in many biological functions. It catalizes as well the introduction of a cis double bond in palmitate to produce the mono-unsaturated fatty acid sapienate, the most abundant fatty acid in sebum. TTT2VDU EC EC 1.14.19.3 TTT2VDU SQ MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQHPGGQRVIGHYAGEDATDAFRAFHPDLEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVLGEWQPIEYGKKKLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIVHKNWVDLAWAVSYYIRFFITYIPFYGILGALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAYRDWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGKLWLDAYLHK TTT2VDU TT Literature-reported TTWTES7 ID TTWTES7 TTWTES7 TN Fatty-acid amide hydrolase 2 (FAAH2) TTWTES7 UP Q6GMR7 TTWTES7 UC FAAH2_HUMAN TTWTES7 BC Carbon-nitrogen hydrolase TTWTES7 SN Oleamide hydrolase 2; Anandamide amidohydrolase 2; Amidase domain-containing protein; AMDD TTWTES7 GN FAAH2 TTWTES7 FC Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates. Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. TTWTES7 EC EC 3.5.1.99 TTWTES7 SQ MAPSFTARIQLFLLRALGFLIGLVGRAALVLGGPKFASKTPRPVTEPLLLLSGMQLAKLIRQRKVKCIDVVQAYINRIKDVNPMINGIVKYRFEEAMKEAHAVDQKLAEKQEDEATLENKWPFLGVPLTVKEAFQLQGMPNSSGLMNRRDAIAKTDATVVALLKGAGAIPLGITNCSELCMWYESSNKIYGRSNNPYDLQHIVGGSSGGEGCTLAAACSVIGVGSDIGGSIRMPAFFNGIFGHKPSPGVVPNKGQFPLAVGAQELFLCTGPMCRYAEDLAPMLKVMAGPGIKRLKLDTKVHLKDLKFYWMEHDGGSFLMSKVDQDLIMTQKKVVVHLETILGASVQHVKLKKMKYSFQLWIAMMSAKGHDGKEPVKFVDLLGDHGKHVSPLWELIKWCLGLSVYTIPSIGLALLEEKLRYSNEKYQKFKAVEESLRKELVDMLGDDGVFLYPSHPTVAPKHHVPLTRPFNFAYTGVFSALGLPVTQCPLGLNAKGLPLGIQVVAGPFNDHLTLAVAQYLEKTFGGWVCPGKF TTWTES7 TT Literature-reported TTR31L7 ID TTR31L7 TTR31L7 TN Fibrinogen (FGG) TTR31L7 UP P02679 TTR31L7 UC FIBG_HUMAN TTR31L7 BC Fibrinogen protein TTR31L7 SN PRO2061; Fibrinogen gamma chain TTR31L7 GN FGG TTR31L7 FC Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways. Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. TTR31L7 PD 4B60; 3HUS; 3H32; 3GHG; 3FIB TTR31L7 SQ MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL TTR31L7 TT Literature-reported TTR31L7 FM Fibrinogen TTIUF3J ID TTIUF3J TTIUF3J TN Fibroblast growth factor-8 (FGF8) TTIUF3J UP P55075 TTIUF3J UC FGF8_HUMAN TTIUF3J BC Growth factor TTIUF3J SN Heparin-binding growth factor 8; HBGF-8; Fibroblast growth factor 8; FGF-8; Androgen-induced growth factor; AIGF TTIUF3J GN FGF8 TTIUF3J FC Required for normal brain, eye, ear and limb development during embryogenesis. Required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Plays a role in neurite outgrowth in hippocampal cells. Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. TTIUF3J PD 2FDB TTIUF3J SQ MGSPRSALSCLLLHLLVLCLQAQEGPGRGPALGRELASLFRAGREPQGVSQQHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPRGHHTTEQSLRFEFLNYPPFTRSLRGSQRTWAPEPR TTIUF3J TT Literature-reported TTIUF3J FM Growth factor TTPGLDJ ID TTPGLDJ TTPGLDJ TN Flavivirus RNA-directed RNA polymerase NS5 (FlaV NS5) TTPGLDJ UP P03314 (2507-3411) TTPGLDJ UC POLG_YEFV1 TTPGLDJ SN Flavivirus Non-structural protein 5 TTPGLDJ GN FlaV NS5 TTPGLDJ FC Capsid protein C: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. TTPGLDJ EC EC 2.1.1.56 TTPGLDJ PD 6IW4; 6IW2; 6IW1; 6IW0; 6EPK TTPGLDJ SQ GSANGKTLGEVWKRELNLLDKRQFELYKRTDIVEVDRDTARRHLAEGKVDTGVAVSRGTAKLRWFHERGYVKLEGRVIDLGCGRGGWCYYAAAQKEVSGVKGFTLGRDGHEKPMNVQSLGWNIITFKDKTDIHRLEPVKCDTLLCDIGESSSSSVTEGERTVRVLDTVEKWLACGVDNFCVKVLAPYMPDVLEKLELLQRRFGGTVIRNPLSRNSTHEMYYVSGARSNVTFTVNQTSRLLMRRMRRPTGKVTLEADVILPIGTRSVETDKGPLDKEAIEERVERIKSEYMTSWFYDNDNPYRTWHYCGSYVTKTSGSAASMVNGVIKILTYPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRKIMKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAIGAYLEEQEQWKTANEAVQDPKFWELVDEERKLHQQGRCRTCVYNMMGKREKKLSEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIRDLAAMDGGGFYADDTAGWDTRITEADLDDEQEILNYMSPHHKKLAQAVMEMTYKNKVVKVLRPAPGGKAYMDVISRRDQRGSGQVVTYALNTITNLKVQLIRMAEAEMVIHHQHVQDCDESVLTRLEAWLTEHGCDRLKRMAVSGDDCVVRPIDDRFGLALSHLNAMSKVRKDISEWQPSKGWNDWENVPFCSHHFHELQLKDGRRIVVPCREQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHKRDMRLLSLAVSSAVPTSWVPQGRTTWSIHGKGEWMTTEDMLEVWNRVWITNNPHMQDKTMVKKWRDVPYLTKRQDKLCGSLIGMTNRATWASHIHLVIHRIRTLIGQEKYTDYLTVMDRYSVDADLQLGELI TTPGLDJ TT Literature-reported TTOJ1NF ID TTOJ1NF TTOJ1NF TN FMLP-related receptor I (FPR2) TTOJ1NF UP P25090 TTOJ1NF UC FPR2_HUMAN TTOJ1NF BC GPCR rhodopsin TTOJ1NF SN RFP; Lipoxin A4 receptor; LXA4 receptor; HM63; G-protein-coupled receptor FPR-Like-1; Formyl peptide receptor-like 1; FPRL1; FPR2; FMLP-R-I TTOJ1NF GN FPR2 TTOJ1NF FC Low affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophils chemotactic factors. Binding of FMLP to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. The activation of LXA4R could result in an anti-inflammatory outcome counteracting the actions of proinflammatory signals such as LTB4 (leukotrieneB4). TTOJ1NF SQ METNFSTPLNEYEEVSYESAGYTVLRILPLVVLGVTFVLGVLGNGLVIWVAGFRMTRTVTTICYLNLALADFSFTATLPFLIVSMAMGEKWPFGWFLCKLIHIVVDINLFGSVFLIGFIALDRCICVLHPVWAQNHRTVSLAMKVIVGPWILALVLTLPVFLFLTTVTIPNGDTYCTFNFASWGGTPEERLKVAITMLTARGIIRFVIGFSLPMSIVAICYGLIAAKIHKKGMIKSSRPLRVLTAVVASFFICWFPFQLVALLGTVWLKEMLFYGKYKIIDILVNPTSSLAFFNSCLNPMLYVFVGQDFRERLIHSLPTSLERALSEDSAPTNDTAANSASPPAETELQAM TTOJ1NF TT Literature-reported TTOJ1NF RC R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events TTT54CI ID TTT54CI TTT54CI TN Folate receptor beta (FOLR2) TTT54CI UP P14207 TTT54CI UC FOLR2_HUMAN TTT54CI BC Folate receptor TTT54CI SN Placental folate-binding protein; Folate receptor, fetal/placental; Folate receptor type-beta; Folate receptor 2; FR-beta; FOLR2 TTT54CI GN FOLR2 TTT54CI FC Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release. TTT54CI PD 4KN2; 4KN1; 4KN0; 4KMZ; 4KMY TTT54CI SQ MVWKWMPLLLLLVCVATMCSAQDRTDLLNVCMDAKHHKTKPGPEDKLHDQCSPWKKNACCTASTSQELHKDTSRLYNFNWDHCGKMEPACKRHFIQDTCLYECSPNLGPWIQQVNQSWRKERFLDVPLCKEDCQRWWEDCHTSHTCKSNWHRGWDWTSGVNKCPAGALCRTFESYFPTPAALCEGLWSHSYKVSNYSRGSGRCIQMWFDSAQGNPNEEVARFYAAAMHVNAGEMLHGTGGLLLSLALMLQLWLLG TTT54CI TT Literature-reported TTD3KOX ID TTD3KOX TTD3KOX TN Forkhead box protein M1 (FOXM1) TTD3KOX UP Q08050 TTD3KOX UC FOXM1_HUMAN TTD3KOX SN Winged-helix factor from INS-1 cells; Winged helix factor from INS-1 cells; WIN; Transcription factor Trident; MPP2; MPM-2 reactive phosphoprotein 2; M-phase phosphoprotein 2; Hepatocyte nuclear factor 3 forkhead homolog 11; HNF-3/fork-head homolog-11; HNF-3/fork-head homolog 11; HFH11; HFH-11; Foxm1b; Foxm1; Forkhead-related protein FKHL16; Forkhead Box (Fox) m1b; FKHL16 TTD3KOX GN FOXM1 TTD3KOX FC Plays a role in the control of cell proliferation. Plays also a role in DNA breaks repair participating in the DNA damage checkpoint response. Transcriptional factor regulating the expression of cell cycle genes essential for DNA replication and mitosis. TTD3KOX PD 3G73 TTD3KOX SQ MKTSPRRPLILKRRRLPLPVQNAPSETSEEEPKRSPAQQESNQAEASKEVAESNSCKFPAGIKIINHPTMPNTQVVAIPNNANIHSIITALTAKGKESGSSGPNKFILISCGGAPTQPPGLRPQTQTSYDAKRTEVTLETLGPKPAARDVNLPRPPGALCEQKRETCADGEAAGCTINNSLSNIQWLRKMSSDGLGSRSIKQEMEEKENCHLEQRQVKVEEPSRPSASWQNSVSERPPYSYMAMIQFAINSTERKRMTLKDIYTWIEDHFPYFKHIAKPGWKNSIRHNLSLHDMFVRETSANGKVSFWTIHPSANRYLTLDQVFKPLDPGSPQLPEHLESQQKRPNPELRRNMTIKTELPLGARRKMKPLLPRVSSYLVPIQFPVNQSLVLQPSVKVPLPLAASLMSSELARHSKRVRIAPKVLLAEEGIAPLSSAGPGKEEKLLFGEGFSPLLPVQTIKEEEIQPGEEMPHLARPIKVESPPLEEWPSPAPSFKEESSHSWEDSSQSPTPRPKKSYSGLRSPTRCVSEMLVIQHRERRERSRSRRKQHLLPPCVDEPELLFSEGPSTSRWAAELPFPADSSDPASQLSYSQEVGGPFKTPIKETLPISSTPSKSVLPRTPESWRLTPPAKVGGLDFSPVQTSQGASDPLPDPLGLMDLSTTPLQSAPPLESPQRLLSSEPLDLISVPFGNSSPSDIDVPKPGSPEPQVSGLAANRSLTEGLVLDTMNDSLSKILLDISFPGLDEDPLGPDNINWSQFIPELQ TTD3KOX TT Literature-reported TTD3KOX RC R-HSA-156711:Polo-like kinase mediated events; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition TTHAVTS ID TTHAVTS TTHAVTS TN Forkhead box protein O1A (FOXO1) TTHAVTS UP Q12778 TTHAVTS UC FOXO1_HUMAN TTHAVTS SN Forkhead in rhabdomyosarcoma; Forkhead box protein O1; FOXO1A; FKHR TTHAVTS GN FOXO1 TTHAVTS FC Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner. Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). TTHAVTS PD 5DUI; 4LG0; 3COA; 3CO7; 3CO6 TTHAVTS SQ MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGSAAANPDAAAGLPSASAAAVSADFMSNLSLLEESEDFPQAPGSVAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQPPPPGPLSQHPPVPPAAAGPLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRSRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGEGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPIQTLQDNKSSYGGMSQYNCAPGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVMMGPNSVMSTYGSQASHNKMMNPSSHTHPGHAQQTSAVNGRPLPHTVSTMPHTSGMNRLTQVKTPVQVPLPHPMQMSALGGYSSVSSCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG TTHAVTS TT Literature-reported TT0MUCI ID TT0MUCI TT0MUCI TN Forkhead box protein P1 (FOXP1) TT0MUCI UP Q9H334 TT0MUCI UC FOXP1_HUMAN TT0MUCI SN Mac-1-regulated forkhead; MFH; FOXP1-ES TT0MUCI GN FOXP1 TT0MUCI FC Transcriptional repressor (PubMed:18347093, PubMed:26647308). Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential. Plays an important role in the specification and differentiation of lung epithelium. Acts cooperatively with FOXP4 to regulate lung secretory epithelial cell fate and regeneration by restricting the goblet cell lineage program; the function may involve regulation of AGR2. Essential transcriptional regulator of B-cell development. Involved in regulation of cardiac muscle cell proliferation. Involved in the columnar organization of spinal motor neurons. Promotes the formation of the lateral motor neuron column (LMC) and the preganglionic motor column (PGC) and is required for respective appropriate motor axon projections. The segment-appropriate generation of spinal chord motor columns requires cooperation with other Hox proteins. Can regulate PITX3 promoter activity; may promote midbrain identity in embryonic stem cell-derived dopamine neurons by regulating PITX3. Negatively regulates the differentiation of T follicular helper cells T(FH)s. Involved in maintenance of hair follicle stem cell quiescence; the function probably involves regulation of FGF18. Represses transcription of various pro-apoptotic genes and cooperates with NF-kappa B-signaling in promoting B-cell expansion by inhibition of caspase-dependent apoptosis (PubMed:25267198). Binds to CSF1R promoter elements and is involved in regulation of monocyte differentiation and macrophage functions; repression of CSF1R in monocytes seems to involve NCOR2 as corepressor (PubMed:15286807, PubMed:18799727, PubMed:18347093). Involved in endothelial cell proliferation, tube formation and migration indicative for a role in angiogenesis; the role in neovascularization seems to implicate suppression of SEMA5B (PubMed:24023716). Can negatively regulate androgen receptor signaling (PubMed:18640093). TT0MUCI PD 2KIU TT0MUCI SQ MMQESGTETKSNGSAIQNGSGGSNHLLECGGLREGRSNGETPAVDIGAADLAHAQQQQQQALQVARQLLLQQQQQQQVSGLKSPKRNDKQPALQVPVSVAMMTPQVITPQQMQQILQQQVLSPQQLQVLLQQQQALMLQQQQLQEFYKKQQEQLQLQLLQQQHAGKQPKEQQQVATQQLAFQQQLLQMQQLQQQHLLSLQRQGLLTIQPGQPALPLQPLAQGMIPTELQQLWKEVTSAHTAEETTGNNHSSLDLTTTCVSSSAPSKTSLIMNPHASTNGQLSVHTPKRESLSHEEHPHSHPLYGHGVCKWPGCEAVCEDFQSFLKHLNSEHALDDRSTAQCRVQMQVVQQLELQLAKDKERLQAMMTHLHVKSTEPKAAPQPLNLVSSVTLSKSASEASPQSLPHTPTTPTAPLTPVTQGPSVITTTSMHTVGPIRRRYSDKYNVPISSADIAQNQEFYKNAEVRPPFTYASLIRQAILESPEKQLTLNEIYNWFTRMFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEVEFQKRRPQKISGNPSLIKNMQSSHAYCTPLNAALQASMAENSIPLYTTASMGNPTLGNLASAIREELNGAMEHTNSNESDSSPGRSPMQAVHPVHVKEEPLDPEEAEGPLSLVTTANHSPDFDHDRDYEDEPVNEDME TT0MUCI TT Literature-reported TT0MUCI KE hsa05206:MicroRNAs in cancer TTW20PQ ID TTW20PQ TTW20PQ TN Formin-like protein 1 (FMNL1) TTW20PQ UP O95466 TTW20PQ UC FMNL1_HUMAN TTW20PQ BC Formin homology family TTW20PQ SN Leukocyte formin; FRL1; FMNL; CLL-associated antigen KW-13; C17orf1B; C17orf1 TTW20PQ GN FMNL1 TTW20PQ FC May play a role in the control of cell motility and survival of macrophages. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. TTW20PQ PD 4YDH TTW20PQ SQ MGNAAGSAEQPAGPAAPPPKQPAPPKQPMPAAGELEERFNRALNCMNLPPDKVQLLSQYDNEKKWELICDQERFQVKNPPAAYIQKLKSYVDTGGVSRKVAADWMSNLGFKRRVQESTQVLRELETSLRTNHIGWVQEFLNEENRGLDVLLEYLAFAQCSVTYDMESTDNGASNSEKNKPLEQSVEDLSKGPPSSVPKSRHLTIKLTPAHSRKALRNSRIVSQKDDVHVCIMCLRAIMNYQSGFSLVMNHPACVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHDIILAAFDNFKEVCGEQHRFEKLMEYFRNEDSNIDFMVACMQFINIVVHSVENMNFRVFLQYEFTHLGLDLYLERLRLTESDKLQVQIQAYLDNIFDVGALLEDTETKNAVLEHMEELQEQVALLTERLRDAENESMAKIAELEKQLSQARKELETLRERFSESTAMGPSRRPPEPEKAPPAAPTRPSALELKVEELEEKGLIRILRGPGDAVSIEILPVAVATPSGGDAPTPGVPTGSPSPDLAPAAEPAPGAAPPPPPPLPGLPSPQEAPPSAPPQAPPLPGSPEPPPAPPLPGDLPPPPPPPPPPPGTDGPVPPPPPPPPPPPGGPPDALGRRDSELGPGVKAKKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEKVLQELDMSDFEEQFKTKSQGPSLDLSALKSKAAQKAPSKATLIEANRAKNLAITLRKGNLGAERICQAIEAYDLQALGLDFLELLMRFLPTEYERSLITRFEREQRPMEELSEEDRFMLCFSRIPRLPERMTTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNSSKRGAAYGFRLQSLDALLEMKSTDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLADVRSLQRGLELTQREFVRQDDCMVLKEFLRANSPTMDKLLADSKTAQEAFESVVEYFGENPKTTSPGLFFSLFSRFIKAYKKAEQEVEQWKKEAAAQEAGADTPGKGEPPAPKSPPKARRPQMDLISELKRRQQKEPLIYESDRDGAIEDIITVIKTVPFTARTGKRTSRLLCEASLGEEMPL TTW20PQ TT Literature-reported TTQYVKD ID TTQYVKD TTQYVKD TN Fru-2,6-P2ase 2/6PF-2-K (PFK/FBPase 2) TTQYVKD UP O60825 TTQYVKD UC F262_HUMAN TTQYVKD BC Kinase TTQYVKD SN PFKFB2; PFK-2/FBPase-2; 6PF-2-K/Fru-2,6-P2ASE heart-typeisozyme TTQYVKD GN PFKFB2 TTQYVKD FC Synthesis and degradation of fructose 2,6-bisphosphate. TTQYVKD PD 5HTK TTQYVKD SQ MSGASSSEQNNNSYETKTPNLRMSEKKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQCALVALEDVKAYLTEENGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNRENVMEDFLKRIECYKVTYRPLDPDNYDKDLSFIKVINVGQRFLVNRVQDYIQSKIVYYLMNIHVQPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTPVAYGCKVETIKLNVEAVNTHRDKPTNNFPKNQTPVRMRRNSFTPLSSSNTIRRPRNYSVGSRPLKPLSPLRAQDMQEGAD TTQYVKD TT Literature-reported TTP6W8J ID TTP6W8J TTP6W8J TN Fructosamine-3-kinase (FN3K) TTP6W8J UP Q9H479 TTP6W8J UC FN3K_HUMAN TTP6W8J BC Kinase TTP6W8J SN Fructosamine 3 kinase; FN3K; F3K TTP6W8J GN FN3K TTP6W8J FC May initiate a process leading to the deglycation of fructoselysine and of glycated proteins. May play a role in the phosphorylation of 1-deoxy-1-morpholinofructose (DMF), fructoselysine, fructoseglycine, fructose and glycated lysozyme. TTP6W8J EC EC 2.7.1.- TTP6W8J SQ MEQLLRAELRTATLRAFGGPGAGCISEGRAYDTDAGPVFVKVNRRTQARQMFEGEVASLEALRSTGLVRVPRPMKVIDLPGGGAAFVMEHLKMKSLSSQASKLGEQMADLHLYNQKLREKLKEEENTVGRRGEGAEPQYVDKFGFHTVTCCGFIPQVNEWQDDWPTFFARHRLQAQLDLIEKDYADREARELWSRLQVKIPDLFCGLEIVPALLHGDLWSGNVAEDDVGPIIYDPASFYGHSEFELAIALMFGGFPRSFFTAYHRKIPKAPGFDQRLLLYQLFNYLNHWNHFGREYRSPSLGTMRRLLK TTP6W8J TT Literature-reported TT6WCPZ ID TT6WCPZ TT6WCPZ TN Fungal Laccase (Fung lcc1) TT6WCPZ UP Q12570 TT6WCPZ UC LAC1_BOTFU TT6WCPZ BC Diphenol donor oxidoreductase TT6WCPZ SN lcc1; Urishiol oxidase; Fragment; Diphenol oxidase; Benzenediol:oxygen oxidoreductase TT6WCPZ GN Fung lcc1 TT6WCPZ FC Lignin degradation and detoxification of lignin-derived products. TT6WCPZ EC EC 1.10.3.2 TT6WCPZ SQ MKNSFFSSLAKFASLSLAFALPTAEVIPSALEERQSCANTATTRSCWGQYSASTNSYTTVPKTGYWLVVQNTTLSADGVSRPTLNFNGTIPGPQITADWGDDVIVHVTNKLTSNGTSIHWHGIRQLNNAQYDGVPGITQCPIAPGGTLTYKFHADNYGSSWYHSHFILQYGDGLFGPLVINGPATANYDVDLGMLFLNDWNHVPVQSLWDKAKTGAPPTLLTGLMNGTNTYNGAGKKFQTTFTPGLKYRIRVVNTAVDGHFQFSIDGHSFQVIAMDFVPIVPYNATSILVSIAQRYDIIVTANAAVGNYWIRAGWQTACSGNTNAANITGILRYTGSSSTADPTTTSTVTASTSCLDEPLASLVPFVPINPVASSIMKTTLTTGGGQWLFNGSSLLLNWTDPTLLTVLNSGNIWPTEYNVIPIESTTANKGWAVLAISGPNGPNHPIHLHGHDFWTLSQGTGAYTATTALNLVNPPRRDVMTLPTGGHLVIAFQIDNPGSWLMHCHIAWHASEGLALQFVESESSILPTIGTADVSTFQNTCAAWKAWTPTEPFPQDDSGI TT6WCPZ TT Literature-reported TTYVI76 ID TTYVI76 TTYVI76 TN Fungal Protein kinase A (Fung ypkA) TTYVI76 UP Q56921 TTYVI76 UC Q56921_YEREN TTYVI76 BC Kinase TTYVI76 SN Protein kinase A TTYVI76 GN Fung ypkA TTYVI76 FC Exists as a heterotetramer consisting of two regulatory subunits that bind and inactivate two catalytic subunits. TTYVI76 SQ MKIMGTMSPSISLAKAHERISKHWQNPVGELNIEGKRYRIIDNQVVRLNPHSGFSLFREGVGKIFSGKMFSFSIARNLTDTLHAAQKTTSQELRSDIPNALSNLFGAKPQTELPLGWKGKPLSGAPDLEGMRVAETDKFAEGESHISIIETKDKQRLVAKIERSIAEGHLFAELEAYKHIYKTAGKHPNLANVHGMAVVPYGNRKEEALLMDEVDGWRCSDTLRSLADSWKQGKINSEAYWGTIKFIAHRLLDVTNHLAKAGIVHNDIKPGNVVFDRASGEPVVIDLGLHSRSGEQPKGFTESFKAPELGVGNLGASEKSDVFLVVSSLLHGIEGFEKDPEIKPNQGLRFITSEPAHVMDENGYPIHRPGIAGVETAYTRFITDILGVSADSRPDSNEARLHEFLSDGTIDEESAKQILKDTLTGEMSPLPTDVRRITPKKLRELSDLLRTHLSSAATKQLDMGVVLSDLDTMLVALDKAEREGGVDKDQLKSFNSLILKTYSVIGAYIKGREGDTKSSSTEVSPYHRSNFMLSIVEPSLQRIQKHLDQTHSSDIGSLMRAHKHLETLLEVLVTLSQQGQPVTSETYSFLNRLAEAKVTLSQQLNTLQQQQESAKAQLSILINRSGSWADVARQSLLRFDSTRPVVKFGTEQYTAIHRQMMAAHAAITLQEVSEFTDDMRNFTADSIPLLIQLGRSSLMDEHLVEQREKLRELTTIAERLNRLEREWM TTYVI76 TT Literature-reported TT2OW84 ID TT2OW84 TT2OW84 TN Fungal Pyridoxin biosynthesis protein SNZ1 (Fung SNZ1) TT2OW84 UP Q03148 TT2OW84 UC SNZ1_YEAST TT2OW84 SN SNZ1; PDX1 homolog 1; Fung P35 TT2OW84 GN Fung SNZ1 TT2OW84 FC Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. TT2OW84 EC EC 4.3.3.6 TT2OW84 PD 3O07; 3O06; 3O05; 3FEM TT2OW84 SQ MTGEDFKIKSGLAQMLKGGVIMDVVTPEQAKIAEKSGACAVMALESIPADMRKSGKVCRMSDPKMIKDIMNSVSIPVMAKVRIGHFVEAQIIEALEVDYIDESEVLTPADWTHHIEKDKFKVPFVCGAKDLGEALRRINEGAAMIRTKGEAGTGDVSEAVKHIRRITEEIKACQQLKSEDDIAKVAEEMRVPVSLLKDVLEKGKLPVVNFAAGGVATPADAALLMQLGCDGVFVGSGIFKSSNPVRLATAVVEATTHFDNPSKLLEVSSDLGELMGGVSIESISHASNGVRLSEIGW TT2OW84 TT Literature-reported TTIEJ23 ID TTIEJ23 TTIEJ23 TN Fungal RNA triphosphatase (Fung CET1) TTIEJ23 UP O13297 TTIEJ23 UC CET1_YEAST TTIEJ23 BC Phosphoric monoester hydrolase TTIEJ23 SN TPase; Polynucleotide 5'-triphosphatase; MRNA capping enzyme beta subunit; MRNA 5'-triphosphatase; CET1 TTIEJ23 GN Fung CET1 TTIEJ23 FC First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end. TTIEJ23 PD 3KYH; 1D8I; 1D8H TTIEJ23 SQ MSYTDNPPQTKRALSLDDLVNHDENEKVKLQKLSEAANGSRPFAENLESDINQTETGQAAPIDNYKESTGHGSHSQKPKSRKSSNDDEETDTDDEMGASGEINFDSEMDFDYDKQHRNLLSNGSPPMNDGSDANAKLEKPSDDSIHQNSKSDEEQRIPKQGNEGNIASNYITQVPLQKQKQTEKKIAGNAVGSVVKKEEEANAAVDNIFEEKATLQSKKNNIKRDLEVLNEISASSKPSKYRNVPIWAQKWKPTIKALQSINVKDLKIDPSFLNIIPDDDLTKSVQDWVYATIYSIAPELRSFIELEMKFGVIIDAKGPDRVNPPVSSQCVFTELDAHLTPNIDASLFKELSKYIRGISEVTENTGKFSIIESQTRDSVYRVGLSTQRPRFLRMSTDIKTGRVGQFIEKRHVAQLLLYSPKDSYDVKISLNLELPVPDNDPPEKYKSQSPISERTKDRVSYIHNDSCTRIDITKVENHNQNSKSRQSETTHEVELEINTPALLNAFDNITNDSKEYASLIRTFLNNGTIIRRKLSSLSYEIFEGSKKVM TTIEJ23 TT Literature-reported TTX5KEQ ID TTX5KEQ TTX5KEQ TN Fused homolog (STK36) TTX5KEQ UP Q9NRP7 TTX5KEQ UC STK36_HUMAN TTX5KEQ BC Kinase TTX5KEQ SN Serine/threonine-protein kinase 36; KIAA1278 TTX5KEQ GN STK36 TTX5KEQ FC Controls the activity of the transcriptional regulators GLI1, GLI2 and GLI3 by opposing the effect of SUFU and promoting their nuclear localization. GLI2 requires an additional function of STK36 to become transcriptionally active, but the enzyme does not need to possess an active kinase catalytic site for this to occur. Required for postnatal development, possibly by regulating the homeostasis of cerebral spinal fluid or ciliary function. Essential for construction of the central pair apparatus of motile cilia. Serine/threonine protein kinase which plays an important role in the sonic hedgehog (Shh) pathway by regulating the activity of GLI transcription factors. TTX5KEQ EC EC 2.7.11.1 TTX5KEQ SQ MEKYHVLEMIGEGSFGRVYKGRRKYSAQVVALKFIPKLGRSEKELRNLQREIEIMRGLRHPNIVHMLDSFETDKEVVVVTDYAEGELFQILEDDGKLPEDQVQAIAAQLVSALYYLHSHRILHRDMKPQNILLAKGGGIKLCDFGFARAMSTNTMVLTSIKGTPLYMSPELVEERPYDHTADLWSVGCILYELAVGTPPFYATSIFQLVSLILKDPVRWPSTISPCFKNFLQGLLTKDPRQRLSWPDLLYHPFIAGHVTIITEPAGPDLGTPFTSRLPPELQVLKDEQAHRLAPKGNQSRILTQAYKRMAEEAMQKKHQNTGPALEQEDKTSKVAPGTAPLPRLGATPQESSLLAGILASELKSSWAKSGTGEVPSAPRENRTTPDCERAFPEERPEVLGQRSTDVVDLENEEPDSDNEWQHLLETTEPVPIQLKAPLTLLCNPDFCQRIQSQLHEAGGQILKGILEGASHILPAFRVLSSLLSSCSDSVALYSFCREAGLPGLLLSLLRHSQESNSLQQQSWYGTFLQDLMAVIQAYFACTFNLERSQTSDSLQVFQEAANLFLDLLGKLLAQPDDSEQTLRRDSLMCFTVLCEAMDGNSRAISKAFYSSLLTTQQVVLDGLLHGLTVPQLPVHTPQGAPQVSQPLREQSEDIPGAISSALAAICTAPVGLPDCWDAKEQVCWHLANQLTEDSSQLRPSLISGLQHPILCLHLLKVLYSCCLVSEGLCRLLGQEPLALESLFMLIQGKVKVVDWEESTEVTLYFLSLLVFRLQNLPCGMEKLGSDVATLFTHSHVVSLVSAAACLLGQLGQQGVTFDLQPMEWMAAATHALSAPAEVRLTPPGSCGFYDGLLILLLQLLTEQGKASLIRDMSSSEMWTVLWHRFSMVLRLPEEASAQEGELSLSSPPSPEPDWTLISPQGMAALLSLAMATFTQEPQLCLSCLSQHGSILMSILKHLLCPSFLNQLRQAPHGSEFLPVVVLSVCQLLCFPFALDMDADLLIGVLADLRDSEVAAHLLQVCCYHLPLMQVELPISLLTRLALMDPTSLNQFVNTVSASPRTIVSFLSVALLSDQPLLTSDLLSLLAHTARVLSPSHLSFIQELLAGSDESYRPLRSLLGHPENSVRAHTYRLLGHLLQHSMALRGALQSQSGLLSLLLLGLGDKDPVVRCSASFAVGNAAYQAGPLGPALAAAVPSMTQLLGDPQAGIRRNVASALGNLGPEGLGEELLQCEVPQRLLEMACGDPQPNVKEAALIALRSLQQEPGIHQVLVSLGASEKLSLLSLGNQSLPHSSPRPASAKHCRKLIHLLRPAHSM TTX5KEQ TT Literature-reported TTVK4ZO ID TTVK4ZO TTVK4ZO TN G protein coupled receptor 81 (HCAR1) TTVK4ZO UP Q9BXC0 TTVK4ZO UC HCAR1_HUMAN TTVK4ZO BC GPCR rhodopsin TTVK4ZO SN Hydroxycarboxylic acid receptor 1; HCAR1; Gprotein coupled receptor 81; Gprotein coupled receptor 104 TTVK4ZO GN HCAR1 TTVK4ZO FC Acts as a receptor for L-lactate and mediates its anti- lipolytic effect through a G(i)-protein-mediated pathway. TTVK4ZO SQ MYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITCYLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYNKLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEWH TTVK4ZO TT Literature-reported TTVK4ZO KE hsa04024:cAMP signaling pathway TTVK4ZO RC R-HSA-418594:G alpha (i) signalling events TTO897C ID TTO897C TTO897C TN G protein coupled receptor 87 (GPR87) TTO897C UP Q9BY21 TTO897C UC GPR87_HUMAN TTO897C BC GPCR rhodopsin TTO897C SN GPR87; G-protein coupled receptor 95; G-protein coupled receptor 87 TTO897C GN GPR87 TTO897C FC Receptor for lysophosphatidic acid (LPA). Necessary for p53/TP53-dependent survival in response to DNA damage. TTO897C SQ MGFNLTLAKLPNNELHGQESHNSGNRSDGPGKNTTLHNEFDTIVLPVLYLIIFVASILLNGLAVWIFFHIRNKTSFIFYLKNIVVADLIMTLTFPFRIVHDAGFGPWYFKFILCRYTSVLFYANMYTSIVFLGLISIDRYLKVVKPFGDSRMYSITFTKVLSVCVWVIMAVLSLPNIILTNGQPTEDNIHDCSKLKSPLGVKWHTAVTYVNSCLFVAVLVILIGCYIAISRYIHKSSRQFISQSSRKRKHNQSIRVVVAVFFTCFLPYHLCRIPFTFSHLDRLLDESAQKILYYCKEITLFLSACNVCLDPIIYFFMCRSFSRRLFKKSNIRTRSESIRSLQSVRRSEVRIYYDYTDV TTO897C TT Literature-reported TTTCXO0 ID TTTCXO0 TTTCXO0 TN G protein-coupled receptor kinase 5 (GRK5) TTTCXO0 UP P34947 TTTCXO0 UC GRK5_HUMAN TTTCXO0 SN GPRK5; G protein-coupled receptor kinase GRK5 TTTCXO0 GN GRK5 TTTCXO0 FC Serine/threonine kinase that phosphorylates preferentially the activated forms of a variety of G-protein-coupled receptors (GPCRs). Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their down-regulation. Phosphorylates a variety of GPCRs, including adrenergic receptors, muscarinic acetylcholine receptors (more specifically Gi-coupled M2/M4 subtypes), dopamine receptors and opioid receptors. In addition to GPCRs, also phosphorylates various substrates: Hsc70-interacting protein/ST13, TP53/p53, HDAC5, and arrestin-1/ARRB1. Phosphorylation of ARRB1 by GRK5 inhibits G-protein independent MAPK1/MAPK3 signaling downstream of 5HT4-receptors. Phosphorylation of HDAC5, a repressor of myocyte enhancer factor 2 (MEF2) leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. Phosphorylation of TP53/p53, a crucial tumor suppressor, inhibits TP53/p53-mediated apoptosis. Phosphorylation of ST13 regulates internalization of the chemokine receptor. Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro). TTTCXO0 EC EC 2.7.11.16 TTTCXO0 PD 4TND; 4TNB TTTCXO0 SQ MELENIVANTVLLKAREGGGGKRKGKSKKWKEILKFPHISQCEDLRRTIDRDYCSLCDKQPIGRLLFRQFCETRPGLECYIQFLDSVAEYEVTPDEKLGEKGKEIMTKYLTPKSPVFIAQVGQDLVSQTEEKLLQKPCKELFSACAQSVHEYLRGEPFHEYLDSMFFDRFLQWKWLERQPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGDLIRGRVGTVGYMAPEVLNNQRYGLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSHKFSEEAKSICKMLLTKDAKQRLGCQEEGAAEVKRHPFFRNMNFKRLEAGMLDPPFVPDPRAVYCKDVLDIEQFSTVKGVNLDHTDDDFYSKFSTGSVSIPWQNEMIETECFKELNVFGPNGTLPPDLNRNHPPEPPKKGLLQRLFKRQHQNNSKSSPSSKTSFNHHINSNHVSSNSTGSS TTTCXO0 TT Patented-recorded TT5IZRB ID TT5IZRB TT5IZRB TN Galactocerebrosidase (GALC) TT5IZRB UP P54803 TT5IZRB UC GALC_HUMAN TT5IZRB BC Glycosylase TT5IZRB SN Galactosylceramide betagalactosidase; Galactosylceramide beta-galactosidase; Galactosylceramidase; Galactocerebroside betagalactosidase; Galactocerebroside beta-galactosidase; GALCERase TT5IZRB GN GALC TT5IZRB FC Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon. Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. TT5IZRB EC EC 3.2.1.46 TT5IZRB SQ MAEWLLSASWQRRAKAMTAAAGSAGRAAVPLLLCALLAPGGAYVLDDSDGLGREFDGIGAVSGGGATSRLLVNYPEPYRSQILDYLFKPNFGASLHILKVEIGGDGQTTDGTEPSHMHYALDENYFRGYEWWLMKEAKKRNPNITLIGLPWSFPGWLGKGFDWPYVNLQLTAYYVVTWIVGAKRYHDLDIDYIGIWNERSYNANYIKILRKMLNYQGLQRVKIIASDNLWESISASMLLDAELFKVVDVIGAHYPGTHSAKDAKLTGKKLWSSEDFSTLNSDMGAGCWGRILNQNYINGYMTSTIAWNLVASYYEQLPYGRCGLMTAQEPWSGHYVVESPVWVSAHTTQFTQPGWYYLKTVGHLEKGGSYVALTDGLGNLTIIIETMSHKHSKCIRPFLPYFNVSQQFATFVLKGSFSEIPELQVWYTKLGKTSERFLFKQLDSLWLLDSDGSFTLSLHEDELFTLTTLTTGRKGSYPLPPKSQPFPSTYKDDFNVDYPFFSEAPNFADQTGVFEYFTNIEDPGEHHFTLRQVLNQRPITWAADASNTISIIGDYNWTNLTIKCDVYIETPDTGGVFIAGRVNKGGILIRSARGIFFWIFANGSYRVTGDLAGWIIYALGRVEVTAKKWYTLTLTIKGHFTSGMLNDKSLWTDIPVNFPKNGWAAIGTHSFEFAQFDNFLVEATR TT5IZRB TT Literature-reported TT5IZRB FM Glycosylases TT62BC7 ID TT62BC7 TT62BC7 TN Gamma-glutamyl transferase 7 (GGT7) TT62BC7 UP Q9UJ14 TT62BC7 UC GGT7_HUMAN TT62BC7 BC Peptidase TT62BC7 SN Glutathione hydrolase 7; Gamma-glutamyltranspeptidase 7; Gamma-glutamyltransferase-like 5; Gamma-glutamyltransferase-like 3; Gamma-glutamyltransferase 7 light chain; Gamma-glutamyltransferase 7; GGTL5; GGTL3; GGT7; GGT 7 TT62BC7 GN GGT7 TT62BC7 FC Involved in the pathway glutathione metabolism, which is part of Sulfur metabolism. Cleaves glutathione conjugates. Glutathione hydrolase activity. Hypoglycin A gamma-glutamyl transpeptidase activity. Leukotriene C4 gamma-glutamyl transferase activity. Peptidyltransferase activity. TT62BC7 EC EC 3.4.19.13 TT62BC7 SQ MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDSFLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATGVTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPHSSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLHEAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPLPGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEKPVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALASRLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMGPDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPLSFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLARGRLHPDLQSNLLQVDSEFTEEEIEFLEARGHHVEKVDVLSWVHGSRRTNNFIIAVKDPRSPDAAGATIL TT62BC7 TT Literature-reported TT6TKEN ID TT6TKEN TT6TKEN TN Gamma-hydroxybutyrate receptor (SLC52A2) TT6TKEN UP Q9HAB3 TT6TKEN UC S52A2_HUMAN TT6TKEN BC Eukaryoticriboflavin transporter TT6TKEN SN SLC52A2; Protein GPR172A; PERV-A receptor 1; GPR172A TT6TKEN GN SLC52A2 TT6TKEN FC Riboflavintransporter. Riboflavin transport is Na(+)- independent but moderately pH-sensitive. Activity is strongly inhibited by riboflavin analogs, such as lumiflavin. Weakly inhibited by flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN). In case of infection by retroviruses, acts as a cell receptor to retroviral envelopes similar to the porcine endogenous retrovirus (PERV-A). TT6TKEN SQ MAAPTPARPVLTHLLVALFGMGSWAAVNGIWVELPVVVKELPEGWSLPSYVSVLVALGNLGLLVVTLWRRLAPGKDEQVPIRVVQVLGMVGTALLASLWHHVAPVAGQLHSVAFLALAFVLALACCASNVTFLPFLSHLPPRFLRSFFLGQGLSALLPCVLALVQGVGRLECPPAPINGTPGPPLDFLERFPASTFFWALTALLVASAAAFQGLLLLLPPPPSVPTGELGSGLQVGAPGAEEEVEESSPLQEPPSQAAGTTPGPDPKAYQLLSARSACLLGLLAATNALTNGVLPAVQSFSCLPYGRLAYHLAVVLGSAANPLACFLAMGVLCRSLAGLGGLSLLGVFCGGYLMALAVLSPCPPLVGTSAGVVLVVLSWVLCLGVFSYVKVAASSLLHGGGRPALLAAGVAIQVGSLLGAVAMFPPTSIYHVFHSRKDCADPCDS TT6TKEN TT Literature-reported TTRGZX3 ID TTRGZX3 TTRGZX3 TN Gap junction beta-2 protein (Cx26) TTRGZX3 UP P29033 TTRGZX3 UC CXB2_HUMAN TTRGZX3 BC Gap junction-forming connexin TTRGZX3 SN Connexin-26 TTRGZX3 GN GJB2 TTRGZX3 FC Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore. Structural component of gap junctions. TTRGZX3 PD 5KJG; 5KJ3; 5ERA; 5ER7; 3IZ2 TTRGZX3 SQ MDWGTLQTILGGVNKHSTSIGKIWLTVLFIFRIMILVVAAKEVWGDEQADFVCNTLQPGCKNVCYDHYFPISHIRLWALQLIFVSTPALLVAMHVAYRRHEKKRKFIKGEIKSEFKDIEEIKTQKVRIEGSLWWTYTSSIFFRVIFEAAFMYVFYVMYDGFSMQRLVKCNAWPCPNTVDCFVSRPTEKTVFTVFMIAVSGICILLNVTELCYLLIRYCSGKSKKPV TTRGZX3 TT Literature-reported TTOZAFI ID TTOZAFI TTOZAFI TN Gap junction delta-2 protein (Cx36) TTOZAFI UP Q9UKL4 TTOZAFI UC CXD2_HUMAN TTOZAFI BC Gap junction-forming connexin TTOZAFI SN GJA9; Connexin-36 TTOZAFI GN GJD2 TTOZAFI FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTOZAFI PD 2N6A TTOZAFI SQ MGEWTILERLLEAAVQQHSTMIGRILLTVVVIFRILIVAIVGETVYDDEQTMFVCNTLQPGCNQACYDRAFPISHIRYWVFQIIMVCTPSLCFITYSVHQSAKQRERRYSTVFLALDRDPPESIGGPGGTGGGGSGGGKREDKKLQNAIVNGVLQNTENTSKETEPDCLEVKELTPHPSGLRTASKSKLRRQEGISRFYIIQVVFRNALEIGFLVGQYFLYGFSVPGLYECNRYPCIKEVECYVSRPTEKTVFLVFMFAVSGICVVLNLAELNHLGWRKIKLAVRGAQAKRKSIYEIRNKDLPRVSVPNFGRTQSSDSAYV TTOZAFI TT Literature-reported TT45KOB ID TT45KOB TT45KOB TN GATA-binding factor 3 (GATA3) TT45KOB UP P23771 TT45KOB UC GATA3_HUMAN TT45KOB BC Zinc-finger TT45KOB SN Trans-acting T-cell-specific transcription factor GATA-3 TT45KOB GN GATA3 TT45KOB FC Transcriptional activator which binds to the enhancer of the T-cell receptor alpha and delta genes. Binds to the consensus sequence 5'-AGATAG-3'. Required for the T-helper 2 (Th2) differentiation process following immune and inflammatory responses. TT45KOB PD 4HCA; 4HC9; 4HC7 TT45KOB SQ MEVTADQPRWVSHHHPAVLNGQHPDTHHPGLSHSYMDAAQYPLPEEVDVLFNIDGQGNHVPPYYGNSVRATVQRYPPTHHGSQVCRPPLLHGSLPWLDGGKALGSHHTASPWNLSPFSKTSIHHGSPGPLSVYPPASSSSLSGGHASPHLFTFPPTPPKDVSPDPSLSTPGSAGSARQDEKECLKYQVPLPDSMKLESSHSRGSMTALGGASSSTHHPITTYPPYVPEYSSGLFPPSSLLGGSPTGFGCKSRPKARSSTGRECVNCGATSTPLWRRDGTGHYLCNACGLYHKMNGQNRPLIKPKRRLSAARRAGTSCANCQTTTTTLWRRNANGDPVCNACGLYYKLHNINRPLTMKKEGIQTRNRKMSSKSKKCKKVHDSLEDFPKNSSFNPAALSRHMSSLSHISPFSHSSHMLTTPTPMHPPSSLSFGPHHPSSMVTAMG TT45KOB TT Literature-reported TT45KOB FM Zinc-finger TT1VDN2 ID TT1VDN2 TT1VDN2 TN GATA-binding factor 4 (GATA4) TT1VDN2 UP P43694 TT1VDN2 UC GATA4_HUMAN TT1VDN2 BC Zinc-finger TT1VDN2 SN Transcription factor GATA-4; GATA-4; GATA binding factor-4 TT1VDN2 GN GATA4 TT1VDN2 FC In cooperation with TBX5, it binds to cardiac super-enhancers and promotes cardiomyocyte gene expression, while it downregulates endocardial and endothelial gene expression. Involved in bone morphogenetic protein (BMP)-mediated induction of cardiac-specific gene expression. Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions. Acts as a transcriptional activator of ANF in cooperation with NKX2-5. Promotes cardiac myocyte enlargement. Required during testicular development. May play a role in sphingolipid signaling by regulating the expression of sphingosine-1-phosphate degrading enzyme, spingosine-1-phosphate lyase. Transcriptional activator that binds to the consensus sequence 5'-AGATAG-3' and plays a key role in cardiac development and function. TT1VDN2 PD 2M9W TT1VDN2 SQ MYQSLAMAANHGPPPGAYEAGGPGAFMHGAGAASSPVYVPTPRVPSSVLGLSYLQGGGAGSASGGASGGSSGGAASGAGPGTQQGSPGWSQAGADGAAYTPPPVSPRFSFPGTTGSLAAAAAAAAAREAAAYSSGGGAAGAGLAGREQYGRAGFAGSYSSPYPAYMADVGASWAAAAAASAGPFDSPVLHSLPGRANPAARHPNLDMFDDFSEGRECVNCGAMSTPLWRRDGTGHYLCNACGLYHKMNGINRPLIKPQRRLSASRRVGLSCANCQTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMRKEGIQTRKRKPKNLNKSKTPAAPSGSESLPPASGASSNSSNATTSSSEEMRPIKTEPGLSSHYGHSSSVSQTFSVSAMSGHGPSIHPVLSALKLSPQGYASPVSQSPQTSSKQDSWNSLVLADSHGDIITA TT1VDN2 TT Literature-reported TT1VDN2 FM Zinc-finger TTUH7OM ID TTUH7OM TTUH7OM TN Gelsolin (GSN) TTUH7OM UP P06396 TTUH7OM UC GELS_HUMAN TTUH7OM SN GSN; Brevin; Actindepolymerizing factor; AGEL TTUH7OM GN GSN TTUH7OM FC Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. {ECO:0000269|PubMed:20393563}. TTUH7OM PD 6H1F; 5UBO; 5O2Z; 5H3N; 5H3M TTUH7OM SQ MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNRYERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKLYKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALKTASDFITKMDYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGLGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA TTUH7OM TT Literature-reported TTUH7OM KE hsa04666:Fc gamma R-mediated phagocytosis; hsa04810:Regulation of actin cytoskeleton; hsa05203:Viral carcinogenesis TTUH7OM RC R-HSA-264870:Caspase-mediated cleavage of cytoskeletal proteins; R-HSA-977225:Amyloid formation TTBQMJ8 ID TTBQMJ8 TTBQMJ8 TN Glucose-6-phosphatase (G6PC) TTBQMJ8 UP P35575 TTBQMJ8 UC G6PC_HUMAN TTBQMJ8 BC Phosphoric monoester hydrolase TTBQMJ8 SN Glucose-6-phosphatase alpha; G6Pase-alpha; G6Pase; G6PT; G-6-Pase TTBQMJ8 GN G6PC TTBQMJ8 FC Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels. Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. TTBQMJ8 EC EC 3.1.3.9 TTBQMJ8 SQ MEEGMNVLHDFGIQSTHYLQVNYQDSQDWFILVSVIADLRNAFYVLFPIWFHLQEAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETFSHIHSIYNASLKKYFLITFFLFSFAIGFYLLLKGLGVDLLWTLEKAQRWCEQPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMYRESCKGKLSKWLPFRLSSIVASLVLLHVFDSLKPPSQVELVFYVLSFCKSAVVPLASVSVIPYCLAQVLGQPHKKSL TTBQMJ8 TT Clinical trial TTBQMJ8 FM Phosphoric monoester hydrolases TT7EV4P ID TT7EV4P TT7EV4P TN Glucose-6-phosphatase 2 (G6PC2) TT7EV4P UP Q9NQR9 TT7EV4P UC G6PC2_HUMAN TT7EV4P BC Phosphoric monoester hydrolase TT7EV4P SN IGRP; G6PC2 TT7EV4P GN G6PC2 TT7EV4P FC May hydrolyze glucose-6-phosphate to glucose in the endoplasmic reticulum. May be responsible for glucose production through glycogenolysis and gluconeogenesis. TT7EV4P EC EC 3.1.3.9 TT7EV4P SQ MDFLHRNGVLIIQHLQKDYRAYYTFLNFMSNVGDPRNIFFIYFPLCFQFNQTVGTKMIWVAVIGDWLNLIFKWILFGHRPYWWVQETQIYPNHSSPCLEQFPTTCETGPGSPSGHAMGASCVWYVMVTAALSHTVCGMDKFSITLHRLTWSFLWSVFWLIQISVCISRVFIATHFPHQVILGVIGGMLVAEAFEHTPGIQTASLGTYLKTNLFLFLFAVGFYLLLRVLNIDLLWSVPIAKKWCANPDWIHIDTTPFAGLVRNLGVLFGLGFAINSEMFLLSCRGGNNYTLSFRLLCALTSLTILQLYHFLQIPTHEEHLFYVLSFCKSASIPLTVVAFIPYSVHMLMKQSGKKSQ TT7EV4P TT Literature-reported TT1KPBZ ID TT1KPBZ TT1KPBZ TN Glucose-6-phosphate translocase (SLC37A4) TT1KPBZ UP O43826 TT1KPBZ UC G6PT1_HUMAN TT1KPBZ BC Major facilitator TT1KPBZ SN Transformation-related gene 19 protein; TRG19; TRG-19; Solute carrier family 37 member 4; PRO0685; Glucose-6-phosphate exchanger SLC37A4; Glucose-5-phosphate transporter; Glucose 5-phosphate transporter; G6PT1 TT1KPBZ GN SLC37A4 TT1KPBZ FC Transports cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocates inorganic phosphate into the opposite direction. Forms with glucose-6-phosphatase the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it plays a central role in homeostatic regulation of blood glucose levels. Inorganic phosphate and glucose-6-phosphate antiporter of the endoplasmic reticulum. TT1KPBZ SQ MAAQGYGYYRTVIFSAMFGGYSLYYFNRKTFSFVMPSLVEEIPLDKDDLGFITSSQSAAYAISKFVSGVLSDQMSARWLFSSGLLLVGLVNIFFAWSSTVPVFAALWFLNGLAQGLGWPPCGKVLRKWFEPSQFGTWWAILSTSMNLAGGLGPILATILAQSYSWRSTLALSGALCVVVSFLCLLLIHNEPADVGLRNLDPMPSEGKKGSLKEESTLQELLLSPYLWVLSTGYLVVFGVKTCCTDWGQFFLIQEKGQSALVGSSYMSALEVGGLVGSIAAGYLSDRAMAKAGLSNYGNPRHGLLLFMMAGMTVSMYLFRVTVTSDSPKLWILVLGAVFGFSSYGPIALFGVIANESAPPNLCGTSHAIVGLMANVGGFLAGLPFSTIAKHYSWSTAFWVAEVICAASTAAFFLLRNIRTKMGRVSKKAE TT1KPBZ TT Literature-reported TT1KPBZ FM Major facilitator superfamily TT1KPBZ KE hsa04973:Carbohydrate digestion and absorption TT1KPBZ RC R-HSA-70153:Glucose transport TT0K5RG ID TT0K5RG TT0K5RG TN Glutamate receptor ionotropic kainate 2 (GRIK2) TT0K5RG UP Q13002 TT0K5RG UC GRIK2_HUMAN TT0K5RG BC Glutamate-gated ion channel TT0K5RG SN Glutamate receptor ionotropic, kainate 2; Glutamate receptor 6; GluR6; GluR-6; GluK2; Excitatory amino acid receptor 4; EAA4 TT0K5RG GN GRIK2 TT0K5RG FC L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus. Modulates cell surface expression of NETO2. Ionotropic glutamate receptor. TT0K5RG PD 5CMM; 3QXM TT0K5RG SQ MKIIFPILSNPVFRRTVKLLLCLLWIGYSQGTTHVLRFGGIFEYVESGPMGAEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFMSLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPASGLNMTESQKGKPANITDSLSNRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDANGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEESKEASALGVQNIGGIFIVLAAGLVLSVFVAVGEFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA TT0K5RG TT Literature-reported TTNFESW ID TTNFESW TTNFESW TN Glutamate--cysteine ligase modifier (GCLM) TTNFESW UP Q9UB86 TTNFESW UC GSH0_HUMAN TTNFESW BC Aldo/keto reductase family TTNFESW SN Glutamate--cysteine ligase modifier subunit; Gamma-glutamylcysteine synthetase regulatory subunit; Gamma-ECS regulatory subunit; GCS light chain TTNFESW GN GCLM TTNFESW FC cytosol, glutamate-cysteine ligase complex, enzyme regulator activity, glutamate-cysteine ligase catalytic subunit binding, glutamate metabolic process, glutathione biosynthetic process, positive regulation of glutamate-cysteine ligase activity, regulation of blood vessel size, response to drug, response to oxidative stress. TTNFESW SQ MGTDSRAAKALLARARTLHLQTGNLLNWGRLRKKCPSTHSEELHDCIQKTLNEWSSQINPDLVREFPDVLECTVSHAVEKINPDEREEMKVSAKLFIVESNSSSSTRSAVDMACSVLGVAQLDSVIIASPPIEDGVNLSLEHLQPYWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCVMPPDLTAFAKQFDIQLLTHNDPKELLSEASFQEALQESIPDIQAHEWVPLWLLRYSVIVKSRGIIKSKGYILQAKRRGS TTNFESW TT Literature-reported TTNFESW KE hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways TTKGEP3 ID TTKGEP3 TTKGEP3 TN Glutamic acid decarboxylase 1 (GAD1) TTKGEP3 UP Q99259 TTKGEP3 UC DCE1_HUMAN TTKGEP3 SN Glutamate decarboxylase 67 kDa isoform; Glutamate decarboxylase 1; GAD67; GAD-67; GAD; 67 kDa glutamic acid decarboxylase TTKGEP3 GN GAD1 TTKGEP3 FC Catalyzes the production of GABA. TTKGEP3 EC EC 4.1.1.15 TTKGEP3 PD 3VP6; 2OKJ TTKGEP3 SQ MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEKSRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEVVDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWSSKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAPKIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL TTKGEP3 TT Literature-reported TT4P8DE ID TT4P8DE TT4P8DE TN Glutathione S-transferase A1 (GSTA1) TT4P8DE UP P08263 TT4P8DE UC GSTA1_HUMAN TT4P8DE SN GTH1; GSTA1-1; GST-epsilon; GST class-alpha member 1; GST HA subunit 1; Androst-5-ene-3,17-dione isomerase; 13-hydroperoxyoctadecadienoate peroxidase TT4P8DE GN GSTA1 TT4P8DE FC Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds (Probable). Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). It also catalyzes the isomerization of D5-androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may therefore play an important role in hormone biosynthesis. Through its glutathione-dependent peroxidase activity toward the fatty acid hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it is also involved in the metabolism of oxidized linoleic acid. TT4P8DE EC EC 2.5.1.18 TT4P8DE PD 6ATR; 6ATQ; 6ATP; 6ATO; 5LD0 TT4P8DE SQ MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF TT4P8DE TT Literature-reported TTNLFBE ID TTNLFBE TTNLFBE TN Glutathione S-transferase A2 (GSTA2) TTNLFBE UP P09210 TTNLFBE UC GSTA2_HUMAN TTNLFBE SN GTH2; GSTA2-2; GST2; GST-gamma; GST class-alpha member 2; GST HA subunit 2 TTNLFBE GN GSTA2 TTNLFBE FC Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. TTNLFBE EC EC 2.5.1.18 TTNLFBE PD 4ACS; 2WJU; 2VCT; 1AGS TTNLFBE SQ MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAKLALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF TTNLFBE TT Literature-reported TT29VDX ID TT29VDX TT29VDX TN Glutathione S-transferase A3 (GSTA3) TT29VDX UP Q16772 TT29VDX UC GSTA3_HUMAN TT29VDX SN Glutathione S-transferase A3-3; GST class-alpha member 3 TT29VDX GN GSTA3 TT29VDX FC Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,20-dione, precursors to testosterone and progesterone, respectively. TT29VDX EC EC 2.5.1.18 TT29VDX PD 2VCV; 1TDI TT29VDX SQ MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLNEMILLLPLCRPEEKDAKIALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISLVELLYYVEELDSSLISNFPLLKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARKIFRF TT29VDX TT Literature-reported TTZW8NS ID TTZW8NS TTZW8NS TN Glutathione S-transferase LANCL1 (LANCL1) TTZW8NS UP O43813 TTZW8NS UC LANC1_HUMAN TTZW8NS SN p40; LanC-like protein 1; GPR69A; 40 kDa erythrocyte membrane protein TTZW8NS GN LANCL1 TTZW8NS FC Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (By similarity). May play a role in EPS8 signaling. Binds glutathione. TTZW8NS EC EC 2.5.1.18 TTZW8NS PD 3E6U; 3.00E+73 TTZW8NS SQ MAQRAFPNPYADYNKSLAEGYFDAAGRLTPEFSQRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLYDVFGDPAYLQLAHGYVKQSLNCLTKRSITFLCGDAGPLAVAAVLYHKMNNEKQAEDCITRLIHLNKIDPHAPNEMLYGRIGYIYALLFVNKNFGVEKIPQSHIQQICETILTSGENLARKRNFTAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSQGKLHSLVKPSVDYVCQLKFPSGNYPPCIGDNRDLLVHWCHGAPGVIYMLIQAYKVFREEKYLCDAYQCADVIWQYGLLKKGYGLCHGSAGNAYAFLTLYNLTQDMKYLYRACKFAEWCLEYGEHGCRTPDTPFSLFEGMAGTIYFLADLLVPTKARFPAFEL TTZW8NS TT Literature-reported TTWO3SH ID TTWO3SH TTWO3SH TN Glutathione S-transferase omega-1 (GSTO-1) TTWO3SH UP P78417 TTWO3SH UC GSTO1_HUMAN TTWO3SH SN SPG-R; S-(Phenacyl)glutathione reductase; Monomethylarsonic acid reductase; MMA(V) reductase; Glutathione-dependent dehydroascorbate reductase; Glutathione S-transferase omega 1-1; GSTTLP28; GSTO-1; GSTO 1-1 TTWO3SH GN GSTO1 TTWO3SH FC Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. TTWO3SH EC EC 2.5.1.18 TTWO3SH PD 6MHD; 6MHC; 6MHB; 5YVO; 5YVN TTWO3SH SQ MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELFSKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYGL TTWO3SH TT Preclinical TTVEWR4 ID TTVEWR4 TTVEWR4 TN Glutathione synthetase (GSS) TTVEWR4 UP P48637 TTVEWR4 UC GSHB_HUMAN TTVEWR4 SN Glutathione synthase; GSH-S; GSH synthetase TTVEWR4 GN GSS TTVEWR4 FC Catalyzes the oxidation of GSH to glutathione disulfide (GSSG) by reducing free radicals and reactive oxygen species such as hydrogen peroxide. Uses GSH to clean up various metabolites, xenobiotics, and electrophiles to mercapturates for excretion. TTVEWR4 EC EC 6.3.2.3 TTVEWR4 PD 2HGS TTVEWR4 SQ MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSALLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVFLGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKILSNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFEDISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQLAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSRFVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVVQCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV TTVEWR4 TT Literature-reported TTI0138 ID TTI0138 TTI0138 TN Glycine transporter-2 (SLC6A5) TTI0138 UP Q9Y345 TTI0138 UC SC6A5_HUMAN TTI0138 BC Neurotransmitter:sodium symporter TTI0138 SN Solute carrier family 6 member 5; Sodium-and chloride-dependent glycine transporter 2; SLC6A5; GlyT2; GlyT-2 TTI0138 GN SLC6A5 TTI0138 FC Terminates the action of glycine by its high affinity sodium-dependent reuptake into presynaptic terminals. May be responsible for the termination of neurotransmission at strychnine-sensitive glycinergic synapses. TTI0138 SQ MDCSAPKEMNKLPANSPEAAAAQGHPDGPCAPRTSPEQELPAAAAPPPPRVPRSASTGAQTFQSADARACEAERPGVGSCKLSSPRAQAASAALRDLREAQGAQASPPPGSSGPGNALHCKIPFLRGPEGDANVSVGKGTLERNNTPVVGWVNMSQSTVVLATDGITSVLPGSVATVATQEDEQGDENKARGNWSSKLDFILSMVGYAVGLGNVWRFPYLAFQNGGGAFLIPYLMMLALAGLPIFFLEVSLGQFASQGPVSVWKAIPALQGCGIAMLIISVLIAIYYNVIICYTLFYLFASFVSVLPWGSCNNPWNTPECKDKTKLLLDSCVISDHPKIQIKNSTFCMTAYPNVTMVNFTSQANKTFVSGSEEYFKYFVLKISAGIEYPGEIRWPLALCLFLAWVIVYASLAKGIKTSGKVVYFTATFPYVVLVILLIRGVTLPGAGAGIWYFITPKWEKLTDATVWKDAATQIFFSLSAAWGGLITLSSYNKFHNNCYRDTLIVTCTNSATSIFAGFVIFSVIGFMANERKVNIENVADQGPGIAFVVYPEALTRLPLSPFWAIIFFLMLLTLGLDTMFATIETIVTSISDEFPKYLRTHKPVFTLGCCICFFIMGFPMITQGGIYMFQLVDTYAASYALVIIAIFELVGISYVYGLQRFCEDIEMMIGFQPNIFWKVCWAFVTPTILTFILCFSFYQWEPMTYGSYRYPNWSMVLGWLMLACSVIWIPIMFVIKMHLAPGRFIERLKLVCSPQPDWGPFLAQHRGERYKNMIDPLGTSSLGLKLPVKDLELGTQC TTI0138 TT Literature-reported TTI0138 RC R-HSA-442660:Na+/Cl- dependent neurotransmitter transporters TTTPCNU ID TTTPCNU TTTPCNU TN G-protein coupled receptor 39 (GPR39) TTTPCNU UP O43194 TTTPCNU UC GPR39_HUMAN TTTPCNU BC GPCR rhodopsin TTTPCNU SN Gprotein coupled receptor 39; GPR39 TTTPCNU GN GPR39 TTTPCNU FC Zn(2+) acts as a agonist. Thisreceptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated mainly through G(q)-alpha and G(12)/G(13) proteins. Involved in regulation of body weight, gastrointestinal mobility, hormone secretion and cell death. TTTPCNU SQ MASPSLPGSDCSQIIDHSHVPEFEVATWIKITLILVYLIIFVMGLLGNSATIRVTQVLQKKGYLQKEVTDHMVSLACSDILVFLIGMPMEFYSIIWNPLTTSSYTLSCKLHTFLFEACSYATLLHVLTLSFERYIAICHPFRYKAVSGPCQVKLLIGFVWVTSALVALPLLFAMGTEYPLVNVPSHRGLTCNRSSTRHHEQPETSNMSICTNLSSRWTVFQSSIFGAFVVYLVVLLSVAFMCWNMMQVLMKSQKGSLAGGTRPPQLRKSESEESRTARRQTIIFLRLIVVTLAVCWMPNQIRRIMAAAKPKHDWTRSYFRAYMILLPFSETFFYLSSVINPLLYTVSSQQFRRVFVQVLCCRLSLQHANHEKRLRVHAHSTTDSARFVQRPLLFASRRQSSARRTEKIFLSTFQSEAEPQSKSQSLSLESLEPNSGAKPANSAAENGFQEHEV TTTPCNU TT Literature-reported TTTPCNU RC R-HSA-373076:Class A/1 (Rhodopsin-like receptors) TT4MXVG ID TT4MXVG TT4MXVG TN Growth/differentiation factor 15 (GDF15) TT4MXVG UP Q99988 TT4MXVG UC GDF15_HUMAN TT4MXVG BC Growth factor TT4MXVG SN Prostate differentiation factor; Placental bone morphogenetic protein; Placental TGF-beta; NSAID-regulated gene 1 protein; NSAID-activated gene 1 protein; NRG-1; NAG-1; Macrophage inhibitory cytokine 1; MIC1; MIC-1; GDF-15 TT4MXVG GN GDF15 TT4MXVG FC Regulates food intake, energy expenditure and body weight in response to metabolic and toxin-induced stresses. Binds to its receptor, GFRAL, and activates GFRAL-expressing neurons localized in the area postrema and nucleus tractus solitarius of the brainstem. It then triggers the activation of neurons localized within the parabrachial nucleus and central amygdala, which contitutes part of the 'emergency circuit' that shapes feeding responses to stressful conditions. On hepatocytes, inhibits growth hormone signaling (By similarity). TT4MXVG PD 5VZ4; 5VZ3; 5VT2 TT4MXVG SQ MPGQELRTVNGSQMLLVLLVLSWLPHGGALSLAEASRASFPGPSELHSEDSRFRELRKRYEDLLTRLRANQSWEDSNTDLVPAPAVRILTPEVRLGSGGHLHLRISRAALPEGLPEASRLHRALFRLSPTASRSWDVTRPLRRQLSLARPQAPALHLRLSPPPSQSDQLLAESSSARPQLELHLRPQAARGRRRARARNGDHCPLGPGRCCRLHTVRASLEDLGWADWVLSPREVQVTMCIGACPSQFRAANMHAQIKTSLHRLKPDTVPAPCCVPASYNPMVLIQKTDTGVSLQTYDDLLAKDCHCI TT4MXVG TT Literature-reported TTHO7TF ID TTHO7TF TTHO7TF TN GTPase HRas (HRAS) TTHO7TF UP P01112 TTHO7TF UC RASH_HUMAN TTHO7TF BC Small GTPase TTHO7TF SN p21ras; cHras; c-H-ras; Transforming protein p21; HaRas; Ha-Ras; H-Ras-1; GTPase HRas, Nterminally processed TTHO7TF GN HRAS TTHO7TF FC Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Involved in the activation of Ras protein signal transduction. TTHO7TF PD 821P; 721P; 6Q21; 6D5W; 6D5V TTHO7TF SQ MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS TTHO7TF TT Literature-reported TTHO7TF FM Ras family TTYPTHI ID TTYPTHI TTYPTHI TN Haemophilus influenzae Immunoglobulin A1 protease (Hae-influ iga) TTYPTHI UP P42782 TTYPTHI UC IGA1_HAEIF TTYPTHI BC Peptidase TTYPTHI SN iga; IGA1 protease TTYPTHI GN Hae-influ iga TTYPTHI FC Virulence factor; cleaves host immunoglobulin A producing intact Fc and Fab fragments. TTYPTHI EC EC 3.4.21.72 TTYPTHI SQ MLNKKFKLNFIALTVAYALTPYTEAALVRDDVDYQIFRDFAENKGKFSVGATNVLVKDKNNKDLGTALPNGIPMIDFSVVDVDKRIATLINPQYVVGVKHVSNGVSELHFGNLNGNMNNGNAKAHRDVSSEENRYFSVEKNEYPTKLNGKTVTTEDQTQKRREDYYMPRLDKFVTEVAPIEASTASSDAGTYNDQNKYPAFVRLGSGSQFIYKKGDNYSLILNNHEVGGNNLKLVGDAYTYGIAGTPYKVNHENNGLIGFGNSKEEHSDPKGILSQDPLTNYAVLGDSGSPLFVYDREKGKWLFLGSYDFWAGYNKKSWQEWNIYKSQFTKDVLNKDSAGSLIGSKTDYSWSSNGKTSTITGGEKSLNVDLADGKDKPNHGKSVTFEGSGTLTLNNNIDQGAGGLFFEGDYEVKGTSDNTTWKGAGVSVAEGKTVTWKVHNPQYDRLAKIGKGTLIVEGTGDNKGSLKVGDGTVILKQQTNGSGQHAFASVGIVSGRSTLVLNDDKQVDPNSIYFGFRGGRLDLNGNSLTFDHIRNIDDGARLVNHNMTNASNITITGESLITDPNTITPYNIDAPDEDNPYAFRRIKDGGQLYLNLENYTYYALRKGASTRSELPKNSGESNENWLYMGKTSDEAKRNVMNHINNERMNGFNGYFGEEEGKNNGNLNVTFKGKSEQNRFLLTGGTNLNGDLTVEKGTLFLSGRPTPHARDIAGISSTKKDPHFAENNEVVVEDDWINRNFKATTMNVTGNASLYSGRNVANITSNITASNKAQVHIGYKTGDTVCVRSDYTGYVTCTTDKLSDKALNSFNPTNLRGNVNLTESANFVLGKANLFGTIQSRGNSQVRLTENSHWHLTGNSDVHQLDLANGHIHLNSADNSNNVTKYNTLTVNSLSGNGSFYYLTDLSNKQGDKVVVTKSATGNFTLQVADKTGEPNHNELTLFDASKAQRDHLNVSLVGNTVDLGAWKYKLRNVNGRYDLYNPEVEKRNQTVDTTNITTPNNIQADVPSVPSNNEEIARVDEAPVPPPAPATPSETTETVAENSKQESKTVEKNEQDATETTAQNREVAKEAKSNVKANTQTNEVAQSGSETKETQTTETKETATVEKEEKAKVETEKTQEVPKVTSQVSPKQEQSETVQPQAEPARENDPTVNIKEPQSQTNTTADTEQPAKETSSNVEQPVTESTTVNTGNSVVENPENTTPATTQPTVNSESSNKPKNRHRRSVRSVPHNVEPATTSSNDRSTVALCDLTSTNTNAVLSDARAKAQFVALNVGKAVSQHISQLEMNNEGQYNVWVSNTSMNKNYSSSQYRRFSSKSTQTQLGWDQTISNNVQLGGVFTYVRNSNNFDKATSKNTLAQVNFYSKYYADNHWYLGIDLGYGKFQSKLQTNHNAKFARHTAQFGLTAGKAFNLGNFGITPIVGVRYSYLSNADFALDQARIKVNPISVKTAFAQVDLSYTYHLGEFSVTPILSARYDANQGSGKINVNGYDFAYNVENQQQYNAGLKLKYHNVKLSLIGGLTKAKQAEKQKTAELKLSFSF TTYPTHI TT Literature-reported TTFLMXC ID TTFLMXC TTFLMXC TN Haemophilus influenzae Iron-transporter ferric ion-binding (Hae-influ fbpA) TTFLMXC UP P35755 TTFLMXC UC FBPA_HAEIN TTFLMXC BC ABC transporter TTFLMXC SN Major ferric iron binding protein; MIRP; Iron-regulated 40 kDa protein; Fe(3+)-binding protein; Fe(+3)Iron-utilization periplasmic protein precursor-binding protein TTFLMXC GN Hae-influ fbpA TTFLMXC FC Part of the ABC transporter complex FbpABC (TC 3.A.1.10.1) involved in Fe(3+) ions import. This protein specifically binds Fe(3+) and is involved in its transmembrane transport. TTFLMXC PD 3ODB; 3OD7; 3KN8; 3KN7; 2O6A TTFLMXC SQ MQFKHFKLATLAAALAFSANSFADITVYNGQHKEAATAVAKAFEQETGIKVTLNSGKSEQLAGQLKEEGDKTPADVFYTEQTATFADLSEAGLLAPISEQTIQQTAQKGVPLAPKKDWIALSGRSRVVVYDHTKLSEKDMEKSVLDYATPKWKGKIGYVSTSGAFLEQVVALSKMKGDKVALNWLKGLKENGKLYAKNSVALQAVENGEVPAALINNYYWYNLAKEKGVENLKSRLYFVRHQDPGALVSYSGAAVLKASKNQAEAQKFVDFLASKKGQEALVAARAEYPLRADVVSPFNLEPYEKLEAPVVSATTAQDKEHAIKLIEEAGLK TTFLMXC TT Literature-reported TTWUDYC ID TTWUDYC TTWUDYC TN Haemophilus influenzae NadR protein (Hae-influ nadR) TTWUDYC UP P44308 TTWUDYC UC NADR_HAEIN TTWUDYC BC Nicotinamide ribonucleoside uptake permease TTWUDYC SN nadR; Transcriptional regulator nadR TTWUDYC GN Hae-influ nadR TTWUDYC FC This enzyme has twoactivities: nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity catalyzes the transfer of the AMP moiety of ATP to nicotinamide ribonucleotide to form NAD(+). TTWUDYC PD 1LW7 TTWUDYC SQ MGFTTGREFHPALRMRAKYNAKYLGTKSEREKYFHLAYNKHTQFLRYQEQIMSKTKEKKVGVIFGKFYPVHTGHINMIYEAFSKVDELHVIVCSDTVRDLKLFYDSKMKRMPTVQDRLRWMQQIFKYQKNQIFIHHLVEDGIPSYPNGWQSWSEAVKTLFHEKHFEPSIVFSSEPQDKAPYEKYLGLEVSLVDPDRTFFNVSATKIRTTPFQYWKFIPKEARPFFAKTVAILGGESSGKSVLVNKLAAVFNTTSAWEYGREFVFEKLGGDEQAMQYSDYPQMALGHQRYIDYAVRHSHKIAFIDTDFITTQAFCIQYEGKAHPFLDSMIKEYPFDVTILLKNNTEWVDDGLRSLGSQKQRQQFQQLLKKLLDKYKVPYIEIESPSYLDRYNQVKAVIEKVLNEEEISELQNTTFPIKGTSQ TTWUDYC TT Literature-reported TTPXAWS ID TTPXAWS TTPXAWS TN Heat shock protein 40 (HSP40) TTPXAWS UP P25685 TTPXAWS UC DNJB1_HUMAN TTPXAWS BC Heat shock protein TTPXAWS SN Heat shock 40 kDa protein 1; HSP40; HDJ-1; DnaJ protein homolog 1; DnaJ homolog subfamily B member 1; DNAJB1 TTPXAWS GN DNAJB1 TTPXAWS FC Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. TTPXAWS PD 6BYR; 4WB7; 3AGZ; 3AGY; 3AGX TTPXAWS SQ MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI TTPXAWS TT Literature-reported TTIENCJ ID TTIENCJ TTIENCJ TN Hedgehog protein (SHH) TTIENCJ UP Q15465 TTIENCJ UC SHH_HUMAN TTIENCJ BC Hedgehog TTIENCJ SN Sonic hedgehog protein C-product; Sonic hedgehog protein; SHH; HHG-1 TTIENCJ GN SHH TTIENCJ FC Intercellular signal essential for a variety of patterning events duringdevelopment: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior- posterior axis of the developinglimb bud. Displays both floor plate- and motor neuron-inducing activity. The threshold concentration of N-product required for motor neuron induction is 5-fold lower than that required for floor plate induction. Activates the transcription of target genes by interacting with its receptor PTCH1 to prevent normal inhibition by PTCH1 on the constitutive signaling activity of SMO. TTIENCJ PD 6OEV; 6E1H; 6DMY; 3MXW; 3M1N TTIENCJ SQ MLLLARCLLLVLVSSLLVCSGLACGPGRGFGKRRHPKKLTPLAYKQFIPNVAEKTLGASGRYEGKISRNSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDKLNALAISVMNQWPGVKLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRSKYGMLARLAVEAGFDWVYYESKAHIHCSVKAENSVAAKSGGCFPGSATVHLEQGGTKLVKDLSPGDRVLAADDQGRLLYSDFLTFLDRDDGAKKVFYVIETREPRERLLLTAAHLLFVAPHNDSATGEPEASSGSGPPSGGALGPRALFASRVRPGQRVYVVAERDGDRRLLPAAVHSVTLSEEAAGAYAPLTAQGTILINRVLASCYAVIEEHSWAHRAFAPFRLAHALLAALAPARTDRGGDSGGGDRGGGGGRVALTAPGAADAPGAGATAGIHWYSQLLYQIGTWLLDSEALHPLGMAVKSS TTIENCJ TT Literature-reported TTQFZWR ID TTQFZWR TTQFZWR TN Hepatitis C virus Core protein messenger RNA (HCV Core mRNA) TTQFZWR UP P26664 TTQFZWR UC POLG_HCV1 TTQFZWR BC mRNA target TTQFZWR SN p70 (2-191) (mRNA); p56 (2-191) (mRNA); p27 (2-191) (mRNA); gp70 (2-191) (mRNA); gp68 (2-191) (mRNA); gp35 (2-191) (mRNA); gp32 (2-191) (mRNA); NS5B (2-191) (mRNA); NS3P (2-191) (mRNA); NS1 (2-191) (mRNA); Hepacivirin (2-191) (mRNA); Genome polyprotein (2-191) (mRNA); Capsid protein C (mRNA) TTQFZWR GN HCV Core mRNA TTQFZWR FC Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis). Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. TTQFZWR PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TTQFZWR SQ MSTNPKPQKKNKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRTWAQPGYPWPLYGNEGCGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSTGLYHVTNDCPNSSIVYEAADAILHTPGCVPCVREGNASRCWVAMTPTVATRDGKLPATQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRRHWTTQGCNCSIYPGHITGHRMAWDMMMNWSPTTALVMAQLLRIPQAILDMIAGAHWGVLAGIAYFSMVGNWAKVLVVLLLFAGVDAETHVTGGSAGHTVSGFVSLLAPGAKQNVQLINTNGSWHLNSTALNCNDSLNTGWLAGLFYHHKFNSSGCPERLASCRPLTDFDQGWGPISYANGSGPDQRPYCWHYPPKPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGENDTDVFVLNNTRPPLGNWFGCTWMNSTGFTKVCGAPPCVIGGAGNNTLHCPTDCFRKHPDATYSRCGSGPWITPRCLVDYPYRLWHYPCTINYTIFKIRMYVGGVEHRLEAACNWTRGERCDLEDRDRSELSPLLLTTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVVLLFLLLADARVCSCLWMMLLISQAEAALENLVILNAASLAGTHGLVSFLVFFCFAWYLKGKWVPGAVYTFYGMWPLLLLLLALPQRAYALDTEVAASCGGVVLVGLMALTLSPYYKRYISWCLWWLQYFLTRVEAQLHVWIPPLNVRGGRDAVILLMCAVHPTLVFDITKLLLAVFGPLWILQASLLKVPYFVRVQGLLRFCALARKMIGGHYVQMVIIKLGALTGTYVYNHLTPLRDWAHNGLRDLAVAVEPVVFSQMETKLITWGADTAACGDIINGLPVSARRGREILLGPADGMVSKGWRLLAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCVVIVGRVVLSGKPAIIPDREVLYREFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTASRQAEVIAPAVQTNWQKLETFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTSQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAAIGSVGLGKVLIDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPCSGSWLRDIWDWICEVLSDFKTWLKAKLMPQLPGIPFVSCQRGYKGVWRVDGIMHTRCHCGAEITGHVKNGTMRIVGPRTCRNMWSGTFPINAYTTGPCTPLPAPNYTFALWRVSAEEYVEIRQVGDFHYVTGMTTDNLKCPCQVPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQLPCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSVASSSASQLSAPSLKATCTANHDSPDAELIEANLLWRQEMGGNITRVESENKVVILDSFDPLVAEEDEREISVPAEILRKSRRFAQALPVWARPDYNPPLVETWKKPDYEPPVVHGCPLPPPKSPPVPPPRKKRTVVLTESTLSTALAELATRSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDAESYSSMPPLEGEPGDPDLSDGSWSTVSSEANAEDVVCCSMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRQKKVTFDRLQVLDSHYQDVLKEVKAAASKVKANLLSVEEACSLTPPHSAKSKFGYGAKDVRCHARKAVTHINSVWKDLLEDNVTPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVTKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGFSYDTRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCRASGVLTTSCGNTLTCYIKARAACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALDCEIYGACYSIEPLDLPPIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRARSVRARLLARGGRAAICGKYLFNWAVRTKLKLTPIAAAGQLDLSGWFTAGYSGGDIYHSVSHARPRWIWFCLLLLAAGVGIYLLPNR TTQFZWR TT Patented-recorded TTQFZWR FM mRNA target TTYO7TW ID TTYO7TW TTYO7TW TN Hepatitis C virus Protease NS2-3/3 (HCV NS2-3/3) TTYO7TW UP P26662 (810-1657) TTYO7TW UC POLG_HCV1 TTYO7TW SN HCV p23/p70 TTYO7TW GN HCV NS2-3/3 TTYO7TW FC NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication. TTYO7TW EC EC 3.4.-.- TTYO7TW PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TTYO7TW SQ LDTEVAASCGGVVLVGLMALTLSPYYKRYISWCLWWLQYFLTRVEAQLHVWIPPLNVRGGRDAVILLMCAVHPTLVFDITKLLLAVFGPLWILQASLLKVPYFVRVQGLLRFCALARKMIGGHYVQMVIIKLGALTGTYVYNHLTPLRDWAHNGLRDLAVAVEPVVFSQMETKLITWGADTAACGDIINGLPVSARRGREILLGPADGMVSKGWRLLAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVV TTYO7TW TT Literature-reported TT0PHL4 ID TT0PHL4 TT0PHL4 TN Hepatocellular carcinoma-associated antigen 90 (TPX2) TT0PHL4 UP Q9ULW0 TT0PHL4 UC TPX2_HUMAN TT0PHL4 BC TPX2 family TT0PHL4 SN Restricted expression proliferation-associated protein 100; Protein fls353; Hepatocellular carcinoma-associated antigen 519; HCA519; Differentially expressed in cancerous and non-cancerous lung cells 2; DIL2; DIL-2; C20orf2; C20orf1 TT0PHL4 GN TPX2 TT0PHL4 FC Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules (PubMed:18663142, PubMed:19208764). Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation (PubMed:18663142, PubMed:19208764). TPX2 is inactivated upon binding to importin-alpha (PubMed:26165940). At the onset of mitosis, GOLGA2 interacts with importin-alpha, liberating TPX2 from importin-alpha, allowing TPX2 to activates AURKA kinase and stimulates local microtubule nucleation (PubMed:26165940). TT0PHL4 PD 6BJC; 5LXM; 4C3P; 3HA6; 3E5A TT0PHL4 SQ MSQVKSSYSYDAPSDFINFSSLDDEGDTQNIDSWFEEKANLENKLLGKNGTGGLFQGKTPLRKANLQQAIVTPLKPVDNTYYKEAEKENLVEQSIPSNACSSLEVEAAISRKTPAQPQRRSLRLSAQKDLEQKEKHHVKMKAKRCATPVIIDEILPSKKMKVSNNKKKPEEEGSAHQDTAEKNASSPEKAKGRHTVPCMPPAKQKFLKSTEEQELEKSMKMQQEVVEMRKKNEEFKKLALAGIGQPVKKSVSQVTKSVDFHFRTDERIKQHPKNQEEYKEVNFTSELRKHPSSPARVTKGCTIVKPFNLSQGKKRTFDETVSTYVPLAQQVEDFHKRTPNRYHLRSKKDDINLLPSKSSVTKICRDPQTPVLQTKHRARAVTCKSTAELEAEELEKLQQYKFKARELDPRILEGGPILPKKPPVKPPTEPIGFDLEIEKRIQERESKKKTEDEHFEFHSRPCPTKILEDVVGVPEKKVLPITVPKSPAFALKNRIRMPTKEDEEEDEPVVIKAQPVPHYGVPFKPQIPEARTVEICPFSFDSRDKERQLQKEKKIKELQKGEVPKFKALPLPHFDTINLPEKKVKNVTQIEPFCLETDRRGALKAQTWKHQLEEELRQQKEAACFKARPNTVISQEPFVPKKEKKSVAEGLSGSLVQEPFQLATEKRAKERQELEKRMAEVEAQKAQQLEEARLQEEEQKKEELARLRRELVHKANPIRKYQGLEIKSSDQPLTVPVSPKFSTRFHC TT0PHL4 TT Literature-reported TTRV5YJ ID TTRV5YJ TTRV5YJ TN Hepcidin messenger RNA (HAMP mRNA) TTRV5YJ UP P81172 TTRV5YJ UC HEPC_HUMAN TTRV5YJ BC mRNA target TTRV5YJ SN UNQ487/PRO1003 (mRNA); Putative liver tumor regressor (mRNA); PLTR (mRNA); Liver-expressed antimicrobial peptide 1 (mRNA); LEAP1 (mRNA); LEAP-1 (mRNA); Hepcidin (mRNA); HEPC (mRNA) TTRV5YJ GN HAMP TTRV5YJ FC Acts by promoting endocytosis and degradation of ferroportin, leading to the retention of iron in iron-exporting cells and decreased flow of iron into plasma. Controls the major flows of iron into plasma: absorption of dietary iron in the intestine, recycling of iron by macrophages, which phagocytose old erythrocytes and other cells, and mobilization of stored iron from hepatocytes. Liver-produced hormone that constitutes the main circulating regulator of iron absorption and distribution across tissues. TTRV5YJ PD 4QAE; 3H0T; 2KEF; 1M4F; 1M4E TTRV5YJ SQ MALSSQIWAACLLLLLLLASLTSGSVFPQQTGQLAELQPQDRAGARASWMPMFQRRRRRDTHFPICIFCCGCCHRSKCGMCCKT TTRV5YJ TT Literature-reported TTRV5YJ FM mRNA target TT79TKF ID TT79TKF TT79TKF TN HepG2 glucose transporter (SLC2A1) TT79TKF UP P11166 TT79TKF UC GTR1_HUMAN TT79TKF BC Major facilitator TT79TKF SN Solute carrier family 2, facilitated glucose transporter member 1; HepG2 glucosetransporter; Glucose transporter type 1, erythrocyte/brain; GLUT1; GLUT-1 TT79TKF GN SLC2A1 TT79TKF FC Facilitative glucose transporter. This isoform may be responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses. TT79TKF PD 5EQI; 5EQH; 5EQG; 4PYP; 1SUK TT79TKF SQ MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHDLQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAILMTIALALLEQLPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGMCFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPEELFHPLGADSQV TT79TKF TT Preclinical TT79TKF FM Major facilitator superfamily TT4KCSR ID TT4KCSR TT4KCSR TN Herpes simplex virus DNA polymerase processivity factor (HSV UL42) TT4KCSR UP P10226 TT4KCSR UC PAP_HHV11 TT4KCSR BC Herpesviridae DNA polymerase TT4KCSR SN UL42; Protein UL42; Polymerase accessory protein; HSV PAP; DNA-binding protein UL42 TT4KCSR GN HSV UL42 TT4KCSR FC Plays an essential role in viral DNA replication by acting as the polymerase accessory subunit. Associates with the viral polymerase to increase its processivity and forms high- affinity direct interactions with DNA. Facilitates the origin- binding protein UL9 loading onto DNA thus increasing its ability to assemble into a functional complex capable of unwinding duplex DNA. TT4KCSR PD 1DML TT4KCSR SQ MTDSPGGVAPASPVEDASDASLGQPEEGAPCQVVLQGAELNGILQAFAPLRTSLLDSLLVMGDRGILIHNTIFGEQVFLPLEHSQFSRYRWRGPTAAFLSLVDQKRSLLSVFRANQYPDLRRVELAITGQAPFRTLVQRIWTTTSDGEAVELASETLMKRELTSFVVLVPQGTPDVQLRLTRPQLTKVLNATGADSATPTTFELGVNGKFSVFTTSTCVTFAAREEGVSSSTSTQVQILSNALTKAGQAAANAKTVYGENTHRTFSVVVDDCSMRAVLRRLQVGGGTLKFFLTTPVPSLCVTATGPNAVSAVFLLKPQKICLDWLGHSQGSPSAGSSASRASGSEPTDSQDSASDAVSHGDPEDLDGAARAGEAGALHACPMPSSTTRVTPTTKRGRSGGEDARADTALKKPKTGSPTAPPPADPVPLDTEDDSDAADGTAARPAAPDARSGSRYACYFRDLPTGEASPGAFSAFRGGPQTPYGFGFP TT4KCSR TT Literature-reported TTQA9C6 ID TTQA9C6 TTQA9C6 TN Herpes simplex virus E3 ubiquitin-protein ligase ICP0 (HSV ICP0) TTQA9C6 UP P08393 TTQA9C6 UC ICP0_HHV11 TTQA9C6 SN VMW110; Trans-acting transcriptional protein ICP0; RING-type E3 ubiquitin transferase ICP0; Immediate-early protein IE110; E3 ubiquitin-protein ligase ICP0; Alpha-0 protein TTQA9C6 GN HSV ICP0 TTQA9C6 FC Evades nuclear antiviral defenses triggered by dsDNA viruses. Acts during the initial stages of lytic infection and the reactivation of latent viral genome. Prevents the antiviral effect of nuclear bodies by degrading host PML and SP100. Prevents antiviral response to viral DNA induced by IFI16 by degrading it. Additionally, inhibits host IRF3 nuclear signaling to prevent interferon production by the infected cells. Interestingly, the E3 ubiquitin ligase activity associated with the RING finger domain does not seem to be directly required to inhibit the activation of IRF3 but instead plays a critical role in modulating the cellular localization of ICP0. Upon reactivation of latent genome, suppresses the silencing of viral DNA by dissociating either HDAC1 or HDAC2 from the HDAC-RCOR1-REST-KDM1A complex localized at the ND10 structures and causes their dispersal. Two cellular histone ubiquitin ligases RNF8 and RNF168 are also targeted by ICP0 for degradation, leading to a loss of ubiquitinated forms of H2A, a relief of transcriptional repression, and the activation of latent viral genomes. Enhances the localization of host CCND3 to ND10 bodies that serve as precursors of replication compartments to enable efficient viral replication. Like many RING-finger E3 ubiquitin ligases, ICP0 can induce its own ubiquitination, an activity that promotes its instability due to its targeting to the 26S proteasome for degradation. ICP0 restricts this process by recruiting the cellular ubiquitin-specific protease USP7 that cleaves the anchored ubiquitin chains from ICP0, thereby promoting its stabilization. TTQA9C6 EC EC 2.3.2.27 TTQA9C6 PD 5C56; 4WPI; 4WPH TTQA9C6 SQ MEPRPGASTRRPEGRPQREPAPDVWVFPCDRDLPDSSDSEAETEVGGRGDADHHDDDSASEADSTDTELFETGLLGPQGVDGGAVSGGSPPREEDPGSCGGAPPREDGGSDEGDVCAVCTDEIAPHLRCDTFPCMHRFCIPCMKTWMQLRNTCPLCNAKLVYLIVGVTPSGSFSTIPIVNDPQTRMEAEEAVRAGTAVDFIWTGNQRFAPRYLTLGGHTVRALSPTHPEPTTDEDDDDLDDADYVPPAPRRTPRAPPRRGAAAPPVTGGASHAAPQPAAARTAPPSAPIGPHGSSNTNTTTNSSGGGGSRQSRAAAPRGASGPSGGVGVGVGVVEAEAGRPRGRTGPLVNRPAPLANNRDPIVISDSPPASPHRPPAAPMPGSAPRPGPPASAAASGPARPRAAVAPCVRAPPPGPGPRAPAPGAEPAARPADARRVPQSHSSLAQAANQEQSLCRARATVARGSGGPGVEGGHGPSRGAAPSGAAPLPSAASVEQEAAVRPRKRRGSGQENPSPQSTRPPLAPAGAKRAATHPPSDSGPGGRGQGGPGTPLTSSAASASSSSASSSSAPTPAGAASSAAGAASSSASASSGGAVGALGGRQEETSLGPRAASGPRGPRKCARKTRHAETSGAVPAGGLTRYLPISGVSSVVALSPYVNKTITGDCLPILDMETGNIGAYVVLVDQTGNMATRLRAAVPGWSRRTLLPETAGNHVMPPEYPTAPASEWNSLWMTPVGNMLFDQGTLVGALDFRSLRSRHPWSGEQGASTRDEGKQ TTQA9C6 TT Literature-reported TTKVENM ID TTKVENM TTKVENM TN Herpes virus entry mediator ligand (CD258) TTKVENM UP O43557 TTKVENM UC TNF14_HUMAN TTKVENM BC Cytokine: tumor necrosis factor TTKVENM SN UNQ391/PRO726; Tumor necrosis factor ligand superfamily member 14, soluble form; Tumor necrosis factor ligand superfamily member 14; LIGHT; Herpesvirus entry mediator ligand; HVEML; HVEM-L TTKVENM GN TNFSF14 TTKVENM FC Binding to the decoy receptor TNFRSF6B modulates its effects. Acts as a ligand for TNFRSF14/HVEM. Upon binding to TNFRSF14/HVEM, delivers costimulatory signals to T cells, leading to T cell proliferation and IFNG production. Cytokine that binds to TNFRSF3/LTBR. TTKVENM PD 4RSU; 4KGQ; 4KGG; 4KG8; 4J6G TTKVENM SQ MEESVVRPSVFVVDGQTDIPFTRLGRSHRRQSCSVARVGLGLLLLLMGAGLAVQGWFLLQLHWRLGEMVTRLPDGPAGSWEQLIQERRSHEVNPAAHLTGANSSLTGSGGPLLWETQLGLAFLRGLSYHDGALVVTKAGYYYIYSKVQLGGVGCPLGLASTITHGLYKRTPRYPEELELLVSQQSPCGRATSSSRVWWDSSFLGGVVHLEAGEKVVVRVLDERLVRLRDGTRSYFGAFMV TTKVENM TT Literature-reported TTKVENM FM Cytokine: tumor necrosis factor TTWGTC1 ID TTWGTC1 TTWGTC1 TN Herpesvirus entry mediator (CD270) TTWGTC1 UP Q92956 TTWGTC1 UC TNR14_HUMAN TTWGTC1 BC Cytokine receptor TTWGTC1 SN UNQ329/PRO509; Tumor necrosis factor receptor-like 2; Tumor necrosis factor receptor superfamily member 14; TR2; HveA; Herpesvirus entry mediator A; Herpes virus entry mediator A; HVEM TTWGTC1 GN TNFRSF14 TTWGTC1 FC Signals via the TRAF2-TRAF3 E3 ligase pathway to promote immune cell survival and differentiation. Participates in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. In response to ligation of TNFSF14/LIGHT, delivers costimulatory signals to T cells, promoting cell proliferation and effector functions. Interacts with CD160 on NK cells, enhancing IFNG production and anti-tumor immune response. In the context of bacterial infection, acts as a signaling receptor on epithelial cells for CD160 from intraepithelial lymphocytes, triggering the production of antimicrobial proteins and proinflammatory cytokines. Upon binding to CD160 on activated CD4+ T cells, downregulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response. May interact in cis (on the same cell) or in trans (on other cells) with BTLA. In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells. Receptor for four distinct ligands: The TNF superfamily members TNFSF14/LIGHT and homotrimeric LTA/lymphotoxin-alpha and the immunoglobulin superfamily members BTLA and CD160, altogether defining a complex stimulatory and inhibitory signaling network. TTWGTC1 PD 5T2R; 5T2Q; 4RSU; 4FHQ; 2AW2 TTWGTC1 SQ MEPPGDWGPPPWRSTPKTDVLRLVLYLTFLGAPCYAPALPSCKEDEYPVGSECCPKCSPGYRVKEACGELTGTVCEPCPPGTYIAHLNGLSKCLQCQMCDPAMGLRASRNCSRTENAVCGCSPGHFCIVQDGDHCAACRAYATSSPGQRVQKGGTESQDTLCQNCPPGTFSPNGTLEECQHQTKCSWLVTKAGAGTSSSHWVWWFLSGSLVIVIVCSTVGLIICVKRRKPRGDVVKVIVSVQRKRQEAEGEATVIEALQAPPDVTTVAVEETIPSFTGRSPNH TTWGTC1 TT Literature-reported TTWQYB7 ID TTWQYB7 TTWQYB7 TN High mobility group protein B1 (HMGB1) TTWQYB7 UP P09429 TTWQYB7 UC HMGB1_HUMAN TTWQYB7 SN High mobility group protein 1; High mobility group box chromosomal protein 1; HMG1; HMG-1 TTWQYB7 GN HMGB1 TTWQYB7 FC In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogdenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins such as huntingtin (HTT) or TBP. Multifunctional redox sensitive protein with various roles in different cellular compartments. TTWQYB7 PD 6CIM; 6CIL; 6CIK; 6CIJ; 6CG0 TTWQYB7 SQ MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE TTWQYB7 TT Literature-reported TTWQYB7 KE hsa03410:Base excision repair TTWQYB7 RC R-HSA-1810476:RIP-mediated NFkB activation via ZBP1; R-HSA-211227:Activation of DNA fragmentation factor; R-HSA-3134963:DEx/H-box helicases activate type I IFN and inflammatory cytokines production; R-HSA-445989:TAK1 activates NFkB by phosphorylation and activation of IKKs complex; R-HSA-879415:Advanced glycosylation endproduct receptor signaling; R-HSA-933542:TRAF6 mediated NF-kB activation TTXQOZW ID TTXQOZW TTXQOZW TN Histidine ammonia-lyase (HAL) TTXQOZW UP P42357 TTXQOZW UC HUTH_HUMAN TTXQOZW BC Carbon-nitrogen lyase TTXQOZW SN Histidine ammonialyase; Histidase; HIS TTXQOZW GN HAL TTXQOZW FC Histidine ammonia-lyase activity, histidine catabolic process. TTXQOZW EC EC 4.3.1.3 TTXQOZW SQ MPRYTVHVRGEWLAVPCQDAQLTVGWLGREAVRRYIKNKPDNGGFTSVDDAHFLVRRCKGLGLLDNEDRLEVALENNEFVEVVIEGDAMSPDFIPSQPEGVYLYSKYREPEKYIELDGDRLTTEDLVNLGKGRYKIKLTPTAEKRVQKSREVIDSIIKEKTVVYGITTGFGKFARTVIPINKLQELQVNLVRSHSSGVGKPLSPERCRMLLALRINVLAKGYSGISLETLKQVIEMFNASCLPYVPEKGTVGASGDLAPLSHLALGLVGEGKMWSPKSGWADAKYVLEAHGLKPVILKPKEGLALINGTQMITSLGCEAVERASAIARQADIVAALTLEVLKGTTKAFDTDIHALRPHRGQIEVAFRFRSLLDSDHHPSEIAESHRFCDRVQDAYTLRCCPQVHGVVNDTIAFVKNIITTELNSATDNPMVFANRGETVSGGNFHGEYPAKALDYLAIGIHELAAISERRIERLCNPSLSELPAFLVAEGGLNSGFMIAHCTAAALVSENKALCHPSSVDSLSTSAATEDHVSMGGWAARKALRVIEHVEQVLAIELLAACQGIEFLRPLKTTTPLEKVYDLVRSVVRPWIKDRFMAPDIEAAHRLLLEQKVWEVAAPYIEKYRMEHIPESRPLSPTAFSLQFLHKKSTKIPESEDL TTXQOZW TT Literature-reported TTXQOZW FM Carbon-nitrogen lyases TTU2I3J ID TTU2I3J TTU2I3J TN HLA class II antigen DQ-2 alpha (HLA-DQA1) TTU2I3J UP P01909 TTU2I3J UC DQA1_HUMAN TTU2I3J BC MHC class II TTU2I3J SN MHC class II DQA1; HLADQA1; HLADCA; HLA-DQA1; HLA class II histocompatibility antigen, DQ alpha 1 chain; DCalpha; DC1 alpha chain TTU2I3J GN HLA-DQA1 TTU2I3J FC Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs,other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM andMHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. TTU2I3J PD 6MFG; 6MFF; 5KSV; 5KSU; 5KSB TTU2I3J SQ MILNKALMLGALALTTVMSPCGGEDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYVDLGRKETVWCLPVLRQFRFDPQFALTNIAVLKHNLNSLIKRSNSTAATNEVPEVTVFSKSPVTLGQPNILICLVDNIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTLLPSAEESYDCKVEHWGLDKPLLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTVFIIRGLRSVGASRHQGPL TTU2I3J TT Literature-reported TT8UPW6 ID TT8UPW6 TT8UPW6 TN hnRNP A2/B1 messenger RNA (HNRNPA2B1 mRNA) TT8UPW6 UP P22626 TT8UPW6 UC ROA2_HUMAN TT8UPW6 BC mRNA target TT8UPW6 SN hnRNP A2/B1 (mRNA); Heterogeneous nuclear ribonucleoproteins A2/B1 (mRNA); HNRPA2B1 (mRNA) TT8UPW6 GN HNRNPA2B1 TT8UPW6 FC The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm. Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion. Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs. Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. TT8UPW6 PD 5WWG; 5WWF; 5WWE; 5HO4; 5EN1 TT8UPW6 SQ MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY TT8UPW6 TT Literature-reported TT8UPW6 FM mRNA target TTOB49C ID TTOB49C TTOB49C TN Homeodomain interacting protein kinase 2 (HIPK2) TTOB49C UP Q9H2X6 TTOB49C UC HIPK2_HUMAN TTOB49C BC Kinase TTOB49C SN hHIPk2; Homeodomain-interacting protein kinase 2 TTOB49C GN HIPK2 TTOB49C FC Acts as a corepressor of several transcription factors, including SMAD1 and POU4F1/Brn3a and probably NK homeodomain transcription factors. Phosphorylates PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300, CTNNB1, HMGA1 and ZBTB4. Inhibits cell growth and promotes apoptosis through the activation of p53/TP53 both at the transcription level and at the protein level (by phosphorylation and indirect acetylation). The phosphorylation of p53/TP53 may be mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the response to hypoxia by acting as a transcriptional co-suppressor of HIF1A. Mediates transcriptional activation of TP73. In response to TGFB, cooperates with DAXX to activate JNK. Negative regulator through phosphorylation and subsequent proteasomal degradation of CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin signaling pathway acts as an intermediate kinase between MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB. Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-protein ligase activity. Activates CREB1 and ATF1 transcription factors by phosphorylation in response to genotoxic stress. In response to DNA damage, stabilizes PML by phosphorylation. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. Promotes angiogenesis, and is involved in erythroid differentiation, especially during fetal liver erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates EP300 transcription regulation activity. Triggers ZBTB4 protein degradation in response to DNA damage. Modulates HMGA1 DNA-binding affinity. In response to high glucose, triggers phosphorylation-mediated subnuclear localization shifting of PDX1. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Serine/threonine-protein kinase involved in transcription regulation, p53/TP53-mediated cellular apoptosis and regulation of the cell cycle. TTOB49C EC EC 2.7.11.1 TTOB49C SQ MAPVYEGMASHVQVFSPHTLQSSAFCSVKKLKIEPSSNWDMTGYGSHSKVYSQSKNIPLSQPATTTVSTSLPVPNPSLPYEQTIVFPGSTGHIVVTSASSTSVTGQVLGGPHNLMRRSTVSLLDTYQKCGLKRKSEEIENTSSVQIIEEHPPMIQNNASGATVATATTSTATSKNSGSNSEGDYQLVQHEVLCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYNFVRAYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPVLQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDTDSPYPLWRLKTPDDHEAETGIKSKEARKYIFNCLDDMAQVNMTTDLEGSDMLVEKADRREFIDLLKKMLTIDADKRITPIETLNHPFVTMTHLLDFPHSTHVKSCFQNMEICKRRVNMYDTVNQSKTPFITHVAPSTSTNLTMTFNNQLTTVHNQAPSSTSATISLANPEVSILNYPSTLYQPSAASMAAVAQRSMPLQTGTAQICARPDPFQQALIVCPPGFQGLQASPSKHAGYSVRMENAVPIVTQAPGAQPLQIQPGLLAQQAWPSGTQQILLPPAWQQLTGVATHTSVQHATVIPETMAGTQQLADWRNTHAHGSHYNPIMQQPALLTGHVTLPAAQPLNVGVAHVMRQQPTSTTSSRKSKQHQSSVRNVSTCEVSSSQAISSPQRSKRVKENTPPRCAMVHSSPACSTSVTCGWGDVASSTTRERQRQTIVIPDTPSPTVSVITISSDTDEEEEQKHAPTSTVSKQRKNVISCVTVHDSPYSDSSSNTSPYSVQQRAGHNNANAFDTKGSLENHCTGNPRTIIVPPLKTQASEVLVECDSLVPVNTSHHSSSYKSKSSSNVTSTSGHSSGSSSGAITYRQQRPGPHFQQQQPLNLSQAQQHITTDRTGSHRRQQAYITPTMAQAPYSFPHNSPSHGTVHPHLAAAAAAAHLPTQPHLYTYTAPAALGSTGTVAHLVASQGSARHTVQHTAYPASIVHQVPVSMGPRVLPSPTIHPSQYPAQFAHQTYISASPASTVYTGYPLSPAKVNQYPYI TTOB49C TT Literature-reported TTLH8WG ID TTLH8WG TTLH8WG TN HSP27 messenger RNA (HSPB3 mRNA) TTLH8WG UP Q12988 TTLH8WG UC HSPB3_HUMAN TTLH8WG BC mRNA target TTLH8WG SN Protein 3 (mRNA); HspB3 (mRNA); Heat shock protein beta-3 (mRNA); Heat shock 17 kDa protein (mRNA); HSPL27 (mRNA); HSP 17 (mRNA) TTLH8WG GN HSPB3 TTLH8WG FC Inhibitor of actin polymerization. TTLH8WG PD 6F2R TTLH8WG SQ MAKIILRHLIEIPVRYQEEFEARGLEDCRLDHALYALPGPTIVDLRKTRAAQSPPVDSAAETPPREGKSHFQILLDVVQFLPEDIIIQTFEGWLLIKAQHGTRMDEHGFISRSFTRQYKLPDGVEIKDLSAVLCHDGILVVEVKDPVGTK TTLH8WG TT Literature-reported TTLH8WG FM mRNA target TT5SOEU ID TT5SOEU TT5SOEU TN Hsp90 co-chaperone Cdc37 (CDC37) TT5SOEU UP Q16543 TT5SOEU UC CDC37_HUMAN TT5SOEU SN p50Cdc37; Hsp90 co-chaperone Cdc37, N-terminally processed; Hsp90 chaperone protein kinase-targeting subunit; CDC37A TT5SOEU GN CDC37 TT5SOEU FC Inhibits HSP90AA1 ATPase activity. Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. TT5SOEU PD 5HPE; 5FWP; 5FWM; 5FWL; 5FWK TT5SOEU SQ MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTKIKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPGDPLLEAVPKTGDEKDVSV TT5SOEU TT Literature-reported TT5SOEU KE hsa04151:PI3K-Akt signaling pathway TTF3I4E ID TTF3I4E TTF3I4E TN Human papillomavirus E2 region messenger RNA (HPV E2 mRNA) TTF3I4E UP P03122 TTF3I4E UC VE2_BPV1 TTF3I4E BC mRNA target TTF3I4E SN BPV regulatory protein E2 (mRNA) TTF3I4E GN HPV E2 mRNA TTF3I4E FC A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex. Plays a role in the initiation of viral DNA replication. TTF3I4E PD 6BUS; 2JEX; 2JEU; 2BOP; 1JJH TTF3I4E SQ METACERLHVAQETQMQLIEKSSDKLQDHILYWTAVRTENTLLYAARKKGVTVLGHCRVPHSVVCQERAKQAIEMQLSLQELSKTEFGDEPWSLLDTSWDRYMSEPKRCFKKGARVVEVEFDGNASNTNWYTVYSNLYMRTEDGWQLAKAGADGTGLYYCTMAGAGRIYYSRFGDEAARFSTTGHYSVRDQDRVYAGVSSTSSDFRDRPDGVWVASEGPEGDPAGKEAEPAQPVSSLLGSPACGPIRAGLGWVRDGPRSHPYNFPAGSGGSILRSSSTPVQGTVPVDLASRQEEEEQSPDSTEEEPVTLPRRTTNDGFHLLKAGGSCFALISGTANQVKCYRFRVKKNHRHRYENCTTTWFTVADNGAERQGQAQILITFGSPSQRQDFLKHVPLPPGMNISGFTASLDF TTF3I4E TT Literature-reported TTF3I4E FM mRNA target TT7OU0X ID TT7OU0X TT7OU0X TN Human papillomavirus-18 E6 region messenger RNA (HPV-18 E6 mRNA) TT7OU0X UP P06463 TT7OU0X UC VE6_HPV18 TT7OU0X BC mRNA target TT7OU0X SN HPV-18 protein E6 (mRNA); HPV-18 E6 (mRNA) TT7OU0X GN HPV-18 E6 mRNA TT7OU0X FC Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway. Plays a major role in the induction and maintenance of cellular transformation. TT7OU0X PD 5K4F; 5IC3; 4JOR; 2I0L; 2I0I TT7OU0X SQ MARFEDPTRRPYKLPDLCTELNTSLQDIEITCVYCKTVLELTEVFEFAFKDLFVVYRDSIPHAACHKCIDFYSRIRELRHYSDSVYGDTLEKLTNTGLYNLLIRCLRCQKPLNPAEKLRHLNEKRRFHNIAGHYRGQCHSCCNRARQERLQRRRETQV TT7OU0X TT Literature-reported TT7OU0X FM mRNA target TTIWZ0O ID TTIWZ0O TTIWZ0O TN Huntingtin messenger RNA (HTT mRNA) TTIWZ0O UP P42858 TTIWZ0O UC HD_HUMAN TTIWZ0O BC mRNA target TTIWZ0O SN IT15 (mRNA); Huntington disease protein (mRNA); Huntingtin (mRNA); HD protein (mRNA); HD (mRNA) TTIWZ0O GN HTT TTIWZ0O FC May play a role in microtubule-mediated transport or vesicle function. TTIWZ0O PD 6N8C; 6EZ8; 4RAV; 4FED; 4FEC TTIWZ0O SQ MATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQQQQQPPPPPPPPPPPQLPQPPPQAQPLLPQPQPPPPPPPPPPGPAVAEEPLHRPKKELSATKKDRVNHCLTICENIVAQSVRNSPEFQKLLGIAMELFLLCSDDAESDVRMVADECLNKVIKALMDSNLPRLQLELYKEIKKNGAPRSLRAALWRFAELAHLVRPQKCRPYLVNLLPCLTRTSKRPEESVQETLAAAVPKIMASFGNFANDNEIKVLLKAFIANLKSSSPTIRRTAAGSAVSICQHSRRTQYFYSWLLNVLLGLLVPVEDEHSTLLILGVLLTLRYLVPLLQQQVKDTSLKGSFGVTRKEMEVSPSAEQLVQVYELTLHHTQHQDHNVVTGALELLQQLFRTPPPELLQTLTAVGGIGQLTAAKEESGGRSRSGSIVELIAGGGSSCSPVLSRKQKGKVLLGEEEALEDDSESRSDVSSSALTASVKDEISGELAASSGVSTPGSAGHDIITEQPRSQHTLQADSVDLASCDLTSSATDGDEEDILSHSSSQVSAVPSDPAMDLNDGTQASSPISDSSQTTTEGPDSAVTPSDSSEIVLDGTDNQYLGLQIGQPQDEDEEATGILPDEASEAFRNSSMALQQAHLLKNMSHCRQPSDSSVDKFVLRDEATEPGDQENKPCRIKGDIGQSTDDDSAPLVHCVRLLSASFLLTGGKNVLVPDRDVRVSVKALALSCVGAAVALHPESFFSKLYKVPLDTTEYPEEQYVSDILNYIDHGDPQVRGATAILCGTLICSILSRSRFHVGDWMGTIRTLTGNTFSLADCIPLLRKTLKDESSVTCKLACTAVRNCVMSLCSSSYSELGLQLIIDVLTLRNSSYWLVRTELLETLAEIDFRLVSFLEAKAENLHRGAHHYTGLLKLQERVLNNVVIHLLGDEDPRVRHVAAASLIRLVPKLFYKCDQGQADPVVAVARDQSSVYLKLLMHETQPPSHFSVSTITRIYRGYNLLPSITDVTMENNLSRVIAAVSHELITSTTRALTFGCCEALCLLSTAFPVCIWSLGWHCGVPPLSASDESRKSCTVGMATMILTLLSSAWFPLDLSAHQDALILAGNLLAASAPKSLRSSWASEEEANPAATKQEEVWPALGDRALVPMVEQLFSHLLKVINICAHVLDDVAPGPAIKAALPSLTNPPSLSPIRRKGKEKEPGEQASVPLSPKKGSEASAASRQSDTSGPVTTSKSSSLGSFYHLPSYLKLHDVLKATHANYKVTLDLQNSTEKFGGFLRSALDVLSQILELATLQDIGKCVEEILGYLKSCFSREPMMATVCVQQLLKTLFGTNLASQFDGLSSNPSKSQGRAQRLGSSSVRPGLYHYCFMAPYTHFTQALADASLRNMVQAEQENDTSGWFDVLQKVSTQLKTNLTSVTKNRADKNAIHNHIRLFEPLVIKALKQYTTTTCVQLQKQVLDLLAQLVQLRVNYCLLDSDQVFIGFVLKQFEYIEVGQFRESEAIIPNIFFFLVLLSYERYHSKQIIGIPKIIQLCDGIMASGRKAVTHAIPALQPIVHDLFVLRGTNKADAGKELETQKEVVVSMLLRLIQYHQVLEMFILVLQQCHKENEDKWKRLSRQIADIILPMLAKQQMHIDSHEALGVLNTLFEILAPSSLRPVDMLLRSMFVTPNTMASVSTVQLWISGILAILRVLISQSTEDIVLSRIQELSFSPYLISCTVINRLRDGDSTSTLEEHSEGKQIKNLPEETFSRFLLQLVGILLEDIVTKQLKVEMSEQQHTFYCQELGTLLMCLIHIFKSGMFRRITAAATRLFRSDGCGGSFYTLDSLNLRARSMITTHPALVLLWCQILLLVNHTDYRWWAEVQQTPKRHSLSSTKLLSPQMSGEEEDSDLAAKLGMCNREIVRRGALILFCDYVCQNLHDSEHLTWLIVNHIQDLISLSHEPPVQDFISAVHRNSAASGLFIQAIQSRCENLSTPTMLKKTLQCLEGIHLSQSGAVLTLYVDRLLCTPFRVLARMVDILACRRVEMLLAANLQSSMAQLPMEELNRIQEYLQSSGLAQRHQRLYSLLDRFRLSTMQDSLSPSPPVSSHPLDGDGHVSLETVSPDKDWYVHLVKSQCWTRSDSALLEGAELVNRIPAEDMNAFMMNSEFNLSLLAPCLSLGMSEISGGQKSALFEAAREVTLARVSGTVQQLPAVHHVFQPELPAEPAAYWSKLNDLFGDAALYQSLPTLARALAQYLVVVSKLPSHLHLPPEKEKDIVKFVVATLEALSWHLIHEQIPLSLDLQAGLDCCCLALQLPGLWSVVSSTEFVTHACSLIYCVHFILEAVAVQPGEQLLSPERRTNTPKAISEEEEEVDPNTQNPKYITAACEMVAEMVESLQSVLALGHKRNSGVPAFLTPLLRNIIISLARLPLVNSYTRVPPLVWKLGWSPKPGGDFGTAFPEIPVEFLQEKEVFKEFIYRINTLGWTSRTQFEETWATLLGVLVTQPLVMEQEESPPEEDTERTQINVLAVQAITSLVLSAMTVPVAGNPAVSCLEQQPRNKPLKALDTRFGRKLSIIRGIVEQEIQAMVSKRENIATHHLYQAWDPVPSLSPATTGALISHEKLLLQINPERELGSMSYKLGQVSIHSVWLGNSITPLREEEWDEEEEEEADAPAPSSPPTSPVNSRKHRAGVDIHSCSQFLLELYSRWILPSSSARRTPAILISEVVRSLLVVSDLFTERNQFELMYVTLTELRRVHPSEDEILAQYLVPATCKAAAVLGMDKAVAEPVSRLLESTLRSSHLPSRVGALHGVLYVLECDLLDDTAKQLIPVISDYLLSNLKGIAHCVNIHSQQHVLVMCATAFYLIENYPLDVGPEFSASIIQMCGVMLSGSEESTPSIIYHCALRGLERLLLSEQLSRLDAESLVKLSVDRVNVHSPHRAMAALGLMLTCMYTGKEKVSPGRTSDPNPAAPDSESVIVAMERVSVLFDRIRKGFPCEARVVARILPQFLDDFFPPQDIMNKVIGEFLSNQQPYPQFMATVVYKVFQTLHSTGQSSMVRDWVMLSLSNFTQRAPVAMATWSLSCFFVSASTSPWVAAILPHVISRMGKLEQVDVNLFCLVATDFYRHQIEEELDRRAFQSVLEVVAAPGSPYHRLLTCLRNVHKVTTC TTIWZ0O TT Literature-reported TTIWZ0O FM mRNA target TTQF4TK ID TTQF4TK TTQF4TK TN Hydroxymethylglutaryl-CoA synthase 1 (HMGCS1) TTQF4TK UP Q01581 TTQF4TK UC HMCS1_HUMAN TTQF4TK SN Hydroxymethylglutaryl-CoA synthase, cytoplasmic; HMGCS; HMG-CoA synthase; 3-hydroxy-3-methylglutaryl coenzyme A synthase 1 TTQF4TK GN HMGCS1 TTQF4TK FC This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase. TTQF4TK EC EC 2.3.3.10 TTQF4TK PD 2P8U TTQF4TK SQ MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQAKMGFCTDREDINSLCMTVVQNLMERNNLSYDCIGRLEVGTETIIDKSKSVKTNLMQLFEESGNTDIEGIDTTNACYGGTAAVFNAVNWIESSSWDGRYALVVAGDIAVYATGNARPTGGVGAVALLIGPNAPLIFERGLRGTHMQHAYDFYKPDMLSEYPIVDGKLSIQCYLSALDRCYSVYCKKIHAQWQKEGNDKDFTLNDFGFMIFHSPYCKLVQKSLARMLLNDFLNDQNRDKNSIYSGLEAFGDVKLEDTYFDRDVEKAFMKASSELFSQKTKASLLVSNQNGNMYTSSVYGSLASVLAQYSPQQLAGKRIGVFSYGSGLAATLYSLKVTQDATPGSALDKITASLCDLKSRLDSRTGVAPDVFAENMKLREDTHHLVNYIPQGSIDSLFEGTWYLVRVDEKHRRTYARRPTPNDDTLDEGVGLVHSNIATEHIPSPAKKVPRLPATAAEPEAAVISNGEH TTQF4TK TT Literature-reported TTZT9R2 ID TTZT9R2 TTZT9R2 TN Hydroxysteroid dehydrogenase 3-beta (HSD3B) TTZT9R2 UP P14060; P26439 TTZT9R2 UC 3BHS1_HUMAN; 3BHS2_HUMAN TTZT9R2 BC Short-chain dehydrogenases reductase TTZT9R2 SN 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase TTZT9R2 GN HSD3B1; HSD3B2 TTZT9R2 FC Catalyzes the biosynthesis of the steroid progesterone from pregnenolone, 17-hydroxyprogesterone from 17-hydroxypregnenolone, and androstenedione from dehydroepiandrosterone (DHEA) in the adrenal gland. Also catalyzes the oxidative conversion of 5-3-hydroxysteroids to the 4-3-keto configuration and is, therefore, essential for the biosynthesis of all classes of hormonal steroids, namely progesterone, glucocorticoids, mineralocorticoids, androgens, and estrogens. TTZT9R2 SQ MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALQDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSLVDRHKETLKSKTQ TTZT9R2 TT Literature-reported TTNB6UQ ID TTNB6UQ TTNB6UQ TN Hyperpolarization cyclic nucleotide-gated channel 1 (HCN1) TTNB6UQ UP O60741 TTNB6UQ UC HCN1_HUMAN TTNB6UQ BC Voltage-gated ion channel TTNB6UQ SN Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1; Brain cyclic nucleotide-gated channel 1; BCNG1; BCNG-1 TTNB6UQ GN HCN1 TTNB6UQ FC Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). May mediate responses to sour stimuli. Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. TTNB6UQ PD 5U6P; 5U6O TTNB6UQ SQ MEGGGKPNSSSNSRDDGNSVFPAKASATGAGPAAAEKRLGTPPGGGGAGAKEHGNSVCFKVDGGGGGGGGGGGGEEPAGGFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAVEKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNVASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVEKGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIGYGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADMRQKIHDYYEHRYQGKIFDEENILNELNDPLREEIVNFNCRKLVATMPLFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIAPINYPQMTTLNSTSSTTTPTSRMRTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPVQSPLAARTFHYASPTASQLSLMQQQPQQQVQQSQPPQTQPQQPSPQPQTPGSSTPKNEVHKSTQALHNTNLTREVRPLSASQPSLPHEVSTLISRPHPTVGESLASIPQPVTAVPGTGLQAGGRSTVPQRVTLFRQMSSGAIPPNRGVPPAPPPPAAALPRESSSVLNTDPDAEKPRFASNL TTNB6UQ TT Literature-reported TT9EUT4 ID TT9EUT4 TT9EUT4 TN Hyperpolarization cyclic nucleotide-gated channel 2 (HCN2) TT9EUT4 UP Q9UL51 TT9EUT4 UC HCN2_HUMAN TT9EUT4 BC Voltage-gated ion channel TT9EUT4 SN Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2; Brain cyclic nucleotide-gated channel 2; BCNG2; BCNG-2 TT9EUT4 GN HCN2 TT9EUT4 FC Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current. Modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages. Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. TT9EUT4 PD 3U10; 2MPF TT9EUT4 SQ MDARGGGGRPGESPGATPAPGPPPPPPPAPPQQQPPPPPPPAPPPGPGPAPPQHPPRAEALPPEAADEGGPRGRLRSRDSSCGRPGTPGAASTAKGSPNGECGRGEPQCSPAGPEGPARGPKVSFSCRGAASGPAPGPGPAEEAGSEEAGPAGEPRGSQASFMQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPRNCWVSINGMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLNSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPPQVTSAIATLQQAAAMSFCPQVARPLVGPLALGSPRLVRRPPPGPAPAAASPGPPPPASPPGAPASPRAPRTSPYGGLPAAPLAGPALPARRLSRASRPLSASQPSLPHGAPGPAASTRPASSSTPRLGPTPAARAAAPSPDRRDSASPGAAGGLDPQDSARSRLSSNL TT9EUT4 TT Literature-reported TTQP04A ID TTQP04A TTQP04A TN Hyperpolarization cyclic nucleotide-gated channel 4 (HCN4) TTQP04A UP Q9Y3Q4 TTQP04A UC HCN4_HUMAN TTQP04A BC Voltage-gated ion channel TTQP04A SN Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 TTQP04A GN HCN4 TTQP04A FC Contributes to the native pacemaker currents in heart (If) that regulate the rhythm of heart beat. May contribute to the native pacemaker currents in neurons (Ih). May mediate responses to sour stimuli. Hyperpolarization-activated ion channel with very slow activation and inactivation exhibiting weak selectivity for potassium over sodium ions. TTQP04A PD 6GYO; 6GYN; 4NVP; 4KL1; 4HBN TTQP04A SQ MDKLPPSMRKRLYSLPQQVGAKAWIMDEEEDAEEEGAGGRQDPSRRSIRLRPLPSPSPSAAAGGTESRSSALGAADSEGPARGAGKSSTNGDCRRFRGSLASLGSRGGGSGGTGSGSSHGHLHDSAEERRLIAEGDASPGEDRTPPGLAAEPERPGASAQPAASPPPPQQPPQPASASCEQPSVDTAIKVEGGAAAGDQILPEAEVRLGQAGFMQRQFGAMLQPGVNKFSLRMFGSQKAVEREQERVKSAGFWIIHPYSDFRFYWDLTMLLLMVGNLIIIPVGITFFKDENTTPWIVFNVVSDTFFLIDLVLNFRTGIVVEDNTEIILDPQRIKMKYLKSWFMVDFISSIPVDYIFLIVETRIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIVNLIGMMLLLCHWDGCLQFLVPMLQDFPDDCWVSINNMVNNSWGKQYSYALFKAMSHMLCIGYGRQAPVGMSDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPPDTRQRIHDYYEHRYQGKMFDEESILGELSEPLREEIINFNCRKLVASMPLFANADPNFVTSMLTKLRFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKETKLADGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVALDRLDRIGKKNSILLHKVQHDLNSGVFNYQENEIIQQIVQHDREMAHCAHRVQAAASATPTPTPVIWTPLIQAPLQAAAATTSVAIALTHHPRLPAAIFRPPPGSGLGNLGAGQTPRHLKRLQSLIPSALGSASPASSPSQVDTPSSSSFHIQQLAGFSAPAGLSPLLPSSSSSPPPGACGSPSAPTPSAGVAATTIAGFGHFHKALGGSLSSSDSPLLTPLQPGARSPQAAQPSPAPPGARGGLGLPEHFLPPPPSSRSPSSSPGQLGQPPGELSLGLATGPLSTPETPPRQPEPPSLVAGASGGASPVGFTPRGGLSPPGHSPGPPRTFPSAPPRASGSHGSLLLPPASSPPPPQVPQRRGTPPLTPGRLTQDLKLISASQPALPQDGAQTLRRASPHSSGESMAAFPLFPRAGGGSGGSGSSGGLGPPGRPYGAIPGQHVTLPRKTSSGSLPPPLSLFGARATSSGGPPLTAGPQREPGARPEPVRSKLPSNL TTQP04A TT Literature-reported TTU4QSN ID TTU4QSN TTU4QSN TN IGFBP2 messenger RNA (IGFBP2 mRNA) TTU4QSN UP P18065 TTU4QSN UC IBP2_HUMAN TTU4QSN BC mRNA target TTU4QSN SN Insulinlike growth factorbinding protein 2 (mRNA); Insulin-like growth factor-binding protein 2 (mRNA); IGFbinding protein 2 (mRNA); IGFBP-2 (mRNA); IGF-binding protein 2 (mRNA); IBP2 (mRNA); IBP-2 (mRNA); BP2 (mRNA) TTU4QSN GN IGFBP2 TTU4QSN FC IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Inhibits IGF-mediated growth and developmental rates. TTU4QSN PD 2H7T TTU4QSN SQ MLPRVGCPALPLPPPPLLPLLLLLLGASGGGGGARAEVLFRCPPCTPERLAACGPPPVAPPAAVAAVAGGARMPCAELVREPGCGCCSVCARLEGEACGVYTPRCGQGLRCYPHPGSELPLQALVMGEGTCEKRRDAEYGASPEQVADNGDDHSEGGLVENHVDSTMNMLGGGGSAGRKPLKSGMKELAVFREKVTEQHRQMGKGGKHHLGLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDERGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKLIQGAPTIRGDPECHLFYNEQQEARGVHTQRMQ TTU4QSN TT Literature-reported TTU4QSN FM mRNA target TTDWEA8 ID TTDWEA8 TTDWEA8 TN IGFBP5 messenger RNA (IGFBP5 mRNA) TTDWEA8 UP P24593 TTDWEA8 UC IBP5_HUMAN TTDWEA8 BC mRNA target TTDWEA8 SN Insulin-like growth factor-binding protein 5 (mRNA); IGFBP-5 (mRNA); IGF-binding protein 5 (mRNA); IBP5 (mRNA); IBP-5 (mRNA) TTDWEA8 GN IGFBP5 TTDWEA8 FC IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. TTDWEA8 PD 1H59; 1BOE TTDWEA8 SQ MVLLTAVLLLLAAYAGPAQSLGSFVHCEPCDEKALSMCPPSPLGCELVKEPGCGCCMTCALAEGQSCGVYTERCAQGLRCLPRQDEEKPLHALLHGRGVCLNEKSYREQVKIERDSREHEEPTTSEMAEETYSPKIFRPKHTRISELKAEAVKKDRRKKLTQSKFVGGAENTAHPRIISAPEMRQESEQGPCRRHMEASLQELKASPRMVPRAVYLPNCDRKGFYKRKQCKPSRGRKRGICWCVDKYGMKLPGMEYVDGDFQCHTFDSSNVE TTDWEA8 TT Literature-reported TTDWEA8 FM mRNA target TTO8F0B ID TTO8F0B TTO8F0B TN IL4R messenger RNA (IL4R mRNA) TTO8F0B UP P24394 TTO8F0B UC IL4RA_HUMAN TTO8F0B BC mRNA target TTO8F0B SN Interleukin-4 receptor subunit alpha (mRNA); IL4RA (mRNA); IL-4RA (mRNA); IL-4R-alpha (mRNA); IL-4R subunit alpha (mRNA); IL-4 receptor subunit alpha (mRNA); CD124 antigen (mRNA); CD124 (mRNA); 582J2.1 (mRNA) TTO8F0B GN IL4R TTO8F0B FC Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2. Receptor for both interleukin 4 and interleukin 13. TTO8F0B PD 5E4E; 3BPO; 3BPN; 3BPL; 1ITE TTO8F0B SQ MGWLCSGLLFPVSCLVLLQVASSGNMKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWAGQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNYLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLRIAASTLKSGISYRARVRAWAQCYNTTWSEWSPSTKWHNSYREPFEQHLLLGVSVSCIVILAVCLLCYVSITKIKKEWWDQIPNPARSRLVAIIIQDAQGSQWEKRSRGQEPAKCPHWKNCLTKLLPCFLEHNMKRDEDPHKAAKEMPFQGSGKSAWCPVEISKTVLWPESISVVRCVELFEAPVECEEEEEVEEEKGSFCASPESSRDDFQEGREGIVARLTESLFLDLLGEENGGFCQQDMGESCLLPPSGSTSAHMPWDEFPSAGPKEAPPWGKEQPLHLEPSPPASPTQSPDNLTCTETPLVIAGNPAYRSFSNSLSQSPCPRELGPDPLLARHLEEVEPEMPCVPQLSEPTTVPQPEPETWEQILRRNVLQHGAAAAPVSAPTSGYQEFVHAVEQGGTQASAVVGLGPPGEAGYKAFSSLLASSAVSPEKCGFGASSGEEGYKPFQDLIPGCPGDPAPVPVPLFTFGLDREPPRSPQSSHLPSSSPEHLGLEPGEKVEDMPKPPLPQEQATDPLVDSLGSGIVYSALTCHLCGHLKQCHGQEDGGQTPVMASPCCGCCCGDRSSPPTTPLRAPDPSPGGVPLEASLCPASLAPSGISEKSKSSSSFHPAPGNAQSSSQTPKIVNFVSVGPTYMRVS TTO8F0B TT Literature-reported TTO8F0B FM mRNA target TTCK85E ID TTCK85E TTCK85E TN Immune costimulatory protein B7H4 (VTCN1) TTCK85E UP Q7Z7D3 TTCK85E UC VTCN1_HUMAN TTCK85E BC Immunoglobulin TTCK85E SN VTCN1; V-set domain-containing T-cell activation inhibitor 1; T-cell costimulatory molecule B7x; Protein B7S1; B7h.5 TTCK85E GN VTCN1 TTCK85E FC Negatively regulates T-cell-mediated immune response byinhibiting T-cell activation, proliferation, cytokine production and development of cytotoxicity. When expressed on the cell surface of tumor macrophages, plays an important role, together with regulatory T-cells (Treg), in the suppression of tumor- associated antigen-specific T-cell immunity. Involved in promoting epithelial cell transformation. TTCK85E PD 4GOS TTCK85E SQ MASLGQILFWSIISIIIILAGAIALIIGFGISGRHSITVTTVASAGNIGEDGILSCTFEPDIKLSDIVIQWLKEGVLGLVHEFKEGKDELSEQDEMFRGRTAVFADQVIVGNASLRLKNVQLTDAGTYKCYIITSKGKGNANLEYKTGAFSMPEVNVDYNASSETLRCEAPRWFPQPTVVWASQVDQGANFSEVSNTSFELNSENVTMKVVSVLYNVTINNTYSCMIENDIAKATGDIKVTESEIKRRSHLQLLNSKASLCVSSFFAISWALLPLSPYLMLK TTCK85E TT Literature-reported TTZK4I3 ID TTZK4I3 TTZK4I3 TN Immunoglobulin gamma Fc receptor I (FCGR1) TTZK4I3 UP P12314 TTZK4I3 UC FCGR1_HUMAN TTZK4I3 BC Immunoglobulin TTZK4I3 SN IgG Fc receptor I; FcRI; Fc-gamma RI; FCGR1A; CD64 antigen; CD64 TTZK4I3 GN FCGR1A TTZK4I3 FC High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses. TTZK4I3 PD 4ZNE; 4X4M; 4W4O; 3RJD TTZK4I3 SQ MWFLTTLLLWVPVDGQVDTTKAVITLQPPWVSVFQEETVTLHCEVLHLPGSSSTQWFLNGTATQTSTPSYRITSASVNDSGEYRCQRGLSGRSDPIQLEIHRGWLLLQVSSRVFTEGEPLALRCHAWKDKLVYNVLYYRNGKAFKFFHWNSNLTILKTNISHNGTYHCSGMGKHRYTSAGISVTVKELFPAPVLNASVTSPLLEGNLVTLSCETKLLLQRPGLQLYFSFYMGSKTLRGRNTSSEYQILTARREDSGLYWCEAATEDGNVLKRSPELELQVLGLQLPTPVWFHVLFYLAVGIMFLVNTVLWVTIRKELKRKKKWDLEISLDSGHEKKVISSLQEDRHLEEELKCQEQKEEQLQEGVHRKEPQGAT TTZK4I3 TT Literature-reported TTHOJ5F ID TTHOJ5F TTHOJ5F TN Importin beta (KPNB1) TTHOJ5F UP Q14974 TTHOJ5F UC IMB1_HUMAN TTHOJ5F BC Eukaryotic nuclear pore complex TTHOJ5F SN Pore targeting complex 97 kDa subunit; PTAC97; Nuclear factor p97; NTF97; Karyopherin subunit beta1; Karyopherin subunit beta-1; Importin90; Importin-90; Importin subunit beta1; Importin subunit beta-1 TTHOJ5F GN KPNB1 TTHOJ5F FC Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports SNAI1 and PRKCI into the nucleus. Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. TTHOJ5F PD 6N89; 6N88; 3W5K; 3LWW; 2QNA TTHOJ5F SQ MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDPSVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKNYAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDIALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA TTHOJ5F TT Literature-reported TTXAUJ8 ID TTXAUJ8 TTXAUJ8 TN Influenza M messenger RNA (Influenza M mRNA) TTXAUJ8 UP O70632 TTXAUJ8 UC M2_I97A1 TTXAUJ8 BC mRNA target TTXAUJ8 SN Proton channel protein M2 (mRNA); Matrix protein 2 (mRNA); M (mRNA) TTXAUJ8 GN Influenza M mRNA TTXAUJ8 FC After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. TTXAUJ8 PD 6MPN; 6MPM; 6MPL; 4RWC; 4RWB TTXAUJ8 SQ MSLLTEVETLTRNGWGCRCSDSSDPLVVAASIIGILHLILWILDRLFFKCIYRRFKYGLKRGPSTEGVPESMREEYRQEQQNAVDVDDGHFVNIELE TTXAUJ8 TT Literature-reported TTXAUJ8 FM mRNA target TTM27B5 ID TTM27B5 TTM27B5 TN Influenza NA messenger RNA (Influenza NA mRNA) TTM27B5 UP Q9W7Y7 TTM27B5 UC NRAM_I97A1 TTM27B5 BC mRNA target TTM27B5 SN Neuraminidase (mRNA); NA of influenza (mRNA) TTM27B5 GN Influenza NA mRNA TTM27B5 FC Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication. Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. TTM27B5 EC EC 3.2.1.18 TTM27B5 SQ MNPNQKIITIGSICMVVGIISLMLQIGNIISVWVSHIIQTWHPNQPEPCNQSINFYTEQAAASVTLAGNSSLCPISGWAIYSKDNSIRIGSKGDVFVIREPFISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPYRTLMSCPVGEAPSPYNSRFESVAWSASACHDGISWLTIGISGPDNGAVAVLKYNGIITDTIKSWRNNILRTQESECACVNGSCFTVMTDGPSNEQASYKIFKIEKGRVVKSVELNAPNYHYEECSCYPDAGEITCVCRDNWHGSNRPWVSFNQNLEYQIGYICSGVFGDSPRPNDGTGSCGPVSLNGAYGVKGFSFKYGNGVWIGRTKSTSSRSGFEMIWDPNGWTETDSSFSLKQDIIAITDWSGYSGSFIQHPELTGLNCMRPCFWVELIRGRPKEKTIWTSGSSISFCGVNSDTVGWSWPDGADLPFTIDK TTM27B5 TT Literature-reported TTM27B5 FM mRNA target TTW0PHM ID TTW0PHM TTW0PHM TN Inositol polyphosphate 1-phosphatase (INPP1) TTW0PHM UP P49441 TTW0PHM UC INPP_HUMAN TTW0PHM BC Phosphoric monoester hydrolase TTW0PHM SN IPPase; IPP TTW0PHM GN INPP1 TTW0PHM FC Removes the phosphate group at position 1 of the inositol ring from the polyphosphates inositol 1,4-bisphosphate and inositol 1,3,4-trisphophosphate. TTW0PHM EC EC 3.1.3.57 TTW0PHM SQ MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEVIKQNMENKFPGLEKNIFGEESNEFTNDWGEKITLRLCSTEEETAELLSKVLNGNKVASEALARVVHQDVAFTDPTLDSTEINVPQDILGIWVDPIDSTYQYIKGSADIKSNQGIFPCGLQCVTILIGVYDIQTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTNMHSLQLTISRRNGSETHTGNTGSEAAFSPSFSAVISTSEKETIKAALSRVCGDRIFGAAGAGYKSLCVVQGLVDIYIFSEDTTFKWDSCAAHAILRAMGGGIVDLKECLERNPETGLDLPQLVYHVENEGAAGVDRWANKGGLIAYRSRKRLETFLSLLVQNLAPAETHT TTW0PHM TT Literature-reported TTCJTWF ID TTCJTWF TTCJTWF TN Insulin-like growth factor-binding protein 1 (IGFBP1) TTCJTWF UP P08833 TTCJTWF UC IBP1_HUMAN TTCJTWF BC Insulin-like growth factor binding TTCJTWF SN Placental protein 12; PP12; KITLG; IGFBP-1; IGF-binding protein 1; IBP1; IBP-1 TTCJTWF GN IGFBP1 TTCJTWF FC IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes cell migration. TTCJTWF PD 2DSQ; 1ZT5; 1ZT3 TTCJTWF SQ MSEVPVARVWLVLLLLTVQVGVTAGAPWQCAPCSAEKLALCPPVSASCSEVTRSAGCGCCPMCALPLGAACGVATARCARGLSCRALPGEQQPLHALTRGQGACVQESDASAPHAAEAGSPESPESTEITEEELLDNFHLMAPSEEDHSILWDAISTYDGSKALHVTNIKKWKEPCRIELYRVVESLAKAQETSGEEISKFYLPNCNKNGFYHSRQCETSMDGEAGLCWCVYPWNGKRIPGSPEIRGDPNCQIYFNVQN TTCJTWF TT Literature-reported TTCJTWF FM Insulin-like growth factor binding TT8FDB0 ID TT8FDB0 TT8FDB0 TN Insulin-like growth factor-binding protein 2 (IGFBP2) TT8FDB0 UP P18065 TT8FDB0 UC IBP2_HUMAN TT8FDB0 BC Insulin-like growth factor binding TT8FDB0 SN IGFBP-2; IGF-binding protein 2; IBP2; IBP-2; BP2 TT8FDB0 GN IGFBP2 TT8FDB0 FC Inhibits IGF-mediated growth and developmental rates. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. TT8FDB0 PD 2H7T TT8FDB0 SQ MLPRVGCPALPLPPPPLLPLLLLLLGASGGGGGARAEVLFRCPPCTPERLAACGPPPVAPPAAVAAVAGGARMPCAELVREPGCGCCSVCARLEGEACGVYTPRCGQGLRCYPHPGSELPLQALVMGEGTCEKRRDAEYGASPEQVADNGDDHSEGGLVENHVDSTMNMLGGGGSAGRKPLKSGMKELAVFREKVTEQHRQMGKGGKHHLGLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDERGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKLIQGAPTIRGDPECHLFYNEQQEARGVHTQRMQ TT8FDB0 TT Literature-reported TT8FDB0 FM Insulin-like growth factor binding TTLAYV8 ID TTLAYV8 TTLAYV8 TN Insulin-like growth factor-binding protein 6 (IGFBP6) TTLAYV8 UP P24592 TTLAYV8 UC IBP6_HUMAN TTLAYV8 BC Insulin-like growth factor binding TTLAYV8 SN IGFBP-6; IGF-binding protein 6; IBP6; IBP-6 TTLAYV8 GN IGFBP6 TTLAYV8 FC IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. TTLAYV8 PD 1RMJ TTLAYV8 SQ MTPHRLLPPLLLLLALLLAASPGGALARCPGCGQGVQAGCPGGCVEEEDGGSPAEGCAEAEGCLRREGQECGVYTPNCAPGLQCHPPKDDEAPLRALLLGRGRCLPARAPAVAEENPKESKPQAGTARPQDVNRRDQQRNPGTSTTPSQPNSAGVQDTEMGPCRRHLDSVLQQLQTEVYRGAQTLYVPNCDHRGFYRKRQCRSSQGQRRGPCWCVDRMGKSLPGSPDGNGSSSCPTGSSG TTLAYV8 TT Literature-reported TTB69FJ ID TTB69FJ TTB69FJ TN Integrin alpha-M (ITGAM) TTB69FJ UP P11215 TTB69FJ UC ITAM_HUMAN TTB69FJ BC Integrin TTB69FJ SN Neutrophil adherence receptor; Leukocyte adhesion receptor MO1; Cell surface glycoprotein Mac-1; Cell surface glycoprotein MAC-1 subunit alpha; Cell surface glycoprotein MAC-1 alpha subunit; CR3A; CR-3 alpha chain; CD11b; CD11 antigen-like family member B TTB69FJ GN ITGAM TTB69FJ FC It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin ITGAM/ITGB2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain. Regulates neutrophil migration. In association with beta subunit ITGB2/CD18, required for CD177-PRTN3-mediated activation of TNF primed neutrophils. May regulate phagocytosis-induced apoptosis in extravasated neutrophils. May play a role in mast cell development. Required with TYROBP/DAP12 in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development. Integrin ITGAM/ITGB2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles and pathogens. TTB69FJ PD 4XW2; 4M76; 3QA3; 3Q3G; 2LKJ TTB69FJ SQ MALRVLLLTALTLCHGFNLDTENAMTFQENARGFGQSVVQLQGSRVVVGAPQEIVAANQRGSLYQCDYSTGSCEPIRLQVPVEAVNMSLGLSLAATTSPPQLLACGPTVHQTCSENTYVKGLCFLFGSNLRQQPQKFPEALRGCPQEDSDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHTATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASKPPRDHVFQVNNFEALKTIQNQLREKIFAIEGTQTGSSSSFEHEMSQEGFSAAITSNGPLLSTVGSYDWAGGVFLYTSKEKSTFINMTRVDSDMNDAYLGYAAAIILRNRVQSLVLGAPRYQHIGLVAMFRQNTGMWESNANVKGTQIGAYFGASLCSVDVDSNGSTDLVLIGAPHYYEQTRGGQVSVCPLPRGRARWQCDAVLYGEQGQPWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNRGAVYLFHGTSGSGISPSHSQRIAGSKLSPRLQYFGQSLSGGQDLTMDGLVDLTVGAQGHVLLLRSQPVLRVKAIMEFNPREVARNVFECNDQVVKGKEAGEVRVCLHVQKSTRDRLREGQIQSVVTYDLALDSGRPHSRAVFNETKNSTRRQTQVLGLTQTCETLKLQLPNCIEDPVSPIVLRLNFSLVGTPLSAFGNLRPVLAEDAQRLFTALFPFEKNCGNDNICQDDLSITFSFMSLDCLVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLDLSYRKVSTLQNQRSQRSWRLACESASSTEVSGALKSTSCSINHPIFPENSEVTFNITFDVDSKASLGNKLLLKANVTSENNMPRTNKTEFQLELPVKYAVYMVVTSHGVSTKYLNFTASENTSRVMQHQYQVSNLGQRSLPISLVFLVPVRLNQTVIWDRPQVTFSENLSSTCHTKERLPSHSDFLAELRKAPVVNCSIAVCQRIQCDIPFFGIQEEFNATLKGNLSFDWYIKTSHNHLLIVSTAEILFNDSVFTLLPGQGAFVRSQTETKVEPFEVPNPLPLIVGSSVGGLLLLALITAALYKLGFFKRQYKDMMSEGGPPGAEPQ TTB69FJ TT Clinical trial TT8NBXR ID TT8NBXR TT8NBXR TN Integrin beta-3 (ITGB3) TT8NBXR UP P05106 TT8NBXR UC ITB3_HUMAN TT8NBXR BC Integrin TT8NBXR SN GPIIIa; GP3A; CD61 TT8NBXR GN ITGB3 TT8NBXR FC Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. Fibrinogen binding enhances SELP expression in activated platelets. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling. ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling. ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling. ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling. ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. TT8NBXR PD 6CKB; 6BXJ; 6BXF; 6BXB; 6AVU TT8NBXR SQ MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT TT8NBXR TT Literature-reported TT8NBXR FM Integrin TTIF29E ID TTIF29E TTIF29E TN Integrin beta-8 (ITGB8) TTIF29E UP P26012 TTIF29E UC ITB8_HUMAN TTIF29E BC Integrin TTIF29E SN Integrin subunit beta 8 TTIF29E GN ITGB8 TTIF29E FC It recognizes the sequence R-G-D in its ligands. Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation on the surface of activated regulatory T-cells (Tregs). Required during vasculogenesis. Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for fibronectin. TTIF29E PD 6DJP TTIF29E SQ MCGSALAFFTAAFVCLQNDRRGPASFLWAAWVFSLVLGLGQGEDNRCASSNAASCARCLALGPECGWCVQEDFISGGSRSERCDIVSNLISKGCSVDSIEYPSVHVIIPTENEINTQVTPGEVSIQLRPGAEANFMLKVHPLKKYPVDLYYLVDVSASMHNNIEKLNSVGNDLSRKMAFFSRDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTMEHPSLGQLSEKLIDNNINVIFAVQGKQFHWYKDLLPLLPGTIAGEIESKAANLNNLVVEAYQKLISEVKVQVENQVQGIYFNITAICPDGSRKPGMEGCRNVTSNDEVLFNVTVTMKKCDVTGGKNYAIIKPIGFNETAKIHIHRNCSCQCEDNRGPKGKCVDETFLDSKCFQCDENKCHFDEDQFSSESCKSHKDQPVCSGRGVCVCGKCSCHKIKLGKVYGKYCEKDDFSCPYHHGNLCAGHGECEAGRCQCFSGWEGDRCQCPSAAAQHCVNSKGQVCSGRGTCVCGRCECTDPRSIGRFCEHCPTCYTACKENWNCMQCLHPHNLSQAILDQCKTSCALMEQQHYVDQTSECFSSPSYLRIFFIIFIVTFLIGLLKVLIIRQVILQWNSNKIKSSSDYRVSASKKDKLILQSVCTRAVTYRREKPEEIKMDISKLNAHETFRCNF TTIF29E TT Patented-recorded TTIF29E FM Integrin TTYR7OH ID TTYR7OH TTYR7OH TN Interferon regulatory factor 3 (IRF3) TTYR7OH UP Q14653 TTYR7OH UC IRF3_HUMAN TTYR7OH SN IRF-3 TTYR7OH GN IRF3 TTYR7OH FC Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages. Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. TTYR7OH PD 5JER; 5JEO; 5JEM; 5JEL; 5JEK TTYR7OH SQ MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTLPDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGHGPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPGES TTYR7OH TT Literature-reported TTYR7OH KE hsa04620:Toll-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa05133:Pertussis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05203:Viral carcinogenesis TTYR7OH RC R-HSA-1169408:ISG15 antiviral mechanism; R-HSA-3134973:LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production; R-HSA-877300:Interferon gamma signaling; R-HSA-909733:Interferon alpha/beta signaling; R-HSA-918233:TRAF3-dependent IRF activation pathway; R-HSA-933541:TRAF6 mediated IRF7 activation; R-HSA-936440:Negative regulators of RIG-I/MDA5 signaling; R-HSA-936964:Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TTRF4Q2 ID TTRF4Q2 TTRF4Q2 TN Interferon-lambda 3 (IFNL3) TTRF4Q2 UP Q8IZI9 TTRF4Q2 UC IFNL3_HUMAN TTRF4Q2 BC Cytokine: interferon TTRF4Q2 SN ZCYTO22; Interleukin28C; Interleukin28B; Interleukin-28C; Interleukin-28B; Interferon lambda3; Interferon lambda-3; IL28C; IL28B; IL-28C; IL-28B; IFNlambda3; IFN-lambda-3; Cytokine Zcyto22 TTRF4Q2 GN IFNL3 TTRF4Q2 FC Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression. Cytokine with antiviral, antitumour and immunomodulatory activities. TTRF4Q2 PD 5T5W; 3HHC TTRF4Q2 SQ MTGDCMPVLVLMAAVLTVTGAVPVARLRGALPDARGCHIAQFKSLSPQELQAFKRAKDALEESLLLKDCKCRSRLFPRTWDLRQLQVRERPVALEAELALTLKVLEATADTDPALGDVLDQPLHTLHHILSQLRACIQPQPTAGPRTRGRLHHWLHRLQEAPKKESPGCLEASVTFNLFRLLTRDLNCVASGDLCV TTRF4Q2 TT Literature-reported TTWS50K ID TTWS50K TTWS50K TN Interleukin 1 receptor accessory protein (IL1RAP) TTWS50K UP Q9NPH3 TTWS50K UC IL1AP_HUMAN TTWS50K BC Cytokine receptor TTWS50K SN Interleukin1 receptor 3; Interleukin-1 receptor accessory protein; Interleukin-1 receptor 3; IL1RAcP; IL1R3; IL1 receptor accessory protein; IL-1RAcP; IL-1R3; IL-1R-3; IL-1 receptor accessory protein; C3orf13 TTWS50K GN IL1RAP TTWS50K FC Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Coreceptor for IL1RL1 in the IL-33 signaling system. Can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD. May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells. Coreceptor for IL1RL2 in the IL-36 signaling system. TTWS50K PD 4DEP; 3O4O TTWS50K SQ MTLLWCVVSLYFYGILQSDASERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKFNYSTAHSAGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSPMKLPVHKLYIEYGIQRITCPNVDGYFPSSVKPTITWYMGCYKIQNFNNVIPEGMNLSFLIALISNNGNYTCVVTYPENGRTFHLTRTLTVKVVGSPKNAVPPVIHSPNDHVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDITIDVTINESISHSRTEDETRTQILSIKKVTSEDLKRSYVCHARSAKGEVAKAAKVKQKVPAPRYTVELACGFGATVLLVVILIVVYHVYWLEMVLFYRAHFGTDETILDGKEYDIYVSYARNAEEEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGIVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLENMASRGNINVILVQYKAVKETKVKELKRAKTVLTVIKWKGEKSKYPQGRFWKQLQVAMPVKKSPRRSSSDEQGLSYSSLKNV TTWS50K TT Clinical trial TTWS50K FM Interleukin receptor family TTNEAMG ID TTNEAMG TTNEAMG TN Interleukin 13 receptor alpha-1 (IL13RA1) TTNEAMG UP P78552 TTNEAMG UC I13R1_HUMAN TTNEAMG BC Cytokine receptor TTNEAMG SN Interleukin-13 receptor subunit alpha-1; IL13RA; IL13R; IL-13RA1; IL-13RA-1; IL-13R-alpha-1; IL-13R subunit alpha-1; IL-13R alpha-1 chain; IL-13 receptor subunit alpha-1; Cancer/testis antigen 19; CT19; CD213a1 antigen; CD213a1 TTNEAMG GN IL13RA1 TTNEAMG FC Together with IL4RA can form a functional receptor for IL13. Also serves as an alternate accessory protein to the common cytokine receptor gamma chain for interleukin-4 (IL4) signaling, but cannot replace the function of IL2RG in allowing enhanced interleukin-2 (IL2) binding activity. Binds with low affinity to interleukin-13 (IL13). TTNEAMG PD 5E4E; 4HWB; 3BPO; 3BPN TTNEAMG SQ MEWPARLCGLWALLLCAGGGGGGGGAAPTETQPPVTNLSVSVENLCTVIWTWNPPEGASSNCSLWYFSHFGDKQDKKIAPETRRSIEVPLNERICLQVGSQCSTNESEKPSILVEKCISPPEGDPESAVTELQCIWHNLSYMKCSWLPGRNTSPDTNYTLYYWHRSLEKIHQCENIFREGQYFGCSFDLTKVKDSSFEQHSVQIMVKDNAGKIKPSFNIVPLTSRVKPDPPHIKNLSFHNDDLYVQWENPQNFISRCLFYEVEVNNSQTETHNVFYVQEAKCENPEFERNVENTSCFMVPGVLPDTLNTVRIRVKTNKLCYEDDKLWSNWSQEMSIGKKRNSTLYITMLLIVPVIVAGAIIVLLLYLKRLKIIIFPPIPDPGKIFKEMFGDQNDDTLHWKKYDIYEKQTKEETDSVVLIENLKKASQ TTNEAMG TT Literature-reported TTNEAMG FM Cytokine receptor TTZUJVE ID TTZUJVE TTZUJVE TN Interleukin 18 receptor (IL18RAP) TTZUJVE UP O95256 TTZUJVE UC I18RA_HUMAN TTZUJVE BC Cytokine receptor TTZUJVE SN Interleukin18 receptor beta; Interleukin18 receptor accessory proteinlike; Interleukin18 receptor accessory protein; Interleukin1 receptor 7; Interleukin-18 receptor beta; Interleukin-18 receptor accessory protein-like; Interleukin-18 receptor accessory protein; Interleukin-1 receptor 7; IL1RAcPL; IL1R7; IL1R accessory proteinlike; IL18Rbeta; IL18RAcP; IL18 receptor accessory protein; IL-1RAcPL; IL-1R7; IL-1R-7; IL-1R accessory protein-like; IL-18Rbeta; IL-18RAcP; IL-18R-beta; IL-18 receptor accessory protein; CDw218b; CD218b; CD218 antigenlike family member B; CD218 antigen-like family member B; Accessory proteinlike; Accessory protein-like; AcPL TTZUJVE GN IL18RAP TTZUJVE FC May play a role in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells. Within the IL18 receptor complex, does not mediate IL18-binding, but involved in IL18-dependent signal transduction, leading to NF-kappa-B and JNK activation. TTZUJVE PD 3WO4 TTZUJVE SQ MLCLGWIFLWLVAGERIKGFNISGCSTKKLLWTYSTRSEEEFVLFCDLPEPQKSHFCHRNRLSPKQVPEHLPFMGSNDLSDVQWYQQPSNGDPLEDIRKSYPHIIQDKCTLHFLTPGVNNSGSYICRPKMIKSPYDVACCVKMILEVKPQTNASCEYSASHKQDLLLGSTGSISCPSLSCQSDAQSPAVTWYKNGKLLSVERSNRIVVDEVYDYHQGTYVCDYTQSDTVSSWTVRAVVQVRTIVGDTKLKPDILDPVEDTLEVELGKPLTISCKARFGFERVFNPVIKWYIKDSDLEWEVSVPEAKSIKSTLKDEIIERNIILEKVTQRDLRRKFVCFVQNSIGNTTQSVQLKEKRGVVLLYILLGTIGTLVAVLAASALLYRHWIEIVLLYRTYQSKDQTLGDKKDFDAFVSYAKWSSFPSEATSSLSEEHLALSLFPDVLENKYGYSLCLLERDVAPGGVYAEDIVSIIKRSRRGIFILSPNYVNGPSIFELQAAVNLALDDQTLKLILIKFCYFQEPESLPHLVKKALRVLPTVTWRGLKSVPPNSRFWAKMRYHMPVKNSQGFTWNQLRITSRIFQWKGLSRTETTGRSSQPKEW TTZUJVE TT Literature-reported TTW4R0B ID TTW4R0B TTW4R0B TN Interleukin-16 (IL16) TTW4R0B UP Q14005 TTW4R0B UC IL16_HUMAN TTW4R0B BC Cytokine: interleukin TTW4R0B SN Prointerleukin16; Pro-interleukin-16; LCF; Interleukin16 TTW4R0B GN IL16 TTW4R0B FC Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4. Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. TTW4R0B PD 5FB8; 1X6D; 1I16 TTW4R0B SQ MESHSRAGKSRKSAKFRSISRSLMLCNAKTSDDGSSPDEKYPDPFEISLAQGKEGIFHSSVQLADTSEAGPSSVPDLALASEAAQLQAAGNDRGKTCRRIFFMKESSTASSREKPGKLEAQSSNFLFPKACHQRARSNSTSVNPYCTREIDFPMTKKSAAPTDRQPYSLCSNRKSLSQQLDCPAGKAAGTSRPTRSLSTAQLVQPSGGLQASVISNIVLMKGQAKGLGFSIVGGKDSIYGPIGIYVKTIFAGGAAAADGRLQEGDEILELNGESMAGLTHQDALQKFKQAKKGLLTLTVRTRLTAPPSLCSHLSPPLCRSLSSSTCITKDSSSFALESPSAPISTAKPNYRIMVEVSLQKEAGVGLGIGLCSVPYFQCISGIFVHTLSPGSVAHLDGRLRCGDEIVEISDSPVHCLTLNEVYTILSHCDPGPVPIIVSRHPDPQVSEQQLKEAVAQAVENTKFGKERHQWSLEGVKRLESSWHGRPTLEKEREKNSAPPHRRAQKVMIRSSSDSSYMSGSPGGSPGSGSAEKPSSDVDISTHSPSLPLAREPVVLSIASSRLPQESPPLPESRDSHPPLRLKKSFEILVRKPMSSKPKPPPRKYFKSDSDPQKSLEERENSSCSSGHTPPTCGQEARELLPLLLPQEDTAGRSPSASAGCPGPGIGPQTKSSTEGEPGWRRASPVTQTSPIKHPLLKRQARMDYSFDTTAEDPWVRISDCIKNLFSPIMSENHGHMPLQPNASLNEEEGTQGHPDGTPPKLDTANGTPKVYKSADSSTVKKGPPVAPKPAWFRQSLKGLRNRASDPRGLPDPALSTQPAPASREHLGSHIRASSSSSSIRQRISSFETFGSSQLPDKGAQRLSLQPSSGEAAKPLGKHEEGRFSGLLGRGAAPTLVPQQPEQVLSSGSPAASEARDPGVSESPPPGRQPNQKTLPPGPDPLLRLLSTQAEESQGPVLKMPSQRARSFPLTRSQSCETKLLDEKTSKLYSISSQVSSAVMKSLLCLPSSISCAQTPCIPKEGASPTSSSNEDSAANGSAETSALDTGFSLNLSELREYTEGLTEAKEDDDGDHSSLQSGQSVISLLSSEELKKLIEEVKVLDEATLKQLDGIHVTILHKEEGAGLGFSLAGGADLENKVITVHRVFPNGLASQEGTIQKGNEVLSINGKSLKGTTHHDALAILRQAREPRQAVIVTRKLTPEAMPDLNSSTDSAASASAASDVSVESTAEATVCTVTLEKMSAGLGFSLEGGKGSLHGDKPLTINRIFKGAASEQSETVQPGDEILQLGGTAMQGLTRFEAWNIIKALPDGPVTIVIRRKSLQSKETTAAGDS TTW4R0B TT Literature-reported TT87RWS ID TT87RWS TT87RWS TN Interleukin-19 (IL19) TT87RWS UP Q9UHD0 TT87RWS UC IL19_HUMAN TT87RWS BC Cytokine: interleukin TT87RWS SN ZMDA1; NG.1; Melanoma differentiation-associated protein-like protein; IL-19 TT87RWS GN IL19 TT87RWS FC Up-regulates IL-6 and TNF-alpha and induces apoptosis. May play some important roles in inflammatory responses. TT87RWS PD 1N1F TT87RWS SQ MKLQCVSLWLLGTILILCSVDNHGLRRCLISTDMHHIEESFQEIKRAIQAKDTFPNVTILSTLETLQIIKPLDVCCVTKNLLAFYVDRVFKDHQEPNPKILRKISSIANSFLYMQKTLRQCQEQRQCHCRQEATNATRVIHDNYDQLEVHAAAIKSLGELDVFLAWINKNHEVMFSA TT87RWS TT Literature-reported TTD4G7L ID TTD4G7L TTD4G7L TN Interleukin-32 (IL32) TTD4G7L UP P24001 TTD4G7L UC IL32_HUMAN TTD4G7L BC Cytokine: interleukin TTD4G7L SN Tumor necrosis factor alpha-inducing factor; TAIF; Natural killer cells protein 4; NK4; IL-32 TTD4G7L GN IL32 TTD4G7L FC It induces various cytokines such as TNFA/TNF-alpha and IL8. It activates typical cytokine signal pathways of NF-kappa-B and p38 MAPK. Cytokine that may play a role in innate and adaptive immune responses. TTD4G7L SQ MCFPKVLSDDMKKLKARMVMLLPTSAQGLGAWVSACDTEDTVGHLGPWRDKDPALWCQLCLSSQHQAIERFYDKMQNAESGRGQVMSSLAELEDDFKEGYLETVAAYYEEQHPELTPLLEKERDGLRCRGNRSPVPDVEDPATEEPGESFCDKVMRWFQAMLQRLQTWWHGVLAWVKEKVVALVHAVQALWKQFQSFCCSLSELFMSSFQSYGAPRGDKEELTPQKCSEPQSSK TTD4G7L TT Literature-reported TTD4G7L KE hsa04060:Cytokine-cytokine receptor interaction TTP4ICS ID TTP4ICS TTP4ICS TN Intestinal GlcNAc-6-sulfotransferase (CHST5) TTP4ICS UP Q9GZS9 TTP4ICS UC CHST5_HUMAN TTP4ICS BC Transferases of sulfur-containing groups TTP4ICS SN N-acetylglucosamine-6-O-sulfotransferase; N-acetylglucosamine 6-O-sulfotransferase; LSST; L-selectin ligand sulfotransferase GST-3; L-selectin ligand sulfotransferase; Intestinal N-acetylglucosamine-6-O-sulfotransferase; High endothelial cell GlcNAc 6-O-sulfotransferase; HEC-GlcNAc6ST; GlcNAc 6-O-sulfotransferase; Carbohydrate sulfotransferase GST-3; CHST5 TTP4ICS GN CHST5 TTP4ICS FC Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues and O-linked sugars of mucin-type acceptors. Acts on the non-reducing terminal GlcNAc of short carbohydrate substrates. However, it does not transfer sulfate to longer carbohydrate substrates that have poly-N-acetyllactosamine structures. Has no activitytoward keratan. Not involved in generating HEV-expressed ligands for SELL. Its substrate specificity may be influenced by its subcellular location. TTP4ICS EC EC 2.8.2.- TTP4ICS SQ MGMRARVPKVAHSTRRPPAARMWLPRFSSKTVTVLLLAQTTCLLLFIISRPGPSSPAGGEDRVHVLVLSSWRSGSSFLGQLFSQHPDVFYLMEPAWHVWTTLSQGSAATLHMAVRDLMRSIFLCDMDVFDAYMPQSRNLSAFFNWATSRALCSPPACSAFPRGTISKQDVCKTLCTRQPFSLAREACRSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREAAGPILARDNGIVLGTNGKWVEADPHLRLIREVCRSHVRIAEAATLKPPPFLRGRYRLVRFEDLAREPLAEIRALYAFTGLTLTPQLEAWIHNITHGSGIGKPIEAFHTSSRNARNVSQAWRHALPFTKILRVQEVCAGALQLLGYRPVYSADQQRDLTLDLVLPRGPDHFSWASPD TTP4ICS TT Literature-reported TT9YLCR ID TT9YLCR TT9YLCR TN Intrinsic factor-B12 receptor (CUBN) TT9YLCR UP O60494 TT9YLCR UC CUBN_HUMAN TT9YLCR BC Growth factor TT9YLCR SN Intrinsic factor-vitamin B12 receptor; Cubilin; CUBN TT9YLCR GN CUBN TT9YLCR FC Cotransporter which plays a role in lipoprotein, vitamin and iron metabolism, by facilitating their uptake. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the GIF-cobalamin complex. The binding of all ligands requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. Interaction with LRP2 mediates its trafficking throughout vesicles and facilitates the uptake of specific ligands like GC, hemoglobin, ALB, TF and SCGB1A1. Interaction with AMN controls its trafficking to the plasma membrane and facilitates endocytosis of ligands. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface. TT9YLCR PD 6GJE; 3KQ4 TT9YLCR SQ MMNMSLPFLWSLLTLLIFAEVNGEAGELELQRQKRSINLQQPRMATERGNLVFLTGSAQNIEFRTGSLGKIKLNDEDLSECLHQIQKNKEDIIELKGSAIGLPQNISSQIYQLNSKLVDLERKFQGLQQTVDKKVCSSNPCQNGGTCLNLHDSFFCICPPQWKGPLCSADVNECEIYSGTPLSCQNGGTCVNTMGSYSCHCPPETYGPQCASKYDDCEGGSVARCVHGICEDLMREQAGEPKYSCVCDAGWMFSPNSPACTLDRDECSFQPGPCSTLVQCFNTQGSFYCGACPTGWQGNGYICEDINECEINNGGCSVAPPVECVNTPGSSHCQACPPGYQGDGRVCTLTDICSVSNGGCHPDASCSSTLGSLPLCTCLPGYTGNGYGPNGCVQLSNICLSHPCLNGQCIDTVSGYFCKCDSGWTGVNCTENINECLSNPCLNGGTCVDGVDSFSCECTRLWTGALCQVPQQVCGESLSGINGSFSYRSPDVGYVHDVNCFWVIKTEMGKVLRITFTFFRLESMDNCPHEFLQVYDGDSSSAFQLGRFCGSSLPHELLSSDNALYFHLYSEHLRNGRGFTVRWETQQPECGGILTGPYGSIKSPGYPGNYPPGRDCVWIVVTSPDLLVTFTFGTLSLEHHDDCNKDYLEIRDGPLYQDPLLGKFCTTFSVPPLQTTGPFARIHFHSDSQISDQGFHITYLTSPSDLRCGGNYTDPEGELFLPELSGPFTHTRQCVYMMKQPQGEQIQINFTHVELQCQSDSSQNYIEVRDGETLLGKVCGNGTISHIKSITNSVWIRFKIDASVEKASFRAVYQVACGDELTGEGVIRSPFFPNVYPGERTCRWTIHQPQSQVILLNFTVFEIGSSAHCETDYVEIGSSSILGSPENKKYCGTDIPSFITSVYNFLYVTFVKSSSTENHGFMAKFSAEDLACGEILTESTGTIQSPGHPNVYPHGINCTWHILVQPNHLIHLMFETFHLEFHYNCTNDYLEVYDTDSETSLGRYCGKSIPPSLTSSGNSLMLVFVTDSDLAYEGFLINYEAISAATACLQDYTDDLGTFTSPNFPNNYPNNWECIYRITVRTGQLIAVHFTNFSLEEAIGNYYTDFLEIRDGGYEKSPLLGIFYGSNLPPTIISHSNKLWLKFKSDQIDTRSGFSAYWDGSSTGCGGNLTTSSGTFISPNYPMPYYHSSECYWWLKSSHGSAFELEFKDFHLEHHPNCTLDYLAVYDGPSSNSHLLTQLCGDEKPPLIRSSGDSMFIKLRTDEGQQGRGFKAEYRQTCENVVIVNQTYGILESIGYPNPYSENQHCNWTIRATTGNTVNYTFLAFDLEHHINCSTDYLELYDGPRQMGRYCGVDLPPPGSTTSSKLQVLLLTDGVGRREKGFQMQWFVYGCGGELSGATGSFSSPGFPNRYPPNKECIWYIRTDPGSSIQLTIHDFDVEYHSRCNFDVLEIYGGPDFHSPRIAQLCTQRSPENPMQVSSTGNELAIRFKTDLSINGRGFNASWQAVTGGCGGIFQAPSGEIHSPNYPSPYRSNTDCSWVIRVDRNHRVLLNFTDFDLEPQDSCIMAYDGLSSTMSRLARTCGREQLANPIVSSGNSLFLRFQSGPSRQNRGFRAQFRQACGGHILTSSFDTVSSPRFPANYPNNQNCSWIIQAQPPLNHITLSFTHFELERSTTCARDFVEILDGGHEDAPLRGRYCGTDMPHPITSFSSALTLRFVSDSSISAGGFHTTVTASVSACGGTFYMAEGIFNSPGYPDIYPPNVECVWNIVSSPGNRLQLSFISFQLEDSQDCSRDFVEIREGNATGHLVGRYCGNSFPLNYSSIVGHTLWVRFISDGSGSGTGFQATFMKIFGNDNIVGTHGKVASPFWPENYPHNSNYQWTVNVNASHVVHGRILEMDIEEIQNCYYDKLRIYDGPSIHARLIGAYCGTQTESFSSTGNSLTFHFYSDSSISGKGFLLEWFAVDAPDGVLPTIAPGACGGFLRTGDAPVFLFSPGWPDSYSNRVDCTWLIQAPDSTVELNILSLDIESHRTCAYDSLVIRDGDNNLAQQLAVLCGREIPGPIRSTGEYMFIRFTSDSSVTRAGFNASFHKSCGGYLHADRGIITSPKYPETYPSNLNCSWHVLVQSGLTIAVHFEQPFQIPNGDSSCNQGDYLVLRNGPDICSPPLGPPGGNGHFCGSHASSTLFTSDNQMFVQFISDHSNEGQGFKIKYEAKSLACGGNVYIHDADSAGYVTSPNHPHNYPPHADCIWILAAPPETRIQLQFEDRFDIEVTPNCTSNYLELRDGVDSDAPILSKFCGTSLPSSQWSSGEVMYLRFRSDNSPTHVGFKAKYSIAQCGGRVPGQSGVVESIGHPTLPYRDNLFCEWHLQGLSGHYLTISFEDFNLQNSSGCEKDFVEIWDNHTSGNILGRYCGNTIPDSIDTSSNTAVVRFVTDGSVTASGFRLRFESSMEECGGDLQGSIGTFTSPNYPNPNPHGRICEWRITAPEGRRITLMFNNLRLATHPSCNNEHVIVFNGIRSNSPQLEKLCSSVNVSNEIKSSGNTMKVIFFTDGSRPYGGFTASYTSSEDAVCGGSLPNTPEGNFTSPGYDGVRNYSRNLNCEWTLSNPNQGNSSISIHFEDFYLESHQDCQFDVLEFRVGDADGPLMWRLCGPSKPTLPLVIPYSQVWIHFVTNERVEHIGFHAKYSFTDCGGIQIGDSGVITSPNYPNAYDSLTHCSSLLEAPQGHTITLTFSDFDIEPHTTCAWDSVTVRNGGSPESPIIGQYCGNSNPRTIQSGSNQLVVTFNSDHSLQGGGFYATWNTQTLGCGGIFHSDNGTIRSPHWPQNFPENSRCSWTAITHKSKHLEISFDNNFLIPSGDGQCQNSFVKVWAGTEEVDKALLATGCGNVAPGPVITPSNTFTAVFQSQEAPAQGFSASFVSRCGSNFTGPSGYIISPNYPKQYDNNMNCTYVIEANPLSVVLLTFVSFHLEARSAVTGSCVNDGVHIIRGYSVMSTPFATVCGDEMPAPLTIAGPVLLNFYSNEQITDFGFKFSYRIISCGGVFNFSSGIITSPAYSYADYPNDMHCLYTITVSDDKVIELKFSDFDVVPSTSCSHDYLAIYDGANTSDPLLGKFCGSKRPPNVKSSNNSMLLVFKTDSFQTAKGWKMSFRQTLGPQQGCGGYLTGSNNTFASPDSDSNGMYDKNLNCVWIIIAPVNKVIHLTFNTFALEAASTRQRCLYDYVKLYDGDSENANLAGTFCGSTVPAPFISSGNFLTVQFISDLTLEREGFNATYTIMDMPCGGTYNATWTPQNISSPNSSDPDVPFSICTWVIDSPPHQQVKITVWALQLTSQDCTQNYLQLQDSPQGHGNSRFQFCGRNASAVPVFYSSMSTAMVIFKSGVVNRNSRMSFTYQIADCNRDYHKAFGNLRSPGWPDNYDNDKDCTVTLTAPQNHTISLFFHSLGIENSVECRNDFLEVRNGSNSNSPLLGKYCGTLLPNPVFSQNNELYLRFKSDSVTSDRGYEIIWTSSPSGCGGTLYGDRGSFTSPGYPGTYPNNTYCEWVLVAPAGRLVTINFYFISIDDPGDCVQNYLTLYDGPNASSPSSGPYCGGDTSIAPFVASSNQVFIKFHADYARRPSAFRLTWDS TT9YLCR TT Literature-reported TTXF0ZW ID TTXF0ZW TTXF0ZW TN Inward rectifier potassium channel Kir2.3 (KCNJ4) TTXF0ZW UP P48050 TTXF0ZW UC KCNJ4_HUMAN TTXF0ZW BC Inward rectifier potassium channel TTXF0ZW SN Potassium channel, inwardly rectifying subfamily J member 4; Inward rectifier potassium channel 4; Inward rectifier K(+) channel Kir2.3; IRK3; IRK-3; Hippocampal inward rectifier; HRK1; HIRK2; HIR TTXF0ZW GN KCNJ4 TTXF0ZW FC Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). TTXF0ZW PD 3GJ9 TTXF0ZW SQ MHGHSRNGQAHVPRRKRRNRFVKKNGQCNVYFANLSNKSQRYMADIFTTCVDTRWRYMLMIFSAAFLVSWLFFGLLFWCIAFFHGDLEASPGVPAAGGPAAGGGGAAPVAPKPCIMHVNGFLGAFLFSVETQTTIGYGFRCVTEECPLAVIAVVVQSIVGCVIDSFMIGTIMAKMARPKKRAQTLLFSHHAVISVRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPYMTQEGEYLPLDQRDLNVGYDIGLDRIFLVSPIIIVHEIDEDSPLYGMGKEELESEDFEIVVILEGMVEATAMTTQARSSYLASEILWGHRFEPVVFEEKSHYKVDYSRFHKTYEVAGTPCCSARELQESKITVLPAPPPPPSAFCYENELALMSQEEEEMEEEAAAAAAVAAGLGLEAGSKEEAGIIRMLEFGSHLDLERMQASLPLDNISYRRESAI TTXF0ZW TT Literature-reported TTGM19J ID TTGM19J TTGM19J TN Inward rectifier potassium channel Kir3.1 (KCNJ3) TTGM19J UP P48549 TTGM19J UC KCNJ3_HUMAN TTGM19J BC Inward rectifier potassium channel TTGM19J SN Potassium channel, inwardly rectifying subfamily J member 3; KCNJ3; Inward rectifier K(+) channel Kir3.1; GIRK1; G proteinactivated inward rectifier potassium channel 1 TTGM19J GN KCNJ3 TTGM19J FC This potassium channel is controlled byG proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat. TTGM19J SQ MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQDPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQTEQFEIVVILEGIVETTGMTCQARTSYTEDEVLWGHRFFPVISLEEGFFKVDYSQFHATFEVPTPPYSVKEQEEMLLMSSPLIAPAITNSKERHNSVECLDGLDDITTKLPSKLQKITGREDFPKKLLRMSSTTSEKAYSLGDLPMKLQRISSVPGNSEEKLVSKTTKMLSDPMSQSVADLPPKLQKMAGGAARMEGNLPAKLRKMNSDRFT TTGM19J TT Literature-reported TTGM19J KE hsa04713:Circadian entrainment; hsa04723:Retrograde endocannabinoid signaling; hsa04724:Glutamatergic synapse; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04728:Dopaminergic synapse; hsa04915:Estrogen signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05032:Morphine addiction TTGM19J RC R-HSA-1296041:Activation of G protein gated Potassium channels; R-HSA-997272:Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits TTH1769 ID TTH1769 TTH1769 TN IP3 receptor isoform 3 (ITPR3) TTH1769 UP Q14573 TTH1769 UC ITPR3_HUMAN TTH1769 BC Ryanodine-inositol triphosphate calcium channel TTH1769 SN Type 3 inositol 1,4,5-trisphosphate receptor; Type 3 InsP3 receptor; InsP3R3; Inositol 1,4,5-trisphosphate receptor type 3; IP3R 3 TTH1769 GN ITPR3 TTH1769 FC Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. TTH1769 PD 6DRC; 6DRA; 6DR2; 6DR0; 6DQZ TTH1769 SQ MSEMSSFLHIGDIVSLYAEGSVNGFISTLGLVDDRCVVEPAAGDLDNPPKKFRDCLFKVCPMNRYSAQKQYWKAKQTKQDKEKIADVVLLQKLQHAAQMEQKQNDTENKKVHGDVVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTLDATGNEGSWLFIQPFWKLRSNGDNVVVGDKVILNPVNAGQPLHASNYELSDNAGCKEVNSVNCNTSWKINLFMQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLYRFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQGRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEIRDLDFANDASSMLASAVEKLNEGFISQNDRRFVIQLLEDLVFFVSDVPNNGQNVLDIMVTKPNRERQKLMREQNILKQVFGILKAPFREKGGEGPLVRLEELSDQKNAPYQHMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAEDTITALLHNNRKLLEKHITKTEVETFVSLVRKNREPRFLDYLSDLCVSNHIAIPVTQELICKCVLDPKNSDILIRTELRPVKEMAQSHEYLSIEYSEEEVWLTWTDKNNEHHEKSVRQLAQEARAGNAHDENVLSYYRYQLKLFARMCLDRQYLAIDEISQQLGVDLIFLCMADEMLPFDLRASFCHLMLHVHVDRDPQELVTPVKFARLWTEIPTAITIKDYDSNLNASRDDKKNKFANTMEFVEDYLNNVVSEAVPFANEEKNKLTFEVVSLAHNLIYFGFYSFSELLRLTRTLLGIIDCVQGPPAMLQAYEDPGGKNVRRSIQGVGHMMSTMVLSRKQSVFSAPSLSAGASAAEPLDRSKFEENEDIVVMETKLKILEILQFILNVRLDYRISYLLSVFKKEFVEVFPMQDSGADGTAPAFDSTTANMNLDRIGEQAEAMFGVGKTSSMLEVDDEGGRMFLRVLIHLTMHDYAPLVSGALQLLFKHFSQRQEAMHTFKQVQLLISAQDVENYKVIKSELDRLRTMVEKSELWVDKKGSGKGEEVEAGAAKDKKERPTDEEGFLHPPGEKSSENYQIVKGILERLNKMCGVGEQMRKKQQRLLKNMDAHKVMLDLLQIPYDKGDAKMMEILRYTHQFLQKFCAGNPGNQALLHKHLHLFLTPGLLEAETMQHIFLNNYQLCSEISEPVLQHFVHLLATHGRHVQYLDFLHTVIKAEGKYVKKCQDMIMTELTNAGDDVVVFYNDKASLAHLLDMMKAARDGVEDHSPLMYHISLVDLLAACAEGKNVYTEIKCTSLLPLEDVVSVVTHEDCITEVKMAYVNFVNHCYVDTEVEMKEIYTSNHIWTLFENFTLDMARVCSKREKRVADPTLEKYVLSVVLDTINAFFSSPFSENSTSLQTHQTIVVQLLQSTTRLLECPWLQQQHKGSVEACIRTLAMVAKGRAILLPMDLDAHISSMLSSGASCAAAAQRNASSYKATTRAFPRVTPTANQWDYKNIIEKLQDIITALEERLKPLVQAELSVLVDVLHWPELLFLEGSEAYQRCESGGFLSKLIQHTKDLMESEEKLCIKVLRTLQQMLLKKTKYGDRGNQLRKMLLQNYLQNRKSTSRGDLPDPIGTGLDPDWSAIAATQCRLDKEGATKLVCDLITSTKNEKIFQESIGLAIHLLDGGNTEIQKSFHNLMMSDKKSERFFKVLHDRMKRAQQETKSTVAVNMNDLGSQPHEDREPVDPTTKGRVASFSIPGSSSRYSLGPSLRRGHEVSERVQSSEMGTSVLIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDIMCGSTTGGLGLLGLYINEDNVGLVIQTLETLTEYCQGPCHENQTCIVTHESNGIDIITALILNDISPLCKYRMDLVLQLKDNASKLLLALMESRHDSENAERILISLRPQELVDVIKKAYLQEEERENSEVSPREVGHNIYILALQLSRHNKQLQHLLKPVKRIQEEEAEGISSMLSLNNKQLSQMLKSSAPAQEEEEDPLAYYENHTSQIEIVRQDRSMEQIVFPVPGICQFLTEETKHRLFTTTEQDEQGSKVSDFFDQSSFLHNEMEWQRKLRSMPLIYWFSRRMTLWGSISFNLAVFINIIIAFFYPYMEGASTGVLDSPLISLLFWILICFSIAALFTKRYSIRPLIVALILRSIYYLGIGPTLNILGALNLTNKIVFVVSFVGNRGTFIRGYKAMVMDMEFLYHVGYILTSVLGLFAHELFYSILLFDLIYREETLFNVIKSVTRNGRSILLTALLALILVYLFSIVGFLFLKDDFILEVDRLPNNHSTASPLGMPHGAAAFVDTCSGDKMDCVSGLSVPEVLEEDRELDSTERACDTLLMCIVTVMNHGLRNGGGVGDILRKPSKDESLFPARVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVSFEEHIKLEHNMWNYLYFIVLVRVKNKTDYTGPESYVAQMIKNKNLDWFPRMRAMSLVSNEGEGEQNEIRILQDKLNSTMKLVSHLTAQLNELKEQMTEQRKRRQRLGFVDVQNCISR TTH1769 TT Literature-reported TTVOH3T ID TTVOH3T TTVOH3T TN ISG15 messenger RNA (ISG15 mRNA) TTVOH3T UP P05161 TTVOH3T UC ISG15_HUMAN TTVOH3T BC mRNA target TTVOH3T SN hUCRP (mRNA); Ubiquitin-like protein ISG15 (mRNA); Ubiquitin cross-reactive protein (mRNA); UCRP (mRNA); Interferon-induced 17 kDa protein (mRNA); Interferon-induced 15 kDa protein (mRNA); IP17 (mRNA); G1P2 (mRNA) TTVOH3T GN ISG15 TTVOH3T FC ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Its target proteins include IFIT1, MX1/MxA, PPM1B, UBE2L6, UBA7, CHMP5, CHMP2A, CHMP4B and CHMP6. Can also isgylate: EIF2AK2/PKR which results in its activation, DDX58/RIG-I which inhibits its function in antiviral signaling response, EIF4E2 which enhances its cap structure-binding activity and translation-inhibition activity, UBE2N and UBE2E1 which negatively regulates their activity, IRF3 which inhibits its ubiquitination and degradation and FLNB which prevents its ability to interact with the upstream activators of the JNK cascade therby inhibiting IFNA-induced JNK signaling. Exhibits antiviral activity towards both DNA and RNA viruses, including influenza A, HIV-1 and Ebola virus. Restricts HIV-1 and ebola virus via disruption of viral budding. Inhibits the ubiquitination of HIV-1 Gag and host TSG101 and disrupts their interaction, thereby preventing assembly and release of virions from infected cells. Inhibits Ebola virus budding mediated by the VP40 protein by disrupting ubiquitin ligase activity of NEDD4 and its ability to ubiquitinate VP40. ISGylates influenza A virus NS1 protein which causes a loss of function of the protein and the inhibition of virus replication. The secreted form of ISG15 can: induce natural killer cell proliferation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity. The secreted form acts through the integrin ITGAL/ITGB2 receptor to initiate activation of SRC family tyrosine kinases including LYN, HCK and FGR which leads to secretion of IFNG and IL10; the interaction is mediated by ITGAL. Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. TTVOH3T PD 6FFA; 6BI8; 5W8U; 5W8T; 5TL6 TTVOH3T SQ MGWDLTVKMLAGNEFQVSLSSSMSVSELKAQITQKIGVHAFQQRLAVHPSGVALQDRVPLASQGLGPGSTVLLVVDKCDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRGGGTEPGGRS TTVOH3T TT Literature-reported TTVOH3T FM mRNA target TTBISK4 ID TTBISK4 TTBISK4 TN Jumonji domain-containing protein 1C (JMJD1C) TTBISK4 UP Q15652 TTBISK4 UC JHD2C_HUMAN TTBISK4 SN Thyroid receptor-interacting protein 8; TRIP8; TRIP-8; TR-interacting protein 8; Probable JmjC domain-containing histone demethylation protein 2C; KIAA1380; JHDM2C TTBISK4 GN JMJD1C TTBISK4 FC Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity). TTBISK4 EC EC 1.14.11.- TTBISK4 PD 5FZO; 2YPD TTBISK4 SQ MAVETRAELVGKRFLCVAVGDEARSERWESGRGWRSWRAGVIRAVSHRDSRNPDLAVYVEFDDLEWDKREWVKVYEDFSTFLVEYHLIWAKRNDPSQTQGSKSKQIQWPALTFKPLVERNIPSSVTAVEFLVDKQLDFLTEDSAFQPYQDDIDSLNPVLRDNPQLHEEVKVWVKEQKVQEIFMQGPYSLNGYRVRVYRQDSATQWFTGIITHHDLFTRTMIVMNDQVLEPQNVDPSMVQMTFLDDVVHSLLKGENIGITSRRRSRANQNVNAVHSHYTRAQANSPRPAMNSQAAVPKQNTHQQQQQRSIRPNKRKGSDSSIPDEEKMKEEKYDYISRGENPKGKNKHLMNKRRKPEEDEKKLNMKRLRTDNVSDFSESSDSENSNKRIIDNSSEQKPENELKNKNTSKINGEEGKPHNNEKAGEETLKNSQPPWDQIQEDKKHEEAEKRKSVDTQLQEDMIIHSSEQSTVSDHNSNDLLPQECNMDKTHTMELLPKEKFVSRPPTPKCVIDITNDTNLEKVAQENSSTFGLQTLQKMDPNVSDSKHSIANAKFLETAKKDSDQSWVSDVVKVDLTQSSVTNASSGNDHLNMEKEKYVSYISPLSAVSVMEDKLHKRSPPPETIKSKLNTSVDTHKIKSSPSPEVVKPKITHSPDSVKSKATYVNSQATGERRLANKIEHELSRCSFHPIPTRSSTLETTKSPLIIDKNEHFTVYRDPALIGSETGANHISPFLSQHPFPLHSSSHRTCLNPGTHHPALTPAPHLLAGSSSQTPLPTINTHPLTSGPHHAVHHPHLLPTVLPGVPTASLLGGHPRLESAHASSLSHLALAHQQQQQLLQHQSPHLLGQAHPSASYNQLGLYPIIWQYPNGTHAYSGLGLPSSKWVHPENAVNAEASLRRNSPSPWLHQPTPVTSADGIGLLSHIPVRPSSAEPHRPLKITAHSSPPLTKTLVDHHKEELERKAFMEPLRSVASTSAKNDLDLNRSQTGKDCHLHRHFVDPVLNQLQRPPQETGERLNKYKEEHRRILQESIDVAPFTTKIKGLEGERENYSRVASSSSSPKSHIIKQDMDVERSVSDLYKMKHSVPQSLPQSNYFTTLSNSVVNEPPRSYPSKEVSNIYGDKQSNALAAAAANPQTLTSFITSLSKPPPLIKHQPESEGLVGKIPEHLPHQIASHSVTTFRNDCRSPTHLTVSSTNTLRSMPALHRAPVFHPPIHHSLERKEGSYSSLSPPTLTPVMPVNAGGKVQESQKPPTLIPEPKDSQANFKSSSEQSLTEMWRPNNNLSKEKTEWHVEKSSGKLQAAMASVIVRPSSSTKTDSMPAMQLASKDRVSERSSAGAHKTDCLKLAEAGETGRIILPNVNSDSVHTKSEKNFQAVSQGSVPSSVMSAVNTMCNTKTDVITSAADTTSVSSWGGSEVISSLSNTILASTSSECVSSKSVSQPVAQKQECKVSTTAPVTLASSKTGSVVQPSSGFSGTTDFIHLKKHKAALAAAQYKSSNASETEPNAIKNQTLSASLPLDSTVICSTINKANSVGNGQASQTSQPNYHTKLKKAWLTRHSEEDKNTNKMENSGNSVSEIIKPCSVNLIASTSSDIQNSVDSKIIVDKYVKDDKVNRRKAKRTYESGSESGDSDESESKSEQRTKRQPKPTYKKKQNDLQKRKGEIEEDLKPNGVLSRSAKERSKLKLQSNSNTGIPRSVLKDWRKVKKLKQTGESFLQDDSCCEIGPNLQKCRECRLIRSKKGEEPAHSPVFCRFYYFRRLSFSKNGVVRIDGFSSPDQYDDEAMSLWTHENFEDDELDIETSKYILDIIGDKFCQLVTSEKTALSWVKKDAKIAWKRAVRGVREMCDACEATLFNIHWVCQKCGFVVCLDCYKAKERKSSRDKELYAWMKCVKGQPHDHKHLMPTQIIPGSVLTDLLDAMHTLREKYGIKSHCHCTNKQNLQVGNFPTMNGVSQVLQNVLNHSNKISLCMPESQQQNTPPKSEKNGGSSPESDVGTDNKLTPPESQSPLHWLADLAEQKAREEKKENKELTLENQIKEEREQDNSESPNGRTSPLVSQNNEQGSTLRDLLTTTAGKLRVGSTDAGIAFAPVYSMGAPSSKSGRTMPNILDDIIASVVENKIPPSKTSKINVKPELKEEPEESIISAVDENNKLYSDIPHSWICEKHILWLKDYKNSSNWKLFKECWKQGQPAVVSGVHKKMNISLWKAESISLDFGDHQADLLNCKDSIISNANVKEFWDGFEEVSKRQKNKSGETVVLKLKDWPSGEDFKTMMPARYEDLLKSLPLPEYCNPEGKFNLASHLPGFFVRPDLGPRLCSAYGVVAAKDHDIGTTNLHIEVSDVVNILVYVGIAKGNGILSKAGILKKFEEEDLDDILRKRLKDSSEIPGALWHIYAGKDVDKIREFLQKISKEQGLEVLPEHDPIRDQSWYVNKKLRQRLLEEYGVRTCTLIQFLGDAIVLPAGALHQVQNFHSCIQVTEDFVSPEHLVESFHLTQELRLLKEEINYDDKLQVKNILYHAVKEMVRALKIHEDEVEDMEEN TTBISK4 TT Literature-reported TTREN0G ID TTREN0G TTREN0G TN Junction plakoglobin (JUP) TTREN0G UP P14923 TTREN0G UC PLAK_HUMAN TTREN0G BC Beta-catenin TTREN0G SN Plakoglobin; Desmoplakin-3; Desmoplakin III; DP3; Catenin gamma; CTNNG TTREN0G GN JUP TTREN0G FC The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton. Common junctional plaque protein. TTREN0G PD 3IFQ TTREN0G SQ MEVMNLMEQPIKVTEWQQTYTYDSGIHSGANTCVPSVSSKGIMEEDEACGRQYTLKKTTTYTQGVPPSQGDLEYQMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQATNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQALVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSDVATKQEGLESVLKILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVAAGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKRVSVELTNSLFKHDPAAWEAAQSMIPINEPYGDDMDATYRPMYSSDVPLDPLEMHMDMDGDYPIDTYSDGLRPPYPTADHMLA TTREN0G TT Literature-reported TT3C8EG ID TT3C8EG TT3C8EG TN Junctional adhesion molecule A (F11R) TT3C8EG UP Q9Y624 TT3C8EG UC JAM1_HUMAN TT3C8EG BC Immunoglobulin TT3C8EG SN Platelet adhesion molecule 1; Platelet F11 receptor; PAM-1; Junctional adhesion molecule 1; JCAM; JAM1; JAM-A; JAM-1; CD321 TT3C8EG GN F11R TT3C8EG FC Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity). Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (By similarity). Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration. Involved in platelet activation. TT3C8EG PD 4ODB; 3TSZ; 3EOY; 1NBQ TT3C8EG SQ MGTKAQVERKLLCLFILAILLCSLALGSVTVHSSEPEVRIPENNPVKLSCAYSGFSSPRVEWKFDQGDTTRLVCYNNKITASYEDRVTFLPTGITFKSVTREDTGTYTCMVSEEGGNSYGEVKVKLIVLVPPSKPTVNIPSSATIGNRAVLTCSEQDGSPPSEYTWFKDGIVMPTNPKSTRAFSNSSYVLNPTTGELVFDPLSASDTGEYSCEARNGYGTPMTSNAVRMEAVERNVGVIVAAVLVTLILLGILVFGIWFAYSRGHFDRTKKGTSSKKVIYSQPSARSEGEFKQTSSFLV TT3C8EG TT Literature-reported TT3C8EG FM Immunoglobulin superfamily TTHL1TV ID TTHL1TV TTHL1TV TN Kinase suppressor of Ras-1 (KSR1) TTHL1TV UP Q13476 TTHL1TV UC KSR1_HUMAN TTHL1TV BC Kinase TTHL1TV SN Kinase suppressor of Ras 1; KSR TTHL1TV GN KSR1 TTHL1TV FC Promotes phosphorylation of Raf family members and activation of downstream MAP kinases. Promotes activation of MAPK1 and/or MAPK3, both in response to EGF and to cAMP. Does not have kinase activity by itself. Scaffolding protein that is part of a multiprotein signaling complex. TTHL1TV PD 5VYK TTHL1TV SQ MDRAALRAAAMGEKKEGGGGGDAAAAEGGAGAAASRALQQCGQLQKLIDISIGSLRGLRTKCAVSNDLTQQEIRTLEAKLVRYICKQRQCKLSVAPGERTPELNSYPRFSDWLYTFNVRPEVVQEIPRDLTLDALLEMNEAKVKETLRRCGASGDECGRLQYALTCLRKVTGLGGEHKEDSSWSSLDARRESGSGPSTDTLSAASLPWPPGSSQLGRAGNSAQGPRSISVSALPASDSPTPSFSEGLSDTCIPLHASGRLTPRALHSFITPPTTPQLRRHTKLKPPRTPPPPSRKVFQLLPSFPTLTRSKSHESQLGNRIDDVSSMRFDLSHGSPQMVRRDIGLSVTHRFSTKSWLSQVCHVCQKSMIFGVKCKHCRLKCHNKCTKEAPACRISFLPLTRLRRTESVPSDINNPVDRAAEPHFGTLPKALTKKEHPPAMNHLDSSSNPSSTTSSTPSSPAPFPTSSNPSSATTPPNPSPGQRDSRFNFPAAYFIHHRQQFIFPVPSAGHCWKCLLIAESLKENAFNISAFAHAAPLPEAADGTRLDDQPKADVLEAHEAEAEEPEAGKSEAEDDEDEVDDLPSSRRPWRGPISRKASQTSVYLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREGRRENQLKLSHDWLCYLAPEIVREMTPGKDEDQLPFSKAADVYAFGTVWYELQARDWPLKNQAAEASIWQIGSGEGMKRVLTSVSLGKEVSEILSACWAFDLQERPSFSLLMDMLEKLPKLNRRLSHPGHFWKSADINSSKVVPRFERFGLGVLESSNPKM TTHL1TV TT Literature-reported TTCJPAH ID TTCJPAH TTCJPAH TN Kinesin heavy chain neuron-specific 1 (KIF5A) TTCJPAH UP Q12840 TTCJPAH UC KIF5A_HUMAN TTCJPAH BC Kinesin-like protein family TTCJPAH SN NKHC; Kinesin heavy chain isoform 5A; KIF5A TTCJPAH GN KIF5A TTCJPAH FC Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). TTCJPAH PD 4UY0; 4UXY; 4UXT TTCJPAH SQ MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEEAALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNSLFQNYQNLYLQATPSSTSDMYFANSCTSSGATSSGGPLASYQKANMDNGNATDINDNRSDLPCGYEAEDQAKLFPLHQETAAS TTCJPAH TT Literature-reported TT254XD ID TT254XD TT254XD TN Kynurenic acid receptor (GPR35) TT254XD UP Q9HC97 TT254XD UC GPR35_HUMAN TT254XD BC GPCR rhodopsin TT254XD SN KYNA receptor; Gprotein coupled receptor 35; GPR35 TT254XD GN GPR35 TT254XD FC Acts as a receptor for kynurenic acid, an intermediate in the tryptophan metabolic pathway. The activity of this receptor is mediated by G-proteins that elicit calcium mobilization and inositol phosphate production through G(qi/o) proteins. TT254XD SQ MNGTYNTCGSSDLTWPPAIKLGFYAYLGVLLVLGLLLNSLALWVFCCRMQQWTETRIYMTNLAVADLCLLCTLPFVLHSLRDTSDTPLCQLSQGIYLTNRYMSISLVTAIAVDRYVAVRHPLRARGLRSPRQAAAVCAVLWVLVIGSLVARWLLGIQEGGFCFRSTRHNFNSMAFPLLGFYLPLAVVVFCSLKVVTALAQRPPTDVGQAEATRKAARMVWANLLVFVVCFLPLHVGLTVRLAVGWNACALLETIRRALYITSKLSDANCCLDAICYYYMAKEFQEASALAVAPSAKAHKSQDSLCVTLA TT254XD TT Literature-reported TT9JAGO ID TT9JAGO TT9JAGO TN LDL receptor related protein-1 (LRP-1) TT9JAGO UP Q07954 TT9JAGO UC LRP1_HUMAN TT9JAGO BC Low density lipoprotein receptor TT9JAGO SN Alpha-2-macroglobulin receptor; A2MR TT9JAGO GN LRP1 TT9JAGO FC Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission. Acts as an alpha-2-macroglobulin receptor. Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. TT9JAGO PD 2KNY; 2KNX; 2FYL; 2FYJ; 1J8E TT9JAGO SQ MLTPPLLLLLPLLSALVAAAIDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCQPNEHNCLGTELCVPMSRLCNGVQDCMDGSDEGPHCRELQGNCSRLGCQHHCVPTLDGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFICGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANAQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVGGAPPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDADGVTCLANPSYVPPPQCQPGEFACANSRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHTDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKSCEGVTHVCDPSVKFGCKDSARCISKAWVCDGDNDCEDNSDEENCESLACRPPSHPCANNTSVCLPPDKLCDGNDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGPDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTVHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGQGPCSHLCLINYNRTVSCACPHLMKLHKDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMANMDGSNRTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSGLEVIDAMRSQLGKATALAIMGDKLWWADQVSEKMGTCSKADGSGSVVLRNSTTLVMHMKVYDESIQLDHKGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGQYPRIERSRLDGTERVVLVNVSISWPNGISVDYQDGKLYWCDARTDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGSKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGRGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSRRITIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNEQHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKHVGSNMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQDDLTCRAVNSSCRAQDEFECANGECINFSLTCDGVPHCKDKSDEKPSYCNSRRCKKTFRQCSNGRCVSNMLWCNGADDCGDGSDEIPCNKTACGVGEFRCRDGTCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCEHGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCADGADESIAAGCLYNSTCDDREFMCQNRQCIPKHFVCDHDRDCADGSDESPECEYPTCGPSEFRCANGRCLSSRQWECDGENDCHDQSDEAPKNPHCTSQEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDSSDERGCHINECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADVDECSTTFPCSQRCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSSRSVIVDTKITWPNGLTLDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGTNKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGSDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFVCPPNRPFRCKNDRVCLWIGRQCDGTDNCGDGTDEEDCEPPTAHTTHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASICGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQAFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLVNLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCNLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEHCRNGGTCAASPSGMPTCRCPTGFTGPKCTQQVCAGYCANNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGYCENFGTCQMAADGSRQCRCTAYFEGSRCEVNKCSRCLEGACVVNKQSGDVTCNCTDGRVAPSCLTCVGHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEHVFSQQQPGHIASILIPLLLLLLLVLVAGVVFWYKRRVQGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA TT9JAGO TT Literature-reported TTPH1AJ ID TTPH1AJ TTPH1AJ TN LDL receptor related protein-2 (LRP-2) TTPH1AJ UP P98164 TTPH1AJ UC LRP2_HUMAN TTPH1AJ BC Low density lipoprotein receptor TTPH1AJ SN Megalin; Lowdensity lipoprotein receptorrelated protein 2; Low-density lipoprotein receptor-related protein 2; Gp330; Glycoprotein 330 TTPH1AJ GN LRP2 TTPH1AJ FC Acts together with CUBN to mediate endocytosis of high-density lipoproteins. Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B. In the kidney, mediates the tubular uptake and clearance of leptin. Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium. Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight. Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells. Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP. Mediates renal uptake of metallothionein-bound heavy metals. Together with CUBN, mediates renal reabsorption of myoglobin. Mediates renal uptake and subsequent lysosomal degradation of APOM. Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1. Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney. Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1. Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH. Also mediates ShhN transcytosis. In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon. Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH. During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure. In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed. In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid. Involved in neurite branching. During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells. Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent. Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG. Mediates endocytosis of angiotensin-2. Also mediates endocytosis of angiotensis 1-7. Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation. Required for embryonic heart development. Required for normal hearing, possibly through interaction with estrogen in the inner ear. Multiligand endocytic receptor. TTPH1AJ PD 2M0P TTPH1AJ SQ MDRGPAAVACTLLLALVACLAPASGQECDSAHFRCGSGHCIPADWRCDGTKDCSDDADEIGCAVVTCQQGYFKCQSEGQCIPNSWVCDQDQDCDDGSDERQDCSQSTCSSHQITCSNGQCIPSEYRCDHVRDCPDGADENDCQYPTCEQLTCDNGACYNTSQKCDWKVDCRDSSDEINCTEICLHNEFSCGNGECIPRAYVCDHDNDCQDGSDEHACNYPTCGGYQFTCPSGRCIYQNWVCDGEDDCKDNGDEDGCESGPHDVHKCSPREWSCPESGRCISIYKVCDGILDCPGREDENNTSTGKYCSMTLCSALNCQYQCHETPYGGACFCPPGYIINHNDSRTCVEFDDCQIWGICDQKCESRPGRHLCHCEEGYILERGQYCKANDSFGEASIIFSNGRDLLIGDIHGRSFRILVESQNRGVAVGVAFHYHLQRVFWTDTVQNKVFSVDINGLNIQEVLNVSVETPENLAVDWVNNKIYLVETKVNRIDMVNLDGSYRVTLITENLGHPRGIAVDPTVGYLFFSDWESLSGEPKLERAFMDGSNRKDLVKTKLGWPAGVTLDMISKRVYWVDSRFDYIETVTYDGIQRKTVVHGGSLIPHPFGVSLFEGQVFFTDWTKMAVLKANKFTETNPQVYYQASLRPYGVTVYHSLRQPYATNPCKDNNGGCEQVCVLSHRTDNDGLGFRCKCTFGFQLDTDERHCIAVQNFLIFSSQVAIRGIPFTLSTQEDVMVPVSGNPSFFVGIDFDAQDSTIFFSDMSKHMIFKQKIDGTGREILAANRVENVESLAFDWISKNLYWTDSHYKSISVMRLADKTRRTVVQYLNNPRSVVVHPFAGYLFFTDWFRPAKIMRAWSDGSHLLPVINTTLGWPNGLAIDWAASRLYWVDAYFDKIEHSTFDGLDRRRLGHIEQMTHPFGLAIFGEHLFFTDWRLGAIIRVRKADGGEMTVIRSGIAYILHLKSYDVNIQTGSNACNQPTHPNGDCSHFCFPVPNFQRVCGCPYGMRLASNHLTCEGDPTNEPPTEQCGLFSFPCKNGRCVPNYYLCDGVDDCHDNSDEQLCGTLNNTCSSSAFTCGHGECIPAHWRCDKRNDCVDGSDEHNCPTHAPASCLDTQYTCDNHQCISKNWVCDTDNDCGDGSDEKNCNSTETCQPSQFNCPNHRCIDLSFVCDGDKDCVDGSDEVGCVLNCTASQFKCASGDKCIGVTNRCDGVFDCSDNSDEAGCPTRPPGMCHSDEFQCQEDGICIPNFWECDGHPDCLYGSDEHNACVPKTCPSSYFHCDNGNCIHRAWLCDRDNDCGDMSDEKDCPTQPFRCPSWQWQCLGHNICVNLSVVCDGIFDCPNGTDESPLCNGNSCSDFNGGCTHECVQEPFGAKCLCPLGFLLANDSKTCEDIDECDILGSCSQHCYNMRGSFRCSCDTGYMLESDGRTCKVTASESLLLLVASQNKIIADSVTSQVHNIYSLVENGSYIVAVDFDSISGRIFWSDATQGKTWSAFQNGTDRRVVFDSSIILTETIAIDWVGRNLYWTDYALETIEVSKIDGSHRTVLISKNLTNPRGLALDPRMNEHLLFWSDWGHHPRIERASMDGSMRTVIVQDKIFWPCGLTIDYPNRLLYFMDSYLDYMDFCDYNGHHRRQVIASDLIIRHPYALTLFEDSVYWTDRATRRVMRANKWHGGNQSVVMYNIQWPLGIVAVHPSKQPNSVNPCAFSRCSHLCLLSSQGPHFYSCVCPSGWSLSPDLLNCLRDDQPFLITVRQHIIFGISLNPEVKSNDAMVPIAGIQNGLDVEFDDAEQYIYWVENPGEIHRVKTDGTNRTVFASISMVGPSMNLALDWISRNLYSTNPRTQSIEVLTLHGDIRYRKTLIANDGTALGVGFPIGITVDPARGKLYWSDQGTDSGVPAKIASANMDGTSVKTLFTGNLEHLECVTLDIEEQKLYWAVTGRGVIERGNVDGTDRMILVHQLSHPWGIAVHDSFLYYTDEQYEVIERVDKATGANKIVLRDNVPNLRGLQVYHRRNAAESSNGCSNNMNACQQICLPVPGGLFSCACATGFKLNPDNRSCSPYNSFIVVSMLSAIRGFSLELSDHSETMVPVAGQGRNALHVDVDVSSGFIYWCDFSSSVASDNAIRRIKPDGSSLMNIVTHGIGENGVRGIAVDWVAGNLYFTNAFVSETLIEVLRINTTYRRVLLKVTVDMPRHIVVDPKNRYLFWADYGQRPKIERSFLDCTNRTVLVSEGIVTPRGLAVDRSDGYVYWVDDSLDIIARIRINGENSEVIRYGSRYPTPYGITVFENSIIWVDRNLKKIFQASKEPENTEPPTVIRDNINWLRDVTIFDKQVQPRSPAEVNNNPCLENNGGCSHLCFALPGLHTPKCDCAFGTLQSDGKNCAISTENFLIFALSNSLRSLHLDPENHSPPFQTINVERTVMSLDYDSVSDRIYFTQNLASGVGQISYATLSSGIHTPTVIASGIGTADGIAFDWITRRIYYSDYLNQMINSMAEDGSNRTVIARVPKPRAIVLDPCQGYLYWADWDTHAKIERATLGGNFRVPIVNSSLVMPSGLTLDYEEDLLYWVDASLQRIERSTLTGVDREVIVNAAVHAFGLTLYGQYIYWTDLYTQRIYRANKYDGSGQIAMTTNLLSQPRGINTVVKNQKQQCNNPCEQFNGGCSHICAPGPNGAECQCPHEGNWYLANNRKHCIVDNGERCGASSFTCSNGRCISEEWKCDNDNDCGDGSDEMESVCALHTCSPTAFTCANGRCVQYSYRCDYYNDCGDGSDEAGCLFRDCNATTEFMCNNRRCIPREFICNGVDNCHDNNTSDEKNCPDRTCQSGYTKCHNSNICIPRVYLCDGDNDCGDNSDENPTYCTTHTCSSSEFQCASGRCIPQHWYCDQETDCFDASDEPASCGHSERTCLADEFKCDGGRCIPSEWICDGDNDCGDMSDEDKRHQCQNQNCSDSEFLCVNDRPPDRRCIPQSWVCDGDVDCTDGYDENQNCTRRTCSENEFTCGYGLCIPKIFRCDRHNDCGDYSDERGCLYQTCQQNQFTCQNGRCISKTFVCDEDNDCGDGSDELMHLCHTPEPTCPPHEFKCDNGRCIEMMKLCNHLDDCLDNSDEKGCGINECHDPSISGCDHNCTDTLTSFYCSCRPGYKLMSDKRTCVDIDECTEMPFVCSQKCENVIGSYICKCAPGYLREPDGKTCRQNSNIEPYLIFSNRYYLRNLTIDGYFYSLILEGLDNVVALDFDRVEKRLYWIDTQRQVIERMFLNKTNKETIINHRLPAAESLAVDWVSRKLYWLDARLDGLFVSDLNGGHRRMLAQHCVDANNTFCFDNPRGLALHPQYGYLYWADWGHRAYIGRVGMDGTNKSVIISTKLEWPNGITIDYTNDLLYWADAHLGYIEYSDLEGHHRHTVYDGALPHPFAITIFEDTIYWTDWNTRTVEKGNKYDGSNRQTLVNTTHRPFDIHVYHPYRQPIVSNPCGTNNGGCSHLCLIKPGGKGFTCECPDDFRTLQLSGSTYCMPMCSSTQFLCANNEKCIPIWWKCDGQKDCSDGSDELALCPQRFCRLGQFQCSDGNCTSPQTLCNAHQNCPDGSDEDRLLCENHHCDSNEWQCANKRCIPESWQCDTFNDCEDNSDEDSSHCASRTCRPGQFRCANGRCIPQAWKCDVDNDCGDHSDEPIEECMSSAHLCDNFTEFSCKTNYRCIPKWAVCNGVDDCRDNSDEQGCEERTCHPVGDFRCKNHHCIPLRWQCDGQNDCGDNSDEENCAPRECTESEFRCVNQQCIPSRWICDHYNDCGDNSDERDCEMRTCHPEYFQCTSGHCVHSELKCDGSADCLDASDEADCPTRFPDGAYCQATMFECKNHVCIPPYWKCDGDDDCGDGSDEELHLCLDVPCNSPNRFRCDNNRCIYSHEVCNGVDDCGDGTDETEEHCRKPTPKPCTEYEYKCGNGHCIPHDNVCDDADDCGDWSDELGCNKGKERTCAENICEQNCTQLNEGGFICSCTAGFETNVFDRTSCLDINECEQFGTCPQHCRNTKGSYECVCADGFTSMSDRPGKRCAAEGSSPLLLLPDNVRIRKYNLSSERFSEYLQDEEYIQAVDYDWDPKDIGLSVVYYTVRGEGSRFGAIKRAYIPNFESGRNNLVQEVDLKLKYVMQPDGIAVDWVGRHIYWSDVKNKRIEVAKLDGRYRKWLISTDLDQPAAIAVNPKLGLMFWTDWGKEPKIESAWMNGEDRNILVFEDLGWPTGLSIDYLNNDRIYWSDFKEDVIETIKYDGTDRRVIAKEAMNPYSLDIFEDQLYWISKEKGEVWKQNKFGQGKKEKTLVVNPWLTQVRIFHQLRYNKSVPNLCKQICSHLCLLRPGGYSCACPQGSSFIEGSTTECDAAIELPINLPPPCRCMHGGNCYFDETDLPKCKCPSGYTGKYCEMAFSKGISPGTTAVAVLLTILLIVVIGALAIAGFFHYRRTGSLLPALPKLPSLSSLVKPSENGNGVTFRSGADLNMDIGVSGFGPETAIDRSMAMSEDFVMEMGKQPIIFENPMYSARDSAVKVVQPIQVTVSENVDNKNYGSPINPSEIVPETNPTSPAADGTQVTKWNLFKRKSKQTTNFENPIYAQMENEQKESVAATPPPSPSLPAKPKPPSRRDPTPTYSATEDTFKDTANLVKEDSEV TTPH1AJ TT Literature-reported TTVFA2D ID TTVFA2D TTVFA2D TN Leishmania GDP-mannose pyrophosphorylase (Leishm exgmp) TTVFA2D UP Q9BLW4 TTVFA2D UC Q9BLW4_LEIME TTVFA2D BC Transferases of phosphorus-containing groups TTVFA2D SN GDP-mannose pyrophosphorylase TTVFA2D GN Leishm exgmp TTVFA2D FC Assembles as a hexamer of 240 kDa in several Leishmania species. Critical for cell integrity and survival. TTVFA2D EC EC 2.7.7.22 TTVFA2D SQ MSASDGQGMRAVILVGGFGTRLRPLTLTTPKPLVPFCNKPMIIHQIEALKAVGVTEVILAVAYRPEAMKEQMDEWSRKLGVSFVFSVEEDPLGTAGPLALARDILMQDDKPFFVLNSDVTCMFPLQELLDFHKARGGEGTIMVSQVTQWEKYGVVVYSQQSYQIERFVEKPSSFLGDRVNAGIYIFNKSILDRIPPCRTSIEKEIFPAMAAEGELYAFNLEGFWMDVGQPKDYILGMTKFIPSLLDGDRKTEQLHTEATEHQHGGRFTVVGASLIDPSAKIGDGAVIGPCASIGANCVIGESCRIDNAAILENSKVGKGTMVSRSIVGWNNRIGSWCHIEDISVLGDDVEVKDGVVLIGTKVLPNKDVGEHHFQAGIIM TTVFA2D TT Literature-reported TTTK61E ID TTTK61E TTTK61E TN Leukocyte antigen CD97 (CD97) TTTK61E UP P48960 TTTK61E UC CD97_HUMAN TTTK61E BC GPCR secretin TTTK61E SN CD97 antigen subunit beta; CD97 antigen TTTK61E GN CD97 TTTK61E FC Plays an essential role in leukocyte migration. Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. TTTK61E PD 2BOU TTTK61E SQ MGGRVFLAFCVWLTLPGAETQDSRGCARWCPQNSSCVNATACRCNPGFSSFSEIITTPTETCDDINECATPSKVSCGKFSDCWNTEGSYDCVCSPGYEPVSGAKTFKNESENTCQDVDECQQNPRLCKSYGTCVNTLGSYTCQCLPGFKFIPEDPKVCTDVNECTSGQNPCHSSTHCLNNVGSYQCRCRPGWQPIPGSPNGPNNTVCEDVDECSSGQHQCDSSTVCFNTVGSYSCRCRPGWKPRHGIPNNQKDTVCEDMTFSTWTPPPGVHSQTLSRFFDKVQDLGRDSKTSSAEVTIQNVIKLVDELMEAPGDVEALAPPVRHLIATQLLSNLEDIMRILAKSLPKGPFTYISPSNTELTLMIQERGDKNVTMGQSSARMKLNWAVAAGAEDPGPAVAGILSIQNMTTLLANASLNLHSKKQAELEEIYESSIRGVQLRRLSAVNSIFLSHNNTKELNSPILFAFSHLESSDGEAGRDPPAKDVMPGPRQELLCAFWKSDSDRGGHWATEGCQVLGSKNGSTTCQCSHLSSFAILMAHYDVEDWKLTLITRVGLALSLFCLLLCILTFLLVRPIQGSRTTIHLHLCICLFVGSTIFLAGIENEGGQVGLRCRLVAGLLHYCFLAAFCWMSLEGLELYFLVVRVFQGQGLSTRWLCLIGYGVPLLIVGVSAAIYSKGYGRPRYCWLDFEQGFLWSFLGPVTFIILCNAVIFVTTVWKLTQKFSEINPDMKKLKKARALTITAIAQLFLLGCTWVFGLFIFDDRSLVLTYVFTILNCLQGAFLYLLHCLLNKKVREEYRKWACLVAGGSKYSEFTSTTSGTGHNQTRALRASESGI TTTK61E TT Literature-reported TT1JZG6 ID TT1JZG6 TT1JZG6 TN Leukocyte receptor tyrosine kinase (LTK) TT1JZG6 UP P29376 TT1JZG6 UC LTK_HUMAN TT1JZG6 BC Kinase TT1JZG6 SN TYK1; Protein tyrosine kinase 1; Leukocyte tyrosine kinase receptor TT1JZG6 GN LTK TT1JZG6 FC The exact function of this protein is not known. Studies with chimeric proteins (replacing its extracellular region with that of several known growth factor receptors, such as EGFR and CSFIR) demonstrate its ability to promote growth and specifically neurite outgrowth, and cell survival. Signaling appears to involve the PI3 kinase pathway. Involved in regulation of the secretory pathway involving endoplasmic reticulum (ER) export sites (ERESs) and ER to Golgi transport. Receptor with a tyrosine-protein kinase activity. TT1JZG6 EC EC 2.7.10.1 TT1JZG6 SQ MGCWGQLLVWFGAAGAILCSSPGSQETFLRSSPLPLASPSPRDPKVSAPPSILEPASPLNSPGTEGSWLFSTCGASGRHGPTQTQCDGAYAGTSVVVTVGAAGQLRGVQLWRVPGPGQYLISAYGAAGGKGAKNHLSRAHGVFVSAIFSLGLGESLYILVGQQGEDACPGGSPESQLVCLGESRAVEEHAAMDGSEGVPGSRRWAGGGGGGGGATYVFRVRAGELEPLLVAAGGGGRAYLRPRDRGRTQASPEKLENRSEAPGSGGRGGAAGGGGGWTSRAPSPQAGRSLQEGAEGGQGCSEAWATLGWAAAGGFGGGGGACTAGGGGGGYRGGDASETDNLWADGEDGVSFIHPSSELFLQPLAVTENHGEVEIRRHLNCSHCPLRDCQWQAELQLAECLCPEGMELAVDNVTCMDLHKPPGPLVLMVAVVATSTLSLLMVCGVLILVKQKKWQGLQEMRLPSPELELSKLRTSAIRTAPNPYYCQVGLGPAQSWPLPPGVTEVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQYCTQDPDVLNSLLPMELGPTPEEEGTSGLGNRSLECLRPPQPQELSPEKLKSWGGSPLGPWLSSGLKPLKSRGLQPQNLWNPTYRS TT1JZG6 TT Literature-reported TT69NEG ID TT69NEG TT69NEG TN Liver receptor homolog-1 (NR5A2) TT69NEG UP O00482 TT69NEG UC NR5A2_HUMAN TT69NEG BC Nuclear hormone receptor TT69NEG SN LRH1; CYP7A promoterbinding factor; B1binding factor; Alpha1fetoprotein transcription factor TT69NEG GN NR5A2 TT69NEG FC Together with the oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an essential transcriptional regulator of lipid metabolism. Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex. Binds to the sequence element 5'-AACGACCGACCTTGAG-3' of the enhancer II of hepatitis B virus genes, a critical cis-element of their expression and regulation. May be responsible for the liver-specific activity of enhancer II, probably in combination with other hepatocyte transcription factors. Key regulator of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. May also contribute to the regulation of pancreas-specific genes and play important roles in embryonic development. Activates the transcription of CYP2C38. Nuclear receptor that acts as a key metabolic sensor by regulating the expression of genes involved in bile acid synthesis, cholesterol homeostasis and triglyceride synthesis. TT69NEG PD 5UNJ; 5SYZ; 5L11; 5L0M; 4RWV TT69NEG SQ MSSNSDTGDLQESLKHGLTPIGAGLPDRHGSPIPARGRLVMLPKVETEALGLARSHGEQGQMPENMQVSQFKMVNYSYDEDLEELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKRYTCIENQNCQIDKTQRKRCPYCRFQKCLSVGMKLEAVRADRMRGGRNKFGPMYKRDRALKQQKKALIRANGLKLEAMSQVIQAMPSDLTISSAIQNIHSASKGLPLNHAALPPTDYDRSPFVTSPISMTMPPHGSLQGYQTYGHFPSRAIKSEYPDPYTSSPESIMGYSYMDSYQTSSPASIPHLILELLKCEPDEPQVQAKIMAYLQQEQANRSKHEKLSTFGLMCKMADQTLFSIVEWARSSIFFRELKVDDQMKLLQNCWSELLILDHIYRQVVHGKEGSIFLVTGQQVDYSIIASQAGATLNNLMSHAQELVAKLRSLQFDQREFVCLKFLVLFSLDVKNLENFQLVEGVQEQVNAALLDYTMCNYPQQTEKFGQLLLRLPEIRAISMQAEEYLYYKHLNGDVPYNNLLIEMLHAKRA TT69NEG TT Literature-reported TT69NEG FM Nuclear hormone receptor family TTV76RD ID TTV76RD TTV76RD TN Long transient receptor potential channel 6 (TRPM6) TTV76RD UP Q9BX84 TTV76RD UC TRPM6_HUMAN TTV76RD BC Transient receptor potential catioin channel TTV76RD SN Transient receptor potential cation channel subfamily M member 6; Melastatin-related TRP cation channel 6; Channel kinase 2; CHAK2 TTV76RD GN TRPM6 TTV76RD FC Essential ion channel and serine/threonine-protein kinase. Crucial for magnesium homeostasis. Has an important role in epithelial magnesium transport and in the active magnesium absorption in the gut and kidney. Isoforms of the type M6-kinase lack the ion channel region. TTV76RD EC EC 2.7.11.1 TTV76RD SQ MKEQPVLERLQSQKSWIKGVFDKRECSTIIPSSKNPHRCTPVCQVCQNLIRCYCGRLIGDHAGIDYSWTISAAKGKESEQWSVEKHTTKSPTDTFGTINFQDGEHTHHAKYIRTSYDTKLDHLLHLMLKEWKMELPKLVISVHGGIQNFTMPSKFKEIFSQGLVKAAETTGAWIITEGINTGVSKHVGDALKSHSSHSLRKIWTVGIPPWGVIENQRDLIGKDVVCLYQTLDNPLSKLTTLNSMHSHFILSDDGTVGKYGNEMKLRRNLEKYLSLQKIHCRSRQGVPVVGLVVEGGPNVILSVWETVKDKDPVVVCEGTGRAADLLAFTHKHLADEGMLRPQVKEEIICMIQNTFNFSLKQSKHLFQILMECMVHRDCITIFDADSEEQQDLDLAILTALLKGTNLSASEQLNLAMAWDRVDIAKKHILIYEQHWKPDALEQAMSDALVMDRVDFVKLLIEYGVNLHRFLTIPRLEELYNTKQGPTNTLLHHLVQDVKQHTLLSGYRITLIDIGLVVEYLIGRAYRSNYTRKHFRALYNNLYRKYKHQRHSSGNRNESAESTLHSQFIRTAQPYKFKEKSIVLHKSRKKSKEQNVSDDPESTGFLYPYNDLLVWAVLMKRQKMAMFFWQHGEEATVKAVIACILYRAMAHEAKESHMVDDASEELKNYSKQFGQLALDLLEKAFKQNERMAMTLLTYELRNWSNSTCLKLAVSGGLRPFVSHTCTQMLLTDMWMGRLKMRKNSWLKIIISIILPPTILTLEFKSKAEMSHVPQSQDFQFMWYYSDQNASSSKESASVKEYDLERGHDEKLDENQHFGLESGHQHLPWTRKVYEFYSAPIVKFWFYTMAYLAFLMLFTYTVLVEMQPQPSVQEWLVSIYIFTNAIEVVREICISEPGKFTQKVKVWISEYWNLTETVAIGLFSAGFVLRWGDPPFHTAGRLIYCIDIIFWFSRLLDFFAVNQHAGPYVTMIAKMTANMFYIVIIMAIVLLSFGVARKAILSPKEPPSWSLARDIVFEPYWMIYGEVYAGEIDVCSSQPSCPPGSFLTPFLQAVYLFVQYIIMVNLLIAFFNNVYLDMESISNNLWKYNRYRYIMTYHEKPWLPPPLILLSHVGLLLRRLCCHRAPHDQEEGDVGLKLYLSKEDLKKLHDFEEQCVEKYFHEKMEDVNCSCEERIRVTSERVTEMYFQLKEMNEKVSFIKDSLLSLDSQVGHLQDLSALTVDTLKVLSAVDTLQEDEALLAKRKHSTCKKLPHSWSNVICAEVLGSMEIAGEKKYQYYSMPSSLLRSLAGGRHPPRVQRGALLEITNSKREATNVRNDQERQETQSSIVVSGVSPNRQAHSKYGQFLLVPSNLKRVPFSAETVLPLSRPSVPDVLATEQDIQTEVLVHLTGQTPVVSDWASVDEPKEKHEPIAHLLDGQDKAEQVLPTLSCTPEPMTMSSPLSQAKIMQTGGGYVNWAFSEGDETGVFSIKKKWQTCLPSTCDSDSSRSEQHQKQAQDSSLSDNSTRSAQSSECSEVGPWLQPNTSFWINPLRRYRPFARSHSFRFHKEEKLMKICKIKNLSGSSEIGQGAWVKAKMLTKDRRLSKKKKNTQGLQVPIITVNACSQSDQLNPEPGENSISEEEYSKNWFTVSKFSHTGVEPYIHQKMKTKEIGQCAIQISDYLKQSQEDLSKNSLWNSRSTNLNRNSLLKSSIGVDKISASLKSPQEPHHHYSAIERNNLMRLSQTIPFTPVQLFAGEEITVYRLEESSPLNLDKSMSSWSQRGRAAMIQVLSREEMDGGLRKAMRVVSTWSEDDILKPGQVFIVKSFLPEVVRTWHKIFQESTVLHLCLREIQQQRAAQKLIYTFNQVKPQTIPYTPRFLEVFLIYCHSANQWLTIEKYMTGEFRKYNNNNGDEITPTNTLEELMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEVKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRKLKLPDLKRNDYSPERINSTFGLEIKIESAEEPPARETGRNSPEDDMQL TTV76RD TT Literature-reported TTFPVZO ID TTFPVZO TTFPVZO TN Long transient receptor potential channel 7 (TRPM7) TTFPVZO UP Q96QT4 TTFPVZO UC TRPM7_HUMAN TTFPVZO BC Transient receptor potential catioin channel TTFPVZO SN Transient receptor potential cation channel subfamily M member 7; LTrpC-7; LTRPC7; Channel-kinase 1; CHAK1 TTFPVZO GN TRPM7 TTFPVZO FC Essential ion channel and serine/threonine-protein kinase. Divalent cation channel permeable to calcium and magnesium. Has a central role in magnesium ion homeostasis and in the regulation of anoxic neuronal cell death. Involved in TNF-induced necroptosis downstream of MLKL by mediating calcium influx. The kinase activity is essential for the channel function. May be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1). TTFPVZO EC EC 2.7.11.1 TTFPVZO SQ MSQKSWIESTLTKRECVYIIPSSKDPHRCLPGCQICQQLVRCFCGRLVKQHACFTASLAMKYSDVKLGDHFNQAIEEWSVEKHTEQSPTDAYGVINFQGGSHSYRAKYVRLSYDTKPEVILQLLLKEWQMELPKLVISVHGGMQKFELHPRIKQLLGKGLIKAAVTTGAWILTGGVNTGVAKHVGDALKEHASRSSRKICTIGIAPWGVIENRNDLVGRDVVAPYQTLLNPLSKLNVLNNLHSHFILVDDGTVGKYGAEVRLRRELEKTINQQRIHARIGQGVPVVALIFEGGPNVILTVLEYLQESPPVPVVVCEGTGRAADLLAYIHKQTEEGGNLPDAAEPDIISTIKKTFNFGQNEALHLFQTLMECMKRKELITVFHIGSDEHQDIDVAILTALLKGTNASAFDQLILTLAWDRVDIAKNHVFVYGQQWLVGSLEQAMLDALVMDRVAFVKLLIENGVSMHKFLTIPRLEELYNTKQGPTNPMLFHLVRDVKQGNLPPGYKITLIDIGLVIEYLMGGTYRCTYTRKRFRLIYNSLGGNNRRSGRNTSSSTPQLRKSHESFGNRADKKEKMRHNHFIKTAQPYRPKIDTVMEEGKKKRTKDEIVDIDDPETKRFPYPLNELLIWACLMKRQVMARFLWQHGEESMAKALVACKIYRSMAYEAKQSDLVDDTSEELKQYSNDFGQLAVELLEQSFRQDETMAMKLLTYELKNWSNSTCLKLAVSSRLRPFVAHTCTQMLLSDMWMGRLNMRKNSWYKVILSILVPPAILLLEYKTKAEMSHIPQSQDAHQMTMDDSENNFQNITEEIPMEVFKEVRILDSNEGKNEMEIQMKSKKLPITRKFYAFYHAPIVKFWFNTLAYLGFLMLYTFVVLVQMEQLPSVQEWIVIAYIFTYAIEKVREIFMSEAGKVNQKIKVWFSDYFNISDTIAIISFFIGFGLRFGAKWNFANAYDNHVFVAGRLIYCLNIIFWYVRLLDFLAVNQQAGPYVMMIGKMVANMFYIVVIMALVLLSFGVPRKAILYPHEAPSWTLAKDIVFHPYWMIFGEVYAYEIDVCANDSVIPQICGPGTWLTPFLQAVYLFVQYIIMVNLLIAFFNNVYLQVKAISNIVWKYQRYHFIMAYHEKPVLPPPLIILSHIVSLFCCICKRRKKDKTSDGPKLFLTEEDQKKLHDFEEQCVEMYFNEKDDKFHSGSEERIRVTFERVEQMCIQIKEVGDRVNYIKRSLQSLDSQIGHLQDLSALTVDTLKTLTAQKASEASKVHNEITRELSISKHLAQNLIDDGPVRPSVWKKHGVVNTLSSSLPQGDLESNNPFHCNILMKDDKDPQCNIFGQDLPAVPQRKEFNFPEAGSSSGALFPSAVSPPELRQRLHGVELLKIFNKNQKLGSSSTSIPHLSSPPTKFFVSTPSQPSCKSHLETGTKDQETVCSKATEGDNTEFGAFVGHRDSMDLQRFKETSNKIKILSNNNTSENTLKRVSSLAGFTDCHRTSIPVHSKQAEKISRRPSTEDTHEVDSKAALIPDWLQDRPSNREMPSEEGTLNGLTSPFKPAMDTNYYYSAVERNNLMRLSQSIPFTPVPPRGEPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRAVKVQCTWSEHDILKSGHLYIIKSFLPEVVNTWSSIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEIIPTNTLEEIMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAEEKRSCDMVFGPANLGEDAIKNFRAKHHCNSCCRKLKLPDLKRNDYTPDKIIFPQDEPSDLNLQPGNSTKESESTNSVRLML TTFPVZO TT Literature-reported TT3KLDP ID TT3KLDP TT3KLDP TN L-Tryptophan hydroxylase 2 (TPH2) TT3KLDP UP Q8IWU9 TT3KLDP UC TPH2_HUMAN TT3KLDP SN Tryptophan 5-monooxygenase 2; Tryptophan 5-hydroxylase 2; Neuronal tryptophan hydroxylase; NTPH TT3KLDP GN TPH2 TT3KLDP FC Rate-limiting enzyme in the synthesis of serotonin (5-hydroxytryptamine, or 5HT). Has functions in peripheral tissues, including the maintenance of vascular tone and gut motility. TT3KLDP EC EC 1.14.16.4 TT3KLDP PD 4V06 TT3KLDP SQ MQPAMMMFSSKYWARRGFSLDSAVPEEHQLLGSSTLNKPNSGKNDDKGNKGSSKREAATESGKTAVVFSLKNEVGGLVKALRLFQEKRVNMVHIESRKSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNPPENIWTEEEELEDVPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYIRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTCLQECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMNQYLGI TT3KLDP TT Literature-reported TT8S9AV ID TT8S9AV TT8S9AV TN Lymphocyte antigen 96 (LY96) TT8S9AV UP Q9Y6Y9 TT8S9AV UC LY96_HUMAN TT8S9AV SN MD-2 protein; MD-2; LY96; ESOP-1 TT8S9AV GN LY96 TT8S9AV FC Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria. Enhances TLR4-dependent activation of NF-kappa-B. Cells expressing both MD2 and TLR4, but not TLR4 alone, respond to LPS. TT8S9AV PD 4G8A; 3ULA; 3FXI; 2Z65; 2.00E+59 TT8S9AV SQ MLPFLFFSTLFSSIFTEAQKQYWVCNSSDASISYTYCDKMQYPISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGSDDDYSFCRALKGETVNTTISFSFKGIKFSKGKYKCVVEAISGSPEEMLFCLEFVILHQPNSN TT8S9AV TT Literature-reported TT8S9AV KE hsa04064:NF-kappa B signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa05130:Pathogenic Escherichia coli infection; hsa05133:Pertussis; hsa05145:Toxoplasmosis TT8S9AV RC R-HSA-140534:Ligand-dependent caspase activation; R-HSA-166016:Toll Like Receptor 4 (TLR4) Cascade; R-HSA-166058:MyD88:Mal cascade initiated on plasma membrane; R-HSA-166166:MyD88-independent TLR3/TLR4 cascade; R-HSA-2562578:TRIF-mediated programmed cell death; R-HSA-5602498:MyD88 deficiency (TLR2/4); R-HSA-5603041:IRAK4 deficiency (TLR2/4); R-HSA-936964:Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon; R-HSA-937041:IKK complex recruitment mediated by RIP1; R-HSA-937072:TRAF6 mediated induction of TAK1 complex TTHQ6US ID TTHQ6US TTHQ6US TN Lymphotoxin-beta (LTB) TTHQ6US UP Q06643 TTHQ6US UC TNFC_HUMAN TTHQ6US BC Cytokine: tumor necrosis factor TTHQ6US SN Tumor necrosis factor ligand superfamily member 3; Tumor necrosis factor C; TNF-C; LTB; LT-beta TTHQ6US GN LTB TTHQ6US FC Cytokine that binds to LTBR/TNFRSF3. May play a specific role in immune response regulation. Provides the membrane anchor for the attachment of the heterotrimeric complex to the cell surface. Isoform 2 is probably non-functional. TTHQ6US PD 4MXW TTHQ6US SQ MGALGLEGRGGRLQGRGSLLLAVAGATSLVTLLLAVPITVLAVLALVPQDQGGLVTETADPGAQAQQGLGFQKLPEEEPETDLSPGLPAAHLIGAPLKGQGLGWETTKEQAFLTSGTQFSDAEGLALPQDGLYYLYCLVGYRGRAPPGGGDPQGRSVTLRSSLYRAGGAYGPGTPELLLEGAETVTPVLDPARRQGYGPLWYTSVGFGGLVQLRRGERVYVNISHPDMVDFARGKTFFGAVMVG TTHQ6US TT Literature-reported TT8XTY2 ID TT8XTY2 TT8XTY2 TN Lysine-specific demethylase 2A (KDM2A) TT8XTY2 UP Q9Y2K7 TT8XTY2 UC KDM2A_HUMAN TT8XTY2 SN FBXL11; FBL7; F-box/LRR-repeat protein 11; F-box protein Lilina; F-box protein FBL7; F-box and leucine-rich repeat protein 11; CXXC8; CXXC-type zinc finger protein 8; [Histone-H3]-lysine-36 demethylase 1A; KIAA1004; JmjC domain-containing histone demethylation protein 1A; JHDM1A TT8XTY2 GN KDM2A TT8XTY2 FC Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis. Regulates circadian gene expression by repressing the transcriptional activator activity of CLOCK-ARNTL/BMAL1 heterodimer and RORA in a catalytically-independent manner. TT8XTY2 EC EC 1.14.11.27 TT8XTY2 PD 6C16; 6BYH; 4BBQ; 2YU2; 2YU1 TT8XTY2 SQ MEPEEERIRYSQRLRGTMRRRYEDDGISDDEIEGKRTFDLEEKLHTNKYNANFVTFMEGKDFNVEYIQRGGLRDPLIFKNSDGLGIKMPDPDFTVNDVKMCVGSRRMVDVMDVNTQKGIEMTMAQWTRYYETPEEEREKLYNVISLEFSHTRLENMVQRPSTVDFIDWVDNMWPRHLKESQTESTNAILEMQYPKVQKYCLMSVRGCYTDFHVDFGGTSVWYHIHQGGKVFWLIPPTAHNLELYENWLLSGKQGDIFLGDRVSDCQRIELKQGYTFVIPSGWIHAVYTPTDTLVFGGNFLHSFNIPMQLKIYNIEDRTRVPNKFRYPFYYEMCWYVLERYVYCITNRSHLTKEFQKESLSMDLELNGLESGNGDEEAVDREPRRLSSRRSVLTSPVANGVNLDYDGLGKTCRSLPSLKKTLAGDSSSDCSRGSHNGQVWDPQCAPRKDRQVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELANSDPKLALTGVPIVQWPKRDKLKFPTRPKVRVPTIPITKPHTMKPAPRLTPVRPAAASPIVSGARRRRVRCRKCKACVQGECGVCHYCRDMKKFGGPGRMKQSCVLRQCLAPRLPHSVTCSLCGEVDQNEETQDFEKKLMECCICNEIVHPGCLQMDGEGLLNEELPNCWECPKCYQEDSSEKAQKRKMEESDEEAVQAKVLRPLRSCDEPLTPPPHSPTSMLQLIHDPVSPRGMVTRSSPGAGPSDHHSASRDERFKRRQLLRLQATERTMVREKENNPSGKKELSEVEKAKIRGSYLTVTLQRPTKELHGTSIVPKLQAITASSANLRHSPRVLVQHCPARTPQRGDEEGLGGEEEEEEEEEEEDDSAEEGGAARLNGRGSWAQDGDESWMQREVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTKIDLSRCKAIVPQALSGIIKRQPVSLDLSWTNISKKQLTWLVNRLPGLKDLLLAGCSWSAVSALSTSSCPLLRTLDLRWAVGIKDPQIRDLLTPPADKPGQDNRSKLRNMTDFRLAGLDITDATLRLIIRHMPLLSRLDLSHCSHLTDQSSNLLTAVGSSTRYSLTELNMAGCNKLTDQTLIYLRRIANVTLIDLRGCKQITRKACEHFISDLSINSLYCLSDEKLIQKIS TT8XTY2 TT Literature-reported TTKXS4A ID TTKXS4A TTKXS4A TN Lysine-specific demethylase 3A (KDM3A) TTKXS4A UP Q9Y4C1 TTKXS4A UC KDM3A_HUMAN TTKXS4A BC Paired donor oxygen oxidoreductase TTKXS4A SN TSGA; KIAA0742; Jumonji domain-containing protein 1A; JmjC domain-containing histone demethylation protein 2A; JMJD1A; JMJD1; JHDM2A TTKXS4A GN KDM3A TTKXS4A FC Preferentially demethylates mono- and dimethylated H3 'Lys-9' residue, with a preference for dimethylated residue, while it has weak or no activity on trimethylated H3 'Lys-9'. Demethylation of Lys residue generates formaldehyde and succinate. Involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes, resulting in H3 'Lys-9' demethylation and transcriptional activation. Involved in spermatogenesis by regulating expression of target genes such as PRM1 and TNP1 which are required for packaging and condensation of sperm chromatin. Involved in obesity resistance through regulation of metabolic genes such as PPARA and UCP1. Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. TTKXS4A EC EC 1.14.11.- TTKXS4A SQ MVLTLGESWPVLVGRRFLSLSAADGSDGSHDSWDVERVAEWPWLSGTIRAVSHTDVTKKDLKVCVEFDGESWRKRRWIEVYSLLRRAFLVEHNLVLAERKSPEISERIVQWPAITYKPLLDKAGLGSITSVRFLGDQQRVFLSKDLLKPIQDVNSLRLSLTDNQIVSKEFQALIVKHLDESHLLKGDKNLVGSEVKIYSLDPSTQWFSATVINGNPASKTLQVNCEEIPALKIVDPSLIHVEVVHDNLVTCGNSARIGAVKRKSSENNGTLVSKQAKSCSEASPSMCPVQSVPTTVFKEILLGCTAATPPSKDPRQQSTPQAANSPPNLGAKIPQGCHKQSLPEEISSCLNTKSEALRTKPDVCKAGLLSKSSQIGTGDLKILTEPKGSCTQPKTNTDQENRLESVPQALTGLPKECLPTKASSKAELEIANPPELQKHLEHAPSPSDVSNAPEVKAGVNSDSPNNCSGKKVEPSALACRSQNLKESSVKVDNESCCSRSNNKIQNAPSRKSVLTDPAKLKKLQQSGEAFVQDDSCVNIVAQLPKCRECRLDSLRKDKEQQKDSPVFCRFFHFRRLQFNKHGVLRVEGFLTPNKYDNEAIGLWLPLTKNVVGIDLDTAKYILANIGDHFCQMVISEKEAMSTIEPHRQVAWKRAVKGVREMCDVCDTTIFNLHWVCPRCGFGVCVDCYRMKRKNCQQGAAYKTFSWLKCVKSQIHEPENLMPTQIIPGKALYDVGDIVHSVRAKWGIKANCPCSNRQFKLFSKPASKEDLKQTSLAGEKPTLGAVLQQNPSVLEPAAVGGEAASKPAGSMKPACPASTSPLNWLADLTSGNVNKENKEKQPTMPILKNEIKCLPPLPPLSKSSTVLHTFNSTILTPVSNNNSGFLRNLLNSSTGKTENGLKNTPKILDDIFASLVQNKTTSDLSKRPQGLTIKPSILGFDTPHYWLCDNRLLCLQDPNNKSNWNVFRECWKQGQPVMVSGVHHKLNSELWKPESFRKEFGEQEVDLVNCRTNEIITGATVGDFWDGFEDVPNRLKNEKEPMVLKLKDWPPGEDFRDMMPSRFDDLMANIPLPEYTRRDGKLNLASRLPNYFVRPDLGPKMYNAYGLITPEDRKYGTTNLHLDVSDAANVMVYVGIPKGQCEQEEEVLKTIQDGDSDELTIKRFIEGKEKPGALWHIYAAKDTEKIREFLKKVSEEQGQENPADHDPIHDQSWYLDRSLRKRLHQEYGVQGWAIVQFLGDVVFIPAGAPHQVHNLYSCIKVAEDFVSPEHVKHCFWLTQEFRYLSQTHTNHEDKLQVKNVIYHAVKDAVAMLKASESSFGKP TTKXS4A TT Literature-reported TTDIJUQ ID TTDIJUQ TTDIJUQ TN Lysine-specific demethylase 6B (KDM6B) TTDIJUQ UP O15054 TTDIJUQ UC KDM6B_HUMAN TTDIJUQ SN Lysine demethylase 6B; KIAA0346; Jumonji domain-containing protein 3; JmjC domain-containing protein 3; JMJD3 TTDIJUQ GN KDM6B TTDIJUQ FC Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation. Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression by acting as a link between T-box factors and the SMARCA4-containing SWI/SNF remodeling complex (By similarity). TTDIJUQ EC EC 1.14.11.- TTDIJUQ PD 6F6D; 5OY3; 5FP3; 4ASK; 2XXZ TTDIJUQ SQ MHRAVDPPGARAAREAFALGGLSCAGAWSSCPPHPPPRSAWLPGGRCSASIGQPPLPAPLPPSHGSSSGHPSKPYYAPGAPTPRPLHGKLESLHGCVQALLREPAQPGLWEQLGQLYESEHDSEEATRCYHSALRYGGSFAELGPRIGRLQQAQLWNFHTGSCQHRAKVLPPLEQVWNLLHLEHKRNYGAKRGGPPVKRAAEPPVVQPVPPAALSGPSGEEGLSPGGKRRRGCNSEQTGLPPGLPLPPPPLPPPPPPPPPPPPPLPGLATSPPFQLTKPGLWSTLHGDAWGPERKGSAPPERQEQRHSLPHPYPYPAPAYTAHPPGHRLVPAAPPGPGPRPPGAESHGCLPATRPPGSDLRESRVQRSRMDSSVSPAATTACVPYAPSRPPGLPGTTTSSSSSSSSNTGLRGVEPNPGIPGADHYQTPALEVSHHGRLGPSAHSSRKPFLGAPAATPHLSLPPGPSSPPPPPCPRLLRPPPPPAWLKGPACRAAREDGEILEELFFGTEGPPRPAPPPLPHREGFLGPPASRFSVGTQDSHTPPTPPTPTTSSSNSNSGSHSSSPAGPVSFPPPPYLARSIDPLPRPPSPAQNPQDPPLVPLTLALPPAPPSSCHQNTSGSFRRPESPRPRVSFPKTPEVGPGPPPGPLSKAPQPVPPGVGELPARGPRLFDFPPTPLEDQFEEPAEFKILPDGLANIMKMLDESIRKEEEQQQHEAGVAPQPPLKEPFASLQSPFPTDTAPTTTAPAVAVTTTTTTTTTTTATQEEEKKPPPALPPPPPLAKFPPPSQPQPPPPPPPSPASLLKSLASVLEGQKYCYRGTGAAVSTRPGPLPTTQYSPGPPSGATALPPTSAAPSAQGSPQPSASSSSQFSTSGGPWARERRAGEEPVPGPMTPTQPPPPLSLPPARSESEVLEEISRACETLVERVGRSATDPADPVDTAEPADSGTERLLPPAQAKEEAGGVAAVSGSCKRRQKEHQKEHRRHRRACKDSVGRRPREGRAKAKAKVPKEKSRRVLGNLDLQSEEIQGREKSRPDLGGASKAKPPTAPAPPSAPAPSAQPTPPSASVPGKKAREEAPGPPGVSRADMLKLRSLSEGPPKELKIRLIKVESGDKETFIASEVEERRLRMADLTISHCAADVVRASRNAKVKGKFRESYLSPAQSVKPKINTEEKLPREKLNPPTPSIYLESKRDAFSPVLLQFCTDPRNPITVIRGLAGSLRLNLGLFSTKTLVEASGEHTVEVRTQVQQPSDENWDLTGTRQIWPCESSRSHTTIAKYAQYQASSFQESLQEEKESEDEESEEPDSTTGTPPSSAPDPKNHHIIKFGTNIDLSDAKRWKPQLQELLKLPAFMRVTSTGNMLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFAVHEHYWETISAFCDRHGVDYLTGSWWPILDDLYASNIPVYRFVQRPGDLVWINAGTVHWVQATGWCNNIAWNVGPLTAYQYQLALERYEWNEVKNVKSIVPMIHVSWNVARTVKISDPDLFKMIKFCLLQSMKHCQVQRESLVRAGKKIAYQGRVKDEPAYYCNECDVEVFNILFVTSENGSRNTYLVHCEGCARRRSAGLQGVVVLEQYRTEELAQAYDAFTLAPASTSR TTDIJUQ TT Literature-reported TT0NYMP ID TT0NYMP TT0NYMP TN Lysine-specific demethylase 7A (KDM7A) TT0NYMP UP Q6ZMT4 TT0NYMP UC KDM7A_HUMAN TT0NYMP SN Lysine-specific demethylase 7; KIAA1718; KDM7; JmjC domain-containing histone demethylation protein 1D; JHDM1D TT0NYMP GN KDM7A TT0NYMP FC Histone demethylase required for brain development. Specifically demethylates dimethylated 'Lys-9' and 'Lys-27' (H3K9me2 and H3K27me2, respectively) of histone H3 and monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby playing a central role in histone code. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: in presence of H3K4me3, it has no demethylase activity toward H3K9me2, while it has high activity toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate. TT0NYMP EC EC 1.14.11.- TT0NYMP PD 3U78; 3KVB; 3KVA; 3KV9; 3KV6 TT0NYMP SQ MAGAAAAVAAGAAAGAAAAAVSVAAPGRASAPPPPPPVYCVCRQPYDVNRFMIECDICKDWFHGSCVGVEEHHAVDIDLYHCPNCAVLHGSSLMKKRRNWHRHDYTEIDDGSKPVQAGTRTFIKELRSRVFPSADEIIIKMHGSQLTQRYLEKHGFDVPIMVPKLDDLGLRLPSPTFSVMDVERYVGGDKVIDVIDVARQADSKMTLHNYVKYFMNPNRPKVLNVISLEFSDTKMSELVEVPDIAKKLSWVENYWPDDSVFPKPFVQKYCLMGVQDSYTDFHIDFGGTSVWYHVLWGEKIFYLIKPTDENLARYESWSSSVTQSEVFFGDKVDKCYKCVVKQGHTLFVPTGWIHAVLTSQDCMAFGGNFLHNLNIGMQLRCYEMEKRLKTPDLFKFPFFEAICWFVAKNLLETLKELREDGFQPQTYLVQGVKALHTALKLWMKKELVSEHAFEIPDNVRPGHLIKELSKVIRAIEEENGKPVKSQGIPIVCPVSRSSNEATSPYHSRRKMRKLRDHNVRTPSNLDILELHTREVLKRLEMCPWEEDILSSKLNGKFNKHLQPSSTVPEWRAKDNDLRLLLTNGRIIKDERQPFADQSLYTADSENEEDKRRTKKAKMKIEESSGVEGVEHEESQKPLNGFFTRVKSELRSRSSGYSDISESEDSGPECTALKSIFTTEESESSGDEKKQEITSNFKEESNVMRNFLQKSQKPSRSEIPIKRECPTSTSTEEEAIQGMLSMAGLHYSTCLQRQIQSTDCSGERNSLQDPSSCHGSNHEVRQLYRYDKPVECGYHVKTEDPDLRTSSWIKQFDTSRFHPQDLSRSQKCIRKEGSSEISQRVQSRNYVDSSGSSLQNGKYMQNSNLTSGACQISNGSLSPERPVGETSFSVPLHPTKRPASNPPPISNQATKGKRPKKGMATAKQRLGKILKLNRNGHARFFV TT0NYMP TT Literature-reported TT9AYVR ID TT9AYVR TT9AYVR TN Lysophosphatidic acid acyltransferase beta (LPAATB) TT9AYVR UP O15120 TT9AYVR UC PLCB_HUMAN TT9AYVR BC Acyltransferase TT9AYVR SN Lysophosphatidic acid acyltransferase-beta; LPAAT-beta; AGPAT2; 1-acylglycerol-3-phosphate O-acyltransferase 2; 1-AGPAT 2; 1-AGP acyltransferase 2 TT9AYVR GN AGPAT2 TT9AYVR FC Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. TT9AYVR EC EC 2.3.1.51 TT9AYVR SQ MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENMSIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAKRELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGDLLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAADVPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ TT9AYVR TT Literature-reported TTB7Y8I ID TTB7Y8I TTB7Y8I TN Lysophosphatidic acid receptor 2 (LPAR2) TTB7Y8I UP Q9HBW0 TTB7Y8I UC LPAR2_HUMAN TTB7Y8I BC GPCR rhodopsin TTB7Y8I SN Lysophosphatidic acid receptor Edg-4; LPA2; LPA-2; LPA receptor 2; EDG4 TTB7Y8I GN LPAR2 TTB7Y8I FC Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key role in phospholipase C-beta (PLC-beta) signaling pathway. Stimulates phospholipase C (PLC) activity in a manner that is independent of RALA activation. Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. TTB7Y8I PD 4P0C TTB7Y8I SQ MVIMGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASNRRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVATLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSRMAPLLSRSYLAVWALSSLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLVKTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDAEMRRTFRRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL TTB7Y8I TT Literature-reported TTPL1TK ID TTPL1TK TTPL1TK TN Lysophosphatidic acid transferase (AGPAT1) TTPL1TK UP Q99943 TTPL1TK UC PLCA_HUMAN TTPL1TK BC Acyltransferase TTPL1TK SN Protein G15; AGPAT1; 1acylsnglycerol3phosphate acyltransferase alpha; 1acylglycerol3phosphate Oacyltransferase 1; 1AGPAT 1; 1AGP acyltransferase 1 TTPL1TK GN AGPAT1 TTPL1TK FC Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. TTPL1TK EC EC 2.3.1.51 TTPL1TK SQ MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRGRNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGRCVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGTRNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTEGLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG TTPL1TK TT Literature-reported TT4E26T ID TT4E26T TT4E26T TN Lysyl oxidase (LOX) TT4E26T UP P28300 TT4E26T UC LYOX_HUMAN TT4E26T BC CH-NH(2) donor oxidoreductase TT4E26T SN Protein-lysine 6-oxidase TT4E26T GN LOX TT4E26T FC Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture. Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. TT4E26T EC EC 1.4.3.13 TT4E26T SQ MRFAWTVLLLGPLQLCALVHCAPPAAGQQQPPREPPAAPGAWRQQIQWENNGQVFSLLSLGSQYQPQRRRDPGAAVPGAANASAQQPRTPILLIRDNRTAAARTRTAGSSGVTAGRPRPTARHWFQAGYSTSRAREAGASRAENQTAPGEVPALSNLRPPSRVDGMVGDDPYNPYKYSDDNPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAAEENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY TT4E26T TT Literature-reported TT4E26T FM Oxidoreductases acting on CH-NH2 group of donors TTON5JB ID TTON5JB TTON5JB TN MADH6 messenger RNA (MADH6 mRNA) TTON5JB UP O43541 TTON5JB UC SMAD6_HUMAN TTON5JB BC mRNA target TTON5JB SN hSMAD6 (mRNA); Smad6 (mRNA); SMAD family member 6 (mRNA); SMAD 6 (mRNA); Mothers against decapentaplegic homolog 6 (mRNA); Mothers against DPP homolog 6 (mRNA); MADH6 (mRNA); MAD homolog 6 (mRNA) TTON5JB GN SMAD6 TTON5JB FC Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of proinflammatory genes. May block the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory elements in target promoter regions. Acts as a mediator of TGF-beta and BMP antiflammatory activity. TTON5JB SQ MFRSKRSGLVRRLWRSRVVPDREEGGSGGGGGGDEDGSLGSRAEPAPRAREGGGCGRSEVRPVAPRRPRDAVGQRGAQGAGRRRRAGGPPRPMSEPGAGAGSSLLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDASDPLAGAALEPAGGGRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFAAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPRDEYKPLDLSDSTLSYTETEATNSLITAPGEFSDASMSPDATKPSHWCSVAYWEHRTRVGRLYAVYDQAVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGFGILLSKEPDGVWAYNRGEHPIFVNSPTLDAPGGRALVVRKVPPGYSIKVFDFERSGLQHAPEPDAADGPYDPNSVRISFAKGWGPCYSRQFITSCPCWLEILLNNPR TTON5JB TT Literature-reported TTON5JB FM mRNA target TTON5JB KE hsa04144:Endocytosis; hsa04350:TGF-beta signaling pathway TT9Z4YD ID TT9Z4YD TT9Z4YD TN Malonyl-CoA decarboxylase (MLYCD) TT9Z4YD UP O95822 TT9Z4YD UC DCMC_HUMAN TT9Z4YD SN Malonyl-CoA decarboxylase, mitochondrial; MCD TT9Z4YD GN MLYCD TT9Z4YD FC Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation. TT9Z4YD EC EC 4.1.1.9 TT9Z4YD PD 4F0X; 2YGW TT9Z4YD SQ MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL TT9Z4YD TT Literature-reported TTMG71U ID TTMG71U TTMG71U TN Mannose receptor (MRC1) TTMG71U UP P22897 TTMG71U UC MRC1_HUMAN TTMG71U BC Fibronectin protein TTMG71U SN Macrophage mannose receptor 1like protein 1; Macrophage mannose receptor 1-like protein 1; Macrophage mannose receptor 1; MRC1L1; MMR; Human mannose receptor; Ctype lectin domain family 13 member Dlike; Ctype lectin domain family 13 member D; CLEC13DL; CLEC13D; CD206; C-type lectin domain family 13 member D-like; C-type lectin domain family 13 member D TTMG71U GN MRC1 TTMG71U FC Binds both sulfated and non-sulfated polysaccharide chains. Mediates the endocytosis of glycoproteins by macrophages. TTMG71U PD 5XTW; 5XTS; 1EGI; 1EGG TTMG71U SQ MRLPLLLVFASVIPGAVLLLDTRQFLIYNEDHKRCVDAVSPSAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQKWECKNDTLLGIKGEDLFFNYGNRQEKNIMLYKGSGLWSRWKIYGTTDNLCSRGYEAMYTLLGNANGATCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDTDKLFGYCPLKFEGSESLWNKDPLTSVSYQINSKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSGLWIGLNSLSFNSGWQWSDRSPFRYLNWLPGSPSAEPGKSCVSLNPGKNAKWENLECVQKLGYICKKGNTTLNSFVIPSESDVPTHCPSQWWPYAGHCYKIHRDEKKIQRDALTTCRKEGGDLTSIHTIEELDFIISQLGYEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLRGEPSHENNRQEDCVVMKGKDGYWADRGCEWPLGYICKMKSRSQGPEIVEVEKGCRKGWKKHHFYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRPEKYFWTGLSDIQTKGTFQWTIEEEVRFTHWNSDMPGRKPGCVAMRTGIAGGLWDVLKCDEKAKFVCKHWAEGVTHPPKPTTTPEPKCPEDWGASSRTSLCFKLYAKGKHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHKLFWLGLTYGSPSEGFTWSDGSPVSYENWAYGEPNNYQNVEYCGELKGDPTMSWNDINCEHLNNWICQIQKGQTPKPEPTPAPQDNPPVTEDGWVIYKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDAQSAYFIGLLISLDKKFAWMDGSKVDYVSWATGEPNFANEDENCVTMYSNSGFWNDINCGYPNAFICQRHNSSINATTVMPTMPSVPSGCKEGWNFYSNKCFKIFGFMEEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSAWTGLNDVNSEHTFLWTDGRGVHYTNWGKGYPGGRRSSLSYEDADCVVIIGGASNEAGKWMDDTCDSKRGYICQTRSDPSLTNPPATIQTDGFVKYGKSSYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQMETSNERVWIALNSNLTDNQYTWTDKWRVRYTNWAADEPKLKSACVYLDLDGYWKTAHCNESFYFLCKRSDEIPATEPPQLPGRCPESDHTAWIPFHGHCYYIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLKSKTNFWIGLFRNVEGTWLWINNSPVSFVNWNTGDPSGERNDCVALHASSGFWSNIHCSSYKGYICKRPKIIDAKPTHELLTTKADTRKMDPSKPSSNVAGVVIIVILLILTGAGLAAYFFYKKRRVHLPQEGAFENTLYFNSQSSPGTSDMKDLVGNIEQNEHSVI TTMG71U TT Literature-reported TTMG71U FM Fibronectin TT1RSX7 ID TT1RSX7 TT1RSX7 TN MAPK/ERK kinase kinase 4 (MAP3K4) TT1RSX7 UP Q9Y6R4 TT1RSX7 UC M3K4_HUMAN TT1RSX7 BC Kinase TT1RSX7 SN Mitogen-activated protein kinase kinase kinase 4; MTK1; MEKK4; MEKK 4; MEK kinase 4; MAPKKK4; MAP three kinase 1; KIAA0213 TT1RSX7 GN MAP3K4 TT1RSX7 FC Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. Component of a protein kinase signal transduction cascade. TT1RSX7 EC EC 2.7.11.25 TT1RSX7 SQ MREAAAALVPPPAFAVTPAAAMEEPPPPPPPPPPPPEPETESEPECCLAARQEGTLGDSACKSPESDLEDFSDETNTENLYGTSPPSTPRQMKRMSTKHQRNNVGRPASRSNLKEKMNAPNQPPHKDTGKTVENVEEYSYKQEKKIRAALRTTERDRKKNVQCSFMLDSVGGSLPKKSIPDVDLNKPYLSLGCSNAKLPVSVPMPIARPARQTSRTDCPADRLKFFETLRLLLKLTSVSKKKDREQRGQENTSGFWLNRSNELIWLELQAWHAGRTINDQDFFLYTARQAIPDIINEILTFKVDYGSFAFVRDRAGFNGTSVEGQCKATPGTKIVGYSTHHEHLQRQRVSFEQVKRIMELLEYIEALYPSLQALQKDYEKYAAKDFQDRVQALCLWLNITKDLNQKLRIMGTVLGIKNLSDIGWPVFEIPSPRPSKGNEPEYEGDDTEGELKELESSTDESEEEQISDPRVPEIRQPIDNSFDIQSRDCISKKLERLESEDDSLGWGAPDWSTEAGFSRHCLTSIYRPFVDKALKQMGLRKLILRLHKLMDGSLQRARIALVKNDRPVEFSEFPDPMWGSDYVQLSRTPPSSEEKCSAVSWEELKAMDLPSFEPAFLVLCRVLLNVIHECLKLRLEQRPAGEPSLLSIKQLVRECKEVLKGGLLMKQYYQFMLQEVLEDLEKPDCNIDAFEEDLHKMLMVYFDYMRSWIQMLQQLPQASHSLKNLLEEEWNFTKEITHYIRGGEAQAGKLFCDIAGMLLKSTGSFLEFGLQESCAEFWTSADDSSASDEIRRSVIEISRALKELFHEARERASKALGFAKMLRKDLEIAAEFRLSAPVRDLLDVLKSKQYVKVQIPGLENLQMFVPDTLAEEKSIILQLLNAAAGKDCSKDSDDVLIDAYLLLTKHGDRARDSEDSWGTWEAQPVKVVPQVETVDTLRSMQVDNLLLVVMQSAHLTIQRKAFQQSIEGLMTLCQEQTSSQPVIAKALQQLKNDALELCNRISNAIDRVDHMFTSEFDAEVDESESVTLQQYYREAMIQGYNFGFEYHKEVVRLMSGEFRQKIGDKYISFARKWMNYVLTKCESGRGTRPRWATQGFDFLQAIEPAFISALPEDDFLSLQALMNECIGHVIGKPHSPVTGLYLAIHRNSPRPMKVPRCHSDPPNPHLIIPTPEGFSTRSMPSDARSHGSPAAAAAAAAAAVAASRPSPSGGDSVLPKSISSAHDTRGSSVPENDRLASIAAELQFRSLSRHSSPTEERDEPAYPRGDSSGSTRRSWELRTLISQSKDTASKLGPIEAIQKSVRLFEEKRYREMRRKNIIGQVCDTPKSYDNVMHVGLRKVTFKWQRGNKIGEGQYGKVYTCISVDTGELMAMKEIRFQPNDHKTIKETADELKIFEGIKHPNLVRYFGVELHREEMYIFMEYCDEGTLEEVSRLGLQEHVIRLYSKQITIAINVLHEHGIVHRDIKGANIFLTSSGLIKLGDFGCSVKLKNNAQTMPGEVNSTLGTAAYMAPEVITRAKGEGHGRAADIWSLGCVVIEMVTGKRPWHEYEHNFQIMYKVGMGHKPPIPERLSPEGKDFLSHCLESDPKMRWTASQLLDHSFVKVCTDEE TT1RSX7 TT Literature-reported TT1RSX7 FM Kinase TTFS4VU ID TTFS4VU TTFS4VU TN MAPK-activated protein kinase 3 (MAPKAPK3) TTFS4VU UP Q16644 TTFS4VU UC MAPK3_HUMAN TTFS4VU SN MAPKAPK3 TTFS4VU GN MAPKAPK3 TTFS4VU FC Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X2-S, where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins, such as TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression. TTFS4VU EC EC 2.7.11.1 TTFS4VU PD 3SHE; 3R1N; 3FXW; 3FHR TTFS4VU SQ MDGETAEEQGGPVPPPVAPGGPGLGGAPGGRREPKKYAVTDDYQLSKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARQEVDHHWQASGGPHIVCILDVYENMHHGKRCLLIIMECMEGGELFSRIQERGDQAFTEREAAEIMRDIGTAIQFLHSHNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRLGQYGFPNPEWSEVSEDAKQLIRLLLKTDPTERLTITQFMNHPWINQSMVVPQTPLHTARVLQEDKDHWDEVKEEMTSALATMRVDYDQVKIKDLKTSNNRLLNKRRKKQAGSSSASQGCNNQ TTFS4VU TT Literature-reported TT3YV20 ID TT3YV20 TT3YV20 TN Mas-related gene 2 (MRGX2) TT3YV20 UP Q96LB1 TT3YV20 UC MRGX2_HUMAN TT3YV20 BC GPCR rhodopsin TT3YV20 SN Masrelated Gprotein coupled receptormember X2; MRGPRX2 TT3YV20 GN MRGPRX2 TT3YV20 FC Mast cell-specific receptor for basic secretagogues (PubMed:25517090). Basic secretagogues are a set of cationic amphiphilic drugs, as well as endo- and exogenous peptides, which share basic head group combined with a hydrophobic core of the molecule. Recognizes and binds small molecules containing a cyclized a tetrahydroisoquinoline (THIQ), such as non-steroidal neuromuscular blocking drugs (NMBDs), including tubocurarine and atracurium. Mediates mast cell responsiveness and side effects of small-molecule therapeutic drugs by acting as a specific receptor for basic secretagogues drugs in mast cells: binding to drugs induces pseudo-allergic reactions characterized by histamine release, inflammation and airway contraction. Acts as a receptor for a number of ligands, including peptides: acts as a receptor of cortistatin-14, a regulator of sleep regulation locomotor activity, and cortical function (PubMed:12915402). Acts as a receptor for proadrenomedullin N- terminal peptides PAMP-12, and atlower extent PAMP-20 (PubMed:15823563). Acts as a receptor for antibacterial protein LL-37, promoting chemotaxis, degranulation and chemokine production in mast cells (PubMed:22069323). Acts as a receptor for PMX-53 peptide, a potent antagonist of C5AR1/CD88 (PubMed:21441599). Acts as a receptor for beta-defensins (PubMed:23698749). Acts as a receptor for complanadine A, an alkaloid (PubMed:24930830). {ECO:0000250|UniProtKB:Q3UG50, ECO:0000269|PubMed:15823563, ECO:0000269|PubMed:21441599, ECO:0000269|PubMed:22069323, ECO:0000269|PubMed:23698749, ECO:0000269|PubMed:24930830, ECO:0000269|PubMed:25517090, ECO:0000305|PubMed:12915402}. TT3YV20 SQ MDPTTPAWGTESTTVNGNDQALLLLCGKETLIPVFLILFIALVGLVGNGFVLWLLGFRMRRNAFSVYVLSLAGADFLFLCFQIINCLVYLSNFFCSISINFPSFFTTVMTCAYLAGLSMLSTVSTERCLSVLWPIWYRCRRPRHLSAVVCVLLWALSLLLSILEGKFCGFLFSDGDSGWCQTFDFITAAWLIFLFMVLCGSSLALLVRILCGSRGLPLTRLYLTILLTVLVFLLCGLPFGIQWFLILWIWKDSDVLFCHIHPVSVVLSSLNSSANPIIYFFVGSFRKQWRLQQPILKLALQRALQDIAEVDHSEGCFRQGTPEMSRSSLV TT3YV20 TT Literature-reported TTNSTO3 ID TTNSTO3 TTNSTO3 TN Matrix metalloproteinase-15 (MMP-15) TTNSTO3 UP P51511 TTNSTO3 UC MMP15_HUMAN TTNSTO3 BC Peptidase TTNSTO3 SN SMCP-2; Membrane-type-2 matrix metalloproteinase; Membrane-type matrix metalloproteinase 2; MTMMP2; MT2MMP; MT2-MMP; MT-MMP 2 TTNSTO3 GN MMP15 TTNSTO3 FC May activate progelatinase A. Endopeptidase that degrades various components of the extracellular matrix. TTNSTO3 EC EC 3.4.24.- TTNSTO3 SQ MGSDPSAPGRPGWTGSLLGDREEAARPRLLPLLLVLLGCLGLGVAAEDAEVHAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWMKRPRCGVPDQFGVRVKANLRRRRKRYALTGRKWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEDIRLRRQKEADIMVLFASGFHGDSSPFDGTGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLRGIQQLYGTPDGQPQPTQPLPTVTPRRPGRPDHRPPRPPQPPPPGGKPERPPKPGPPVQPRATERPDQYGPNICDGDFDTVAMLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGDISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKPISVWQGIPASPKGAFLSNDAAYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGCQEHVEPGPRWPDVARPPFNPHGGAEPGADSAEGDVGDGDGDFGAGVNKDGGSRVVVQMEEVARTVNVVMVLVPLLLLLCVLGLTYALVQMQRKGAPRVLLYCKRSLQEWV TTNSTO3 TT Literature-reported TTVSZKN ID TTVSZKN TTVSZKN TN Matrix metalloproteinase-17 (MMP17) TTVSZKN UP Q9ULZ9 TTVSZKN UC MMP17_HUMAN TTVSZKN BC Peptidase TTVSZKN SN Membrane-type-4 matrix metalloproteinase; Membrane-type matrix metalloproteinase 4; MTMMP4; MT4MMP; MT4-MMP; MT-MMP 4; MMP-17 TTVSZKN GN MMP17 TTVSZKN FC Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin. TTVSZKN EC EC 3.4.24.- TTVSZKN SQ MRRRAARGPGPPPPGPGLSRLPLPLLLLLALGTRGGCAAPAPAPRAEDLSLGVEWLSRFGYLPPADPTTGQLQTQEELSKAITAMQQFGGLEATGILDEATLALMKTPRCSLPDLPVLTQARRRRQAPAPTKWNKRNLSWRVRTFPRDSPLGHDTVRALMYYALKVWSDIAPLNFHEVAGSAADIQIDFSKADHNDGYPFDGPGGTVAHAFFPGHHHTAGDTHFDDDEAWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGPVGDPLRYGLPYEDKVRVWQLYGVRESVSPTAQPEEPPLLPEPPDNRSSAPPRKDVPHRCSTHFDAVAQIRGEAFFFKGKYFWRLTRDRHLVSLQPAQMHRFWRGLPLHLDSVDAVYERTSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDFSLPPGGIDAAFSWAHNDRTYFFKDQLYWRYDDHTRHMDPGYPAQSPLWRGVPSTLDDAMRWSDGASYFFRGQEYWKVLDGELEVAPGYPQSTARDWLVCGDSQADGSVAAGVDAAEGPRAPPGQHDQSRSEDGYEVCSCTSGASSPPGAPGPLVAATMLLLLPPLSPGALWTAAQALTL TTVSZKN TT Literature-reported TTS17MG ID TTS17MG TTS17MG TN Melanin-concentrating hormone receptor 2 (MCHR2) TTS17MG UP Q969V1 TTS17MG UC MCHR2_HUMAN TTS17MG BC GPCR rhodopsin TTS17MG SN SLT; MCHR-2; MCH2R; MCH2 protein; MCH-R2; MCH-2R; MCH(2) receptor; MCH receptor 2; GPRv17; GPR145; G-protein coupled receptor 145; G protein coupled receptor 145 TTS17MG GN MCHR2 TTS17MG FC Receptor for melanin-concentrating hormone, coupled to G proteins that activate phosphoinositide hydrolysis. TTS17MG SQ MNPFHASCWNTSAELLNKSWNKEFAYQTASVVDTVILPSMIGIICSTGLVGNILIVFTIIRSRKKTVPDIYICNLAVADLVHIVGMPFLIHQWARGGEWVFGGPLCTIITSLDTCNQFACSAIMTVMSVDRYFALVQPFRLTRWRTRYKTIRINLGLWAASFILALPVWVYSKVIKFKDGVESCAFDLTSPDDVLWYTLYLTITTFFFPLPLILVCYILILCYTWEMYQQNKDARCCNPSVPKQRVMKLTKMVLVLVVVFILSAAPYHVIQLVNLQMEQPTLAFYVGYYLSICLSYASSSINPFLYILLSGNFQKRLPQIQRRATEKEINNMGNTLKSHF TTS17MG TT Literature-reported TTS17MG RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events TTBXIM9 ID TTBXIM9 TTBXIM9 TN Membrane-associated lectin type-C (CD209) TTBXIM9 UP Q9NNX6 TTBXIM9 UC CD209_HUMAN TTBXIM9 SN Surface C-type lectin DC-SIGN; Probable mannose-binding C-type lectin DC-SIGN; MDC-SIGN1A type I isoform; Dendritic cell-specific ICAM-3-grabbing nonintegrin 1; Dendritic cell-specific ICAM-3-grabbing non-integrin 1; DC-specific ICAM-3 grabbing nonintegrin; DC-SIGN1; DC-SIGN; CLEC4L; CD209 antigen; CD 209; C-type lectin domain family 4 member L TTBXIM9 GN CD209 TTBXIM9 FC Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response. TTBXIM9 PD 2XR6; 2XR5; 2IT6; 2IT5; 2B6B TTBXIM9 SQ MSDSKEPRLQQLGLLEEEQLRGLGFRQTRGYKSLAGCLGHGPLVLQLLSFTLLAGLLVQVSKVPSSISQEQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTWLKAAVGELPEKSKMQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVERLCHPCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA TTBXIM9 TT Literature-reported TTBXIM9 FM Transmembrane protein TTBXIM9 KE hsa04145:Phagosome; hsa05152:Tuberculosis; hsa05162:Measles TTBXIM9 RC R-HSA-5621575:CD209 (DC-SIGN) signaling TTOXF5J ID TTOXF5J TTOXF5J TN Metalloreductase STEAP2 (STEAP2) TTOXF5J UP Q8NFT2 TTOXF5J UC STEA2_HUMAN TTOXF5J BC Metal ion oxidoreductase TTOXF5J SN STEAP2 TTOXF5J GN STEAP2 TTOXF5J FC Metalloreductase that hasthe ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor. TTOXF5J EC EC 1.16.1.- TTOXF5J SQ MESISMMGSPKSLSETFLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGSRNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNMRINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIELARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYARNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQCRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMYISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFEEEYYRFYTPPNFVLALVLPSIVILGKIILFLPCISRKLKRIKKGWEKSQFLEEGMGGTIPHVSPERVTVM TTOXF5J TT Literature-reported TTO4HUS ID TTO4HUS TTO4HUS TN Metastasis associated gene-1 (MTA1) TTO4HUS UP Q13330 TTO4HUS UC MTA1_HUMAN TTO4HUS SN Metastasisassociated protein MTA1; Metastasis-associated protein MTA1 TTO4HUS GN MTA1 TTO4HUS FC As a part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Involved in the epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C, IFI16 and HDAC4/5/6-dependent manner. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression. Isoform Short binds to ESR1 and sequesters it in the cytoplasm and enhances its non-genomic responses. With TFCP2L1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation. Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. TTO4HUS PD 6G16; 5ICN; 5FXY; 4PC0; 4PBZ TTO4HUS SQ MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSTLIALADKHATLSVCYKAGPGADNGEEGEIEEEMENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTLLADKGEIRVGNRYQADITDLLKEGEEDGRDQSRLETQVWEAHNPLTDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNNVKAGVVNGTGAPGQSPGAGRACESCYTTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRSNMSPHGLPARSSGSPKFAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQSPLVLKQAVRKPLEAVLRYLETHPRPPKPDPVKSVSSVLSSLTPAKVAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGLANHGQARHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPPRPPPPAPVNDEPIVIED TTO4HUS TT Literature-reported TT1L79K ID TT1L79K TT1L79K TN Methionyl aminopeptidase 1 (METAP1) TT1L79K UP P53582 TT1L79K UC MAP11_HUMAN TT1L79K SN Peptidase M 1; Methionine aminopeptidase 1; MetAP 1; MAP 1; KIAA0094 TT1L79K GN METAP1 TT1L79K FC Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle. TT1L79K EC EC 3.4.11.18 TT1L79K PD 5YR7; 5YR6; 5YR5; 5YR4; 5YKP TT1L79K SQ MAAVETRVCETDGCSSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKDEKAKREVSSWTVEGDINTDPWAGYRYTGKLRPHYPLMPTRPVPSYIQRPDYADHPLGMSESEQALKGTSQIKLLSSEDIEGMRLVCRLAREVLDVAAGMIKPGVTTEEIDHAVHLACIARNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRPLQEGDIVNVDITLYRNGYHGDLNETFFVGEVDDGARKLVQTTYECLMQAIDAVKPGVRYRELGNIIQKHAQANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKSGHVFTIEPMICEGGWQDETWPDGWTAVTRDGKRSAQFEHTLLVTDTGCEILTRRLDSARPHFMSQF TT1L79K TT Literature-reported TTTUZ3O ID TTTUZ3O TTTUZ3O TN MLK-related kinase (MLTK) TTTUZ3O UP Q9NYL2 TTTUZ3O UC M3K20_HUMAN TTTUZ3O SN ZAK; Sterile alpha motif- and leucine zipper-containing kinase AZK; Mixed lineage kinase-related kinase; Mitogen-activated protein kinase kinase kinase MLT; Mitogen-activated protein kinase kinase kinase 20; MRK; MLTK; MLK-like mitogen-activated protein triple kinase; Leucine zipper- and sterile alpha motif-containing kinase; Human cervical cancer suppressor gene 4 protein; HCCS4; HCCS-4 TTTUZ3O GN MAP3K20 TTTUZ3O FC Stress-activated component of a protein kinase signal transduction cascade. Regulates the JNK and p38 pathways. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Pro-apoptotic. Role in regulation of S and G2 cell cycle checkpoint by direct phosphorylation of CHEK2. Involved in limb development. TTTUZ3O EC EC 2.7.11.25 TTTUZ3O PD 5X5O; 5HES TTTUZ3O SQ MSSLGASFVQIKFDDLQFFENCGGGSFGSVYRAKWISQDKEVAVKKLLKIEKEAEILSVLSHRNIIQFYGVILEPPNYGIVTEYASLGSLYDYINSNRSEEMDMDHIMTWATDVAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHNHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERLTIPSSCPRSFAELLHQCWEADAKKRPSFKQIISILESMSNDTSLPDKCNSFLHNKAEWRCEIEATLERLKKLERDLSFKEQELKERERRLKMWEQKLTEQSNTPLLPSFEIGAWTEDDVYCWVQQLVRKGDSSAEMSVYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKLTHDYINLFHFPPLIKDSGGEPEENEEKIVNLELVFGFHLKPGTGPQDCKWKMYMEMDGDEIAITYIKDVTFNTNLPDAEILKMTKPPFVMEKWIVGIAKSQTVECTVTYESDVRTPKSTKHVHSIQWSRTKPQDEVKAVQLAIQTLFTNSDGNPGSRSDSSADCQWLDTLRMRQIASNTSLQRSQSNPILGSPFFSHFDGQDSYAAAVRRPQVPIKYQQITPVNQSRSSSPTQYGLTKNFSSLHLNSRDSGFSSGNTDTSSERGRYSDRSRNKYGRGSISLNSSPRGRYSGKSQHSTPSRGRYPGKFYRVSQSALNPHQSPDFKRSPRDLHQPNTIPGMPLHPETDSRASEEDSKVSEGGWTKVEYRKKPHRPSPAKTNKERARGDHRGWRNF TTTUZ3O TT Literature-reported TTF8O7H ID TTF8O7H TTF8O7H TN Mycobacterium 30kDa major secretory protein (MycB fbpB) TTF8O7H UP P31952 TTF8O7H UC A85B_MYCTU TTF8O7H BC Acyltransferase TTF8O7H SN Mycolyl transferase 85B; Fibronectin-binding protein B; Extracellular alpha-antigen; Antigen 85B; Antigen 85 complex B; Ag85B; 85B; 30 kDa extracellular protein TTF8O7H GN MycB fbpB TTF8O7H FC Proteins of the antigen 85 complex are responsible for the high affinity of mycobacteria to fibronectin. Possesses a mycolyltransferase activity required for the biogenesis of trehalose dimycolate (cord factor). TTF8O7H PD 5TS1; 5TRZ; 1F0P; 1F0N TTF8O7H SQ MTDVSRKIRAWGRRLMIGTAAAVVLPGLVGLAGGAATAGAFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGNNSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSIVMPVGGQSSFYSDWYSPACGKAGCQTYKWETFLTSELPQWLSANRAVKPTGSAAIGLSMAGSSAMILAAYHPQQFIYAGSLSALLDPSQGMGPSLIGLAMGDAGGYKAADMWGPSSDPAWERNDPTQQIPKLVANNTRLWVYCGNGTPNELGGANIPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFPPNGTHSWEYWGAQLNAMKGDLQSSLGAG TTF8O7H TT Literature-reported TTHJWVK ID TTHJWVK TTHJWVK TN Mycobacterium Bisphosphoglycerate phosphoglycerate mutase (MycB gpmI) TTHJWVK UP P47669 TTHJWVK UC GPMI_MYCGE TTHJWVK BC Intramolecular transferases TTHJWVK SN gpmI; Phosphoglyceromutase; Phosphoglycerate mutase; IPGM; BPG-independent PGAM TTHJWVK GN MycB gpmI TTHJWVK FC Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. TTHJWVK SQ MHKKVLLAILDGYGISNAIYGNAVQNANTPMLDELINSYPCVLLDASGEAVGLPMGQIGNSEVGHLNIGAGRVVYTGLSLINQHIKDRSFFANKAFLKTIEHVEKNHSKIHLIGLFSNGGVHSHNEHLLALIELFSKHAKVVLHLFGDGRDVAPCSLKQDLEKLMIFLKNYPNVVIGTIGGRYYGMDRDQRWDREMIAYKALLGVSKNKFNDPIGYIETQYQNQITDEFIYPAINANLNSDQFALNNNDGVIFFNFRPDRARQMSHLIFNSNYYNYQPELKRKENLFFVTMMNYEGIVPSEFAFPPQTIKNSLGEVIANNNLKQLRIAETEKYAHVTFFFDGGFEVNLSNETKTLIPSLKVATYDLAPEMSCKAITDALLEKLNNFDFTVLNFANPDMVGHTGNYQACIKALEALDVQIKRIVDFCKANQITMFLTADHGNAEVMIDNNNNPVTKHTINPVPFVCTDKNVNFNQTGILANIAPTILEYLNLSKPKEMTAKSLLKNNN TTHJWVK TT Literature-reported TTHJWVK KE mge00010:Glycolysis / Gluconeogenesis; mge00260:Glycine, serine and threonine metabolism; mge00680:Methane metabolism; mge01100:Metabolic pathways; mge01110:Biosynthesis of secondary metabolites; mge01120:Microbial metabolism in diverse environments; mge01130:Biosynthesis of antibiotics; mge01200:Carbon metabolism; mge01230:Biosynthesis of amino acids TTLOHU4 ID TTLOHU4 TTLOHU4 TN Mycobacterium Decaprenylphosphoryl-beta-D-ribose oxidase (McyB dprE1) TTLOHU4 UP P9WJF1 TTLOHU4 UC DPRE1_MYCTU TTLOHU4 SN FAD-dependent decaprenylphosphoryl-beta-D-ribofuranose 2-oxidase; Decaprenylphosphoryl-beta-D-ribose oxidase; Decaprenylphosphoryl-beta-D-ribose 2-epimerase flavoprotein subunit; Decaprenylphosphoryl-beta-D-ribofuranose 2'-oxidase; Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE1; Decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase; Decaprenyl-phosphoribose 2'-epimerase subunit 1 TTLOHU4 GN McyB dprE1 TTLOHU4 FC Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans. DprE1 catalyzes the first step of epimerization, namely FAD-dependent oxidation of the C2' hydroxyl of DPR to yield the keto intermediate decaprenyl-phospho-2'-keto-D-arabinose (DPX). The intermediate DPX is then transferred to DprE2 subunit of the epimerase complex, most probably through a 'substrate channel' at the interface of DprE1-DprE2 complex. Can also use farnesyl-phosphoryl-beta-D-ribofuranose (FPR) as substrate in vitro. Appears to be essential for the growth and survival of M.tuberculosis. TTLOHU4 EC EC 1.1.98.3 TTLOHU4 PD 6HFW; 6HFV; 6HF3; 6HF0; 6HEZ TTLOHU4 SQ MLSVGATTTATRLTGWGRTAPSVANVLRTPDAEMIVKAVARVAESGGGRGAIARGLGRSYGDNAQNGGGLVIDMTPLNTIHSIDADTKLVDIDAGVNLDQLMKAALPFGLWVPVLPGTRQVTVGGAIACDIHGKNHHSAGSFGNHVRSMDLLTADGEIRHLTPTGEDAELFWATVGGNGLTGIIMRATIEMTPTSTAYFIADGDVTASLDETIALHSDGSEARYTYSSAWFDAISAPPKLGRAAVSRGRLATVEQLPAKLRSEPLKFDAPQLLTLPDVFPNGLANKYTFGPIGELWYRKSGTYRGKVQNLTQFYHPLDMFGEWNRAYGPAGFLQYQFVIPTEAVDEFKKIIGVIQASGHYSFLNVFKLFGPRNQAPLSFPIPGWNICVDFPIKDGLGKFVSELDRRVLEFGGRLYTAKDSRTTAETFHAMYPRVDEWISVRRKVDPLRVFASDMARRLELL TTLOHU4 TT Clinical trial TTAGENB ID TTAGENB TTAGENB TN Mycobacterium Malonyl-CoA:acyl carrier transacylase (MycB fabD) TTAGENB UP P63459 TTAGENB UC FABD_MYCBO TTAGENB BC Acyltransferase TTAGENB SN Malonyl CoA-acyl carrier protein transacylase; MCT TTAGENB GN MycB fabD TTAGENB FC Essential for the biosynthesis of fatty acids in all bacteria. Catalyzes the transacylation of malonate from malonyl-CoA to activated holo-ACP, to generate malonyl-ACP, which is an elongation substrate in fatty acid biosynthesis. TTAGENB EC EC 2.3.1.39 TTAGENB SQ MIALLAPGQGSQTEGMLSPWLQLPGAADQIAAWSKAADLDLARLGTTASTEEITDTAVAQPLIVAATLLAHQELARRCVLAGKDVIVAGHSVGEIAAYAIAGVIAADDAVALAATRGAEMAKACATEPTGMSAVLGGDETEVLSRLEQLDLVPANRNAAGQIVAAGRLTALEKLAEDPPAKARVRALGVAGAFHTEFMAPALDGFAAAAANIATADPTATLLSNRDGKPVTSAAAAMDTLVSQLTQPVRWDLCTATLREHTVTAIVEFPPAGTLSGIAKRELRGVPARAVKSPADLDELANL TTAGENB TT Literature-reported TTU3AL1 ID TTU3AL1 TTU3AL1 TN Mycobacterium Meta-cleavage product hydrolase (MycB HsaD) TTU3AL1 UP P9WNH5 TTU3AL1 UC HSAD_MYCTU TTU3AL1 SN Meta-cleavage product hydrolase; MCP hydrolase; HOPDA hydrolase; 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase; 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase TTU3AL1 GN MycB HsaD TTU3AL1 FC Catalyzes the hydrolysis of a carbon-carbon bond in 4,5: 9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate (4,9-DSHA) to yield 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oate (DOHNAA) and 2-hydroxy-hexa-2,4-dienoate (HHD). Is also able to catalyze the hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) and the synthetic analog 8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid (HOPODA). TTU3AL1 EC EC 3.7.1.17 TTU3AL1 PD 5JZS; 5JZB; 2WUG; 2WUF; 2WUE TTU3AL1 SQ MTATEELTFESTSRFAEVDVDGPLKLHYHEAGVGNDQTVVLLHGGGPGAASWTNFSRNIAVLARHFHVLAVDQPGYGHSDKRAEHGQFNRYAAMALKGLFDQLGLGRVPLVGNSLGGGTAVRFALDYPARAGRLVLMGPGGLSINLFAPDPTEGVKRLSKFSVAPTRENLEAFLRVMVYDKNLITPELVDQRFALASTPESLTATRAMGKSFAGADFEAGMMWREVYRLRQPVLLIWGREDRVNPLDGALVALKTIPRAQLHVFGQCGHWVQVEKFDEFNKLTIEFLGGGR TTU3AL1 TT Literature-reported TTOZVUM ID TTOZVUM TTOZVUM TN Mycobacterium Phosphoglucosamine mutase (MycB glmM) TTOZVUM UP A5U8B7 TTOZVUM UC GLMM_MYCTA TTOZVUM BC Intramolecular transferases TTOZVUM SN glmM of Mycobacterium tuberculosis TTOZVUM GN MycB glmM TTOZVUM FC Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. TTOZVUM EC EC 5.4.2.10 TTOZVUM SQ MGRLFGTDGVRGVANRELTAELALALGAAAARRLSRSGAPGRRVAVLGRDPRASGEMLEAAVIAGLTSEGVDALRVGVLPTPAVAYLTGAYDADFGVMISASHNPMPDNGIKIFGPGGHKLDDDTEDQIEDLVLGVSRGPGLRPAGAGIGRVIDAEDATERYLRHVAKAATARLDDLAVVVDCAHGAASSAAPRAYRAAGARVIAINAEPNGRNINDGCGSTHLDPLRAAVLAHRADLGLAHDGDADRCLAVDANGDLVDGDAIMVVLALAMKEAGELACNTLVATVMSNLGLHLAMRSAGVTVRTTAVGDRYVLEELRAGDYSLGGEQSGHIVMPALGSTGDGIVTGLRLMTRMVQTGSSLSDLASAMRTLPQVLINVEVVDKATAAAAPSVRTAVEQAAAELGDTGRILLRPSGTEPMIRVMVEAADEGVAQRLAATVADAVSTAR TTOZVUM TT Literature-reported TT0Z3HD ID TT0Z3HD TT0Z3HD TN Mycobacterium Sphingomyelinase (MycB spmT) TT0Z3HD UP P9WKQ1 TT0Z3HD UC SMASE_MYCTU TT0Z3HD BC SpmT family TT0Z3HD SN SMase TT0Z3HD GN MycB spmT TT0Z3HD FC Catalyzes the cleavage of sphingomyelin, a major lipid in eukaryotic cells, into ceramide and phosphocholine, which are then utilized by M.tuberculosis as carbon, nitrogen and phosphorus sources, respectively. Thus, enables M.tuberculosis to utilize sphingomyelin as a source of several essential nutrients for intracellular growth during infection. Furthermore, lyses erythrocytes and constitutes the main hemolytic factor of M.tuberculosis. TT0Z3HD EC EC 3.1.4.12 TT0Z3HD SQ MDYAKRIGQVGALAVVLGVGAAVTTHAIGSAAPTDPSSSSTDSPVDACSPLGGSASSLAAIPGASVPQVGVRQVDPGSIPDDLLNALIDFLAAVRNGLVPIIENRTPVANPQQVSVPEGGTVGPVRFDACDPDGNRMTFAVRERGAPGGPQHGIVTVDQRTASFIYTADPGFVGTDTFSVNVSDDTSLHVHGLAGYLGPFHGHDDVATVTVFVGNTPTDTISGDFSMLTYNIAGLPFPLSSAILPRFFYTKEIGKRLNAYYVANVQEDFAYHQFLIKKSKMPSQTPPEPPTLLWPIGVPFSDGLNTLSEFKVQRLDRQTWYECTSDNCLTLKGFTYSQMRLPGGDTVDVYNLHTNTGGGPTTNANLAQVANYIQQNSAGRAVIVTGDFNARYSDDQSALLQFAQVNGLTDAWVQVEHGPTTPPFAPTCMVGNECELLDKIFYRSGQGVTLQAVSYGNEAPKFFNSKGEPLSDHSPAVVGFHYVADNVAVR TT0Z3HD TT Literature-reported TTQAFX5 ID TTQAFX5 TTQAFX5 TN Myelin-oligodendrocyte glycoprotein (MOG) TTQAFX5 UP Q16653 TTQAFX5 UC MOG_HUMAN TTQAFX5 BC Immunoglobulin TTQAFX5 SN Myelinoligodendrocyte glycoprotein; MOG TTQAFX5 GN MOG TTQAFX5 FC Mediates homophilic cell-cell adhesion. Minor component of the myelin sheath. May be involved in completion and/or maintenance of the myelin sheath and in cell- cell communication. {ECO:0000250}. TTQAFX5 PD 1Q70 TTQAFX5 SQ MASLSRPSLPSCLCSFLLLLLLQVSSSYAGQFRVIGPRHPIRALVGDEVELPCRISPGKNATGMEVGWYRPPFSRVVHLYRNGKDQDGDQAPEYRGRTELLKDAIGEGKVTLRIRNVRFSDEGGFTCFFRDHSYQEEAAMELKVEDPFYWVSPGVLVLLAVLPVLLLQITVGLIFLCLQYRLRGKLRAEIENLHRTFDPHFLRVPCWKITLFVIVPVLGPLVALIICYNWLHRRLAGQFLEELRNPF TTQAFX5 TT Literature-reported TTHLGB2 ID TTHLGB2 TTHLGB2 TN Myosin light chain kinase 2 (MYLK2) TTHLGB2 UP Q9H1R3 TTHLGB2 UC MYLK2_HUMAN TTHLGB2 SN MYLK2 TTHLGB2 GN MYLK2 TTHLGB2 FC Implicated in the level of global muscle contraction and cardiac function. Phosphorylates a specific serine in the N-terminus of a myosin light chain. TTHLGB2 EC EC 2.7.11.18 TTHLGB2 PD 3KF9; 2LV6 TTHLGB2 SQ MATENGAVELGIQNPSTDKAPKGPTGERPLAAGKDPGPPDPKKAPDPPTLKKDAKAPASEKGDGTLAQPSTSSQGPKGEGDRGGGPAEGSAGPPAALPQQTATPETSVKKPKAEQGASGSQDPGKPRVGKKAAEGQAAARRGSPAFLHSPSCPAIISSSEKLLAKKPPSEASELTFEGVPMTHSPTDPRPAKAEEGKNILAESQKEVGEKTPGQAGQAKMQGDTSRGIEFQAVPSEKSEVGQALCLTAREEDCFQILDDCPPPPAPFPHRMVELRTGNVSSEFSMNSKEALGGGKFGAVCTCMEKATGLKLAAKVIKKQTPKDKEMVLLEIEVMNQLNHRNLIQLYAAIETPHEIVLFMEYIEGGELFERIVDEDYHLTEVDTMVFVRQICDGILFMHKMRVLHLDLKPENILCVNTTGHLVKIIDFGLARRYNPNEKLKVNFGTPEFLSPEVVNYDQISDKTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLSGNWYFDEETFEAVSDEAKDFVSNLIVKDQRARMNAAQCLAHPWLNNLAEKAKRCNRRLKSQILLKKYLMKRRWKKNFIAVSAANRFKKISSSGALMALGV TTHLGB2 TT Literature-reported TTY2TCU ID TTY2TCU TTY2TCU TN Myotubularin (MTM1) TTY2TCU UP Q13496 TTY2TCU UC MTM1_HUMAN TTY2TCU BC Phosphoric monoester hydrolase TTY2TCU SN MTM1 TTY2TCU GN MTM1 TTY2TCU FC Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine- containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis. TTY2TCU EC EC 3.1.3.95 TTY2TCU SQ MASASTSKYNSHSLENESIKRTSRDGVNRDLTEAVPRLPGETLITDKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSSLILDVPLGVISRIEKMGGATSRGENSYGLDITCKDMRNLRFALKQEGHSRRDMFEILTRYAFPLAHSLPLFAFLNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRITFINKCYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKDDEKYLDVIRETNKQISKLTIYDARPSVNAVANKATGGGYESDDAYHNAELFFLDIHNIHVMRESLKKVKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSFYRSIEGFEILVQKEWISFGHKFASRIGHGDKNHTDADRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLIIILDHLYSCRFGTFLFNCESARERQKVTERTVSLWSLINSNKEKFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRIKQQQPNPVEQRYMELLALRDEYIKRLEELQLANSAKLSDPPTSPSSPSQMMPHVQTHF TTY2TCU TT Literature-reported TTAZB7S ID TTAZB7S TTAZB7S TN N-acetylgalactosaminyltransferase 2 (CHPF) TTAZB7S UP Q8IZ52 TTAZB7S UC CHSS2_HUMAN TTAZB7S BC Hexosyltransferase TTAZB7S SN Nacetylgalactosaminylproteoglycan 3betaglucuronosyltransferase II; GlucuronosylNacetylgalactosaminylproteoglycan 4betaNacetylgalactosaminyltransferase II; Chondroitinpolymerizing factor; Chondroitin sulfate synthase 2; Chondroitin glucuronyltransferase 2; ChPF TTAZB7S GN CHPF TTAZB7S FC Has both beta-1,3-glucuronic acid and beta-1,4-N- acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Isoform 2 may facilitate PARK2 transport into the mitochondria. In collaboration with PARK2, isoform 2 may enhance cell viability and protect cells from oxidative stress. TTAZB7S EC EC 2.4.1.175 TTAZB7S SQ MRASLLLSVLRPAGPVAVGISLGFTLSLLSVTWVEEPCGPGPPQPGDSELPPRGNTNAARRPNSVQPGAEREKPGAGEGAGENWEPRVLPYHPAQPGQAAKKAVRTRYISTELGIRQRLLVAVLTSQTTLPTLGVAVNRTLGHRLERVVFLTGARGRRAPPGMAVVTLGEERPIGHLHLALRHLLEQHGDDFDWFFLVPDTTYTEAHGLARLTGHLSLASAAHLYLGRPQDFIGGEPTPGRYCHGGFGVLLSRMLLQQLRPHLEGCRNDIVSARPDEWLGRCILDATGVGCTGDHEGVHYSHLELSPGEPVQEGDPHFRSALTAHPVRDPVHMYQLHKAFARAELERTYQEIQELQWEIQNTSHLAVDGDQAAAWPVGIPAPSRPASRFEVLRWDYFTEQHAFSCADGSPRCPLRGADRADVADVLGTALEELNRRYHPALRLQKQQLVNGYRRFDPARGMEYTLDLQLEALTPQGGRRPLTRRVQLLRPLSRVEILPVPYVTEASRLTVLLPLAAAERDLAPGFLEAFATAALEPGDAAAALTLLLLYEPRQAQRVAHADVFAPVKAHVAELERRFPGARVPWLSVQTAAPSPLRLMDLLSKKHPLDTLFLLAGPDTVLTPDFLNRCRMHAISGWQAFFPMHFQAFHPAVAPPQGPGPPELGRDTGRFDRQAASEACFYNSDYVAARGRLAAASEQEEELLESLDVYELFLHFSSLHVLRAVEPALLQRYRAQTCSARLSEDLYHRCLQSVLEGLGSRTQLAMLLFEQEQGNST TTAZB7S TT Literature-reported TTQA8DT ID TTQA8DT TTQA8DT TN N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase (PIGL) TTQA8DT UP Q9Y2B2 TTQA8DT UC PIGL_HUMAN TTQA8DT BC Carbon-nitrogen hydrolase TTQA8DT SN Phosphatidylinositol-glycan biosynthesis, class L protein; PIGL; PIG-L; GlcNAc-PI de-N-acetylase TTQA8DT GN PIGL TTQA8DT FC Involved in thesecond step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol. TTQA8DT EC EC 3.5.1.89 TTQA8DT SQ MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPTVLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGMQWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVLTLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIFSRYMRINSLSFL TTQA8DT TT Literature-reported TTZCG0Q ID TTZCG0Q TTZCG0Q TN N-acylglucosamine 2-epimerase (RENBP) TTZCG0Q UP P51606 TTZCG0Q UC RENBP_HUMAN TTZCG0Q BC Racemases and epimerases TTZCG0Q SN RnBP; Renin-binding protein; RENBP; N-acetyl-D-glucosamine 2-epimerase; GlcNAc 2-epimerase; AGE TTZCG0Q GN RENBP TTZCG0Q FC Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. TTZCG0Q EC EC 5.1.3.8 TTZCG0Q SQ MSKGLPARQDMEKERETLQAWKERVGQELDRVVAFWMEHSHDQEHGGFFTCLGREGRVYDDLKYVWLQGRQVWMYCRLYRTFERFRHAQLLDAAKAGGEFLLRYARVAPPGKKCAFVLTRDGRPVKVQRTIFSECFYTMAMNELWRATGEVRYQTEAVEMMDQIVHWVQEDASGLGRPQLQGAPAAEPMAVPMMLLNLVEQLGEADEELAGKYAELGDWCARRILQHVQRDGQAVLENVSEGGKELPGCLGRQQNPGHTLEAGWFLLRHCIRKGDPELRAHVIDKFLLLPFHSGWDPDHGGLFYFQDADNFCPTQLEWAMKLWWPHSEAMIAFLMGYSDSGDPVLLRLFYQVAEYTFRQFRDPEYGEWFGYLSREGKVALSIKGGPFKGCFHVPRCLAMCEEMLGALLSRPAPAPSPAPTPACRGAE TTZCG0Q TT Literature-reported TTFMCB6 ID TTFMCB6 TTFMCB6 TN NAPE-hydrolyzing phospholipase D (NAPE-PLD) TTFMCB6 UP Q6IQ20 TTFMCB6 UC NAPEP_HUMAN TTFMCB6 SN NAPE-PLD; N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D; N-acyl phosphatidylethanolamine phospholipase D; C7orf18 TTFMCB6 GN NAPEPLD TTFMCB6 FC Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce N-acylethanolamines (NAEs) and phosphatidic acid. Responsible for the generation of these bioactive fatty acid ethanolamides (FAEs), including anandamide (N-arachidonoylethanolamine), the ligand of cannabinoid and vanilloid receptors. As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose (By similarity). TTFMCB6 EC EC 3.1.4.54 TTFMCB6 PD 4QN9 TTFMCB6 SQ MDENESNQSLMTSSQYPKEAVRKRQNSARNSGASDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNPSIPNVLRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGVREAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEHYLEPPVKLNEALERYGLNAEDFFVLKHGESRYLNNDDENF TTFMCB6 TT Literature-reported TTH2QRX ID TTH2QRX TTH2QRX TN Neuronal acetylcholine receptor alpha-5 (CHRNA5) TTH2QRX UP P30532 TTH2QRX UC ACHA5_HUMAN TTH2QRX BC Neurotransmitter receptor TTH2QRX SN NACHRA5; CHRNA5 TTH2QRX GN CHRNA5 TTH2QRX FC After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. TTH2QRX SQ MAARGSGPRALRLLLLVQLVAGRCGLAGAAGGAQRGLSEPSSIAKHEDSLLKDLFQDYERWVRPVEHLNDKIKIKFGLAISQLVDVDEKNQLMTTNVWLKQEWIDVKLRWNPDDYGGIKVIRVPSDSVWTPDIVLFDNADGRFEGTSTKTVIRYNGTVTWTPPANYKSSCTIDVTFFPFDLQNCSMKFGSWTYDGSQVDIILEDQDVDKRDFFDNGEWEIVSATGSKGNRTDSCCWYPYVTYSFVIKRLPLFYTLFLIIPCIGLSFLTVLVFYLPSNEGEKICLCTSVLVSLTVFLLVIEEIIPSSSKVIPLIGEYLVFTMIFVTLSIMVTVFAINIHHRSSSTHNAMAPLVRKIFLHTLPKLLCMRSHVDRYFTQKEETESGSGPKSSRNTLEAALDSIRYITRHIMKENDVREVVEDWKFIAQVLDRMFLWTFLFVSIVGSLGLFVPVIYKWANILIPVHIGNANK TTH2QRX TT Literature-reported TTH2QRX RC R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors; R-HSA-629597:Highly calcium permeable nicotinic acetylcholine receptors TTWAQU2 ID TTWAQU2 TTWAQU2 TN Neuropathy target esterase (PNPLA6) TTWAQU2 UP Q8IY17 TTWAQU2 UC PLPL6_HUMAN TTWAQU2 BC Carboxylic ester hydrolase TTWAQU2 SN Patatin-like phospholipase domain-containing protein 6; NTE TTWAQU2 GN PNPLA6 TTWAQU2 FC Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. TTWAQU2 EC EC 3.1.1.5 TTWAQU2 SQ MEAPLQTGMMGTSSHGLATNSSGAKVAERDGFQDVLAPGEGSAGRICGAQPVPFVPQVLGVMIGAGVAVVVTAVLILLVVRRLRVPKTPAPDGPRYRFRKRDKVLFYGRKIMRKVSQSTSSLVDTSVSATSRPRMRKKLKMLNIAKKILRIQKETPTLQRKEPPPAVLEADLTEGDLANSHLPSEVLYMLKNVRVLGHFEKPLFLELCRHMVFQRLGQGDYVFRPGQPDASIYVVQDGLLELCLPGPDGKECVVKEVVPGDSVNSLLSILDVITGHQHPQRTVSARAARDSTVLRLPVEAFSAVFTKYPESLVRVVQIIMVRLQRVTFLALHNYLGLTNELFSHEIQPLRLFPSPGLPTRTSPVRGSKRMVSTSATDEPRETPGRPPDPTGAPLPGPTGDPVKPTSLETPSAPLLSRCVSMPGDISGLQGGPRSDFDMAYERGRISVSLQEEASGGSLAAPARTPTQEPREQPAGACEYSYCEDESATGGCPFGPYQGRQTSSIFEAAKQELAKLMRIEDPSLLNSRVLLHHAKAGTIIARQGDQDVSLHFVLWGCLHVYQRMIDKAEDVCLFVAQPGELVGQLAVLTGEPLIFTLRAQRDCTFLRISKSDFYEIMRAQPSVVLSAAHTVAARMSPFVRQMDFAIDWTAVEAGRALYRQGDRSDCTYIVLNGRLRSVIQRGSGKKELVGEYGRGDLIGVVEALTRQPRATTVHAVRDTELAKLPEGTLGHIKRRYPQVVTRLIHLLSQKILGNLQQLQGPFPAGSGLGVPPHSELTNPASNLATVAILPVCAEVPMVAFTLELQHALQAIGPTLLLNSDIIRARLGASALDSIQEFRLSGWLAQQEDAHRIVLYQTDASLTPWTVRCLRQADCILIVGLGDQEPTLGQLEQMLENTAVRALKQLVLLHREEGAGPTRTVEWLNMRSWCSGHLHLRCPRRLFSRRSPAKLHELYEKVFSRRADRHSDFSRLARVLTGNTIALVLGGGGARGCSHIGVLKALEEAGVPVDLVGGTSIGSFIGALYAEERSASRTKQRAREWAKSMTSVLEPVLDLTYPVTSMFTGSAFNRSIHRVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSLWRYVRASMTLSGYLPPLCDPKDGHLLMDGGYINNLPADIARSMGAKTVIAIDVGSQDETDLSTYGDSLSGWWLLWKRLNPWADKVKVPDMAEIQSRLAYVSCVRQLEVVKSSSYCEYLRPPIDCFKTMDFGKFDQIYDVGYQYGKAVFGGWSRGNVIEKMLTDRRSTDLNESRRADVLAFPSSGFTDLAEIVSRIEPPTSYVSDGCADGEESDCLTEYEEDAGPDCSRDEGGSPEGASPSTASEMEEEKSILRQRRCLPQEPPGSATDA TTWAQU2 TT Literature-reported TT64REZ ID TT64REZ TT64REZ TN Neuropeptide Y (NPY) TT64REZ UP P01303 TT64REZ UC NPY_HUMAN TT64REZ SN Pro-neuropeptide Y TT64REZ GN NPY TT64REZ FC NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. TT64REZ PD 1RON; 1QFA TT64REZ SQ MLGNKRLGLSGLTLALSLLVCLGALAEAYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRYGKRSSPETLISDLLMRESTENVPRTRLEDPAMW TT64REZ TT Literature-reported TT64REZ KE hsa04024:cAMP signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa05034:Alcoholism TT64REZ RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events TTRXUVC ID TTRXUVC TTRXUVC TN Neuropilin-2 (NRP2) TTRXUVC UP O60462 TTRXUVC UC NRP2_HUMAN TTRXUVC BC Neuropilin and tolloid-like TTRXUVC SN Vascular endothelial cell growth factor 165 receptor 2; VEGF165R2; Neuropilin2 TTRXUVC GN NRP2 TTRXUVC FC High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF. TTRXUVC PD 6GH8; 5DQ0; 5DN2; 4QDS; 4QDR TTRXUVC SQ MDMFPLTWVFLALYFSRHQVRGQPDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWIVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSMLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPKMEIILQFLIFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSELRSSTGILSLTFHTDMAVAKDGFSARYYLVHQEPLENFQCNVPLGMESGRIANEQISASSTYSDGRWTPQQSRLHGDDNGWTPNLDSNKEYLQVDLRFLTMLTAIATQGAISRETQNGYYVKSYKLEVSTNGEDWMVYRHGKNHKVFQANNDATEVVLNKLHAPLLTRFVRIRPQTWHSGIALRLELFGCRVTDAPCSNMLGMLSGLIADSQISASSTQEYLWSPSAARLVSSRSGWFPRIPQAQPGEEWLQVDLGTPKTVKGVIIQGARGGDSITAVEARAFVRKFKVSYSLNGKDWEYIQDPRTQQPKLFEGNMHYDTPDIRRFDPIPAQYVRVYPERWSPAGIGMRLEVLGCDWTDSKPTVETLGPTVKSEETTTPYPTEEEATECGENCSFEDDKDLQLPSGFNCNFDFLEEPCGWMYDHAKWLRTTWASSSSPNDRTFPDDRNFLRLQSDSQREGQYARLISPPVHLPRSPVCMEFQYQATGGRGVALQVVREASQESKLLWVIREDQGGEWKHGRIILPSYDMEYQIVFEGVIGKGRSGEIAIDDIRISTDVPLENCMEPISAFAGENFKVDIPEIHEREGYEDEIDDEYEVDWSNSSSATSGSGAPSTDKEKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKVKMNHQKCCSEA TTRXUVC TT Literature-reported TTRXUVC FM Neuropilin family TT2JYUE ID TT2JYUE TT2JYUE TN Neurotrypsin (PRSS12) TT2JYUE UP P56730 TT2JYUE UC NETR_HUMAN TT2JYUE BC Peptidase TT2JYUE SN Serine protease 12; PRSS12; Motopsin; Leydin TT2JYUE GN PRSS12 TT2JYUE FC Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations. TT2JYUE EC EC 3.4.21.- TT2JYUE SQ MTLARFVLALMLGALPEVVGFDSVLNDSLHHSHRHSPPAGPHYPYYLPTQQRPPRTRPPPPLPRFPRPPRALPAQRPHALQAGHTPRPHPWGCPAGEPWVSVTDFGAPCLRWAEVPPFLERSPPASWAQLRGQRHNFCRSPDGAGRPWCFYGDARGKVDWGYCDCRHGSVRLRGGKNEFEGTVEVYASGVWGTVCSSHWDDSDASVICHQLQLGGKGIAKQTPFSGLGLIPIYWSNVRCRGDEENILLCEKDIWQGGVCPQKMAAAVTCSFSHGPTFPIIRLAGGSSVHEGRVELYHAGQWGTVCDDQWDDADAEVICRQLGLSGIAKAWHQAYFGEGSGPVMLDEVRCTGNELSIEQCPKSSWGEHNCGHKEDAGVSCTPLTDGVIRLAGGKGSHEGRLEVYYRGQWGTVCDDGWTELNTYVVCRQLGFKYGKQASANHFEESTGPIWLDDVSCSGKETRFLQCSRRQWGRHDCSHREDVSIACYPGGEGHRLSLGFPVRLMDGENKKEGRVEVFINGQWGTICDDGWTDKDAAVICRQLGYKGPARARTMAYFGEGKGPIHVDNVKCTGNERSLADCIKQDIGRHNCRHSEDAGVICDYFGKKASGNSNKESLSSVCGLRLLHRRQKRIIGGKNSLRGGWPWQVSLRLKSSHGDGRLLCGATLLSSCWVLTAAHCFKRYGNSTRSYAVRVGDYHTLVPEEFEEEIGVQQIVIHREYRPDRSDYDIALVRLQGPEEQCARFSSHVLPACLPLWRERPQKTASNCYITGWGDTGRAYSRTLQQAAIPLLPKRFCEERYKGRFTGRMLCAGNLHEHKRVDSCQGDSGGPLMCERPGESWVVYGVTSWGYGCGVKDSPGVYTKVSAFVPWIKSVTKL TT2JYUE TT Literature-reported TTKTLAI ID TTKTLAI TTKTLAI TN Neutrophil gelatinase-associated lipocalin (LCN2) TTKTLAI UP P80188 TTKTLAI UC NGAL_HUMAN TTKTLAI BC Calycin family TTKTLAI SN p25; Siderocalin LCN2; Oncogene 24p3; NGAL; Lipocalin-2; LCN2; 25 kDa alpha-2-microglobulin-related subunit of MMP-9 TTKTLAI GN LCN2 TTKTLAI FC Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5- DHBA), a siderophore that shares structural similarities withbacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis. Involved in innate immunity, possibly by sequestrating iron, leading to limit bacterial growth. . TTKTLAI PD 6GR0; 6GQZ; 5NKN; 5N48; 5N47 TTKTLAI SQ MPLGLLWLGLALLGALHAQAQDSTSDLIPAPPLSKVPLQQNFQDNQFQGKWYVVGLAGNAILREDKDPQKMYATIYELKEDKSYNVTSVLFRKKKCDYWIRTFVPGCQPGEFTLGNIKSYPGLTSYLVRVVSTNYNQHAMVFFKKVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG TTKTLAI TT Literature-reported TTO5QT2 ID TTO5QT2 TTO5QT2 TN NIMA-related kinase 1 (NEK1) TTO5QT2 UP Q96PY6 TTO5QT2 UC NEK1_HUMAN TTO5QT2 SN Serine/threonine-protein kinase Nek1; Renal carcinoma antigen NY-REN-55; NimA-related protein kinase 1; Never in mitosis A-related kinase 1; KIAA1901 TTO5QT2 GN NEK1 TTO5QT2 FC Phosphorylates serines and threonines, but also appears to possess tyrosine kinase activity. Involved in DNA damage checkpoint control and for proper DNA damage repair. In response to injury that includes DNA damage, NEK1 phosphorylates VDAC1 to limit mitochondrial cell death. May be implicated in the control of meiosis (By similarity). Involved in cilium assembly. TTO5QT2 EC EC 2.7.11.1 TTO5QT2 PD 4B9D; 4APC TTO5QT2 SQ MEKYVRLQKIGEGSFGKAILVKSTEDGRQYVIKEINISRMSSKEREESRREVAVLANMKHPNIVQYRESFEENGSLYIVMDYCEGGDLFKRINAQKGVLFQEDQILDWFVQICLALKHVHDRKILHRDIKSQNIFLTKDGTVQLGDFGIARVLNSTVELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYELCTLKHAFEAGSMKNLVLKIISGSFPPVSLHYSYDLRSLVSQLFKRNPRDRPSVNSILEKGFIAKRIEKFLSPQLIAEEFCLKTFSKFGSQPIPAKRPASGQNSISVMPAQKITKPAAKYGIPLAYKKYGDKKLHEKKPLQKHKQAHQTPEKRVNTGEERRKISEEAARKRRLEFIEKEKKQKDQIISLMKAEQMKRQEKERLERINRAREQGWRNVLSAGGSGEVKAPFLGSGGTIAPSSFSSRGQYEHYHAIFDQMQQQRAEDNEAKWKREIYGRGLPERGILPGVRPGFPYGAAGHHHFPDADDIRKTLKRLKAVSKQANANRQKGQLAVERAKQVEEFLQRKREAMQNKARAEGHMVYLARLRQIRLQNFNERQQIKAKLRGEKKEANHSEGQEGSEEADMRRKKIESLKAHANARAAVLKEQLERKRKEAYEREKKVWEEHLVAKGVKSSDVSPPLGQHETGGSPSKQQMRSVISVTSALKEVGVDSSLTDTRETSEEMQKTNNAISSKREILRRLNENLKAQEDEKGKQNLSDTFEINVHEDAKEHEKEKSVSSDRKKWEAGGQLVIPLDELTLDTSFSTTERHTVGEVIKLGPNGSPRRAWGKSPTDSVLKILGEAELQLQTELLENTTIRSEISPEGEKYKPLITGEKKVQCISHEINPSAIVDSPVETKSPEFSEASPQMSLKLEGNLEEPDDLETEILQEPSGTNKDESLPCTITDVWISEEKETKETQSADRITIQENEVSEDGVSSTVDQLSDIHIEPGTNDSQHSKCDVDKSVQPEPFFHKVVHSEHLNLVPQVQSVQCSPEESFAFRSHSHLPPKNKNKNSLLIGLSTGLFDANNPKMLRTCSLPDLSKLFRTLMDVPTVGDVRQDNLEIDEIEDENIKEGPSDSEDIVFEETDTDLQELQASMEQLLREQPGEEYSEEEESVLKNSDVEPTANGTDVADEDDNPSSESALNEEWHSDNSDGEIASECECDSVFNHLEELRLHLEQEMGFEKFFEVYEKIKAIHEDEDENIEICSKIVQNILGNEHQHLYAKILHLVMADGAYQEDNDE TTO5QT2 TT Literature-reported TTHOI91 ID TTHOI91 TTHOI91 TN NIMA-related kinase 6 (NEK6) TTHOI91 UP Q9HC98 TTHOI91 UC NEK6_HUMAN TTHOI91 BC Kinase TTHOI91 SN Serine/threonine-protein kinase Nek6; Protein kinase SID6-1512; NimA-related protein kinase 6; Never in mitosis A-related kinase 6 TTHOI91 GN NEK6 TTHOI91 FC Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence. Protein kinase which plays an important role in mitotic cell cycle progression. TTHOI91 EC EC 2.7.11.1 TTHOI91 SQ MAGQPGHMPHGGSSNNLCHTLGPVHPPDPQRHPNTLSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPGEHYSEKLRELVSMCICPDPHQRPDIGYVHQVAKQMHIWMSST TTHOI91 TT Literature-reported TTJ5SWP ID TTJ5SWP TTJ5SWP TN NIMA-related kinase 7 (NEK7) TTJ5SWP UP Q8TDX7 TTJ5SWP UC NEK7_HUMAN TTJ5SWP SN Serine/threonine-protein kinase Nek7; NimA-related protein kinase 7; Never in mitosis A-related kinase 7 TTJ5SWP GN NEK7 TTJ5SWP FC Protein kinase which plays an important role in mitotic cell cycle progression. Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. Phosphorylates RPS6KB1. TTJ5SWP EC EC 2.7.11.1 TTJ5SWP PD 6GT1; 5DE2; 2WQN; 2WQM TTJ5SWP SQ MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASS TTJ5SWP TT Literature-reported TTK2O1Q ID TTK2O1Q TTK2O1Q TN Nodal homolog (NODAL) TTK2O1Q UP Q96S42 TTK2O1Q UC NODAL_HUMAN TTK2O1Q BC Growth factor TTK2O1Q SN nodal growth differentiation factor; HTX5 TTK2O1Q GN NODAL TTK2O1Q FC Essential for mesoderm formation and axial patterning during embryonic development. TTK2O1Q PD 4N1D TTK2O1Q SQ MHAHCLPFLLHAWWALLQAGAATVATALLRTRGQPSSPSPLAYMLSLYRDPLPRADIIRSLQAEDVAVDGQNWTFAFDFSFLSQQEDLAWAELRLQLSSPVDLPTEGSLAIEIFHQPKPDTEQASDSCLERFQMDLFTVTLSQVTFSLGSMVLEVTRPLSKWLKHPGALEKQMSRVAGECWPRPPTPPATNVLLMLYSNLSQEQRQLGGSTLLWEAESSWRAQEGQLSWEWGKRHRRHHLPDRSQLCRKVKFQVDFNLIGWGSWIIYPKQYNAYRCEGECPNPVGEEFHPTNHAYIQSLLKRYQPHRVPSTCCAPVKTKPLSMLYVDNGRVLLDHHKDMIVEECGCL TTK2O1Q TT Literature-reported TTK2O1Q FM Transforming growth factor TTIGH2W ID TTIGH2W TTIGH2W TN Normal cross-reacting antigen (CD66c) TTIGH2W UP P40199 TTIGH2W UC CEAM6_HUMAN TTIGH2W BC Immunoglobulin TTIGH2W SN Nonspecific crossreacting antigen; Non-specific crossreacting antigen; NCA; Carcinoembryonic antigen-related cell adhesion molecule 6; CD66c antigen TTIGH2W GN CEACAM6 TTIGH2W FC Intercellular adhesion occurs in a calcium- and fibronectin-independent manner. Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM5 and CEACAM8. Heterophilic interaction with CEACAM8 occurs in activated neutrophils. Plays a role in neutrophil adhesion to cytokine-activated endothelial cells. Plays a role as an oncogene by promoting tumor progression; positively regulates cell migration, cell adhesion to endothelial cells and cell invasion. Also involved in the metastatic cascade process by inducing gain resistance to anoikis of pancreatic adenocarcinoma and colorectal carcinoma cells. Cell surface glycoprotein that plays a role in cell adhesion and tumor progression. TTIGH2W PD 4YIQ; 4Y8A; 4WTZ; 4WHC TTIGH2W SQ MGPPSAPPCRLHVPWKEVLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLAHNLPQNRIGYSWYKGERVDGNSLIVGYVIGTQQATPGPAYSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPEVQNTTYLWWVNGQSLPVSPRLQLSNGNMTLTLLSVKRNDAGSYECEIQNPASANRSDPVTLNVLYGPDGPTISPSKANYRPGENLNLSCHAASNPPAQYSWFINGTFQQSTQELFIPNITVNNSGSYMCQAHNSATGLNRTTVTMITVSGSAPVLSAVATVGITIGVLARVALI TTIGH2W TT Clinical trial TTIGH2W FM Immunoglobulin superfamily TTM9IYA ID TTM9IYA TTM9IYA TN NPR1 messenger RNA (NPR1 mRNA) TTM9IYA UP P16066 TTM9IYA UC ANPRA_HUMAN TTM9IYA BC mRNA target TTM9IYA SN NPR-A (mRNA); Guanylate cyclase A (mRNA); GC-A (mRNA); Atrial natriuretic peptide receptor type A (mRNA); Atrial natriuretic peptide receptor 1 (mRNA); ANPRA (mRNA); ANPR-A (mRNA); ANP-A (mRNA) TTM9IYA GN NPR1 TTM9IYA FC Has guanylate cyclase activity upon binding of the ligand. Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. TTM9IYA EC EC 4.6.1.2 TTM9IYA SQ MPGPRRPAGSRLRLLLLLLLPPLLLLLRGSHAGNLTVAVVLPLANTSYPWSWARVGPAVELALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAAVDLKWEHNPAVFLGPGCVYAAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWERQALMLYAYRPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGRVIYICSSPDAFRTLMLLALEAGLCGEDYVFFHLDIFGQSLQGGQGPAPRRPWERGDGQDVSARQAFQAAKIITYKDPDNPEYLEFLKQLKHLAYEQFNFTMEDGLVNTIPASFHDGLLLYIQAVTETLAHGGTVTDGENITQRMWNRSFQGVTGYLKIDSSGDRETDFSLWDMDPENGAFRVVLNYNGTSQELVAVSGRKLNWPLGYPPPDIPKCGFDNEDPACNQDHLSTLEVLALVGSLSLLGILIVSFFIYRKMQLEKELASELWRVRWEDVEPSSLERHLRSAGSRLTLSGRGSNYGSLLTTEGQFQVFAKTAYYKGNLVAVKRVNRKRIELTRKVLFELKHMRDVQNEHLTRFVGACTDPPNICILTEYCPRGSLQDILENESITLDWMFRYSLTNDIVKGMLFLHNGAICSHGNLKSSNCVVDGRFVLKITDYGLESFRDLDPEQGHTVYAKKLWTAPELLRMASPPVRGSQAGDVYSFGIILQEIALRSGVFHVEGLDLSPKEIIERVTRGEQPPFRPSLALQSHLEELGLLMQRCWAEDPQERPPFQQIRLTLRKFNRENSSNILDNLLSRMEQYANNLEELVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAVIDNFDVYKVETIGDAYMVVSGLPVRNGRLHACEVARMALALLDAVRSFRIRHRPQEQLRLRIGIHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGEALKIHLSSETKAVLEEFGGFELELRGDVEMKGKGKVRTYWLLGERGSSTRG TTM9IYA TT Literature-reported TTM9IYA FM mRNA target TTJQB49 ID TTJQB49 TTJQB49 TN Nuclear hormone receptor NOR-1 (NR4A3) TTJQB49 UP Q92570 TTJQB49 UC NR4A3_HUMAN TTJQB49 BC Nuclear hormone receptor family. NR4 subfamily TTJQB49 SN Neuron-derived orphan receptor 1; NOR1; Mitogen-induced nuclear orphan receptor; MINOR; CSMF; CHN TTJQB49 GN NR4A3 TTJQB49 FC Transcriptional activator that binds to regulatory elements in promoter regions in a cell- and response element (target)-specific manner. Induces gene expression by binding as monomers to the NR4A1 response element (NBRE) 5'-AAAAGGTCA-3' site and as homodimers to the Nur response element (NurRE) site in the promoter of their regulated target genes. Plays a role in the regulation of proliferation, survival and differentiation of many different cell types and also in metabolism and inflammation. Mediates proliferation of vascular smooth muscle, myeloid progenitor cell and type B pancreatic cells; promotes mitogen-induced vascular smooth muscle cell proliferation through transactivation of SKP2 promoter by binding a NBRE site. Upon PDGF stimulation, stimulates vascular smooth muscle cell proliferation by regulating CCND1 and CCND2 expression. In islets, induces type B pancreatic cell proliferation through up-regulation of genes that activate cell cycle, as well as genes that cause degradation of the CDKN1A. Negatively regulates myeloid progenitor cell proliferation by repressing RUNX1 in a NBRE site-independent manner. During inner ear, plays a role as a key mediator of the proliferative growth phase of semicircular canal development. Mediates also survival of neuron and smooth muscle cells; mediates CREB-induced neuronal survival, and during hippocampus development, plays a critical role in pyramidal cell survival and axonal guidance. Is required for S phase entry of the cell cycle and survival of smooth muscle cells by inducing CCND1, resulting in RB1 phosphorylation. Binds to NBRE motif in CCND1 promoter, resulting in the activation of the promoter and CCND1 transcription. Plays also a role in inflammation; upon TNF stimulation, mediates monocyte adhesion by inducing the expression of VCAM1 and ICAM1 by binding to the NBRE consensus site. In mast cells activated by Fc-epsilon receptor cross-linking, promotes the synthesis and release of cytokines but impairs events leading to degranulation. Plays also a role in metabolism; by modulating feeding behavior; and by playing a role in energy balance by inhibiting the glucocorticoid-induced orexigenic neuropeptides AGRP expression, at least in part by forming a complex with activated NR3C1 on the AGRP- glucocorticoid response element (GRE), and thus weakening the DNA binding activity of NR3C1. Upon catecholamines stimulation, regulates gene expression that controls oxidative metabolism in skeletal muscle. Plays a role in glucose transport by regulating translocation of the SLC2A4 glucose transporter to the cell surface (PubMed:24022864). Finally, during gastrulation plays a crucial role in the formation of anterior mesoderm by controlling cell migration. Inhibits adipogenesis. Also participates in cardiac hypertrophy by activating PARP1. TTJQB49 SQ MPCVQAQYSPSPPGSSYAAQTYSSEYTTEIMNPDYTKLTMDLGSTEITATATTSLPSISTFVEGYSSNYELKPSCVYQMQRPLIKVEEGRAPSYHHHHHHHHHHHHHHQQQHQQPSIPPASSPEDEVLPSTSMYFKQSPPSTPTTPAFPPQAGALWDEALPSAPGCIAPGPLLDPPMKAVPTVAGARFPLFHFKPSPPHPPAPSPAGGHHLGYDPTAAAALSLPLGAAAAAGSQAAALESHPYGLPLAKRAAPLAFPPLGLTPSPTASSLLGESPSLPSPPSRSSSSGEGTCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRFQKCLSVGMVKEVVRTDSLKGRRGRLPSKPKSPLQQEPSQPSPPSPPICMMNALVRALTDSTPRDLDYSRYCPTDQAAAGTDAEHVQQFYNLLTASIDVSRSWAEKIPGFTDLPKEDQTLLIESAFLELFVLRLSIRSNTAEDKFVFCNGLVLHRLQCLRGFGEWLDSIKDFSLNLQSLNLDIQALACLSALSMITERHGLKEPKRVEELCNKITSSLKDHQSKGQALEPTESKVLGALVELRKICTLGLQRIFYLKLEDLVSPPSIIDKLFLDTLPF TTJQB49 TT Literature-reported TTJQB49 KE hsa05202:Transcriptional misregulation in cancer TT65FL0 ID TT65FL0 TT65FL0 TN Omphalocele kinase 1 (NUAK1) TT65FL0 UP O60285 TT65FL0 UC NUAK1_HUMAN TT65FL0 BC Kinase TT65FL0 SN OMPHK1; NUAK family SNF1-like kinase 1; KIAA0537; ARK5; AMPK-related protein kinase 5 TT65FL0 GN NUAK1 TT65FL0 FC Phosphorylates ATM, CASP6, LATS1, PPP1R12A and p53/TP53. Acts as a regulator of cellular senescence and cellular ploidy by mediating phosphorylation of 'Ser-464' of LATS1, thereby controlling its stability. Controls cell adhesion by regulating activity of the myosin protein phosphatase 1 (PP1) complex. Acts by mediating phosphorylation of PPP1R12A subunit of myosin PP1: phosphorylated PPP1R12A then interacts with 14-3-3, leading to reduced dephosphorylation of myosin MLC2 by myosin PP1. May be involved in DNA damage response: phosphorylates p53/TP53 at 'Ser-15' and 'Ser-392' and is recruited to the CDKN1A/WAF1 promoter to participate to transcription activation by p53/TP53. May also act as a tumor malignancy-associated factor by promoting tumor invasion and metastasis under regulation and phosphorylation by AKT1. Suppresses Fas-induced apoptosis by mediating phosphorylation of CASP6, thereby suppressing the activation of the caspase and the subsequent cleavage of CFLAR. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with STK11, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair. Serine/threonine-protein kinase involved in various processes such as cell adhesion, regulation of cell ploidy and senescence, cell proliferation and tumor progression. TT65FL0 EC EC 2.7.11.1 TT65FL0 SQ MEGAAAPVAGDRPDLGLGAPGSPREAVAGATAALEPRKPHGVKRHHHKHNLKHRYELQETLGKGTYGKVKRATERFSGRVVAIKSIRKDKIKDEQDMVHIRREIEIMSSLNHPHIISIYEVFENKDKIVIIMEYASKGELYDYISERRRLSERETRHFFRQIVSAVHYCHKNGVVHRDLKLENILLDDNCNIKIADFGLSNLYQKDKFLQTFCGSPLYASPEIVNGRPYRGPEVDSWALGVLLYTLVYGTMPFDGFDHKNLIRQISSGEYREPTQPSDARGLIRWMLMVNPDRRATIEDIANHWWVNWGYKSSVCDCDALHDSESPLLARIIDWHHRSTGLQADTEAKMKGLAKPTTSEVMLERQRSLKKSKKENDFAQSGQDAVPESPSKLSSKRPKGILKKRSNSEHRSHSTGFIEGVVGPALPSTFKMEQDLCRTGVLLPSSPEAEVPGKLSPKQSATMPKKGILKKTQQRESGYYSSPERSESSELLDSNDVMGSSIPSPSPPDPARVTSHSLSCRRKGILKHSSKYSAGTMDPALVSPEMPTLESLSEPGVPAEGLSRSYSRPSSVISDDSVLSSDSFDLLDLQENRPARQRIRSCVSAENFLQIQDFEGLQNRPRPQYLKRYRNRLADSSFSLLTDMDDVTQVYKQALEICSKLN TT65FL0 TT Literature-reported TTY3LAZ ID TTY3LAZ TTY3LAZ TN Opioid receptor sigma 2 (PGRMC1) TTY3LAZ UP O00264 TTY3LAZ UC PGRC1_HUMAN TTY3LAZ BC GPCR rhodopsin TTY3LAZ SN mPR; PGRMC; Membraneassociated progesterone receptor component 1; Membrane-associated progesterone receptor component 1; IZA; HPR6.6; Dap1 TTY3LAZ GN PGRMC1 TTY3LAZ FC Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs). Component of a progesterone-binding protein complex. TTY3LAZ PD 4X8Y TTY3LAZ SQ MAAEDVVATGADPSDLESGGLLHEIFTSPLNLLLLGLCIFLLYKIVRGDQPAASGDSDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTAAQQETLSDWESQFTFKYHHVGKLLKEGEEPTVYSDEEEPKDESARKND TTY3LAZ TT Literature-reported TTY3LAZ FM GPCR rhodopsin TTTU49Q ID TTTU49Q TTTU49Q TN Optic atrophy protein 1 (OPA1) TTTU49Q UP O60313 TTTU49Q UC OPA1_HUMAN TTTU49Q BC Carbon-carbon hydrolase TTTU49Q SN OPA1; Dynaminlike 120 kDa protein, mitochondrial; Dynaminlike 120 kDa protein, form S1 TTTU49Q GN OPA1 TTTU49Q FC Dynamin-like 120 kDa protein, form S1: Inactive form produced by cleavage at S1 position by OMA1 following stress conditions that induce loss of mitochondrial membrane potential, leading to negative regulation of mitochondrial fusion. TTTU49Q EC EC 3.6.5.5 TTTU49Q SQ MWRLRRAAVACEVCQSLVKHSSGIKGSLPLQKLHLVSRSIYHSHHPTLKLQRPQLRTSFQQFSSLTNLPLRKLKFSPIKYGYQPRRNFWPARLATRLLKLRYLILGSAVGGGYTAKKTFDQWKDMIPDLSEYKWIVPDIVWEIDEYIDFEKIRKALPSSEDLVKLAPDFDKIVESLSLLKDFFTSGSPEETAFRATDRGSESDKHFRKVSDKEKIDQLQEELLHTQLKYQRILERLEKENKELRKLVLQKDDKGIHHRKLKKSLIDMYSEVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVTLSEGPHHVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVDAERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQIIEGKLFPMKALGYFAVVTGKGNSSESIEAIREYEEEFFQNSKLLKTSMLKAHQVTTRNLSLAVSDCFWKMVRESVEQQADSFKATRFNLETEWKNNYPRLRELDRNELFEKAKNEILDEVISLSQVTPKHWEEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPKGKEHDDIFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQARLKDTENAIENMVGPDWKKRWLYWKNRTQEQCVHNETKNELEKMLKCNEEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNLCRRGFYYYQRHFVDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKIKLLTGKRVQLAEDLKKVREIQEKLDAFIEALHQEK TTTU49Q TT Literature-reported TTU5HJP ID TTU5HJP TTU5HJP TN Orexin (HCRT) TTU5HJP UP O43612 TTU5HJP UC OREX_HUMAN TTU5HJP SN Hypocretin; Hcrt TTU5HJP GN HCRT TTU5HJP FC Neuropeptides that play a significant role in the regulationof food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. Orexin-A binds to both OX1R and OX2R with a high affinity, whereas orexin-B binds only to OX2R with a similar high affinity. TTU5HJP PD 1WSO; 1UVQ; 1R02; 1CQ0 TTU5HJP SQ MNLPSTKVSWAAVTLLLLLLLLPPALLSSGAAAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRSGPPGLQGRLQRLLQASGNHAAGILTMGRRAGAEPAPRPCLGRRCSAPAAASVAPGGQSGI TTU5HJP TT Literature-reported TTU5HJP RC R-HSA-416476:G alpha (q) signalling events TTTK36V ID TTTK36V TTTK36V TN Orphan nuclear receptor DAX-1 (NR0B1) TTTK36V UP P51843 TTTK36V UC NR0B1_HUMAN TTTK36V BC Nuclear hormone receptor TTTK36V SN Nuclear receptor subfamily 0 group B member 1; Nuclear receptor DAX-1; DSS-AHC critical region on the X chromosome protein 1; DAX1; AHC TTTK36V GN NR0B1 TTTK36V FC Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency. Orphan nuclear receptor. TTTK36V PD 4RWV TTTK36V SQ MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI TTTK36V TT Literature-reported TTTK36V FM Nuclear hormone receptor family TT9HKN3 ID TT9HKN3 TT9HKN3 TN Orphan nuclear receptor NURR1 (NR4A2) TT9HKN3 UP P43354 TT9HKN3 UC NR4A2_HUMAN TT9HKN3 BC Nuclear hormone receptor TT9HKN3 SN Transcriptionally-inducible nuclear receptor; Transcriptionally inducible nuclear receptor; TINUR; Nuclear receptor subfamily 4 group A member 2; NURR1; NOT; Immediate-early response protein NOT TT9HKN3 GN NR4A2 TT9HKN3 FC It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. TT9HKN3 PD 6DDA; 5YD6; 5Y41; 1OVL TT9HKN3 SQ MPCVQAQYGSSPQGASPASQSYSYHSSGEYSSDFLTPEFVKFSMDLTNTEITATTSLPSFSTFMDNYSTGYDVKPPCLYQMPLSGQQSSIKVEDIQMHNYQQHSHLPPQSEEMMPHSGSVYYKPSSPPTPTTPGFQVQHSPMWDDPGSLHNFHQNYVATTHMIEQRKTPVSRLSLFSFKQSPPGTPVSSCQMRFDGPLHVPMNPEPAGSHHVVDGQTFAVPNPIRKPASMGFPGLQIGHASQLLDTQVPSPPSRGSPSNEGLCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKSPQEPSPPSPPVSLISALVRAHVDSNPAMTSLDYSRFQANPDYQMSGDDTQHIQQFYDLLTGSMEIIRGWAEKIPGFADLPKADQDLLFESAFLELFVLRLAYRSNPVEGKLIFCNGVVLHRLQCVRGFGEWIDSIVEFSSNLQNMNIDISAFSCIAALAMVTERHGLKEPKRVEELQNKIVNCLKDHVTFNNGGLNRPNYLSKLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPAIIDKLFLDTLPF TT9HKN3 TT Literature-reported TT9HKN3 FM Zinc-finger TT25A9Q ID TT25A9Q TT25A9Q TN Orphan nuclear receptor SHP (NR0B2) TT25A9Q UP Q15466 TT25A9Q UC NR0B2_HUMAN TT25A9Q BC Nuclear hormone receptor TT25A9Q SN Small heterodimer partner; Short heterodimer partner; SHP; Nuclear receptor subfamily 0 group B member 2 TT25A9Q GN NR0B2 TT25A9Q FC Specifically inhibits transactivation of the nuclear receptor with which it interacts. Inhibits transcriptional activity of NEUROD1 on E-box-containing promoter by interfering with the coactivation function of the p300/CBP-mediated transcription complex for NEUROD1. Essential component of the liver circadian clock which via its interaction with NR1D1 and RORG regulates NPAS2-mediated hepatic lipid metabolism. Regulates the circadian expression of cytochrome P450 (CYP) enzymes. Represses: NR5A2 and HNF4A to down-regulate CYP2C38, NFLI3 to up-regulate CYP2A5, BHLHE41/HNF1A axis to up-regulate CYP1A2, CYP2E1 and CYP3A11, and NR1D1 to up-regulate CYP2B10, CYP4A10 and CYP4A14. Transcriptional regulator that acts as a negative regulator of receptor-dependent signaling pathways. TT25A9Q PD 5UFS; 4ONI; 4DOR; 2Z4J; 2Q3Y TT25A9Q SQ MSTSQPGACPCQGAASRPAILYALLSSSLKAVPRPRSRCLCRQHRPVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAEAPVPSILKKILLEEPSSSGGSGQLPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPDVPGLQAASHIGHLQQEAHWVLCEVLEPWCPAAQGRLTRVLLTASTLKSIPTSLLGDLFFRPIIGDVDIAGLLGDMLLLR TT25A9Q TT Literature-reported TT25A9Q FM Nuclear hormone receptor family TT71Q5Y ID TT71Q5Y TT71Q5Y TN Osteoclast-associated receptor (OSCAR) TT71Q5Y UP Q8IYS5 TT71Q5Y UC OSCAR_HUMAN TT71Q5Y BC Leukocyte receptor complex TT71Q5Y SN hOSCAR; Polymeric immunoglobulin receptor 3; PolyIg receptor 3; PIgR3; Osteoclastassociated immunoglobulinlike receptor; OSCAR TT71Q5Y GN OSCAR TT71Q5Y FC Regulator of osteoclastogenesis which plays an importantbone-specific function in osteoclast differentiation. TT71Q5Y PD 5EIV; 5EIQ; 5CJB; 5CJ8 TT71Q5Y SQ MALVLILQLLTLWPLCHTDITPSVPPASYHPKPWLGAQPATVVTPGVNVTLRCRAPQPAWRFGLFKPGEIAPLLFRDVSSELAEFFLEEVTPAQGGIYRCCYRRPDWGPGVWSQPSDVLELLVTEELPRPSLVALPGPVVGPGANVSLRCAGRLRNMSFVLYREGVAAPLQYRHSAQPWADFTLLGARAPGTYSCYYHTPSAPYVLSQRSEVLVISWEGEGPEARPASSAPGMQAPGPPPSDPGAQAPSLSSFRPRGLVLQPLLPQTQDSWDPAPPPSDPGV TT71Q5Y TT Literature-reported TT7ZY03 ID TT7ZY03 TT7ZY03 TN Oxidative stress responsive 1 (OXSR1) TT7ZY03 UP O95747 TT7ZY03 UC OXSR1_HUMAN TT7ZY03 SN Serine/threonine-protein kinase OSR1; Oxidative stress-responsive 1 protein; KIAA1101 TT7ZY03 GN OXSR1 TT7ZY03 FC Phosphorylates RELL1, RELL2 and RELT. Phosphorylates PAK1. Phosphorylates PLSCR1 in the presence of RELT. TT7ZY03 EC EC 2.7.11.1 TT7ZY03 PD 3DAK; 2VWI; 2V3S TT7ZY03 SQ MSEDSSALPWSINRDDYELQEVIGSGATAVVQAAYCAPKKEKVAIKRINLEKCQTSMDELLKEIQAMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKSGVLDESTIATILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPSLETGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAKNKEFLQEKTLQRAPTISERAKKVRRVPGSSGRLHKTEDGGWEWSDDEFDEESEEGKAAISQLRSPRVKESISNSELFPTTDPVGTLLQVPEQISAHLPQPAGQIATQPTQVSLPPTAEPAKTAQALSSGSGSQETKIPISLVLRLRNSKKELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLVIVAANLQKIVEEPQSNRSVTFKLASGVEGSDIPDDGKLIGFAQLSIS TT7ZY03 TT Literature-reported TTC6IX5 ID TTC6IX5 TTC6IX5 TN Oxidoreductase HTATIP2 (HTATIP2) TTC6IX5 UP Q9BUP3 TTC6IX5 UC HTAI2_HUMAN TTC6IX5 SN HIV-1 TAT-interactive protein 2; 30 kDa HIV-1 TAT-interacting protein TTC6IX5 GN HTATIP2 TTC6IX5 FC Oxidoreductase required for tumor suppression. NAPDH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. Isoform 1 is a metastasis suppressor with proapoptotic as well as antiangiogenic properties. Isoform 2 has an antiapoptotic effect. TTC6IX5 EC EC 1.1.1.- TTC6IX5 PD 2BKA TTC6IX5 SQ MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYASAFQGHDVGFCCLGTTRGKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSNFLYLQVKGEVEAKVEELKFDRYSVFRPGVLLCDRQESRPGEWLVRKFFGSLPDSWASGHSVPVVTVVRAMLNNVVRPRDKQMELLENKAIHDLGKAHGSLKP TTC6IX5 TT Literature-reported TTHW8O3 ID TTHW8O3 TTHW8O3 TN PAI-1 messenger RNA (PAI-1 mRNA) TTHW8O3 UP P05121 TTHW8O3 UC PAI1_HUMAN TTHW8O3 BC mRNA target TTHW8O3 SN Serpin E1 (mRNA); Plasminogen activator inhibitor type 1 (mRNA); Plasminogen activator inhibitor 1 (mRNA); PLANH1 (mRNA); PAI1 (mRNA); PAI-1 (mRNA); PAI (mRNA); Endothelial plasminogen activator inhibitor (mRNA) TTHW8O3 GN SERPINE1 TTHW8O3 FC Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair. It is involved in cellular and replicative senescence. Plays a role in alveolar type 2 cells senescence in the lung. Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis. Serine protease inhibitor. TTHW8O3 PD 9PAI; 6I8S; 5ZLZ; 5BRR; 4IC0 TTHW8O3 SQ MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP TTHW8O3 TT Literature-reported TTHW8O3 FM mRNA target TT79U1M ID TT79U1M TT79U1M TN Pancreatic eIF2-alpha kinase (HsPEK) TT79U1M UP Q9NZJ5 TT79U1M UC E2AK3_HUMAN TT79U1M SN PERK; HsPEK; Eukaryotic translation initiation factor 2-alpha kinase 3 TT79U1M GN EIF2AK3 TT79U1M FC Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' during the unfolded protein response (UPR) and in response to low amino acid availability. Converts phosphorylated eIF-2-alpha/EIF2S1 either in a global protein synthesis inhibitor, leading to a reduced overall utilization of amino acids, or to a translation initiation activator of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function. TT79U1M EC EC 2.7.11.1 TT79U1M PD 5SV7; 4YZS; 4X7O; 4X7N; 4X7L TT79U1M SQ MERAISPGLLVRALLLLLLLLGLAARTVAAGRARGLPAPTAEAAFGLGAAAAPTSATRVPAAGAVAAAEVTVEDAEALPAAAGEQEPRGPEPDDETELRPRGRSLVIISTLDGRIAALDPENHGKKQWDLDVGSGSLVSSSLSKPEVFGNKMIIPSLDGALFQWDQDRESMETVPFTVESLLESSYKFGDDVVLVGGKSLTTYGLSAYSGKVRYICSALGCRQWDSDEMEQEEDILLLQRTQKTVRAVGPRSGNEKWNFSVGHFELRYIPDMETRAGFIESTFKPNENTEESKIISDVEEQEAAIMDIVIKVSVADWKVMAFSKKGGHLEWEYQFCTPIASAWLLKDGKVIPISLFDDTSYTSNDDVLEDEEDIVEAARGATENSVYLGMYRGQLYLQSSVRISEKFPSSPKALESVTNENAIIPLPTIKWKPLIHSPSRTPVLVGSDEFDKCLSNDKFSHEEYSNGALSILQYPYDNGYYLPYYKRERNKRSTQITVRFLDNPHYNKNIRKKDPVLLLHWWKEIVATILFCIIATTFIVRRLFHPHPHRQRKESETQCQTENKYDSVSGEANDSSWNDIKNSGYISRYLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAIKRIRLPNRELAREKVMREVKALAKLEHPGIVRYFNAWLEAPPEKWQEKMDEIWLKDESTDWPLSSPSPMDAPSVKIRRMDPFATKEHIEIIAPSPQRSRSFSVGISCDQTSSSESQFSPLEFSGMDHEDISESVDAAYNLQDSCLTDCDVEDGTMDGNDEGHSFELCPSEASPYVRSRERTSSSIVFEDSGCDNASSKEEPKTNRLHIGNHCANKLTAFKPTSSKSSSEATLSISPPRPTTLSLDLTKNTTEKLQPSSPKVYLYIQMQLCRKENLKDWMNGRCTIEERERSVCLHIFLQIAEAVEFLHSKGLMHRDLKPSNIFFTMDDVVKVGDFGLVTAMDQDEEEQTVLTPMPAYARHTGQVGTKLYMSPEQIHGNSYSHKVDIFSLGLILFELLYPFSTQMERVRTLTDVRNLKFPPLFTQKYPCEYVMVQDMLSPSPMERPEAINIIENAVFEDLDFPGKTVLRQRSRSLSSSGTKHSRQSNNSHSPLPSN TT79U1M TT Literature-reported TTC0V1J ID TTC0V1J TTC0V1J TN PAS domain-containing serine/threonine-protein kinase (PASK) TTC0V1J UP Q96RG2 TTC0V1J UC PASK_HUMAN TTC0V1J SN hPASK; PASKIN; PAS-kinase; KIAA0135 TTC0V1J GN PASK TTC0V1J FC Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate to respiratory regulation. TTC0V1J EC EC 2.7.11.1 TTC0V1J PD 3DLS; 1LL8 TTC0V1J SQ MEDGGLTAFEEDQRCLSQSLPLPVSAEGPAAQTTAEPSRSFSSAHRHLSRRNGLSRLCQSRTALSEDRWSSYCLSSLAAQNICTSKLHCPAAPEHTDPSEPRGSVSCCSLLRGLSSGWSSPLLPAPVCNPNKAIFTVDAKTTEILVANDKACGLLGYSSQDLIGQKLTQFFLRSDSDVVEALSEEHMEADGHAAVVFGTVVDIISRSGEKIPVSVWMKRMRQERRLCCVVVLEPVERVSTWVAFQSDGTVTSCDSLFAHLHGYVSGEDVAGQHITDLIPSVQLPPSGQHIPKNLKIQRSVGRARDGTTFPLSLKLKSQPSSEEATTGEAAPVSGYRASVWVFCTISGLITLLPDGTIHGINHSFALTLFGYGKTELLGKNITFLIPGFYSYMDLAYNSSLQLPDLASCLDVGNESGCGERTLDPWQGQDPAEGGQDPRINVVLAGGHVVPRDEIRKLMESQDIFTGTQTELIAGGQLLSCLSPQPAPGVDNVPEGSLPVHGEQALPKDQQITALGREEPVAIESPGQDLLGESRSEPVDVKPFASCEDSEAPVPAEDGGSDAGMCGLCQKAQLERMGVSGPSGSDLWAGAAVAKPQAKGQLAGGSLLMHCPCYGSEWGLWWRSQDLAPSPSGMAGLSFGTPTLDEPWLGVENDREELQTCLIKEQLSQLSLAGALDVPHAELVPTECQAVTAPVSSCDLGGRDLCGGCTGSSSACYALATDLPGGLEAVEAQEVDVNSFSWNLKELFFSDQTDQTSSNCSCATSELRETPSSLAVGSDPDVGSLQEQGSCVLDDRELLLLTGTCVDLGQGRRFRESCVGHDPTEPLEVCLVSSEHYAASDRESPGHVPSTLDAGPEDTCPSAEEPRLNVQVTSTPVIVMRGAAGLQREIQEGAYSGSCYHRDGLRLSIQFEVRRVELQGPTPLFCCWLVKDLLHSQRDSAARTRLFLASLPGSTHSTAAELTGPSLVEVLRARPWFEEPPKAVELEGLAACEGEYSQKYSTMSPLGSGAFGFVWTAVDKEKNKEVVVKFIKKEKVLEDCWIEDPKLGKVTLEIAILSRVEHANIIKVLDIFENQGFFQLVMEKHGSGLDLFAFIDRHPRLDEPLASYIFRQLVSAVGYLRLKDIIHRDIKDENIVIAEDFTIKLIDFGSAAYLERGKLFYTFCGTIEYCAPEVLMGNPYRGPELEMWSLGVTLYTLVFEENPFCELEETVEAAIHPPYLVSKELMSLVSGLLQPVPERRTTLEKLVTDPWVTQPVNLADYTWEEVFRVNKPESGVLSAASLEMGNRSLSDVAQAQELCGGPVPGEAPNGQGCLHPGDPRLLTS TTC0V1J TT Literature-reported TTSCHFW ID TTSCHFW TTSCHFW TN Peptidyl arginine deiminase type III (PADI3) TTSCHFW UP Q9ULW8 TTSCHFW UC PADI3_HUMAN TTSCHFW SN Protein-arginine deiminase type-3; Protein-arginine deiminase type III; Peptidylarginine deiminase III; PDI3; PAD3 TTSCHFW GN PADI3 TTSCHFW FC Catalyzes the deimination of arginine residues of proteins. TTSCHFW EC EC 3.5.3.15 TTSCHFW PD 6CE1 TTSCHFW SQ MSLQRIVRVSLEHPTSAVCVAGVETLVDIYGSVPEGTEMFEVYGTPGVDIYISPNMERGRERADTRRWRFDATLEIIVVMNSPSNDLNDSHVQISYHSSHEPLPLAYAVLYLTCVDISLDCDLNCEGRQDRNFVDKRQWVWGPSGYGGILLVNCDRDDPSCDVQDNCDQHVHCLQDLEDMSVMVLRTQGPAALFDDHKLVLHTSSYDAKRAQVFHICGPEDVCEAYRHVLGQDKVSYEVPRLHGDEERFFVEGLSFPDAGFTGLISFHVTLLDDSNEDFSASPIFTDTVVFRVAPWIMTPSTLPPLEVYVCRVRNNTCFVDAVAELARKAGCKLTICPQAENRNDRWIQDEMELGYVQAPHKTLPVVFDSPRNGELQDFPYKRILGPDFGYVTREPRDRSVSGLDSFGNLEVSPPVVANGKEYPLGRILIGGNLPGSSGRRVTQVVRDFLHAQKVQPPVELFVDWLAVGHVDEFLSFVPAPDGKGFRMLLASPGACFKLFQEKQKCGHGRALLFQGVVDDEQVKTISINQVLSNKDLINYNKFVQSCIDWNREVLKRELGLAECDIIDIPQLFKTERKKATAFFPDLVNMLVLGKHLGIPKPFGPIINGCCCLEEKVRSLLEPLGLHCTFIDDFTPYHMLHGEVHCGTNVCRKPFSFKWWNMVP TTSCHFW TT Literature-reported TT0NZIC ID TT0NZIC TT0NZIC TN Phenylethanolamine N-methyltransferase (PNMT) TT0NZIC UP P11086 TT0NZIC UC PNMT_HUMAN TT0NZIC SN PNMTase; PENT; Noradrenaline N-methyltransferase TT0NZIC GN PNMT TT0NZIC FC Converts noradrenaline to adrenaline. TT0NZIC EC EC 2.1.1.28 TT0NZIC PD 4MQ4; 4MIK; 4DM3; 3KR2; 3KR1 TT0NZIC SQ MSGADRSPNAGAAPDSAPGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEEPGAFNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVREALVRSGYKVRDLRTYIMPAHLQTGVDDVKGVFFAWAQKVGL TT0NZIC TT Literature-reported TT735V2 ID TT735V2 TT735V2 TN Phosphatidylethanolamine N-methyltransferase (PEMT) TT735V2 UP Q9UBM1 TT735V2 UC PEMT_HUMAN TT735V2 BC Methyltransferase TT735V2 SN PEMT2; PEAMT TT735V2 GN PEMT TT735V2 FC Catalyzes three sequential methylation of phosphatidylethanolamine (pe) by adomet, thus producing phosphatidylcholine (pc). TT735V2 EC EC 2.1.1.17 TT735V2 SQ MTRLLGYVDPLDPSFVAAVITITFNPLYWNVVARWEHKTRKLSRAFGSPYLACYSLSVTILLLNFLRSHCFTQAMLSQPRMESLDTPAAYSLGLALLGLGVVLVLSSFFALGFAGTFLGDYFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIVALLYEEPFTAEIYRQKASGSHKRS TT735V2 TT Literature-reported TT1BGU8 ID TT1BGU8 TT1BGU8 TN Phosphatidylethanolamine-binding protein 1 (PEBP1) TT1BGU8 UP P30086 TT1BGU8 UC PEBP1_HUMAN TT1BGU8 BC Phosphatidylethanolamine-binding protein family TT1BGU8 SN Raf kinase inhibitor protein; RKIP; Prostatic-binding protein; PEBP-1; PEBP; PBP; Neuropolypeptide h3; Hippocampal cholinergic neurostimulating peptide; HCNPpp; HCNP TT1BGU8 GN PEBP1 TT1BGU8 FC Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase. Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation. TT1BGU8 PD 2QYQ; 2L7W; 1BEH; 1BD9 TT1BGU8 SQ MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSGTVLSDYVGSGPPKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK TT1BGU8 TT Literature-reported TTNPL3B ID TTNPL3B TTNPL3B TN Phosphatidylinositol-4-kinase beta (PI4KB) TTNPL3B UP Q9UBF8 TTNPL3B UC PI4KB_HUMAN TTNPL3B SN PtdIns 4-kinase beta; Phosphatidylinositol 4-kinase beta; PIK4CB; PI4Kbeta; PI4K92; PI4K-beta; NPIK TTNPL3B GN PI4KB TTNPL3B FC Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By similarity). TTNPL3B EC EC 2.7.1.67 TTNPL3B PD 6GL3; 5NAS; 5LX2; 5FBW; 5FBV TTNPL3B SQ MGDTVVEPAPLKPTSEPTSGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAVSSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGAAVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM TTNPL3B TT Literature-reported TTTWC79 ID TTTWC79 TTTWC79 TN Phosphodiesterase 11A (PDE11A) TTTWC79 UP Q9HCR9 TTTWC79 UC PDE11_HUMAN TTTWC79 BC Phosphoric diester hydrolase TTTWC79 SN cAMP and cGMP phosphodiesterase 11A; Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A TTTWC79 GN PDE11A TTTWC79 FC Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively. Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. TTTWC79 EC EC 3.1.4.35 TTTWC79 SQ MAASRLDFGEVETFLDRHPELFEDYLMRKGKQEMVEKWLQRHSQGQGALGPRPSLAGTSSLAHSTCRGGSSVGGGTGPNGSAHSQPLPGGGDCGGVPLSPSWAGGSRGDGNLQRRASQKELRKSFARSKAIHVNRTYDEQVTSRAQEPLSSVRRRALLRKASSLPPTTAHILSALLESRVNLPRYPPTAIDYKCHLKKHNERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEGAAAGKKTLVSKFFDVHAGTPLLPCSSTENSNEVQVPWGKGIIGYVGEHGETVNIPDAYQDRRFNDEIDKLTGYKTKSLLCMPIRSSDGEIIGVAQAINKIPEGAPFTEDDEKVMQMYLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVKFTKSFELMSPKCSADAENSFKESMEKSSYSDWLINNSIAELVASTGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNSNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQSVALDVLSYHATCSKAEVDKFKAANIPLVSELAIDDIHFDDFSLDVDAMITAALRMFMELGMVQKFKIDYETLCRWLLTVRKNYRMVLYHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSALAQLYGTSATLEHHHFNHAVMILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGEYDWNIKNHRDIFRSMLMTACDLGAVTKPWEISRQVAELVTSEFFEQGDRERLELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNVKLKPMLDSVATNRSKWEELHQKRLLASTASSSPASVMVAKEDRN TTTWC79 TT Literature-reported TTBYG4O ID TTBYG4O TTBYG4O TN Phospholipase A2 group IVC (PLA2G4C) TTBYG4O UP Q9UP65 TTBYG4O UC PA24C_HUMAN TTBYG4O BC Carboxylic ester hydrolase TTBYG4O SN cPLA2-gamma; PLA2G4C TTBYG4O GN PLA2G4C TTBYG4O FC Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid. TTBYG4O EC EC 3.1.1.4 TTBYG4O SQ MGSSEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYTNDGDMEALEADLKHRFTRQEWDLAKSLQKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQPSWQEARAPETWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWGSALGNTEVIREYIFDQLRNLTLKGLWRRAVANAKSIGHLIFARLLRLQESSQGEHPPPEDEGGEPEHTWLTEMLENWTRTSLEKQEQPHEDPERKGSLSNLMDFVKKTGICASKWEWGTTHNFLYKHGGIRDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFETIRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDIEAWSDTYDTFKLADTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLYYPKDSARSCCLA TTBYG4O TT Literature-reported TTLPGU7 ID TTLPGU7 TTLPGU7 TN Phospholipase C-beta-1 (PLCB1) TTLPGU7 UP Q9NQ66 TTLPGU7 UC PLCB1_HUMAN TTLPGU7 BC Phosphoric diester hydrolase TTLPGU7 SN Phospholipase C-beta1; Phospholipase C-I; Phosphoinositide phospholipase C-beta-1; Phosphoinositide phospholipase C; PLC-beta-1; PLC-I; PLC-154; KIAA0581; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 TTLPGU7 GN PLCB1 TTLPGU7 FC The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. TTLPGU7 EC EC 3.1.4.11 TTLPGU7 SQ MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLSGEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKKKLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYLRRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKPKLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSSEELGGDIPGKEFDTPL TTLPGU7 TT Literature-reported TTLPGU7 FM Phosphoric diester hydrolases TTXMI0C ID TTXMI0C TTXMI0C TN Phosphomevalonate kinase (PMVK) TTXMI0C UP Q15126 TTXMI0C UC PMVK_HUMAN TTXMI0C SN hPMK; PMKase; PMKI TTXMI0C GN PMVK TTXMI0C FC Regulated in response to dietary sterol levels and that this regulation is coordinate with 3-hydroxy-3-methylglutaryl coenzyme A reductase, the rate-limiting enzyme of cholesterol biosynthesis. TTXMI0C EC EC 2.7.4.2 TTXMI0C PD 3CH4 TTXMI0C SQ MAPLGGAPRLVLLFSGKRKSGKDFVTEALQSRLGADVCAVLRLSGPLKEQYAQEHGLNFQRLLDTSTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQPIWLVSDTRRVSDIQWFREAYGAVTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDWVIENHGVEQRLEEQLENLIEFIRSRL TTXMI0C TT Literature-reported TTI5WS6 ID TTI5WS6 TTI5WS6 TN Phosphorylase kinase testis gamma 2 (PHKG2) TTI5WS6 UP P15735 TTI5WS6 UC PHKG2_HUMAN TTI5WS6 SN Phosphorylase kinase subunit gamma-2; Phosphorylase b kinase gamma catalytic chain, liver/testis isoform; PSK-C3; PHK-gamma-T; PHK-gamma-LT TTI5WS6 GN PHKG2 TTI5WS6 FC Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. May regulate glycogeneolysis in the testis. In vitro, phosphorylates PYGM (By similarity). TTI5WS6 EC EC 2.7.11.19 TTI5WS6 PD 2Y7J TTI5WS6 SQ MTLDVGPEDELPDWAAAKEFYQKYDPKDVIGRGVSSVVRRCVHRATGHEFAVKIMEVTAERLSPEQLEEVREATRRETHILRQVAGHPHIITLIDSYESSSFMFLVFDLMRKGELFDYLTEKVALSEKETRSIMRSLLEAVSFLHANNIVHRDLKPENILLDDNMQIRLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKCSMDETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQILMLRMIMEGQYQFSSPEWDDRSSTVKDLISRLLQVDPEARLTAEQALQHPFFERCEGSQPWNLTPRQRFRVAVWTVLAAGRVALSTHRVRPLTKNALLRDPYALRSVRHLIDNCAFRLYGHWVKKGEQQNRAALFQHRPPGPFPIMGPEEEGDSAAITEDEAVLVLG TTI5WS6 TT Literature-reported TTB4S01 ID TTB4S01 TTB4S01 TN PKC-delta-interacting protein kinase (RIPK4) TTB4S01 UP P57078 TTB4S01 UC RIPK4_HUMAN TTB4S01 BC Protein kinase superfamily. TKL Ser/Thr protein kinase family TTB4S01 SN DIK; Ankyrin repeat domain-containing protein 3; ANKRD3 TTB4S01 GN RIPK4 TTB4S01 FC Involved in stratified epithelial development. It is a direct transcriptional target of TP63. Plays a role in NF-kappa-B activation. TTB4S01 EC EC 2.7.11.1 TTB4S01 SQ MEGDGGTPWALALLRTFDAGEFTGWEKVGSGGFGQVYKVRHVHWKTWLAIKCSPSLHVDDRERMELLEEAKKMEMAKFRYILPVYGICREPVGLVMEYMETGSLEKLLASEPLPWDLRFRIIHETAVGMNFLHCMAPPLLHLDLKPANILLDAHYHVKISDFGLAKCNGLSHSHDLSMDGLFGTIAYLPPERIREKSRLFDTKHDVYSFAIVIWGVLTQKKPFADEKNILHIMVKVVKGHRPELPPVCRARPRACSHLIRLMQRCWQGDPRVRPTFQGNGLNGELIRQVLAALLPVTGRWRSPGEGFRLESEVIIRVTCPLSSPQEITSETEDLCEKPDDEVKETAHDLDVKSPPEPRSEVVPARLKRASAPTFDNDYSLSELLSQLDSGVSQAVEGPEELSRSSSESKLPSSGSGKRLSGVSSVDSAFSSRGSLSLSFEREPSTSDLGTTDVQKKKLVDAIVSGDTSKLMKILQPQDVDLALDSGASLLHLAVEAGQEECAKWLLLNNANPNLSNRRGSTPLHMAVERRVRGVVELLLARKISVNAKDEDQWTALHFAAQNGDESSTRLLLEKNASVNEVDFEGRTPMHVACQHGQENIVRILLRRGVDVSLQGKDAWLPLHYAAWQGHLPIVKLLAKQPGVSVNAQTLDGRTPLHLAAQRGHYRVARILIDLCSDVNVCSLLAQTPLHVAAETGHTSTARLLLHRGAGKEAMTSDGYTALHLAARNGHLATVKLLVEEKADVLARGPLNQTALHLAAAHGHSEVVEELVSADVIDLFDEQGLSALHLAAQGRHAQTVETLLRHGAHINLQSLKFQGGHGPAATLLRRSKT TTB4S01 TT Literature-reported TT0C8BY ID TT0C8BY TT0C8BY TN Plasma retinol-binding protein (RBP4) TT0C8BY UP P02753 TT0C8BY UC RET4_HUMAN TT0C8BY BC Calycin family TT0C8BY SN Retinol-binding protein 4; RBP4; RBP; Plasma retinol-binding protein(1-176); PRBP TT0C8BY GN RBP4 TT0C8BY FC Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli. TT0C8BY PD 5NUB; 5NUA; 5NU9; 5NU8; 5NU7 TT0C8BY SQ MKWVWALLLLAALGSGRAERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDETGQMSATAKGRVRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSCRLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELCLARQYRLIVHNGYCDGRSERNLL TT0C8BY TT Patented-recorded TT9PCE0 ID TT9PCE0 TT9PCE0 TN Plasmodium CDK PfPK5 (Malaria PfPK5) TT9PCE0 UP Q07785 TT9PCE0 UC CDC2H_PLAFK TT9PCE0 BC Kinase TT9PCE0 SN PfPK5; PK5; Cell division control protein 2 homolog; CRK2 TT9PCE0 GN Malaria PfPK5 TT9PCE0 FC It is required in higher cells for entry into S-phase and mitosis. Component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II. Plays a key role in the control of the eukaryotic cell cycle. TT9PCE0 PD 1V0P; 1V0O; 1V0B; 1OB3; 1LCH TT9PCE0 SQ MEKYHGLEKIGEGTYGVVYKAQNNYGETFALKKIRLEKEDEGIPSTTIREISILKELKHSNIVKLYDVIHTKKRLVLVFEHLDQDLKKLLDVCEGGLESVTAKSFLLQLLNGIAYCHDRRVLHRDLKPQNLLINREGELKIADFGLARAFGIPVRKYTHEVVTLWYRAPDVLMGSKKYSTTIDIWSVGCIFAEMVNGTPLFPGVSEADQLMRIFRILGTPNSKNWPNVTELPKYDPNFTVYEPLPWESFLKGLDESGIDLLSKMLKLDPNQRITAKQALEHAYFKENN TT9PCE0 TT Literature-reported TTQ4N7K ID TTQ4N7K TTQ4N7K TN Plasmodium CDK PfPK6 (Malaria PfPK6) TTQ4N7K UP Q8IDW1 TTQ4N7K UC Q8IDW1_PLAF7 TTQ4N7K BC Kinase TTQ4N7K SN Protein kinase 6; PF3D7_1337100; CDK-related protein kinase 6 TTQ4N7K GN Malaria PfPK6 TTQ4N7K FC Cyclin-dependent protein serine/threonine kinase activity, protein phosphorylation. TTQ4N7K EC EC 2.7.11.22 TTQ4N7K SQ MNRIDISNFDFLYVIGKGTYGIVYKALDKKENNFVAIKKIINLCDENYGISKCILRELTILQKIKHKNIINLKYVFYGKDIEDKLKGENLENSCLYLAFEYCDIDLFNLIKKHNLNIKEIKYIIFELLLALSYFHSNNYIHRDIKPENIFITSEGEIKLGDLGMSVEKSDHMTPTVVTLWYRAPEILLKSTNYDQKVDIWSLGCLFMELIQGRPLFPGKNDCTQLELIYLLLGDKDKLTTVDKERKDMFPYFEINMLKDAIDDEHTLDLISKMLIYDPNYRISSKEALKHPCFQDIEQVKFSYNF TTQ4N7K TT Literature-reported TTX6NHY ID TTX6NHY TTX6NHY TN Plasmodium Cytochrome C oxidoreductase (Malaria MT-CO1) TTX6NHY UP Q02766 TTX6NHY UC COX1_PLAFA TTX6NHY BC Heme-copper respiratory oxidase family TTX6NHY SN MT-CO1; Cytochrome c oxidase subunit 1; Cytochrome c oxidase polypeptide I TTX6NHY GN Malaria MT-CO1 TTX6NHY FC Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c aretransferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. TTX6NHY EC EC 1.9.3.1 TTX6NHY SQ MVLNRYSLITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICTYMSSNFGMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNLRENSIVILWSMLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIFK TTX6NHY TT Literature-reported TTSDL7Z ID TTSDL7Z TTSDL7Z TN Plasmodium Delta-aminolevulinic acid synthetase (Malaria DAAS) TTSDL7Z UP Q27733 TTSDL7Z UC Q27733_PLAFA TTSDL7Z BC Acyltransferase TTSDL7Z SN Delta-aminolevulinic acid synthetase TTSDL7Z GN Malaria DAAS TTSDL7Z FC Vital for parasite haem synthesis and parasite survival. TTSDL7Z EC EC 2.3.1.37 TTSDL7Z SQ MRKKRTLKVSINEIKKYCPFVKNIQFLYNTNEKKNNLVLSVMSDLCPVGKAINEKHFIIIDNKSKINIIKILKQANMQSKVLVQCIKNKNIEKENMSNDDLLKSGKRNNNVLFYDILEKNKNDHSFQINDNTIQKNNIIYKYINSLDEYKLFKNNCNNNLKDLLNKLYTDKRYRIFTILNKYRINYPNVYIENNKLMLPSFYEFYQKYGYKPCIGNIRYQLSASFEDNNKNICSFSHKNKENYLFNFWNLHIDNVSNEKTVVWCSNDYLCLSNNEKIIEVGIETLKKIGNSSGGTRNISGSLLNHTHLEYIIAKWYNKESSLLFTSGYIANVGALETLGKLLNLIYISDEMNHASIINGIRESRCEKFIFKHNDMNDLERILYNLRINKQYENRKIMIVFESIYSMSGHISNIEYIVQLAKKYNALTYVDEVHAVGLYGNKGSGYLEELHLCNHIDIINGTLSKAIGSLGGFICANKYYIDVIRSYSSHFIFTTSLTPVNINTSAEAIHIIQNDMSLRKKLTQVVNKTKQKLQERGIQVLHNNSHIVVLMINSAEKCKQICDDLLKEYNIYIQPINYPTVPMGMERIRITPSPFHTDEQIFKLVNSLYTLFKKYQVNMFDKKNKHTLMKL TTSDL7Z TT Literature-reported TT09NOX ID TT09NOX TT09NOX TN Plasmodium Dihydroorotase (Malaria dho) TT09NOX UP A9CSR1 TT09NOX UC A9CSR1_PLAFA TT09NOX BC Carbon-nitrogen hydrolase TT09NOX SN Dihydroorotase TT09NOX GN Malaria dho TT09NOX FC A Zn2+ amidohydrolase superfamily that catalyzes reversible cyclization of N-carbamoyl-L-aspartate (L-CA) to form L-dihydroorotate (L-DHO). TT09NOX EC EC 3.5.2.3 TT09NOX SQ MKNYFYIPIADDMHCHLRQGDMLDFTVNSIRRGGCNRVLVMPNTHPIISTCSDAQKYLYQLKSRDDDIEYLMTLYLNKNTDENDILSNYYKCNLQGVKIYPSNVTTNSSDGITSLEPYYKVFHALEKLNKSIHIHCEEPNINPLYAEEKYLPHIHDLAIKFPGLNIVLEHISSSESINVIKEFRNVAGSITPHHLYLTIDDVVNMDIYDHAIDNTYIEKYIKNTYHYCKPLPKLLEDKIALQDVIKDDFPRVFLGSDSAPHYKVMKRKPYYKPGIYTQPFLINYVAHILNKFDALDKMENFTSKNASLFLNLAEKKKLAKYYICVEKHPFKLPREYNGVVPFLAGKTLDYDIHYVSKF TT09NOX TT Literature-reported TTVL895 ID TTVL895 TTVL895 TN Plasmodium Enopyruvyl shikimate phosphate synthase (Malaria ESPS) TTVL895 UP 0A1C3KAW3 TTVL895 UC A0A1C3KAW3_PLAMA TTVL895 BC Alkyl aryl transferase TTVL895 SN aroA of Aeropyrum pernix; Probable 3-phosphoshikimate 1-carboxyvinyltransferase of Aeropyrum pernix; EPSPS of Aeropyrum pernix; EPSP synthase of Aeropyrum pernix; 5-enolpyruvylshikimate-3-phosphate synthase of Aeropyrum pernix TTVL895 GN Malaria ESPS TTVL895 FC Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3- phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. TTVL895 EC EC 1.1.1.25 TTVL895 SQ MCNKKCGPKCNEKYSEGGRNKGRTTNSSVEMIKHKNILSENKKRNRSDVEKYVQEEYTISDKFKGIIKQMINNHGTGSFEIGNVLIIVLNMKKYHDKSEKCKEFGKMLQEISISSKNELICFADTNIMDLLHFTYHLYFKGAHGTVALHSIEVYILTSLFKTSNAKEHKRGLSEALRLAILNDKNMFIRIKKNDLNYFVKNLKYFLNKCILNIRDIIKKGENNAKYIHVLSFGNTIGNAIKNVIKNSPGCTYINDRDYINYGIFYELKIMYELDAIDMLLLLNIEEIMIKYKLKYKLDSNFVNYYTNDIITYLHKTHSSTTNEIPLVHILNINKIQKNVLVHTPLSIIIKVFYPFICLSPFHNISTTSAQEGEFIGIVNEDRDGMIHTSTTIDMVQKKKEHTIRKINYVYLQGVGNKSEIIRVIYVSTMGRQNVRIENMNLCFDVIVFIKILKDLNFQIFLKKKKSNDIYTNVNRTVIRNCLFINGNVEQTVFLFKNFIFQKKIILNIYNSGTVCRFLLPLLCLYICKQNLKAKEEKKQLLKYIILKGDEQMESHRVINPLVNVVLKCFKYVKIKYLKKKNYLPICIYVKREIHESYTLFCSNDVAIDNYHSSQFVSSMLLISVYSETDTCIRLKFKKIHNCLNRSKKIKVKKEQKKKKITIFRKYIKRKEVSRFKCSYYTMLSICWSCNGKKCNSINKGSTLCCKCSSSPDFNFDENYRHPRKRYNWYNFGYPINEIRNRMNSSNFSTTSKAFIDLTVRVMKLWGVRVKMKRNNYTIKKNEKYLLYSNNNDSTSIRGIAGNRSSIKSRTSNRICRSGGNKNERFNNVHYKYASMINRKHHFNDSRHILFPGIHNKKEKMLVYSLHGRGEKSSKGSCDTCKQKGVDEVKKEVHNNPHEEYNFVMLKQKEKVDQINNKEKEEDKNISNDVTNDGGYTLVKNILRYEINNDLGLYFYFIIGSLIKRQNCVIFLKLNINRMKLKNVGKGYYKIETIDFQKNVLNYFLLNILLLLGINMYINMNDEIRKIYLLTSKRMNIKKKKIIRHLEKAIRNKWKRKNGYYKKRHRNIYTTACYGVNNSTCEHLSQGECTFKYYIFEKIYMKYKIMHFRNVLLKIVVDAEYFSDDFFSICVLFCYYLLTHERENNTELLFKIKNIHNQNIKESIRILNAVLILKICFHNILFIFCDNNSIYITKTHHQIQNCLFFKCKREHWALLCTSSDNNERKNNSSSIGSNSNNGNNNRRSRCKKKLFFNNSKYVINDDQELYLYIDAKKDHRIIFMATILSLIFKNIIIDNSYEVEKSYPHFYEQARKYLEININYVNSDNVKFHNFEEVNNYNILNEQDSKSCVEVISSSIESHESTYSCTDASRSDVDMLKNYKSPTMSTEGNYSINTRSKKLINKHTNCNSLNRPMENNTCTEKNFYKTNGAHIIHKKEANRTHRSTRGNLYFMNHEYWKTSNLNLKNVVMKKTKKCIHRKRAPKGIINLCNLTNPMLQLHTCGSTGSIASEENELTVMRCGERKGIISRKGIFTVSNSGGSDSYSDSYSDSYSDSFMKCNEDPSNERSNECNKDHSNERSNGSSKWFERRGGTEEGYQTKLRLNLRERLRSGKSSSFLNKVKNQLNGDKTNLFLPSDTNYMRTYKYEEVKVNNGNVFYLLKEINNLNVHIICGIRNVGKSYLGHRIENSLVIDIDEYILNGQISFDKLTIDDFRFYEYITFVSALYLSYCLLTLKNYLWANISGSISCNDRGDVWSNIQSSMHGNDDKKDVFLCRAENSKVCINRSCVAVHAYFDNIFFCMGNDIIFYNKKINDLYYNLKNKLLTCKNYDINSITIVLGGGIIEFYKSRQVLKKLKNVVLIKRNKRELCDICINDNVKPKLSGNIKEIINRRTVLFDELNSFHFSIPSEIKISNHIKNLKESRNKLIVSSFINFFNYKFFVKPTILDWGAIRTLSIHLKFFHSFDYELLRSSYDVVEIVYEHIGSTKDGQSEQKDGSGQRGCVEQRGCNERRCRGEELDMGGQHDQRGKNRKYAKNEEKLLALAIFIIRSYTTKPIAVKLHTSIFHAQFFKIKNRCTKLKKDGKKNVAHLFCNNLLNVLYKYKINIVEVDIKFLKVVKYFLAHKKKKANIFFIISKHRNKVNKLKIKSDLNKLNIFHADLIKLTYNYASKSDKEFLSKTINAYNSHRLINTKLSRIKNVYNNTNEEISLYSCYVNNSFVFLYNNVTHLEYQKTNLRNLETGKNSKNIENHNYDENKKNRDFYHNNFMYGFYYQKVKSIISYVPTEGDK TTVL895 TT Literature-reported TTNISW4 ID TTNISW4 TTNISW4 TN Plasmodium MECDP-synthase (Malaria ISPF) TTNISW4 UP P62368 TTNISW4 UC ISPF_PLAF7 TTNISW4 BC Phosphorus-oxygen lyase TTNISW4 SN MECPS; MECDP-synthase; ISPF TTNISW4 GN Malaria ISPF TTNISW4 FC Converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2- phosphate into 2C-methyl-D-erythritol 2,4-cyclodiphosphate and CMP. TTNISW4 PD 4C82; 4C81 TTNISW4 SQ MFLKGYTSNVVLIILTFFILLTKEEKNIKNNISGYCFLNFGLKKNAIIKKREKQNLKLFCYNGIRIGQGYDIHKIKVLDEEYNTYANNDFNKNEQSFKTLTLGGVKINNVLVLSHSDGDIIYHSIVDSILGALGSLDIGTLFPDKDEKNKNKNSAIFLRYARLLIYKKNYDIGNVDINVIAQVPKISNIRKNIIKNISTVLNIDESQISVKGKTHEKLGVIGEKKAIECFANILLIPKNS TTNISW4 TT Literature-reported TTMDS9W ID TTMDS9W TTMDS9W TN Plasmodium Phosphoethanolamine N-methyltransferase (Malaria PNM) TTMDS9W UP Q8IDQ9 TTMDS9W UC Q8IDQ9_PLAF7 TTMDS9W BC Transferases of one-carbon groups TTMDS9W SN Phosphoethanolamine N-methyltransferase TTMDS9W GN Malaria PNM TTMDS9W FC Golgi apparatus, phosphoethanolamine N-methyltransferase activity, phosphatidylcholine biosynthetic process TTMDS9W EC EC 2.1.1.103 TTMDS9W SQ MTLIENLNSDKTFLENNQYTDEGVKVYEFIFGENYISSGGLEATKKILSDIELNENSKVLDIGSGLGGGCMYINEKYGAHTHGIDICSNIVNMANERVSGNNKIIFEANDILTKEFPENNFDLIYSRDAILHLSLENKNKLFQKCYKWLKPTGTLLITDYCATEKENWDDEFKEYVKQRKYTLITVEEYADILTACNFKNVVSKDLSDYWNQLLEVEHKYLHENKEEFLKLFSEKKFISLDDGWSRKIKDSKRKMQRWGYFKATKN TTMDS9W TT Literature-reported TT5A6VQ ID TT5A6VQ TT5A6VQ TN Plasmodium Plasmepsin 4 (Malaria PLA4) TT5A6VQ UP Q8IM16 TT5A6VQ UC Q8IM16_PLAF7 TT5A6VQ SN Plasmepsin IV TT5A6VQ GN Malaria PLA4 TT5A6VQ FC Plays a crucial role in this critical process which yields nutrients for parasite growth. TT5A6VQ EC EC 3.4.23.- TT5A6VQ PD 1LS5 TT5A6VQ SQ MALTVKEEEFSNTLIKNASAFDRLKLGNLKNLKIQKKLQFLYLILFVLITGVFFFFLIGNFYSHRKLYQVIKNTKHTTIGFKIDRPHDKVLSSVLKNKLSTYVKESFKFFKSGYAQKGYLGSENDSIELDDVANLMFYGEGQIGTNKQPFMFIFDTGSANLWVPSVNCDSIGCSTKHLYDASASKSYEKDGTKVEISYGSGTVRGYFSKDVISLGDLSLPYKFIEVTDADDLEPIYSGSEFDGILGLGWKDLSIGSIDPVVVELKKQNKIDNALFTFYLPVHDKHVGYLTIGGIESDFYEGPLTYEKLNHDLYWQIDLDIHFGKYVMQKANAVVDSGTSTITAPTSFLNKFFRDMNVIKVPFLPLYVTTCDNDDLPTLEFHSRNNKYTLEPEFYMDPLSDIDPALCMLYILPVDIDDNTFILGDPFMRKYFTVFDYEKESVGFAVAKNL TT5A6VQ TT Literature-reported TTPJMCU ID TTPJMCU TTPJMCU TN Platelet glycoprotein 4 (CD36) TTPJMCU UP P16671 TTPJMCU UC CD36_HUMAN TTPJMCU BC Long chain fatty acid translocase TTPJMCU SN Thrombospondin receptor; Platelet glycoprotein IV; Platelet collagen receptor; PAS-4; PAS IV; Leukocyte differentiation antigen CD36; Glycoprotein IIIb; GPIV; GPIIIB; GP4; GP3B; Fatty acid translocase; FAT TTPJMCU GN CD36 TTPJMCU FC Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor-ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine. Binds long-chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption. In the small intestine, plays a role in proximal absorption of dietary fatty acid and cholesterol for optimal chylomicron formation, possibly through the activation of MAPK1/3 (ERK1/2) signaling pathway. Involved in oral fat perception and preferences. Detection into the tongue of long-chain fatty acids leads to a rapid and sustained rise in flux and protein content of pancreatobiliary secretions. In taste receptor cells, mediates the induction of an increase in intracellular calcium levels by long-chain fatty acids, leading to the activation of the gustatory neurons in the nucleus of the solitary tract. Important factor in both ventromedial hypothalamus neuronal sensing of long-chain fatty acid and the regulation of energy and glucose homeostasis. Receptor for thombospondins, THBS1 and THBS2, mediating their antiangiogenic effects. As a coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42, interacts with the heterodimer TLR4:TLR6, the complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion, through the priming and activation of the NLRP3 inflammasome. Selective and nonredundant sensor of microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell surface, leading to the NF-kappa-B-dependent production of TNF, via MYD88 signaling pathway and subsequently is targeted to the Golgi in a lipid-raft dependent pathway. Multifunctional glycoprotein that acts as receptor for a broad range of ligands. TTPJMCU PD 5LGD TTPJMCU SQ MGCDRNCGLIAGAVIGAVLAVFGGILMPVGDLLIQKTIKKQVVLEEGTIAFKNWVKTGTEVYRQFWIFDVQNPQEVMMNSSNIQVKQRGPYTYRVRFLAKENVTQDAEDNTVSFLQPNGAIFEPSLSVGTEADNFTVLNLAVAAASHIYQNQFVQMILNSLINKSKSSMFQVRTLRELLWGYRDPFLSLVPYPVTTTVGLFYPYNNTADGVYKVFNGKDNISKVAIIDTYKGKRNLSYWESHCDMINGTDAASFPPFVEKSQVLQFFSSDICRSIYAVFESDVNLKGIPVYRFVLPSKAFASPVENPDNYCFCTEKIISKNCTSYGVLDISKCKEGRPVYISLPHFLYASPDVSEPIDGLNPNEEEHRTYLDIEPITGFTLQFAKRLQVNLLVKPSEKIQVLKNLKRNYIVPILWLNETGTIGDEKANMFRSQVTGKINLLGLIEMILLSVGVVMFVAFMISYCACRSKTIK TTPJMCU TT Literature-reported TTNQ760 ID TTNQ760 TTNQ760 TN Polyamine oxidase (PAOX) TTNQ760 UP Q6QHF9 TTNQ760 UC PAOX_HUMAN TTNQ760 BC CH-NH donor oxidoreductase TTNQ760 SN Peroxisomal N(1)acetylspermine/spermidine oxidase; PAOX TTNQ760 GN PAOX TTNQ760 FC Flavoenzyme which catalyzes the oxidation of N(1)- acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)- acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. TTNQ760 EC EC 1.5.3.13 TTNQ760 SQ MESTGSVGEAPGGPRVLVVGGGIAGLGAAQRLCGHSAFPHLRVLEATARAGGRIRSERCFGGVVEVGAHWIHGPSRGNPVFQLAAEYGLLGEKELSQENQLVETGGHVGLPSVSYASSGASVSLQLVAEMATLFYGLIDQTREFLHAAETPVPSVGEYLKKEIGQHVAGWTEDEETRKLKLAVLNSFFNLECCVSGTHSMDLVALAPFGEYTVLPGLDCTFSKGYQGLTNCMMAALPEDTVVFEKPVKTIHWNGSFQEAAFPGETFPVSVECEDGDRFPAHHVIVTVPLGFLREHLDTFFDPPLPAEKAEAIRKIGFGTNNKIFLEFEEPFWEPDCQLIQLVWEDTSPLEDAAPELQDAWFRKLIGFVVLPAFASVHVLCGFIAGLESEFMETLSDEEVLLCLTQVLRRVTGNPRLPAPKSVLRSRWHSAPYTRGSYSYVAVGSTGGDLDLLAQPLPADGAGAQLQILFAGEATHRTFYSTTHGALLSGWREADRLLSLWAPQVQQPRPRL TTNQ760 TT Literature-reported TTIPNSR ID TTIPNSR TTIPNSR TN Polycomb complex protein BMI-1 (BMI1) TTIPNSR UP P35226 TTIPNSR UC BMI1_HUMAN TTIPNSR BC Zinc-finger TTIPNSR SN RNF51; RING finger protein 51; Polycomb group RING finger protein 4; PCGF4 TTIPNSR GN BMI1 TTIPNSR FC PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. TTIPNSR PD 5FR6; 4R8P; 3RPG; 2NA1; 2H0D TTIPNSR SQ MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEDKRIITDDEIISLSIEFFDQNRLDRKVNKDKEKSKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSGNHQSSFANRPRKSSVNGSSATSSG TTIPNSR TT Literature-reported TTIPNSR FM Zinc-finger TTKSQ3W ID TTKSQ3W TTKSQ3W TN PPAR-gamma coactivator 1-beta (PPARGC1B) TTKSQ3W UP Q86YN6 TTKSQ3W UC PRGC2_HUMAN TTKSQ3W BC RNA recognition motif TTKSQ3W SN Peroxisome proliferator-activated receptor gamma coactivator 1-beta; PPARGC1; PPARGC-1-beta; PGC1B; PGC1; PGC-1-related estrogen receptor alpha coactivator; PGC-1-beta; PERC TTKSQ3W GN PPARGC1B TTKSQ3W FC Plays a role of stimulator of transcription factors and nuclear receptors activities. Activates transcriptional activity of estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and glucocorticoid receptor in the presence of glucocorticoids. May play a role in constitutive non-adrenergic-mediated mitochondrial biogenesis as suggested by increased basal oxygen consumption and mitochondrial number when overexpressed. May be involved in fat oxidation and non-oxidative glucose metabolism and in the regulation of energy expenditure. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. TTKSQ3W PD 6D0Y; 3SP6 TTKSQ3W SQ MAGNDCGALLDEELSSFFLNYLADTQGGGSGEEQLYADFPELDLSQLDASDFDSATCFGELQWCPENSETEPNQYSPDDSELFQIDSENEALLAELTKTLDDIPEDDVGLAAFPALDGGDALSCTSASPAPSSAPPSPAPEKPSAPAPEVDELSLLQKLLLATSYPTSSSDTQKEGTAWRQAGLRSKSQRPCVKADSTQDKKAPMMQSQSRSCTELHKHLTSAQCCLQDRGLQPPCLQSPRLPAKEDKEPGEDCPSPQPAPASPRDSLALGRADPGAPVSQEDMQAMVQLIRYMHTYCLPQRKLPPQTPEPLPKACSNPSQQVRSRPWSRHHSKASWAEFSILRELLAQDVLCDVSKPYRLATPVYASLTPRSRPRPPKDSQASPGRPSSVEEVRIAASPKSTGPRPSLRPLRLEVKREVRRPARLQQQEEEDEEEEEEEEEEEKEEEEEWGRKRPGRGLPWTKLGRKLESSVCPVRRSRRLNPELGPWLTFADEPLVPSEPQGALPSLCLAPKAYDVERELGSPTDEDSGQDQQLLRGPQIPALESPCESGCGDMDEDPSCPQLPPRDSPRCLMLALSQSDPTFGKKSFEQTLTVELCGTAGLTPPTTPPYKPTEEDPFKPDIKHSLGKEIALSLPSPEGLSLKATPGAAHKLPKKHPERSELLSHLRHATAQPASQAGQKRPFSCSFGDHDYCQVLRPEGVLQRKVLRSWEPSGVHLEDWPQQGAPWAEAQAPGREEDRSCDAGAPPKDSTLLRDHEIRASLTKHFGLLETALEEEDLASCKSPEYDTVFEDSSSSSGESSFLPEEEEEEGEEEEEDDEEEDSGVSPTCSDHCPYQSPPSKANRQLCSRSRSSSGSSPCHSWSPATRRNFRCESRGPCSDRTPSIRHARKRREKAIGEGRVVYIQNLSSDMSSRELKRRFEVFGEIEECEVLTRNRRGEKYGFITYRCSEHAALSLTKGAALRKRNEPSFQLSYGGLRHFCWPRYTDYDSNSEEALPASGKSKYEAMDFDSLLKEAQQSLH TTKSQ3W TT Literature-reported TT9JL72 ID TT9JL72 TT9JL72 TN PRKAR1A messenger RNA (PRKAR1A mRNA) TT9JL72 UP P10644 TT9JL72 UC KAP0_HUMAN TT9JL72 BC mRNA target TT9JL72 SN cAMP-dependent protein kinase type I-alpha regulatory subunit (mRNA); Tissue-specific extinguisher-1 (mRNA); Tissue-specific extinguisher 1 (mRNA); TSE1 (mRNA); RIalpha subunit of cAMP-dependent protein kinase (mRNA); PRKAR1 (mRNA); PKR1 (mRNA); PKA RIalpha-subunit (mRNA); CAMP-dependent protein kinase (PKA) (mRNA) TT9JL72 GN PRKAR1A TT9JL72 FC Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. TT9JL72 PD 5KJZ; 5KJY; 5KJX TT9JL72 SQ MESGSTAASEEARSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEAKQIQNLQKAGTRTDSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFSVSFIAGETVIQQGDEGDNFYVIDQGETDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV TT9JL72 TT Literature-reported TT9JL72 FM mRNA target TT7K6AD ID TT7K6AD TT7K6AD TN Progastricsin pepsinogen C (PGC) TT7K6AD UP P20142 TT7K6AD UC PEPC_HUMAN TT7K6AD SN Pepsinogen C; Gastricsin TT7K6AD GN PGC TT7K6AD FC Hydrolyzes a variety of proteins. TT7K6AD EC EC 3.4.23.3 TT7K6AD PD 1HTR; 1AVF TT7K6AD SQ MKWMVVVLVCLQLLEAAVVKVPLKKFKSIRETMKEKGLLGEFLRTHKYDPAWKYRFGDLSVTYEPMAYMDAAYFGEISIGTPPQNFLVLFDTGSSNLWVPSVYCQSQACTSHSRFNPSESSTYSTNGQTFSLQYGSGSLTGFFGYDTLTVQSIQVPNQEFGLSENEPGTNFVYAQFDGIMGLAYPALSVDEATTAMQGMVQEGALTSPVFSVYLSNQQGSSGGAVVFGGVDSSLYTGQIYWAPVTQELYWQIGIEEFLIGGQASGWCSEGCQAIVDTGTSLLTVPQQYMSALLQATGAQEDEYGQFLVNCNSIQNLPSLTFIINGVEFPLPPSSYILSNNGYCTVGVEPTYLSSQNGQPLWILGDVFLRSYYSVYDLGNNRVGFATAA TT7K6AD TT Literature-reported TTB9CIL ID TTB9CIL TTB9CIL TN Prokineticin receptor-1 (PROKR1) TTB9CIL UP Q8TCW9 TTB9CIL UC PKR1_HUMAN TTB9CIL BC GPCR rhodopsin TTB9CIL SN Prokineticin receptor 1; PROKR1; Gprotein coupled receptor ZAQ; Gprotein coupled receptor 73; GPR73a TTB9CIL GN PROKR1 TTB9CIL FC Receptor for prokineticin 1. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase. May play a role during early pregnancy. TTB9CIL SQ METTMGFMDDNATNTSTSFLSVLNPHGAHATSFPFNFSYSDYDMPLDEDEDVTNSRTFFAAKIVIGMALVGIMLVCGIGNFIFIAALVRYKKLRNLTNLLIANLAISDFLVAIVCCPFEMDYYVVRQLSWEHGHVLCTSVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLRPRMKCQTATGLIALVWTVSILIAIPSAYFTTETVLVIVKSQEKIFCGQIWPVDQQLYYKSYFLFIFGIEFVGPVVTMTLCYARISRELWFKAVPGFQTEQIRKRLRCRRKTVLVLMCILTAYVLCWAPFYGFTIVRDFFPTVFVKEKHYLTAFYIVECIAMSNSMINTLCFVTVKNDTVKYFKKIMLLHWKASYNGGKSSADLDLKTIGMPATEEVDCIRLK TTB9CIL TT Patented-recorded TTB9CIL RC R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events TT2ZUPY ID TT2ZUPY TT2ZUPY TN Prostate derived ETS factor (SPDEF) TT2ZUPY UP O95238 TT2ZUPY UC SPDEF_HUMAN TT2ZUPY BC E26 transformation-specific ETS TT2ZUPY SN SAM pointed domain-containing Ets transcription factor; Prostate-specific Ets; Prostate-derived Ets factor; Prostate epithelium-specific Ets transcription factor; PSE; PDEF TT2ZUPY GN SPDEF TT2ZUPY FC Binds to 5'-GGAT-3' DNA sequences. May play a role in the regulation of the prostate gland and/or prostate cancer development. Acts as a transcriptional activator for SERPINB5 promoter. May function as an androgen-independent transactivator of the prostate-specific antigen (PSA) promoter. TT2ZUPY PD 2DKX; 1YO5 TT2ZUPY SQ MGSASPGLSSVSPSHLLLPPDTVSRTGLEKAAAGAVGLERRDWSPSPPATPEQGLSAFYLSYFDMLYPEDSSWAAKAPGASSREEPPEEPEQCPVIDSQAPAGSLDLVPGGLTLEEHSLEQVQSMVVGEVLKDIETACKLLNITADPMDWSPSNVQKWLLWTEHQYRLPPMGKAFQELAGKELCAMSEEQFRQRSPLGGDVLHAHLDIWKSAAWMKERTSPGAIHYCASTSEESWTDSEVDSSCSGQPIHLWQFLKELLLKPHSYGRFIRWLNKEKGIFKIEDSAQVARLWGIRKNRPAMNYDKLSRSIRQYYKKGIIRKPDISQRLVYQFVHPI TT2ZUPY TT Literature-reported TTVOJAI ID TTVOJAI TTVOJAI TN Protein arginine methyltransferase 1 (PRMT1) TTVOJAI UP Q99873 TTVOJAI UC ANM1_HUMAN TTVOJAI BC Methyltransferase TTVOJAI SN Protein arginine N-methyltransferase 1; Interferon receptor 1-bound protein 4; IR1B4; Histone-arginine N-methyltransferase PRMT1; HRMT1L2; HMT2 TTVOJAI GN PRMT1 TTVOJAI FC Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates RBM15, promoting ubiquitination and degradation of RBM15. Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity. Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner. Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4 and SERBP1. TTVOJAI EC EC 2.1.1.319 TTVOJAI SQ MAAAEAANCIMENFVATLANGMSLQPPLEEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLYARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR TTVOJAI TT Clinical trial TTL4XSQ ID TTL4XSQ TTL4XSQ TN Protein arginine methyltransferase 3 (PRMT3) TTL4XSQ UP O60678 TTL4XSQ UC ANM3_HUMAN TTL4XSQ SN Protein arginine N-methyltransferase 3; Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3; HRMT1L3 TTL4XSQ GN PRMT3 TTL4XSQ FC Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins. TTL4XSQ EC EC 2.1.1.- TTL4XSQ PD 4RYL; 4QQN; 4HSG; 3SMQ; 2FYT TTL4XSQ SQ MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEYLKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYPDICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIKHIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLTLNNSTQTYGLQ TTL4XSQ TT Literature-reported TTTGPSD ID TTTGPSD TTTGPSD TN Protein C-ets-1 (ETS1) TTTGPSD UP P14921 TTTGPSD UC ETS1_HUMAN TTTGPSD BC E26 transformation-specific ETS TTTGPSD SN P54; EWSR2 TTTGPSD GN ETS1 TTTGPSD FC Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts. May control the differentiation, survival and proliferation of lymphoid cells. May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion. Transcription factor. TTTGPSD PD 5ZMC; 4LG0; 4L18; 4L0Z; 4L0Y TTTGPSD SQ MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMNGAALCALGKDCFLELAPDFVGDILWEHLEILQKEDVKPYQVNGVNPAYPESRYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILRDPLQTDTLQNDYFAIKQEVVTPDNMCMGRTSRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDADE TTTGPSD TT Literature-reported TTY36UA ID TTY36UA TTY36UA TN Protein enabled homolog MENA (ENAH) TTY36UA UP Q8N8S7 TTY36UA UC ENAH_HUMAN TTY36UA SN MENA TTY36UA GN ENAH TTY36UA FC Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation. TTY36UA PD 5NEG; 5NDU; 5ND0; 5NCP; 5NCG TTY36UA SQ MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQETGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERLERERMERERLERERLERERLERERLEQEQLERERQERERQERLERQERLERQERLERQERLDRERQERQERERLERLERERQERERQEQLEREQLEWERERRISSAAAPASVETPLNSVLGDSSASEPGLQAASQPAETPSQQGIVLGPLAPPPPPPLPPGPAQASVALPPPPGPPPPPPLPSTGPPPPPPPPPLPNQVPPPPPPPPAPPLPASGFFLASMSEDNRPLTGLAAAIAGAKLRKVSRMEDTSFPSGGNAIGVNSASSKTDTGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDKGEDSEPVTSKASSTSTPEPTRKPWERTNTMNGSKSPVISRRDSPRKNQIVFDNRSYDSLHRPKSTPLSQPSANGVQTEGLDYDRLKQDILDEMRKELTKLKEELIDAIRQELSKSNTA TTY36UA TT Literature-reported TTY36UA KE hsa04015:Rap1 signaling pathway; hsa04360:Axon guidance; hsa04810:Regulation of actin cytoskeleton TTDWFCQ ID TTDWFCQ TTDWFCQ TN Protein kinase G2 (PRKG2) TTDWFCQ UP Q13237 TTDWFCQ UC KGP2_HUMAN TTDWFCQ SN cGMP-dependent protein kinase II; cGMP-dependent protein kinase 2; cGKII; cGK2; cGK 2; PRKGR2 TTDWFCQ GN PRKG2 TTDWFCQ FC Crucial regulator of intestinal secretion and bone growth (By similarity). Phosphorylates and activates CFTR on the plasma membrane. Plays a key role in intestinal secretion by regulating cGMP-dependent translocation of CFTR in jejunum (By similarity). Acts downstream of NMDAR to activate the plasma membrane accumulation of GRIA1/GLUR1 in synapse and increase synaptic plasticity. Phosphorylates GRIA1/GLUR1 at Ser-863 (By similarity). Acts as regulator of gene expression and activator of the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2 in mechanically stimulated osteoblasts. Under fluid shear stress, mediates ERK activation and subsequent induction of FOS, FOSL1/FRA1, FOSL2/FRA2 and FOSB that play a key role in the osteoblast anabolic response to mechanical stimulation (By similarity). TTDWFCQ EC EC 2.7.11.12 TTDWFCQ PD 6BQ8; 5JIZ; 5JIX; 5C8W; 5C6C TTDWFCQ SQ MGNGSVKPKHSKHPDGHSGNLTTDALRNKVTELERELRRKDAEIQEREYHLKELREQLSKQTVAIAELTEELQNKCIQLNKLQDVVHMQGGSPLQASPDKVPLEVHRKTSGLVSLHSRRGAKAGVSAEPTTRTYDLNKPPEFSFEKARVRKDSSEKKLITDALNKNQFLKRLDPQQIKDMVECMYGRNYQQGSYIIKQGEPGNHIFVLAEGRLEVFQGEKLLSSIPMWTTFGELAILYNCTRTASVKAITNVKTWALDREVFQNIMRRTAQARDEQYRNFLRSVSLLKNLPEDKLTKIIDCLEVEYYDKGDYIIREGEEGSTFFILAKGKVKVTQSTEGHDQPQLIKTLQKGEYFGEKALISDDVRSANIIAEENDVACLVIDRETFNQTVGTFEELQKYLEGYVANLNRDDEKRHAKRSMSNWKLSKALSLEMIQLKEKVARFSSSSPFQNLEIIATLGVGGFGRVELVKVKNENVAFAMKCIRKKHIVDTKQQEHVYSEKRILEELCSPFIVKLYRTFKDNKYVYMLLEACLGGELWSILRDRGSFDEPTSKFCVACVTEAFDYLHRLGIIYRDLKPENLILDAEGYLKLVDFGFAKKIGSGQKTWTFCGTPEYVAPEVILNKGHDFSVDFWSLGILVYELLTGNPPFSGVDQMMTYNLILKGIEKMDFPRKITRRPEDLIRRLCRQNPTERLGNLKNGINDIKKHRWLNGFNWEGLKARSLPSPLQRELKGPIDHSYFDKYPPEKGMPPDELSGWDKDF TTDWFCQ TT Literature-reported TTF0OQ7 ID TTF0OQ7 TTF0OQ7 TN Protein kinase R (PKR) TTF0OQ7 UP P19525 TTF0OQ7 UC E2AK2_HUMAN TTF0OQ7 SN eIF-2A protein kinase 2; Protein kinase RNA-activated; PRKR; PKR; P1/eIF-2A protein kinase; Interferon-inducible RNA-dependent protein kinase; Interferon-induced, double-stranded RNA-activated protein kinase; Eukaryotic translation initiation factor 2-alpha kinase 2 TTF0OQ7 GN EIF2AK2 TTF0OQ7 FC IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1). Inhibits viral replication via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (EIF2S1), this phosphorylation impairs the recycling of EIF2S1 between successive rounds of initiation leading to inhibition of translation which eventually results in shutdown of cellular and viral protein synthesis. Also phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes. Can trigger apoptosis via FADD-mediated activation of CASP8. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin. TTF0OQ7 EC EC 2.7.11.1 TTF0OQ7 PD 3UIU; 2A1A; 2A19; 1QU6 TTF0OQ7 SQ MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKKAVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAKRSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC TTF0OQ7 TT Literature-reported TTENJAB ID TTENJAB TTENJAB TN Protein phosphatase 1D (PPM1D) TTENJAB UP O15297 TTENJAB UC PPM1D_HUMAN TTENJAB BC Phosphoric monoester hydrolase TTENJAB SN p53-induced protein phosphatase 1; WIP1; Protein phosphatase magnesium-dependent 1 delta; Protein phosphatase 2C isoform delta; PP2C-delta TTENJAB GN PPM1D TTENJAB FC Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins. Mediates MAPK14 dephosphorylation and inactivation. Is also an important regulator of global heterochromatin silencing and critical in maintaining genome integrity. Involved in the negative regulation of p53 expression. TTENJAB EC EC 3.1.3.16 TTENJAB SQ MAGLYSLGVSVFSDQGGRKYMEDVTQIVVEPEPTAEEKPSPRRSLSQPLPPRPSPAALPGGEVSGKGPAVAAREARDPLPDAGASPAPSRCCRRRSSVAFFAVCDGHGGREAAQFAREHLWGFIKKQKGFTSSEPAKVCAAIRKGFLACHLAMWKKLAEWPKTMTGLPSTSGTTASVVIIRGMKMYVAHVGDSGVVLGIQDDPKDDFVRAVEVTQDHKPELPKERERIEGLGGSVMNKSGVNRVVWKRPRLTHNGPVRRSTVIDQIPFLAVARALGDLWSYDFFSGEFVVSPEPDTSVHTLDPQKHKYIILGSDGLWNMIPPQDAISMCQDQEEKKYLMGEHGQSCAKMLVNRALGRWRQRMLRADNTSAIVICISPEVDNQGNFTNEDELYLNLTDSPSYNSQETCVMTPSPCSTPPVKSLEEDPWPRVNSKDHIPALVRSNAFSENFLEVSAEIARENVQGVVIPSKDPEPLEENCAKALTLRIHDSLNNSLPIGLVPTNSTNTVMDQKNLKMSTPGQMKAQEIERTPPTNFKRTLEESNSGPLMKKHRRNGLSRSSGAQPASLPTTSQRKNSVKLTMRRRLRGQKKIGNPLLHQHRKTVCVC TTENJAB TT Literature-reported TTENJAB FM Phosphoric monoester hydrolases TT1VNCG ID TT1VNCG TT1VNCG TN Protein-cysteine N-palmitoyltransferase HHAT (HHAT) TT1VNCG UP Q5VTY9 TT1VNCG UC HHAT_HUMAN TT1VNCG BC Acyltransferase TT1VNCG SN Skinny hedgehog protein 1; Melanoma antigen recognized by T-cells 2; MART-2; Hedgehog acyltransferase; HHAT TT1VNCG GN HHAT TT1VNCG FC Catalyzes N-terminal palmitoylation of SHH; which is required for SHH signaling. May bind GTP. . TT1VNCG EC EC 2.3.1.- TT1VNCG SQ MLPRWELALYLLASLGFHFYSFYEVYKVSREHEEELDQEFELETDTLFGGLKKDATDFEWSFWMEWGKQWLVWLLLGHMVVSQMATLLARKHRPWILMLYGMWACWCVLGTPGVAMVLLHTTISFCVAQFRSQLLTWLCSLLLLSTLRLQGVEEVKRRWYKTENEYYLLQFTLTVRCLYYTSFSLELCWQQLPAASTSYSFPWMLAYVFYYPVLHNGPILSFSEFIKQMQQQEHDSLKASLCVLALGLGRLLCWWWLAELMAHLMYMHAIYSSIPLLETVSCWTLGGLALAQVLFFYVKYLVLFGVPALLMRLDGLTPPALPRCVSTMFSFTGMWRYFDVGLHNFLIRYVYIPVGGSQHGLLGTLFSTAMTFAFVSYWHGGYDYLWCWAALNWLGVTVENGVRRLVETPCIQDSLARYFSPQARRRFHAALASCSTSMLILSNLVFLGGNEVGKTYWNRIFIQGWPWVTLSVLGFLYCYSHVGIAWAQTYATD TT1VNCG TT Literature-reported TTWKPGB ID TTWKPGB TTWKPGB TN Proteus vulgaris Chondroitin ABC endolyase 1 (PROVU cABC1) TTWKPGB UP P59807 TTWKPGB UC CABC1_PROVU TTWKPGB SN cABC I; INN=Condoliase; Endochondroitinase ABC; Chondroitinase ABC I; Chondroitin sulfate ABC lyase I; Chondroitin sulfate ABC endolyase; Chondroitin ABC lyase I; Chondroitin ABC endoeliminase; ChS ABC lyase I TTWKPGB GN PROVU cABC1 TTWKPGB FC Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM). TTWKPGB EC EC 4.2.2.20 TTWKPGB PD 1HN0 TTWKPGB SQ MPIFRFTALAMTLGLLSAPYNAMAATSNPAFDPKNLMQSEIYHFAQNNPLADFSSDKNSILTLSDKRSIMGNQSLLWKWKGGSSFTLHKKLIVPTDKEASKAWGRSSTPVFSFWLYNEKPIDGYLTIDFGEKLISTSEAQAGFKVKLDFTGWRAVGVSLNNDLENREMTLNATNTSSDGTQDSIGRSLGAKVDSIRFKAPSNVSQGEIYIDRIMFSVDDARYQWSDYQVKTRLSEPEIQFHNVKPQLPVTPENLAAIDLIRQRLINEFVGGEKETNLALEENISKLKSDFDALNIHTLANGGTQGRHLITDKQIIIYQPENLNSQDKQLFDNYVILGNYTTLMFNISRAYVLEKDPTQKAQLKQMYLLMTKHLLDQGFVKGSALVTTHHWGYSSRWWYISTLLMSDALKEANLQTQVYDSLLWYSREFKSSFDMKVSADSSDLDYFNTLSRQHLALLLLEPDDQKRINLVNTFSHYITGALTQVPPGGKDGLRPDGTAWRHEGNYPGYSFPAFKNASQLIYLLRDTPFSVGESGWNNLKKAMVSAWIYSNPEVGLPLAGRHPFNSPSLKSVAQGYYWLAMSAKSSPDKTLASIYLAISDKTQNESTAIFGETITPASLPQGFYAFNGGAFGIHRWQDKMVTLKAYNTNVWSSEIYNKDNRYGRYQSHGVAQIVSNGSQLSQGYQQEGWDWNRMQGATTIHLPLKDLDSPKPHTLMQRGERGFSGTSSLEGQYGMMAFDLIYPANLERFDPNFTAKKSVLAADNHLIFIGSNINSSDKNKNVETTLFQHAITPTLNTLWINGQKIENMPYQTTLQQGDWLIDSNGNGYLITQAEKVNVSRQHQVSAENKNRQPTEGNFSSAWIDHSTRPKDASYEYMVFLDATPEKMGEMAQKFRENNGLYQVLRKDKDVHIILDKLSNVTGYAFYQPASIEDKWIKKVNKPAIVMTHRQKDTLIVSAVTPDLNMTRQKAATPVTINVTINGKWQSADKNSEVKYQVSGDNTELTFTSYFGIPQEIKLSPLP TTWKPGB TT Literature-reported TTE2W36 ID TTE2W36 TTE2W36 TN Proto-oncogene c-Fos (c-Fos) TTE2W36 UP P01100 TTE2W36 UC FOS_HUMAN TTE2W36 BC Basic leucine zipper bZIP TTE2W36 SN G0S7; G0/G1 switch regulatory protein 7; Cellular oncogene fos; C-fos TTE2W36 GN FOS TTE2W36 FC In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum. Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. TTE2W36 PD 1S9K; 1FOS; 1A02 TTE2W36 SQ MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL TTE2W36 TT Literature-reported TTDRBPW ID TTDRBPW TTDRBPW TN Pseudomonas Aspartate carbamoyltransferase (Pseudo pyrB) TTDRBPW UP Q59711 TTDRBPW UC PYRB_PSEPU TTDRBPW BC Methyltransferase TTDRBPW SN PYRB; L-aspartic acid transcarbamylase; L-aspartate transcarbamoylase; Aspartate transcarbamylase; ATCase; ACTase TTDRBPW GN Pseudo pyrB TTDRBPW FC Involved in allosteric regulation of aspartate carbamoyltransferase. TTDRBPW EC EC 2.1.3.2 TTDRBPW SQ MTPIDAKRPLQLNDQGQLRHFLSLDGLPRELLTEILDTADSFLEVGARAVKKVPLLRGKTVCNVFFENSTRTRTTFELAAQRLSADVISLNVSTSSTSKGETLFDTLRNLEAMAADMFVVRHSDSGAAHFIAEHVCPDVAVINGGDGRHAHPTQGMLDMLTIRRHKGSFENLSVAIVGDILHSRVARSDMLALKALGCPDIRVIGPKTLIPIGIEQYGVKVYTDLAEGLKDVDVVIMLRLQRERMAGGLLPSEGEFYRLFGLTTARLACAKPDAIVMHPGPINRGVEIESAVADGKHSVILNQVTYGIAVRMAVLSMAMSGQNAQRQFDQENAQ TTDRBPW TT Literature-reported TTLP3GX ID TTLP3GX TTLP3GX TN Pseudomonas Phosphomannomutase/phosphoglucomutase (Pseudo algC) TTLP3GX UP P26276 TTLP3GX UC ALGC_PSEAE TTLP3GX BC Intramolecular transferases TTLP3GX SN algC; PMM/PGM; PMM / PGM TTLP3GX GN Pseudo algC TTLP3GX FC Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generatinga bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). TTLP3GX PD 4MRQ; 4IL8; 3RSM; 3C04; 3BKQ TTLP3GX SQ MSTAKAPTLPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVLEGKSGVMLTGSHNPPDYNGFKIVVAGETLANEQIQALRERIEKNDLASGVGSVEQVDILPRYFKQIRDDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALLAGEMSGHVFFKERWFGFDDGIYSAARLLEILSQDQRDSEHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQLKAVDSSLPVPF TTLP3GX TT Literature-reported TTKIH76 ID TTKIH76 TTKIH76 TN Pyridine nucleotide transhydrogenase (NNT) TTKIH76 UP Q13423 TTKIH76 UC NNTM_HUMAN TTKIH76 SN Nicotinamide nucleotide transhydrogenase; NAD(P) transhydrogenase, mitochondrial TTKIH76 GN NNT TTKIH76 FC The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland. TTKIH76 EC EC 7.1.1.1 TTKIH76 PD 1U31; 1PT9; 1DJL TTKIH76 SQ MANLLKTVVTGCSCPLLSNLGSCKGLRVKKDFLRTFYTHQELWCKAPVKPGIPYKQLTVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLASDLVVKVRAPMVNPTLGVHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFTGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEFIEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYIHKGITHIGYTDLPSRMATQASTLYSNNITKLLKAISPDKDNFYFDVKDDFDFGTMGHVIRGTVVMKDGKVIFPAPTPKNIPQGAPVKQKTVAELEAEKAATITPFRKTMSTASAYTAGLTGILGLGIAAPNLAFSQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAISGLTAVGGLALMGGHLYPSTTSQGLAALAAFISSVNIAGGFLVTQRMLDMFKRPTDPPEYNYLYLLPAGTFVGGYLAALYSGYNIEQIMYLGSGLCCVGALAGLSTQGTARLGNALGMIGVAGGLAATLGVLKPGPELLAQMSGAMALGGTIGLTIAKRIQISDLPQLVAAFHSLVGLAAVLTCIAEYIIEYPHFATDAAANLTKIVAYLGTYIGGVTFSGSLIAYGKLQGLLKSAPLLLPGRHLLNAGLLAASVGGIIPFMVDPSFTTGITCLGSVSALSAVMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTIVGALIGSSGAILSYIMCVAMNRSLANVILGGYGTTSTAGGKPMEISGTHTEINLDNAIDMIREANSIIITPGYGLCAAKAQYPIADLVKMLTEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINHDFPDTDLVLVIGANDTVNSAAQEDPNSIIAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDALQAKVRESYQK TTKIH76 TT Literature-reported TTVSRUA ID TTVSRUA TTVSRUA TN RalA binding protein 1 (RALBP1) TTVSRUA UP Q15311 TTVSRUA UC RBP1_HUMAN TTVSRUA BC Non ABC multidrug exporter TTVSRUA SN RalBP1; RalA-binding protein 1; Ral-interacting protein 1; RLIP76; RLIP1; Dinitrophenyl S-glutathione ATPase; DNP-SG ATPase; 76 kDa Ral-interacting protein TTVSRUA GN RALBP1 TTVSRUA FC Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin. Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. TTVSRUA PD 2MBG; 2KWI; 2KWH TTVSRUA SQ MTECFLPPTSSPSEHRRVEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDILHEPPDVVSDDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQIDVPNLKPIFGIPLADAVERTMMYDGIRLPAVFRECIDYVEKYGMKCEGIYRVSGIKSKVDELKAAYDREESTNLEDYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTETEKVQEFQRLLKELPECNYLLISWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVFFTHVQELFGNVVLKQVMKPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIERLRAEIAEIQSRQQHGRSETEEYSSESESESEDEEELQIILEDLQRQNEELEIKNNHLNQAIHEEREAIIELRVQLRLLQMQRAKAEQQAQEDEEPEWRGGAVQPPRDGVLEPKAAKEQPKAGKEPAKPSPSRDRKETSI TTVSRUA TT Literature-reported TTVSRUA FM Non abc multidrug exporter TT25NY8 ID TT25NY8 TT25NY8 TN Ras-like protein TC25 (RAC1) TT25NY8 UP P63000 TT25NY8 UC RAC1_HUMAN TT25NY8 SN p21-Rac1; TC25; MIG5; Cell migration-inducing gene 5 protein TT25NY8 GN RAC1 TT25NY8 FC Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion, migration and differentiation, and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In neurons, is involved in dendritic spine formation and synaptic plasticity (By similarity). In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3. TT25NY8 EC EC 3.6.5.2 TT25NY8 PD 6BC1; 6AGP; 5O33; 5N6O; 5HZH TT25NY8 SQ MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL TT25NY8 TT Literature-reported TTF6WAQ ID TTF6WAQ TTF6WAQ TN Ras-related protein Rab-7a (RAB7A) TTF6WAQ UP P51149 TTF6WAQ UC RAB7A_HUMAN TTF6WAQ BC Small GTPase TTF6WAQ SN RAB7 TTF6WAQ GN RAB7A TTF6WAQ FC Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S. aureus and M. tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e. g. Salmonella) and sometimes by excluding RAB7A function (e. g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA. Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation. Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway. Required for the exosomal release of SDCBP, CD63 and syndecan. Key regulator in endo-lysosomal trafficking. TTF6WAQ PD 6IYB; 3LAW; 1YHN; 1T91 TTF6WAQ SQ MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWCYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPIKLDKNDRAKASAESCSC TTF6WAQ TT Literature-reported TTF6WAQ FM Small GTPase superfamily TTFRES8 ID TTFRES8 TTFRES8 TN Regulator of G-protein signaling 16 (RGS16) TTFRES8 UP O15492 TTFRES8 UC RGS16_HUMAN TTFRES8 SN hRGS-r; Retinally abundant regulator of G-protein signaling; Retinal-specific RGS; RGSR; RGS-r; A28-RGS14P TTFRES8 GN RGS16 TTFRES8 FC Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Plays an important role in the phototransduction cascade by regulating the lifetime and effective concentration of activated transducin alpha. May regulate extra and intracellular mitogenic signals. Regulates G protein-coupled receptor signaling cascades. TTFRES8 PD 2IK8; 2BT2 TTFRES8 SQ MCRTLAAFPTTCLERAKEFKTRLGIFLHKSELGCDTGSTGKFEWGSKHSKENRNFSEDVLGWRESFDLLLSSKNGVAAFHAFLKTEFSEENLEFWLACEEFKKIRSATKLASRAHQIFEEFICSEAPKEVNIDHETHELTRMNLQTATATCFDAAQGKTRTLMEKDSYPRFLKSPAYRDLAAQASAASATLSSCSLDEPSHT TTFRES8 TT Patented-recorded TTVRZUO ID TTVRZUO TTVRZUO TN Reticulon-4 receptor (RTN4R) TTVRZUO UP Q9BZR6 TTVRZUO UC RTN4R_HUMAN TTVRZUO SN UNQ330/PRO526; RTN4R; Nogo-66 receptor; Nogo receptor; NgR TTVRZUO GN RTN4R TTVRZUO FC Receptor for RTN4, OMG and MAG. Mediates axonal growth inhibition and may play a role in regulating axonal regeneration and plasticity in the adult central nervous system. Acts in conjunction with RTN4 and LIGO1 in regulating neuronal precursor cell motility during cortical development. TTVRZUO PD 1P8T; 1OZN TTVRZUO SQ MKRASAGGSRLLAWVLWLQAWQVAAPCPGACVCYNEPKVTTSCPQQGLQAVPVGIPAASQRIFLHGNRISHVPAASFRACRNLTILWLHSNVLARIDAAAFTGLALLEQLDLSDNAQLRSVDPATFHGLGRLHTLHLDRCGLQELGPGLFRGLAALQYLYLQDNALQALPDDTFRDLGNLTHLFLHGNRISSVPERAFRGLHSLDRLLLHQNRVAHVHPHAFRDLGRLMTLYLFANNLSALPTEALAPLRALQYLRLNDNPWVCDCRARPLWAWLQKFRGSSSEVPCSLPQRLAGRDLKRLAANDLQGCAVATGPYHPIWTGRATDEEPLGLPKCCQPDAADKASVLEPGRPASAGNALKGRVPPGDSPPGNGSGPRHINDSPFGTLPGSAEPPLTAVRPEGSEPPGFPTSGPRRRPGCSRKNRTRSHCRLGQAGSGGGGTGDSEGSGALPSLTCSLTPLGLALVLWTVLGPC TTVRZUO TT Literature-reported TTVRZUO RC R-HSA-193634:Axonal growth inhibition (RHOA activation) TTUA38Z ID TTUA38Z TTUA38Z TN Retinoblastoma-binding protein 9 (RBBP9) TTUA38Z UP O75884 TTUA38Z UC RBBP9_HUMAN TTUA38Z SN Retinoblastoma-binding protein 10; RBBP10; RBBP-9; RBBP-10; Putative hydrolase RBBP9; Protein BOG; BOG; B5T-overexpressed gene protein TTUA38Z GN RBBP9 TTUA38Z FC May play a role in the transformation process due to its capacity to confer resistance to the growth-inhibitory effects of TGF-beta1 through interaction with retinoblastoma and the subsequent displacement of E2F-1. TTUA38Z EC EC 3.-.-.- TTUA38Z PD 2QS9 TTUA38Z SQ MASPSKAVIVPGNGGGDVTTHGWYGWVKKELEKIPGFQCLAKNMPDPITARESIWLPFMETELHCDEKTIIIGHSSGAIAAMRYAETHRVYAIVLVSAYTSDLGDENERASGYFTRPWQWEKIKANCPYIVQFGSTDDPFLPWKEQQEVADRLETKLHKFTDCGHFQNTEFHELITVVKSLLKVPA TTUA38Z TT Literature-reported TT3KYWB ID TT3KYWB TT3KYWB TN Ribosomal protein S6 kinase alpha-6 (RSK6) TT3KYWB UP Q9UK32 TT3KYWB UC KS6A6_HUMAN TT3KYWB SN pp90RSK4; p90RSK6; p90-RSK 6; S6K-alpha-6; Ribosomal S6 kinase 4; RSK4; RSK-4; 90 kDa ribosomal protein S6 kinase 6 TT3KYWB GN RPS6KA6 TT3KYWB FC Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis. TT3KYWB EC EC 2.7.11.1 TT3KYWB PD 6G78; 6G77; 6G76 TT3KYWB SQ MLPFAPQDEPWDREMEVFSGGGASSGEVNGLKMVDEPMEEGEADSCHDEGVVKEIPITHHVKEGYEKADPAQFELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRLGSEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQLFKGFSFVATSIAEEYKITPITSANVLPIVQINGNAAQFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQPKRNDVSHVVKGAMVATYSALTHKTFQPVLEPVAASSLAQRRSMKKRTSTGL TT3KYWB TT Patented-recorded TTODWGT ID TTODWGT TTODWGT TN RING-box protein 2 (RNF7) TTODWGT UP Q9UBF6 TTODWGT UC RBX2_HUMAN TTODWGT BC Zinc-finger TTODWGT SN Sensitive to apoptosis gene protein; SAG; Regulator of cullins 2; Rbx2; ROC2; RING finger protein 7; CKII beta-binding protein 1; CKBBP1 TTODWGT GN RNF7 TTODWGT FC CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the substrate. Promotes the neddylation of CUL5 via its interaction with UBE2F. May play a role in protecting cells from apoptosis induced by redox agents. Probable component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. TTODWGT PD 2ECL TTODWGT SQ MADVEDGEETCALASHSGSSGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK TTODWGT TT Literature-reported TTODWGT FM Zinc-finger TTNAFOU ID TTNAFOU TTNAFOU TN Rotamase D (PPID) TTNAFOU UP Q08752 TTNAFOU UC PPID_HUMAN TTNAFOU BC Cis-trans-isomerase TTNAFOU SN Peptidylprolyl isomerase D; Peptidyl-prolyl cis-trans isomerase D; PPIase D; Cyclophilin-related protein; Cyclophilin-40; CYP40; CYP-40; 40 kDa peptidyl-prolyl cis-trans isomerase TTNAFOU GN PPID TTNAFOU FC Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines. PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. TTNAFOU EC EC 5.2.1.8 TTNAFOU SQ MSHPSPQAKPSNPSNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGHTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKLCVIAECGELKEGDDGGIFPKDGSGDSHPDFPEDADIDLKDVDKILLITEDLKNIGNTFFKSQNWEMAIKKYAEVLRYVDSSKAVIETADRAKLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKIKAQKDKEKAVYAKMFA TTNAFOU TT Patented-recorded TTNAFOU FM Cis-trans-isomerases TTCDFR1 ID TTCDFR1 TTCDFR1 TN S100 calcium-binding protein A3 (S100A3) TTCDFR1 UP P33764 TTCDFR1 UC S10A3_HUMAN TTCDFR1 BC S100 calcium-binding protein TTCDFR1 SN S100E; Protein S-100E TTCDFR1 GN S100A3 TTCDFR1 FC Binds both calcium and zinc. May be involved in calcium-dependent cuticle cell differentiation, hair shaft and hair cuticular barrier formation. TTCDFR1 PD 3NSO; 3NSL; 3NSK; 3NSI; 1KSO TTCDFR1 SQ MARPLEQAVAAIVCTFQEYAGRCGDKYKLCQAELKELLQKELATWTPTEFRECDYNKFMSVLDTNKDCEVDFVEYVRSLACLCLYCHEYFKDCPSEPPCSQ TTCDFR1 TT Literature-reported TT716MY ID TT716MY TT716MY TN S100 calcium-binding protein A6 (S100A6) TT716MY UP P06703 TT716MY UC S10A6_HUMAN TT716MY BC S100 calcium-binding protein TT716MY SN Protein S100-A6; Prolactin receptor-associated protein; PRA; MLN 4; Growth factor-inducible protein 2A9; Calcyclin; CACY TT716MY GN S100A6 TT716MY FC May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative. May function as calcium sensor and modulator, contributing to cellular calcium signaling. TT716MY PD 4YBH; 2M1K; 1K9P; 1K9K; 1K96 TT716MY SQ MACPLDQAIGLLVAIFHKYSGREGDKHTLSKKELKELIQKELTIGSKLQDAEIARLMEDLDRNKDQEVNFQEYVTFLGALALIYNEALKG TT716MY TT Literature-reported TT1H6LC ID TT1H6LC TT1H6LC TN Salt-inducible kinase 1 (SIK1) TT1H6LC UP P57059 TT1H6LC UC SIK1_HUMAN TT1H6LC BC Kinase TT1H6LC SN Serine/threonine-protein kinase SNF1LK; Serine/threonine-protein kinase SNF1-like kinase 1; Serine/threonine-protein kinase SIK1; SNF1LK; SIK-1; SIK TT1H6LC GN SIK1 TT1H6LC FC Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, CRTC1/TORC1. Inhibits CREB activity by phosphorylating and inhibiting activity of TORCs, the CREB-specific coactivators, like CRTC2/TORC2 and CRTC3/TORC3 in response to cAMP signaling. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators CRTC1/TORC1 and CRTC2/TORC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1. In concert with CRTC1/TORC1, regulates the light-induced entrainment of the circadian clock by attenuating PER1 induction; represses CREB-mediated transcription of PER1 by phosphorylating and deactivating CRTC1/TORC1. Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. TT1H6LC EC EC 2.7.11.1 TT1H6LC SQ MVIMSEFSADPAGQGQGQQKPLRVGFYDIERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDSSNLEKIYREVQLMKLLNHPHIIKLYQVMETKDMLYIVTEFAKNGEMFDYLTSNGHLSENEARKKFWQILSAVEYCHDHHIVHRDLKTENLLLDGNMDIKLADFGFGNFYKSGEPLSTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPFFMSQDCESLIRRMLVVDPARRITIAQIRQHRWMRAEPCLPGPACPAFSAHSYTSNLGDYDEQALGIMQTLGVDRQRTVESLQNSSYNHFAAIYYLLLERLKEYRNAQCARPGPARQPRPRSSDLSGLEVPQEGLSTDPFRPALLCPQPQTLVQSVLQAEMDCELQSSLQWPLFFPVDASCSGVFRPRPVSPSSLLDTAISEEARQGPGLEEEQDTQESLPSSTGRRHTLAEVSTRLSPLTAPCIVVSPSTTASPAEGTSSDSCLTFSASKSPAGLSGTPATQGLLGACSPVRLASPFLGSQSATPVLQAQGGLGGAVLLPVSFQEGRRASDTSLTQGLKAFRQQLRKTTRTKGFLGLNKIKGLARQVCQAPASRASRGGLSPFHAPAQSPGLHGGAAGSREGWSLLEEVLEQQRLLQLQHHPAAAPGCSQAPQPAPAPFVIAPCDGPGAAPLPSTLLTSGLPLLPPPLLQTGASPVASAAQLLDTHLHIGTGPTALPAVPPPRLARLAPGCEPLGLLQGDCEMEDLMPCSLGTFVLVQ TT1H6LC TT Literature-reported TTCUGZR ID TTCUGZR TTCUGZR TN Salt-inducible kinase 2 (SIK2) TTCUGZR UP Q9H0K1 TTCUGZR UC SIK2_HUMAN TTCUGZR SN Serine/threonine-protein kinase SNF1-like kinase 2; Serine/threonine-protein kinase SIK2; SNF1LK2; SIK-2; Qin-induced kinase; QIK; KIAA0781 TTCUGZR GN SIK2 TTCUGZR FC Phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing TORCs, the CREB-specific coactivators. TTCUGZR EC EC 2.7.11.1 TTCUGZR SQ MVMADGPRHLQRGPVRVGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWMLIEVPVQRPVLYPQEQENEPSIGEFNEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYFLLVERLKSHRSSFPVEQRLDGRQRRPSTIAEQTVAKAQTVGLPVTMHSPNMRLLRSALLPQASNVEAFSFPASGCQAEAAFMEEECVDTPKVNGCLLDPVPPVLVRKGCQSLPSNMMETSIDEGLETEGEAEEDPAHAFEAFQSTRSGQRRHTLSEVTNQLVVMPGAGKIFSMNDSPSLDSVDSEYDMGSVQRDLNFLEDNPSLKDIMLANQPSPRMTSPFISLRPTNPAMQALSSQKREVHNRSPVSFREGRRASDTSLTQGIVAFRQHLQNLARTKGILELNKVQLLYEQIGPEADPNLAPAAPQLQDLASSCPQEEVSQQQESVSTLPASVHPQLSPRQSLETQYLQHRLQKPSLLSKAQNTCQLYCKEPPRSLEQQLQEHRLQQKRLFLQKQSQLQAYFNQMQIAESSYPQPSQQLPLPRQETPPPSQQAPPFSLTQPLSPVLEPSSEQMQYSPFLSQYQEMQLQPLPSTSGPRAAPPLPTQLQQQQPPPPPPPPPPRQPGAAPAPLQFSYQTCELPSAASPAPDYPTPCQYPVDGAQQSDLTGPDCPRSPGLQEAPSSYDPLALSELPGLFDCEMLDAVDPQHNGYVLVN TTCUGZR TT Literature-reported TTANOZH ID TTANOZH TTANOZH TN SCN1A messenger RNA (SCN1A mRNA) TTANOZH UP P35498 TTANOZH UC SCN1A_HUMAN TTANOZH BC mRNA target TTANOZH SN Voltage-gated sodium channel subunit alpha Nav1.1 (mRNA); Sodium channel protein type I subunit alpha (mRNA); Sodium channel protein type 1 subunit alpha (mRNA); Sodium channel protein brain I subunit alpha (mRNA); SCN1 (mRNA) TTANOZH GN SCN1A TTANOZH FC Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Plays a key role in brain, probably by regulating the moment when neurotransmitters are released in neurons. Involved in sensory perception of mechanical pain: activation in somatosensory neurons induces pain without neurogenic inflammation and produces hypersensitivity to mechanical, but not thermal stimuli. Mediates the voltage-dependent sodium ion permeability of excitable membranes. TTANOZH SQ MEQTVLVPPGPDSFNFFTRESLAAIERRIAEEKAKNPKPDKKDDDENGPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAIFRFSATSALYILTPFNPLRKIAIKILVHSLFSMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKIIARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCIQWPPTNASLEEHSIEKNITVNYNGTLINETVFEFDWKSYIQDSRYHYFLEGFLDALLCGNSSDAGQCPEGYMCVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMIEQLKKQQEAAQQAATATASEHSREPSAAGRLSDSSSEASKLSSKSAKERRNRRKKRKQKEQSGGEEKDEDEFQKSESEDSIRRKGFRFSIEGNRLTYEKRYSSPHQSLLSIRGSLFSPRRNSRTSLFSFRGRAKDVGSENDFADDEHSTFEDNESRRDSLFVPRRHGERRNSNLSQTSRSSRMLAVFPANGKMHSTVDCNGVVSLVGGPSVPTSPVGQLLPEVIIDKPATDDNGTTTETEMRKRRSSSFHVSMDFLEDPSQRQRAMSIASILTNTVEELEESRQKCPPCWYKFSNIFLIWDCSPYWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTDHFNNVLTVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVTLSLVELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKDCVCKIASDCQLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLTVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDNEMNNLQIAVDRMHKGVAYVKRKIYEFIQQSFIRKQKILDEIKPLDDLNNKKDSCMSNHTAEIGKDLDYLKDVNGTTSGIGTGSSVEKYIIDESDYMSFINNPSLTVTVPIAVGESDFENLNTEDFSSESDLEESKEKLNESSSSSEGSTVDIGAPVEEQPVVEPEETLEPEACFTEGCVQRFKCCQINVEEGRGKQWWNLRRTCFRIVEHNWFETFIVFMILLSSGALAFEDIYIDQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGYQTYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINTTTGDRFDIEDVNNHTDCLKLIERNETARWKNVKVNFDNVGFGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEESLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSEYVTTILSRINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPNKVNPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFMEFEKLSQFAAALEPPLNLPQPNKLQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYQPITTTLKRKQEEVSAVIIQRAYRRHLLKRTVKQASFTYNKNKIKGGANLLIKEDMIIDRINENSITEKTDLTMSTAACPPSYDRVTKPIVEKHEQEGKDEKAKGK TTANOZH TT Patented-recorded TTANOZH FM mRNA target TTANOZH KE hsa04728:Dopaminergic synapse TTANOZH RC R-HSA-445095:Interaction between L1 and Ankyrins TTLZK1U ID TTLZK1U TTLZK1U TN Secondary lymphoid-tissue chemokine (CCL21) TTLZK1U UP O00585 TTLZK1U UC CCL21_HUMAN TTLZK1U BC Cytokine: CC chemokine TTLZK1U SN UNQ784/PRO1600; Small-inducible cytokine A21; SLC; SCYA21; C-C motif chemokine 21; Beta-chemokine exodus-2; 6Ckine TTLZK1U GN CCL21 TTLZK1U FC Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4. Inhibits hemopoiesis and stimulates chemotaxis. TTLZK1U PD 5EKI; 2L4N TTLZK1U SQ MAQSLALSLLILVLAFGIPRTQGSDGGAQDCCLKYSQRKIPAKVVRSYRKQEPSLGCSIPAILFLPRKRSQAELCADPKELWVQQLMQHLDKTPSPQKPAQGCRKDRGASKTGKKGKGSKGCKRTERSQTPKGP TTLZK1U TT Literature-reported TTP34DQ ID TTP34DQ TTP34DQ TN Serine/threonine-protein kinase 33 (STK33) TTP34DQ UP Q9BYT3 TTP34DQ UC STK33_HUMAN TTP34DQ BC Kinase TTP34DQ SN STK33 TTP34DQ GN STK33 TTP34DQ FC Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME. Not essential for the survival of KRAS-dependent AML cell lines. TTP34DQ EC EC 2.7.11.1 TTP34DQ SQ MADSGLDKKSTKCPDCSSASQKDVLCVCSSKTRVPPVLVVEMSQTSSIGSAESLISLERKKEKNINRDITSRKDLPSRTSNVERKASQQQWGRGNFTEGKVPHIRIENGAAIEEIYTFGRILGKGSFGIVIEATDKETETKWAIKKVNKEKAGSSAVKLLEREVNILKSVKHEHIIHLEQVFETPKKMYLVMELCEDGELKEILDRKGHFSENETRWIIQSLASAIAYLHNNDIVHRDLKLENIMVKSSLIDDNNEINLNIKVTDFGLAVKKQSRSEAMLQATCGTPIYMAPEVISAHDYSQQCDIWSIGVVMYMLLRGEPPFLASSEEKLFELIRKGELHFENAVWNSISDCAKSVLKQLMKVDPAHRITAKELLDNQWLTGNKLSSVRPTNVLEMMKEWKNNPESVEENTTEEKNKPSTEEKLKSYQPWGNVPDANYTSDEEEEKQSTAYEKQFPATSKDNFDMCSSSFTSSKLLPAEIKGEMEKTPVTPSQGTATKYPAKSGALSRTKKKL TTP34DQ TT Literature-reported TTNM0P7 ID TTNM0P7 TTNM0P7 TN Serine/threonine-protein kinase cot (COT) TTNM0P7 UP P41279 TTNM0P7 UC M3K8_HUMAN TTNM0P7 SN Tumor progression locus 2; TPL-2; Proto-oncogene c-Cot; Mitogen-activated protein kinase kinase kinase 8; ESTF; Cancer Osaka thyroid oncogene; COT TTNM0P7 GN MAP3K8 TTNM0P7 FC Required for lipopolysaccharide (LPS)-induced, TLR4-mediated activation of the MAPK/ERK pathway in macrophages, thus being critical for production of the proinflammatory cytokine TNF-alpha (TNF) during immune responses. Involved in the regulation of T-helper cell differentiation and IFNG expression in T-cells. Involved in mediating host resistance to bacterial infection through negative regulation of type I interferon (IFN) production. In vitro, activates MAPK/ERK pathway in response to IL1 in an IRAK1-independent manner, leading to up-regulation of IL8 and CCL4. Transduces CD40 and TNFRSF1A signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. May also play a role in the transduction of TNF signals that activate JNK and NF-kappa-B in some cell types. In adipocytes, activates MAPK/ERK pathway in an IKBKB-dependent manner in response to IL1B and TNF, but not insulin, leading to induction of lipolysis. Plays a role in the cell cycle. Isoform 1 shows some transforming activity, although it is much weaker than that of the activated oncogenic variant. TTNM0P7 EC EC 2.7.11.25 TTNM0P7 PD 5IU2; 4Y85; 4Y83 TTNM0P7 SQ MEYMSTGSDNKEEIDLLIKHLNVSDVIDIMENLYASEEPAVYEPSLMTMCQDSNQNDERSKSLLLSGQEVPWLSSVRYGTVEDLLAFANHISNTAKHFYGQRPQESGILLNMVITPQNGRYQIDSDVLLIPWKLTYRNIGSDFIPRGAFGKVYLAQDIKTKKRMACKLIPVDQFKPSDVEIQACFRHENIAELYGAVLWGETVHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKKVIHHDIKPSNIVFMSTKAVLVDFGLSVQMTEDVYFPKDLRGTEIYMSPEVILCRGHSTKADIYSLGATLIHMQTGTPPWVKRYPRSAYPSYLYIIHKQAPPLEDIADDCSPGMRELIEASLERNPNHRPRAADLLKHEALNPPREDQPRCQSLDSALLERKRLLSRKELELPENIADSSCTGSTEESEMLKRQRSLYIDLGALAGYFNLVRGPPTLEYG TTNM0P7 TT Literature-reported TT8AH9I ID TT8AH9I TT8AH9I TN Serine/threonine-protein kinase Nek8 (NEK8) TT8AH9I UP Q86SG6 TT8AH9I UC NEK8_HUMAN TT8AH9I BC Protein kinase superfamily. NEK Ser/Thr protein kinase family TT8AH9I SN Nima-related protein kinase 12a; NimA-related protein kinase 8; Never in mitosis A-related kinase 8; NEK12A; JCK TT8AH9I GN NEK8 TT8AH9I FC Required for renal tubular integrity. May regulate local cytoskeletal structure in kidney tubule epithelial cells. May regulate ciliary biogenesis through targeting of proteins to the cilia. Plays a role in organogenesis and is involved in the regulation of the Hippo signaling pathway. TT8AH9I EC EC 2.7.11.1 TT8AH9I SQ MEKYERIRVVGRGAFGIVHLCLRKADQKLVIIKQIPVEQMTKEERQAAQNECQVLKLLNHPNVIEYYENFLEDKALMIAMEYAPGGTLAEFIQKRCNSLLEEETILHFFVQILLALHHVHTHLILHRDLKTQNILLDKHRMVVKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMSGTFAPISDRYSPELRQLVLSLLSLEPAQRPPLSHIMAQPLCIRALLNLHTDVGSVRMRRAEKSVAPSNTGSRTTSVRCRGIPRGPVRPAIPPPLSSVYAWGGGLGTPLRLPMLNTEVVQVAAGRTQKAGVTRSGRLILWEAPPLGAGGGSLLPGAVEQPQPQFISRFLEGQSGVTIKHVACGDFFTACLTDRGIIMTFGSGSNGCLGHGSLTDISQPTIVEALLGYEMVQVACGASHVLALSTERELFAWGRGDSGRLGLGTRESHSCPQQVPMPPGQEAQRVVCGIDSSMILTVPGQALACGSNRFNKLGLDHLSLGEEPVPHQQVEEALSFTLLGSAPLDQEPLLSIDLGTAHSAAVTASGDCYTFGSNQHGQLGTNTRRGSRAPCKVQGLEGIKMAMVACGDAFTVAIGAESEVYSWGKGARGRLGRRDEDAGLPRPVQLDETHPYTVTSVSCCHGNTLLAVRSVTDEPVPP TT8AH9I TT Literature-reported TTJ9UMX ID TTJ9UMX TTJ9UMX TN Serine/threonine-protein kinase WNK1 (WNK1) TTJ9UMX UP Q9H4A3 TTJ9UMX UC WNK1_HUMAN TTJ9UMX SN p65; hWNK1; Protein kinase with no lysine 1; Protein kinase lysine-deficient 1; Kinase deficient protein; KDP; HSN2; Erythrocyte 65 kDa protein TTJ9UMX GN WNK1 TTJ9UMX FC Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival, and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SCNN1A, SCNN1B, SCNN1D and SGK1. Controls sodium and chloride ion transport by inhibiting the activity of WNK4, by either phosphorylating the kinase or via an interaction between WNK4 and the autoinhibitory domain of WNK1. WNK4 regulates the activity of the thiazide-sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation. WNK1 may also play a role in actin cytoskeletal reorganization. Phosphorylates NEDD4L. Acts as a scaffold to inhibit SLC4A4, SLC26A6 as well as CFTR activities and surface expression, recruits STK39 which mediates the inhibition (By similarity). TTJ9UMX EC EC 2.7.11.1 TTJ9UMX PD 6FBK; 5WE8; 5WDY; 5TF9; 4PWN TTJ9UMX SQ MSGGAAEKQSSTPGSLFLSPPAPAPKNGSSSDSSVGEKLGAAAADAVTGRTEEYRRRRHTMDKDSRGAAATTTTTEHRFFRRSVICDSNATALELPGLPLSLPQPSIPAAVPQSAPPEPHREETVTATATSQVAQQPPAAAAPGEQAVAGPAPSTVPSSTSKDRPVSQPSLVGSKEEPPPARSGSGGGSAKEPQEERSQQQDDIEELETKAVGMSNDGRFLKFDIEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLTKSERQRFKEEAEMLKGLQHPNIVRFYDSWESTVKGKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKPASFDKVAIPEVKEIIEGCIRQNKDERYSIKDLLNHAFFQEETGVRVELAEEDDGEKIAIKLWLRIEDIKKLKGKYKDNEAIEFSFDLERDVPEDVAQEMVESGYVCEGDHKTMAKAIKDRVSLIKRKREQRQLVREEQEKKKQEESSLKQQVEQSSASQTGIKQLPSASTGIPTASTTSASVSTQVEPEEPEADQHQQLQYQQPSISVLSDGTVDSGQGSSVFTESRVSSQQTVSYGSQHEQAHSTGTVPGHIPSTVQAQSQPHGVYPPSSVAQGQSQGQPSSSSLTGVSSSQPIQHPQQQQGIQQTAPPQQTVQYSLSQTSTSSEATTAQPVSQPQAPQVLPQVSAGKQLPVSQPVPTIQGEPQIPVATQPSVVPVHSGAHFLPVGQPLPTPLLPQYPVSQIPISTPHVSTAQTGFSSLPITMAAGITQPLLTLASSATTAAIPGVSTVVPSQLPTLLQPVTQLPSQVHPQLLQPAVQSMGIPANLGQAAEVPLSSGDVLYQGFPPRLPPQYPGDSNIAPSSNVASVCIHSTVLSPPMPTEVLATPGYFPTVVQPYVESNLLVPMGGVGGQVQVSQPGGSLAQAPTTSSQQAVLESTQGVSQVAPAEPVAVAQTQATQPTTLASSVDSAHSDVASGMSDGNENVPSSSGRHEGRTTKRHYRKSVRSRSRHEKTSRPKLRILNVSNKGDRVVECQLETHNRKMVTFKFDLDGDNPEEIATIMVNNDFILAIERESFVDQVREIIEKADEMLSEDVSVEPEGDQGLESLQGKDDYGFSGSQKLEGEFKQPIPASSMPQQIGIPTSSLTQVVHSAGRRFIVSPVPESRLRESKVFPSEITDTVAASTAQSPGMNLSHSASSLSLQQAFSELRRAQMTEGPNTAPPNFSHTGPTFPVVPPFLSSIAGVPTTAAATAPVPATSSPPNDISTSVIQSEVTVPTEEGIAGVATSTGVVTSGGLPIPPVSESPVLSSVVSSITIPAVVSISTTSPSLQVPTSTSEIVVSSTALYPSVTVSATSASAGGSTATPGPKPPAVVSQQAAGSTTVGATLTSVSTTTSFPSTASQLCIQLSSSTSTPTLAETVVVSAHSLDKTSHSSTTGLAFSLSAPSSSSSPGAGVSSYISQPGGLHPLVIPSVIASTPILPQAAGPTSTPLLPQVPSIPPLVQPVANVPAVQQTLIHSQPQPALLPNQPHTHCPEVDSDTQPKAPGIDDIKTLEEKLRSLFSEHSSSGAQHASVSLETSLVIESTVTPGIPTTAVAPSKLLTSTTSTCLPPTNLPLGTVALPVTPVVTPGQVSTPVSTTTSGVKPGTAPSKPPLTKAPVLPVGTELPAGTLPSEQLPPFPGPSLTQSQQPLEDLDAQLRRTLSPEMITVTSAVGPVSMAAPTAITEAGTQPQKGVSQVKEGPVLATSSGAGVFKMGRFQVSVAADGAQKEGKNKSEDAKSVHFESSTSESSVLSSSSPESTLVKPEPNGITIPGISSDVPESAHKTTASEAKSDTGQPTKVGRFQVTTTANKVGRFSVSKTEDKITDTKKEGPVASPPFMDLEQAVLPAVIPKKEKPELSEPSHLNGPSSDPEAAFLSRDVDDGSGSPHSPHQLSSKSLPSQNLSQSLSNSFNSSYMSSDNESDIEDEDLKLELRRLRDKHLKEIQDLQSRQKHEIESLYTKLGKVPPAVIIPPAAPLSGRRRRPTKSKGSKSSRSSSLGNKSPQLSGNLSGQSAASVLHPQQTLHPPGNIPESGQNQLLQPLKPSPSSDNLYSAFTSDGAISVPSLSAPGQGTSSTNTVGATVNSQAAQAQPPAMTSSRKGTFTDDLHKLVDNWARDAMNLSGRRGSKGHMNYEGPGMARKFSAPGQLCISMTSNLGGSAPISAASATSLGHFTKSMCPPQQYGFPATPFGAQWSGTGGPAPQPLGQFQPVGTASLQNFNISNLQKSISNPPGSNLRTT TTJ9UMX TT Literature-reported TTA76X0 ID TTA76X0 TTA76X0 TN Short transient receptor potential channel 1 (TRPC1) TTA76X0 UP P48995 TTA76X0 UC TRPC1_HUMAN TTA76X0 BC Transient receptor potential catioin channel TTA76X0 SN TrpC1; Transient receptor protein 1; TRP-1 TTA76X0 GN TRPC1 TTA76X0 FC Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Seems to be also activated by intracellular calcium store depletion. TTA76X0 SQ MMAALYPSTDLSGASSSSLPSSPSSSSPNEVMALKDVREVKEENTLNEKLFLLACDKGDYYMVKKILEENSSGDLNINCVDVLGRNAVTITIENENLDILQLLLDYGCQSADALLVAIDSEVVGAVDILLNHRPKRSSRPTIVKLMERIQNPEYSTTMDVAPVILAAHRNNYEILTMLLKQDVSLPKPHAVGCECTLCSAKNKKDSLRHSRFRLDIYRCLASPALIMLTEEDPILRAFELSADLKELSLVEVEFRNDYEELARQCKMFAKDLLAQARNSRELEVILNHTSSDEPLDKRGLLEERMNLSRLKLAIKYNQKEFVSQSNCQQFLNTVWFGQMSGYRRKPTCKKIMTVLTVGIFWPVLSLCYLIAPKSQFGRIIHTPFMKFIIHGASYFTFLLLLNLYSLVYNEDKKNTMGPALERIDYLLILWIIGMIWSDIKRLWYEGLEDFLEESRNQLSFVMNSLYLATFALKVVAHNKFHDFADRKDWDAFHPTLVAEGLFAFANVLSYLRLFFMYTTSSILGPLQISMGQMLQDFGKFLGMFLLVLFSFTIGLTQLYDKGYTSKEQKDCVGIFCEQQSNDTFHSFIGTCFALFWYIFSLAHVAIFVTRFSYGEELQSFVGAVIVGTYNVVVVIVLTKLLVAMLHKSFQLIANHEDKEWKFARAKLWLSYFDDKCTLPPPFNIIPSPKTICYMISSLSKWICSHTSKGKVKRQNSLKEWRNLKQKRDENYQKVMCCLVHRYLTSMRQKMQSTDQATVENLNELRQDLSKFRNEIRDLLGFRTSKYAMFYPRN TTA76X0 TT Literature-reported TTA76X0 RC R-HSA-3295583:TRP channels; R-HSA-418890:Role of second messengers in netrin-1 signaling; R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers TTWOE1T ID TTWOE1T TTWOE1T TN Signal transducer and activator of transcription 6 (STAT6) TTWOE1T UP P42226 TTWOE1T UC STAT6_HUMAN TTWOE1T BC Transcription factor TTWOE1T SN IL-4 Stat TTWOE1T GN STAT6 TTWOE1T FC Involved in IL4/interleukin-4- and IL3/interleukin-3-mediated signaling. Carries out a dual function: signal transduction and activation of transcription. TTWOE1T PD 5NWX; 5NWM; 5D39; 4Y5W; 4Y5U TTWOE1T SQ MSLWGLVSKMPPEKVQRLYVDFPQHLRHLLGDWLESQPWEFLVGSDAFCCNLASALLSDTVQHLQASVGEQGEGSTILQHISTLESIYQRDPLKLVATFRQILQGEKKAVMEQFRHLPMPFHWKQEELKFKTGLRRLQHRVGEIHLLREALQKGAEAGQVSLHSLIETPANGTGPSEALAMLLQETTGELEAAKALVLKRIQIWKRQQQLAGNGAPFEESLAPLQERCESLVDIYSQLQQEVGAAGGELEPKTRASLTGRLDEVLRTLVTSCFLVEKQPPQVLKTQTKFQAGVRFLLGLRFLGAPAKPPLVRADMVTEKQARELSVPQGPGAGAESTGEIINNTVPLENSIPGNCCSALFKNLLLKKIKRCERKGTESVTEEKCAVLFSASFTLGPGKLPIQLQALSLPLVVIVHGNQDNNAKATILWDNAFSEMDRVPFVVAERVPWEKMCETLNLKFMAEVGTNRGLLPEHFLFLAQKIFNDNSLSMEAFQHRSVSWSQFNKEILLGRGFTFWQWFDGVLDLTKRCLRSYWSDRLIIGFISKQYVTSLLLNEPDGTFLLRFSDSEIGGITIAHVIRGQDGSPQIENIQPFSAKDLSIRSLGDRIRDLAQLKNLYPKKPKDEAFRSHYKPEQMGKDGRGYVPATIKMTVERDQPLPTPELQMPTMVPSYDLGMAPDSSMSMQLGPDMVPQVYPPHSHSIPPYQGLSPEESVNVLSAFQEPHLQMPPSLGQMSLPFDQPHPQGLLPCQPQEHAVSSPDPLLCSDVTMVEDSCLSQPVTAFPQGTWIGEDIFPPLLPPTEQDLTKLLLEGQGESGGGSLGAQPLLQPSHYGQSGISMSHMDLRANPSW TTWOE1T TT Literature-reported TTOVUPC ID TTOVUPC TTOVUPC TN Similar to dipeptidyl aminopeptidase-like protein (DPP10) TTOVUPC UP Q8N608 TTOVUPC UC DPP10_HUMAN TTOVUPC BC Prolyl oligopeptidase family TTOVUPC SN KIAA1492; Inactive dipeptidyl peptidase 10; Dipeptidyl peptidase-like protein 2; Dipeptidyl peptidase X; Dipeptidyl peptidase IV-related protein 3; DPRP3; DPRP-3; DPP X; DPL2 TTOVUPC GN DPP10 TTOVUPC FC Promotes cell surface expression of the potassium channel KCND2. Modulates the activity and gating characteristics of the potassium channel KCND2. Has no dipeptidyl aminopeptidase activity. TTOVUPC PD 4WJL TTOVUPC SQ MNQTASVSHHIKCQPSKTIKELGSNSPPQRNWKGIAIALLVILVVCSLITMSVILLTPDELTNSSETRLSLEDLFRKDFVLHDPEARWINDTDVVYKSENGHVIKLNIETNATTLLLENTTFVTFKASRHSVSPDLKYVLLAYDVKQIFHYSYTASYVIYNIHTREVWELNPPEVEDSVLQYAAWGVQGQQLIYIFENNIYYQPDIKSSSLRLTSSGKEEIIFNGIADWLYEEELLHSHIAHWWSPDGERLAFLMINDSLVPTMVIPRFTGALYPKGKQYPYPKAGQVNPTIKLYVVNLYGPTHTLELMPPDSFKSREYYITMVKWVSNTKTVVRWLNRAQNISILTVCETTTGACSKKYEMTSDTWLSQQNEEPVFSRDGSKFFMTVPVKQGGRGEFHHVAMFLIQSKSEQITVRHLTSGNWEVIKILAYDETTQKIYFLSTESSPRGRQLYSASTEGLLNRQCISCNFMKEQCTYFDASFSPMNQHFLLFCEGPRVPVVSLHSTDNPAKYFILESNSMLKEAILKKKIGKPEIKILHIDDYELPLQLSLPKDFMDRNQYALLLIMDEEPGGQLVTDKFHIDWDSVLIDMDNVIVARFDGRGSGFQGLKILQEIHRRLGSVEVKDQITAVKFLLKLPYIDSKRLSIFGKGYGGYIASMILKSDEKLFKCGSVVAPITDLKLYASAFSERYLGMPSKEESTYQAASVLHNVHGLKEENILIIHGTADTKVHFQHSAELIKHLIKAGVNYTMQVYPDEGHNVSEKSKYHLYSTILKFFSDCLKEEISVLPQEPEEDE TTOVUPC TT Literature-reported TTSIYJ6 ID TTSIYJ6 TTSIYJ6 TN SLAM family member 6 (SLAMF6) TTSIYJ6 UP Q96DU3 TTSIYJ6 UC SLAF6_HUMAN TTSIYJ6 BC Immunoglobulin TTSIYJ6 SN SLAMF6; NTB-A; NK-T-B-antigen; CD352; Activating NK receptor TTSIYJ6 GN SLAMF6 TTSIYJ6 FC Triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors. TTSIYJ6 PD 2IF7 TTSIYJ6 SQ MLWLFQSLLFVFCFGPGNVVSQSSLTPLMVNGILGESVTLPLEFPAGEKVNFITWLFNETSLAFIVPHETKSPEIHVTNPKQGKRLNFTQSYSLQLSNLKMEDTGSYRAQISTKTSAKLSSYTLRILRQLRNIQVTNHSQLFQNMTCELHLTCSVEDADDNVSFRWEALGNTLSSQPNLTVSWDPRISSEQDYTCIAENAVSNLSFSVSAQKLCEDVKIQYTDTKMILFMVSGICIVFGFIILLLLVLRKRRDSLSLSTQRTQGPAESARNLEYVSVSPTNNTVYASVTHSNRETEIWTPRENDTITIYSTINHSKESKPTFSRATALDNVV TTSIYJ6 TT Literature-reported TTD81N3 ID TTD81N3 TTD81N3 TN Small ribosomal subunit protein eS12 (RPS12) TTD81N3 UP P25398 TTD81N3 UC RS12_HUMAN TTD81N3 BC Ribosomal protein TTD81N3 SN 40S ribosomal protein S12 TTD81N3 GN RPS12 TTD81N3 FC A component of the 40S ribosome subunit. Ribosome, the organelle that catalyzes protein synthesis, consists of a small 40S subunit and a large 60S subunit. Increased expression in colorectal cancers compared to matched normal colonic mucosa. TTD81N3 PD 6QZP; 6G5I; 6G5H; 6G53; 6G51 TTD81N3 SQ MAEEGIAAGGVMDVNTALQEVLKTALIHDGLARGIREAAKALDKRQAHLCVLASNCDEPMYVKLVEALCAEHQINLIKVDDNKKLGEWVGLCKIDREGKPRKVVGCSCVVVKDYGKESQAKDVIEEYFKCKK TTD81N3 TT Literature-reported TTSVGQ5 ID TTSVGQ5 TTSVGQ5 TN SMN1 messenger RNA (SMN1 mRNA) TTSVGQ5 UP Q16637 TTSVGQ5 UC SMN_HUMAN TTSVGQ5 BC mRNA target TTSVGQ5 SN Survival motor neuron protein mRNA; SMNT mRNA; SMNC mRNA; SMN mRNA; Gemin-1 mRNA; Component of gems 1 mRNA TTSVGQ5 GN SMN1 TTSVGQ5 FC The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). TTSVGQ5 PD 5XJU; 5XJT; 5XJS; 5XJR; 5XJQ TTSVGQ5 SQ MAMSSGGSGGGVPEQEDSVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDICETSGKPKTTPKRKPAKKNKSQKKNTAASLQQWKVGDKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDLLSPICEVANNIEQNAQENENESQVSTDESENSRSPGNKSDNIKPKSAPWNSFLPPPPPMPGPRLGPGKPGLKFNGPPPPPPPPPPHLLSCWLPPFPSGPPIIPPPPPICPDSLDDADALGSMLISWYMSGYHTGYYMGFRQNQKEGRCSHSLN TTSVGQ5 TT Literature-reported TTSVGQ5 FM mRNA target TTPO9ZI ID TTPO9ZI TTPO9ZI TN SNCA messenger RNA (SNCA mRNA) TTPO9ZI UP P37840 TTPO9ZI UC SYUA_HUMAN TTPO9ZI BC mRNA target TTPO9ZI SN PARK1 (mRNA); NonA4 component of amyloid precursor (mRNA); NonA beta component of AD amyloid (mRNA); Non-A4 component of amyloid precursor (mRNA); Non-A beta component of AD amyloid (mRNA); NACP (mRNA) TTPO9ZI GN SNCA TTPO9ZI FC Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores. Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis. Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5. This chaperone activity is important to sustain normal SNARE-complex assembly during aging. Plays also a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity. Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. TTPO9ZI PD 6H6B; 6FLT; 6CU8; 6CU7; 6CT7 TTPO9ZI SQ MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA TTPO9ZI TT Literature-reported TTPO9ZI FM mRNA target TT5B6HJ ID TT5B6HJ TT5B6HJ TN Sodium pump alpha-2 (ATP1A2) TT5B6HJ UP P50993 TT5B6HJ UC AT1A2_HUMAN TT5B6HJ BC Cation transporting ATPase TT5B6HJ SN Sodium/potassium-transporting ATPase subunit alpha-2; Sodium/potassium-transporting ATPase alpha2; Sodium pump 2; Na+/K+ ATPase 2; Na(+)/K(+) ATPase alpha-2 subunit; KIAA0778; Alpha(+)Sodium/potassium-transporting ATPase alpha-2 chain TT5B6HJ GN ATP1A2 TT5B6HJ FC This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients. TT5B6HJ EC EC 7.2.2.13 TT5B6HJ SQ MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDVLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPMSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY TT5B6HJ TT Literature-reported TT5B6HJ FM Acid anhydrides hydrolase TTH6UZY ID TTH6UZY TTH6UZY TN Solute carrier family 12 member 5 (SLC12A5) TTH6UZY UP Q9H2X9 TTH6UZY UC S12A5_HUMAN TTH6UZY BC Cation-chloride cotransporter TTH6UZY SN hKCC2; SLC12A5; Neuronal K-Cl cotransporter; K-Cl cotransporter 2; Electroneutral potassium-chloride cotransporter 2 TTH6UZY GN SLC12A5 TTH6UZY FC Mediates electroneutral potassium-chloride cotransportin mature neurons. Transport occurs under isotonic conditions, but is activated 20-fold by cell swelling. Important for Cl(-) homeostasis in neurons. TTH6UZY SQ MSRRFTVTSLPPAGPARSPDPESRRHSVADPRHLPGEDVKGDGNPKESSPFINSTDTEKGKEYDGKNMALFEEEMDTSPMVSSLLSGLANYTNLPQGSREHEEAENNEGGKKKPVQAPRMGTFMGVYLPCLQNIFGVILFLRLTWVVGIAGIMESFCMVFICCSCTMLTAISMSAIATNGVVPAGGSYYMISRSLGPEFGGAVGLCFYLGTTFAGAMYILGTIEILLAYLFPAMAIFKAEDASGEAAAMLNNMRVYGTCVLTCMATVVFVGVKYVNKFALVFLGCVILSILAIYAGVIKSAFDPPNFPICLLGNRTLSRHGFDVCAKLAWEGNETVTTRLWGLFCSSRFLNATCDEYFTRNNVTEIQGIPGAASGLIKENLWSSYLTKGVIVERSGMTSVGLADGTPIDMDHPYVFSDMTSYFTLLVGIYFPSVTGIMAGSNRSGDLRDAQKSIPTGTILAIATTSAVYISSVVLFGACIEGVVLRDKFGEAVNGNLVVGTLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAISRDGIVPFLQVFGHGKANGEPTWALLLTACICEIGILIASLDEVAPILSMFFLMCYMFVNLACAVQTLLRTPNWRPRFRYYHWTLSFLGMSLCLALMFICSWYYALVAMLIAGLIYKYIEYRGAEKEWGDGIRGLSLSAARYALLRLEEGPPHTKNWRPQLLVLVRVDQDQNVVHPQLLSLTSQLKAGKGLTIVGSVLEGTFLENHPQAQRAEESIRRLMEAEKVKGFCQVVISSNLRDGVSHLIQSGGLGGLQHNTVLVGWPRNWRQKEDHQTWRNFIELVRETTAGHLALLVTKNVSMFPGNPERFSEGSIDVWWIVHDGGMLMLLPFLLRHHKVWRKCKMRIFTVAQMDDNSIQMKKDLTTFLYHLRITAEVEVVEMHESDISAYTYEKTLVMEQRSQILKQMHLTKNEREREIQSITDESRGSIRRKNPANTRLRLNVPEETAGDSEEKPEEEVQLIHDQSAPSCPSSSPSPGEEPEGEGETDPEKVHLTWTKDKSVAEKNKGPSPVSSEGIKDFFSMKPEWENLNQSNVRRMHTAVRLNEVIVKKSRDAKLVLLNMPGPPRNRNGDENYMEFLEVLTEHLDRVMLVRGGGREVITIYS TTH6UZY TT Literature-reported TTH6UZY KE hsa04727:GABAergic synapse TTH6UZY RC R-HSA-426117:Cation-coupled Chloride cotransporters TT8DFHE ID TT8DFHE TT8DFHE TN Solute carrier family 12 member 6 (SLC12A6) TT8DFHE UP Q9UHW9 TT8DFHE UC S12A6_HUMAN TT8DFHE BC Cation-chloride cotransporter TT8DFHE SN SLC12A6; Electroneutral potassium-chloride cotransporter 3 TT8DFHE GN SLC12A6 TT8DFHE FC Mediates electroneutral potassium-chloride cotransport. May be activated by cell swelling. May contribute to cell volume homeostasis in single cells. TT8DFHE SQ MHPPETTTKMASVRFMVTPTKIDDIPGLSDTSPDLSSRSSSRVRFSSRESVPETSRSEPMSEMSGATTSLATVALDPPSDRTSHPQDVIEDLSQNSITGEHSQLLDDGHKKARNAYLNNSNYEEGDEYFDKNLALFEEEMDTRPKVSSLLNRMANYTNLTQGAKEHEEAENITEGKKKPTKTPQMGTFMGVYLPCLQNIFGVILFLRLTWVVGTAGVLQAFAIVLICCCCTMLTAISMSAIATNGVVPAGGSYFMISRALGPEFGGAVGLCFYLGTTFAAAMYILGAIEIFLVYIVPRAAIFHSDDALKESAAMLNNMRVYGTAFLVLMVLVVFIGVRYVNKFASLFLACVIVSILAIYAGAIKSSFAPPHFPVCMLGNRTLSSRHIDVCSKTKEINNMTVPSKLWGFFCNSSQFFNATCDEYFVHNNVTSIQGIPGLASGIITENLWSNYLPKGEIIEKPSAKSSDVLGSLNHEYVLVDITTSFTLLVGIFFPSVTGIMAGSNRSGDLKDAQKSIPIGTILAILTTSFVYLSNVVLFGACIEGVVLRDKFGDAVKGNLVVGTLSWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIAKDNIIPFLRVFGHSKANGEPTWALLLTAAIAELGILIASLDLVAPILSMFFLMCYLFVNLACALQTLLRTPNWRPRFRYYHWALSFMGMSICLALMFISSWYYAIVAMVIAGMIYKYIEYQGAEKEWGDGIRGLSLSAARFALLRLEEGPPHTKNWRPQLLVLLKLDEDLHVKHPRLLTFASQLKAGKGLTIVGSVIVGNFLENYGEALAAEQTIKHLMEAEKVKGFCQLVVAAKLREGISHLIQSCGLGGMKHNTVVMGWPNGWRQSEDARAWKTFIGTVRVTTAAHLALLVAKNISFFPSNVEQFSEGNIDVWWIVHDGGMLMLLPFLLKQHKVWRKCSIRIFTVAQLEDNSIQMKKDLATFLYHLRIEAEVEVVEMHDSDISAYTYERTLMMEQRSQMLRHMRLSKTERDREAQLVKDRNSMLRLTSIGSDEDEETETYQEKVHMTWTKDKYMASRGQKAKSMEGFQDLLNMRPDQSNVRRMHTAVKLNEVIVNKSHEAKLVLLNMPGPPRNPEGDENYMEFLEVLTEGLERVLLVRGGGSEVITIYS TT8DFHE TT Literature-reported TT8DFHE RC R-HSA-426117:Cation-coupled Chloride cotransporters TT20AYF ID TT20AYF TT20AYF TN Solute carrier family 27 member 4 (SLC27A4) TT20AYF UP O95186 TT20AYF UC S27A4_HUMAN TT20AYF BC Carbon-sulfur ligase TT20AYF SN Long-chain fatty acid transport protein 4; Fatty acid transport protein 4; FATP4; FATP-4; ACSVL4 TT20AYF GN SLC27A4 TT20AYF FC Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids (VLCFAs). Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones (By similarity). TT20AYF EC EC 6.2.1.- TT20AYF SQ MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLLKVKAKVRQCLQERRTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAIVKDPLFYLDAQKGRYVPLDQEAYSRIQAGEEKL TT20AYF TT Literature-reported TTE5VI6 ID TTE5VI6 TTE5VI6 TN Sphingomyelin phosphodiesterase 2 (SMPD2) TTE5VI6 UP O60906 TTE5VI6 UC NSMA_HUMAN TTE5VI6 BC Phosphoric diester hydrolase TTE5VI6 SN SMPD2; Neutral sphingomyelinase; NSMase; N-SMase; Lyso-platelet activating factor-phospholipase C; Lyso-PAF-PLC TTE5VI6 GN SMPD2 TTE5VI6 FC Converts sphingomyelin to ceramide. Hydrolyze 1-acyl-2- lyso-sn-glycero-3-phosphocholine (lyso-PC) and 1-O-alkyl-2-lyso- sn-glycero-3-phosphocholine (lyso-platelet-activating factor). The physiological substrate seems to be Lyso-PAF. TTE5VI6 EC EC 3.1.4.12 TTE5VI6 SQ MKPNFSLRLRIFNLNCWGIPYLSKHRADRMRRLGDFLNQESFDLALLEEVWSEQDFQYLRQKLSPTYPAAHHFRSGIIGSGLCVFSKHPIQELTQHIYTLNGYPYMIHHGDWFSGKAVGLLVLHLSGMVLNAYVTHLHAEYNRQKDIYLAHRVAQAWELAQFIHHTSKKADVVLLCGDLNMHPEDLGCCLLKEWTGLHDAYLETRDFKGSEEGNTMVPKNCYVSQQELKPFPFGVRIDYVLYKAVSGFYISCKSFETTTGFDPHRGTPLSDHEALMATLFVRHSPPQQNPSSTHGPAERSPLMCVLKEAWTELGLGMAQARWWATFASYVIGLGLLLLALLCVLAAGGGAGEAAILLWTPSVGLVLWAGAFYLFHVQEVNGLYRAQAELQHVLGRAREAQDLGPEPQPALLLGQQEGDRTKEQ TTE5VI6 TT Literature-reported TTN0VRB ID TTN0VRB TTN0VRB TN Sphingosine-1-phosphate phosphatase 1 (SGPP1) TTN0VRB UP Q9BX95 TTN0VRB UC SGPP1_HUMAN TTN0VRB BC Phosphoric monoester hydrolase TTN0VRB SN hSPPase1; hSPP1; Spp1; Sphingosine-1-phosphatase 1; SPPase1; SGPP1 TTN0VRB GN SGPP1 TTN0VRB FC Has enzymatic activity against both sphingosine 1- phosphate (S1P) and dihydro-S1P. Regulates intracellular and extracellular S1P levels. TTN0VRB EC EC 3.1.3.- TTN0VRB SQ MSLRQRLAQLVGRLQDPQKVARFQRLCGVEAPPRRSADRREDEKAEAPLAGDPRLRGRQPGAPGGPQPPGSDRNQCPAKPDGGGAPNGVRNGLAAELGPASPRRAGALRRNSLTGEEGQLARVSNWPLYCLFCFGTELGNELFYILFFPFWIWNLDPLVGRRLVVIWVLVMYLGQCTKDIIRWPRPASPPVVKLEVFYNSEYSMPSTHAMSGTAIPISMVLLTYGRWQYPLIYGLILIPCWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFYPFVDLIDNFNQTHKYAPFIIIGLHLALGIFSFTLDTWSTSRGDTAEILGSGAGIACGSHVTYNMGLVLDPSLDTLPLAGPPITVTLFGKAILRILIGMVFVLIIRDVMKKITIPLACKIFNIPCDDIRKARQHMEVELPYRYITYGMVGFSITFFVPYIFFFIGIS TTN0VRB TT Literature-reported TTDYP7I ID TTDYP7I TTDYP7I TN Sphingosine-1-phosphate receptor 3 (S1PR3) TTDYP7I UP Q99500 TTDYP7I UC S1PR3_HUMAN TTDYP7I BC GPCR rhodopsin TTDYP7I SN Sphingosine 1-phosphate receptor Edg-3; S1PR3; S1P3; S1P receptor Edg-3; S1P receptor 3; Endothelial differentiation G-protein coupled receptor 3 TTDYP7I GN S1PR3 TTDYP7I FC Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis. TTDYP7I SQ MATALPPRLQPVRGNETLREHYQYVGKLAGRLKEASEGSTLTTVLFLVICSFIVLENLMVLIAIWKNNKFHNRMYFFIGNLALCDLLAGIAYKVNILMSGKKTFSLSPTVWFLREGSMFVALGASTCSLLAIAIERHLTMIKMRPYDANKRHRVFLLIGMCWLIAFTLGALPILGWNCLHNLPDCSTILPLYSKKYIAFCISIFTAILVTIVILYARIYFLVKSSSRKVANHNNSERSMALLRTVVIVVSVFIACWSPLFILFLIDVACRVQACPILFKAQWFIVLAVLNSAMNPVIYTLASKEMRRAFFRLVCNCLVRGRGARASPIQPALDPSRSKSSSSNNSSHSPKVKEDLPHTAPSSCIMDKNAALQNGIFCN TTDYP7I TT Patented-recorded TTDYP7I KE hsa04071:Sphingolipid signaling pathway; hsa04080:Neuroactive ligand-receptor interaction TTDYP7I RC R-HSA-418594:G alpha (i) signalling events; R-HSA-419408:Lysosphingolipid and LPA receptors TTZ8C5Q ID TTZ8C5Q TTZ8C5Q TN Sphingosine-1-phosphate receptor 4 (S1PR4) TTZ8C5Q UP O95977 TTZ8C5Q UC S1PR4_HUMAN TTZ8C5Q BC GPCR rhodopsin TTZ8C5Q SN Sphingosine 1-phosphate receptor Edg-6; Sphingosine 1-phosphate receptor 4; S1P4; S1P receptor Edg-6; S1P receptor 4; Endothelial differentiation G-protein coupled receptor 6; EDG6 TTZ8C5Q GN S1PR4 TTZ8C5Q FC Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. May be involved in cell migration processes that are specific for lymphocytes. TTZ8C5Q PD 2DCO TTZ8C5Q SQ MNATGTPVAPESCQQLAAGGHSRLIVLHYNHSGRLAGRGGPEDGGLGALRGLSVAASCLVVLENLLVLAAITSHMRSRRWVYYCLVNITLSDLLTGAAYLANVLLSGARTFRLAPAQWFLREGLLFTALAASTFSLLFTAGERFATMVRPVAESGATKTSRVYGFIGLCWLLAALLGMLPLLGWNCLCAFDRCSSLLPLYSKRYILFCLVIFAGVLATIMGLYGAIFRLVQASGQKAPRPAARRKARRLLKTVLMILLAFLVCWGPLFGLLLADVFGSNLWAQEYLRGMDWILALAVLNSAVNPIIYSFRSREVCRAVLSFLCCGCLRLGMRGPGDCLARAVEAHSGASTTDSSLRPRDSFRGSRSLSFRMREPLSSISSVRSI TTZ8C5Q TT Literature-reported TTI27M4 ID TTI27M4 TTI27M4 TN Staphylococcus ATP-dependent protease ClpP (Stap-coc CLPP) TTI27M4 UP P63786 TTI27M4 UC CLPP_STAAW TTI27M4 SN Stap-coc Endopeptidase Clp; ATP-dependent Clp protease proteolytic subunit TTI27M4 GN Stap-coc CLPP TTI27M4 FC Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. TTI27M4 EC EC 3.4.21.92 TTI27M4 PD 4EMP; 4EMM; 3STA; 3ST9 TTI27M4 SQ MNLIPTVIETTNRGERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDTDRDNFLTAEEAKEYGLIDEVMVPETK TTI27M4 TT Literature-reported TTN6GE9 ID TTN6GE9 TTN6GE9 TN Staphylococcus D-amino acid aminotransferase (Stap-coc dat) TTN6GE9 UP P54694 TTN6GE9 UC DAAA_STAHA TTN6GE9 BC Transaminase TTN6GE9 SN Stap-coc dat; DAAT; D-aspartate aminotransferase; D-amino acid transaminase; D-alanine aminotransferase TTN6GE9 GN Stap-coc dat TTN6GE9 FC Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine andan alpha- keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D- amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components. TTN6GE9 EC EC 2.6.1.21 TTN6GE9 SQ MTKVFINGEFIDQNEAKVSYEDRGYVFGDGIYEYIRAYDGKLFTVTEHFERFIRSASEIQLDLGYTVEELIDVVRELLKVNNIQNGGIYIQATRGVAPRNHSFPTPEVKPVIMAFAKSYDRPYDDLENGINAATVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNAGEAIQHRGETVTEGASSNVYAIKDGAIYTHPVNNYILNGITRKVIKWISEDEDIPFKEETFTVEFLKNADEVIVSSTSAEVTPVVKIDGEQVGDGKVGPVTRQLQEGFNKYIESRSS TTN6GE9 TT Literature-reported TT8HWCD ID TT8HWCD TT8HWCD TN Staphylococcus DHNA-CoA synthase (Stap-coc menB) TT8HWCD UP Q5HH38 TT8HWCD UC MENB_STAAC TT8HWCD BC Carbon-carbon lyase TT8HWCD SN DHNA-CoA synthase; 1,4-dihydroxy-2-naphthoyl-CoA synthase TT8HWCD GN Stap-coc menB TT8HWCD FC Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA). TT8HWCD PD 2UZF TT8HWCD SQ MTNRQWETLREYDEIKYEFYEGIAKVTINRPEVRNAFTPKTVAEMIDAFSRARDDQNVSVIVLTGEGDLAFCSGGDQKKRGHGGYVGEDQIPRLNVLDLQRLIRIIPKPVIAMVKGYAVGGGNVLNVVCDLTIAADNAIFGQTGPKVGSFDAGYGSGYLARIVGHKKAREIWYLCRQYNAQEALDMGLVNTVVPLEKVEDETVQWCKEIMKHSPTALRFLKAAMNADTDGLAGLQQMAGDATLLYYTTDEAKEGRDAFKEKRDPDFDQFPKFP TT8HWCD TT Literature-reported TTR413K ID TTR413K TTR413K TN Staphylococcus Quinolone resistance protein norA (Stap-coc norA) TTR413K UP P0A0J7 TTR413K UC NORA_STAAU TTR413K BC Major facilitator superfamily TTR413K SN norA TTR413K GN Stap-coc norA TTR413K FC Involved in quinolone resistance. May constitute a membrane-associated active efflux pump of hydrophilic quinolones. TTR413K SQ MNKQIFVLYFNIFLIFLGIGLVIPVLPVYLKDLGLTGSDLGLLVAAFALSQMIISPFGGTLADKLGKKLIICIGLILFSVSEFMFAVGHNFSVLMLSRVIGGMSAGMVMPGVTGLIADISPSHQKAKNFGYMSAIINSGFILGPGIGGFMAEVSHRMPFYFAGALGILAFIMSIVLIHDPKKSTTSGFQKLEPQLLTKINWKVFITPVILTLVLSFGLSAFETLYSLYTADKVNYSPKDISIAITGGGIFGALFQIYFFDKFMKYFSELTFIAWSLLYSVVVLILLVFANGYWSIMLISFVVFIGFDMIRPAITNYFSNIAGERQGFAGGLNSTFTSMGNFIGPLIAGALFDVHIEAPIYMAIGVSLAGVVIVLIEKQHRAKLKEQNM TTR413K TT Literature-reported TT30FX2 ID TT30FX2 TT30FX2 TN Staphylococcus Replicative DNA helicase (Stap-coc dnaC) TT30FX2 UP W8U2K6 TT30FX2 UC W8U2K6_STAAU TT30FX2 BC Acid anhydride hydrolase TT30FX2 SN Replicative DNA helicase TT30FX2 GN Stap-coc dnaC TT30FX2 FC Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. TT30FX2 EC EC 3.6.4.12 TT30FX2 SQ MDRMYEQNQMPHNNEAEQSVLGSIIIDPELINTTQEVLLPESFYRGAHQHIFRAMMHLNEDNKEIDVVTLMDQLSTEGTLNEAGGPQYLAELSTNVPTTRNVQYYTDIVSKHALKRRLIQTADSIANDGYNDELELDAILSDAERRILELSSSRESDGFKDIRDVLGQVYETAEELDQNSGQTPGIPTGYRDLDQMTAGFNRNDLIILAARPSVGKTAFALNIAQKVATHEDMYTVGIFSLEMGADQLATRMICSSGNVDSNRLRTGTMTEEDWSRFTIAVGKLSRTKIFIDDTPGIRINDLRSKCRRLKQEHGLDMIVIDYLQLIQGSGSRASDNRQQEVSEISRTLKALARELECPVIALSQLSRGVEQRQDKRPMMSDIRESGSIEQDADIVAFLYRDDYYNRGGDEDDDDDGGFEPQTNDENGEIEIIIAKQRNGPTGTVKLHFMKQYNKFTDIDYAHADMM TT30FX2 TT Literature-reported TT8K4DE ID TT8K4DE TT8K4DE TN STE20-related serine/threonine-protein kinase (SLK) TT8K4DE UP Q9H2G2 TT8K4DE UC SLK_HUMAN TT8K4DE SN hSLK; STE20-related kinase; STE20-like kinase TT8K4DE GN SLK TT8K4DE FC Mediates apoptosis and actin stress fiber dissolution. TT8K4DE EC EC 2.7.11.1 TT8K4DE PD 6HVD; 4USF; 2UV2; 2JFM; 2JFL TT8K4DE SQ MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEDFWEIIGELGDGAFGKVYKAQNKETSVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLDALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSSNFKDFLKKCLEKNVDARWTTSQLLQHPFVTVDSNKPIRELIAEAKAEVTEEVEDGKEEDEEEETENSLPIPASKRASSDLSIASSEEDKLSQNACILESVSEKTERSNSEDKLNSKILNEKPTTDEPEKAVEDINEHITDAQLEAMTELHDRTAVIKENEREKRPKLENLPDTEDQETVDINSVSEGKENNIMITLETNIEHNLKSEEEKDQEKQQMFENKLIKSEEIKDTILQTVDLVSQETGEKEANIQAVDSEVGLTKEDTQEKLGEDDKTQKDVISNTSDVIGTCEAADVAQKVDEDSAEDTQSNDGKEVVEVGQKLINKPMVGPEAGGTKEVPIKEIVEMNEIEEGKNKEQAINSSENIMDINEEPGTTEGEEITESSSTEEMEVRSVVADTDQKALGSEVQDASKVTTQIDKEKKEIPVSIKKEPEVTVVSQPTEPQPVLIPSININSDSGENKEEIGSLSKTETILPPESENPKENDNDSGTGSTADTSSIDLNLSISSFLSKTKDSGSISLQETRRQKKTLKKTRKFIVDGVEVSVTTSKIVTDSDSKTEELRFLRRQELRELRFLQKEEQRAQQQLNSKLQQQREQIFRRFEQEMMSKKRQYDQEIENLEKQQKQTIERLEQEHTNRLRDEAKRIKGEQEKELSKFQNMLKNRKKEVINEVEKAPKELRKELMKRRKEELAQSQHAQEQEFVQKQQQELDGSLKKIIQQQKAELANIERECLNNKQQLMRAREAAIWELEERHLQEKHQLLKQQLKDQYFMQRHQLLKRHEKETEQMQRYNQRLIEELKNRQTQERARLPKIQRSEAKTRMAMFKKSLRINSTATPDQDRDKIKQFAAQEEKRQKNERMAQHQKHENQMRDLQLQCEANVRELHQLQNEKCHLLVEHETQKLKELDEEHSQELKEWREKLRPRKKTLEEEFARKLQEQEVFFKMTGESECLNPSTQSRISKFYPIPSLHSTGS TT8K4DE TT Literature-reported TTI5OJM ID TTI5OJM TTI5OJM TN Streptococcus Signal peptidase I (Stre-coc lepB) TTI5OJM UP O07344 TTI5OJM UC LEP_STRPN TTI5OJM BC Peptidase TTI5OJM SN Signal peptidase I; SPase I; Leader peptidase I TTI5OJM GN Stre-coc lepB TTI5OJM FC Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. TTI5OJM EC EC 3.4.21.89 TTI5OJM SQ MNSFKNFLKEWGLFLLILSLLALSRIFFWSNVRVEGHSMDPTLADGEILFVVKHLPIDRFDIVVAHEEDGNKDIVKRVIGMPGDTIRYENDKLYINDKETDEPYLADYIKRFKDDKLQSTYSGKGFEGNKGTFFRSIAQKAQAFTVDVNYNTNFSFTVPEGEYLLLGDDRLVSSDSRHVGTFKAKDITGEAKFRLWPITRIGTF TTI5OJM TT Literature-reported TTFHEWL ID TTFHEWL TTFHEWL TN Streptomyces RNA methyltransferase (Stre-myc carB) TTFHEWL UP P13079 TTFHEWL UC CARB_STRTH TTFHEWL BC Methyltransferase TTFHEWL SN carB; RNA methyltransferase TTFHEWL GN Stre-myc carB TTFHEWL FC Probable RNA methylase. Confers resistance to carbomycin and several other macrolides, lincomycin and vernamycin B, but not to all macrolide-lincosamide-streptogramin B antibiotics. TTFHEWL EC EC 2.1.1.- TTFHEWL SQ MAALLKRILRRRMAEKRSGRGRMAAARTTGAQSRKTAQRSGRSEADRRRRVHGQNFLVDRETVQRFVRFADPDPGEVVLEVGAGNGAITRELARLCRRVVAYEIDRHFADRLREATAEDPRIEVVAGDFLKTSQPKVPFSVVGNIPFGNTADIVDWCLNARRLRTTTLVTQLEYARKRTGGYRRWSRLTVATWPEVEWRMGERISRRWFRPVPAVDSAVLRLERRPVPLIPPGLMHDFRDLVETGFTGKGGSLDASLRRRFPARRVAAGFRRARLEQGVVVAYVTPGQWITLFEELHGR TTFHEWL TT Literature-reported TT5H2F0 ID TT5H2F0 TT5H2F0 TN Syndecan-2 (SDC2) TT5H2F0 UP P34741 TT5H2F0 UC SDC2_HUMAN TT5H2F0 BC Peptide translocating syndecan TT5H2F0 SN SYND2; Heparan sulfate proteoglycan core protein; HSPG1; HSPG; Fibroglycan; CD362 TT5H2F0 GN SDC2 TT5H2F0 FC Cell surface proteoglycan that bears heparan sulfate. Regulates dendritic arbor morphogenesis (By similarity). TT5H2F0 PD 6ITH TT5H2F0 SQ MRRAWILLTLGLVACVSAESRAELTSDKDMYLDNSSIEEASGVYPIDDDDYASASGSGADEDVESPELTTSRPLPKILLTSAAPKVETTTLNIQNKIPAQTKSPEETDKEKVHLSDSERKMDPAEEDTNVYTEKHSDSLFKRTEVLAAVIAGGVIGFLFAIFLILLLVYRMRKKDEGSYDLGERKPSSAAYQKAPTKEFYA TT5H2F0 TT Literature-reported TT5H2F0 FM Syndecan proteoglycan TT8XKYM ID TT8XKYM TT8XKYM TN Synovial apoptosis inhibitor 1 (SYVN1) TT8XKYM UP Q86TM6 TT8XKYM UC SYVN1_HUMAN TT8XKYM BC Acyltransferase TT8XKYM SN RING-type E3 ubiquitin transferase synoviolin; KIAA1810; HRD1; E3 ubiquitinprotein ligase synoviolin; E3 ubiquitin-protein ligase synoviolin TT8XKYM GN SYVN1 TT8XKYM FC Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis. Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1. Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. TT8XKYM EC EC 2.3.2.27 TT8XKYM SQ MFRTAVMMAASLALTGAVVAHAYYLKHQFYPTVVYLTKSSPSMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTETCLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVDFMERSPNISWLFHCRIVSLMFLLGILDFLFVSHAYHSILTRGASVQLVFGFEYAILMTMVLTIFIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPLFAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRASLPAQSPPPPEPADQGPPPAPHPPPLLPQPPNFPQGLLPPFPPGMFPLWPPMGPFPPVPPPPSSGEAVAPPSTSAAALSRPSGAATTTAAGTSATAASATASGPGSGSAPEAGPAPGFPFPPPWMGMPLPPPFAFPPMPVPPAGFAGLTPEELRALEGHERQHLEARLQSLRNIHTLLDAAMLQINQYLTVLASLGPPRPATSVNSTEETATTVVAAASSTSIPSSEATTPTPGASPPAPEMERPPAPESVGTEEMPEDGEPDAAELRRRRLQKLESPVAH TT8XKYM TT Literature-reported TT8XKYM FM Carbon-nitrogen ligase TTO7L0V ID TTO7L0V TTO7L0V TN TAO kinase 3 (TAOK3) TTO7L0V UP Q9H2K8 TTO7L0V UC TAOK3_HUMAN TTO7L0V SN hKFC-A; Thousand and one amino acid protein 3; Serine/threonine-protein kinase TAO3; MAP3K18; Kinase from chicken homolog A; KDS; Jun kinase-inhibitory kinase; JNK/SAPK-inhibitory kinase; JIK; Dendritic cell-derived protein kinase; DPK; Cutaneous T-cell lymphoma-associated antigen HD-CL-09; CTCL-associated antigen HD-CL-09 TTO7L0V GN TAOK3 TTO7L0V FC Serine/threonine-protein kinase that acts as a regulator of the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Inhibits basal activity of MAPK8/JNK cascade and diminishes its activation in response epidermal growth factor (EGF). TTO7L0V EC EC 2.7.11.1 TTO7L0V PD 6BDN TTO7L0V SQ MRKGVLKDPEIADLFYKDDPEELFIGLHEIGHGSFGAVYFATNAHTSEVVAIKKMSYSGKQTHEKWQDILKEVKFLRQLKHPNTIEYKGCYLKEHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALHGLAYLHSHALIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLQSNEWTDSFRRFVDYCLQKIPQERPTSAELLRHDFVRRDRPLRVLIDLIQRTKDAVRELDNLQYRKMKKILFQETRNGPLNESQEDEEDSEHGTSLNREMDSLGSNHSIPSMSVSTGSQSSSVNSMQEVMDESSSELVMMHDDESTINSSSSVVHKKDHVFIRDEAGHGDPRPEPRPTQSVQSQALHYRNRERFATIKSASLVTRQIHEHEQENELREQMSGYKRMRRQHQKQLIALENKLKAEMDEHRLKLQKEVETHANNSSIELEKLAKKQVAIIEKEAKVAAADEKKFQQQILAQQKKDLTTFLESQKKQYKICKEKIKEEMNEDHSTPKKEKQERISKHKENLQHTQAEEEAHLLTQQRLYYDKNCRFFKRKIMIKRHEVEQQNIREELNKKRTQKEMEHAMLIRHDESTRELEYRQLHTLQKLRMDLIRLQHQTELENQLEYNKRRERELHRKHVMELRQQPKNLKAMEMQIKKQFQDTCKVQTKQYKALKNHQLEVTPKNEHKTILKTLKDEQTRKLAILAEQYEQSINEMMASQALRLDEAQEAECQALRLQLQQEMELLNAYQSKIKMQTEAQHERELQKLEQRVSLRRAHLEQKIEEELAALQKERSERIKNLLERQEREIETFDMESLRMGFGNLVTLDFPKEDYR TTO7L0V TT Literature-reported TTHPOGR ID TTHPOGR TTHPOGR TN Tau messenger RNA (TAU mRNA) TTHPOGR UP P10636 TTHPOGR UC TAU_HUMAN TTHPOGR BC mRNA target TTHPOGR SN tau phosphorylation (mRNA); TAU (mRNA); Paired helical filamenttau (mRNA); Paired helical filament-tau (mRNA); PHFtau (mRNA); PHF-tau (mRNA); Neurofibrillary tangle protein (mRNA); Microtubule-associated protein tau (mRNA); MTBT1 (mRNA); MAPTL (mRNA) TTHPOGR GN MAPT TTHPOGR FC The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. TTHPOGR PD 6QJQ; 6QJP; 6QJM; 6QJH; 6NWQ TTHPOGR SQ MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPAQDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSSDPLIQPSSPAVCPEPPSSPKYVSSVTSRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL TTHPOGR TT Literature-reported TTHPOGR FM mRNA target TTQGAVX ID TTQGAVX TTQGAVX TN Telomerase protein component 1 (TEP1) TTQGAVX UP Q99973 TTQGAVX UC TEP1_HUMAN TTQGAVX SN p80 telomerase homolog; p240; Telomerase-associated protein 1; Telomerase protein 1; TP1; TLP1 TTQGAVX GN TEP1 TTQGAVX FC Component of the ribonucleoprotein vaults particle, a multi-subunit structure involved in nucleo-cytoplasmic transport. Responsible for the localizing and stabilizing vault RNA (vRNA) association in the vault ribonucleoprotein particle. Binds to TERC. Component of the telomerase ribonucleoprotein complex that is essential for the replication of chromosome termini. TTQGAVX SQ MEKLHGHVSAHPDILSLENRCLAMLPDLQPLEKLHQHVSTHSDILSLKNQCLATLPDLKTMEKPHGYVSAHPDILSLENQCLATLSDLKTMEKPHGHVSAHPDILSLENRCLATLSSLKSTVSASPLFQSLQISHMTQADLYRVNNSNCLLSEPPSWRAQHFSKGLDLSTCPIALKSISATETAQEATLGRWFDSEEKKGAETQMPSYSLSLGEEEEVEDLAVKLTSGDSESHPEPTDHVLQEKKMALLSLLCSTLVSEVNMNNTSDPTLAAIFEICRELALLEPEFILKASLYARQQLNVRNVANNILAIAAFLPACRPHLRRYFCAIVQLPSDWIQVAELYQSLAEGDKNKLVPLPACLRTAMTDKFAQFDEYQLAKYNPRKHRAKRHPRRPPRSPGMEPPFSHRCFPRYIGFLREEQRKFEKAGDTVSEKKNPPRFTLKKLVQRLHIHKPAQHVQALLGYRYPSNLQLFSRSRLPGPWDSSRAGKRMKLSRPETWERELSLRGNKASVWEELIENGKLPFMAMLRNLCNLLRVGISSRHHELILQRLQHAKSVIHSRQFPFRFLNAHDAIDALEAQLRNQALPFPSNITLMRRILTRNEKNRPRRRFLCHLSRQQLRMAMRIPVLYEQLKREKLRVHKARQWKYDGEMLNRYRQALETAVNLSVKHSLPLLPGRTVLVYLTDANADRLCPKSNPQGPPLNYALLLIGMMITRAEQVDVVLCGGDTLKTAVLKAEEGILKTAIKLQAQVQEFDENDGWSLNTFGKYLLSLAGQRVPVDRVILLGQSMDDGMINVAKQLYWQRVNSKCLFVGILLRRVQYLSTDLNPNDVTLSGCTDAILKFIAEHGASHLLEHVGQMDKIFKIPPPPGKTGVQSLRPLEEDTPSPLAPVSQQGWRSIRLFISSTFRDMHGERDLLLRSVLPALQARAAPHRISLHGIDLRWGVTEEETRRNRQLEVCLGEVENAQLFVGILGSRYGYIPPSYNLPDHPHFHWAQQYPSGRSVTEMEVMQFLNRNQRLQPSAQALIYFRDSSFLSSVPDAWKSDFVSESEEAARRISELKSYLSRQKGITCRRYPCEWGGVAAGRPYVGGLEEFGQLVLQDVWNMIQKLYLQPGALLEQPVSIPDDDLVQATFQQLQKPPSPARPRLLQDTVQRLMLPHGRLSLVTGQSGQGKTAFLASLVSALQAPDGAKVASLVFFHFSGARPDQGLALTLLRRLCTYLRGQLKEPGALPSTYRSLVWELQQRLLPKSAESLHPGQTQVLIIDGADRLVDQNGQLISDWIPKKLPRCVHLVLSVSSDAGLGETLEQSQGAHVLALGPLEASARARLVREELALYGKRLEESPFNNQMRLLLVKRESGRPLYLRLVTDHLRLFTLYEQVSERLRTLPATVPLLLQHILSTLEKEHGPDVLPQALTALEVTRSGLTVDQLHGVLSVWRTLPKGTKSWEEAVAAGNSGDPYPMGPFACLVQSLRSLLGEGPLERPGARLCLPDGPLRTAAKRCYGKRPGLEDTAHILIAAQLWKTCDADASGTFRSCPPEALGDLPYHLLQSGNRGLLSKFLTNLHVVAAHLELGLVSRLLEAHALYASSVPKEEQKLPEADVAVFRTFLRQQASILSQYPRLLPQQAANQPLDSPLCHQASLLSRRWHLQHTLRWLNKPRTMKNQQSSSLSLAVSSSPTAVAFSTNGQRAAVGTANGTVYLLDLRTWQEEKSVVSGCDGISACLFLSDDTLFLTAFDGLLELWDLQHGCRVLQTKAHQYQITGCCLSPDCRLLATVCLGGCLKLWDTVRGQLAFQHTYPKSLNCVAFHPEGQVIATGSWAGSISFFQVDGLKVTKDLGAPGASIRTLAFNVPGGVVAVGRLDSMVELWAWREGARLAAFPAHHGFVAAALFLHAGCQLLTAGEDGKVQVWSGSLGRPRGHLGSLSLSPALSVALSPDGDRVAVGYRADGIRIYKISSGSQGAQGQALDVAVSALAWLSPKVLVSGAEDGSLQGWALKECSLQSLWLLSRFQKPVLGLATSQELLASASEDFTVQLWPRQLLTRPHKAEDFPCGTELRGHEGPVSCCSFSTDGGSLATGGRDRSLLCWDVRTPKTPVLIHSFPACHRDWVTGCAWTKDNLLISCSSDGSVGLWDPESGQRLGQFLGHQSAVSAVAAVEEHVVSVSRDGTLKVWDHQGVELTSIPAHSGPISHCAAAMEPRAAGQPGSELLVVTVGLDGATRLWHPLLVCQTHTLLGHSGPVRAAAVSETSGLMLTASEDGSVRLWQVPKEADDTCIPRSSAAVTAVAWAPDGSMAVSGNQAGELILWQEAKAVATAQAPGHIGALIWSSAHTFFVLSADEKISEWQVKLRKGSAPGNLSLHLNRILQEDLGVLTSLDWAPDGHFLILAKADLKLLCMKPGDAPSEIWSSYTENPMILSTHKEYGIFVLQPKDPGVLSFLRQKESGEFEERLNFDINLENPSRTLISITQAKPESESSFLCASSDGILWNLAKCSPEGEWTTGNMWQKKANTPETQTPGTDPSTCRESDASMDSDASMDSEPTPHLKTRQRRKIHSGSVTALHVLPELLVTASKDRDVKLWERPSMQLLGLFRCEGSVSCLEPWLGANSTLQLAVGDVQGNVYFLNWE TTQGAVX TT Literature-reported TT9AXQM ID TT9AXQM TT9AXQM TN TGFA messenger RNA (TGFA mRNA) TT9AXQM UP P01135 TT9AXQM UC TGFA_HUMAN TT9AXQM BC mRNA target TT9AXQM SN TGF-alpha (40-89) (mRNA); TGF type 1 (40-89) (mRNA); Protransforming growth factor alpha (40-89) (mRNA); ETGF (40-89) (mRNA); EGF-like TGF (40-89) (mRNA) TT9AXQM GN TGFA TT9AXQM FC TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar. TT9AXQM PD 5KN5; 4TGF; 3TGF; 3.00E+50; 2TGF TT9AXQM SQ MVPSAGQLALFALGIVLAACQALENSTSPLSADPPVAAAVVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLAVVAASQKKQAITALVVVSIVALAVLIITCVLIHCCQVRKHCEWCRALICRHEKPSALLKGRTACCHSETVV TT9AXQM TT Literature-reported TT9AXQM FM mRNA target TTFGN19 ID TTFGN19 TTFGN19 TN TGF-beta-stimulated factor 1 (STK16) TTFGN19 UP O75716 TTFGN19 UC STK16_HUMAN TTFGN19 SN hPSK; Tyrosine-protein kinase STK16; TSF1; TSF-1; Serine/threonine-protein kinase 16; Protein kinase PKL12; PKL12; Myristoylated and palmitoylated serine/threonine-protein kinase; MPSK1; MPSK TTFGN19 GN STK16 TTFGN19 FC Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. TTFGN19 EC EC 2.7.11.1 TTFGN19 PD 2BUJ TTFGN19 SQ MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQHTTQI TTFGN19 TT Literature-reported TTL0E3Y ID TTL0E3Y TTL0E3Y TN Thioredoxin domain-contained protein 12 (TXNDC12) TTL0E3Y UP O95881 TTL0E3Y UC TXD12_HUMAN TTL0E3Y SN hTLP19; UNQ713/PRO1376; Thioredoxin-like protein p19; Thioredoxin domain-containing protein 12; TLP19; Endoplasmic reticulum resident protein 19; Endoplasmic reticulum resident protein 18; ERp19; ERp18; ER protein 19; ER protein 18 TTL0E3Y GN TXNDC12 TTL0E3Y FC Possesses significant protein thiol-disulfide oxidase activity. TTL0E3Y EC EC 1.8.4.2 TTL0E3Y PD 2K8V; 1SEN TTL0E3Y SQ METRPRLGATCLLGFSFLLLVISSDGHNGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDPSGKVHPEIINENGNPSYKYFYVSAEQVVQGMKEAQERLTGDAFRKKHLEDEL TTL0E3Y TT Literature-reported TTRMZ0N ID TTRMZ0N TTRMZ0N TN Thymic stromal lymphoprotein receptor (CRLF2) TTRMZ0N UP Q9HC73 TTRMZ0N UC CRLF2_HUMAN TTRMZ0N BC Cytokine receptor TTRMZ0N SN Thymic stromal lymphopoietin protein receptor; TSLP receptor; ILXR; Cytokine receptorlike factor 2; Cytokine receptorlike 2; CRLF2 TTRMZ0N GN CRLF2 TTRMZ0N FC Receptor for thymic stromal lymphopoietin (TSLP). Forms a functional complex with TSLP and IL7R which is capable of stimulating cell proliferation through activation of STAT3 and STAT5. Also activates JAK2. Implicated in the development of the hematopoietic system. TTRMZ0N PD 5J12; 5J11 TTRMZ0N SQ MGRLVLLWGAAVFLLGGWMALGQGGAAEGVQIQIIYFNLETVQVTWNASKYSRTNLTFHYRFNGDEAYDQCTNYLLQEGHTSGCLLDAEQRDDILYFSIRNGTHPVFTASRWMVYYLKPSSPKHVRFSWHQDAVTVTCSDLSYGDLLYEVQYRSPFDTEWQSKQENTCNVTIEGLDAEKCYSFWVRVKAMEDVYGPDTYPSDWSEVTCWQRGEIRDACAETPTPPKPKLSKFILISSLAILLMVSLLLLSLWKLWRVKKFLIPSVPDPKSIFPGLFEIHQGNFQEWITDTQNVAHLHKMAGAEQESGPEEPLVVQLAKTEAESPRMLDPQTEEKEASGGSLQLPHQPLQGGDVVTIGGFTFVMNDRSYVAL TTRMZ0N TT Literature-reported TTMVAIU ID TTMVAIU TTMVAIU TN Thymosin beta-4 (TMSB4X) TTMVAIU UP P62328 TTMVAIU UC TYB4_HUMAN TTMVAIU BC Thymosin family TTMVAIU SN TMSB4X; T beta-4; Fx TTMVAIU GN TMSB4X TTMVAIU FC Seraspenide inhibits the entry of hematopoietic pluripotent stem cellsinto the S-phase. TTMVAIU PD 4PL8; 4PL7; 3TU5; 1UY5 TTMVAIU SQ MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES TTMVAIU TT Literature-reported TTKHTGE ID TTKHTGE TTKHTGE TN Thyroid receptor-interacting protein 10 (TRIP10) TTKHTGE UP Q15642 TTKHTGE UC CIP4_HUMAN TTKHTGE SN hSTP; TRIP-10; TR-interacting protein 10; Salt tolerant protein; STP; STOT; Protein Felic; Cdc42-interacting protein 4; CIP4 TTKHTGE GN TRIP10 TTKHTGE FC Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL. Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling. TTKHTGE PD 2KE4; 2EFK; 2CT4 TTKHTGE SQ MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN TTKHTGE TT Literature-reported TTKHTGE KE hsa04910:Insulin signaling pathway TTPB1W3 ID TTPB1W3 TTPB1W3 TN TRAF2 and NCK interacting kinase (TNIK) TTPB1W3 UP Q9UKE5 TTPB1W3 UC TNIK_HUMAN TTPB1W3 SN TRAF2 and NCK-interacting protein kinase; KIAA0551 TTPB1W3 GN TNIK TTPB1W3 FC Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading. Phosphorylates SMAD1 on Thr-322. TTPB1W3 EC EC 2.7.11.1 TTPB1W3 PD 5D7A; 5CWZ; 5AX9; 2X7F TTPB1W3 SQ MASDSPARSLDEIDLSALRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPPGMDDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKSKKWSKKFQSFIESCLVKNHSQRPATEQLMKHPFIRDQPNERQVRIQLKDHIDRTKKKRGEKDETEYEYSGSEEEEEENDSGEPSSILNLPGESTLRRDFLRLQLANKERSEALRRQQLEQQQRENEEHKRQLLAERQKRIEEQKEQRRRLEEQQRREKELRKQQEREQRRHYEEQMRREEERRRAEHEQEYIRRQLEEEQRQLEILQQQLLHEQALLLEYKRKQLEEQRQAERLQRQLKQERDYLVSLQHQRQEQRPVEKKPLYHYKEGMSPSEKPAWAKEVEERSRLNRQSSPAMPHKVANRISDPNLPPRSESFSISGVQPARTPPMLRPVDPQIPHLVAVKSQGPALTASQSVHEQPTKGLSGFQEALNVTSHRVEMPRQNSDPTSENPPLPTRIEKFDRSSWLRQEEDIPPKVPQRTTSISPALARKNSPGNGSALGPRLGSQPIRASNPDLRRTEPILESPLQRTSSGSSSSSSTPSSQPSSQGGSQPGSQAGSSERTRVRANSKSEGSPVLPHEPAKVKPEESRDITRPSRPASYKKAIDEDLTALAKELRELRIEETNRPMKKVTDYSSSSEESESSEEEEEDGESETHDGTVAVSDIPRLIPTGAPGSNEQYNVGMVGTHGLETSHADSFSGSISREGTLMIRETSGEKKRSGHSDSNGFAGHINLPDLVQQSHSPAGTPTEGLGRVSTHSQEMDSGTEYGMGSSTKASFTPFVDPRVYQTSPTDEDEEDEESSAAALFTSELLRQEQAKLNEARKISVVNVNPTNIRPHSDTPEIRKYKKRFNSEILCAALWGVNLLVGTENGLMLLDRSGQGKVYNLINRRRFQQMDVLEGLNVLVTISGKKNKLRVYYLSWLRNRILHNDPEVEKKQGWITVGDLEGCIHYKVVKYERIKFLVIALKNAVEIYAWAPKPYHKFMAFKSFADLQHKPLLVDLTVEEGQRLKVIFGSHTGFHVIDVDSGNSYDIYIPSHIQGNITPHAIVILPKTDGMEMLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIHSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVFFMTLNRNSMMNW TTPB1W3 TT Literature-reported TTULOD8 ID TTULOD8 TTULOD8 TN Transcription factor E2-alpha (TCF3) TTULOD8 UP P15923 TTULOD8 UC TFE2_HUMAN TTULOD8 SN bHLHb21; Transcription factor ITF-1; Transcription factor 3; TCF-3; Kappa-E2-binding factor; Immunoglobulin transcription factor 1; Immunoglobulin enhancer-binding factor E12/E47; ITF1; E2A; Class B basic helix-loop-helix protein 21 TTULOD8 GN TCF3 TTULOD8 FC Transcriptional regulator. Involved in the initiation of neuronal differentiation. Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation. Dimers bind DNA on E-box motifs: 5'-CANNTG-3'. Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer. Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region. TTULOD8 PD 3U5V; 2YPB; 2YPA; 2MH0; 1HLH TTULOD8 SQ MNQPQRMAPVGTDKELSDLLDFSMMFPLPVTNGKGRPASLAGAQFGGSGLEDRPSSGSWGSGDQSSSSFDPSRTFSEGTHFTESHSSLSSSTFLGPGLGGKSGERGAYASFGRDAGVGGLTQAGFLSGELALNSPGPLSPSGMKGTSQYYPSYSGSSRRRAADGSLDTQPKKVRKVPPGLPSSVYPPSSGEDYGRDATAYPSAKTPSSTYPAPFYVADGSLHPSAELWSPPGQAGFGPMLGGGSSPLPLPPGSGPVGSSGSSSTFGGLHQHERMGYQLHGAEVNGGLPSASSFSSAPGATYGGVSSHTPPVSGADSLLGSRGTTAGSSGDALGKALASIYSPDHSSNNFSSSPSTPVGSPQGLAGTSQWPRAGAPGALSPSYDGGLHGLQSKIEDHLDEAIHVLRSHAVGTAGDMHTLLPGHGALASGFTGPMSLGGRHAGLVGGSHPEDGLAGSTSLMHNHAALPSQPGTLPDLSRPPDSYSGLGRAGATAAASEIKREEKEDEENTSAADHSEEEKKELKAPRARTSPDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLNSEKPQTKLLILHQAVSVILNLEQQVRERNLNPKAACLKRREEEKVSGVVGDPQMVLSAPHPGLSEAHNPAGHM TTULOD8 TT Literature-reported TTULOD8 KE hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa05166:Human T-cell leukemia virus 1 infection; hsa05202:Transcriptional misregulation in cancer TT8MG4S ID TT8MG4S TT8MG4S TN Transferrin receptor protein 1 (TFRC) TT8MG4S UP P02786 TT8MG4S UC TFR1_HUMAN TT8MG4S BC Peptidase TT8MG4S SN Trfr; TfR1; TfR; TR protein; T9; P90; CD71 antigen; CD71 TT8MG4S GN TFRC TT8MG4S FC Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake. Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. TT8MG4S PD 6H5I; 6GSR; 6D05; 6D04; 6D03 TT8MG4S SQ MMDQARSAFSNLFGGEPLSYTRFSLARQVDGDNSHVEMKLAVDEEENADNNTKANVTKPKRCSGSICYGTIAVIVFFLIGFMIGYLGYCKGVEPKTECERLAGTESPVREEPGEDFPAARRLYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF TT8MG4S TT Clinical trial TT8MG4S FM Peptidase TTP6BIJ ID TTP6BIJ TTP6BIJ TN Transgelin-2 (TAGLN2) TTP6BIJ UP P37802 TTP6BIJ UC TAGL2_HUMAN TTP6BIJ BC Calponin family TTP6BIJ SN SM22-alpha homolog; KIAA0120; Epididymis tissue protein Li 7e TTP6BIJ GN TAGLN2 TTP6BIJ FC cytosol, extracellular exosome, extracellular region, vesicle, cadherin binding, epithelial cell differentiation, platelet degranulation. TTP6BIJ PD 1WYM TTP6BIJ SQ MANRGPAYGLSREVQQKIEKQYDADLEQILIQWITTQCRKDVGRPQPGRENFQNWLKDGTVLCELINALYPEGQAPVKKIQASTMAFKQMEQISQFLQAAERYGINTTDIFQTVDLWEGKNMACVQRTLMNLGGLAVARDDGLFSGDPNWFPKKSKENPRNFSDNQLQEGKNVIGLQMGTNRGASQAGMTGYGMPRQIL TTP6BIJ TT Literature-reported TTBECWA ID TTBECWA TTBECWA TN Transient receptor potential cation channel V2 (TRPV2) TTBECWA UP Q9Y5S1 TTBECWA UC TRPV2_HUMAN TTBECWA BC Transient receptor potential catioin channel TTBECWA SN Vanilloid receptor-like protein 1; VRL-1; VRL; TrpV2; Transient receptor potential cation channel subfamily V member 2; Osm-9-like TRP channel 2; OTRPC2 TTBECWA GN TRPV2 TTBECWA FC Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF-I, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH. TTBECWA PD 2F37 TTBECWA SQ MTSPSSSPVFRLETLDGGQEDGSEADRGKLDFGSGLPPMESQFQGEDRKFAPQIRVNLNYRKGTGASQPDPNRFDRDRLFNAVSRGVPEDLAGLPEYLSKTSKYLTDSEYTEGSTGKTCLMKAVLNLKDGVNACILPLLQIDRDSGNPQPLVNAQCTDDYYRGHSALHIAIEKRSLQCVKLLVENGANVHARACGRFFQKGQGTCFYFGELPLSLAACTKQWDVVSYLLENPHQPASLQATDSQGNTVLHALVMISDNSAENIALVTSMYDGLLQAGARLCPTVQLEDIRNLQDLTPLKLAAKEGKIEIFRHILQREFSGLSHLSRKFTEWCYGPVRVSLYDLASVDSCEENSVLEIIAFHCKSPHRHRMVVLEPLNKLLQAKWDLLIPKFFLNFLCNLIYMFIFTAVAYHQPTLKKQAAPHLKAEVGNSMLLTGHILILLGGIYLLVGQLWYFWRRHVFIWISFIDSYFEILFLFQALLTVVSQVLCFLAIEWYLPLLVSALVLGWLNLLYYTRGFQHTGIYSVMIQKVILRDLLRFLLIYLVFLFGFAVALVSLSQEAWRPEAPTGPNATESVQPMEGQEDEGNGAQYRGILEASLELFKFTIGMGELAFQEQLHFRGMVLLLLLAYVLLTYILLLNMLIALMSETVNSVATDSWSIWKLQKAISVLEMENGYWWCRKKQRAGVMLTVGTKPDGSPDERWCFRVEEVNWASWEQTLPTLCEDPSGAGVPRTLENPVLASPPKEDEDGASEENYVPVQLLQSN TTBECWA TT Literature-reported TTBKQL3 ID TTBKQL3 TTBKQL3 TN Trypanosoma Dihydrolipoamide dehydrogenase (Trypano LPD) TTBKQL3 UP P90597 TTBKQL3 UC DLDH_TRYCR TTBKQL3 BC Sulfur donor oxidoreductase TTBKQL3 SN Lipoamide dehydrogenase; LipDH; LPD; Glycine cleavage system L protein; Dihydrolipoamide dehydrogenase TTBKQL3 GN Trypano LPD TTBKQL3 FC Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. TTBKQL3 PD 2QAE TTBKQL3 SQ MFRRCAVKLNPYDVVVIGGGPGGYVASIKAAQLGMKTACVEKRGALGGTCLNVGCIPSKALLHATHVYHDAHANFARYGLMGGEGVTMDSAKMQQQKERAVKGLTGGVEYLFKKNKVTYYKGEGSFETAHSIRVNGLDGKQEMFETKKTIIATGSEPTELPFLPFDEKVVLSSTGALALPRVPKTMVVIGGGVIGLELGSVWARLGAKVTVVEFAPRCAPTLDEDVTNALVGALAKNEKMKFMTSTKVVGGTNNGDSVSLEVEGKNGKRETVTCEALLVSVGRRPFTGGLGLDKINVAKNERGFVKIGDHFETSIPDVYAIGDVVDKGPMLAHKAEDEGVACAEILAGKPGHVNYGVIPAVIYTMPEVASVGKSEEELKKEGVAYKVGKFPFNANSRAKAVSTEDGFVKVLVDKATDRILGVHIVCTTAGELIGEACLAMEYGASSEDVGRTCHAHPTMSEALKEACMALVAKTINF TTBKQL3 TT Literature-reported TTG3TSY ID TTG3TSY TTG3TSY TN Trypanosoma Trypanothione synthetase (Trypano TRS) TTG3TSY UP Q9GT49 TTG3TSY UC TRYS_TRYCC TTG3TSY BC Carbon-nitrogen ligase TTG3TSY SN TRS; Cf-TS TTG3TSY GN Trypano TRS TTG3TSY FC Bifunctional enzyme which catalyzes the formation oftrypanothione (N(1),N(8)-bis(glutathionyl)spermidine) from glutathione and spermidine. Converts spermidine or glutathionylspermidine into trypanothione. Can also convert aminopropylcadaverine into glutothionylaminopropylcadaverine and homotrypanothione. Also has low amidase activity, hydrolyzing trypanothione, homotrypanothione or glutathionylspermidine to form glutathione and the corresponding polyamine. TTG3TSY EC EC 6.3.1.9 TTG3TSY SQ MPTLQSLAVPFGCVQGYAPGGIPAYSNKHESYFSGERSIDGNLFCGFKYQCVEFARRWLFERKSLVLPDVDWAVHIFNLKEVSDARTGKPVRCVAIRNGTAAKPVVDSLLIYPSDDYSPVGHVAAITEVGDKWVRIADQNHRFHKWDANYAAELPLIHEKGVWTILDPLEDEVLKPLGWVTFPDTPDRNPNEPLVLHESLHFKRGELPTLRRLTFTPTSREKDWLDLTNEAEAYFADVCGIDVKNPKLEKASYYQMNRELYLDCAKYGNQLHQMFLEATKFVLGSDELLRLFCIPEEYWPRLRHSWETQPHAITGRFDFAFDEDTQQFKCFEYNADSASTLLECGVIQQKWARSVGLDDGTTYSSGSLVSSRLQLAWEMAEVTGRVHFLIDNDDEEHYTALYVMQHASAAGLETKLCVLFDEFHFDENGVVVDSDGVAVTTVWKTWMWETAIADHQKARVQRGNDWRPTPKDEVRLCDILLGPNWDLRVFEPMWKIIPSNKAILPIIYNKHPDHPALLRASYELTVELQRTGYVRKPIVGRVGRNVTVTEASGDIAAKSDGDFSDRDMVYQELFRLPERDGYYAILGGWVIGDVYCGTGVREDKTIITGLESPFSALRVYQGAQRRPLTHEDLDKAEAAAVGGGLKT TTG3TSY TT Literature-reported TTX1MY7 ID TTX1MY7 TTX1MY7 TN Twist-related protein 1 (TWIST1) TTX1MY7 UP Q15672 TTX1MY7 UC TWST1_HUMAN TTX1MY7 SN bHLHa38; TWIST; H-twist; Class A basic helix-loop-helix protein 38 TTX1MY7 GN TWIST1 TTX1MY7 FC Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator: NPAS2-ARNTL/BMAL1 heterodimer. TTX1MY7 PD 2MJV TTX1MY7 SQ MMQDVSSSPVSPADDSLSNSEEEPDRQQPPSGKRGGRKRRSSRRSAGGGAGPGGAAGGGVGGGDEPGSPAQGKRGKKSAGCGGGGGAGGGGGSSSGGGSPQSYEELQTQRVMANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLYQVLQSDELDSKMASCSYVAHERLSYAFSVWRMEGAWSMSASH TTX1MY7 TT Literature-reported TTX1MY7 KE hsa05205:Proteoglycans in cancer TTIEMFN ID TTIEMFN TTIEMFN TN TYRO3 tyrosine kinase receptor (TYRO3) TTIEMFN UP Q06418 TTIEMFN UC TYRO3_HUMAN TTIEMFN SN Tyrosine-protein kinase receptor TYRO3; Tyrosine-protein kinase TIF; Tyrosine-protein kinase SKY; Tyrosine-protein kinase RSE; Tyrosine-protein kinase DTK; Tyrosine-protein kinase BYK; TIF; SKY; RSE; DTK; BYK TTIEMFN GN TYRO3 TTIEMFN FC Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. TTIEMFN EC EC 2.7.10.1 TTIEMFN PD 1RHF TTIEMFN SQ MALRRSMGRPGLPPLPLPPPPRLGLLLAALASLLLPESAAAGLKLMGAPVKLTVSQGQPVKLNCSVEGMEEPDIQWVKDGAVVQNLDQLYIPVSEQHWIGFLSLKSVERSDAGRYWCQVEDGGETEISQPVWLTVEGVPFFTVEPKDLAVPPNAPFQLSCEAVGPPEPVTIVWWRGTTKIGGPAPSPSVLNVTGVTQSTMFSCEAHNLKGLASSRTATVHLQALPAAPFNITVTKLSSSNASVAWMPGADGRALLQSCTVQVTQAPGGWEVLAVVVPVPPFTCLLRDLVPATNYSLRVRCANALGPSPYADWVPFQTKGLAPASAPQNLHAIRTDSGLILEWEEVIPEAPLEGPLGPYKLSWVQDNGTQDELTVEGTRANLTGWDPQKDLIVRVCVSNAVGCGPWSQPLVVSSHDRAGQQGPPHSRTSWVPVVLGVLTALVTAAALALILLRKRRKETRFGQAFDSVMARGEPAVHFRAARSFNRERPERIEATLDSLGISDELKEKLEDVLIPEQQFTLGRMLGKGEFGSVREAQLKQEDGSFVKVAVKMLKADIIASSDIEEFLREAACMKEFDHPHVAKLVGVSLRSRAKGRLPIPMVILPFMKHGDLHAFLLASRIGENPFNLPLQTLIRFMVDIACGMEYLSSRNFIHRDLAARNCMLAEDMTVCVADFGLSRKIYSGDYYRQGCASKLPVKWLALESLADNLYTVQSDVWAFGVTMWEIMTRGQTPYAGIENAEIYNYLIGGNRLKQPPECMEDVYDLMYQCWSADPKQRPSFTCLRMELENILGQLSVLSASQDPLYINIERAEEPTAGGSLELPGRDQPYSGAGDGSGMGAVGGTPSDCRYILTPGGLAEQPGQAEHQPESPLNETQRLLLLQQGLLPHSSC TTIEMFN TT Clinical trial TTPOGS1 ID TTPOGS1 TTPOGS1 TN Tyrosine-protein kinase Fgr (FGR) TTPOGS1 UP P09769 TTPOGS1 UC FGR_HUMAN TTPOGS1 BC Kinase TTPOGS1 SN p58c-Fgr; p58-Fgr; p55-Fgr; SRC2; Proto-oncogene c-Fgr; Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog TTPOGS1 GN FGR TTPOGS1 FC Promotes mast cell degranulation, release of inflammatory cytokines and IgE-mediated anaphylaxis. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as MS4A2/FCER1B, FCGR2A and/or FCGR2B. Acts downstream of ITGB1 and ITGB2, and regulates actin cytoskeleton reorganization, cell spreading and adhesion. Depending on the context, activates or inhibits cellular responses. Functions as negative regulator of ITGB2 signaling, phagocytosis and SYK activity in monocytes. Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages. Functions as positive regulator of cell migration and regulates cytoskeleton reorganization via RAC1 activation. Phosphorylates SYK (in vitro) and promotes SYK-dependent activation of AKT1 and MAP kinase signaling. Phosphorylates PLD2 in antigen-stimulated mast cells, leading to PLD2 activation and the production of the signaling molecules lysophosphatidic acid and diacylglycerol. Promotes activation of PIK3R1. Phosphorylates FASLG, and thereby regulates its ubiquitination and subsequent internalization. Phosphorylates ABL1. Promotes phosphorylation of CBL, CTTN, PIK3R1, PTK2/FAK1, PTK2B/PYK2 and VAV2. Phosphorylates HCLS1 that has already been phosphorylated by SYK, but not unphosphorylated HCLS1. Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors devoid of kinase activity and contributes to the regulation of immune responses, including neutrophil, monocyte, macrophage and mast cell functions, cytoskeleton remodeling in response to extracellular stimuli, phagocytosis, cell adhesion and migration. TTPOGS1 EC EC 2.7.10.2 TTPOGS1 SQ MGCVFCKKLEPVATAKEDAGLEGDFRSYGAADHYGPDPTKARPASSFAHIPNYSNFSSQAINPGFLDSGTIRGVSGIGVTLFIALYDYEARTEDDLTFTKGEKFHILNNTEGDWWEARSLSSGKTGCIPSNYVAPVDSIQAEEWYFGKIGRKDAERQLLSPGNPQGAFLIRESETTKGAYSLSIRDWDQTRGDHVKHYKIRKLDMGGYYITTRVQFNSVQELVQHYMEVNDGLCNLLIAPCTIMKPQTLGLAKDAWEISRSSITLERRLGTGCFGDVWLGTWNGSTKVAVKTLKPGTMSPKAFLEEAQVMKLLRHDKLVQLYAVVSEEPIYIVTEFMCHGSLLDFLKNPEGQDLRLPQLVDMAAQVAEGMAYMERMNYIHRDLRAANILVGERLACKIADFGLARLIKDDEYNPCQGSKFPIKWTAPEAALFGRFTIKSDVWSFGILLTELITKGRIPYPGMNKREVLEQVEQGYHMPCPPGCPASLYEAMEQTWRLDPEERPTFEYLQSFLEDYFTSAEPQYQPGDQT TTPOGS1 TT Literature-reported TTNHIXL ID TTNHIXL TTNHIXL TN Tyrosine-protein kinase ITK (ITK) TTNHIXL UP Q08881 TTNHIXL UC ITK_HUMAN TTNHIXL SN Tyrosine-protein kinase Lyk; Tyrosine-protein kinase ITK/TSK; LYK; Kinase EMT; Interleukin-2-inducible T-cell kinase; IL-2-inducible T-cell kinase TTNHIXL GN ITK TTNHIXL FC Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Phosphorylates TBX21 at 'Tyr-530' and mediates its interaction with GATA3 (By similarity). TTNHIXL EC EC 2.7.10.2 TTNHIXL PD 4RFM; 4QD6; 4PQN; 4PPC; 4PPB TTNHIXL SQ MNNFILLEEQLIKKSQQKRRTSPSNFKVRFFVLTKASLAYFEDRHGKKRTLKGSIELSRIKCVEIVKSDISIPCHYKYPFQVVHDNYLLYVFAPDRESRQRWVLALKEETRNNNSLVPKYHPNFWMDGKWRCCSQLEKLATGCAQYDPTKNASKKPLPPTPEDNRRPLWEPEETVVIALYDYQTNDPQELALRRNEEYCLLDSSEIHWWRVQDRNGHEGYVPSSYLVEKSPNNLETYEWYNKSISRDKAEKLLLDTGKEGAFMVRDSRTAGTYTVSVFTKAVVSENNPCIKHYHIKETNDNPKRYYVAEKYVFDSIPLLINYHQHNGGGLVTRLRYPVCFGRQKAPVTAGLRYGKWVIDPSELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLFAAETLLGMCLDVCEGMAYLEEACVIHRDLAARNCLVGENQVIKVSDFGMTRFVLDDQYTSSTGTKFPVKWASPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCWKERPEDRPAFSRLLRQLAEIAESGL TTNHIXL TT Literature-reported TTRMCYJ ID TTRMCYJ TTRMCYJ TN Tyrosine-protein kinase STYK1 (STYK1) TTRMCYJ UP Q6J9G0 TTRMCYJ UC STYK1_HUMAN TTRMCYJ BC Protein kinase superfamily. Tyr protein kinase family TTRMCYJ SN Serine/threonine/tyrosine kinase 1; Protein PK-unique; Novel oncogene with kinase domain; NOK TTRMCYJ GN STYK1 TTRMCYJ FC Probable tyrosine protein-kinase, which has strong transforming capabilities on a variety of cell lines. When overexpressed, it can also induce tumor cell invasion as well as metastasis in distant organs. May act by activating both MAP kinase and phosphatidylinositol 3'-kinases (PI3K) pathways. TTRMCYJ EC EC 2.7.10.2 TTRMCYJ SQ MGMTRMLLECSLSDKLCVIQEKQYEVIIVPTLLVTIFLILLGVILWLFIREQRTQQQRSGPQGIAPVPPPRDLSWEAGHGGNVALPLKETSVENFLGATTPALAKLQVPREQLSEVLEQICSGSCGPIFRANMNTGDPSKPKSVILKALKEPAGLHEVQDFLGRIQFHQYLGKHKNLVQLEGCCTEKLPLYMVLEDVAQGDLLSFLWTCRRDVMTMDGLLYDLTEKQVYHIGKQVLLALEFLQEKHLFHGDVAARNILMQSDLTAKLCGLGLAYEVYTRGAISSTQTIPLKWLAPERLLLRPASIRADVWSFGILLYEMVTLGAPPYPEVPPTSILEHLQRRKIMKRPSSCTHTMYSIMKSCWRWREADRPSPRELRLRLEAAIKTADDEAVLQVPELVVPELYAAVAGIRVESLFYNYSML TTRMCYJ TT Literature-reported TT8M1DP ID TT8M1DP TT8M1DP TN Tyrosine-protein kinase TXK (TXK) TT8M1DP UP P42681 TT8M1DP UC TXK_HUMAN TT8M1DP SN Resting lymphocyte kinase; RLK; Protein-tyrosine kinase 4; PTK4 TT8M1DP GN TXK TT8M1DP FC Non-receptor tyrosine kinase that plays a redundant role with ITK in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of TXK to the cell membrane, where it is phosphorylated at Tyr-420. Phosphorylation leads to TXK full activation. Contributes also to signaling from many receptors and participates in multiple downstream pathways, including regulation of the actin cytoskeleton. Like ITK, can phosphorylate PLCG1, leading to its localization in lipid rafts and activation, followed by subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. With PARP1 and EEF1A1, TXK forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFNG to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Phosphorylates both PARP1 and EEF1A1. Phosphorylates also key sites in LCP2 leading to the up-regulation of Th1 preferred cytokine IL-2. Phosphorylates 'Tyr-201' of CTLA4 which leads to the association of PI-3 kinase with the CTLA4 receptor. TT8M1DP EC EC 2.7.10.2 TT8M1DP PD 2DM0 TT8M1DP SQ MILSSYNTIQSVFCCCCCCSVQKRQMRTQISLSTDEELPEKYTQRRRPWLSQLSNKKQSNTGRVQPSKRKPLPPLPPSEVAEEKIQVKALYDFLPREPCNLALRRAEEYLILEKYNPHWWKARDRLGNEGLIPSNYVTENKITNLEIYEWYHRNITRNQAEHLLRQESKEGAFIVRDSRHLGSYTISVFMGARRSTEAAIKHYQIKKNDSGQWYVAERHAFQSIPELIWYHQHNAAGLMTRLRYPVGLMGSCLPATAGFSYEKWEIDPSELAFIKEIGSGQFGVVHLGEWRSHIQVAIKAINEGSMSEEDFIEEAKVMMKLSHSKLVQLYGVCIQRKPLYIVTEFMENGCLLNYLRENKGKLRKEMLLSVCQDICEGMEYLERNGYIHRDLAARNCLVSSTCIVKISDFGMTRYVLDDEYVSSFGAKFPIKWSPPEVFLFNKYSSKSDVWSFGVLMWEVFTEGKMPFENKSNLQVVEAISEGFRLYRPHLAPMSIYEVMYSCWHEKPEGRPTFAELLRAVTEIAETW TT8M1DP TT Literature-reported TTJLTNM ID TTJLTNM TTJLTNM TN Ubiquitin carboxyl-terminal hydrolase 44 (USP44) TTJLTNM UP Q9H0E7 TTJLTNM UC UBP44_HUMAN TTJLTNM BC Peptidase C19 family. USP44 subfamily TTJLTNM SN Ubiquitin-specific-processing protease 44; Ubiquitin thioesterase 44; Deubiquitinating enzyme 44 TTJLTNM GN USP44 TTJLTNM FC Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Acts as a negative regulator of histone H2B (H2BK120ub1) ubiquitination. TTJLTNM EC EC 3.4.19.12 TTJLTNM SQ MLAMDTCKHVGQLQLAQDHSSLNPQKWHCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDNTTGDLKLLRRTLSAIKSQNYHCTTRSGRFLRSMGTGDDSYFLHDGAQSLLQSEDQLYTALWHRRRILMGKIFRTWFEQSPIGRKKQEEPFQEKIVVKREVKKRRQELEYQVKAELESMPPRKSLRLQGLAQSTIIEIVSVQVPAQTPASPAKDKVLSTSENEISQKVSDSSVKRRPIVTPGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAMTASEKTRSCKHPPVTDTVVYQMNECQEKDTGFVCSRQSSLSSGLSGGASKGRKMELIQPKEPTSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKDIASQPCLVTEMLAKFTETEALEGKIYVCDQCNSKRRRFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQRVTENGHSKLLPPELLLGSQHPNEDADTSSNEILS TTJLTNM TT Literature-reported TT47RXJ ID TT47RXJ TT47RXJ TN Ubiquitin carboxyl-terminal hydrolase BAP1 (BAP1) TT47RXJ UP Q92560 TT47RXJ UC BAP1_HUMAN TT47RXJ BC Peptidase C12 family. BAP1 subfamily TT47RXJ SN KIAA0272; Cerebral protein 6; BRCA1-associated protein 1 TT47RXJ GN BAP1 TT47RXJ FC Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor. TT47RXJ EC EC 3.4.19.12 TT47RXJ SQ MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNNMFFAHQLIPNSCATHALLSVLLNCSSVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYEARLHVLKVNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKSASNKSPLVLEANRAPAASEGNHTDGAEEAAGSCAQAPSHSPPNKPKLVVKPPGSSLNGVHPNPTPIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRVPVRPPQQYSDDEDDYEDDEEDDVQNTNSALRYKGKGTGKPGALSGSADGQLSVLQPNTINVLAEKLKESQKDLSIPLSIKTSSGAGSPAVAVPTHSQPSPTPSNESTDTASEIGSAFNSPLRSPIRSANPTRPSSPVTSHISKVLFGEDDSLLRVDCIRYNRAVRDLGPVISTGLLHLAEDGVLSPLALTEGGKGSSPSIRPIQGSQGSSSPVEKEVVEATDSREKTGMVRPGEPLSGEKYSPKELLALLKCVEAEIANYEACLKEEVEKRKKFKIDDQRRTHNYDEFICTFISMLAQEGMLANLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ TT47RXJ TT Literature-reported TTXHWA7 ID TTXHWA7 TTXHWA7 TN Ubiquitin-activating enzyme E1 (UBAE1) TTXHWA7 UP P22314 TTXHWA7 UC UBA1_HUMAN TTXHWA7 SN Ubiquitin-like modifier-activating enzyme 1; UBE1; Protein A1S9; A1S9T TTXHWA7 GN UBA1 TTXHWA7 FC Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites. TTXHWA7 EC EC 6.2.1.45 TTXHWA7 PD 6DC6; 4P22 TTXHWA7 SQ MSSSPLSKKRRVSGPDPKPGSNCSPAQSVLSEVPSVPTNGMAKNGSEADIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDKCLQRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDPKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEVQGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR TTXHWA7 TT Patented-recorded TTYENHQ ID TTYENHQ TTYENHQ TN Unc-51 like kinase 3 (ULK3) TTYENHQ UP Q6PHR2 TTYENHQ UC ULK3_HUMAN TTYENHQ SN Unc-51-like kinase 3; Serine/threonine-protein kinase ULK3 TTYENHQ GN ULK3 TTYENHQ FC Serine/threonine protein kinase that acts as a regulator of Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative regulator of SHH signaling in the absence of SHH ligand: interacts with SUFU, thereby inactivating the protein kinase activity and preventing phosphorylation of GLI proteins (GLI1, GLI2 and/or GLI3). Positively regulates SHH signaling in the presence of SHH: dissociates from SUFU, autophosphorylates and mediates phosphorylation of GLI2, activating it and promoting its nuclear translocation. Phosphorylates in vitro GLI2, as well as GLI1 and GLI3, although less efficiently. Also acts as a regulator of autophagy: following cellular senescence, able to induce autophagy. TTYENHQ EC EC 2.7.11.1 TTYENHQ PD 6FDZ; 6FDY; 4WZX TTYENHQ SQ MAGPGWGPPRLDGFILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDSDNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSPLYMAPEMVCQRQYDARVDLWSMGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPLLSRDCRDLLQRLLERDPSRRISFQDFFAHPWVDLEHMPSGESLGRATALVVQAVKKDQEGDSAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKAIVSSSNQALLRQGTSARDLLREMARDKPRLLAALEVASAAMAKEEAAGGEQDALDLYQHSLGELLLLLAAEPPGRRRELLHTEVQNLMARAEYLKEQVKMRESRWEADTLDKEGLSESVRSSCTLQ TTYENHQ TT Literature-reported TT165DP ID TT165DP TT165DP TN UNR-interacting protein (STRAP) TT165DP UP Q9Y3F4 TT165DP UC STRAP_HUMAN TT165DP BC WD repeat STRAP family TT165DP SN WD-40 repeat protein PT-WD; UNRIP; MAWD; MAP activator with WD repeats TT165DP GN STRAP TT165DP FC The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein. TT165DP SQ MAMRQTPLTCSGHTRPVVDLAFSGITPYGYFLISACKDGKPMLRQGDTGDWIGTFLGHKGAVWGATLNKDATKAATAAADFTAKVWDAVSGDELMTLAHKHIVKTVDFTQDSNYLLTGGQDKLLRIYDLNKPEAEPKEISGHTSGIKKALWCSEDKQILSADDKTVRLWDHATMTEVKSLNFNMSVSSMEYIPEGEILVITYGRSIAFHSAVSLDPIKSFEAPATINSASLHPEKEFLVAGGEDFKLYKYDYNSGEELESYKGHFGPIHCVRFSPDGELYASGSEDGTLRLWQTVVGKTYGLWKCVLPEEDSGELAKPKIGFPETTEEELEEIASENSDCIFPSAPDVKA TT165DP TT Literature-reported TT165DP KE hsa03013:RNA transport TTWVJU1 ID TTWVJU1 TTWVJU1 TN Urea transporter 1 (SLC14A1) TTWVJU1 UP Q13336 TTWVJU1 UC UT1_HUMAN TTWVJU1 BC Urea transporter family TTWVJU1 SN Urea transporter, erythrocyte; UTE; UT1; Solute carrier family 14 member 1; RACH1; JK; HUT11 TTWVJU1 GN SLC14A1 TTWVJU1 FC Urea channel that facilitates transmembrane urea transport down a concentration gradient. A constriction of the transmembrane channel functions as selectivity filter through which urea is expected to pass in dehydrated form. The rate of urea conduction is increased by hypotonic stress. Plays an important role in the kidney medulla collecting ducts, where it allows rapid equilibration between the lumen of the collecting ducts and the interstitium, and thereby prevents water loss driven by the high concentration of urea in the urine. Facilitates urea transport across erythrocyte membranes. May also play a role in transmembrane water transport, possibly by indirect means. TTWVJU1 PD 6QD5 TTWVJU1 SQ MEDSPTMVRVDSPTMVRGENQVSPCQGRRCFPKALGYVTGDMKELANQLKDKPVVLQFIDWILRGISQVVFVNNPVSGILILVGLLVQNPWWALTGWLGTVVSTLMALLLSQDRSLIASGLYGYNATLVGVLMAVFSDKGDYFWWLLLPVCAMSMTCPIFSSALNSMLSKWDLPVFTLPFNMALSMYLSATGHYNPFFPAKLVIPITTAPNISWSDLSALELLKSIPVGVGQIYGCDNPWTGGIFLGAILLSSPLMCLHAAIGSLLGIAAGLSLSAPFEDIYFGLWGFNSSLACIAMGGMFMALTWQTHLLALGCALFTAYLGVGMANFMAEVGLPACTWPFCLATLLFLIMTTKNSNIYKMPLSKVTYPEENRIFYLQAKKRMVESPL TTWVJU1 TT Literature-reported TTUTZHV ID TTUTZHV TTUTZHV TN Vascular cell adhesion protein 1 (VCAM1) TTUTZHV UP P19320 TTUTZHV UC VCAM1_HUMAN TTUTZHV SN Vascular cell adhesion molecule 1; VCAM-1; V-CAM 1; INCAM-100; CD106 antigen; CD106 TTUTZHV GN VCAM1 TTUTZHV FC Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation. Important in cell-cell recognition. TTUTZHV PD 1VSC; 1VCA; 1IJ9 TTUTZHV SQ MPGKMVVILGASNILWIMFAASQAFKIETTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGIQVEIYSFPKDPEIHLSGPLEAGKPITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGKVLVCRAKLHIDEMDSVPTVRQAVKELQVYISPKNTVISVNPSTKLQEGGSVTMTCSSEGLPAPEIFWSKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIVQEKPFTVEISPGPRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGKVRSEGTNSTLTLSPVSFENEHSYLCTVTCGHKKLEKGIQVELYSFPRDPEIEMSGGLVNGSSVTVSCKVPSVYPLDRLEIELLKGETILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGKALVCQAKLHIDDMEFEPKQRQSTQTLYVNVAPRDTTVLVSPSSILEEGSSVNMTCLSQGFPAPKILWSRQLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVELIIQVTPKDIKLTAFPSESVKEGDTVIISCTCGNVPETWIILKKKAETGDTVLKSIDGAYTIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQGRENNKDYFSPELLVLYFASSLIIPAIGMIIYFARKANMKGSYSLVEAQKSKV TTUTZHV TT Literature-reported TTUTZHV FM Transmembrane protein TTEST6I ID TTEST6I TTEST6I TN Vascular endothelial cell growth inhibitor (TNFSF15) TTEST6I UP O95150 TTEST6I UC TNF15_HUMAN TTEST6I BC Cytokine: tumor necrosis factor TTEST6I SN Tumor necrosis factor ligand superfamily member 15, secreted form; Tumor necrosis factor ligand superfamily member 15; TNFSF15; TNF ligand-related molecule 1 TTEST6I GN TNFSF15 TTEST6I FC Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis. TTEST6I PD 3MI8; 3K51; 2RJL; 2RJK; 2RE9 TTEST6I SQ MAEDLGLSFGETASVEMLPEHGSCRPKARSSSARWALTCCLVLLPFLAGLTTYLLVSQLRAQGEACVQFQALKGQEFAPSHQQVYAPLRADGDKPRAHLTVVRQTPTQHFKNQFPALHWEHELGLAFTKNRMNYTNKFLLIPESGDYFIYSQVTFRGMTSECSEIRQAGRPNKPDSITVVITKVTDSYPEPTQLLMGTKSVCEVGSNWFQPIYLGAMFSLQEGDKLMVNVSDISLVDYTKEDKTFFGAFLL TTEST6I TT Literature-reported TTREV7X ID TTREV7X TTREV7X TN Virus Cysteine proteinase (Viru VCATH) TTREV7X UP O91466 TTREV7X UC CATV_GVCPM TTREV7X BC Peptidase TTREV7X SN Viral cathepsin; VCATH; V-cath; CP of Cydia pomonella granulosis virus TTREV7X GN Viru VCATH TTREV7X FC Cysteine protease that plays an essential role in host liquefactionto facilitate horizontal transmission of the virus. May participate in the degradation of foreign protein expressed by the baculovirus system. TTREV7X EC EC 3.4.22.50 TTREV7X SQ MTKLLNFVILASVLTVTAHALTYDLNNSDELFKNFAIKYNKTYVSDEERAIKLENFKNNLKMINEKNMASKYAVFDINEYSDLNKNALLRRTTGFRLGLKKNPSAFTMTECSVVVIKDEPQALLPETLDWRDKHGVTPVKNQMECGSCWAFSTIANIESLYNIKYDKALNLSEQHLVNCDNINNGCAGGLMHWALESILQEGGVVSAENEPYYGFDGVCKKSPFELSISGSRRYVLQNENKLRELLVVNGPISVAIDVSDLINYKAGIADICENNEGLNHAVLLVGYGVKNDVPYWILKNSWGAEWGEEGYFRVQRDKNSCGMMNEYASSAIL TTREV7X TT Literature-reported TTG2PX9 ID TTG2PX9 TTG2PX9 TN Virus Replicase polyprotein 1ab (Viru rep) TTG2PX9 UP P0C6X7 TTG2PX9 UC R1AB_CVHSA TTG2PX9 BC Viral RNA helicase TTG2PX9 SN rep of Human SARS coronavirus; pp1ab; ORF1ab polyprotein TTG2PX9 GN Viru rep TTG2PX9 FC O-methyltransferase: Methyltransferase that mediates mRNAcap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. TTG2PX9 PD 5NFY; 5N5O; 5N19; 5F22; 5E6J TTG2PX9 SQ MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTNHGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELGTDPIEDYEQNWNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAWFTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVASPQECNNMHLSTLMKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKGGRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFHLNEEVAIILASFSASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIPDLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAYVTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVEFLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQCIRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYCALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAVVKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGLPLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAANIHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQKPVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRARAGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGVSIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQMTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENTSITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFTKSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYCNGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVECTTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIISTDDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLIEYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEYCRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDTTSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAACAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDDAARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINRLCEEMLDNRATLQAIASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPLMQSADASTFLNRVCGVSAARLTPCGTGTSTDVVYRAFDIYNEKVAGFAKFLKTNCCRFQEKDEEGNLLDSYFVVKRHTMSNYQHEETIYNLVKDCPAVAVHDFFKFRVDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQSLLKTVQFCDAMRDAGIVGVLTLDNQDLNGNWYDFGDFVQVAPGCGVPIVDSYYSLLMPILTLTRALAAESHMDADLAKPLIKWDLLKYDFTEERLCLFDRYFKYWDQTYHPNCINCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVETPHLMGWDYPKCDRAMPNMLRIMASLVLARKHNTCCNLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDHEFVDEFYAYLRKHFSMMILSDDAVVCYNSNYAAQGLVASIKNFKAVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNVNRFNVAITRAKIGILCIMSDRDLYDKLQFTSLEIPRRNVATLQAENVTGLFKDCSKIITGLHPTQAPTHLSVDIKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFITREEAIRHVRAWIGFDVEGCHATRDAVGTNLPLQLGFSTGVNLVAVPTGYVDTENNTEFTRVNAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSDTLKGLSDRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDKRATCFSTSSDTYACWNHSVGFDYVYNPFMIDVQQWGFTGNLQSNHDQHCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWSVEYPIIGDELRVNSACRKVQHMVVKSALLADKFPVLHDIGNPKAIKCVPQAEVEWKFYDAQPCSDKAYKIEELFYSYATHHDKFTDGVCLFWNCNVDRYPANAIVCRFDTRVLSNLNLPGCDGGSLYVNKHAFHTPAFDKSAFTNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRHHANEYRQYLDAYNMMISAGFSLWIYKQFDTYNLWNTFTRLQSLENVAYNVVNKGHFDGHAGEAPVSIINNAVYTKVDGIDVEIFENKTTLPVNVAFELWAKRNIKPVPEIKILNNLGVDIAANTVIWDYKREAPAHVSTIGVCTMTDIAKKPTESACSSLTVLFDGRVEGQVDLFRNARNGVLITEGSVKGLTPSKGPAQASVNGVTLIGESVKTQFNYFKKVDGIIQQLPETYFTQSRDLEDFKPRSQMETDFLELAMDEFIQRYKLEGYAFEHIVYGDFSHGQLGGLHLMIGLAKRSQDSPLKLEDFIPMDSTVKNYFITDAQTGSSKCVCSVIDLLLDDFVEIIKSQDLSVISKVVKVTIDYAEISFMLWCKDGHVETFYPKLQASQAWQPGVAMPNLYKMQRMLLEKCDLQNYGENAVIPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGTAVLRQWLPTGTLLVDSDLNDFVSDADSTLIGDCATVHTANKWDLIISDMYDPRTKHVTKENDSKEGFFTYLCGFIKQKLALGGSIAVKITEHSWNADLYKLMGHFSWWTAFVTNVNASSSEAFLIGANYLGKPKEQIDGYTMHANYIFWRNTNPIQLSSYSLFDMSKFPLKLRGTAVMSLKENQINDMIYSLLEKGRLIIRENNRVVVSSDILVNN TTG2PX9 TT Literature-reported TTTLDZK ID TTTLDZK TTTLDZK TN Vitamin D3 up-regulated protein 1 (VDUP1) TTTLDZK UP Q9H3M7 TTTLDZK UC TXNIP_HUMAN TTTLDZK BC Arrestin protein TTTLDZK SN Vitamin D(3) up-regulating protein-1; Thioredoxin-interacting protein; Thioredoxin-binding protein 2 TTTLDZK GN TXNIP TTTLDZK FC Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1). May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. TTTLDZK PD 5DZD; 5DWS; 5DF6; 5CQ2; 4ROJ TTTLDZK SQ MVMFKKIKSFEVVFNDPEKVYGSGEKVAGRVIVEVCEVTRVKAVRILACGVAKVLWMQGSQQCKQTSEYLRYEDTLLLEDQPTGENEMVIMRPGNKYEYKFGFELPQGPLGTSFKGKYGCVDYWVKAFLDRPSQPTQETKKNFEVVDLVDVNTPDLMAPVSAKKEKKVSCMFIPDGRVSVSARIDRKGFCEGDEISIHADFENTCSRIVVPKAAIVARHTYLANGQTKVLTQKLSSVRGNHIISGTCASWRGKSLRVQKIRPSILGCNILRVEYSLLIYVSVPGSKKVILDLPLVIGSRSGLSSRTSSMASRTSSEMSWVDLNIPDTPEAPPCYMDVIPEDHRLESPTTPLLDDMDGSQDSPIFMYAPEFKFMPPPTYTEVDPCILNNNVQ TTTLDZK TT Literature-reported TT94HRF ID TT94HRF TT94HRF TN Voltage-gated calcium channel alpha Cav1.1 (CACNA1S) TT94HRF UP Q13698 TT94HRF UC CAC1S_HUMAN TT94HRF BC Voltage-gated ion channel TT94HRF SN Voltage-gated calcium channel subunit alpha Cav1.1; Voltage-dependent L-type calcium channel subunit alpha-1S; Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle; CACNL1A3; CACN1; CACH1 TT94HRF GN CACNA1S TT94HRF FC Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. TT94HRF PD 6B27; 2VAY TT94HRF SQ MEPSSPQDEGLRKKQPKKPVPEILPRPPRALFCLTLENPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNSLNLGLEKLEYFFLIVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFTIVFLGVFTVILEQVNVIQSHTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYFIGTDIVATVENEEPSPCARTGSGRRCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCITMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLDEDLRGYMSWITQGEVMDVEDFREGKLSLDEGGSDTESLYEIAGLNKIIQFIRHWRQWNRIFRWKCHDIVKSKVFYWLVILIVALNTLSIASEHHNQPLWLTRLQDIANRVLLSLFTTEMLMKMYGLGLRQYFMSIFNRFDCFVVCSGILEILLVESGAMTPLGISVLRCIRLLRIFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFIVIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWTSMMYNGIMAYGGPSYPGMLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEEKKRRKMSKGLPDKSEEEKSTMAKKLEQKPKGEGIPTTAKLKIDEFESNVNEVKDPYPSADFPGDDEEDEPEIPLSPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKIRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRADSMRNQILKHFDIGFTSVFTVEIVLKMTTYGAFLHKGSFCRNYFNMLDLLVVAVSLISMGLESSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCMFVAISTIGNIVLVTTLLQFMFACIGVQLFKGKFFRCTDLSKMTEEECRGYYYVYKDGDPMQIELRHREWVHSDFHFDNVLSAMMSLFTVSTFEGWPQLLYKAIDSNAEDVGPIYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYIVTSSYFEYLMFALIMLNTICLGMQHYNQSEQMNHISDILNVAFTIIFTLEMILKLMAFKARGYFGDPWNVFDFLIVIGSIIDVILSEIDTFLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLIKLLSRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIALVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKLCDPESDYAPGEEYTCGTNFAYYYFISFYMLCAFLVINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDIVQIQAGLRTIEEEAAPEICRTVSGDLAAEEELERAMVEAAMEEGIFRRTGGLFGQVDNFLERTNSLPPVMANQRPLQFAEIEMEEMESPVFLEDFPQDPRTNPLARANTNNANANVAYGNSNHSNSHVFSSVHYEREFPEETETPATRGRALGQPCRVLGPHSKPCVEMLKGLLTQRAMPRGQAPPAPCQCPRVESSMPEDRKSSTPGSLHEETPHSRSTRENTSRCSAPATALLIQKALVRGGLGTLAADANFIMATGQALADACQMEPEEVEIMATELLKGREAPEGMASSLGCLNLGSSLGSLDQHQGSQETLIPPRL TT94HRF TT Literature-reported TT9XKUC ID TT9XKUC TT9XKUC TN Voltage-gated potassium channel Kv10.1 (KCNH1) TT9XKUC UP O95259 TT9XKUC UC KCNH1_HUMAN TT9XKUC BC Voltage-gated ion channel TT9XKUC SN hEAG1; h-eag; Voltage-gated potassium channel subunit Kv10.1; Potassium voltage-gated channel subfamily H member 1; EAG1; EAG channel 1; EAG TT9XKUC GN KCNH1 TT9XKUC FC Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs). Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel. TT9XKUC PD 5J7E TT9XKUC SQ MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTIEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSAFMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSIGDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNVLTEHASANHSLVKASVVTVRESPATPVSFQAASTSGVPDHAKLQAPGSECLGPKGGGGDCAKRKSWARFKDACGKSEDWNKVSKAESMETLPERTKASGEATLKKTDSCDSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVRHELKEDIKALNAKMTNIEKQLSEILRILTSRRSSQSPQELFEISRPQSPESERDIFGAS TT9XKUC TT Literature-reported TT5OEKU ID TT5OEKU TT5OEKU TN Voltage-gated potassium channel Kv2.1 (KCNB1) TT5OEKU UP Q14721 TT5OEKU UC KCNB1_HUMAN TT5OEKU BC Voltage-gated ion channel TT5OEKU SN Voltage-gated potassium channel subunit Kv2.1; Rectifier potassium channel Kv2.1; Potassium voltage-gated channel subfamily B member 1; Potassium channel Kv2.1; H-DRK1; DRK1 TT5OEKU GN KCNB1 TT5OEKU FC Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain. Plays also a role in the regulation of exocytosis independently of its electrical function. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes. Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells. Channel properties are also modulated by cytoplasmic ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Major contributor to the slowly inactivating delayed-rectifier voltage-gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle cells. Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation. Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus. Contributes to the regulation of glucose-induced action potential amplitude and duration in pancreatic beta cells, hence limiting calcium influx and insulin secretion. Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells. May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval. Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury. May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions. Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits. Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose-induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner. Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. TT5OEKU SQ MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLEVCDDYSLDDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQSTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDDTKFKSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNMKDAFARSIEMMDIVVEKNGENMGKKDKVQDNHLSPNKWKWTKRTLSETSSSKSFETKEQGSPEKARSSSSPQHLNVQQLEDMYNKMAKTQSQPILNTKESAAQSKPKEELEMESIPSPVAPLPTRTEGVIDMRSMSSIDSFISCATDFPEATRFSHSPLTSLPSKTGGSTAPEVGWRGALGASGGRFVEANPSPDASQHSSFFIESPKSSMKTNNPLKLRALKVNFMEGDPSPLLPVLGMYHDPLRNRGSAAAAVAGLECATLLDKAVLSPESSIYTTASAKTPPRSPEKHTAIAFNFEAGVHQYIDADTDDEGQLLYSVDSSPPKSLPGSTSPKFSTGTRSEKNHFESSPLPTSPKFLRQNCIYSTEALTGKGPSGQEKCKLENHISPDVRVLPGGGAHGSTRDQSI TT5OEKU TT Literature-reported TT5OEKU FM Voltage-gated ion channel TT5OEKU RC R-HSA-1296072:Voltage gated Potassium channels; R-HSA-381676:Glucagon-like Peptide-1 (GLP1) regulates insulin secretion TTODZF1 ID TTODZF1 TTODZF1 TN Voltage-gated potassium channel Kv3.4 (KCNC4) TTODZF1 UP Q03721 TTODZF1 UC KCNC4_HUMAN TTODZF1 BC Voltage-gated ion channel TTODZF1 SN Voltage-gated potassium channel subunit Kv3.4; Potassium voltage-gated channel subfamily C member 4; KSHIIIC; C1orf30 TTODZF1 GN KCNC4 TTODZF1 FC This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. TTODZF1 PD 1ZTN; 1B4I; 1B4G TTODZF1 SQ MISSVCVSSYRGRKSGNKPPSKTCLKEEMAKGEASEKIIINVGGTRHETYRSTLRTLPGTRLAWLADPDGGGRPETDGGGVGSSGSSGGGGCEFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELTFWGIDETDVEPCCWMTYRQHRDAEEALDIFESPDGGGSGAGPSDEAGDDERELALQRLGPHEGGAGHGAGSGGCRGWQPRMWALFEDPYSSRAARVVAFASLFFILVSITTFCLETHEAFNIDRNVTEILRVGNITSVHFRREVETEPILTYIEGVCVLWFTLEFLVRIVCCPDTLDFVKNLLNIIDFVAILPFYLEVGLSGLSSKAARDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGARPSDPRGNDHTDFKNIPIGFWWAVVTMTTLGYGDMYPKTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKRKKHVPRPAQLESPMYCKSEETSPRDSTCSDTSPPAREEGMIERKRADSKQNGDANAVLSDEEGAGLTQPLASSPTPEERRALRRSTTRDRNKKAAACFLLSTGDYACADGSVRKGTFVLRDLPLQHSPEAACPPTAGTLFLPH TTODZF1 TT Literature-reported TTWVL5Q ID TTWVL5Q TTWVL5Q TN Voltage-gated potassium channel Kv7.5 (KCNQ5) TTWVL5Q UP Q9NR82 TTWVL5Q UC KCNQ5_HUMAN TTWVL5Q BC Voltage-gated ion channel TTWVL5Q SN Voltage-gated potassium channel subunit Kv7.5; Potassium voltage-gated channel subfamily KQT member 5; Potassium channel subunit alpha KvLQT5; KQT-like 5 TTWVL5Q GN KCNQ5 TTWVL5Q FC Therefore, it is important in the regulation of neuronal excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991. Activated by niflumic acid and the anticonvulsant retigabine. As the native M-channel, the potassium channel composed of KCNQ3 and KCNQ5 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1. Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. TTWVL5Q PD 6B8Q TTWVL5Q SQ MPRHHAGGEEGGAAGLWVKSGAAAAAAGGGRLGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAATLGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFIYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLSAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSVSIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSPSTDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGTDDVYDEKGCQCDVSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQILGKGQITSDKKSREKITAEHETTDDLSMLGRVVKVEKQVQSIESKLDCLLDIYQQVLRKGSASALALASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLSRSTSANISRGLQFILTPNEFSAQTFYALSPTMHSQATQVPISQSDGSAVAATNTIANQINTAPKPAAPTTLQIPPPLPAIKHLPRPETLHPNPAGLQESISDVTTCLVASKENVQVAQSNLTKDRSMRKSFDMGGETLLSVCPMVPKDLGKSLSVQNLIRSTEELNIQLSGSESSGSRGSQDFYPKWRESKLFITDEEVGPEETETDTFDAAPQPAREAAFASDSLRTGRSRSSQSICKAGESTDALSLPHVKLK TTWVL5Q TT Literature-reported TTLJTUF ID TTLJTUF TTLJTUF TN Voltage-gated sodium channel alpha Nav1.2 (SCN2A) TTLJTUF UP Q99250 TTLJTUF UC SCN2A_HUMAN TTLJTUF BC Voltage-gated ion channel TTLJTUF SN Voltage-gated sodium channelsubunit alpha Nav1.2; Sodium channel protein type II subunit alpha; Sodium channel protein brainII subunit alpha; SCN2A; HBSC II TTLJTUF GN SCN2A TTLJTUF FC Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. TTLJTUF PD 6J8E; 4RLY; 4JPZ; 2KAV TTLJTUF SQ MAQSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGKSLPFIYGDIPPEMVSVPLEDLDPYYINKKTFIVLNKGKAISRFSATPALYILTPFNPIRKLAIKILVHSLFNMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSSFEINITSFFNNSLDGNGTTFNRTVSIFNWDEYIEDKSHFYFLEGQNDALLCGNSSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAAAAAASAESRDFSGAGGIGVFSESSSVASKLSSKSEKELKNRRKKKKQKEQSGEEEKNDRVRKSESEDSIRRKGFRFSLEGSRLTYEKRFSSPHQSLLSIRGSLFSPRRNSRASLFSFRGRAKDIGSENDFADDEHSTFEDNDSRRDSLFVPHRHGERRHSNVSQASRASRVLPILPMNGKMHSAVDCNGVVSLVGGPSTLTSAGQLLPEGTTTETEIRKRRSSSYHVSMDLLEDPTSRQRAMSIASILTNTMEELEESRQKCPPCWYKFANMCLIWDCCKPWLKVKHLVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLSVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKISNDCELPRWHMHDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLTVFMMVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKRKIREFIQKAFVRKQKALDEIKPLEDLNNKKDSCISNHTTIEIGKDLNYLKDGNGTTSGIGSSVEKYVVDESDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESDMEESKEKLNATSSSEGSTVDIGAPAEGEQPEVEPEESLEPEACFTEDCVRKFKCCQISIEEGKGKLWWNLRKTCYKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQVYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINYTTGEMFDVSVVNNYSECKALIESNQTARWKNVKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEDNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTKQVFDISIMILICLNMVTMMVETDDQSQEMTNILYWINLVFIVLFTGECVLKLISLRYYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSGPPDCDPDKDHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFAKLSDFADALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEVSAIIIQRAYRRYLLKQKVKKVSSIYKKDKGKECDGTPIKEDTLIDKLNENSTPEKTDMTPSTTSPPSYDSVTKPEKEKFEKDKSEKEDKGKDIRESKK TTLJTUF TT Literature-reported TTI7FDX ID TTI7FDX TTI7FDX TN WNK lysine-deficient protein kinase 3 (WNK3) TTI7FDX UP Q9BYP7 TTI7FDX UC WNK3_HUMAN TTI7FDX SN Serine/threonine-protein kinase WNK3; Protein kinase with no lysine 3; Protein kinase lysine-deficient 3; KIAA1566 TTI7FDX GN WNK3 TTI7FDX FC Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Phosphorylates WNK4. Regulates the phosphorylation of SLC12A1 and SLC12A2. Increases Ca(2+) influx mediated by TRPV5 and TRPV6 by enhancing their membrane expression level via a kinase-dependent pathway. Inhibits the activity of KCNJ1 by decreasing its expression at the cell membrane in a non-catalytic manner. TTI7FDX EC EC 2.7.11.1 TTI7FDX PD 5O2C; 5O2B; 5O26; 5O23; 5O21 TTI7FDX SQ MATDSGDPASTEDSEKPDGISFENRVPQVAATLTVEARLKEKNSTFSASGETVERKRFFRKSVEMTEDDKVAESSPKDERIKAAMNIPRVDKLPSNVLRGGQEVKYEQCSKSTSEISKDCFKEKNEKEMEEEAEMKAVATSPSGRFLKFDIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESILKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLMRTSFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTDPEVKEIIEGCIRQNKSERLSIRDLLNHAFFAEDTGLRVELAEEDDCSNSSLALRLWVEDPKKLKGKHKDNEAIEFSFNLETDTPEEVAYEMVKSGFFHESDSKAVAKSIRDRVTPIKKTREKKPAGCLEERRDSQCKSMGNVFPQPQNTTLPLAPAQQTGAECEETEVDQHVRQQLLQRKPQQHCSSVTGDNLSEAGAASVIHSDTSSQPSVAYSSNQTMGSQMVSNIPQAEVNVPGQIYSSQQLVGHYQQVSGLQKHSKLTQPQILPLVQGQSTVLPVHVLGPTVVSQPQVSPLTVQKVPQIKPVSQPVGAEQQAALLKPDLVRSLNQDVATTKENVSSPDNPSGNGKQDRIKQRRASCPRPEKGTKFQLTVLQVSTSGDNMVECQLETHNNKMVTFKFDVDGDAPEDIADYMVEDNFVLESEKEKFVEELRAIVGQAQEILHVHFATERATGVDSITVDSNSSQTGSSEQVQINSTSTQTSNESAPQSSPVGRWRFCINQTIRNRETQSPPSLQHSMSAVPGRHPLPSPKNTSNKEISRDTLLTIENNPCHRALFTSKSEHKDVVDGKISECASVETKQPAILYQVEDNRQIMAPVTNSSSYSTTSVRAVPAECEGLTKQASIFIPVYPCHQTASQADALMSHPGESTQTSGNSLTTLAFDQKPQTLSVQQPAMDAEFISQEGETTVNTEASSPKTVIPTQTPGLEPTTLQPTTVLESDGERPPKLEFADNRIKTLDEKLRNLLYQEHSISSIYPESQKDTQSIDSPFSSSAEDTLSCPVTEVIAISHCGIKDSPVQSPNFQQTGSKLLSNVAASQPANISVFKRDLNVITSVPSELCLHEMSSDASLPGDPEAYPAAVSSGGAIHLQTGGGYFGLSFTCPSLKNPISKKSWTRKLKSWAYRLRQSTSFFKRSKVRQVETEEMRSAIAPDPIPLTRESTADTRALNRCKAMSGSFQRGRFQVITIPQQQSAKMTSFGIEHISVFSETNHSSEEAFIKTAKSQLVEIEPATQNPKTSFSYEKLQALQETCKENKGVPKQGDNFLSFSAACETDVSSVTPEKEFEETSATGSSMQSGSELLLKEREILTAGKQPSSDSEFSASLAGSGKSVAKTGPESNQCLPHHEEQAYAQTQSSLFYSPSSPMSSDDESEIEDEDLKVELQRLREKHIQEVVNLQTQQNKELQELYERLRSIKDSKTQSTEIPLPPASPRRPRSFKSKLRSRPQSLTHVDNGIVATGKSCLINELENPLCVESNAASCQQSPASKKGMFTDDLHKLVDDWTKEAVGNSLIKPSLNQLKQSQHKLETENWNKVSENTPSTMGYTSTWISSLSQIRGAVPTSLPQGLSLPSFPGPLSSYGMPHVCQYNAVAGAGYPVQWVGISGTTQQSVVIPAQSGGPFQPGMNMQAFPTSSVQNPATIPPGPK TTI7FDX TT Literature-reported TTQZULJ ID TTQZULJ TTQZULJ TN Zinc finger protein 762 (ZIK1) TTQZULJ UP Q3SY52 TTQZULJ UC ZIK1_HUMAN TTQZULJ BC Krueppel C2H2-type zinc-finger protein family TTQZULJ SN ZNF762 TTQZULJ GN ZIK1 TTQZULJ FC May be a transcriptional repressor. TTQZULJ SQ MAAAALRAPTQVTVSPETHMDLTKGCVTFEDIAIYFSQDEWGLLDEAQRLLYLEVMLENFALVASLGCGHGTEDEETPSDQNVSVGVSQSKAGSSTQKTQSCEMCVPVLKDILHLADLPGQKPYLVGECTNHHQHQKHHSAKKSLKRDMDRASYVKCCLFCMSLKPFRKWEVGKDLPAMLRLLRSLVFPGGKKPGTITECGEDIRSQKSHYKSGECGKASRHKHTPVYHPRVYTGKKLYECSKCGKAFRGKYSLVQHQRVHTGERPWECNECGKFFSQTSHLNDHRRIHTGERPYECSECGKLFRQNSSLVDHQKIHTGARPYECSQCGKSFSQKATLVKHQRVHTGERPYKCGECGNSFSQSAILNQHRRIHTGAKPYECGQCGKSFSQKATLIKHQRVHTGERPYKCGDCGKSFSQSSILIQHRRIHTGARPYECGQCGKSFSQKSGLIQHQVVHTGERPYECNKCGNSFSQCSSLIHHQKCHNT TTQZULJ TT Literature-reported TTQZULJ KE hsa05168:Herpes simplex virus 1 infection TTTO3QN ID TTTO3QN TTTO3QN TN Zinc finger protein RFP (TRIM27) TTTO3QN UP P14373 TTTO3QN UC TRI27_HUMAN TTTO3QN BC TRIM/RBCC family TTTO3QN SN Tripartite motif-containing protein 27; Ret finger protein; RNF76; RING-type E3 ubiquitin transferase TRIM27; RING finger protein 76 TTTO3QN GN TRIM27 TTTO3QN FC E3 ubiquitin-protein ligase that mediates ubiquitination of PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-cell activation. Acts as a regulator of retrograde transport: together with MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASHC1, leading to promote endosomal F-actin assembly (PubMed:23452853). Has a transcriptional repressor activity by cooperating with EPC1. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA. TTTO3QN EC EC 2.3.2.27 TTTO3QN SQ MASGSVAECLQQETTCPVCLQYFAEPMMLDCGHNICCACLARCWGTAETNVSCPQCRETFPQRHMRPNRHLANVTQLVKQLRTERPSGPGGEMGVCEKHREPLKLYCEEDQMPICVVCDRSREHRGHSVLPLEEAVEGFKEQIQNQLDHLKRVKDLKKRRRAQGEQARAELLSLTQMEREKIVWEFEQLYHSLKEHEYRLLARLEELDLAIYNSINGAITQFSCNISHLSSLIAQLEEKQQQPTRELLQDIGDTLSRAERIRIPEPWITPPDLQEKIHIFAQKCLFLTESLKQFTEKMQSDMEKIQELREAQLYSVDVTLDPDTAYPSLILSDNLRQVRYSYLQQDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVCRKGGVTSAPQNGFWAVSLWYGKEYWALTSPMTALPLRTPLQRVGIFLDYDAGEVSFYNVTERCHTFTFSHATFCGPVRPYFSLSYSGGKSAAPLIICPMSGIDGFSGHVGNHGHSMETSP TTTO3QN TT Literature-reported TTY3BRA ID TTY3BRA TTY3BRA TN ZNF217 messenger RNA (ZNF217 mRNA) TTY3BRA UP O75362 TTY3BRA UC ZN217_HUMAN TTY3BRA BC mRNA target TTY3BRA SN Zinc finger protein 217 (mRNA); ZABC1 (mRNA) TTY3BRA GN ZNF217 TTY3BRA FC Promotes cell proliferation and antagonizes cell death. Promotes phosphorylation of AKT1 at 'Ser-473'. Binds to the promoters of target genes and functions as repressor. TTY3BRA PD 4IS1; 4F2J; 3UK3; 2HU2 TTY3BRA SQ MQSKVTGNMPTQSLLMYMDGPEVIGSSLGSPMEMEDALSMKGTAVVPFRATQEKNVIQIEGYMPLDCMFCSQTFTHSEDLNKHVLMQHRPTLCEPAVLRVEAEYLSPLDKSQVRTEPPKEKNCKENEFSCEVCGQTFRVAFDVEIHMRTHKDSFTYGCNMCGRRFKEPWFLKNHMRTHNGKSGARSKLQQGLESSPATINEVVQVHAAESISSPYKICMVCGFLFPNKESLIEHRKVHTKKTAFGTSSAQTDSPQGGMPSSREDFLQLFNLRPKSHPETGKKPVRCIPQLDPFTTFQAWQLATKGKVAICQEVKESGQEGSTDNDDSSSEKELGETNKGSCAGLSQEKEKCKHSHGEAPSVDADPKLPSSKEKPTHCSECGKAFRTYHQLVLHSRVHKKDRRAGAESPTMSVDGRQPGTCSPDLAAPLDENGAVDRGEGGSEDGSEDGLPEGIHLDKNDDGGKIKHLTSSRECSYCGKFFRSNYYLNIHLRTHTGEKPYKCEFCEYAAAQKTSLRYHLERHHKEKQTDVAAEVKNDGKNQDTEDALLTADSAQTKNLKRFFDGAKDVTGSPPAKQLKEMPSVFQNVLGSAVLSPAHKDTQDFHKNAADDSADKVNKNPTPAYLDLLKKRSAVETQANNLICRTKADVTPPPDGSTTHNLEVSPKEKQTETAADCRYRPSVDCHEKPLNLSVGALHNCPAISLSKSLIPSITCPFCTFKTFYPEVLMMHQRLEHKYNPDVHKNCRNKSLLRSRRTGCPPALLGKDVPPLSSFCKPKPKSAFPAQSKSLPSAKGKQSPPGPGKAPLTSGIDSSTLAPSNLKSHRPQQNVGVQGAATRQQQSEMFPKTSVSPAPDKTKRPETKLKPLPVAPSQPTLGSSNINGSIDYPAKNDSPWAPPGRDYFCNRSASNTAAEFGEPLPKRLKSSVVALDVDQPGANYRRGYDLPKYHMVRGITSLLPQDCVYPSQALPPKPRFLSSSEVDSPNVLTVQKPYGGSGPLYTCVPAGSPASSSTLEGKRPVSYQHLSNSMAQKRNYENFIGNAHYRPNDKKT TTY3BRA TT Literature-reported TTY3BRA FM mRNA target TT9KJ1X ID TT9KJ1X TT9KJ1X TN 5-HT 5B receptor (HTR5B) TT9KJ1X UP Q9P2D3 TT9KJ1X UC HTR5B_HUMAN TT9KJ1X BC GPCR rhodopsin TT9KJ1X SN KIAA1414; HEATR5B; HEAT repeat-containing protein 5B TT9KJ1X GN HTR5B TT9KJ1X FC endocytic vesicle, membrane, endocytosis, protein localization, retrograde transport, endosome to Golgi. TT9KJ1X SQ MELAHSLLLNEEALAQITEAKRPVFIFEWLRFLDKVLVAANKTDVKEKQKKLVEQLTGLISSSPGPPTRKLLAKNLAALYSIGDTFTVFQTLDKCNDIIRNKDDTAAYLPTKLAAVACVGAFYEKMGRMLGSAFPETVNNLLKSLKSAESQGRSEILMSLQKVLSGLGGAAASSHRDIYKNARSLLTDRSMAVRCAVAKCLLELQNEAVFMWTAELENIATLCFKALENSNYGVRVAVSKLLGTVMATALMPKQATVMRQNVKRATFDEVLELMATGFLRGGSGFLKSGGEMLKVGGSVNREVRVGVTQAYVVFVTTLGGQWLERSFATFLSHVLDLVSHPRATQTHVEAVYSRRCVSFILRATVGSLLGEKAQIAAAKEICQAIGKQMKAVEAVVNDTSGENKSGAADIAASQHVMVCALQELGSLVQSLNATASPLIQEASIGLLEIVTSVLLHPSMAARLAAAWCLRCVAVALPFQLTPFLDRCAERLNNLKTSPEAVSGYSFAMAALLGGVHQCPLGIPHAKGKMVVSIAEDLLRTAAQNSRLSLQRTQAGWLLLGALMTLGPSVVRYHLPKMLLLWRNVFPRSLKELEAEKARGDSFTWQVTLEGRAGALCAMRSFVAHCPELLTEDVIRKLMTPIECAMTMMSHIPSVMKAHGAHLKASAAMVRLRLYDILALLPPKTYEGSFNALLRELVAEFTLTDNSANTTTSLLRSLCHYDDSVLLGSWLQETDHKSIEDQLQPNSASGSGALEHDPSSIYLRIPAGEAVPGPLPLGVSVIDASVALFGVVFPHVSYKHRLQMLDHFAECVKQAKGVRQQAVQLNIFTAVLSALKGLAENKSTLGPEEVRKSALTLVMGPLDNPNPILRCAAGEALGRMAQVVGEATFIARMAQYSFDKLKSARDVVSRTGHSLALGCLHRYVGGIGSGQHLKTSVSILLALAQDGTSPEVQTWSLHSLALIVDSSGPMYRGYVEPTLSLVLTLLLTVPPSHTEVHQCLGRCLGAIITTVGPELQGNGATTSTIRSSCLVGCAITQDHSDSLVQAAAISCLQQLHMFAPRHVNLSSLVPSLCVHLCSSHLLLRRAAVACLRQLAQREAAEVCEYAMSLAKNTGDKESSSANVSPFAPGVSSRTDIHCRHQGVNITETGLEGLLFGMLDRETDRKLCSDIHDTLGHMLSSLAVEKLSHWLMLCKDVLAASSDMSTATLLSSGKDEEAEKKDEMDDDTMFTTLGEEDKSKPFVAPRWATRVFAADCLCRIINLCENADQAHFDLALARSAKLRNPTNDLLVLHLSDLIRMAFMAATDHSNQLRMAGLQALEDIIKKFASVPEPEFPGHVILEQYQANVGAALRPAFSQDTPSDIIAKACQVCSTWIGSGVVSDLNDLRRVHNLLVSSLDKVQAGKGSSSQLYRESATTMEKLAVLKAWAEVYVVAMNIKKEAESKPKRAIKNTDDDDDDCGTIDELPPDSLITLVQPELPTLSRLWLAALKDYALLTLPAEFSSQLPPDGGAFYTPETIDTARLHYRNSWAPILHAVALWLNSTGFTCSESTEAAAISGLQKRSTSVNLNQASGAVGSAKSLPEINKDRMHLILGVSIQFLCSPRPEEPIEHVTACLQALHTLLDSPYARVHIAEDQLIGVELLSVLHRLLLTWNPSSVQLLVTGVVQQIVRAAQDYLQEKRNTLNEDDMEKEACTVLGEGGDSGGLIPGKSLVFATMELLMFILVRHMPHLSTKVSDSPSHIATKTRLSEESARLVAATVTILSDLPSLCSPAGCMTILPTILFLIARILKDTAIKSADNQVPPPVSAALQGIKSIVTLSMAKTEAGVQKQWTALIRSTLACILEYSQPEDSVPTPDEVSMLTAIALFLWSASNEIIGVQSLQNGCMNRFKNALNSCDPWVQAKCYQLLLSVFQHSNRALSTPYIHSLAPIVVEKLKAVERNRPASNIELLAVQEGIKVLETLVALGEEQNRVQLLALLVPTLISYLLDENSFASASSASKDLHEFALQNLMHIGPLYPHAFKTVMGAAPELKVRLETAVRASQASKAKAAARQPAPAIHSAPTIKLKTSFF TT9KJ1X TT Literature-reported TT4OLB0 ID TT4OLB0 TT4OLB0 TN A disintegrin and metalloproteinase (ADAM) TT4OLB0 UP Q99965; Q9H2U9 TT4OLB0 UC ADAM2_HUMAN; ADAM7_HUMAN TT4OLB0 BC Peptidase TT4OLB0 SN Disintegrin and metalloproteinase domain-containing protein; ADAM TT4OLB0 GN ADAM2; ADAM7 TT4OLB0 FC Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein. TT4OLB0 SQ MWRVLFLLSGLGGLRMDSNFDSLPVQITVPEKIRSIIKEGIESQASYKIVIEGKPYTVNLMQKNFLPHNFRVYSYSGTGIMKPLDQDFQNFCHYQGYIEGYPKSVVMVSTCTGLRGVLQFENVSYGIEPLESSVGFEHVIYQVKHKKADVSLYNEKDIESRDLSFKLQSVEPQQDFAKYIEMHVIVEKQLYNHMGSDTTVVAQKVFQLIGLTNAIFVSFNITIILSSLELWIDENKIATTGEANELLHTFLRWKTSYLVLRPHDVAFLLVYREKSNYVGATFQGKMCDANYAGGVVLHPRTISLESLAVILAQLLSLSMGITYDDINKCQCSGAVCIMNPEAIHFSGVKIFSNCSFEDFAHFISKQKSQCLHNQPRLDPFFKQQAVCGNAKLEAGEECDCGTEQDCALIGETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPENHYVQTGHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCEADNLQCGKLICKYVGKFLLQIPRATIIYANISGHLCIAVEFASDHADSQKMWIKDGTSCGSNKVCRNQRCVSSSYLGYDCTTDKCNDRGVCNNKKHCHCSASYLPPDCSVQSDLWPGGSIDSGNFPPVAIPARLPERRYIENIYHSKPMRWPFFLFIPFFIIFCVLIAIMVKVNFQRKKWRTEDYSSDEQPESESEPKG TT4OLB0 TT Literature-reported TTLJKZ0 ID TTLJKZ0 TTLJKZ0 TN Acetyl-CoA transporter (SLC33A1) TTLJKZ0 UP O00400 TTLJKZ0 UC ACATN_HUMAN TTLJKZ0 BC Major facilitator TTLJKZ0 SN Solute carrier family 33 member 1; Acetyl-coenzyme A transporter 1; Acetyl-CoA transporter 1; AT1 protein; AT-1; ACATN TTLJKZ0 GN SLC33A1 TTLJKZ0 FC Negatively regulates BMP signaling. Probable acetyl-CoA transporter necessary for O-acetylation of gangliosides. TTLJKZ0 SQ MSPTISHKDSSRQRRPGNFSHSLDMKSGPLPPGGWDDSHLDSAGREGDREALLGDTGTGDFLKAPQSFRAELSSILLLLFLYVLQGIPLGLAGSIPLILQSKNVSYTDQAFFSFVFWPFSLKLLWAPLVDAVYVKNFGRRKSWLVPTQYILGLFMIYLSTQVDRLLGNTDDRTPDVIALTVAFFLFEFLAATQDIAVDGWALTMLSRENVGYASTCNSVGQTAGYFLGNVLFLALESADFCNKYLRFQPQPRGIVTLSDFLFFWGTVFLITTTLVALLKKENEVSVVKEETQGITDTYKLLFAIIKMPAVLTFCLLILTAKIGFSAADAVTGLKLVEEGVPKEHLALLAVPMVPLQIILPLIISKYTAGPQPLNTFYKAMPYRLLLGLEYALLVWWTPKVEHQGGFPIYYYIVVLLSYALHQVTVYSMYVSIMAFNAKVSDPLIGGTYMTLLNTVSNLGGNWPSTVALWLVDPLTVKECVGASNQNCRTPDAVELCKKLGGSCVTALDGYYVESIICVFIGFGWWFFLGPKFKKLQDEGSSSWKCKRNN TTLJKZ0 TT Patented-recorded TTAHE2N ID TTAHE2N TTAHE2N TN Acrosin (ACR) TTAHE2N UP P10323 TTAHE2N UC ACRO_HUMAN TTAHE2N SN ACRS TTAHE2N GN ACR TTAHE2N FC Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome. TTAHE2N EC EC 3.4.21.10 TTAHE2N SQ MVEMLPTAILLVLAVSVVAKDNATCDGPCGLRFRQNPQGGVRIVGGKAAQHGAWPWMVSLQIFTYNSHRYHTCGGSLLNSRWVLTAAHCFVGKNNVHDWRLVFGAKEITYGNNKPVKAPLQERYVEKIIIHEKYNSATEGNDIALVEITPPISCGRFIGPGCLPHFKAGLPRGSQSCWVAGWGYIEEKAPRPSSILMEARVDLIDLDLCNSTQWYNGRVQPTNVCAGYPVGKIDTCQGDSGGPLMCKDSKESAYVVVGITSWGVGCARAKRPGIYTATWPYLNWIASKIGSNALRMIQSATPPPPTTRPPPIRPPFSHPISAHLPWYFQPPPRPLPPRPPAAQPRPPPSPPPPPPPPASPLPPPPPPPPPTPSSTTKLPQGLSFAKRLQQLIEVLKGKTYSDGKNHYDMETTELPELTSTS TTAHE2N TT Literature-reported TTKZ09F ID TTKZ09F TTKZ09F TN Adenosine monophosphate deaminase (AMPD) TTKZ09F UP P23109; Q01433; Q01432 TTKZ09F UC AMPD1_HUMAN; AMPD2_HUMAN; AMPD3_HUMAN TTKZ09F BC Carbon-nitrogen hydrolase TTKZ09F SN AMP deaminase TTKZ09F GN AMPD1; AMPD2; AMPD3 TTKZ09F FC AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle. TTKZ09F SQ MNVRIFYSVSQSPHSLLSLLFYCAILESRISATMPLFKLPAEEKQIDDAMRNFAEKVFASEVKDEGGRQEISPFDVDEICPISHHEMQAHIFHLETLSTSTEARRKKRFQGRKTVNLSIPLSETSSTKLSHIDEYISSSPTYQTVPDFQRVQITGDYASGVTVEDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESFYPVFTPPVKKGEDPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKHSGHMFSSKSPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLKSTE TTKZ09F TT Literature-reported TT5Z1WV ID TT5Z1WV TT5Z1WV TN Adhesion G protein-coupled receptor B1 (BAI1) TT5Z1WV UP O14514 TT5Z1WV UC AGRB1_HUMAN TT5Z1WV BC GPCR secretin TT5Z1WV SN Brain-specific angiogenesis inhibitor 1; ADGRB1 TT5Z1WV GN BAI1 TT5Z1WV FC Mediates the binding and engulfment of Gram-negative bacteria. Stimulates production of reactive oxygen species by macrophages in response to Gram-negative bacteria, resulting in enhanced microbicidal macrophage activity. In the gastric mucosa, required for recognition and engulfment of apoptotic gastric epithelial cells. Promotes myoblast fusion. Activates the Rho pathway in a G-protein-dependent manner. Inhibits MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity. Required for the formation of dendritic spines by ensuring the correct localization of PARD3 and TIAM1. Potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53/TP53 signal in suppression of glioblastoma. Phosphatidylserine receptor which enhances the engulfment of apoptotic cells. TT5Z1WV SQ MRGQAAAPGPVWILAPLLLLLLLLGRRARAAAGADAGPGPEPCATLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPVPCSGPGRVRTYQFDSFLESTRTYLGVESFDEVLRLCDPSAPLAFLQASKQFLQMRRQQPPQHDGLRPRAGPPGPTDDFSVEYLVVGNRNPSRAACQMLCRWLDACLAGSRSSHPCGIMQTPCACLGGEAGGPAAGPLAPRGDVCLRDAVAGGPENCLTSLTQDRGGHGATGGWKLWSLWGECTRDCGGGLQTRTRTCLPAPGVEGGGCEGVLEEGRQCNREACGPAGRTSSRSQSLRSTDARRREELGDELQQFGFPAPQTGDPAAEEWSPWSVCSSTCGEGWQTRTRFCVSSSYSTQCSGPLREQRLCNNSAVCPVHGAWDEWSPWSLCSSTCGRGFRDRTRTCRPPQFGGNPCEGPEKQTKFCNIALCPGRAVDGNWNEWSSWSACSASCSQGRQQRTRECNGPSYGGAECQGHWVETRDCFLQQCPVDGKWQAWASWGSCSVTCGAGSQRRERVCSGPFFGGAACQGPQDEYRQCGTQRCPEPHEICDEDNFGAVIWKETPAGEVAAVRCPRNATGLILRRCELDEEGIAYWEPPTYIRCVSIDYRNIQMMTREHLAKAQRGLPGEGVSEVIQTLVEISQDGTSYSGDLLSTIDVLRNMTEIFRRAYYSPTPGDVQNFVQILSNLLAEENRDKWEEAQLAGPNAKELFRLVEDFVDVIGFRMKDLRDAYQVTDNLVLSIHKLPASGATDISFPMKGWRATGDWAKVPEDRVTVSKSVFSTGLTEADEASVFVVGTVLYRNLGSFLALQRNTTVLNSKVISVTVKPPPRSLRTPLEIEFAHMYNGTTNQTCILWDETDVPSSSAPPQLGPWSWRGCRTVPLDALRTRCLCDRLSTFAILAQLSADANMEKATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAGASLWSSCVVLPLLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVDRQEEGNGDSGGSFQNGHAQLMTDFEKDVDLACRSVLNKDIAACRTATITGTLKRPSLPEEEKLKLAHAKGPPTNFNSLPANVSKLHLHGSPRYPGGPLPDFPNHSLTLKRDKAPKSSFVGDGDIFKKLDSELSRAQEKALDTSYVILPTATATLRPKPKEEPKYSIHIDQMPQTRLIHLSTAPEASLPARSPPSRQPPSGGPPEAPPAQPPPPPPPPPPPPQQPLPPPPNLEPAPPSLGDPGEPAAHPGPSTGPSTKNENVATLSVSSLERRKSRYAELDFEKIMHTRKRHQDMFQDLNRKLQHAAEKDKEVLGPDSKPEKQQTPNKRPWESLRKAHGTPTWVKKELEPLQPSPLELRSVEWERSGATIPLVGQDIIDLQTEV TT5Z1WV TT Literature-reported TTXWHGF ID TTXWHGF TTXWHGF TN AIMP multisynthetase complex protein 2 (AIMP2) TTXWHGF UP Q13155 TTXWHGF UC AIMP2_HUMAN TTXWHGF SN Protein JTV-1; PRO0992; Multisynthase complex auxiliary component p38; JTV1; Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 TTXWHGF GN AIMP2 TTXWHGF FC Required for assembly and stability of the aminoacyl-tRNA synthase complex. Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor. TTXWHGF PD 6ILD; 5Y6L; 5A5H; 5A34; 5A1N TTXWHGF SQ MPMYQVKPYHGGGAPLRVELPTCMYRLPNVHGRSYGPAPGAGHVQEESNLSLQALESRQDDILKRLYELKAAVDGLSKMIQTPDADLDVTNIIQADEPTTLTTNALDLNSVLGKDYGALKDIVINANPASPPLSLLVLHRLLCEHFRVLSTVHTHSSVKSVPENLLKCFGEQNKKQPRQDYQLGFTLIWKNVPKTQMKFSIQTMCPIEGEGNIARFLFSLFGQKHNAVNATLIDSWVDIAIFQLKEGSSKEKAAVFRSMNSALGKSPWLAGNELTVADVVLWSVLQQIGGCSVTVPANVQRWMRSCENLAPFNTALKLLK TTXWHGF TT Literature-reported TTF7WRM ID TTF7WRM TTF7WRM TN Alanine/serine/cysteine transporter 2 (SLC1A5) TTF7WRM UP Q15758 TTF7WRM UC AAAT_HUMAN TTF7WRM SN Solute carrier family 1 member 5; Sodium-dependent neutral amino acid transporter type 2; RDRC; RDR; RD114/simian type D retrovirus receptor; Neutral amino acid transporter B(0); M7V1; Baboon M7 virus receptor; ATB(0); ASCT2 TTF7WRM GN SLC1A5 TTF7WRM FC Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development. TTF7WRM PD 6GCT; 5MJU; 5LM4; 5LLU; 5LLM TTF7WRM SQ MVADPPRDSKGLAAAEPTANGGLALASIEDQGAAAGGYCGSRDQVRRCLRANLLVLLTVVAVVAGVALGLGVSGAGGALALGPERLSAFVFPGELLLRLLRMIILPLVVCSLIGGAASLDPGALGRLGAWALLFFLVTTLLASALGVGLALALQPGAASAAINASVGAAGSAENAPSKEVLDSFLDLARNIFPSNLVSAAFRSYSTTYEERNITGTRVKVPVGQEVEGMNILGLVVFAIVFGVALRKLGPEGELLIRFFNSFNEATMVLVSWIMWYAPVGIMFLVAGKIVEMEDVGLLFARLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLMMKCVEENNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLSQQSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAVNLPVDHISLILAVDWLVDRSCTVLNVEGDALGAGLLQNYVDRTESRSTEPELIQVKSELPLDPLPVPTEEGNPLLKHYRGPAGDATVASEKESVM TTF7WRM TT Literature-reported TT12MEP ID TT12MEP TT12MEP TN Allograft inflammatory factor-1 (AIF1) TT12MEP UP P55008 TT12MEP UC AIF1_HUMAN TT12MEP SN Protein G1; Ionized calciumbinding adapter molecule 1; Allograft inflammatory factor 1; AIF1 TT12MEP GN AIF1 TT12MEP FC Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T- lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation. TT12MEP PD 2G2B; 2D58 TT12MEP SQ MSQTRDLQGGKAFGLLKAQQEERLDEINKQFLDDPKYSSDEDLPSKLEGFKEKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKKLIGEVSSGSGETFSYPDFLRMMLGKRSAILKMILMYEEKAREKEKPTGPPAKKAISELP TT12MEP TT Literature-reported TTAU3SY ID TTAU3SY TTAU3SY TN Alpha-1-fetoprotein transcription factor (NR5A2) TTAU3SY UP O00482 TTAU3SY UC NR5A2_HUMAN TTAU3SY SN hB1F; Nuclear receptor subfamily 5 group A member 2; Liver receptor homolog 1; LRH-1; Hepatocytic transcription factor; FTF; CYP7A promoter-binding factor; CPF; B1F; B1-binding factor TTAU3SY GN NR5A2 TTAU3SY FC Nuclear receptor that acts as a key metabolic sensor by regulating the expression of genes involved in bile acid synthesis, cholesterol homeostasis and triglyceride synthesis. Together with the oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an essential transcriptional regulator of lipid metabolism. Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex. Binds to the sequence element 5'-AACGACCGACCTTGAG-3' of the enhancer II of hepatitis B virus genes, a critical cis-element of their expression and regulation. May be responsible for the liver-specific activity of enhancer II, probably in combination with other hepatocyte transcription factors. Key regulator of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. May also contribute to the regulation of pancreas-specific genes and play important roles in embryonic development. Activates the transcription of CYP2C38 (By similarity). TTAU3SY PD 5UNJ; 5SYZ; 5L11; 5L0M; 4RWV TTAU3SY SQ MSSNSDTGDLQESLKHGLTPIGAGLPDRHGSPIPARGRLVMLPKVETEALGLARSHGEQGQMPENMQVSQFKMVNYSYDEDLEELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKRYTCIENQNCQIDKTQRKRCPYCRFQKCLSVGMKLEAVRADRMRGGRNKFGPMYKRDRALKQQKKALIRANGLKLEAMSQVIQAMPSDLTISSAIQNIHSASKGLPLNHAALPPTDYDRSPFVTSPISMTMPPHGSLQGYQTYGHFPSRAIKSEYPDPYTSSPESIMGYSYMDSYQTSSPASIPHLILELLKCEPDEPQVQAKIMAYLQQEQANRSKHEKLSTFGLMCKMADQTLFSIVEWARSSIFFRELKVDDQMKLLQNCWSELLILDHIYRQVVHGKEGSIFLVTGQQVDYSIIASQAGATLNNLMSHAQELVAKLRSLQFDQREFVCLKFLVLFSLDVKNLENFQLVEGVQEQVNAALLDYTMCNYPQQTEKFGQLLLRLPEIRAISMQAEEYLYYKHLNGDVPYNNLLIEMLHAKRA TTAU3SY TT Literature-reported TT43L8U ID TT43L8U TT43L8U TN Alpha-2-HS-glycoprotein (AHSG) TT43L8U UP P02765 TT43L8U UC FETUA_HUMAN TT43L8U BC Fetuin family TT43L8U SN PRO2743; Ba-alpha-2-glycoprotein; Alpha2-HS glycoprotein TT43L8U GN AHSG TT43L8U FC Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions. TT43L8U SQ MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIEIDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRKVCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTDCVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCMVFQTQPVSSQPQPEGANEAVPTPVVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSHPRKTRTVVQPSVGAAAGPVVPPCPGRIRHFKV TT43L8U TT Literature-reported TT8CWJG ID TT8CWJG TT8CWJG TN Alpha-crystallin A chain (CRYAA) TT8CWJG UP P02489 TT8CWJG UC CRYAA_HUMAN TT8CWJG BC Heat shock protein TT8CWJG SN HspB4; Heat shock protein beta-4; CRYA1 TT8CWJG GN CRYAA TT8CWJG FC Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Contributes to the transparency and refractive index of the lens. TT8CWJG SQ MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS TT8CWJG TT Literature-reported TT8CWJG FM Heat shock protein TTQD0YT ID TTQD0YT TTQD0YT TN Alpha-endosulfine (ENSA) TTQD0YT UP O43768 TTQD0YT UC ENSA_HUMAN TTQD0YT BC Endosulfine family TTQD0YT SN ENSA; ARPP19e TTQD0YT GN ENSA TTQD0YT FC Endogenous ligand for sulfonylurea receptor. By inhibitingsulfonylurea from binding to the receptor, it reduces k(atp) channel currents and thereby stimulates insulin secretion. TTQD0YT SQ MSQKQEEENPAEETGEEKQDTQEKEGILPERAEEAKLKAKYPSLGQKPGGSDFLMKRLQKGQKYFDSGDYNMAKAKMKNKQLPSAGPDKNLVTGDHIPTPQDLPQRKSSLVTSKLAGGQVE TTQD0YT TT Literature-reported TTN5MZ3 ID TTN5MZ3 TTN5MZ3 TN Ammonium transporter Rh type C (RHCG) TTN5MZ3 UP Q9UBD6 TTN5MZ3 UC RHCG_HUMAN TTN5MZ3 SN Tumor-related protein DRC2; Rhesus blood group family type C glycoprotein; Rh type C glycoprotein; Rh glycoprotein kidney; Rh family type C glycoprotein; RHGK; PDRC2; CDRC2; C15orf6 TTN5MZ3 GN RHCG TTN5MZ3 FC Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion. TTN5MZ3 PD 3HD6 TTN5MZ3 SQ MAWNTNLRWRLPLTCLLLQVIMVILFGVFVRYDFEADAHWWSERTHKNLSDMENEFYYRYPSFQDVHVMVFVGFGFLMTFLQRYGFSAVGFNFLLAAFGIQWALLMQGWFHFLQDRYIVVGVENLINADFCVASVCVAFGAVLGKVSPIQLLIMTFFQVTLFAVNEFILLNLLKVKDAGGSMTIHTFGAYFGLTVTRILYRRNLEQSKERQNSVYQSDLFAMIGTLFLWMYWPSFNSAISYHGDSQHRAAINTYCSLAACVLTSVAISSALHKKGKLDMVHIQNATLAGGVAVGTAAEMMLMPYGALIIGFVCGIISTLGFVYLTPFLESRLHIQDTCGINNLHGIPGIIGGIVGAVTAASASLEVYGKEGLVHSFDFQGFNGDWTARTQGKFQIYGLLVTLAMALMGGIIVGLILRLPFWGQPSDENCFEDAVYWEMPEGNSTVYIPEDPTFKPSGPSVPSVPMVSPLPMASSVPLVP TTN5MZ3 TT Literature-reported TT76B3W ID TT76B3W TT76B3W TN Amphiregulin (AREG) TT76B3W UP P15514 TT76B3W UC AREG_HUMAN TT76B3W SN SDGF; Colorectum cellderived growth factor; Colorectum cell-derived growth factor; CRDGF; AREGB; AR TT76B3W GN AREG TT76B3W FC Autocrine growth factor as well as a mitogen for a broad range of target cells including astrocytes, Schwann cells and fibroblasts. Ligand of the EGF receptor/EGFR. TT76B3W PD 2RNL TT76B3W SQ MRAPLLPPAPVVLSLLILGSGHYAAGLDLNDTYSGKREPFSGDHSADGFEVTSRSEMSSGSEISPVSEMPSSSEPSSGADYDYSEEYDNEPQIPGYIVDDSVRVEQVVKPPQNKTESENTSDKPKRKKKGGKNGKNRRNRKKKNPCNAEFQNFCIHGECKYIEHLEAVTCKCQQEYFGERCGEKSMKTHSMIDSSLSKIALAAIAAFMSAVILTAVAVITVQLRRQYVRKYEGEAEERKKLRQENGNVHAIA TT76B3W TT Literature-reported TTLFY3S ID TTLFY3S TTLFY3S TN AN1-type zinc finger protein 5 (ZFAND5) TTLFY3S UP O76080 TTLFY3S UC ZFAN5_HUMAN TTLFY3S BC Zinc-finger TTLFY3S SN Zinc finger protein 216; Zinc finger A20 domain-containing protein 2; ZNF216; ZA20D2 TTLFY3S GN ZFAND5 TTLFY3S FC May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation. Involved in protein degradation via the ubiquitin-proteasome system. TTLFY3S SQ MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADTSLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSTSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI TTLFY3S TT Literature-reported TTLFY3S FM Zinc-finger TTKFPMH ID TTKFPMH TTKFPMH TN Ankyrin (ANK) TTKFPMH UP P16157 TTKFPMH UC ANK1_HUMAN TTKFPMH SN Erythrocyte ankyrin; Ankyrin-R; Ankyrin-1; ANK-1; ANK TTKFPMH GN ANK1 TTKFPMH FC Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. TTKFPMH PD 3UD2; 3UD1; 3KBU; 3KBT; 3F59 TTKFPMH SQ MPYSVGFREADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETKTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYDAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHVRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKVNAKAKDDQTPLHCAARIGHTNMVKLLLENNANPNLATTAGHTPLHIAAREGHVETVLALLEKEASQACMTKKGFTPLHVAAKYGKVRVAELLLERDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQVEVARSLLQYGGSANAESVQGVTPLHLAAQEGHAEMVALLLSKQANGNLGNKSGLTPLHLVAQEGHVPVADVLIKHGVMVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSDGTTPLAIAKRLGYISVTDVLKVVTDETSFVLVSDKHRMSFPETVDEILDVSEDEGEELISFKAERRDSRDVDEEKELLDFVPKLDQVVESPAIPRIPCAMPETVVIRSEEQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLSTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHRSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLKSKLVPLVQATFPENAVTKRVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLVYANECANFTTNVSARFWLSDCPRTAEAVNFATLLYKELTAVPYMAKFVIFAKMNDPREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMSLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAMPVKVRDSSREPGGSLSFLRKAMKYEDTQHILCHLNITMPPCAKGSGAEDRRRTPTPLALRYSILSESTPGSLSGTEQAEMKMAVISEHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSVALLNLWVIREGQNANMENLYTALQSIDRGEIVNMLEGSGRQSRNLKPDRRHTDRDYSLSPSQMNGYSSLQDELLSPASLGCALSSPLRADQYWNEVAVLDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSSLECSKAEDSDATGHEWKLEGALSEEPRGPELGSLELVEDDTVDSDATNGLIDLLEQEEGQRSEEKLPGSKRQDDATGAGQDSENEVSLVSGHQRGQARITHSPTVSQVTERSQDRLQDWDADGSIVSYLQDAAQGSWQEEVTQGPHSFQGTSTMTEGLEPGGSQEYEKVLVSVSEHTWTEQPEAESSQADRDRRQQGQEEQVQEAKNTFTQVVQGNEFQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQIDLSSADAAQEHEEVTVEGPLEDPSELEVDIDYFMKHSKDHTSTPNP TTKFPMH TT Literature-reported TT0NL6U ID TT0NL6U TT0NL6U TN Annexin A10 (ANXA10) TT0NL6U UP Q9UJ72 TT0NL6U UC ANX10_HUMAN TT0NL6U BC Annexin protein TT0NL6U SN Annexin-14; Annexin-10; ANX14 TT0NL6U GN ANXA10 TT0NL6U FC The expression of the tissue- and tumor-restricted ANXA10 is a marker of liver cell differentiation and growth arrest, and its down-regulation associated with malignant phenotype of hepatocytes, vascular invasion, and progression of HCC, leading to poor prognosis. TT0NL6U SQ MFCGDYVQGTIFPAPNFNPIMDAQMLGGALQGFDCDKDMLINILTQRCNAQRMMIAEAYQSMYGRDLIGDMREQLSDHFKDVMAGLMYPPPLYDAHELWHAMKGVGTDENCLIEILASRTNGEIFQMREAYCLQYSNNLQEDIYSETSGHFRDTLMNLVQGTREEGYTDPAMAAQDAMVLWEACQQKTGEHKTMLQMILCNKSYQQLRLVFQEFQNISGQDMVDAINECYDGYFQELLVAIVLCVRDKPAYFAYRLYSAIHDFGFHNKTVIRILIARSEIDLLTIRKRYKERYGKSLFHDIRNFASGHYKKALLAICAGDAEDY TT0NL6U TT Literature-reported TT9K86S ID TT9K86S TT9K86S TN Anterior gradient protein 2 (AG-2) TT9K86S UP O95994 TT9K86S UC AGR2_HUMAN TT9K86S SN hAG2; Secreted cement gland protein XAG2 homolog; AGR2; AG2 TT9K86S GN AGR2 TT9K86S FC Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells. Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. TT9K86S PD 2LNT; 2LNS TT9K86S SQ MEKIPVSAFLLLVALSYTLARDTTVKPGAKKDTKDSRPKLPQTLSRGWGDQLIWTQTYEEALYKSKTSNKPLMIIHHLDECPHSQALKKVFAENKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYAYEPADTALLLDNMKKALKLLKTEL TT9K86S TT Literature-reported TT7JZI8 ID TT7JZI8 TT7JZI8 TN Antigen peptide transporter 1 (TAP1) TT7JZI8 UP Q03518 TT7JZI8 UC TAP1_HUMAN TT7JZI8 SN Y3; Really interesting new gene 4 protein; RING4; Peptide transporter involved in antigen processing 1; Peptide transporter TAP1; Peptide transporter PSF1; Peptide supply factor 1; PSF1; PSF-1; ATP-binding cassette sub-family B member 2; ABCB2 TT7JZI8 GN TAP1 TT7JZI8 FC Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-10 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules. TT7JZI8 PD 5U1D; 1JJ7 TT7JZI8 SQ MAELLASAGSACSWDFPRAPPSFPPPAASRGGLGGTRSFRPHRGAESPRPGRDRDGVRVPMASSRCPAPRGCRCLPGASLAWLGTVLLLLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGSKSENAGAQGWLAALKPLAAALGLALPGLALFRELISWGAPGSADSTRLLHWGSHPTAFVVSYAAALPAAALWHKLGSLWVPGGQGGSGNPVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQAPADAPE TT7JZI8 TT Literature-reported TTZDCPK ID TTZDCPK TTZDCPK TN Anti-mullerian hormone II receptor (AMHR2) TTZDCPK UP Q16671 TTZDCPK UC AMHR2_HUMAN TTZDCPK SN MRII; MISRII; MISR2; MIS type II receptor; Anti-Muellerian hormone type-2 receptor; Anti-Muellerian hormone type II receptor; AMHR; AMH type II receptor TTZDCPK GN AMHR2 TTZDCPK FC On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone. TTZDCPK EC EC 2.7.11.30 TTZDCPK SQ MLGSLGLWALLPTAVEAPPNRRTCVFFEAPGVRGSTKTLGELLDTGTELPRAIRCLYSRCCFGIWNLTQDRAQVEMQGCRDSDEPGCESLHCDPSPRAHPSPGSTLFTCSCGTDFCNANYSHLPPPGSPGTPGSQGPQAAPGESIWMALVLLGLFLLLLLLLGSIILALLQRKNYRVRGEPVPEPRPDSGRDWSVELQELPELCFSQVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTPTQPQGPAAIMEAGTQRYMAPELLDKTLDLQDWGMALRRADIYSLALLLWEILSRCPDLRPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRCFATDPDGLRELLEDCWDADPEARLTAECVQQRLAALAHPQESHPFPESCPRGCPPLCPEDCTSIPAPTILPCRPQRSACHFSVQQGPCSRNPQPACTLSPV TTZDCPK TT Literature-reported TTF2V7I ID TTF2V7I TTF2V7I TN Apolipoprotein E receptor (LRP1) TTF2V7I UP Q07954 TTF2V7I UC LRP1_HUMAN TTF2V7I SN Prolow-density lipoprotein receptor-related protein 1; LRP-1; CD91; APR; APOER TTF2V7I GN LRP1 TTF2V7I FC Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission. Acts as an alpha-2-macroglobulin receptor. TTF2V7I PD 2KNY; 2KNX; 2FYL; 2FYJ; 1J8E TTF2V7I SQ MLTPPLLLLLPLLSALVAAAIDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCQPNEHNCLGTELCVPMSRLCNGVQDCMDGSDEGPHCRELQGNCSRLGCQHHCVPTLDGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFICGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANAQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVGGAPPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDADGVTCLANPSYVPPPQCQPGEFACANSRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHTDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKSCEGVTHVCDPSVKFGCKDSARCISKAWVCDGDNDCEDNSDEENCESLACRPPSHPCANNTSVCLPPDKLCDGNDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGPDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTVHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGQGPCSHLCLINYNRTVSCACPHLMKLHKDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMANMDGSNRTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSGLEVIDAMRSQLGKATALAIMGDKLWWADQVSEKMGTCSKADGSGSVVLRNSTTLVMHMKVYDESIQLDHKGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGQYPRIERSRLDGTERVVLVNVSISWPNGISVDYQDGKLYWCDARTDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGSKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGRGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSRRITIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNEQHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKHVGSNMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQDDLTCRAVNSSCRAQDEFECANGECINFSLTCDGVPHCKDKSDEKPSYCNSRRCKKTFRQCSNGRCVSNMLWCNGADDCGDGSDEIPCNKTACGVGEFRCRDGTCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCEHGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCADGADESIAAGCLYNSTCDDREFMCQNRQCIPKHFVCDHDRDCADGSDESPECEYPTCGPSEFRCANGRCLSSRQWECDGENDCHDQSDEAPKNPHCTSQEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDSSDERGCHINECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADVDECSTTFPCSQRCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSSRSVIVDTKITWPNGLTLDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGTNKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGSDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFVCPPNRPFRCKNDRVCLWIGRQCDGTDNCGDGTDEEDCEPPTAHTTHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASICGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQAFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLVNLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCNLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEHCRNGGTCAASPSGMPTCRCPTGFTGPKCTQQVCAGYCANNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGYCENFGTCQMAADGSRQCRCTAYFEGSRCEVNKCSRCLEGACVVNKQSGDVTCNCTDGRVAPSCLTCVGHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEHVFSQQQPGHIASILIPLLLLLLLVLVAGVVFWYKRRVQGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA TTF2V7I TT Literature-reported TT64GC2 ID TT64GC2 TT64GC2 TN Apoptosis signal-regulating kinase 2 (MAP3K6) TT64GC2 UP O95382 TT64GC2 UC M3K6_HUMAN TT64GC2 SN MAP3K6 TT64GC2 GN MAP3K6 TT64GC2 FC Component of a protein kinase signal transduction cascade. Activates the JNK, but not ERK or p38 kinase pathways. TT64GC2 EC EC 2.7.11.25 TT64GC2 SQ MAGPCPRSGAERAGSCWQDPLAVALSRGRQLAAPPGRGCARSRPLSVVYVLTREPQPGLEPREGTEAEPLPLRCLREACAQVPRPRPPPQLRSLPFGTLELGDTAALDAFYNADVVVLEVSSSLVQPSLFYHLGVRESFSMTNNVLLCSQADLPDLQALREDVFQKNSDCVGSYTLIPYVVTATGRVLCGDAGLLRGLADGLVQAGVGTEALLTPLVGRLARLLEATPTDSCGYFRETIRRDIRQARERFSGPQLRQELARLQRRLDSVELLSPDIIMNLLLSYRDVQDYSAIIELVETLQALPTCDVAEQHNVCFHYTFALNRRNRPGDRAKALSVLLPLVQLEGSVAPDLYCMCGRIYKDMFFSSGFQDAGHREQAYHWYRKAFDVEPSLHSGINAAVLLIAAGQHFEDSKELRLIGMKLGCLLARKGCVEKMQYYWDVGFYLGAQILANDPTQVVLAAEQLYKLNAPIWYLVSVMETFLLYQHFRPTPEPPGGPPRRAHFWLHFLLQSCQPFKTACAQGDQCLVLVLEMNKVLLPAKLEVRGTDPVSTVTLSLLEPETQDIPSSWTFPVASICGVSASKRDERCCFLYALPPAQDVQLCFPSVGHCQWFCGLIQAWVTNPDSTAPAEEAEGAGEMLEFDYEYTETGERLVLGKGTYGVVYAGRDRHTRVRIAIKEIPERDSRFSQPLHEEIALHRRLRHKNIVRYLGSASQGGYLKIFMEEVPGGSLSSLLRSVWGPLKDNESTISFYTRQILQGLGYLHDNHIVHRDIKGDNVLINTFSGLLKISDFGTSKRLAGITPCTETFTGTLQYMAPEIIDQGPRGYGKAADIWSLGCTVIEMATGRPPFHELGSPQAAMFQVGMYKVHPPMPSSLSAEAQAFLLRTFEPDPRLRASAQTLLGDPFLQPGKRSRSPSSPRHAPRPSDAPSASPTPSANSTTQSQTFPCPQAPSQHPPSPPKRCLSYGGTSQLRVPEEPAAEEPASPEESSGLSLLHQESKRRAMLAAVLEQELPALAENLHQEQKQEQGARLGRNHVEELLRCLGAHIHTPNRRQLAQELRALQGRLRAQGLGPALLHRPLFAFPDAVKQILRKRQIRPHWMFVLDSLLSRAVRAALGVLGPEVEKEAVSPRSEELSNEGDSQQSPGQQSPLPVEPEQGPAPLMVQLSLLRAETDRLREILAGKEREYQALVQRALQRLNEEARTYVLAPEPPTALSTDQGLVQWLQELNVDSGTIQMLLNHSFTLHTLLTYATRDDLIYTRIRGGMVCRIWRAILAQRAGSTPVTSGP TT64GC2 TT Literature-reported TTQEI32 ID TTQEI32 TTQEI32 TN Aquaporin-9 (AQP9) TTQEI32 UP O43315 TTQEI32 UC AQP9_HUMAN TTQEI32 BC Major intrinsic protein TTQEI32 SN Small solute channel 1; SSC1; Aquaglyceroporin-9; AQP-9 TTQEI32 GN AQP9 TTQEI32 FC Forms a water channel with a broad specificity. Also permeable glycerol and urea. Mediates passage of a wide variety of small, non-charged solutes including carbamides, polyols, purines, and pyrimidines. TTQEI32 SQ MQPEGAEKGKSFKQRLVLKSSLAKETLSEFLGTFILIVLGCGCVAQAILSRGRFGGVITINVGFSMAVAMAIYVAGGVSGGHINPAVSLAMCLFGRMKWFKLPFYVGAQFLGAFVGAATVFGIYYDGLMSFAGGKLLIVGENATAHIFATYPAPYLSLANAFADQVVATMILLIIVFAIFDSRNLGAPRGLEPIAIGLLIIVIASSLGLNSGCAMNPARDLSPRLFTALAGWGFEVFRAGNNFWWIPVVGPLVGAVIGGLIYVLVIEIHHPEPDSVFKTEQSEDKPEKYELSVIM TTQEI32 TT Literature-reported TTJ8EWH ID TTJ8EWH TTJ8EWH TN Arginine vasopressin (AVP) TTJ8EWH UP P01185 TTJ8EWH UC NEU2_HUMAN TTJ8EWH SN Vasopressin-neurophysin 2-copeptin; VP; Copeptin; AVP-NPII; ARVP TTJ8EWH GN AVP TTJ8EWH FC Neurophysin 2 specifically binds vasopressin. TTJ8EWH SQ MPDTMLPACFLGLLAFSSACYFQNCPRGGKRAMSDLELRQCLPCGPGGKGRCFGPSICCADELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAAFGVCCNDESCVTEPECREGFHRRARASDRSNATQLDGPAGALLLRLVQLAGAPEPFEPAQPDAY TTJ8EWH TT Literature-reported TTJ8EWH KE hsa04962:Vasopressin-regulated water reabsorption TTJ8EWH RC R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression; R-HSA-388479:Vasopressin-like receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-418555:G alpha (s) signalling events; R-HSA-432040:Vasopressin regulates renal water homeostasis via Aquaporins TTD74YX ID TTD74YX TTD74YX TN Arginyl aminopeptidase (RNPEP) TTD74YX UP Q9H4A4 TTD74YX UC AMPB_HUMAN TTD74YX SN Arginine aminopeptidase; Aminopeptidase B; APB; AP-B TTD74YX GN RNPEP TTD74YX FC Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). TTD74YX EC EC 3.4.11.6 TTD74YX SQ MASGEHSPGSGAARRPLHSAQAVDVASASNFRAFELLHLHLDLRAEFGPPGPGAGSRGLSGTAVLDLRCLEPEGAAELRLDSHPCLEVTAAALRRERPGSEEPPAEPVSFYTQPFSHYGQALCVSFPQPCRAAERLQVLLTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKYKYSALIEVPDGFTAVMSASTWEKRGPNKFFFQMCQPIPSYLIALAIGDLVSAEVGPRSRVWAEPCLIDAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGFTMYAQRRISTILFGAAYTCLEAATGRALLRQHMDITGEENPLNKLRVKIEPGVDPDDTYNETPYEKGFCFVSYLAHLVGDQDQFDSFLKAYVHEFKFRSILADDFLDFYLEYFPELKKKRVDIIPGFEFDRWLNTPGWPPYLPDLSPGDSLMKPAEELAQLWAAEELDMKAIEAVAISPWKTYQLVYFLDKILQKSPLPPGNVKKLGDTYPSISNARNAELRLRWGQIVLKNDHQEDFWKVKEFLHNQGKQKYTLPLYHAMMGGSEVAQTLAKETFASTASQLHSNVVNYVQQIVAPKGS TTD74YX TT Literature-reported TTADIOY ID TTADIOY TTADIOY TN AS1 14-3-3 protein eta (YWHAH) TTADIOY UP Q04917 TTADIOY UC 1433F_HUMAN TTADIOY SN YWHA1; Protein AS1; 14-3-3 protein eta TTADIOY GN YWHAH TTADIOY FC Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1. Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. TTADIOY PD 2C74; 2C63 TTADIOY SQ MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN TTADIOY TT Literature-reported TTWTD7F ID TTWTD7F TTWTD7F TN ASF/SF2-associated protein p32 (C1QBP) TTWTD7F UP Q07021 TTWTD7F UC C1QBP_HUMAN TTWTD7F SN p33; gC1q-R protein; SF2P32; SF2AP32; Mitochondrial matrix protein p32; Hyaluronan-binding protein 1; HABP1; Glycoprotein gC1qBP; GC1QBP; Complement component 1 Q subcomponent-binding protein, mitochondrial; C1qBP TTWTD7F GN C1QBP TTWTD7F FC Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular "heads" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase. May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppression of interleukin-12 production in monocyte-derived dendritic cells. Involved in regulation of antiviral response by inhibiting DDX58- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection. TTWTD7F PD 3RPX; 1P32 TTWTD7F SQ MLPLLRCVPRVLGSSVAGLRAAAPASPFRQLLQPAPRLCTRPFGLLSVRAGSERRPGLLRPRGPCACGCGCGSLHTDGDKAFVDFLSDEIKEERKIQKHKTLPKMSGGWELELNGTEAKLVRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKVEEQEPELTSTPNFVVEVIKNDDGKKALVLDCHYPEDEVGQEDEAESDIFSIREVSFQSTGESEWKDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ TTWTD7F TT Literature-reported TTMWDGU ID TTMWDGU TTMWDGU TN ATP-binding cassette transporter G1 (ABCG1) TTMWDGU UP P45844 TTMWDGU UC ABCG1_HUMAN TTMWDGU BC ABC transporter TTMWDGU SN White protein homolog; WHT1; ATP-binding cassette transporter 8; ATP-binding cassette sub-family G member 1; ABC8 TTMWDGU GN ABCG1 TTMWDGU FC Catalyzes the efflux of phospholipids such as sphingomyelin, cholesterol and its oxygenated derivatives like 7beta-hydroxycholesterol and this transport is coupled to hydrlysis of ATP. The lipid efflux is ALB-dependent. Is an active component of the macrophage lipid export complex. Could also be involved in intracellular lipid transport processes. The role in cellular lipid homeostasis may not be limited to macrophages. Prevents cell death by transporting cytotoxic 7beta-hydroxycholesterol. TTMWDGU SQ MACLMAAFSVGTAMNASSYSAEMTEPKSVCVSVDEVVSSNMEATETDLLNGHLKKVDNNLTEAQRFSSLPRRAAVNIEFRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSRLVRAVREGMCDSDHKRDLGGDAEVNPFLWHRPSEEVKQTKRLKGLRKDSSSMEGCHSFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMGVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGLDREDLHCDIDETCHFQKSEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER TTMWDGU TT Literature-reported TTG6KCU ID TTG6KCU TTG6KCU TN Autophagy-related 2B (ATG2B) TTG6KCU UP Q96BY7 TTG6KCU UC ATG2B_HUMAN TTG6KCU BC Autophagy phagophore-formation transporter TTG6KCU SN C14orf103; Autophagyrelated protein 2 homolog B; Autophagy-related protein 2 homolog B TTG6KCU GN ATG2B TTG6KCU FC Required for both autophagosome formation and regulation of lipid droplet morphology and dispersion. TTG6KCU SQ MPWPFSESIKKRACRYLLQRYLGHFLQEKLSLEQLSLDLYQGTGSLAQVPLDKWCLNEILESADAPLEVTEGFIQSISLSVPWGSLLQDNCALEVRGLEMVFRPRPRPATGSEPMYWSSFMTSSMQLAKECLSQKLTDEQGEGSQPFEGLEKFAETIETVLRRVKVTFIDTVLRIEHVPENSKTGTALEIRIERTVYCDETADESSGINVHQPTAFAHKLLQLSGVSLFWDEFSASAKSSPVCSTAPVETEPKLSPSWNPKIIYEPHPQLTRNLPEIAPSDPVQIGRLIGRLELSLTLKQNEVLPGAKLDVDGQIDSIHLLLSPRQVHLLLDMLAAIAGPENSSKIGLANKDRKNRPMQQEDEYRIQMELNRYYLRKDSLSVGVSSEQSFYETETARTPSSREEEVFFSMADMDMSHSLSSLPPLGDPPNMDLELSLTSTYTNTPAGSPLSATVLQPTWGEFLDHHKEQPVRGSTFPSNLVHPTPLQKTSLPSRSVSVDESRPELIFRLAVGTFSISVLHIDPLSPPETSQNLNPLTPMAVAFFTCIEKIDPARFSTEDFKSFRAVFAEACSHDHLRFIGTGIKVSYEQRQRSASRYFSTDMSIGQMEFLECLFPTDFHSVPPHYTELLTFHSKEETGSHSPVCLQLHYKHSENRGPQGNQARLSSVPHKAELQIKLNPVCCELDISIVDRLNSLLQPQKLATVEMMASHMYTSYNKHISLHKAFTEVFLDDSHSPANCRISVQVATPALNLSVRFPIPDLRSDQERGPWFKKSLQKEILYLAFTDLEFKTEFIGGSTPEQIKLELTFRELIGSFQEEKGDPSIKFFHVSSGVDGDTTSSDDFDWPRIVLKINPPAMHSILERIAAEEEEENDGHYQEEEEGGAHSLKDVCDLRRPAPSPFSSRRVMFENEQMVMPGDPVEMTEFQDKAISNSHYVLELTLPNIYVTLPNKSFYEKLYNRIFNDLLLWEPTAPSPVETFENISYGIGLSVASQLINTFNKDSFSAFKSAVHYDEESGSEEETLQYFSTVDPNYRSRRKKKLDSQNKNSQSFLSVLLNINHGLIAVFTDVKQDNGDLLENKHGEFWLEFNSGSLFCVTKYEGFDDKHYICLHSSSFSLYHKGIVNGVILPTETRLPSSTRPHWLEPTIYSSEEDGLSKTSSDGVGGDSLNMLSVAVKILSDKSESNTKEFLIAVGLKGATLQHRMLPSGLSWHEQILYFLNIADEPVLGYNPPTSFTTFHVHLWSCALDYRPLYLPIRSLLTVETFSVSSSVALDKSSSTLRIILDEAALHLSDKCNTVTINLSRDYVRVMDMGLLELTITAVKSDSDGEQTEPRFELHCSSDVVHIRTCSDSCAALMNLIQYIASYGDLQTPNKADMKPGAFQRRSKVDSSGRSSSRGPVLPEADQQMLRDLMSDAMEEIDMQQGTSSVKPQANGVLDEKSQIQEPCCSDLFLFPDESGNVSQESGPTYASFSHHFISDAMTGVPTENDDFCILFAPKAAMQEKEEEPVIKIMVDDAIVIRDNYFSLPVNKTDTSKAPLHFPIPVIRYVVKEVSLVWHLYGGKDFGIVPPTSPAKSYISPHSSPSHTPTRHGRNTVCGGKGRNHDFLMEIQLSKVKFQHEVYPPCKPDCDSSLSEHPVSRQVFIVQDLEIRDRLATSQMNKFLYLYCSKEMPRKAHSNMLTVKALHVCPESGRSPQECCLRVSLMPLRLNIDQDALFFLKDFFTSLSAEVELQMTPDPEVKKSPGADVTCSLPRHLSTSKEPNLVISFSGPKQPSQNDSANSVEVVNGMEEKNFSAEEASFRDQPVFFREFRFTSEVPIRLDYHGKHVSMDQGTLAGILIGLAQLNCSELKLKRLSYRHGLLGVDKLFSYAITEWLNDIKKNQLPGILGGVGPMHSLVQLVQGLKDLVWLPIEQYRKDGRIVRGFQRGAASFGTSTAMAALELTNRMVQTIQAAAETAYDMVSPGTLSIEPKKTKRFPHHRLAHQPVDLREGVAKAYSVVKEGITDTAQTIYETAAREHESRGVTGAVGEVLRQIPPAVVKPLIVATEATSNVLGGMRNQIRPDVRQDESQKWRHGDD TTG6KCU TT Literature-reported TTLVB9Z ID TTLVB9Z TTLVB9Z TN Autophagy-related protein 7 (ATG7) TTLVB9Z UP O95352 TTLVB9Z UC ATG7_HUMAN TTLVB9Z BC Autophagy phagophore-formation transporter TTLVB9Z SN hAGP7; Ubiquitin-like modifier-activating enzyme ATG7; Ubiquitin-activating enzyme E1-like protein; ATG12-activating enzyme E1 ATG7; APG7L; APG7-like TTLVB9Z GN ATG7 TTLVB9Z FC Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Plays also a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. Plays a role in regulating the liver clock and glucose metabolism by mediating the autophagic degradation of CRY1 (clock repressor) in a time-dependent manner. E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. TTLVB9Z SQ MAAATGDPGLSKLQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDMSAPTPARCCPAIGTLYNTNTLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPESLPLIQGPVGLDQRFSLKQIEALECAYDNLCQTEGVTALPYFLIKYDENMVLVSLLKHYSDFFQGQRTKITIGVYDPCNLAQYPGWPLRNFLVLAAHRWSSSFQSVEVVCFRDRTMQGARDVAHSIIFEVKLPEMAFSPDCPKAVGWEKNQKGGMGPRMVNLSECMDPKRLAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCLGGGKPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVNFSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGLKKPKQQGAGDLCPNHPVASADLLGSSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKVLDQYEREGFNFLAKVFNSSHSFLEDLTGLTLLHQETQAAEIWDMSDDETI TTLVB9Z TT Literature-reported TT69QD2 ID TT69QD2 TT69QD2 TN AXL receptor tyrosine kinase ligand (GAS6) TT69QD2 UP Q14393 TT69QD2 UC GAS6_HUMAN TT69QD2 SN Growth arrest-specific protein 6; GAS-6; AXLLG TT69QD2 GN GAS6 TT69QD2 FC Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. TT69QD2 PD 5VXZ; 4RA0; 2C5D; 1H30 TT69QD2 SQ MAPSLSPGPAALRRAPQLLLLLLAAECALAALLPAREATQFLRPRQRRAFQVFEEAKQGHLERECVEELCSREEAREVFENDPETDYFYPRYLDCINKYGSPYTKNSGFATCVQNLPDQCTPNPCDRKGTQACQDLMGNFFCLCKAGWGGRLCDKDVNECSQENGGCLQICHNKPGSFHCSCHSGFELSSDGRTCQDIDECADSEACGEARCKNLPGSYSCLCDEGFAYSSQEKACRDVDECLQGRCEQVCVNSPGSYTCHCDGRGGLKLSQDMDTCEDILPCVPFSVAKSVKSLYLGRMFSGTPVIRLRFKRLQPTRLVAEFDFRTFDPEGILLFAGGHQDSTWIVLALRAGRLELQLRYNGVGRVTSSGPVINHGMWQTISVEELARNLVIKVNRDAVMKIAVAGDLFQPERGLYHLNLTVGGIPFHEKDLVQPINPRLDGCMRSWNWLNGEDTTIQETVKVNTRMQCFSVTERGSFYPGSGFAFYSLDYMRTPLDVGTESTWEVEVVAHIRPAADTGVLFALWAPDLRAVPLSVALVDYHSTKKLKKQLVVLAVEHTALALMEIKVCDGQEHVVTVSLRDGEATLEVDGTRGQSEVSAAQLQERLAVLERHLRSPVLTFAGGLPDVPVTSAPVTAFYRGCMTLEVNRRLLDLDEAAYKHSDITAHSCPPVEPAAA TT69QD2 TT Clinical trial TTXHT8A ID TTXHT8A TTXHT8A TN Bacterial Acid phosphatase surE (Bact surE) TTXHT8A UP P36664 TTXHT8A UC SURE_ECOLI TTXHT8A BC Phosphoric monoester hydrolase TTXHT8A SN Stationary-phase survival protein surE; Phosphomonoesterase; Glycerophosphatase; Acid Phosphomonoesterase; Acid Phosphatase TTXHT8A GN Bact surE TTXHT8A FC This protein is essential for the survival of e.coli in stationary phase and for survival of heat and osmotic stresses. TTXHT8A SQ MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFENGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLDGHKHYDTAAAVTCSILRALCKEPLRTGRILNINVPDLPLDQIKGIRVTRCGTRHPADQVIPQQDPRGNTLYWIGPPGGKCDAGPGTDFAAVDEGYVSITPLHVDLTAHSAQDVVSDWLNSVGVGTQW TTXHT8A TT Literature-reported TTMEJZ5 ID TTMEJZ5 TTMEJZ5 TN Bacterial Bacitracin transport ATP-binding bcrA (Bact bcrA) TTMEJZ5 UP P42332 TTMEJZ5 UC BCRA_BACLI TTMEJZ5 BC ABC transporter TTMEJZ5 SN BCRA TTMEJZ5 GN Bact bcrA TTMEJZ5 FC Part of the binding-protein-dependent transport system for bacitracin that confer resistance to this antibiotic. Probably responsible for energy coupling to the transport system. TTMEJZ5 SQ MSTIIKTTDLTKMYGSQKSVDHLNINVKQGDIYGFLGRNGAGKTTTIRMLLGLIKPTSGQIEIFGENFFKNKKEILRRIGSIVEVPGFYANLTARENLLINAKIIGIHKKNAIDEVLEIVGLQHETKKLVGKFSLGMKQRLGIARALLHYPELLILDEPTNGLDPIGIKEMRRLIHSLAKERNITIFISSHILSEIEQLVDHVGIIHEGKLLEEIPFDHLKKRNRKYLEFQLSDQNKAVVLMEQHFDIHDYEVHQDGIIRVYSHLGQQGKLNKLFVENGIDVLKITMSEDSLEDYFVKLIGGGTIG TTMEJZ5 TT Literature-reported TT4W1VJ ID TT4W1VJ TT4W1VJ TN Bacterial Celldivision protein FtsZ (Bact ftsZ) TT4W1VJ UP P45485 TT4W1VJ UC FTSZ_WOLSP TT4W1VJ BC Peptidase TT4W1VJ SN FtsZprotein; FtsZ TT4W1VJ GN Bact ftsZ TT4W1VJ FC Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. TT4W1VJ SQ MSIDLSLPELPILHPRITVVGVGGAGGNAVNNMIQSNLQGVNFVVANTDAQALEKSLCDKKIQLGINLTKGLGAGALPDVGKGAAEESIDEIMEHIKDSHMLFITAGMGGGTGTGAAPVIAKAAREARAAVKDRAPKEKKILTVGVVTKPFGFEGVRRMPIAELGLEELQKYVDTLIVIPNQNLFRIANEKTTFSDAFKLADNVLHIGIRGVTDLMVMPGLINLDFADIETVMSEMGKAMIGTGEAEGEDRAISAAEAAISNPLLDNVSMKGAQGILINITGGGDMTLFEVDAAANRVREEVDENANIIFGATFDQAMEGRVRVSVLATGIDGRNNKSETSPISQSEDSEKEKFKWPYSQSESTQDKTLETKPAEQVSEGAKWGSNIYDIPAYLRRKK TT4W1VJ TT Clinical trial TTO3MV6 ID TTO3MV6 TTO3MV6 TN Bacterial GTP-binding protein YihA (Bact engB) TTO3MV6 UP P0A6P7 TTO3MV6 UC ENGB_ECOLI TTO3MV6 SN engB; Probable GTP-binding protein engB TTO3MV6 GN Bact engB TTO3MV6 FC Necessary for normal cell division and for the maintenance of normal septation. Depletion of this protein leads to a severe reduction in growth rate and to extensive filamentation, with a block beyond the stage of segregation. Essential for bacteria survivial. TTO3MV6 PD 1PUI TTO3MV6 SQ MTNLNYQQTHFVMSAPDIRHLPSDTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGYGYAEVPEEMKRKWQRALGEYLEKRQSLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVREAVLAFNGDVQVETFSSLKKQGVDKLRQKLDTWFSEMQPVEETQDGE TTO3MV6 TT Literature-reported TTPUDAR ID TTPUDAR TTPUDAR TN Bacterial Initiator protein DnaA (Bact dnaA) TTPUDAR UP P03004 TTPUDAR UC DNAA_ECOLI TTPUDAR SN Chromosomal replication initiator protein DnaA TTPUDAR GN Bact dnaA TTPUDAR FC Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA-ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring only 1 round of replication per cell cycle. DnaA can inhibit its own gene expression as well as that of other genes such as dam, rpoH, ftsA and mioC. TTPUDAR PD 2E0G; 1J1V TTPUDAR SQ MSLSLWQQCLARLQDELPATEFSMWIRPLQAELSDNTLALYAPNRFVLDWVRDKYLNNINGLLTSFCGADAPQLRFEVGTKPVTQTPQAAVTSNVAAPAQVAQTQPQRAAPSTRSGWDNVPAPAEPTYRSNVNVKHTFDNFVEGKSNQLARAAARQVADNPGGAYNPLFLYGGTGLGKTHLLHAVGNGIMARKPNAKVVYMHSERFVQDMVKALQNNAIEEFKRYYRSVDALLIDDIQFFANKERSQEEFFHTFNALLEGNQQIILTSDRYPKEINGVEDRLKSRFGWGLTVAIEPPELETRVAILMKKADENDIRLPGEVAFFIAKRLRSNVRELEGALNRVIANANFTGRAITIDFVREALRDLLALQEKLVTIDNIQKTVAEYYKIKVADLLSKRRSRSVARPRQMAMALAKELTNHSLPEIGDAFGGRDHTTVLHACRKIEQLREESHDIKEDFSNLIRTLSS TTPUDAR TT Literature-reported TT13OHY ID TT13OHY TT13OHY TN Bacterial Kgp protease (Bact kgp-381) TT13OHY UP P96966 TT13OHY UC P96966_PORGN TT13OHY BC Protease TT13OHY SN Cysteine protease TT13OHY GN Bact kgp-381 TT13OHY FC Important for both nutrition and virulence of P. gingivalis TT13OHY SQ MRKLLLLIAASLLGVGLYAQSAKIKLDAPTTRTTCTNNSFKQFDASFSFNEVELTKVETKGGTFASVSIPGAFPTGEVGSPEVPAVRKLIAVPVGATPVVRVKSFTEQVYSLNQYGSEKLMPHQPSMSKSDDPEKVPFVYNAAAYARKGFVGQELTQVEMLGTMRGVRIAALTINPVQYDVVANQLKVRNNIEIEVSFQGADEVATQRLYDASFSPYFETAYKQLFNRDVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKVTDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKY TT13OHY TT Literature-reported TT3DQUT ID TT3DQUT TT3DQUT TN Bacterial Lantibiotic mersacidin (Bact glmM) TT3DQUT UP P31120 TT3DQUT UC GLMM_ECOLI TT3DQUT SN glmM of Escherichia coli; Protein mrsA; Mersacidin TT3DQUT GN Bact glmM TT3DQUT FC Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Can also catalyze the formation of glucose-6-P from glucose-1-P, although at a 1400-fold lower rate. TT3DQUT EC EC 5.4.2.10 TT3DQUT SQ MSNRKYFGTDGIRGRVGDAPITPDFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAVAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKEISCVDSAELGKASRIVDAAGRYIEFCKATFPNELSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGVNINAEVGATDVRALQARVLAEKADLGIAFDGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGWRIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSGMKMFPQILVNVRYTAGSGDPLEHESVKAVTAEVEAALGNRGRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAVKAV TT3DQUT TT Literature-reported TT6ERZB ID TT6ERZB TT6ERZB TN Bacterial Phosphatidylcholine-specificphospholipase C (Bact plcN) TT6ERZB UP Q9RGS8 TT6ERZB UC PHLN_BURPS TT6ERZB BC Phosphoric diester hydrolase TT6ERZB SN plcN; Phosphatidylcholine-hydrolyzing phospholipase C; Phosphatidylcholine cholinephosphohydrolase; PLC-N; PC-PLC; Non-hemolytic phospholipase C; Lecithinase TT6ERZB GN Bact plcN TT6ERZB FC Hydrolyzes phosphatidylserine as well as phosphatidylcholine. TT6ERZB SQ MTNQNRRDFLRLAAGTAGAAALQLFPPVIREALAIPANRRTGTIRDVEHIVILMQENRSFDHYFGKLRGVRGFGDPRPLALQNGKSVFHQPVLLGPAELLPFHPDASNLGMQFLQDLPHGWQDMHGAWNKGRYDRWIANKGTTTMAYLERDDIPFHYQLADAFTICDAYHCSIPSSTDPNRYYMWTGYVGNDGAGGGPVLGNEEAGYGWSTYPETLEQAGVSWKIYQDIGTGLDAAGSWGWTQNPYIGNYGDNSLLYFNQYRNAQPGSPLYDKARTGTNVSAGGTLFDVLQQDVKNGTLPQVSWICAPEAYSEHPNWPANYGAWYVEQVLKALTSNPDVWSKTALFITYDENDGFFDHVAPPFAPQSRENGLSTVSTAGEIFAGDATHMAGPYGLGPRVPMLVVSPWTKGGWVCSQTFDHTSLLQFIEARFNDRYSVRAPNVTPWRRAVCGDLTSAFNFSSPDGSWPQLPDTSGYAPPDRNRHPSYVPVPPAAQSMPKQEAGLRAARALPYELFVLGRIDQSTGKFKLTFANTGRAGAAFQVTAGNRLDGPWAYTVEARKRLSDEWSTALTLSIYDLTVYGPNGFLCQFRGSTAAALGLSANPEVIYGYDVANGNITLRLSNRGRAAVRLTVTNAYGNAAPRVYELKPGQRINDYWDLRDSHSWYDLSVSDGAPNGFLRRFAGHVETGRPSTSDPLIATA TT6ERZB TT Literature-reported TTA3F9Z ID TTA3F9Z TTA3F9Z TN Bacterial Phosphoenolpyruvate synthase (Bact ppsA) TTA3F9Z UP P56070 TTA3F9Z UC PPSA_HELPY TTA3F9Z BC Kinase TTA3F9Z SN ppsA; Pyruvate,water dikinase; Pyruvate, water dikinase; PEP synthase TTA3F9Z GN Bact ppsA TTA3F9Z FC Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. TTA3F9Z SQ MRYIKFFKELNNKNVNLVGGKNASIGEMFQELVPIGIKVPDGFAITSEAYWYLLEQGGAKQKIIELLENVDATEIDVLKIRSKQIRELIFGTPFPSDLRDEIFQAYEILSQQYHMKEADVAVRSSATAEDLPDASFAGQQDTYLNIKGKTELIHYIKSCLASLFTDRAISYRASRGFDHLKVALSVGVQKMVRADKGSAGVMFSIDTETGFKDAVFITSAWGLGENVVGGTINPDEFYVFKPTLEQNKRPIIKRQLGNKTQKMVYAPRGSEHPTRNIKTTKKEWQSFSLSDEDVLILAKYAIEIEKHYSKEAKQYRPMDIEWAKDGESGEIFIVQARPETVQSQKSKEESQVFEKFKFKNPNEKKEIILQGRAIGSKIGSGKVRIINDLEHMNSFKEGEILVTDNTDPDWEPCMKKASAVITNRGGRTCHAAIVAREIGVPAIVGVSGATDSLYTGMEITVSCAEGEEGYVYAGIYEHEIERVELSNMQETQTKIYINIGNPEKAFGFSQLPNHGVGLARMEMIILNQIKAHPLALVDLHHKKSVKEKNEIENLMAGYANPKDFFVKKIAEGIGMISAAFYPKPVIVRTSDFKSNEYMRMLGGSSYEPNEENPMLGYRGASRYYSESYNEAFSWECEALALVREEMGLTNMKVMIPFLRTIEEGKKVLEILRKNNLESGKNGLEIYIMCELPVNVILADDFLSLFDGFSIGSNDLTQLTLGVDRDSELVSHVFDERNEAMLKMFKKAIEACKRHNKYCGICGQAPSDYPEVTEFLVKEGITSISLNPDSVIPTWNAVAKLEKELKEHGLTEH TTA3F9Z TT Literature-reported TTT4DEI ID TTT4DEI TTT4DEI TN Bacterial Phospho-MurNAc-pentapeptide translocase (Bact MraY) TTT4DEI UP P0A6W3 TTT4DEI UC MRAY_ECOLI TTT4DEI SN UDP-MurNAc-pentapeptide phosphotransferase; Phospho-N-acetylmuramoyl-pentapeptide-transferase TTT4DEI GN Bact MraY TTT4DEI FC First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan. TTT4DEI EC EC 2.7.8.13 TTT4DEI SQ MLVWLAEHLVKYYSGFNVFSYLTFRAIVSLLTALFISLWMGPRMIAHLQKLSFGQVVRNDGPESHFSKRGTPTMGGIMILTAIVISVLLWAYPSNPYVWCVLVVLVGYGVIGFVDDYRKVVRKDTKGLIARWKYFWMSVIALGVAFALYLAGKDTPATQLVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAGGFALVAWATGNMNFASYLHIPYLRHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVETLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLATLKVR TTT4DEI TT Literature-reported TTO4NP3 ID TTO4NP3 TTO4NP3 TN Bacterial Serine/threonine protein phosphatase 1 (Bact pphA) TTO4NP3 UP P55798 TTO4NP3 UC PRP1_ECOLI TTO4NP3 BC Phosphoric monoester hydrolase TTO4NP3 SN pphA; Nuclear PP1 TTO4NP3 GN Bact pphA TTO4NP3 FC Plays a key role in signaling protein misfolding via the CpxR/CPXA transducing system. It also modulates the phosphorylated status of many phosphoproteins in E.coli, some of which acting as major chaperones. Has been shown, in vitro, to act on Ser, Thr and Tyr-phosphorylated substrates. TTO4NP3 SQ MKQPAPVYQRIAGHQWRHIWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPQSLRCLQLLEQHWVCAVRGNHEQMAMDALASQQMSLWLMNGGDWFIALADNQQKQAKTALEKCQHLPFILEVHSRTGKHVIAHADYPDDVYEWQKDVDLHQVLWSRSRLGERQKGQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ TTO4NP3 TT Literature-reported TTCFSA1 ID TTCFSA1 TTCFSA1 TN Bacterial Trehalose-phosphatase (Bact otsB) TTCFSA1 UP P31678 TTCFSA1 UC OTSB_ECOLI TTCFSA1 BC Phosphoric monoester hydrolase TTCFSA1 SN otsB; Trehalose-6-phosphate phosphatase; Trehalose 6-phosphate phosphatase; TPP TTCFSA1 GN Bact otsB TTCFSA1 FC Removes the phosphate from trehalose 6-phosphate (Tre6P) to produce free trehalose. Also catalyzes the dephosphorylation of glucose-6-phosphate (Glu6P) and 2-deoxyglucose-6-phosphate (2dGlu6P). TTCFSA1 SQ MTEPLTETPELSAKYAWFFDLDGTLAEIKPHPDQVVVPDNILQGLQLLATASDGALALISGRSMVELDALAKPYRFPLAGVHGAERRDINGKTHIVHLPDAIARDISVQLHTVIAQYPGAELEAKGMAFALHYRQAPQHEDALMTLAQRITQIWPQMALQQGKCVVEIKPRGTSKGEAIAAFMQEAPFIGRTPVFLGDDLTDESGFAVVNRLGGMSVKIGTGATQASWRLAGVPDVWSWLEMITTALQQKRENNRSDDYESFSRSI TTCFSA1 TT Literature-reported TTC9YX5 ID TTC9YX5 TTC9YX5 TN B-cell lymphoma 6 protein (BCL-6) TTC9YX5 UP P41182 TTC9YX5 UC BCL6_HUMAN TTC9YX5 SN Zinc finger protein 51; Zinc finger and BTB domain-containing protein 27; ZNF51; ZBTB27; Protein LAZ-3; LAZ3; BCL5; BCL-6; BCL-5; B-cell lymphoma 5 protein TTC9YX5 GN BCL6 TTC9YX5 FC Transcriptional repressor mainly required for germinal center (GC) formation and antibody affinity maturation which has different mechanisms of action specific to the lineage and biological functions. Forms complexes with different corepressors and histone deacetylases to repress the transcriptional expression of different subsets of target genes. Represses its target genes by binding directly to the DNA sequence 5'-TTCCTAGAA-3' (BCL6-binding site) or indirectly by repressing the transcriptional activity of transcription factors. In GC B-cells, represses genes that function in differentiation, inflammation, apoptosis and cell cycle control, also autoregulates its transcriptional expression and up-regulates, indirectly, the expression of some genes important for GC reactions, such as AICDA, through the repression of microRNAs expression, like miR155. An important function is to allow GC B-cells to proliferate very rapidly in response to T-cell dependent antigens and tolerate the physiological DNA breaks required for immunglobulin class switch recombination and somatic hypermutation without inducing a p53/TP53-dependent apoptotic response. In follicular helper CD4(+) T-cells (T(FH) cells), promotes the expression of T(FH)-related genes but inhibits the differentiation of T(H)1, T(H)2 and T(H)17 cells. Also required for the establishment and maintenance of immunological memory for both T- and B-cells. Suppresses macrophage proliferation through competition with STAT5 for STAT-binding motifs binding on certain target genes, such as CCL2 and CCND2. In response to genotoxic stress, controls cell cycle arrest in GC B-cells in both p53/TP53-dependedent and -independent manners. Besides, also controls neurogenesis through the alteration of the composition of NOTCH-dependent transcriptional complexes at selective NOTCH targets, such as HES5, including the recruitment of the deacetylase SIRT1 and resulting in an epigenetic silencing leading to neuronal differentiation. TTC9YX5 PD 6EW8; 6EW7; 6EW6; 6CQ1; 6C3N TTC9YX5 SQ MASPADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPEGFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASEAEMVSAIKPPREEFLNSRMLMPQDIMAYRGREVVENNLPLRSAPGCESRAFAPSLYSGLSTPPASYSMYSHLPVSSLLFSDEEFRDVRMPVANPFPKERALPCDSARPVPGEYSRPTLEVSPNVCHSNIYSPKETIPEEARSDMHYSVAEGLKPAAPSARNAPYFPCDKASKEEERPSSEDEIALHFEPPNAPLNRKGLVSPQSPQKSDCQPNSPTESCSSKNACILQASGSPPAKSPTDPKACNWKKYKFIVLNSLNQNAKPEGPEQAELGRLSPRAYTAPPACQPPMEPENLDLQSPTKLSASGEDSTIPQASRLNNIVNRSMTGSPRSSSESHSPLYMHPPKCTSCGSQSPQHAEMCLHTAGPTFPEEMGETQSEYSDSSCENGAFFCNECDCRFSEEASLKRHTLQTHSDKPYKCDRCQASFRYKGNLASHKTVHTGEKPYRCNICGAQFNRPANLKTHTRIHSGEKPYKCETCGARFVQVAHLRAHVLIHTGEKPYPCEICGTRFRHLQTLKSHLRIHTGEKPYHCEKCNLHFRHKSQLRLHLRQKHGAITNTKVQYRVSATDLPPELPKAC TTC9YX5 TT Literature-reported TTGT9C7 ID TTGT9C7 TTGT9C7 TN Bcl-2-related protein A1 (BCL2A1) TTGT9C7 UP Q16548 TTGT9C7 UC B2LA1_HUMAN TTGT9C7 SN Protein GRS; Protein BFL-1; Hemopoietic-specific early response protein; HBPA1; GRS; Bcl2-L-5; Bcl-2-like protein 5; BFL1; BCL2L5 TTGT9C7 GN BCL2A1 TTGT9C7 FC Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection (By similarity). Can inhibit apoptosis induced by serum starvation in the mammary epithelial cell line HC11 (By similarity). TTGT9C7 PD 6MBC; 6MBB; 6E3J; 6E3I; 5WHI TTGT9C7 SQ MTDCEFGYIYRLAQDYLQCVLQIPQPGSGPSKTSRVLQNVAFSVQKEVEKNLKSCLDNVNVVSVDTARTLFNQVMEKEFEDGIINWGRIVTIFAFEGILIKKLLRQQIAPDVDTYKEISYFVAEFIMNNTGEWIRQNGGWENGFVKKFEPKSGWMTFLEVTGKICEMLSLLKQYC TTGT9C7 TT Patented-recorded TT5M7LN ID TT5M7LN TT5M7LN TN Beclin-1 (BECN1) TT5M7LN UP Q14457 TT5M7LN UC BECN1_HUMAN TT5M7LN SN Protein GT197; GT197; Coiledcoil myosinlike BCL2interacting protein; Coiled-coil myosin-like BCL2-interacting protein TT5M7LN GN BECN1 TT5M7LN FC Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. Protects against infection by a neurovirulent strain of Sindbis virus. May play a role in antiviral host defense. Plays a central role in autophagy. TT5M7LN PD 6HOK; 6HOJ; 6HOI; 6DCO; 6DCN TT5M7LN SQ MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK TT5M7LN TT Literature-reported TT5M7LN FM Beclin family TTY7FKA ID TTY7FKA TTY7FKA TN Beta-2-microglobulin (B2M) TTY7FKA UP P61769 TTY7FKA UC B2MG_HUMAN TTY7FKA SN Beta-2-microglobulin TTY7FKA GN B2M TTY7FKA FC Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Exogenously applied M.tuberculosis EsxA or EsxA-EsxB (or EsxA expressed in host) binds B2M and decreases its export to the cell surface (total protein levels do not change), probably leading to defects in class I antigen presentation. TTY7FKA PD 6MTM; 6MTL; 6MT6; 6MT5; 6MT4 TTY7FKA SQ MSRSVALAVLALLSLSGLEAIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM TTY7FKA TT Literature-reported TT5A4DX ID TT5A4DX TT5A4DX TN Beta-adrenergic receptor kinase 2 (ADRBK2) TT5A4DX UP P35626 TT5A4DX UC ARBK2_HUMAN TT5A4DX SN G-protein-coupled receptor kinase 3; Beta-ARK-2; BARK2; ADRBK2 TT5A4DX GN GRK3 TT5A4DX FC Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors. TT5A4DX EC EC 2.7.11.15 TT5A4DX SQ MADLEAVLADVSYLMAMEKSKATPAARASKRIVLPEPSIRSVMQKYLAERNEITFDKIFNQKIGFLLFKDFCLNEINEAVPQVKFYEEIKEYEKLDNEEDRLCRSRQIYDAYIMKELLSCSHPFSKQAVEHVQSHLSKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRFCQWKNVELNIHLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDCDQELYKNFPLVISERWQQEVTETVYEAVNADTDKIEARKRAKNKQLGHEEDYALGKDCIMHGYMLKLGNPFLTQWQRRYFYLFPNRLEWRGEGESRQNLLTMEQILSVEETQIKDKKCILFRIKGGKQFVLQCESDPEFVQWKKELNETFKEAQRLLRRAPKFLNKPRSGTVELPKPSLCHRNSNGL TT5A4DX TT Literature-reported TTPDCTM ID TTPDCTM TTPDCTM TN Beta-arrestin messenger RNA (ARRB mRNA) TTPDCTM UP P49407; P32121 TTPDCTM UC ARRB1_HUMAN; ARRB2_HUMAN TTPDCTM BC mRNA target TTPDCTM SN Non-visual arrestin; Beta-arrestin; Arrestin beta; ARR TTPDCTM GN ARRB1; ARRB2 TTPDCTM FC The extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). TTPDCTM SQ MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTCAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPPNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEPPHREVPENETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKEEEEDGTGSPQLNNR TTPDCTM TT Literature-reported TTPDCTM FM mRNA target TT8SO2I ID TT8SO2I TT8SO2I TN Beta-arrestin-2 (ARRB2) TT8SO2I UP P32121 TT8SO2I UC ARRB2_HUMAN TT8SO2I BC Arrestin protein TT8SO2I SN Non-visual arrestin-3; Betaarrestin2; Arrestin beta2; Arrestin beta-2; ARR2; ARB2 TT8SO2I GN ARRB2 TT8SO2I FC During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires GRK2. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in IL8-mediated granule release in neutrophils. Involved in the internalization of the atypical chemokine receptor ACKR3. Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. TT8SO2I SQ MGEKPGTRVFKKSSPNCKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTCAFRYGREDLDVLGLSFRKDLFIATYQAFPPVPNPPRPPTRLQDRLLRKLGQHAHPFFFTIPQNLPCSVTLQPGPEDTGKACGVDFEIRAFCAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADICLFSTAQYKCPVAQLEQDDQVSPSSTFCKVYTITPLLSDNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIPLPRPQSAAPETDVPVDTNLIEFDTNYATDDDIVFEDFARLRLKGMKDDDYDDQLC TT8SO2I TT Literature-reported TTDS503 ID TTDS503 TTDS503 TN Beta-crystallin B1 (CRYBB1) TTDS503 UP P53674 TTDS503 UC CRBB1_HUMAN TTDS503 SN CRYBB1; Beta B1-crystallin TTDS503 GN CRYBB1 TTDS503 FC Crystallins are the dominant structural components of the vertebrate eye lens. TTDS503 PD 1OKI TTDS503 SQ MSQAAKASASATVAVNPGPDTKGKGAPPAGTSPSPGTTLAPTTVPITSAKAAELPPGNYRLVVFELENFQGRRAEFSGECSNLADRGFDRVRSIIVSAGPWVAFEQSNFRGEMFILEKGEYPRWNTWSSSYRSDRLMSFRPIKMDAQEHKISLFEGANFKGNTIEIQGDDAPSLWVYGFSDRVGSVKVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQSLRRLRDKQWHLEGSFPVLATEPPK TTDS503 TT Literature-reported TTIVY12 ID TTIVY12 TTIVY12 TN Beta-defensin 4A (DEFB4A) TTIVY12 UP O15263 TTIVY12 UC DFB4A_HUMAN TTIVY12 SN hBD2; Skinantimicrobial peptide 1; SAP1; Defensin, beta 2; DEFB4B; DEFB4A; Betadefensin 4A; Betadefensin 2; BD2 TTIVY12 GN DEFB4A TTIVY12 FC Has antibacterial activity. TTIVY12 PD 6CS9; 1FQQ; 1FD4; 1FD3; 1E4Q TTIVY12 SQ MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP TTIVY12 TT Literature-reported TTH1EQO ID TTH1EQO TTH1EQO TN Bifidobacterium Exo-alpha sialidase (BB sialidase) TTH1EQO UP A0A151C7Z8 TTH1EQO UC A0A151C7Z8_BIFBI TTH1EQO SN Exo-alpha-sialidase; BB Sialidase TTH1EQO GN BB sialidase TTH1EQO FC Involved in the degradation of sialyloligosaccharides in human milk and intestinal glycoconjugates. TTH1EQO EC EC 3.2.1.18 TTH1EQO SQ MVRSTKPSLLRRFGALVAAAAMLVVLPAGVSTASAASDDADMLTVTMTRTDALGDEVYVGDTLTYSFTNTNNTSSAFTAFPAESNLSGVLTTGTPNCRYENLAGGASYPCSTASHTITADDLTAGSFTPRTVWKATSDRGGTQVLQDNIVSTGDTVTVKEGKRPDPATIPTDRADGEAVRLATARQNLGTECYRIPALAEAPNGWILAAFDQRPNTAMANGSGVKCWDAPQPNSIVQRISKDGGKSWTPIQYVAQGKNAPERYGYSDPSYVVDKETGEIFLFFVHSYNKGFADSQLGVDESNRNVLHAVVVSSKDNGETWSKPRDITADITKGYENEWKSRFATSGAGIQLKYGKYKGRLIQQYAVGRTTGSNAAVSVYSDDHGKTWQAGNPVTGMLMDENKVVELSDGRVMLNSRPGNGSGYRRVAISEDGGVNYGTVKNETQLPDPNNNAHITRAFPNAPEGSAKAKVLLYSSPRANNEGRANGVVRISLDDGTTWSSGKLYKEGSMAYSVITALSGAAGGGYGLLYEGAWVTGGGIDSHDIMYTHISMDWLGYLSATADDVTASVEEGASTVDVTVPVSNVGSVDYTGVTVTPADLPTGWSASPVNVGALASGTSKDVTVTVNVPATAKKDDVAKIVLRVTGTSAANADATTGFDGSITVNVTEKSEPDPEPEPTITGVSAVTSQAGVKVGDVFDASKVSVTAAMSDGSSKALAAGEYSLSAVDADGKAVDLAEPFAAAGVVTVTVSVPVEGAGPLTASFTIDVAEKSVDPEPKPEPEPKPEPEKPAGPKVDVPTEQPGLSKTGASTAGMSIVFVLLALSGVAALSLRRRSAH TTH1EQO TT Literature-reported TTTG6H1 ID TTTG6H1 TTTG6H1 TN Bone morphogenetic protein 10 (BMP10) TTTG6H1 UP O95393 TTTG6H1 UC BMP10_HUMAN TTTG6H1 BC Growth factor TTTG6H1 SN BMP10 TTTG6H1 GN BMP10 TTTG6H1 FC Required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6, leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors. Inhibits endothelial cell migration and growth. May reduce cell migration and cell matrix adhesion in breast cancer cell lines. TTTG6H1 SQ MGSLVLTLCALFCLAAYLVSGSPIMNLEQSPLEEDMSLFGDVFSEQDGVDFNTLLQSMKDEFLKTLNLSDIPTQDSAKVDPPEYMLELYNKFATDRTSMPSANIIRSFKNEDLFSQPVSFNGLRKYPLLFNVSIPHHEEVIMAELRLYTLVQRDRMIYDGVDRKITIFEVLESKGDNEGERNMLVLVSGEIYGTNSEWETFDVTDAIRRWQKSGSSTHQLEVHIESKHDEAEDASSGRLEIDTSAQNKHNPLLIVFSDDQSSDKERKEELNEMISHEQLPELDNLGLDSFSSGPGEEALLQMRSNIIYDSTARIRRNAKGNYCKRTPLYIDFKEIGWDSWIIAPPGYEAYECRGVCNYPLAEHLTPTKHAIIQALVHLKNSQKASKACCVPTKLEPISILYLDKGVVTYKFKYEGMAVSECGCR TTTG6H1 TT Literature-reported TTD3BSX ID TTD3BSX TTD3BSX TN Bone morphogenetic protein 4 (BMP4) TTD3BSX UP P12644 TTD3BSX UC BMP4_HUMAN TTD3BSX BC Growth factor TTD3BSX SN DVR4; Bone morphogenetic protein 2B; BMP2B; BMP-4; BMP-2B TTD3BSX GN BMP4 TTD3BSX FC Acts in mesoderm induction, tooth development, limb formation and fracture repair. Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibit hair follicle induction. Induces cartilage and bone formation. TTD3BSX SQ MIPGNRMLMVVLLCQVLLGGASHASLIPETGKKKVAEIQGHAGGRRSGQSHELLRDFEATLLQMFGLRRRPQPSKSAVIPDYMRDLYRLQSGEEEEEQIHSTGLEYPERPASRANTVRSFHHEEHLENIPGTSENSAFRFLFNLSSIPENEVISSAELRLFREQVDQGPDWERGFHRINIYEVMKPPAEVVPGHLITRLLDTRLVHHNVTRWETFDVSPAVLRWTREKQPNYGLAIEVTHLHQTRTHQGQHVRISRSLPQGSGNWAQLRPLLVTFGHDGRGHALTRRRRAKRSPKHHSQRARKKNKNCRRHSLYVDFSDVGWNDWIVAPPGYQAFYCHGDCPFPLADHLNSTNHAIVQTLVNSVNSSIPKACCVPTELSAISMLYLDEYDKVVLKNYQEMVVEGCGCR TTD3BSX TT Literature-reported TTD3BSX FM Transforming growth factor TT0JPVF ID TT0JPVF TT0JPVF TN Bone/cartilage proteoglycan I (BGN) TT0JPVF UP P21810 TT0JPVF UC PGS1_HUMAN TT0JPVF BC Small leucine-rich proteoglycan TT0JPVF SN PGS1; BGN TT0JPVF GN BGN TT0JPVF FC May be involved in collagen fiber assembly. TT0JPVF SQ MWPLWRLVSLLALSQALPFEQRGFWDFTLDDGPFMMNDEEASGADTSGVLDPDSVTPTYSAMCPFGCHCHLRVVQCSDLGLKSVPKEISPDTTLLDLQNNDISELRKDDFKGLQHLYALVLVNNKISKIHEKAFSPLRKLQKLYISKNHLVEIPPNLPSSLVELRIHDNRIRKVPKGVFSGLRNMNCIEMGGNPLENSGFEPGAFDGLKLNYLRISEAKLTGIPKDLPETLNELHLDHNKIQAIELEDLLRYSKLYRLGLGHNQIRMIENGSLSFLPTLRELHLDNNKLARVPSGLPDLKLLQVVYLHSNNITKVGVNDFCPMGFGVKRAYYNGISLFNNPVPYWEVQPATFRCVTDRLAIQFGNYKK TT0JPVF TT Literature-reported TT04YCM ID TT04YCM TT04YCM TN Borealin (CDCA8) TT04YCM UP Q53HL2 TT04YCM UC BOREA_HUMAN TT04YCM SN hDasraB; hDasra-B; Pluripotent embryonic stem cellrelated gene 3 protein; Pluripotent embryonic stem cell-related gene 3 protein; PESCRG3; DasraB; Dasra-B; Dasra B; Cell division cycleassociated protein 8; Cell division cycle-associated protein 8 TT04YCM GN CDCA8 TT04YCM FC The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment. Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. TT04YCM PD 2RAX; 2RAW; 2QFA; 2KDD TT04YCM SQ MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK TT04YCM TT Literature-reported TTY0RZT ID TTY0RZT TTY0RZT TN BORIS messenger RNA (CTCFL mRNA) TTY0RZT UP Q8NI51 TTY0RZT UC CTCFL_HUMAN TTY0RZT BC mRNA target TTY0RZT SN Zinc finger protein CTCF-T (mRNA); Transcriptional repressor CTCFL (mRNA); Cancer/testis antigen 27 (mRNA); CTCF-like protein (mRNA); CTCF paralog (mRNA); CT27 (mRNA); CCCTC-binding factor (mRNA); Brother of the regulator of imprinted sites (mRNA); BORIS (mRNA) TTY0RZT GN CTCFL TTY0RZT FC Plays a key role in gene imprinting in male germline, by participating in the establishment of differential methylation at the IGF2/H19 imprinted control region (ICR). Directly binds the unmethylated H19 ICR and recruits the PRMT7 methyltransferase, leading to methylate histone H4 'Arg-3' to form H4R3sme2. This probably leads to recruit de novo DNA methyltransferases at these sites. Seems to act as tumor suppressor. In association with DNMT1 and DNMT3B, involved in activation of BAG1 gene expression by binding to its promoter. Required for dimethylation of H3 lysine 4 (H3K4me2) of MYC and BRCA1 promoters. Testis-specific DNA binding protein responsible for insulator function, nuclear architecture and transcriptional control, which probably acts by recruiting epigenetic chromatin modifiers. TTY0RZT SQ MAATEISVLSEQFTKIKELELMPEKGLKEEEKDGVCREKDHRSPSELEAERTSGAFQDSVLEEEVELVLAPSEESEKYILTLQTVHFTSEAVELQDMSLLSIQQQEGVQVVVQQPGPGLLWLEEGPRQSLQQCVAISIQQELYSPQEMEVLQFHALEENVMVASEDSKLAVSLAETTGLIKLEEEQEKNQLLAERTKEQLFFVETMSGDERSDEIVLTVSNSNVEEQEDQPTAGQADAEKAKSTKNQRKTKGAKGTFHCDVCMFTSSRMSSFNRHMKTHTSEKPHLCHLCLKTFRTVTLLRNHVNTHTGTRPYKCNDCNMAFVTSGELVRHRRYKHTHEKPFKCSMCKYASVEASKLKRHVRSHTGERPFQCCQCSYASRDTYKLKRHMRTHSGEKPYECHICHTRFTQSGTMKIHILQKHGENVPKYQCPHCATIIARKSDLRVHMRNLHAYSAAELKCRYCSAVFHERYALIQHQKTHKNEKRFKCKHCSYACKQERHMTAHIRTHTGEKPFTCLSCNKCFRQKQLLNAHFRKYHDANFIPTVYKCSKCGKGFSRWINLHRHSEKCGSGEAKSAASGKGRRTRKRKQTILKEATKGQKEAAKGWKEAANGDEAAAEEASTTKGEQFPGEMFPVACRETTARVKEEVDEGVTCEMLLNTMDK TTY0RZT TT Literature-reported TTY0RZT FM mRNA target TTV6WMQ ID TTV6WMQ TTV6WMQ TN BR serine/threonine kinase 1 (BRSK1) TTV6WMQ UP Q8TDC3 TTV6WMQ UC BRSK1_HUMAN TTV6WMQ SN hSAD1; Synapses of Amphids Defective homolog 1; Serine/threonine-protein kinase SAD-B; Serine/threonine-protein kinase BRSK1; SADB; SAD1 homolog; SAD1; KIAA1811; Brain-specific serine/threonine-protein kinase 1; Brain-selective kinase 1; BR serine/threonine-protein kinase 1 TTV6WMQ GN BRSK1 TTV6WMQ FC Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C. TTV6WMQ EC EC 2.7.11.1 TTV6WMQ SQ MSSGAKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGGGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGAGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSGGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGAPPRSLQPPPGRPDPELSSSPRRGPPKDKKLLATNGTPLP TTV6WMQ TT Literature-reported TTHZN4X ID TTHZN4X TTHZN4X TN BR serine/threonine kinase 2 (BRSK2) TTHZN4X UP Q8IWQ3 TTHZN4X UC BRSK2_HUMAN TTHZN4X SN Serine/threonine-protein kinase SAD-A; Serine/threonine-protein kinase BRSK2; Serine/threonine-protein kinase 29; STK29; SADA; PEN11B; HUSSY-12; C11orf7; Brain-specific serine/threonine-protein kinase 2; Brain-selective kinase 2; BR serine/threonine-protein kinase 2 TTHZN4X GN BRSK2 TTHZN4X FC Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr-174 can inhibit insulin secretion, BRSK2 phosphorylated at Thr-260 can promote insulin secretion. Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress. TTHZN4X EC EC 2.7.11.1 TTHZN4X SQ MTSTGKDGGAQHAQYVGPYRLEKTLGKGQTGLVKLGVHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSQEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRARLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFISLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPSLSHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDPPAAQHLSDTTNCMEMMTGRLSKCGSPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGPGGDAEYPTGKDTAKMGPPTARREQP TTHZN4X TT Literature-reported TT2MV0R ID TT2MV0R TT2MV0R TN Bromodomain adjacent to zinc finger 2A (BAZ2A) TT2MV0R UP Q9UIF9 TT2MV0R UC BAZ2A_HUMAN TT2MV0R SN hWALp3; Transcription termination factor I-interacting protein 5; Tip5; TTF-I-interacting protein 5; KIAA0314; Bromodomain adjacent to zinc finger domain protein 2A TT2MV0R GN BAZ2A TT2MV0R FC In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription. Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing. Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. TT2MV0R PD 6FKP; 6FI0; 6FHU; 6FGW; 6FGV TT2MV0R SQ MEMEANDHFNFTGLPPAPAASGLKPSPSSGEGLYTNGSPMNFPQQGKSLNGDVNVNGLSTVSHTTTSGILNSAPHSSSTSHLHHPSVAYDCLWNYSQYPSANPGSNLKDPPLLSQFSGGQYPLNGILGGSRQPSSPSHNTNLRAGSQEFWANGTQSPMGLNFDSQELYDSFPDQNFEVMPNGPPSFFTSPQTSPMLGSSIQTFAPSQEVGSGIHPDEAAEKEMTSVVAENGTGLVGSLELEEEQPELKMCGYNGSVPSVESLHQEVSVLVPDPTVSCLDDPSHLPDQLEDTPILSEDSLEPFNSLAPEPVSGGLYGIDDTELMGAEDKLPLEDSPVISALDCPSLNNATAFSLLADDSQTSTSIFASPTSPPVLGESVLQDNSFDLNNGSDAEQEEMETQSSDFPPSLTQPAPDQSSTIQLHPATSPAVSPTTSPAVSLVVSPAASPEISPEVCPAASTVVSPAVFSVVSPASSAVLPAVSLEVPLTASVTSPKASPVTSPAAAFPTASPANKDVSSFLETTADVEEITGEGLTASGSGDVMRRRIATPEEVRLPLQHGWRREVRIKKGSHRWQGETWYYGPCGKRMKQFPEVIKYLSRNVVHSVRREHFSFSPRMPVGDFFEERDTPEGLQWVQLSAEEIPSRIQAITGKRGRPRNTEKAKTKEVPKVKRGRGRPPKVKITELLNKTDNRPLKKLEAQETLNEEDKAKIAKSKKKMRQKVQRGECQTTIQGQARNKRKQETKSLKQKEAKKKSKAEKEKGKTKQEKLKEKVKREKKEKVKMKEKEEVTKAKPACKADKTLATQRRLEERQRQQMILEEMKKPTEDMCLTDHQPLPDFSRVPGLTLPSGAFSDCLTIVEFLHSFGKVLGFDPAKDVPSLGVLQEGLLCQGDSLGEVQDLLVRLLKAALHDPGFPSYCQSLKILGEKVSEIPLTRDNVSEILRCFLMAYGVEPALCDRLRTQPFQAQPPQQKAAVLAFLVHELNGSTLIINEIDKTLESMSSYRKNKWIVEGRLRRLKTVLAKRTGRSEVEMEGPEECLGRRRSSRIMEETSGMEEEEEEESIAAVPGRRGRRDGEVDATASSIPELERQIEKLSKRQLFFRKKLLHSSQMLRAVSLGQDRYRRRYWVLPYLAGIFVEGTEGNLVPEEVIKKETDSLKVAAHASLNPALFSMKMELAGSNTTASSPARARGRPRKTKPGSMQPRHLKSPVRGQDSEQPQAQLQPEAQLHAPAQPQPQLQLQLQSHKGFLEQEGSPLSLGQSQHDLSQSAFLSWLSQTQSHSSLLSSSVLTPDSSPGKLDPAPSQPPEEPEPDEAESSPDPQALWFNISAQMPCNAAPTPPPAVSEDQPTPSPQQLASSKPMNRPSAANPCSPVQFSSTPLAGLAPKRRAGDPGEMPQSPTGLGQPKRRGRPPSKFFKQMEQRYLTQLTAQPVPPEMCSGWWWIRDPEMLDAMLKALHPRGIREKALHKHLNKHRDFLQEVCLRPSADPIFEPRQLPAFQEGIMSWSPKEKTYETDLAVLQWVEELEQRVIMSDLQIRGWTCPSPDSTREDLAYCEHLSDSQEDITWRGRGREGLAPQRKTTNPLDLAVMRLAALEQNVERRYLREPLWPTHEVVLEKALLSTPNGAPEGTTTEISYEITPRIRVWRQTLERCRSAAQVCLCLGQLERSIAWEKSVNKVTCLVCRKGDNDEFLLLCDGCDRGCHIYCHRPKMEAVPEGDWFCTVCLAQQVEGEFTQKPGFPKRGQKRKSGYSLNFSEGDGRRRRVLLRGRESPAAGPRYSEEGLSPSKRRRLSMRNHHSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRIIKNPMDFSTMRERLLRGGYTSSEEFAADALLVFDNCQTFNEDDSEVGKAGHIMRRFFESRWEEFYQGKQANL TT2MV0R TT Literature-reported TT6K8YG ID TT6K8YG TT6K8YG TN Bromodomain adjacent to zinc finger 2B (BAZ2B) TT6K8YG UP Q9UIF8 TT6K8YG UC BAZ2B_HUMAN TT6K8YG SN hWALp4; KIAA1476; Bromodomain adjacent to zinc finger domain protein 2B TT6K8YG GN BAZ2B TT6K8YG FC May play a role in transcriptional regulation interacting with ISWI. TT6K8YG PD 6FI1; 6FHQ; 6FH7; 6FH6; 6FGU TT6K8YG SQ MESGERLPSSAASSTTPTSSSTPSVASVVSKGGLSTGVASLSSTINPCGHLFRTAGDQPFNLSTVSSAFPMVSHPVFGLHSASSGHSEFGGLGTLGTPTALAAHPQLASFPGAEWWRTTDAHTRTGATFFPPLLGIPPLFAPPAQNHDSSSFHSRTSGKSNRNGPEKGVNGSINGSNTSSVIGINTSVLSTTASSSMGQTKSTSSGGGNRKCNQEQSKNQPLDARVDKIKDKKPRKKAMESSSNSDSDSGTSSDTSSEGISSSDSDDLEEDEEEEDQSIEESEDDDSDSESEAQHKSNNQVLLHGISDPKADGQKATEKAQEKRIHQPLPLASESQTHSFQSQQKQPQVLSQQLPFIFQSSQAKEESVNKHTSVIQSTGLVSNVKPLSLVNQAKKETYMKLIVPSPDVLKAGNKNTSEESSLLTSELRSKREQYKQAFPSQLKKQESSKSLKKVIAALSNPKATSSSPAHPKQTLENNHPNPFLTNALLGNHQPNGVIQSVIQEAPLALTTKTKMQSKINENIAAASSTPFSSPVNLSTSGRRTPGNQTPVMPSASPILHSQGKEKAVSNNVNPVKTQHHSHPAKSLVEQFRGTDSDIPSSKDSEDSNEDEEEDDEEEDEEDDEDDESDDSQSESDSNSESDTEGSEEEDDDDKDQDESDSDTEGEKTSMKLNKTTSSVKSPSMSLTGHSTPRNLHIAKAPGSAPAALCSESQSPAFLGTSSSTLTSSPHSGTSKRRRVTDERELRIPLEYGWQRETRIRNFGGRLQGEVAYYAPCGKKLRQYPEVIKYLSRNGIMDISRDNFSFSAKIRVGDFYEARDGPQGMQWCLLKEEDVIPRIRAMEGRRGRPPNPDRQRAREESRMRRRKGRPPNVGNAEFLDNADAKLLRKLQAQEIARQAAQIKLLRKLQKQEQARVAKEAKKQQAIMAAEEKRKQKEQIKIMKQQEKIKRIQQIRMEKELRAQQILEAKKKKKEEAANAKLLEAEKRIKEKEMRRQQAVLLKHQERERRRQHMMLMKAMEARKKAEEKERLKQEKRDEKRLNKERKLEQRRLELEMAKELKKPNEDMCLADQKPLPELPRIPGLVLSGSTFSDCLMVVQFLRNFGKVLGFDVNIDVPNLSVLQEGLLNIGDSMGEVQDLLVRLLSAAVCDPGLITGYKAKTALGEHLLNVGVNRDNVSEILQIFMEAHCGQTELTESLKTKAFQAHTPAQKASVLAFLINELACSKSVVSEIDKNIDYMSNLRRDKWVVEGKLRKLRIIHAKKTGKRDTSGGIDLGEEQHPLGTPTPGRKRRRKGGDSDYDDDDDDDSDDQGDEDDEDEEDKEDKKGKKTDICEDEDEGDQAASVEELEKQIEKLSKQQSQYRRKLFDASHSLRSVMFGQDRYRRRYWILPQCGGIFVEGMESGEGLEEIAKEREKLKKAESVQIKEEMFETSGDSLNCSNTDHCEQKEDLKEKDNTNLFLQKPGSFSKLSKLLEVAKMPPESEVMTPKPNAGANGCTLSYQNSGKHSLGSVQSTATQSNVEKADSNNLFNTGSSGPGKFYSPLPNDQLLKTLTEKNRQWFSLLPRTPCDDTSLTHADMSTASLVTPQSQPPSKSPSPTPAPLGSSAQNPVGLNPFALSPLQVKGGVSMMGLQFCGWPTGVVTSNIPFTSSVPSLGSGLGLSEGNGNSFLTSNVASSKSESPVPQNEKATSAQPAAVEVAKPVDFPSPKPIPEEMQFGWWRIIDPEDLKALLKVLHLRGIREKALQKQIQKHLDYITQACLKNKDVAIIELNENEENQVTRDIVENWSVEEQAMEMDLSVLQQVEDLERRVASASLQVKGWMCPEPASEREDLVYFEHKSFTKLCKEHDGEFTGEDESSAHALERKSDNPLDIAVTRLADLERNIERRIEEDIAPGLRVWRRALSEARSAAQVALCIQQLQKSIAWEKSIMKVYCQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPDGDWFCPACIAKASGQTLKIKKLHVKGKKTNESKKGKKVTLTGDTEDEDSASTSSSLKRGNKDLKKRKMEENTSINLSKQESFTSVKKPKRDDSKDLALCSMILTEMETHEDAWPFLLPVNLKLVPGYKKVIKKPMDFSTIREKLSSGQYPNLETFALDVRLVFDNCETFNEDDSDIGRAGHNMRKYFEKKWTDTFKVS TT6K8YG TT Literature-reported TTT46BN ID TTT46BN TTT46BN TN Bromodomain and PHD finger containing 1 (BRPF1) TTT46BN UP P55201 TTT46BN UC BRPF1_HUMAN TTT46BN SN Protein Br140; Peregrin; Bromodomain and PHD finger-containing protein 1; BR140 TTT46BN GN BRPF1 TTT46BN FC Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Preferentially mediates histone H3-K23 acetylation. Positively regulates the transcription of RUNX1 and RUNX2. TTT46BN PD 6EKQ; 5T4V; 5T4U; 5OWE; 5OWB TTT46BN SQ MGVDFDVKTFCHNLRATKPPYECPVETCRKVYKSYSGIEYHLYHYDHDNPPPPQQTPLRKHKKKGRQSRPANKQSPSPSEVSQSPGREVMSYAQAQRMVEVDLHGRVHRISIFDNLDVVSEDEEAPEEAPENGSNKENTETPAATPKSGKHKNKEKRKDSNHHHHHNVSASTTPKLPEVVYRELEQDTPDAPPRPTSYYRYIEKSAEELDEEVEYDMDEEDYIWLDIMNERRKTEGVSPIPQEIFEYLMDRLEKESYFESHNKGDPNALVDEDAVCCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRCLQSPSRAVDCALCPNKGGAFKQTDDGRWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQRGSGACIQCHKANCYTAFHVTCAQQAGLYMKMEPVRETGANGTSFSVRKTAYCDIHTPPGSARRLPALSHSEGEEDEDEEEDEGKGWSSEKVKKAKAKSRIKMKKARKILAEKRAAAPVVSVPCIPPHRLSKITNRLTIQRKSQFMQRLHSYWTLKRQSRNGVPLLRRLQTHLQSQRNCDQVGRDSEDKNWALKEQLKSWQRLRHDLERARLLVELIRKREKLKRETIKVQQIAMEMQLTPFLILLRKTLEQLQEKDTGNIFSEPVPLSEVPDYLDHIKKPMDFFTMKQNLEAYRYLNFDDFEEDFNLIVSNCLKYNAKDTIFYRAAVRLREQGGAVLRQARRQAEKMGIDFETGMHIPHSLAGDEATHHTEDAAEEERLVLLENQKHLPVEEQLKLLLERLDEVNASKQSVGRSRRAKMIKKEMTALRRKLAHQRETGRDGPERHGPSSRGSLTPHPAACDKDGQTDSAAEESSSQETSKGLGPNMSSTPAHEVGRRTSVLFSKKNPKTAGPPKRPGRPPKNRESQMTPSHGGSPVGPPQLPIMSSLRQRKRGRSPRPSSSSDSDSDKSTEDPPMDLPANGFSGGNQPVKKSFLVYRNDCSLPRSSSDSESSSSSSSSAASDRTSTTPSKQGRGKPSFSRGTFPEDSSEDTSGTENEAYSVGTGRGVGHSMVRKSLGRGAGWLSEDEDSPLDALDLVWAKCRGYPSYPALIIDPKMPREGMFHHGVPIPVPPLEVLKLGEQMTQEAREHLYLVLFFDNKRTWQWLPRTKLVPLGVNQDLDKEKMLEGRKSNIRKSVQIAYHRALQHRSKVQGEQSSETSDSD TTT46BN TT Literature-reported TT1CHFI ID TT1CHFI TT1CHFI TN Bromodomain and PHD finger containing 3 (BRPF3) TT1CHFI UP Q9ULD4 TT1CHFI UC BRPF3_HUMAN TT1CHFI SN KIAA1286; Bromodomain and PHD finger-containing protein 3 TT1CHFI GN BRPF3 TT1CHFI FC Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. TT1CHFI PD 3PFS TT1CHFI SQ MRKPRRKSRQNAEGRRSPSPYSLKCSPTRETLTYAQAQRIVEVDIDGRLHRISIYDPLKIITEDELTAQDITECNSNKENSEQPQFPGKSKKPSSKGKKKESCSKHASGTSFHLPQPSFRMVDSGIQPEAPPLPAAYYRYIEKPPEDLDAEVEYDMDEEDLAWLDMVNEKRRVDGHSLVSADTFELLVDRLEKESYLESRSSGAQQSLIDEDAFCCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPEGQWLCRCCLQSPSRPVDCILCPNKGGAFKQTSDGHWAHVVCAIWIPEVCFANTVFLEPIEGIDNIPPARWKLTCYICKQKGLGAAIQCHKVNCYTAFHVTCAQRAGLFMKIEPMRETSLNGTIFTVRKTAYCEAHSPPGAATARRKGDSPRSISETGDEEGLKEGDGEEEEEEEVEEEEQEAQGGVSGSLKGVPKKSKMSLKQKIKKEPEEAGQDTPSTLPMLAVPQIPSYRLNKICSGLSFQRKNQFMQRLHNYWLLKRQARNGVPLIRRLHSHLQSQRNAEQREQDEKTSAVKEELKYWQKLRHDLERARLLIELIRKREKLKREQVKVQQAAMELELMPFNVLLRTTLDLLQEKDPAHIFAEPVNLSEVPDYLEFISKPMDFSTMRRKLESHLYRTLEEFEEDFNLIVTNCMKYNAKDTIFHRAAVRLRDLGGAILRHARRQAENIGYDPERGTHLPESPKLEDFYRFSWEDVDNILIPENRAHLSPEVQLKELLEKLDLVSAMRSSGARTRRVRLLRREINALRQKLAQPPPPQPPSLNKTVSNGELPAGPQGDAAVLEQALQEEPEDDGDRDDSKLPPPPTLEPTGPAPSLSEQESPPEPPTLKPINDSKPPSRFLKPRKVEEDELLEKSPLQLGNEPLQRLLSDNGINRLSLMAPDTPAGTPLSGVGRRTSVLFKKAKNGVKLQRSPDRVLENGEDHGVAGSPASPASIEEERHSRKRPRSRSCSESEGERSPQQEEETGMTNGFGKHTESGSDSECSLGLSGGLAFEACSGLTPPKRSRGKPALSRVPFLEGVNGDSDYNGSGRSLLLPFEDRGDLEPLELVWAKCRGYPSYPALIIDPKMPREGLLHNGVPIPVPPLDVLKLGEQKQAEAGEKLFLVLFFDNKRTWQWLPRDKVLPLGVEDTVDKLKMLEGRKTSIRKSVQVAYDRAMIHLSRVRGPHSFVTSSYL TT1CHFI TT Literature-reported TT3EUH1 ID TT3EUH1 TT3EUH1 TN Burkholderia Glutamate racemase (BURCJ murI) TT3EUH1 UP B4EEM8 TT3EUH1 UC B4EEM8_BURCJ TT3EUH1 SN Glutamate racemase TT3EUH1 GN BURCJ murI TT3EUH1 FC Provides the (R)-glutamate required for cell wall biosynthesis. TT3EUH1 EC EC 5.1.1.3 TT3EUH1 SQ MTNPSDATALRAAAPVGIFDSGLGGLSVLRAARAHLPDESFVYVADSHHAPYGPRDEAFITERTLAIGEWLAREGAKALVIACNTATARAIAAIRERLSIPLVGVEPGIKPAAALSATGVAGVLATQSTLNSPRFQALLDRYGAGRRFICQPGHGLVEAIERGDTNSPALRALLERYIQPMLDDGADTLVLGCTHYPFFTETIRDLVGERLTIVDTSDAIARQLARVLDERGLRAPAGTHAAPPRFCSTSDGLQLRALASTLLGLDAPVESVTISSPNARACATA TT3EUH1 TT Literature-reported TTBGWN3 ID TTBGWN3 TTBGWN3 TN Butyrophilin-like protein 3 (BTNL3) TTBGWN3 UP Q6UXE8 TTBGWN3 UC BTNL3_HUMAN TTBGWN3 BC Immunoglobulin TTBGWN3 SN UNQ744/PRO1472; COLF4100; Butyrophilin-like receptor; BTNLR TTBGWN3 GN BTNL3 TTBGWN3 FC Regulate the homing and maturation of V7+ and V4+ T cells to the gut epithelium. TTBGWN3 SQ MAFVLILVLSFYELVSGQWQVTGPGKFVQALVGEDAVFSCSLFPETSAEAMEVRFFRNQFHAVVHLYRDGEDWESKQMPQYRGRTEFVKDSIAGGRVSLRLKNITPSDIGLYGCWFSSQIYDEEATWELRVAALGSLPLISIVGYVDGGIQLLCLSSGWFPQPTAKWKGPQGQDLSSDSRANADGYSLYDVEISIIVQENAGSILCSIHLAEQSHEVESKVLIGETFFQPSPWRLASILLGLLCGALCGVVMGMIIVFFKSKGKIQAELDWRRKHGQAELRDARKHAVEVTLDPETAHPKLCVSDLKTVTHRKAPQEVPHSEKRFTRKSVVASQGFQAGKHYWEVDVGQNVGWYVGVCRDDVDRGKNNVTLSPNNGYWVLRLTTEHLYFTFNPHFISLPPSTPPTRVGVFLDYEGGTISFFNTNDQSLIYTLLTCQFEGLLRPYIQHAMYDEEKGTPIFICPVSWG TTBGWN3 TT Literature-reported TTUZ7OA ID TTUZ7OA TTUZ7OA TN Calreticulin (CALR) TTUZ7OA UP P27797 TTUZ7OA UC CALR_HUMAN TTUZ7OA SN grp60; HACBP; Endoplasmic reticulum resident protein 60; ERp60; ERC; Calregulin; CRTC; CRP55 TTUZ7OA GN CALR TTUZ7OA FC Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). TTUZ7OA PD 6ENY; 5V90; 5LK5; 3POW; 3POS TTUZ7OA SQ MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL TTUZ7OA TT Literature-reported TTGFLXM ID TTGFLXM TTGFLXM TN Campylobacter Flavodoxin:quinone reductase (CAMJU FqrB) TTGFLXM UP A0A0M4UFG9 TTGFLXM UC A0A0M4UFG9_CAMJU TTGFLXM BC Iron-sulfur protein donor oxidoreductase TTGFLXM SN NADPH oxidoreductase, putative flavodoxin quinone reductase FqrB TTGFLXM GN CAMJU FqrB TTGFLXM FC Exhibited NADPH quinone reductase activity with menadione or benzoquinone. Reduced flavodoxin (FldA), the electron carrier of PFOR. TTGFLXM SQ MKKIDLIVVGAGPTGIGCAVEAKLKNKEVLILEKSNNICQTLMQFYKDGKRVDKAYKGCEGTNHGHVPFEDGTKESTIETFQNALKEHNIEVEFGSEVESVKNENGVFLVSTAKGVYGCKNIIVAIGRMGKPNKPDYKLPMTLTKIINFNANSVLGNEKILVVGGGNSAAEYAVDLANSNQVSLCYRKKEFTRLNDINLKDIHEAGNSGEVELKLGIDINEVEDDNGKAKVNFTDGTSDIYDRIIYAIGGSTPLDFLQKCGINVDDKGVPLMDENKQSNVKGIFVAGDITTKNGASIVTGLNDAVKILSVL TTGFLXM TT Literature-reported TTCNGJ5 ID TTCNGJ5 TTCNGJ5 TN Candida Elongation factor 2 (Candi EFT2) TTCNGJ5 UP Q5A0M4 TTCNGJ5 UC EF2_CANAL TTCNGJ5 BC Acid anhydrides hydrolase TTCNGJ5 SN EFT2; EF2 TTCNGJ5 GN Candi EFT2 TTCNGJ5 FC Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. TTCNGJ5 SQ MVAFTIEQIRGLMDKVTNVRNMSVIAHVDHGKSTLSDSLVQKAGIISAAKAGDARFMDTRKDEQERGITIKSTAISLYASMTDEDVKDIKQKTDGNSFLVNLIDSPGHVDFSSEVTAALRVTDGALVVVDTVEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQTTKEDLYQTFARTVESVNVIISTYCDPVLGDVQVYPQKGTVAFASGLHGWAFTVRQFANKYSKKFGVDKEKMMERLWGDSYFNPKTKKWTNKDKDADGKPLERAFNMFILDPIFRLFAAIMNFKKDEIPVLLEKLEIQLKGDEKDLEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAETLYEGPSDDPFCTAIRNCDPNADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYQVGKKEDLFLKSIQRTVLMMGRSVEQIDDCPAGNIIGLVGIDQFLLKSGTITTNEAAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEICLQDLENDHAGVPLRISPPVVSYRETVEGESSMVALSKSPNKHNRIYVKAQPIDEEVSLDIENGVINPRDDFKARARILADKHGWDVVDARKIWCFGPDGNGPNLVVDQTKAVQYLNEIKDSVVAAFQWATKEGPIFGENCRSVRVNILDVTLHADAIHRGGGQIIPTMRRVTYASMLLAEPAIQEPVFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGTPLFTVKAYLPVNESFGFTGELRQATGGQAFPQLIFDHWQVMSGDVTDENSKPGAIVKEKRVRAGLKPEVPEYTEYYDKL TTCNGJ5 TT Literature-reported TTIV0HD ID TTIV0HD TTIV0HD TN Candida Elongation factor 3 (Candi TEF3) TTIV0HD UP O93796 TTIV0HD UC EF3_CANGA TTIV0HD BC ABC transporter TTIV0HD SN TEF3; EF-3 TTIV0HD GN Candi TEF3 TTIV0HD FC The main role of EF-3 may be to transduce nucleoside triphosphate energy into mechanical energy for translocation during translation. EF-3 stimulates EF-1-alpha-dependent binding of aminoacyl-tRNA to the ribosome. TTIV0HD SQ MTDSDQSLKVLEELFKNLSVATADNRVEAAQEVASFLNGNIIEHDIPEKFFEELAKAVKDKKTSANFLEAVAHIANEANLSPSVEPFVITLVPEICAKAGDKDKDVQAVASKTLVAISKAINPVAIKAYLPHLTKSLETTNKWQEKVSVLAAISALVDAAKEQVALRMPELIPVLSETMWDTKKEVKEAATATMTKATETVDNKDIERFIPQLISCIADPKQVPETVHLLGATTFVAEVTPATLSIMVPLLSRGLAERETSIKRKAAVIIDNMCKLVEDPQVVAPFLDKLLPGLKNNYATIADPEAREVTLRGLKTLRRVGNVTEDDVLPEISHAGDIETTLGVINELLKGENVAPRFKIVVEYIAAMAGDLIDERVIDQQAWFTHITPYMTIFMHERNAKDVLDEFRKRAVDNIPVGPNFDDEEDEGEDLCNCEFSLAYGAKILLNKTQLRLKRGRRYGLCGPNGAGKSTLMRAIANGQVDGFPTPEECMTVYVEHDIDGTHADTSVLDFVVSSEVGTKEAITAKLVEFGFTEEMINMPISSLSGGWKMKLALARAVLKNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSVIVSHDSGFLDNVCQYIIHYEGLKLRKYKGNLSEFVKKCPTAQSYYELGASDLEFKFPEPGYLEGVKTKQKAIVKVSNMTFQYPGTSKPQISDISFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHAFAHIESHLDKTPSEYIQWRFQTGEDRETMDRANRQINENDAEAMNKIFKIEGTPRRIAGIHARRKFKNTYEYECSFLLGENIGMKSERWVPMMSVDNAWIPRGELVESHSKMVAEVDMKEALASGQFRPLTRKEIEEHCAMLGLDAELVSHSRIRGLSGGQKVKLVLAACSWQRPHLIVLDEPTNYLDRDSLGALSKALKAFEGGVIIITHSAEFTKNLTEEVWAVKDGKMTPSGHNWVSGQGAGPRIEKKEDEEDKFDAMGNKIAGGKKKKKLSSAELRKKKKERMKKKKELGDAYVSSDDEDF TTIV0HD TT Literature-reported TTRIFQ7 ID TTRIFQ7 TTRIFQ7 TN Candida Histidine kinase (Candi chik1) TTRIFQ7 UP O74271 TTRIFQ7 UC O74271_CANAX TTRIFQ7 BC Kinase TTRIFQ7 SN Histidine kinase TTRIFQ7 GN Candi chik1 TTRIFQ7 FC Catalyses the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. TTRIFQ7 SQ MNPTKKPRLSPMQPSVFEILNDPELYSQHCHSLRETLLDHFNHQATLIDTYEHELEKSKNANKAFQQALSEIGTVVISVAMGDLSKKVEIHTVENDPEILKVKITINTMMDQLQTFANEVTKVATEVANGELGGQAKNDGSVGIWRSLTDNVNIMALNLTNQVREIADVTRAVAKGDLSRKINVHAQGEILQLQRTINTMVDQLRTFAFEVSKVARDVGVLGILGGQALIENVEGIWEELTDNVNAMALNLTTQVRNIANVTTAVAKGDLSKKVTADCKGEILDLKLTINQMVDRLQNFALAVTTLSREVGTLGIWGGQANVQDVEGAWKQVTENVNLMATNLTNQVRSIATVTTAVAHGDLSQKIDVHAQGEILQLKNTINKMVDSLQLFASEVSKVAQDVGINGKLGIQAQVSDVDGLWKEITSNVNTMASNLTSQVRAFAQITAAATDGDFTRFITVEASGEMDALKTKINQMVFNLRESLQRNTAAREAAELANSAKSEFLANMSHEIRTPLNGIIGMTQLSLDTELTQYQREMLSIVHNLANSLLTIIDDILDISKIEANRMTVEQIDFSLRGTVFGALKTLAVKAIEKNLDLTYQCDSSFPDNLIGDSFRLRQVILNLAGNAIKFTKEGKVSVSVKKSDKMVLDSKLLLEVCVSDTGIGIEKDKLGLIFDTFCQADGSTTRKFGGTGLGLSISKQLIHLMGGEIWVTSEYGSGSNFYFTVCVSPSNIRYTRQTEQLLPFSSHYVLFVSTEHTQEELDVLRDGIIELGLIPIIVRNIEDATLTEPVKYDIIMIDSIEIAKKLRLLSEVKYIPLVLVHHSIPQLNMRVCIDLGISSYANTPCSITDLASAIIPALESRSISQNSDESVRYKILLAEDNLVNQKLAVRILEKQGHSVEVVENGLEAYEAIKRNKYDVVLMDVQMPVMGGFEATEKIRQWEKKSNPIDSLTFRTPIIALTAHAMLGDREKSLAKGMDDYVSKPLKPKLLMQTINKCIHNINQLKELSRNSRGSDFAKKMTRNTPGSTTRQGSDEGSVEDMIGDTPRQGSVEGGGTSSRPVQRRSATEGSITTISEQIDR TTRIFQ7 TT Literature-reported TTFK7E1 ID TTFK7E1 TTFK7E1 TN Carbohydrate sulfotransferase 15 (CHST15) TTFK7E1 UP Q7LFX5 TTFK7E1 UC CHSTF_HUMAN TTFK7E1 SN hBRAG; N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase; KIAA0598; GalNAc4S-6ST; GALNAC4S6ST; BRAG; B-cell RAG-associated gene protein TTFK7E1 GN CHST15 TTFK7E1 FC Sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo. TTFK7E1 EC EC 2.8.2.33 TTFK7E1 SQ MRHCINCCIQLLPDGAHKQQVNCQGGPHHGHQACPTCKGENKILFRVDSKQMNLLAVLEVRTEGNENWGGFLRFKKGKRCSLVFGLIIMTLVMASYILSGAHQELLISSPFHYGGFPSNPSLMDSENPSDTKEHHHQSSVNNISYMKDYPSIKLIINSITTRIEFTTRQLPDLEDLKKQELHMFSVIPNKFLPNSKSPCWYEEFSGQNTTDPYLTNSYVLYSKRFRSTFDALRKAFWGHLAHAHGKHFRLRCLPHFYIIGQPKCGTTDLYDRLRLHPEVKFSAIKEPHWWTRKRFGIVRLRDGLRDRYPVEDYLDLFDLAAHQIHQGLQASSAKEQSKMNTIIIGEASASTMWDNNAWTFFYDNSTDGEPPFLTQDFIHAFQPNARLIVMLRDPVERLYSDYLYFASSNKSADDFHEKVTEALQLFENCMLDYSLRACVYNNTLNNAMPVRLQVGLYAVYLLDWLSVFDKQQFLILRLEDHASNVKYTMHKVFQFLNLGPLSEKQEALMTKSPASNARRPEDRNLGPMWPITQKILRDFYRPFNARLAQVLADEAFAWKTT TTFK7E1 TT Literature-reported TTMCVJF ID TTMCVJF TTMCVJF TN Cardiac phospholamban (PLN) TTMCVJF UP P26678 TTMCVJF UC PPLA_HUMAN TTMCVJF SN Phospholamban; PLN; PLB TTMCVJF GN PLN TTMCVJF FC Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulatescalcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation. TTMCVJF PD 2HYN; 1ZLL; 1PSL; 1PLP; 1PLN TTMCVJF SQ MEKVQYLTRSAIRRASTIEMPQQARQKLQNLFINFCLILICLLLICIIVMLL TTMCVJF TT Literature-reported TTWZC78 ID TTWZC78 TTWZC78 TN Caterpiller protein 16.1 (NLRC5) TTWZC78 UP Q86WI3 TTWZC78 UC NLRC5_HUMAN TTWZC78 BC NLRP family TTWZC78 SN Nucleotide-binding oligomerization domain protein 4; Nucleotide-binding oligomerization domain protein 27; NOD4; NOD27; CLR16.1 TTWZC78 GN NLRC5 TTWZC78 FC Probable regulator of the NF-kappa-B and type I interferon signaling pathways. May also regulate the type II interferon signaling pathway. Plays a role in homeostatic control of innate immunity and in antiviral defense mechanisms. TTWZC78 SQ MDPVGLQLGNKNLWSCLVRLLTKDPEWLNAKMKFFLPNTDLDSRNETLDPEQRVILQLNKLHVQGSDTWQSFIHCVCMQLEVPLDLEVLLLSTFGYDDGFTSQLGAEGKSQPESQLHHGLKRPHQSCGSSPRRKQCKKQQLELAKKYLQLLRTSAQQRYRSQIPGSGQPHAFHQVYVPPILRRATASLDTPEGAIMGDVKVEDGADVSISDLFNTRVNKGPRVTVLLGKAGMGKTTLAHRLCQKWAEGHLNCFQALFLFEFRQLNLITRFLTPSELLFDLYLSPESDHDTVFQYLEKNADQVLLIFDGLDEALQPMGPDGPGPVLTLFSHLCNGTLLPGCRVMATSRPGKLPACLPAEAAMVHMLGFDGPRVEEYVNHFFSAQPSREGALVELQTNGRLRSLCAVPALCQVACLCLHHLLPDHAPGQSVALLPNMTQLYMQMVLALSPPGHLPTSSLLDLGEVALRGLETGKVIFYAKDIAPPLIAFGATHSLLTSFCVCTGPGHQQTGYAFTHLSLQEFLAALHLMASPKVNKDTLTQYVTLHSRWVQRTKARLGLSDHLPTFLAGLASCTCRPFLSHLAQGNEDCVGAKQAAVVQVLKKLATRKLTGPKVVELCHCVDETQEPELASLTAQSLPYQLPFHNFPLTCTDLATLTNILEHREAPIHLDFDGCPLEPHCPEALVGCGQIENLSFKSRKCGDAFAEALSRSLPTMGRLQMLGLAGSKITARGISHLVKALPLCPQLKEVSFRDNQLSDQVVLNIVEVLPHLPRLRKLDLSSNSICVSTLLCLARVAVTCPTVRMLQAREADLIFLLSPPTETTAELQRAPDLQESDGQRKGAQSRSLTLRLQKCQLQVHDAEALIALLQEGPHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDLSNNGLSVAGVHCVLRAVSACWTLAELHISLQHKTVIFMFAQEPEEQKGPQERAAFLDSLMLQMPSELPLSSRRMRLTHCGLQEKHLEQLCKALGGSCHLGHLHLDFSGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAVLGLVRCFSTLQWLFRLDISFESQHILLRGDKTSRDMWATGSLPDFPAAAKFLGFRQRCIPRSLCLSECPLEPPSLTRLCATLKDCPGPLELQLSCEFLSDQSLETLLDCLPQLPQLSLLQLSQTGLSPKSPFLLANTLSLCPRVKKVDLRSLHHATLHFRSNEEEEGVCCGRFTGCSLSQEHVESLCWLLSKCKDLSQVDLSANLLGDSGLRCLLECLPQVPISGLLDLSHNSISQESALYLLETLPSCPRVREASVNLGSEQSFRIHFSREDQAGKTLRLSECSFRPEHVSRLATGLSKSLQLTELTLTQCCLGQKQLAILLSLVGRPAGLFSLRVQEPWADRARVLSLLEVCAQASGSVTEISISETQQQLCVQLEFPRQEENPEAVALRLAHCDLGAHHSLLVGQLMETCARLQQLSLSQVNLCEDDDASSLLLQSLLLSLSELKTFRLTSSCVSTEGLAHLASGLGHCHHLEELDLSNNQFDEEGTKALMRALEGKWMLKRLDLSHLLLNSSTLALLTHRLSQMTCLQSLRLNRNSIGDVGCCHLSEALRAATSLEELDLSHNQIGDAGVQHLATILPGLPELRKIDLSGNSISSAGGVQLAESLVLCRRLEELMLGCNALGDPTALGLAQELPQHLRVLHLPFSHLGPGGALSLAQALDGSPHLEEISLAENNLAGGVLRFCMELPLLRQIDLVSCKIDNQTAKLLTSSFTSCPALEVILLSWNLLGDEAAAELAQVLPQMGRLKRVDLEKNQITALGAWLLAEGLAQGSSIQVIRLWNNPIPCDMAQHLKSQEPRLDFAFFDNQPQAPWGT TTWZC78 TT Literature-reported TTXUBN2 ID TTXUBN2 TTXUBN2 TN Caveolin 1 (CAV1) TTXUBN2 UP Q03135 TTXUBN2 UC CAV1_HUMAN TTXUBN2 BC Caveolin protein TTXUBN2 SN Caveolin1; Caveolin-1; Cav-1 TTXUBN2 GN CAV1 TTXUBN2 FC Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation. May act as a scaffolding protein within caveolar membranes. TTXUBN2 SQ MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADELSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINLQKEI TTXUBN2 TT Literature-reported TTXUBN2 FM Caveolin family TT2GIDQ ID TT2GIDQ TT2GIDQ TN C-C chemokine receptor type 7 (CCR7) TT2GIDQ UP P32248 TT2GIDQ UC CCR7_HUMAN TT2GIDQ BC GPCR rhodopsin TT2GIDQ SN MIP3 beta receptor; MIP-3 beta receptor; EpsteinBarr virusinduced Gprotein coupled receptor 1; Epstein-Barr virus-induced G-protein coupled receptor 1; EVI1; EBVinduced Gprotein coupled receptor 1; EBV-induced G-protein coupled receptor 1; EBI1; CMKBR7; CDw197; CD197; CCR-7; CCCKR7; CC-CKR-7; CC chemokine receptor type 7; CC CKR7; C-C CKR-7; BLR2 TT2GIDQ GN CCR7 TT2GIDQ FC Probable mediator of EBV effects on B-lymphocytes or of normal lymphocyte functions. Receptor for the MIP-3-beta chemokine. TT2GIDQ SQ MDLGKPMKSVLVVALLVIFQVCLCQDEVTDDYIGDNTTVDYTLFESLCSKKDVRNFKAWFLPIMYSIICFVGLLGNGLVVLTYIYFKRLKTMTDTYLLNLAVADILFLLTLPFWAYSAAKSWVFGVHFCKLIFAIYKMSFFSGMLLLLCISIDRYVAIVQAVSAHRHRARVLLISKLSCVGIWILATVLSIPELLYSDLQRSSSEQAMRCSLITEHVEAFITIQVAQMVIGFLVPLLAMSFCYLVIIRTLLQARNFERNKAIKVIIAVVVVFIVFQLPYNGVVLAQTVANFNITSSTCELSKQLNIAYDVTYSLACVRCCVNPFLYAFIGVKFRNDLFKLFKDLGCLSQEQLRQWSSCRHIRRSSMSVEAETTTTFSP TT2GIDQ TT Clinical trial TT8QVJO ID TT8QVJO TT8QVJO TN CCCH tandem zinc finger protein ZFP36L1 (ERF-1) TT8QVJO UP Q07352 TT8QVJO UC TISB_HUMAN TT8QVJO SN mRNA decay activator protein ZFP36L1; Zinc finger protein 36, C3H1 type-like 1; ZFP36-like 1; TPA-induced sequence 11b; ERF-1; EGF-response factor 1; Butyrate response factor 1; BERG36 TT8QVJO GN ZFP36L1 TT8QVJO FC Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis. Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery. Functions by recruiting the CCR4-NOT deadenylase complex and components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes. Induces also the degradation of ARE-containing mRNAs even in absence of poly(A) tail (By similarity). Binds to 3'-UTR ARE of numerous mRNAs. Positively regulates early adipogenesis by promoting ARE-mediated mRNA decay of immediate early genes (IEGs) (By similarity). Promotes ARE-mediated mRNA decay of mineralocorticoid receptor NR3C2 mRNA in response to hypertonic stress. Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA. Positively regulates monocyte/macrophage cell differentiation by promoting ARE-mediated mRNA decay of the cyclin-dependent kinase CDK6 mRNA. Promotes degradation of ARE-containing pluripotency-associated mRNAs in embryonic stem cells (ESCs), such as NANOG, through a fibroblast growth factor (FGF)-induced MAPK-dependent signaling pathway, and hence attenuates ESC self-renewal and positively regulates mesendoderm differentiation (By similarity). May play a role in mediating pro-apoptotic effects in malignant B-cells by promoting ARE-mediated mRNA decay of BCL2 mRNA. In association with ZFP36L2 maintains quiescence on developing B lymphocytes by promoting ARE-mediated decay of several mRNAs encoding cell cycle regulators that help B cells progress through the cell cycle, and hence ensuring accurate variable-diversity-joining (VDJ) recombination and functional immune cell formation (By similarity). Together with ZFP36L2 is also necessary for thymocyte development and prevention of T-cell acute lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated mRNA decay of the oncogenic transcription factor NOTCH1 mRNA (By similarity). Participates in the delivery of target ARE-mRNAs to processing bodies (PBs). In addition to its cytosolic mRNA-decay function, plays a role in the regulation of nuclear mRNA 3'-end processing; modulates mRNA 3'-end maturation efficiency of the DLL4 mRNA through binding with an ARE embedded in a weak noncanonical polyadenylation (poly(A)) signal in endothelial cells. Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion. Plays a role in vasculogenesis and endocardial development (By similarity). Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis. Plays a role in myoblast cell differentiation (By similarity). TT8QVJO PD 1W0W; 1W0V TT8QVJO SQ MTTTLVSATIFDLSEVLCKGNKMLNYSAPSAGGCLLDRKAVGTPAGGGFPRRHSVTLPSSKFHQNQLLSSLKGEPAPALSSRDSRFRDRSFSEGGERLLPTQKQPGGGQVNSSRYKTELCRPFEENGACKYGDKCQFAHGIHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRALAGARDLSADRPRLQHSFSFAGFPSAAATAAATGLLDSPTSITPPPILSADDLLGSPTLPDGTNNPFAFSSQELASLFAPSMGLPGGGSPTTFLFRPMSESPHMFDSPPSPQDSLSDQEGYLSSSSSSHSGSDSPTLDNSRRLPIFSRLSISDD TT8QVJO TT Literature-reported TTLGFVW ID TTLGFVW TTLGFVW TN CDK inhibitor 1B p27Kip1 (CDKN1B) TTLGFVW UP P46527 TTLGFVW UC CDN1B_HUMAN TTLGFVW SN p27Kip1; KIP1; Cyclindependent kinase inhibitor p27; Cyclin-dependent kinase inhibitor p27; Cyclin-dependent kinase inhibitor 1B TTLGFVW GN CDKN1B TTLGFVW FC Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry. Important regulator of cell cycle progression. TTLGFVW PD 6ATH; 5UQ3; 2AST; 1JSU; 1H27 TTLGFVW SQ MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT TTLGFVW TT Literature-reported TTBRUGA ID TTBRUGA TTBRUGA TN CDK inhibitor 4C p18-INK4c (CDKN2C) TTBRUGA UP P42773 TTBRUGA UC CDN2C_HUMAN TTBRUGA SN P18-INK6; P18-INK4c; P18(INK4c) protein; P18(INK4c); P18 INK4c protein; Cyclin-dependent kinase 6 inhibitor; Cyclin-dependent kinase 4 inhibitor C TTBRUGA GN CDKN2C TTBRUGA FC Inhibits cell growth and proliferation with a correlated dependence on endogenous retinoblastoma protein RB. Interacts strongly with CDK6, weakly with CDK4. TTBRUGA PD 1MX6; 1MX4; 1MX2; 1IHB; 1G3N TTBRUGA SQ MAEPWGNELASAAARGDLEQLTSLLQNNVNVNAQNGFGRTALQVMKLGNPEIARRLLLRGANPDLKDRTGFAVIHDAARAGFLDTLQTLLEFQADVNIEDNEGNLPLHLAAKEGHLRVVEFLVKHTASNVGHRNHKGDTACDLARLYGRNEVVSLMQANGAGGATNLQ TTBRUGA TT Literature-reported TTBYM6V ID TTBYM6V TTBYM6V TN CDK5 activator 1 (CDK5R1) TTBYM6V UP Q15078 TTBYM6V UC CD5R1_HUMAN TTBYM6V SN TPKII regulatory subunit; NCK5A; Cyclindependent kinase 5 regulatory subunit 1; Cyclindependent kinase 5 activator 1, p25; Cyclindependent kinase 5 activator 1; Cyclin-dependent kinase 5 regulatory subunit 1; Cyclin-dependent kinase 5 activator 1; CDK5R TTBYM6V GN CDK5R1 TTBYM6V FC The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. p35 is a neuron specific activator of CDK5. TTBYM6V PD 3O0G; 1UNL; 1UNH; 1UNG; 1H4L TTBYM6V SQ MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKVQPNSSYQNNITHLNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGGSSSVKKAPHPAVTSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR TTBYM6V TT Literature-reported TTBYM6V FM Cyclin-dependent kinase 5 activator TTPK79J ID TTPK79J TTPK79J TN Cellular communication network factor 1 (CCN1) TTPK79J UP O00622 TTPK79J UC CCN1_HUMAN TTPK79J SN Protein GIG1; Protein CYR61; Insulin-like growth factor-binding protein 10; IGFBP10; IGFBP-10; IGF-binding protein 10; IBP-10; GIG1; CYR61; CCN family member 1 TTPK79J GN CCN1 TTPK79J FC Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5. CCN1-mediated gene regulation is dependent on heparin-binding. Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1. Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-v/beta-5 and cell proliferation through integrin alpha-v/beta-3. TTPK79J PD 4D11; 4D0Z TTPK79J SQ MSSRIARALALVVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVTGQCCEEWVCDEDSIKDPMEDQDGLLGKELGFDASEVELTRNNELIAVGKGSSLKRLPVFGMEPRILYNPLQGQKCIVQTTSWSQCSKTCGTGISTRVTNDNPECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCLSVKKYRPKYCGSCVDGRCCTPQLTRTVKMRFRCEDGETFSKNVMMIQSCKCNYNCPHANEAAFPFYRLFNDIHKFRD TTPK79J TT Literature-reported TT6XY5F ID TT6XY5F TT6XY5F TN Cellular communication network factor 6 (CCN6) TT6XY5F UP O95389 TT6XY5F UC WISP3_HUMAN TT6XY5F BC Growth factor TT6XY5F SN WNT1 inducible signaling pathway protein 3; WISP3; WISP-3; UNQ462/PRO790 TT6XY5F GN WISP3 TT6XY5F FC Appears to be required for normal postnatal skeletal growth and cartilage homeostasis. TT6XY5F SQ MQGLLFSTLLLAGLAQFCCRVQGTGPLDTTPEGRPGEVSDAPQRKQFCHWPCKCPQQKPRCPPGVSLVRDGCGCCKICAKQPGEICNEADLCDPHKGLYCDYSVDRPRYETGVCAYLVAVGCEFNQVHYHNGQVFQPNPLFSCLCVSGAIGCTPLFIPKLAGSHCSGAKGGKKSDQSNCSLEPLLQQLSTSYKTMPAYRNLPLIWKKKCLVQATKWTPCSRTCGMGISNRVTNENSNCEMRKEKRLCYIQPCDSNILKTIKIPKGKTCQPTFQLSKAEKFVFSGCSSTQSYKPTFCGICLDKRCCIPNKSKMITIQFDCPNEGSFKWKMLWITSCVCQRNCREPGDIFSELKIL TT6XY5F TT Literature-reported TT9XRNV ID TT9XRNV TT9XRNV TN Ceramide kinase (CERK) TT9XRNV UP Q8TCT0 TT9XRNV UC CERK1_HUMAN TT9XRNV SN hCERK; Lipid kinase 4; LK4; KIAA1646; Acylsphingosine kinase TT9XRNV GN CERK TT9XRNV FC Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. Acts efficiently on natural and analog ceramides (C6, C8, C16 ceramides, and C8-dihydroceramide), to a lesser extent on C2-ceramide and C6-dihydroceramide, but not on other lipids, such as various sphingosines. Shows a greater preference for D-erythro isomer of ceramides. Binds phosphoinositides. TT9XRNV EC EC 2.7.1.138 TT9XRNV SQ MGATGAAEPLQSVLWVKQQRCAVSLEPARALLRWWRSPGPGAGAPGADACSVPVSEIIAVEETDVHGKHQGSGKWQKMEKPYAFTVHCVKRARRHRWKWAQVTFWCPEEQLCHLWLQTLREMLEKLTSRPKHLLVFINPFGGKGQGKRIYERKVAPLFTLASITTDIIVTEHANQAKETLYEINIDKYDGIVCVGGDGMFSEVLHGLIGRTQRSAGVDQNHPRAVLVPSSLRIGIIPAGSTDCVCYSTVGTSDAETSALHIVVGDSLAMDVSSVHHNSTLLRYSVSLLGYGFYGDIIKDSEKKRWLGLARYDFSGLKTFLSHHCYEGTVSFLPAQHTVGSPRDRKPCRAGCFVCRQSKQQLEEEQKKALYGLEAAEDVEEWQVVCGKFLAINATNMSCACRRSPRGLSPAAHLGDGSSDLILIRKCSRFNFLRFLIRHTNQQDQFDFTFVEVYRVKKFQFTSKHMEDEDSDLKEGGKKRFGHICSSHPSCCCTVSNSSWNCDGEVLHSPAIEVRVHCQLVRLFARGIEENPKPDSHS TT9XRNV TT Literature-reported TT09EZF ID TT09EZF TT09EZF TN Charged multivesicular body protein 4B (CHMP4B) TT09EZF UP Q9H444 TT09EZF UC CHM4B_HUMAN TT09EZF SN hVps322; hVps32-2; hSnf72; hSnf7-2; Vps322; Vps32-2; Vacuolar protein sortingassociated protein 322; Vacuolar protein sorting-associated protein 32-2; SNF72; SNF7-2; SNF7 homolog associated with Alix 1; SHAX1; Chromatinmodifying protein 4b; Chromatin-modifying protein 4b; CHMP4b; C20orf178 TT09EZF GN CHMP4B TT09EZF FC MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan. Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. TT09EZF PD 5MK2; 4ABM; 3UM3; 3C3Q TT09EZF SQ MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSIALPSKPAKKKEEEDDDMKELENWAGSM TT09EZF TT Literature-reported TT8XNZ7 ID TT8XNZ7 TT8XNZ7 TN Chloride channel protein 3 (CLC-3) TT8XNZ7 UP P51790 TT8XNZ7 UC CLCN3_HUMAN TT8XNZ7 BC Chloride channel TT8XNZ7 SN H(+)/Cl(-) exchange transporter 3; ClC-3 TT8XNZ7 GN CLCN3 TT8XNZ7 FC Functions as antiporter and contributes to the acidification of the endosome and synaptic vesicle lumen, and may thereby affect vesicle trafficking and exocytosis. May play an important role in neuronal cell function through regulation of membrane excitability by protein kinase C. It could help neuronal cells to establish short-term memory. Mediates the exchange of chloride ions against protons. TT8XNZ7 SQ MESEQLFHRGYYRNSYNSITSASSDEELLDGAGVIMDFQTSEDDNLLDGDTAVGTHYTMTNGGSINSSTHLLDLLDEPIPGVGTYDDFHTIDWVREKCKDRERHRRINSKKKESAWEMTKSLYDAWSGWLVVTLTGLASGALAGLIDIAADWMTDLKEGICLSALWYNHEQCCWGSNETTFEERDKCPQWKTWAELIIGQAEGPGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDCGPLESSSLCDYRNDMNASKIVDDIPDRPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDWFIFKEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNGYPFLDAKEEFTHTTLAADVMRPRRNDPPLAVLTQDNMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESARKKQEGIVGSSRVCFAQHTPSLPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQTANQDPASIMFN TT8XNZ7 TT Literature-reported TTCJRDO ID TTCJRDO TTCJRDO TN Chloride channel protein 6 (ClC-6) TTCJRDO UP P51797 TTCJRDO UC CLCN6_HUMAN TTCJRDO BC Chloride channel TTCJRDO SN KIAA0046; ClC-6; Chloride transport protein 6 TTCJRDO GN CLCN6 TTCJRDO FC Chloride transport protein, initially identified as voltage-gated chloride channel. The presence of the conserved gating glutamate residues suggests that is functions as antiporter. TTCJRDO SQ MAGCRGSLCCCCRWCCCCGERETRTPEELTILGETQEEEDEILPRKDYESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFFVRLFTQLKFGVVQTSVEECSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPEVKCYLNGVKVPGIVRLRTLLCKVLGVLFSVAGGLFVEKEGPMIHSGSVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCSDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHPKPKLVRVLESLLVSLVTTVVVFVASMVLGECRQMSSSSQIGNDSFQLQVTEDVNSSIKTFFCPNDTYNDMATLFFNPQESAILQLFHQDGTFSPVTLALFFVLYFLLACWTYGISVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHIYSGTFALIGAAAFLGGVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDFFNKGIYDIHVGLRGVPLLEWETEVEMDKLRASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNEKEFMKGNQLISNNIKFKKSSILTRAGEQRKRSQSMKSYPSSELRNMCDEHIASEEPAEKEDLLQQMLERRYTPYPNLYPDQSPSEDWTMEERFRPLTFHGLILRSQLVTLLVRGVCYSESQSSASQPRLSYAEMAEDYPRYPDIHDLDLTLLNPRMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTYEFLQARLRQHYQTI TTCJRDO TT Literature-reported TTST1AJ ID TTST1AJ TTST1AJ TN Chloride channel protein 7 (ClC-7) TTST1AJ UP P51798 TTST1AJ UC CLCN7_HUMAN TTST1AJ BC Chloride channel TTST1AJ SN H(+)/Cl(-) exchange transporter 7; ClC-7; Chloride channel 7 alpha subunit TTST1AJ GN CLCN7 TTST1AJ FC Slowly voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the lysosome lumen. TTST1AJ SQ MANVSKKVSWSGRDRDDEEAAPLLRRTARPGGGTPLLNGAGPGAARQSPRSALFRVGHMSSVELDDELLDPDMDPPHPFPKEIPHNEKLLSLKYESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKGNIDKFTEKGGLSFSLLLWATLNAAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPCLQVIEAVLVAAVTATVAFVLIYSSRDCQPLQGGSMSYPLQLFCADGEYNSMAAAFFNTPEKSVVSLFHDPPGSYNPLTLGLFTLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPVTSHSLTAREVMSTPVTCLRRREKVGVIVDVLSDTASNHNGFPVVEHADDTQPARLQGLILRSQLIVLLKHKVFVERSNLGLVQRRLRLKDFRDAYPRFPPIQSIHVSQDERECTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRLGKRGLEELSLAQT TTST1AJ TT Literature-reported TTR68GQ ID TTR68GQ TTR68GQ TN Chloride channel protein ClC-Kb (ClC-K2) TTR68GQ UP P51801 TTR68GQ UC CLCKB_HUMAN TTR68GQ BC Chloride channel TTR68GQ SN ClC-K2; Chloride channel Kb TTR68GQ GN CLCNKB TTR68GQ FC Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. May be important in urinary concentrating mechanisms. TTR68GQ SQ MEEFVGLREGSSGNPVTLQELWGPCPRIRRGIRGGLEWLKQKLFRLGEDWYFLMTLGVLMALVSCAMDLAVESVVRAHQWLYREIGDSHLLRYLSWTVYPVALVSFSSGFSQSITPSSGGSGIPEVKTMLAGVVLEDYLDIKNFGAKVVGLSCTLACGSTLFLGKVGPFVHLSVMMAAYLGRVRTTTIGEPENKSKQNEMLVAAAAVGVATVFAAPFSGVLFSIEVMSSHFSVWDYWRGFFAATCGAFMFRLLAVFNSEQETITSLYKTSFRVDVPFDLPEIFFFVALGGLCGILGSAYLFCQRIFFGFIRNNRFSSKLLATSKPVYSALATLVLASITYPPSAGRFLASRLSMKQHLDSLFDNHSWALMTQNSSPPWPEELDPQHLWWEWYHPRFTIFGTLAFFLVMKFWMLILATTIPMPAGYFMPIFVYGAAIGRLFGETLSFIFPEGIVAGGITNPIMPGGYALAGAAAFSGAVTHTISTALLAFEVTGQIVHALPVLMAVLAANAIAQSCQPSFYDGTVIVKKLPYLPRILGRNIGSHRVRVEHFMNHSITTLAKDMPLEEVVKVVTSTDVAKYPLVESTESQILVGIVRRAQLVQALKAEPPSWAPGHQQCLQDILAAGCPTEPVTLKLSPETSLHEAHNLFELLNLHSLFVTSRGRAVGCVSWVEMKKAISNLTNPPAPK TTR68GQ TT Literature-reported TT8KZG6 ID TT8KZG6 TT8KZG6 TN Chloride intracellular channel protein 1 (CLIC1) TT8KZG6 UP O00299 TT8KZG6 UC CLIC1_HUMAN TT8KZG6 SN hRNCC; Regulatory nuclear chloride ion channel protein; Nuclear chloride ion channel 27; NCC27; G6; Chloride channel ABP TT8KZG6 GN CLIC1 TT8KZG6 FC Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle. TT8KZG6 PD 4K0N; 4K0G; 4JZQ; 4IQA; 3UVH TT8KZG6 SQ MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK TT8KZG6 TT Literature-reported TT90CMU ID TT90CMU TT90CMU TN Cholecystokinin (CCK) TT90CMU UP P06307 TT90CMU UC CCKN_HUMAN TT90CMU BC Gastrin cholecystokinin TT90CMU SN Procholecystokinin; CCK TT90CMU GN CCK TT90CMU FC This peptide hormone induces gall bladder contraction and therelease of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. TT90CMU SQ MNSGVCLCVLMAVLAAGALTQPVPPADPAGSGLQRAEEAPRRQLRVSQRTDGESRAHLGALLARYIQQARKAPSGRMSIVKNLQNLDPSHRISDRDYMGWMDFGRRSAEEYEYPS TT90CMU TT Literature-reported TTBN3HC ID TTBN3HC TTBN3HC TN Chromobox protein homolog 7 (CBX7) TTBN3HC UP O95931 TTBN3HC UC CBX7_HUMAN TTBN3HC SN Chromobox 7 TTBN3HC GN CBX7 TTBN3HC FC PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3). Binds to trimethylated lysine residues in histones, and possibly also other proteins. Regulator of cellular lifespan by maintaining the repression of CDKN2A, but not by inducing telomerase activity. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. TTBN3HC PD 5EPJ; 4MN3; 3GS2; 2L1B; 2L12 TTBN3HC SQ MELSAIGEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVMAYEEKEERDRASGYRKRGPKPKRLLLQRLYSMDLRSSHKAKGKEKLCFSLTCPLGSGSPEGVVKAGAPELVDKGPLVPTLPFPLRKPRKAHKYLRLSRKKFPPRGPNLESHSHRRELFLQEPPAPDVLQAAGEWEPAAQPPEEEADADLAEGPPPWTPALPSSEVTVTDITANSITVTFREAQAAEGFFRDRSGKF TTBN3HC TT Literature-reported TTM5OJN ID TTM5OJN TTM5OJN TN CIRL-1 messenger RNA (CIRL-1 mRNA) TTM5OJN UP O94910 TTM5OJN UC AGRL1_HUMAN TTM5OJN BC mRNA target TTM5OJN SN Lectomedin-2 (mRNA); Latrophilin-1 (mRNA); LPHN1 (mRNA); LEC2 (mRNA); KIAA0821 (mRNA); Calcium-independent alpha-latrotoxin receptor 1 (mRNA); CIRL-1 (mRNA); Adhesion G protein-coupled receptor L1 (mRNA) TTM5OJN GN ADGRL1 TTM5OJN FC Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor probably implicated in the regulation of exocytosis. Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. TTM5OJN SQ MARLAAVLWNLCVTAVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELVFPQEEYPRKNSIQLSAKTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGPGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEDKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGTHGSLKTSAMRSNTRYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGGPEPPRGRNLADAAAFEKMIISELVHNNLRGSSSAAKGPPPPEPPVPPVPGGGGEEEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPSEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPGLEGPGPDGDGQMQLVTSL TTM5OJN TT Literature-reported TTM5OJN FM mRNA target TT3BKTU ID TT3BKTU TT3BKTU TN Citron Rho-interacting kinase (CIT) TT3BKTU UP O14578 TT3BKTU UC CTRO_HUMAN TT3BKTU SN Serine/threonine-protein kinase 21; STK21; KIAA0949; CRIK TT3BKTU GN CIT TT3BKTU FC Plays a role in cytokinesis. Required for KIF14 localization to the central spindle and midbody. Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Displays serine/threonine protein kinase activity. Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2. TT3BKTU EC EC 2.7.11.1 TT3BKTU SQ MLKFKYGARNPLDAGAAEPIASRASRLNLFFQGKPPFMTQQQMSPLSREGILDALFVLFEECSQPALMKIKHVSNFVRKYSDTIAELQELQPSAKDFEVRSLVGCGHFAEVQVVREKATGDIYAMKVMKKKALLAQEQVSFFEEERNILSRSTSPWIPQLQYAFQDKNHLYLVMEYQPGGDLLSLLNRYEDQLDENLIQFYLAELILAVHSVHLMGYVHRDIKPENILVDRTGHIKLVDFGSAAKMNSNKMVNAKLPIGTPDYMAPEVLTVMNGDGKGTYGLDCDWWSVGVIAYEMIYGRSPFAEGTSARTFNNIMNFQRFLKFPDDPKVSSDFLDLIQSLLCGQKERLKFEGLCCHPFFSKIDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSPCQLSPSGFSGEELPFVGFSYSKALGILGRSESVVSGLDSPAKTSSMEKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKATECQHKLLKAKDQGKPEVGEYAKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLQNREDSSEGIRKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKETLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKNRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVMDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKESSTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKMNSPGLQTKEPSSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDGDVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALESVVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLKNSLTHVPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDISPNIFEAVKGCHLFGAGKIENGLCICAAMPSKVVILRYNENLSKYCIRKEIETSEPCSCIHFTNYSILIGTNKFYEIDMKQYTLEEFLDKNDHSLAPAVFAASSNSFPVSIVQVNSAGQREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSAGTPARAYLDIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEHHRGPSTSRSSPNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYREGRTELRRDKSPGRPLEREKSPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV TT3BKTU TT Literature-reported TTMTS9H ID TTMTS9H TTMTS9H TN Claudin-4 (CLDN4) TTMTS9H UP O14493 TTMTS9H UC CLD4_HUMAN TTMTS9H SN WilliamsBeuren syndrome chromosomal region 8 protein; Clostridium perfringens enterotoxin receptor; Claudin4; CPEreceptor; CPER; CLDN4 TTMTS9H GN CLDN4 TTMTS9H FC Plays a major role in tight junction-specific obliteration of the intercellularspace. TTMTS9H PD 5B2G TTMTS9H SQ MASMGLQVMGIALAVLGWLAVMLCCALPMWRVTAFIGSNIVTSQTIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALVIISIIVAALGVLLSVVGGKCTNCLEDESAKAKTMIVAGVVFLLAGLMVIVPVSWTAHNIIQDFYNPLVASGQKREMGASLYVGWAASGLLLLGGGLLCCNCPPRTDKPYSAKYSAARSAAASNYV TTMTS9H TT Literature-reported TTI2YFK ID TTI2YFK TTI2YFK TN CMRF35-like molecule 8 (CD300A) TTI2YFK UP Q9UGN4 TTI2YFK UC CLM8_HUMAN TTI2YFK SN NK inhibitory receptor; Inhibitory receptor protein 60; Immunoglobulin superfamily member 12; IgSF12; IRp60; IRC1/IRC2; HSPC083; CMRF35H; CMRF35-H9; CMRF35-H; CMRF-35-H9; CLM-8; CD300a; CD300 antigen-like family member A TTI2YFK GN CD300A TTI2YFK FC Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 but not TRIF through activation of PTPN6. Inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation. TTI2YFK PD 2Q87 TTI2YFK SQ MWLPWALLLLWVPGCFALSKCRTVAGPVGGSLSVQCPYEKEHRTLNKYWCRPPQIFLCDKIVETKGSAGKRNGRVSIRDSPANLSFTVTLENLTEEDAGTYWCGVDTPWLRDFHDPVVEVEVSVFPASTSMTPASITAAKTSTITTAFPPVSSTTLFAVGATHSASIQEETEEVVNSQLPLLLSLLALLLLLLVGASLLAWRMFQKWIKAGDHSELSQNPKQAATQSELHYANLELLMWPLQEKPAPPREVEVEYSTVASPREELHYASVVFDSNTNRIAAQRPREEEPDSDYSVIRKT TTI2YFK TT Literature-reported TTHMP8B ID TTHMP8B TTHMP8B TN Cofactor of initiator function (CIF) TTHMP8B UP Q6P1X5 TTHMP8B UC TAF2_HUMAN TTHMP8B SN Transcription initiation factor TFIID subunit 2; Transcription initiation factor TFIID 150 kDa subunit; TBP-associated factor 150 kDa; TAFII150; TAFII-150; TAF2; TAF(II)150; RNA polymerase II TBP-associated factor subunit B; 150 kDa cofactor of initiator function TTHMP8B GN TAF2 TTHMP8B FC Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. It requires core promoter-specific cofactors for productive transcription stimulation. TAF2 stabilizes TFIID binding to core promoter. TTHMP8B PD 6MZM; 6MZL; 6MZC; 5FUR TTHMP8B SQ MPLTGVEPARMNRKKGDKGFESPRPYKLTHQVVCINNINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPTLEVCHSESKQRNLNYFSNAYAAAVSAVDPDAGNGELCIKVPSELWKHVDELKVLKIHINFSLDQPKGGLHFVVPSVEGSMAERGAHVFSCGYQNSTRFWFPCVDSYSELCTWKLEFTVDAAMVAVSNGDLVETVYTHDMRKKTFHYMLTIPTAASNISLAIGPFEILVDPYMHEVTHFCLPQLLPLLKHTTSYLHEVFEFYEEILTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQSLAQQFFGCFISRMSWSDEWVLKGISGYIYGLWMKKTFGVNEYRHWIKEELDKIVAYELKTGGVLLHPIFGGGKEKDNPASHLHFSIKHPHTLSWEYYSMFQCKAHLVMRLIENRISMEFMLQVFNKLLSLASTASSQKFQSHMWSQMLVSTSGFLKSISNVSGKDIQPLIKQWVDQSGVVKFYGSFAFNRKRNVLELEIKQDYTSPGTQKYVGPLKVTVQELDGSFNHTLQIEENSLKHDIPCHSKSRRNKKKKIPLMNGEEVDMDLSAMDADSPLLWIRIDPDMSVLRKVEFEQADFMWQYQLRYERDVVAQQESILALEKFPTPASRLALTDILEQEQCFYRVRMSACFCLAKIANSMVSTWTGPPAMKSLFTRMFCCKSCPNIVKTNNFMSFQSYFLQKTMPVAMALLRDVHNLCPKEVLTFILDLIKYNDNRKNKFSDNYYRAEMIDALANSVTPAVSVNNEVRTLDNLNPDVRLILEEITRFLNMEKLLPSYRHTITVSCLRAIRVLQKNGHVPSDPALFKSYAEYGHFVDIRIAALEAVVDYTKVDRSYEELQWLLNMIQNDPVPYVRHKILNMLTKNPPFTKNMESPLCNEALVDQLWKLMNSGTSHDWRLRCGAVDLYFTLFGLSRPSCLPLPELGLVLNLKEKKAVLNPTIIPESVAGNQEAANNPSSHPQLVGFQNPFSSSQDEEEIDMDTVHDSQAFISHHLNMLERPSTPGLSKYRPASSRSALIPQHSAGCDSTPTTKPQWSLELARKGTGKEQAPLEMSMHPAASAPLSVFTKESTASKHSDHHHHHHHEHKKKKKKHKHKHKHKHKHDSKEKDKEPFTFSSPASGRSIRSPSLSD TTHMP8B TT Literature-reported TT5WCAH ID TT5WCAH TT5WCAH TN Collagen VI (COL6A3) TT5WCAH UP P12111 TT5WCAH UC CO6A3_HUMAN TT5WCAH SN COL6A3 TT5WCAH GN COL6A3 TT5WCAH FC Collagen VI acts as a cell-binding protein. TT5WCAH PD 2KNT; 1KUN; 1KTH; 1KNT TT5WCAH SQ MRKHRHLPLVAVFCLFLSGFPTTHAQQQQADVKNGAAADIIFLVDSSWTIGEEHFQLVREFLYDVVKSLAVGENDFHFALVQFNGNPHTEFLLNTYRTKQEVLSHISNMSYIGGTNQTGKGLEYIMQSHLTKAAGSRAGDGVPQVIVVLTDGHSKDGLALPSAELKSADVNVFAIGVEDADEGALKEIASEPLNMHMFNLENFTSLHDIVGNLVSCVHSSVSPERAGDTETLKDITAQDSADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELANIGLALDFVVENHFTRAGGSRVEEGVPQVLVLISAGPSSDEIRYGVVALKQASVFSFGLGAQAASRAELQHIATDDNLVFTVPEFRSFGDLQEKLLPYIVGVAQRHIVLKPPTIVTQVIEVNKRDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALYTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVFIPAEFRAAPLQGMLPGLLAPLRTLSGTPEVHSNKRDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLNTGSALSYVYANHFTEAGGSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSLVYLMDDFSSLPALPQQLIQPLTTYVSGGVEEVPLAQPESKRDILFLFDGSANLVGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALNLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFILAAESLPKIGDLHPQIVNLLKSVHNGAPAPVSGEKDVVFLLDGSEGVRSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPNTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAVAIPTFRQLGTVQQVISERVTQLTREELSRLQPVLQPLPSPGVGGKRDVVFLIDGSQSAGPEFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQINVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIARNADQEELVKISLSPEYVFSVSTFRELPSLEQKLLTPITTLTSEQIQKLLASTRYPPPAVESDAADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLNTGKALEFVARNLFVKSAGSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRLVFTVREFRELPNIEERIMNSFGPSAATPAPPGVDTPPPSRPEKKKADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHANTKVGLEHLRVNHFVPEAGSRLDQRVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSATAFRVGNVQELSELSEQVLETLHDAMHETLCPGVTDAAKACNLDVILGFDGSRDQNVFVAQKGFESKVDAILNRISQMHRVSCSGGRSPTVRVSVVANTPSGPVEAFDFDEYQPEMLEKFRNMRSQHPYVLTEDTLKVYLNKFRQSSPDSVKVVIHFTDGADGDLADLHRASENLRQEGVRALILVGLERVVNLERLMHLEFGRGFMYDRPLRLNLLDLDYELAEQLDNIAEKACCGVPCKCSGQRGDRGPIGSIGPKGIPGEDGYRGYPGDEGGPGERGPPGVNGTQGFQGCPGQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGQDSQERGPKGETGDLGPMGVPGRDGVPGGPGETGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTRGAQGPAGPAGPPGLIGEQGISGPRGSGGAAGAPGERGRTGPLGRKGEPGEPGPKGGIGNRGPRGETGDDGRDGVGSEGRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDSIDQCALIQSIKDKCPCCYGPLECPVFPTELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAESNCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVALTSKQQSLETAMSFVARNTFKRVRNGFLMRKVAVFFSNTPTRASPQLREAVLKLSDAGITPLFLTRQEDRQLINALQINNTAVGHALVLPAGRDLTDFLENVLTCHVCLDICNIDPSCGFGSWRPSFRDRRAAGSDVDIDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPKASQHFARVAVVQHAPSESVDNASMPPVKVEFSLTDYGSKEKLVDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRDLKIVVLMLTGEVPEQQLEEAQRVILQAKCKGYFFVVLGIGRKVNIKEVYTFASEPNDVFFKLVDKSTELNEEPLMRFGRLLPSFVSSENAFYLSPDIRKQCDWFQGDQPTKNLVKFGHKQVNVPNNVTSSPTSNPVTTTKPVTTTKPVTTTTKPVTTTTKPVTIINQPSVKPAAAKPAPAKPVAAKPVATKMATVRPPVAVKPATAAKPVAAKPAAVRPPAAAAAKPVATKPEVPRPQAAKPAATKPATTKPMVKMSREVQVFEITENSAKLHWERAEPPGPYFYDLTVTSAHDQSLVLKQNLTVTDRVIGGLLAGQTYHVAVVCYLRSQVRATYHGSFSTKKSQPPPPQPARSASSSTINLMVSTEPLALTETDICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCAPVLAKPGVISVMGT TT5WCAH TT Literature-reported TT8A9DM ID TT8A9DM TT8A9DM TN Complement C1q component (C1Q) TT8A9DM UP P02746 TT8A9DM UC C1QB_HUMAN TT8A9DM SN C1QB TT8A9DM GN C1QB TT8A9DM FC C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takesplace on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes. TT8A9DM PD 6FCZ; 5HZF; 5HKJ; 2WNV; 2WNU TT8A9DM SQ MMMKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEKGLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKIAFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIFSGFLLFPDMEA TT8A9DM TT Literature-reported TTLA0VS ID TTLA0VS TTLA0VS TN Complement factor P (CFP) TTLA0VS UP P27918 TTLA0VS UC PROP_HUMAN TTLA0VS SN Properdin; CFP TTLA0VS GN CFP TTLA0VS FC A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes. TTLA0VS PD 1W0S; 1W0R TTLA0VS SQ MITEGAQAPRLLLPPLLLLLTLPATGSDPVLCFTQYEESSGKCKGLLGGGVSVEDCCLNTAFAYQKRSGGLCQPCRSPRWSLWSTWAPCSVTCSEGSQLRYRRCVGWNGQCSGKVAPGTLEWQLQACEDQQCCPEMGGWSGWGPWEPCSVTCSKGTRTRRRACNHPAPKCGGHCPGQAQESEACDTQQVCPTHGAWATWGPWTPCSASCHGGPHEPKETRSRKCSAPEPSQKPPGKPCPGLAYEQRRCTGLPPCPVAGGWGPWGPVSPCPVTCGLGQTMEQRTCNHPVPQHGGPFCAGDATRTHICNTAVPCPVDGEWDSWGEWSPCIRRNMKSISCQEIPGQQSRGRTCRGRKFDGHRCAGQQQDIRHCYSIQHCPLKGSWSEWSTWGLCMPPCGPNPTRARQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGRPLPRCEELQGQKLVVEEKRPCLHVPACKDPEEEEL TTLA0VS TT Clinical trial TTDQPXA ID TTDQPXA TTDQPXA TN Connexin-23 (Cx23) TTDQPXA UP A6NN92 TTDQPXA UC CXE1_HUMAN TTDQPXA BC Gap junction-forming connexin TTDQPXA SN Putative gap junction epsilon-1 protein TTDQPXA GN GJE1 TTDQPXA FC Does not form functional gap junctions. Mediates calcium-independent ATP release, suggesting activity as a hemichannel. TTDQPXA SQ MSLNYIKNFYEGCVKPPTVIGQFHTLFFGSIRIFFLGVLGFAVYGNEALHFICDPDKREVNLFCYNQFRPITPQVSFSALQLVIVLVPGALFHLYAACKSINQECILQKPIYTIIYILSVLLRISLAAIAFWLQIYLFGFQVKSLYLCDARSLGENMIIRCMVPEHFEKTIFLIAINTFTTITILLFVAEIFEIIFRRLYFPFRQ TTDQPXA TT Literature-reported TTZ7POK ID TTZ7POK TTZ7POK TN Connexin-25 (Cx25) TTZ7POK UP Q6PEY0 TTZ7POK UC CXB7_HUMAN TTZ7POK BC Gap junction-forming connexin TTZ7POK SN Gap junction beta-7 protein; CX25 TTZ7POK GN GJB7 TTZ7POK FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTZ7POK SQ MSWMFLRDLLSGVNKYSTGTGWIWLAVVFVFRLLVYMVAAEHVWKDEQKEFECNSRQPGCKNVCFDDFFPISQVRLWALQLIMVSTPSLLVVLHVAYHEGREKRHRKKLYVSPGTMDGGLWYAYLISLIVKTGFEIGFLVLFYKLYDGFSVPYLIKCDLKPCPNTVDCFISKPTEKTIFILFLVITSCLCIVLNFIELSFLVLKCFIKCCLQKYLKKPQVLSV TTZ7POK TT Literature-reported TTAU8SJ ID TTAU8SJ TTAU8SJ TN Connexin-30 (Cx30) TTAU8SJ UP O95452 TTAU8SJ UC CXB6_HUMAN TTAU8SJ BC Gap junction-forming connexin TTAU8SJ SN Gap junction beta-6 protein TTAU8SJ GN GJB6 TTAU8SJ FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTAU8SJ SQ MDWGTLHTFIGGVNKHSTSIGKVWITVIFIFRVMILVVAAQEVWGDEQEDFVCNTLQPGCKNVCYDHFFPVSHIRLWALQLIFVSTPALLVAMHVAYYRHETTRKFRRGEKRNDFKDIEDIKKQKVRIEGSLWWTYTSSIFFRIIFEAAFMYVFYFLYNGYHLPWVLKCGIDPCPNLVDCFISRPTEKTVFTIFMISASVICMLLNVAELCYLLLKVCFRRSKRAQTQKNHPNHALKESKQNEMNELISDSGQNAITGFPS TTAU8SJ TT Literature-reported TTYP9NL ID TTYP9NL TTYP9NL TN Connexin-59 (Cx59) TTYP9NL UP P57773 TTYP9NL UC CXA9_HUMAN TTYP9NL BC Gap junction-forming connexin TTYP9NL SN Gap junction alpha-9 protein; GJA10; Cx58; Connexin-58 TTYP9NL GN GJA9 TTYP9NL FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTYP9NL SQ MGDWNLLGDTLEEVHIHSTMIGKIWLTILFIFRMLVLGVAAEDVWNDEQSGFICNTEQPGCRNVCYDQAFPISLIRYWVLQVIFVSSPSLVYMGHALYRLRVLEEERQRMKAQLRVELEEVEFEMPRDRRRLEQELCQLEKRKLNKAPLRGTLLCTYVIHIFTRSVVEVGFMIGQYLLYGFHLEPLFKCHGHPCPNIIDCFVSRPTEKTIFLLFMQSIATISLFLNILEIFHLGFKKIKRGLWGKYKLKKEHNEFHANKAKQNVAKYQSTSANSLKRLPSAPDYNLLVEKQTHTAVYPSLNSSSVFQPNPDNHSVNDEKCILDEQETVLSNEISTLSTSCSHFQHISSNNNKDTHKIFGKELNGNQLMEKRETEGKDSKRNYYSRGHRSIPGVAIDGENNMRQSPQTVFSLPANCDWKPRWLRATWGSSTEHENRGSPPKGNLKGQFRKGTVRTLPPSQGDSQSLDIPNTADSLGGLSFEPGLVRTCNNPVCPPNHVVSLTNNLIGRRVPTDLQI TTYP9NL TT Literature-reported TTQMI2N ID TTQMI2N TTQMI2N TN Connexin-62 (Cx62) TTQMI2N UP Q969M2 TTQMI2N UC CXA10_HUMAN TTQMI2N BC Gap junction-forming connexin TTQMI2N SN Gap junction alpha-10 protein; CX62 TTQMI2N GN GJA10 TTQMI2N FC Involved in tracer coupling between horizontal cells of the retina. May play a role in the regulation of horizontal cell patterning. One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTQMI2N SQ MGDWNLLGGILEEVHSHSTIVGKIWLTILFIFRMLVLRVAAEDVWDDEQSAFACNTRQPGCNNICYDDAFPISLIRFWVLQIIFVSSPSLVYMGHALYRLRAFEKDRQRKKSHLRAQMENPDLDLEEQQRIDRELRRLEEQKRIHKVPLKGCLLRTYVLHILTRSVLEVGFMIGQYILYGFQMHPLYKCTQPPCPNAVDCFVSRPTEKTIFMLFMHSIAAISLLLNILEIFHLGIRKIMRTLYKKSSSEGIEDETGPPFHLKKYSVAQQCMICSSLPERISPLQANNQQQVIRVNVPKSKTMWQIPQPRQLEVDPSNGKKDWSEKDQHSGQLHVHSPCPWAGSAGNQHLGQQSDHSSFGLQNTMSQSWLGTTTAPRNCPSFAVGTWEQSQDPEPSGEPLTDLHSHCRDSEGSMRESGVWIDRSRPGSRKASFLSRLLSEKRHLHSDSGSSGSRNSSCLDFPHWENSPSPLPSVTGHRTSMVRQAALPIMELSQELFHSGCFLFPFFLPGVCMYVCVDREADGGGDYLWRDKIIHSIHSVKFNS TTQMI2N TT Literature-reported TTJLVBO ID TTJLVBO TTJLVBO TN Coronavirus Main proteinase (CoV 1a) TTJLVBO UP P0C6U8 TTJLVBO UC R1A_CVHSA TTJLVBO SN pp1a; Replicase polyprotein 1a; ORF1a polyprotein TTJLVBO GN CoV 1a TTJLVBO FC The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3. TTJLVBO PD 5Y3Q; 5Y3E; 5F22; 4OW0; 4OVZ TTJLVBO SQ MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTNHGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELGTDPIEDYEQNWNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAWFTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVASPQECNNMHLSTLMKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKGGRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFHLNEEVAIILASFSASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIPDLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAYVTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVEFLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQCIRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYCALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAVVKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGLPLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAANIHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQKPVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRARAGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGVSIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQMTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENTSITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFTKSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYCNGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVECTTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIISTDDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLIEYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEYCRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDTTSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAACAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDDAARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINRLCEEMLDNRATLQAIASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPLMQSADASTFLNGFAV TTJLVBO TT Literature-reported TT4GOCR ID TT4GOCR TT4GOCR TN Corticosteroid receptor type I (NR3C2) TT4GOCR UP P08235 TT4GOCR UC MCR_HUMAN TT4GOCR SN MCR; MLR; MR; Mineralocorticoid receptor; Nuclear receptor subfamily 3 group C member 2 TT4GOCR GN NR3C2 TT4GOCR FC Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels. TT4GOCR PD 6GGG; 6GG8; 6GEV; 5MWY; 5MWP TT4GOCR SQ METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNSTQGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYEQQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAVVKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPNVENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSPANINNSRCSVSSPSNTNNRSTLSSPAASTVGSICSPVNNAFSYTASGTSAGSSTLRDVVPSPDTQEKGAQEVPFPKTEEVESAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNSKINSDSSFSVPIKQESTKHSCSGTSFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGFDGNCEGSGFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSARDQSFQHLSSFPPVNTLVESWKSHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPSKICLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRLQKCLQAGMNLGARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEEGTTYIAPAKEPSVNTALVPQLSTISRALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKCPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAMLVEIISDQLPKVESGNAKPLYFHRK TT4GOCR TT Literature-reported TTX0S7F ID TTX0S7F TTX0S7F TN Corynebacterium Pup-protein ligase (Cory pafA) TTX0S7F UP Q8NQE1 TTX0S7F UC PAFA_CORGL TTX0S7F SN Pup-conjugating enzyme; Pup--protein ligase; Proteasome accessory factor A TTX0S7F GN Cory pafA TTX0S7F FC Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine. TTX0S7F PD 4BJR; 4B0T TTX0S7F SQ MSTVESALTRRIMGIETEYGLTFVDGDSKKLRPDEIARRMFRPIVEKYSSSNIFIPNGSRLYLDVGSHPEYATAECDNLTQLINFEKAGDVIADRMAVDAEESLAKEDIAGQVYLFKNNVDSVGNSYGCHENYLVGRSMPLKALGKRLMPFLITRQLICGAGRIHHPNPLDKGESFPLGYCISQRSDHVWEGVSSATTRSRPIINTRDEPHADSHSYRRLHVIVGDANMAEPSIALKVGSTLLVLEMIEADFGLPSLELANDIASIREISRDATGSTLLSLKDGTTMTALQIQQVVFEHASKWLEQRPEPEFSGTSNTEMARVLDLWGRMLKAIESGDFSEVDTEIDWVIKKKLIDRFIQRGNLGLDDPKLAQVDLTYHDIRPGRGLFSVLQSRGMIKRWTTDEAILAAVDTAPDTTRAHLRGRILKAADTLGVPVTVDWMRHKVNRPEPQSVELGDPFSAVNSEVDQLIEYMTVHAESYRS TTX0S7F TT Literature-reported TT9INHD ID TT9INHD TT9INHD TN Creatine kinase (CK) TT9INHD UP P12277; P17540; P12532; P06732 TT9INHD UC KCRB_HUMAN; KCRS_HUMAN; KCRU_HUMAN; KCRM_HUMAN TT9INHD BC Kinase TT9INHD SN Creatine kinase TT9INHD GN CKB; CKMT2; CKMT1A; CKM TT9INHD FC Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. TT9INHD SQ MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTGVDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPNLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQAIDDLMPAQK TT9INHD TT Literature-reported TTDCO2A ID TTDCO2A TTDCO2A TN Crithidia Tryparedoxin (Crithi TryX) TTDCO2A UP O96438 TTDCO2A UC O96438_CRIFA TTDCO2A SN Tryparedoxin I TTDCO2A GN Crithi TryX TTDCO2A FC Mediates the flux of reduction equivalents from the unique redox metabolite trypanothione TTDCO2A PD 1QK8; 1OKD; 1O8X; 1O8W; 1O85 TTDCO2A SQ MSGLDKYLPGIEKLRRGDGEVEVKSLAGKLVFFYFSASWCPPCRGFTPQLIEFYDKFHESKNFEVVFCTWDEEEDGFAGYFAKMPWLAVPFAQSEAVQKLSKHFNVESIPTLIGVDADSGDVVTTRARATLVKDPEGEQFPWKDAP TTDCO2A TT Literature-reported TTGUSRB ID TTGUSRB TTGUSRB TN C-type lectin domain containing 9A (CLEC9A) TTGUSRB UP Q6UXN8 TTGUSRB UC CLC9A_HUMAN TTGUSRB SN CLEC9A TTGUSRB GN CLEC9A TTGUSRB FC Functions as an endocytic receptor on a small subset of myeloid cells specialized for the uptake and processing of material from dead cells. Recognizes filamentous form of actin in association with particular actin-binding domains of cytoskeletal proteins, including spectrin, exposed when cell membranes are damaged, and mediate the cross-presentation of dead-cell associated antigens in a Syk-dependent manner. TTGUSRB PD 3VPP TTGUSRB SQ MHEEEIYTSLQWDSPAPDTYQKCLSSNKCSGACCLVMVISCVFCMGLLTASIFLGVKLLQVSTIAMQQQEKLIQQERALLNFTEWKRSCALQMKYCQAFMQNSLSSAHNSSPCPNNWIQNRESCYYVSEIWSIWHTSQENCLKEGSTLLQIESKEEMDFITGSLRKIKGSYDYWVGLSQDGHSGRWLWQDGSSPSPGLLPAERSQSANQVCGYVKSNSLLSSNCSTWKYFICEKYALRSSV TTGUSRB TT Literature-reported TTPCU0Q ID TTPCU0Q TTPCU0Q TN Cullin-3 (CUL-3) TTPCU0Q UP Q13618 TTPCU0Q UC CUL3_HUMAN TTPCU0Q SN KIAA0617; Cullin3 TTPCU0Q GN CUL3 TTPCU0Q FC BCR complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the BCR complex depends on the BTB domain-containing protein as the substrate recognition component. BCR(KLHL42) is involved in ubiquitination of KATNA1. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, BRMS1, H2AFY and DAXX, GLI2 and GLI3. Can also form a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase activity. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; by mediating ubiquitination of WNK4. The BCR(KLHL20) E3 ubiquitin ligase complex is involved in interferon response and anterograde Golgi to endosome transport: it mediates both ubiquitination leading to degradation and 'Lys-33'-linked ubiquitination. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. The BCR(KLHL25) ubiquitin ligase complex is involved in translational homeostasis by mediating ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1). The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1, leading to remodel the translational program of differentiating cells in favor of neural crest specification. Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and RBX1, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. The BCR(KCTD17) E3 ubiquitin ligase complex mediates ubiquitination and degradation of TCHP, a down-regulator of cilium assembly, thereby inducing ciliogenesis. The BCR(KLHL24) E3 ubiquitin ligase complex mediates ubiquitination of KRT14, controls KRT14 levels during keratinocytes differentiation, and is essential for skin integrity. Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. TTPCU0Q PD 6I2M; 5NLB; 4HXI; 4EOZ; 4APF TTPCU0Q SQ MSNLSKGTGSRKDTKMRIRAFPMTMDEKYVNSIWDLLKNAIQEIQRKNNSGLSFEELYRNAYTMVLHKHGEKLYTGLREVVTEHLINKVREDVLNSLNNNFLQTLNQAWNDHQTAMVMIRDILMYMDRVYVQQNNVENVYNLGLIIFRDQVVRYGCIRDHLRQTLLDMIARERKGEVVDRGAIRNACQMLMILGLEGRSVYEEDFEAPFLEMSAEFFQMESQKFLAENSASVYIKKVEARINEEIERVMHCLDKSTEEPIVKVVERELISKHMKTIVEMENSGLVHMLKNGKTEDLGCMYKLFSRVPNGLKTMCECMSSYLREQGKALVSEEGEGKNPVDYIQGLLDLKSRFDRFLLESFNNDRLFKQTIAGDFEYFLNLNSRSPEYLSLFIDDKLKKGVKGLTEQEVETILDKAMVLFRFMQEKDVFERYYKQHLARRLLTNKSVSDDSEKNMISKLKTECGCQFTSKLEGMFRDMSISNTTMDEFRQHLQATGVSLGGVDLTVRVLTTGYWPTQSATPKCNIPPAPRHAFEIFRRFYLAKHSGRQLTLQHHMGSADLNATFYGPVKKEDGSEVGVGGAQVTGSNTRKHILQVSTFQMTILMLFNNREKYTFEEIQQETDIPERELVRALQSLACGKPTQRVLTKEPKSKEIENGHIFTVNDQFTSKLHRVKIQTVAAKQGESDPERKETRQKVDDDRKHEIEAAIVRIMKSRKKMQHNVLVAEVTQQLKARFLPSPVVIKKRIEGLIEREYLARTPEDRKVYTYVA TTPCU0Q TT Literature-reported TTPCU0Q FM Cullin family TTI8R0P ID TTI8R0P TTI8R0P TN Cullin-7 (CUL-7) TTI8R0P UP Q14999 TTI8R0P UC CUL7_HUMAN TTI8R0P SN KIAA0076 TTI8R0P GN CUL7 TTI8R0P FC Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5. Core component of a Cul7-RING ubiquitin-protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1. Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain. Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development. Does not promote polyubiquitination and proteasomal degradation of p53/TP53. While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions. Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. TTI8R0P PD 2JNG TTI8R0P SQ MVGELRYREFRVPLGPGLHAYPDELIRQRVGHDGHPEYQIRWLILRRGDEGDGGSGQVDCKAEHILLWMSKDEIYANCHKMLGEDGQVIGPSQESAGEVGALDKSVLEEMETDVKSLIQRALRQLEECVGTIPPAPLLHTVHVLSAYASIEPLTGVFKDPRVLDLLMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLSEHPMSFEGIQLPQVPGRVLFSLVKRYLHVTSLLDQLNDSAAEPGAQNTSAPEELSGERGQLELEFSMAMGTLISELVQAMRWDQASDRPRSSARSPGSIFQPQLADVSPGLPAAQAQPSFRRSRRFRPRSEFASGNTYALYVRDTLQPGMRVRMLDDYEEISAGDEGEFRQSNNGVPPVQVFWESTGRTYWVHWHMLEILGFEEDIEDMVEADEYQGAVASRVLGRALPAWRWRPMTELYAVPYVLPEDEDTEECEHLTLAEWWELLFFIKKLDGPDHQEVLQILQENLDGEILDDEILAELAVPIELAQDLLLTLPQRLNDSALRDLINCHVYKKYGPEALAGNQAYPSLLEAQEDVLLLDAQAQAKDSEDAAKVEAKEPPSQSPNTPLQRLVEGYGPAGKILLDLEQALSSEGTQENKVKPLLLQLQRQPQPFLALMQSLDTPETNRTLHLTVLRILKQLVDFPEALLLPWHEAVDACMACLRSPNTDREVLQELIFFLHRLTSVSRDYAVVLNQLGARDAISKALEKHLGKLELAQELRDMVFKCEKHAHLYRKLITNILGGCIQMVLGQIEDHRRTHQPINIPFFDVFLRYLCQGSSVEVKEDKCWEKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHTELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEILGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDMAEDRRSLLHLSSRLNGALRQEQNFADRFLPDDEAAQALGKTCWEALVSPVVQNITSPDEDGISPLGWLLDQYLECQEAVFNPQSRGPAFFSRVRRLTHLLVHVEPCEAPPPVVATPRPKGRNRSHDWSSLATRGLPSSIMRNLTRCWRAVVEKQVNNFLTSSWRDDDFVPRYCEHFNILQNSSSELFGPRAAFLLALQNGCAGALLKLPFLKAAHVSEQFARHIDQQIQGSRIGGAQEMERLAQLQQCLQAVLIFSGLEIATTFEHYYQHYMADRLLGVVSSWLEGAVLEQIGPCFPNRLPQQMLQSLSTSKELQRQFHVYQLQQLDQELLKLEDTEKKIQVGLGASGKEHKSEKEEEAGAAAVVDVAEGEEEEEENEDLYYEGAMPEVSVLVLSRHSWPVASICHTLNPRTCLPSYLRGTLNRYSNFYNKSQSHPALERGSQRRLQWTWLGWAELQFGNQTLHVSTVQMWLLLYLNDLKAVSVESLLAFSGLSADMLNQAIGPLTSSRGPLDLHEQKDIPGGVLKIRDGSKEPRSRWDIVRLIPPQTYLQAEGEDGQNLEKRRNLLNCLIVRILKAHGDEGLHIDQLVCLVLEAWQKGPCPPRGLVSSLGKGSACSSTDVLSCILHLLGKGTLRRHDDRPQVLSYAVPVTVMEPHTESLNPGSSGPNPPLTFHTLQIRSRGVPYASCTATQSFSTFR TTI8R0P TT Literature-reported TTI8R0P FM Cullin family TT2T98G ID TT2T98G TT2T98G TN C-X3-C chemokine receptor 1 (CX3CR1) TT2T98G UP P49238 TT2T98G UC CX3C1_HUMAN TT2T98G BC GPCR rhodopsin TT2T98G SN V28; GPR13; G-protein coupled receptor 13; Fractalkine receptor CX3CR1; Fractalkine receptor; CX3C chemokine receptor 1; CMKBRL1; CMKBLR1; CMK-BRL1; CMK-BRL-1; C-X3-C CKR-1; Beta chemokine receptor-like1; Beta chemokine receptor-like 1 TT2T98G GN CX3CR1 TT2T98G FC Acts as coreceptor with CD4 for HIV-1 virus envelope protein (in vitro). Isoform 2 and isoform 3 seem to be more potent HIV-1 coreceptors than isoform 1. Receptor for the CX3C chemokine fractalkine (CX3CL1); binds to CX3CL1 and mediates both its adhesive and migratory functions. TT2T98G SQ MDQFPESVTENFEYDDLAEACYIGDIVVFGTVFLSIFYSVIFAIGLVGNLLVVFALTNSKKPKSVTDIYLLNLALSDLLFVATLPFWTHYLINEKGLHNAMCKFTTAFFFIGFFGSIFFITVISIDRYLAIVLAANSMNNRTVQHGVTISLGVWAAAILVAAPQFMFTKQKENECLGDYPEVLQEIWPVLRNVETNFLGFLLPLLIMSYCYFRIIQTLFSCKNHKKAKAIKLILLVVIVFFLFWTPYNVMIFLETLKLYDFFPSCDMRKDLRLALSVTETVAFSHCCLNPLIYAFAGEKFRRYLYHLYGKCLAVLCGRSVHVDFSSSESQRSRHGSVLSSNFTYHTSDGDALLLL TT2T98G TT Literature-reported TT2T98G FM GPCR rhodopsin TTW0QOV ID TTW0QOV TTW0QOV TN Cyclic nucleotide-gated channel alpha-3 (CNGA3) TTW0QOV UP Q16281 TTW0QOV UC CNGA3_HUMAN TTW0QOV SN Cyclic nucleotide-gated cation channel alpha-3; Cone photoreceptor cGMP-gated channel subunit alpha; CNG3; CNG-3; CNG channel alpha-3; CNCG3 TTW0QOV GN CNGA3 TTW0QOV FC Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3 (By similarity). Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones. TTW0QOV PD 3SWY TTW0QOV SQ MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAMETRGLADSGQGSFTGQGIARLSRLIFLLRRWAARHVHHQDQGPDSFPDRFRGAELKEVSSQESNAQANVGSQEPADRGRSAWPLAKCNTNTSNNTEEEKKTKKKDAIVVDPSSNLYYRWLTAIALPVFYNWYLLICRACFDELQSEYLMLWLVLDYSADVLYVLDVLVRARTGFLEQGLMVSDTNRLWQHYKTTTQFKLDVLSLVPTDLAYLKVGTNYPEVRFNRLLKFSRLFEFFDRTETRTNYPNMFRIGNLVLYILIIIHWNACIYFAISKFIGFGTDSWVYPNISIPEHGRLSRKYIYSLYWSTLTLTTIGETPPPVKDEEYLFVVVDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSIKQYMQFRKVTKDLETRVIRWFDYLWANKKTVDEKEVLKSLPDKLKAEIAINVHLDTLKKVRIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGKEMYIINEGKLAVVADDGVTQFVVLSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPEAKKALEEKGRQILMKDNLIDEELARAGADPKDLEEKVEQLGSSLDTLQTRFARLLAEYNATQMKMKQRLSQLESQVKGGGDKPLADGEVPGDATKTEDKQQ TTW0QOV TT Clinical trial TT0LJCG ID TT0LJCG TT0LJCG TN Cyclic nucleotide-gated channel beta-3 (CNGB3) TT0LJCG UP Q9NQW8 TT0LJCG UC CNGB3_HUMAN TT0LJCG SN Cyclic nucleotidegated channel beta3; Cyclic nucleotidegated cation channel modulatory subunit; Cyclic nucleotidegated cation channel beta3; Cyclic nucleotide-gated cation channel modulatory subunit; Cyclic nucleotide-gated cation channel beta-3; Cone photoreceptor cGMPgated channel subunit beta; Cone photoreceptor cGMP-gated channel subunit beta; CNG channel beta3; CNG channel beta-3 TT0LJCG GN CNGB3 TT0LJCG FC Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficiency of the channel when coexpressed with CNGA3 (By similarity). Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones. TT0LJCG SQ MFKSLTKVNKVKPIGENNENEQSSRRNEEGSHPSNQSQQTTAQEENKGEEKSLKTKSTPVTSEEPHTNIQDKLSKKNSSGDLTTNPDPQNAAEPTGTVPEQKEMDPGKEGPNSPQNKPPAAPVINEYADAQLHNLVKRMRQRTALYKKKLVEGDLSSPEASPQTAKPTAVPPVKESDDKPTEHYYRLLWFKVKKMPLTEYLKRIKLPNSIDSYTDRLYLLWLLLVTLAYNWNCCFIPLRLVFPYQTADNIHYWLIADIICDIIYLYDMLFIQPRLQFVRGGDIIVDSNELRKHYRTSTKFQLDVASIIPFDICYLFFGFNPMFRANRMLKYTSFFEFNHHLESIMDKAYIYRVIRTTGYLLFILHINACVYYWASNYEGIGTTRWVYDGEGNEYLRCYYWAVRTLITIGGLPEPQTLFEIVFQLLNFFSGVFVFSSLIGQMRDVIGAATANQNYFRACMDDTIAYMNNYSIPKLVQKRVRTWYEYTWDSQRMLDESDLLKTLPTTVQLALAIDVNFSIISKVDLFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVLGGPDGTKVLVTLKAGSVFGEISLLAAGGGNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQKAKTAEATPPRKDLALLFPPKEETPKLFKTLLGGTGKASLARLLKLKREQAAQKKENSEGGEEEGKENEDKQKENEDKQKENEDKGKENEDKDKGREPEEKPLDRPECTASPIAVEEEPHSVRRTVLPRGTSRQSLIISMAPSAEGGEEVLTIEVKEKAKQ TT0LJCG TT Clinical trial TT0LJCG KE hsa04024:cAMP signaling pathway TTCE793 ID TTCE793 TTCE793 TN Cyclic-AMP-dependent transcription factor ATF-3 (ATF3) TTCE793 UP P18847 TTCE793 UC ATF3_HUMAN TTCE793 BC Basic leucine zipper bZIP TTCE793 SN cAMP-dependent transcription factor ATF-3; Cyclic AMP-dependent transcription factor ATF-3; Activating transcription factor 3 TTCE793 GN ATF3 TTCE793 FC Represses transcription from promoters with ATF sites. It may repress transcription by stabilizing the binding of inhibitory cofactors at the promoter. Isoform 2 activates transcription presumably by sequestering inhibitory cofactors away from the promoters. This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. TTCE793 SQ MMLQHPGQVSASEVSASAIVPCLSPPGSLVFEDFANLTPFVKEELRFAIQNKHLCHRMSSALESVTVSDRPLGVSITKAEVAPEEDERKKRRRERNKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLNLHRPTCIVRAQNGRTPEDERNLFIQQIKEGTLQS TTCE793 TT Literature-reported TT1JXNR ID TT1JXNR TT1JXNR TN Cyclin D (CCND3) TT1JXNR UP P30281 TT1JXNR UC CCND3_HUMAN TT1JXNR SN G1/S-specific cyclin-D3 TT1JXNR GN CCND3 TT1JXNR FC Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. TT1JXNR PD 3G33 TT1JXNR SQ MELLCCEGTRHAPRAGPDPRLLGDQRVLQSLLRLEERYVPRASYFQCVQREIKPHMRKMLAYWMLEVCEEQRCEEEVFPLAMNYLDRYLSCVPTRKAQLQLLGAVCMLLASKLRETTPLTIEKLCIYTDHAVSPRQLRDWEVLVLGKLKWDLAAVIAHDFLAFILHRLSLPRDRQALVKKHAQTFLALCATDYTFAMYPPSMIATGSIGAAVQGLGACSMSGDELTELLAGITGTEVDCLRACQEQIEAALRESLREASQTSSSPAPKAPRGSSSQGPSQTSTPTDVTAIHL TT1JXNR TT Literature-reported TTQ7W6D ID TTQ7W6D TTQ7W6D TN Cysteine-rich angiogenic inducer 61 (CYR61) TTQ7W6D UP O00622 TTQ7W6D UC CYR61_HUMAN TTQ7W6D SN CCN1 TTQ7W6D GN CYR61 TTQ7W6D FC Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5. CYR61-mediated gene regulation is dependent on heparin-binding. Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1. Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-v/beta-5 and cell proliferation through integrin alpha-v/beta-3. Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. TTQ7W6D PD 4D11; 4D0Z TTQ7W6D SQ MSSRIARALALVVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVTGQCCEEWVCDEDSIKDPMEDQDGLLGKELGFDASEVELTRNNELIAVGKGSSLKRLPVFGMEPRILYNPLQGQKCIVQTTSWSQCSKTCGTGISTRVTNDNPECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCLSVKKYRPKYCGSCVDGRCCTPQLTRTVKMRFRCEDGETFSKNVMMIQSCKCNYNCPHANEAAFPFYRLFNDIHKFRD TTQ7W6D TT Literature-reported TTBZMIO ID TTBZMIO TTBZMIO TN Cystine/glutamate transporter (SLC7A11) TTBZMIO UP Q9UPY5 TTBZMIO UC XCT_HUMAN TTBZMIO BC Amino acid-polyamine-organocation TTBZMIO SN XCT; X(c)-cystine transporter; X(c)- plasma membrane cystine transporter; Solute carrier family 7 member 11; Calcium channel blocker resistance protein CCBR1; Amino acid transport system xc-; Amino acid transport system XCT TTBZMIO GN SLC7A11 TTBZMIO FC Sodium-independent, high-affinity exchange of anionic amino acids with high specificity for anionic form of cystine and glutamate. TTBZMIO SQ MVRKPVVSTISKGGYLQGNVNGRLPSLGNKEPPGQEKVQLKRKVTLLRGVSIIIGTIIGAGIFISPKGVLQNTGSVGMSLTIWTVCGVLSLFGALSYAELGTTIKKSGGHYTYILEVFGPLPAFVRVWVELLIIRPAATAVISLAFGRYILEPFFIQCEIPELAIKLITAVGITVVMVLNSMSVSWSARIQIFLTFCKLTAILIIIVPGVMQLIKGQTQNFKDAFSGRDSSITRLPLAFYYGMYAYAGWFYLNFVTEEVENPEKTIPLAICISMAIVTIGYVLTNVAYFTTINAEELLLSNAVAVTFSERLLGNFSLAVPIFVALSCFGSMNGGVFAVSRLFYVASREGHLPEILSMIHVRKHTPLPAVIVLHPLTMIMLFSGDLDSLLNFLSFARWLFIGLAVAGLIYLRYKCPDMHRPFKVPLFIPALFSFTCLFMVALSLYSDPFSTGIGFVITLTGVPAYYLFIIWDKKPRWFRIMSEKITRTLQIILEVVPEEDKL TTBZMIO TT Clinical trial TTBZMIO FM Amino acid-polyamine-organocation TT0F26C ID TT0F26C TT0F26C TN Cytochrome c oxidase copper chaperone (COX17) TT0F26C UP Q14061 TT0F26C UC COX17_HUMAN TT0F26C SN Cytochrome c oxidase assembly protein COX17; COX17; CCO assembly protein COX17 TT0F26C GN COX17 TT0F26C FC Copper chaperone for cytochromec oxidase (COX). Binds two copper ions and deliver them to the Cu(A) site of COX. TT0F26C PD 2RNB; 2RN9; 2LGQ; 2L0Y TT0F26C SQ MPGLVDSNPAPPESQEKKPLKPCCACPETKKARDACIIEKGEEHCGHLIEAHKECMRALGFKI TT0F26C TT Literature-reported TTXLYW2 ID TTXLYW2 TTXLYW2 TN Cytochrome P450 4f (P450-4F) TTXLYW2 UP P78329; Q08477 TTXLYW2 UC CP4F2_HUMAN; CP4F3_HUMAN TTXLYW2 BC Paired donor oxygen oxidoreductase TTXLYW2 SN Leukotriene-B(4) omega-hydroxylase; Leukotriene-B(4) 20-monooxygenase; Cytochrome P450-LTB-omega; CYPIVF; 20-hydroxyeicosatetraenoic acid synthase; 20-HETE synthase TTXLYW2 GN CYP4F2; CYP4F3 TTXLYW2 FC Hydroxylates arachidonic acid (20:4n-6) to (18R)- hydroxyarachidonate. Shows little activity against prostaglandin (PG) D2, PGE1, PGE2, PGF2alpha, and leukotriene B4. Catalyzes omega-2 and omega-3-hydroxylation of PGH1 and PGH2. Catalyzes epoxidation of 4,7,10,13,16,19-(Z)-docosahexaenoic acid (22:6n-3) and 7,10,13,16,19-(Z)-docosapentaenoic acid (22:5n-3) and omega-3- hydroxylation of 4,7,10,13,16-(Z)-docosapentaenoic acid (22:5n-6). Catalyzes hydroxylation of PGI2 and carbaprostacyclin. TTXLYW2 SQ MSQLSLSWLGLWPVAASPWLLLLLVGASWLLAHVLAWTYAFYDNCRRLRCFPQPPRRNWFWGHQGMVNPTEEGMRVLTQLVATYPQGFKVWMGPISPLLSLCHPDIIRSVINASAAIAPKDKFFYSFLEPWLGDGLLLSAGDKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQLLASEGSACLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVSKRHHEILLHIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFIDVLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQELLKDREPKEIEWDDLAHLPFLTMCMKESLRLHPPVPVISRHVTQDIVLPDGRVIPKGIICLISVFGTHHNPAVWPDPEVYDPFRFDPENIKERSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS TTXLYW2 TT Literature-reported TT6YF5K ID TT6YF5K TT6YF5K TN Cytokine receptor-like factor 1 (CRLF1) TT6YF5K UP O75462 TT6YF5K UC CRLF1_HUMAN TT6YF5K BC Type I cytokine receptor family. Type 3 subfamily TT6YF5K SN ZcytoR5; Cytokine-like factor 1; CLF-1 TT6YF5K GN CRLF1 TT6YF5K FC Cytokine receptor subunit, possibly playing a regulatory role in the immune system and during fetal development. May be involved in nervous system development. TT6YF5K SQ MPAGRRGPAAQSARRPPPLLPLLLLLCVLGAPRAGSGAHTAVISPQDPTLLIGSSLLATCSVHGDPPGATAEGLYWTLNGRRLPPELSRVLNASTLALALANLNGSRQRSGDNLVCHARDGSILAGSCLYVGLPPEKPVNISCWSKNMKDLTCRWTPGAHGETFLHTNYSLKYKLRWYGQDNTCEEYHTVGPHSCHIPKDLALFTPYEIWVEATNRLGSARSDVLTLDILDVVTTDPPPDVHVSRVGGLEDQLSVRWVSPPALKDFLFQAKYQIRYRVEDSVDWKVVDDVSNQTSCRLAGLKPGTVYFVQVRCNPFGIYGSKKAGIWSEWSHPTAASTPRSERPGPGGGACEPRGGEPSSGPVRRELKQFLGWLKKHAYCSNLSFRLYDQWRAWMQKSHKTRNQDEGILPSGRRGTARGPAR TT6YF5K TT Literature-reported TT5UHA6 ID TT5UHA6 TT5UHA6 TN Cytomegalovirus Immediate-early protein messenger RNA (CMV IE mRNA) TT5UHA6 UP P03169; Q6SWP7; P06434 TT5UHA6 UC VIE1_HCMVT; VIE2_HCMVT; VIE3_HCMVT TT5UHA6 BC mRNA target TT5UHA6 SN Human cytomegalovirus immediate-early protein (mRNA) TT5UHA6 GN CMV IE mRNA TT5UHA6 FC Alters host cell cycle progression, probably through its interaction with host E2F1 or RB1 that overcomes the RB1-mediated repression of E2F-responsive promoters. Plays an important role in transactivating viral early genes as well as activating its own promoter. Targets and disrupts host PML/nuclear domain 10 (ND10). Promotes efficient viral growth by interacting with and directing host SP100 to degradation, leading to enhanced acetylation level of histones. In addition, functions in counteracting the host innate antiviral response. Inhibits the type I interferon pathway by directly interacting with and sequestrating host STAT2. TT5UHA6 SQ MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFERVTEDCNENPEKDVLAELVKQIKVRVDMVRHRIKEHMLKKYTQTEEKFTGAFNMMGGCLQNALDILDKVHEPFEEMKCIGLTMQSMYENYIVPEDKREMWMACIKELHDVSKGAANKLGGALQAKARAKKDELRRKMMYMCYRNIEFFTKNSAFPKTTNGCSQAMAALQNLPQCSPDEIMAYAQKIFKILDEERDKVLTHIDHIFMDILTTCVETMCNEYKVTSDACMMTMYGGISLLSEFCRVLSCYVLEETSVMLAKRPLITKPEVISVMKRRIEEICMKVFAQYILGADPLRVCSPSVDDLRAIAEESDEEEAIVAYTLATRGASSSDSLVSPPESPVPATIPLSSVIVAENSDQEESEQSDEEEEEGAQEEREDTVSVKSEPVSEIEEVAPEEEEDGAEEPTASGGKSTHPMVTRSKADQ TT5UHA6 TT Literature-reported TT5UHA6 FM mRNA target TT8396I ID TT8396I TT8396I TN DDB1- and CUL4-associated factor 2 (DTL) TT8396I UP Q9NZJ0 TT8396I UC DTL_HUMAN TT8396I SN Retinoic acid-regulated nuclear matrix-associated protein; RAMP; Lethal(2) denticleless protein homolog; L2DTL; Denticleless protein homolog; DCAF2; CDW1; CDT2 TT8396I GN DTL TT8396I FC Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2. CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication. CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing. KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration. Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis. The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1. TT8396I PD 6QC0 TT8396I SQ MLFNSVLRQPQLGVLRNGWSSQYPLQSLLTGYQCSGNDEHTSYGETGVPVPPFGCTFSSAPNMEHVLAVANEEGFVRLYNTESQSFRKKCFKEWMAHWNAVFDLAWVPGELKLVTAAGDQTAKFWDVKAGELIGTCKGHQCSLKSVAFSKFEKAVFCTGGRDGNIMVWDTRCNKKDGFYRQVNQISGAHNTSDKQTPSKPKKKQNSKGLAPSVDFQQSVTVVLFQDENTLVSAGAVDGIIKVWDLRKNYTAYRQEPIASKSFLYPGSSTRKLGYSSLILDSTGSTLFANCTDDNIYMFNMTGLKTSPVAIFNGHQNSTFYVKSSLSPDDQFLVSGSSDEAAYIWKVSTPWQPPTVLLGHSQEVTSVCWCPSDFTKIATCSDDNTLKIWRLNRGLEEKPGGDKLSTVGWASQKKKESRPGLVTVTSSQSTPAKAPRAKCNPSNSSPSSAACAPSCAGDLPLPSNTPTFSIKTSPAKARSPINRRGSVSSVSPKPPSSFKMSIRNWVTRTPSSSPPITPPASETKIMSPRKALIPVSQKSSQAEACSESRNRVKRRLDSSCLESVKQKCVKSCNCVTELDGQVENLHLDLCCLAGNQEDLSKDSLGPTKSSKIEGAGTSISEPPSPISPYASESCGTLPLPLRPCGEGSEMVGKENSSPENKNWLLAMAAKRKAENPSPRSPSSQTPNSRRQSGKKLPSPVTITPSSMRKICTYFHRKSQEDFCGPEHSTEL TT8396I TT Literature-reported TT8UA0T ID TT8UA0T TT8UA0T TN Death receptor 6 (CD358) TT8UA0T UP O75509 TT8UA0T UC TNR21_HUMAN TT8UA0T SN UNQ437/PRO868; Tumor necrosis factor receptor superfamily member 21; DR6 TT8UA0T GN TNFRSF21 TT8UA0T FC Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21; this triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Negatively regulates oligodendrocyte survival, maturation and myelination. Plays a role in signaling cascades triggered by stimulation of T-cell receptors, in the adaptive immune response and in the regulation of T-cell differentiation and proliferation. Negatively regulates T-cell responses and the release of cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively regulates the production of IgG, IgM and IgM in response to antigens. May inhibit the activation of JNK in response to T-cell stimulation. Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. TT8UA0T PD 3U3V; 3U3T; 3U3S; 3U3Q; 3U3P TT8UA0T SQ MGTSPSSSTALASCSRIARRATATMIAGSLLLLGFLSTTTAQPEQKASNLIGTYRHVDRATGQVLTCDKCPAGTYVSEHCTNTSLRVCSSCPVGTFTRHENGIEKCHDCSQPCPWPMIEKLPCAALTDRECTCPPGMFQSNATCAPHTVCPVGWGVRKKGTETEDVRCKQCARGTFSDVPSSVMKCKAYTDCLSQNLVVIKPGTKETDNVCGTLPSFSSSTSPSPGTAIFPRPEHMETHEVPSSTYVPKGMNSTESNSSASVRPKVLSSIQEGTVPDNTSSARGKEDVNKTLPNLQVVNHQQGPHHRHILKLLPSMEATGGEKSSTPIKGPKRGHPRQNLHKHFDINEHLPWMIVLFLLLVLVVIVVCSIRKSSRTLKKGPRQDPSAIVEKAGLKKSMTPTQNREKWIYYCNGHGIDILKLVAAQVGSQWKDIYQFLCNASEREVAAFSNGYTADHERAYAALQHWTIRGPEASLAQLISALRQHRRNDVVEKIRGLMEDTTQLETDKLALPMSPSPLSPSPIPSPNAKLENSALLTVEPSPQDKNKGFFVDESEPLLRCDSTSSGSSALSRNGSFITKEKKDTVLRQVRLDPCDLQPIFDDMLHFLNPEELRVIEEIPQAEDKLDRLFEIIGVKSQEASQTLLDSVYSHLPDLL TT8UA0T TT Literature-reported TT1NMGV ID TT1NMGV TT1NMGV TN DEK protein (DEK) TT1NMGV UP P35659 TT1NMGV UC DEK_HUMAN TT1NMGV SN Protein DEK TT1NMGV GN DEK TT1NMGV FC Involved in chromatin organization. TT1NMGV PD 2JX3; 1Q1V TT1NMGV SQ MSASAPAAEGEGTPTQPASEKEPEMPGPREESEEEEDEDDEEEEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTIAQGKGQKLCEIERIHFFLSKKKTDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSVQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKTCSKGSKKERNSSGMARKAKRTKCPEILSDESSSDEDEKKNKEESSDDEDKESEEEPPKKTAKREKPKQKATSKSKKSVKSANVKKADSSTTKKNQNSSKKESESEDSSDDEPLIKKLKKPPTDEELKETIKKLLASANLEEVTMKQICKKVYENYPTYDLTERKDFIKTTVKELIS TT1NMGV TT Literature-reported TT9CFQD ID TT9CFQD TT9CFQD TN Delta-like protein 1 (DLL1) TT9CFQD UP O00548 TT9CFQD UC DLL1_HUMAN TT9CFQD SN H-Delta-1; Drosophila Delta homolog 1; Delta1 TT9CFQD GN DLL1 TT9CFQD FC Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 receptors that binds the extracellular domain (ECD) of Notch receptor in a cis and trans fashion manner. Following transinteraction, ligand cells produce mechanical force that depends of a clathrin-mediated endocytosis, requiring ligand ubiquitination, EPN1 interaction, and actin polymerisation; these events promote Notch receptor extracellular domain (NECD) transendocytosis and triggers Notch signaling through induction of cleavage, hyperphosphorylation, and nuclear accumulation of the intracellular domain of Notch receptors (NICD) (By similarity). Is required for embryonic development and maintenance of adult stem cells in many different tissues and immune systeme; the DLL1-induced Notch signaling is mediated through an intercellular communication that regulates cell lineage, cell specification, cell patterning and morphogenesis through effects on differentiation and proliferation. Plays a role in brain development at different level, namely by regulating neuronal differentiation of neural precursor cells via cell-cell interaction, most likely through the lateral inhibitory system in an endogenous level dependent-manner. During neocortex development, Dll1-Notch signaling transmission is mediated by dynamic interactions between intermediate neurogenic progenitors and radial glia; the cell-cell interactions are mediated via dynamic and transient elongation processes, likely to reactivate/maintain Notch activity in neighboring progenitors, and coordinate progenitor cell division and differentiation across radial and zonal boundaries. During cerebellar development, regulates Bergmann glial monolayer formation and its morphological maturation through a Notch signaling pathway. At the retina and spinal cord level, regulates neurogenesis by preventing the premature differentiation of neural progenitors and also by maintaining progenitors in spinal cord through Notch signaling pathway. Also controls neurogenesis of the neural tube in a progenitor domain-specific fashion along the dorsoventral axis. Maintains quiescence of neural stem cells and plays a role as a fate determinant that segregates asymmetrically to one daughter cell during neural stem cells mitosis, resulting in neuronal differentiation in Dll1-inheriting cell. Plays a role in immune systeme development, namely the development of all T-cells and marginal zone (MZ) B-cells (By similarity). Blocks the differentiation of progenitor cells into the B-cell lineage while promoting the emergence of a population of cells with the characteristics of a T-cell/NK-cell precursor. Also plays a role during muscle development. During early development, inhibits myoblasts differentiation from the medial dermomyotomal lip and later regulates progenitor cell differentiation. Directly modulates cell adhesion and basal lamina formation in satellite cells through Notch signaling. Maintains myogenic progenitors pool by suppressing differentiation through down-regulation of MYOD1 and is required for satellite cell homing and PAX7 expression. During craniofacial and trunk myogenesis suppresses differentiation of cranial mesoderm-derived and somite-derived muscle via MYOD1 regulation but in cranial mesoderm-derived progenitors, is neither required for satellite cell homing nor for PAX7 expression. Also plays a role during pancreatic cell development. During type B pancreatic cell development, may be involved in the initiation of proximodistal patterning in the early pancreatic epithelium. Stimulates multipotent pancreatic progenitor cells proliferation and pancreatic growth by maintaining HES1 expression and PTF1A protein levels. During fetal stages of development, is required to maintain arterial identity and the responsiveness of arterial endothelial cells for VEGFA through regulation of KDR activation and NRP1 expression. Controls sprouting angiogenesis and subsequent vertical branch formation througth regulation on tip cell differentiation. Negatively regulates goblet cell differentiation in intestine and controls secretory fat commitment through lateral inhibition in small intestine. Plays a role during inner ear development; negatively regulates auditory hair cell differentiation. Plays a role during nephron development through Notch signaling pathway. Regulates growth, blood pressure and energy homeostasis (By similarity). TT9CFQD PD 4XBM TT9CFQD SQ MGSRCALALAVLSALLCQVWSSGVFELKLQEFVNKKGLLGNRNCCRGGAGPPPCACRTFFRVCLKHYQASVSPEPPCTYGSAVTPVLGVDSFSLPDGGGADSAFSNPIRFPFGFTWPGTFSLIIEALHTDSPDDLATENPERLISRLATQRHLTVGEEWSQDLHSSGRTDLKYSYRFVCDEHYYGEGCSVFCRPRDDAFGHFTCGERGEKVCNPGWKGPYCTEPICLPGCDEQHGFCDKPGECKCRVGWQGRYCDECIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCKNGATCTNTGQGSYTCSCRPGYTGATCELGIDECDPSPCKNGGSCTDLENSYSCTCPPGFYGKICELSAMTCADGPCFNGGRCSDSPDGGYSCRCPVGYSGFNCEKKIDYCSSSPCSNGAKCVDLGDAYLCRCQAGFSGRHCDDNVDDCASSPCANGGTCRDGVNDFSCTCPPGYTGRNCSAPVSRCEHAPCHNGATCHERGHRYVCECARGYGGPNCQFLLPELPPGPAVVDLTEKLEGQGGPFPWVAVCAGVILVLMLLLGCAAVVVCVRLRLQKHRPPADPCRGETETMNNLANCQREKDISVSIIGATQIKNTNKKADFHGDHSADKNGFKARYPAVDYNLVQDLKGDDTAVRDAHSKRDTKCQPQGSSGEEKGTPTTLRGGEASERKRPDSGCSTSKDTKYQSVYVISEEKDECVIATEV TT9CFQD TT Literature-reported TTQ02HK ID TTQ02HK TTQ02HK TN Dendritic cell-associated C-type lectin 2 (CLEC6A) TTQ02HK UP Q6EIG7 TTQ02HK UC CLC6A_HUMAN TTQ02HK SN Dectin-2; DECTIN2; DC-associated C-type lectin 2; CLECSF10; C-type lectin superfamily member 10; C-type lectin domain family 6 member A TTQ02HK GN CLEC6A TTQ02HK FC Binds high-mannose carbohydrates in a Ca(2+)-dependent manner. Functional receptor for alpha-mannans on C.albicans hypheas. Plays an important role in the host defense against C.albicans infection by inducing TH17 cell differentiation. Recognizes also, in a mannose-dependent manner, allergens from house dust mite and fungi, by promoting cysteinyl leukotriene production. Recognizes soluble elements from the eggs of Shistosoma mansoni altering adaptive immune responses. Transduces signals through an Fc receptor gamma chain /FCER1G and Syk-CARD9-NF-kappa-B-dependent pathway (By similarity). TTQ02HK PD 5VYB TTQ02HK SQ MMQEQQPQSTEKRGWLSLRLWSVAGISIALLSACFIVSCVVTYHFTYGETGKRLSELHSYHSSLTCFSEGTKVPAWGCCPASWKSFGSSCYFISSEEKVWSKSEQNCVEMGAHLVVFNTEAEQNFIVQQLNESFSYFLGLSDPQGNNNWQWIDKTPYEKNVRFWHLGEPNHSAEQCASIVFWKPTGWGWNDVICETRRNSICEMNKIYL TTQ02HK TT Literature-reported TTMYZNX ID TTMYZNX TTMYZNX TN Dengue virus Envelope (DENV E) TTMYZNX UP P17763 (281-775) TTMYZNX UC POLG_DEN1W (281-775) TTMYZNX GN DENV E TTMYZNX TT Preclinical TTNEYST ID TTNEYST TTNEYST TN Dengue virus NS2B/NS3 protease (DENV NS2B/NS3) TTNEYST UP P29990 TTNEYST UC POLG_DEN26 TTNEYST SN Genome polyprotein TTNEYST GN DENV NS2B/NS3 TTNEYST FC Capsid protein C: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. TTNEYST PD 4O6B; 2R69 TTNEYST SQ MNDQRKKAKNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLYMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRSAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCEDTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCTTMGEHRRQKRSVALVPHVGMGLETRTETWMSSEGAWKHVQRIETWILRHPGFTMMAAILAYTIGTTHFQRALIFILLTAVTPSMTMRCIGMSNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFRCKKNMEGKVVQPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSTTEAELTGYGTVTMECSPRTGLDFNEMVLLQMENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVTLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFITDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITPELNHILSENEVKLTIMTGDIKGIMQAGKRSLRPQPTELKYSWKTWGKAKMLSTESHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLKEKQDVFCDSKLMSAAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKNCHWPKSHTLWSNGVLESEMIIPKNLAGPVSQHNYRPGYHTQITGPWHLGKLEMDFDFCDGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVNSLVTAGHGQVDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLIIGNMSFRDLGRVMVMVGATMTDDIGMGVTYLALLAAFKVRPTFAAGLLLRKLTSKALMMTTIGIVLSSQSTTPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAILCVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKTDWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVSILASSLLKNDIPMTGPLVAGGPLTVCYVLTGRSADLELERAADVKWEDQAEISGSSPILSITISEDGSMSIKNEEEEQTLTILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPMGKAELEDGAYRIKQKGILGYSQIGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFKTNAGTIGAVSLDFSPGTSGSPIIDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIIDEEREIPERSWNSGHEWVTDFKGKTVWFVPSIKAGNDIAACLSKNGKKVIQLSRKTFDSEYAKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAGPMPVTHSSAAQRRGRIGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRLRGEARTTFVDLMRRGDLPVWLAYRVAAEGINYADRRWCFDGVKNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPLALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGGILLFLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAATMANEMGFLEKTKKDLGLGSIATQQPESNILDIDLRPASAWTLYAVATTFVTPMLRHSIENSSVNVSLTAIANQATVLMGLGKGWPLSKMDIGVPLLAIGCYSQVNPTTLTAALFLLVAHYAIIGPALQAKASREAQKRAAAGIMKNPTVDGITVIDLDPIPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEVLTLATGPISTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLFSIMKNTTNARRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNMVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFIPPEKCDTLLCDIGESSPNPTVEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMEALQRKYGGALVRNPLSRNSTHEMYWVSNASGNIVSSVNMISRMLINRFTMRYKKATYEPDVDLGSGTRNIGIESEIPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSYETKQTGSASSMVNGVFRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNIMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKNEAMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVFKSIQHLTITEEIAVQNWLARVGRERLSRMAISGDDCVVKPLDDRLPSALTALNDTGKIRKDIQQWEPSRGWNDWTQVPFCSHHFHELIMKDGRVLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYDQMWSLMYFHRRDLRLAANAICSAVPSHWVPTSRTTWSIHAKHEWMTTEDMLTVWNRVWIQENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQAAINQVRSLIGNEEYTDYMPSMKRFRREEEEAGVLW TTNEYST TT Literature-reported TT8S9CM ID TT8S9CM TT8S9CM TN DEP domain-containing protein 1A (DEPDC1) TT8S9CM UP Q5TB30 TT8S9CM UC DEP1A_HUMAN TT8S9CM SN DEPDC1A TT8S9CM GN DEPDC1 TT8S9CM FC May be involved in transcriptional regulation as a transcriptional corepressor. The DEPDC1A-ZNF224 complex may play a critical role in bladder carcinogenesis by repressing the transcription of the A20 gene, leading to transport of NF-KB protein into the nucleus, resulting in suppression of apoptosis of bladder cancer cells. TT8S9CM PD 2YSR TT8S9CM SQ MESQGVPPGPYRATKLWNEVTTSFRAGMPLRKHRQHFKKYGNCFTAGEAVDWLYDLLRNNSNFGPEVTRQQTIQLLRKFLKNHVIEDIKGRWGSENVDDNNQLFRFPATSPLKTLPRRYPELRKNNIENFSKDKDSIFKLRNLSRRTPKRHGLHLSQENGEKIKHEIINEDQENAIDNRELSQEDVEEVWRYVILIYLQTILGVPSLEEVINPKQVIPQYIMYNMANTSKRGVVILQNKSDDLPHWVLSAMKCLANWPRSNDMNNPTYVGFERDVFRTIADYFLDLPEPLLTFEYYELFVNILVVCGYITVSDRSSGIHKIQDDPQSSKFLHLNNLNSFKSTECLLLSLLHREKNKEESDSTERLQISNPGFQERCAKKMQLVNLRNRRVSANDIMGGSCHNLIGLSNMHDLSSNSKPRCCSLEGIVDVPGNSSKEASSVFHQSFPNIEGQNNKLFLESKPKQEFLLNLHSEENIQKPFSAGFKRTSTLTVQDQEELCNGKCKSKQLCRSQSLLLRSSTRRNSYINTPVAEIIMKPNVGQGSTSVQTAMESELGESSATINKRLCKSTIELSENSLLPASSMLTGTQSLLQPHLERVAIDALQLCCLLLPPPNRRKLQLLMRMISRMSQNVDMPKLHDAMGTRSLMIHTFSRCVLCCAEEVDLDELLAGRLVSFLMDHHQEILQVPSYLQTAVEKHLDYLKKGHIENPGDGLFAPLPTYSYCKQISAQEFDEQKVSTSQAAIAELLENIIKNRSLPLKEKRKKLKQFQKEYPLIYQKRFPTTESEAALFGDKPTIKQPMLILRKPKFRSLR TT8S9CM TT Literature-reported TTLYP6D ID TTLYP6D TTLYP6D TN DEP domain-containing protein 6 (DEPTOR) TTLYP6D UP Q8TB45 TTLYP6D UC DPTOR_HUMAN TTLYP6D SN DEPDC6 TTLYP6D GN DEPTOR TTLYP6D FC Negative regulator of the mTORC1 and mTORC2 signaling pathways. Inhibits the kinase activity of both complexes. TTLYP6D SQ MEEGGSTGSAGSDSSTSGSGGAQQRELERMAEVLVTGEQLRLRLHEEKVIKDRRHHLKTYPNCFVAKELIDWLIEHKEASDRETAIKLMQKLADRGIIHHVCDEHKEFKDVKLFYRFRKDDGTFPLDNEVKAFMRGQRLYEKLMSPENTLLQPREEEGVKYERTFMASEFLDWLVQEGEATTRKEAEQLCHRLMEHGIIQHVSNKHPFVDSNLLYQFRMNFRRRRRLMELLNEKSPSSQETHDSPFCLRKQSHDNRKSTSFMSVSPSKEIKIVSAVRRSSMSSCGSSGYFSSSPTLSSSPPVLCNPKSVLKRPVTSEELLTPGAPYARKTFTIVGDAVGWGFVVRGSKPCHIQAVDPSGPAAAAGMKVCQFVVSVNGLNVLHVDYRTVSNLILTGPRTIVMEVMEELEC TTLYP6D TT Literature-reported TTLYP6D KE hsa04140:Autophagy - animal; hsa04150:mTOR signaling pathway TTEO4P8 ID TTEO4P8 TTEO4P8 TN Desmoglein-3 (DSG3) TTEO4P8 UP P32926 TTEO4P8 UC DSG3_HUMAN TTEO4P8 SN PVA; DSG3; Cadherin family member 6; 130 kDa pemphigus vulgaris antigen TTEO4P8 GN DSG3 TTEO4P8 FC Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. TTEO4P8 PD 5EQX TTEO4P8 SQ MMGLFPRTTGALAIFVVVILVHGELRIETKGQYDEEEMTMQQAKRRQKREWVKFAKPCREGEDNSKRNPIAKITSDYQATQKITYRISGVGIDQPPFGIFVVDKNTGDINITAIVDREETPSFLITCRALNAQGLDVEKPLILTVKILDINDNPPVFSQQIFMGEIEENSASNSLVMILNATDADEPNHLNSKIAFKIVSQEPAGTPMFLLSRNTGEVRTLTNSLDREQASSYRLVVSGADKDGEGLSTQCECNIKVKDVNDNFPMFRDSQYSARIEENILSSELLRFQVTDLDEEYTDNWLAVYFFTSGNEGNWFEIQTDPRTNEGILKVVKALDYEQLQSVKLSIAVKNKAEFHQSVISRYRVQSTPVTIQVINVREGIAFRPASKTFTVQKGISSKKLVDYILGTYQAIDEDTNKAASNVKYVMGRNDGGYLMIDSKTAEIKFVKNMNRDSTFIVNKTITAEVLAIDEYTGKTSTGTVYVRVPDFNDNCPTAVLEKDAVCSSSPSVVVSARTLNNRYTGPYTFALEDQPVKLPAVWSITTLNATSALLRAQEQIPPGVYHISLVLTDSQNNRCEMPRSLTLEVCQCDNRGICGTSYPTTSPGTRYGRPHSGRLGPAAIGLLLLGLLLLLLAPLLLLTCDCGAGSTGGVTGGFIPVPDGSEGTIHQWGIEGAHPEDKEITNICVPPVTANGADFMESSEVCTNTYARGTAVEGTSGMEMTTKLGAATESGGAAGFATGTVSGAASGFGAATGVGICSSGQSGTMRTRHSTGGTNKDYADGAISMNFLDSYFSQKAFACAEEDDGQEANDCLLIYDNEGADATGSPVGSVGCCSFIADDLDDSFLDSLGPKFKKLAEISLGVDGEGKEVQPPSKDSGYGIESCGHPIEVQQTGFVKCQTLSGSQGASALSTSGSVQPAVSIPDPLQHGNYLVTETYSASGSLVQPSTAGFDPLLTQNVIVTERVICPISSVPGNLAGPTQLRGSHTMLCTEDPCSRLI TTEO4P8 TT Literature-reported TTB4ZEN ID TTB4ZEN TTB4ZEN TN Development and differentiation-enhancing factor-like 1 (DDEFL1) TTB4ZEN UP Q8TDY4 TTB4ZEN UC ASAP3_HUMAN TTB4ZEN SN UPLC1; Protein up-regulated in liver cancer 1; DDEFL1; Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 TTB4ZEN GN ASAP3 TTB4ZEN FC Promotes cell proliferation. TTB4ZEN PD 3LVR; 3LVQ; 2B0O TTB4ZEN SQ MPEQFSVAEFLAVTAEDLSSPAGAAAFAAKMPRYRGAALAREEILEGDQAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLGNSHLSQNSHELSTGFLNLAVFTREVAALFKNLIQNLNNIVSFPLDSLMKGQLRDGRQDSKKQLEKAWKDYEAKMAKLEKERDRARVTGGIPGEVAQDMQRERRIFQLHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPFIEKLAASVHALHQAQEDELQKLTQLRDSLRGTLQLESREEHLSRKNSGCGYSIHQHQGNKQFGTEKVGFLYKKSDGIRRVWQKRKCGVKYGCLTISHSTINRPPVKLTLLTCQVRPNPEEKKCFDLVTHNRTYHFQAEDEHECEAWVSVLQNSKDEALSSAFLGEPSAGPGSWGSAGHDGEPHDLTKLLIAEVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTSFNEVMEAQLPSHGGPKPSAESDMGTRRDYIMAKYVEHRFARRCTPEPQRLWTAICNRDLLSVLEAFANGQDFGQPLPGPDAQAPEELVLHLAVKVANQASLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARKKHHKECEELLEQAQAGTFAFPLHVDYSWVISTEPGSDSEEDEEEKRCLLKLPAQAHWASGRLDISNKTYETVASLGAATPQGESEDCPPPLPVKNSSRTLVQGCARHASGDRSEVSSLSSEAPETPESLGSPASSSSLMSPLEPGDPSQAPPNSEEGLREPPGTSRPSLTSGTTPSEMYLPVRFSSESTRSYRRGARSPEDGPSARQPLPRRNVPVGITEGDGSRTGSLPASSVQLLQD TTB4ZEN TT Literature-reported TTXZDEN ID TTXZDEN TTXZDEN TN Diacylglycerol lipase beta (DAGLB) TTXZDEN UP Q8NCG7 TTXZDEN UC DGLB_HUMAN TTXZDEN SN Sn1-specific diacylglycerol lipase beta; KCCR13L; DGL-beta TTXZDEN GN DAGLB TTXZDEN FC Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses. TTXZDEN EC EC 3.1.1.- TTXZDEN SQ MPGMVLFGRRWAIASDDLVFPGFFELVVRVLWWIGILTLYLMHRGKLDCAGGALLSSYLIVLMILLAVVICTVSAIMCVSMRGTICNPGPRKSMSKLLYIRLALFFPEMVWASLGAAWVADGVQCDRTVVNGIIATVVVSWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDCCRSRTTDYDLVGGDQLNCHFGSILHTTGLQYRDFIHVSFHDKVYELPFLVALDHRKESVVVAVRGTMSLQDVLTDLSAESEVLDVECEVQDRLAHKGISQAARYVYQRLINDGILSQAFSIAPEYRLVIVGHSLGGGAAALLATMLRAAYPQVRCYAFSPPRGLWSKALQEYSQSFIVSLVLGKDVIPRLSVTNLEDLKRRILRVVAHCNKPKYKILLHGLWYELFGGNPNNLPTELDGGDQEVLTQPLLGEQSLLTRWSPAYSFSSDSPLDSSPKYPPLYPPGRIIHLQEEGASGRFGCCSAAHYSAKWSHEAEFSKILIGPKMLTDHMPDILMRALDSVVSDRAACVSCPAQGVSSVDVA TTXZDEN TT Literature-reported TTST5KX ID TTST5KX TTST5KX TN Dickkopf-related protein 2 (DKK2) TTST5KX UP Q9UBU2 TTST5KX UC DKK2_HUMAN TTST5KX BC Dickkopf protein TTST5KX SN hDkk2; hDkk-2; UNQ682/PRO1316; Dkk2; Dkk-2; Dickkopfrelated protein 2; Dickkopf2; Dickkopf-2 TTST5KX GN DKK2 TTST5KX FC DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. TTST5KX SQ MAALMRSKDSSCCLLLLAAVLMVESSQIGSSRAKLNSIKSSLGGETPGQAANRSAGMYQGLAFGGSKKGKNLGQAYPCSSDKECEVGRYCHSPHQGSSACMVCRRKKKRCHRDGMCCPSTRCNNGICIPVTESILTPHIPALDGTRHRDRNHGHYSNHDLGWQNLGRPHTKMSHIKGHEGDPCLRSSDCIEGFCCARHFWTKICKPVLHQGEVCTKQRKKGSHGLEIFQRCDCAKGLSCKVWKDATYSSKARLHVCQKI TTST5KX TT Literature-reported TTST5KX FM Dickkopf family TTN74LE ID TTN74LE TTN74LE TN Direct IAP-binding protein with low pI (DIABLO) TTN74LE UP Q9NR28 TTN74LE UC DBLOH_HUMAN TTN74LE SN Smac protein; Smac; Second mitochondria-derived activator of caspase; Direct IAP binding protein with low pI; Diablo homolog, mitochondrial TTN74LE GN DIABLO TTN74LE FC Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance. Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. TTN74LE PD 4TX5; 3UIJ; 3UIH; 3D9U; 1XB1 TTN74LE SQ MAALKSWLSRSVTSFFRYRQCLCVPVVANFKKRCFSELIRPWHKTVTIGFGVTLCAVPIAQKSEPHSLSSEALMRRAVSLVTDSTSTFLSQTTYALIEAITEYTKAVYTLTSLYRQYTSLLGKMNSEEEDEVWQVIIGARAEMTSKHQEYLKLETTWMTAVGLSEMAAEAAYQTGADQASITARNHIQLVKLQVEEVHQLSRKAETKLAEAQIEELRQKTQEEGEERAESEQEAYLRED TTN74LE TT Literature-reported TTYVQ9C ID TTYVQ9C TTYVQ9C TN DNA fragmentation factor alpha (DFFA) TTYVQ9C UP O00273 TTYVQ9C UC DFFA_HUMAN TTYVQ9C SN Inhibitor of caspase-3-activated Dnase; Inhibitor of CAD; ICAD; H13; DNA fragmentation factor subunit alpha; DNA fragmentation factor 45 kDa subunit; DFF45; DFF1; DFF-45 TTYVQ9C GN DFFA TTYVQ9C FC Inhibitor of the caspase-activated DNase (DFF40). TTYVQ9C PD 1KOY; 1IYR; 1IBX TTYVQ9C SQ MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQLKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLDQREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRETSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLRSISASKASPPGDLQNPKRARQDPT TTYVQ9C TT Literature-reported TTISG27 ID TTISG27 TTISG27 TN DNA mismatch repair protein Mlh1 (MLH1) TTISG27 UP P40692 TTISG27 UC MLH1_HUMAN TTISG27 SN MutL protein homolog 1; COCA2 TTISG27 GN MLH1 TTISG27 FC DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis. Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). TTISG27 PD 5U5P; 4P7A; 3RBN TTISG27 SQ MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIRKQYISEESTLSGQQSEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC TTISG27 TT Literature-reported TTCAWRT ID TTCAWRT TTCAWRT TN DNA mismatch repair protein MSH2 (MSH2) TTCAWRT UP P43246 TTCAWRT UC MSH2_HUMAN TTCAWRT SN hMSH2; MutS protein homolog 2; Mismatch repair gene Msh2 TTCAWRT GN MSH2 TTCAWRT FC Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Recruits DNA helicase MCM9 to chromatin which unwinds the mismatch containg DNA strand. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis. Component of the post-replicative DNA mismatch repair system (MMR). TTCAWRT PD 3THZ; 3THY; 3THX; 3THW; 2O8F TTCAWRT SQ MAVQPKETLQLESAAEVGFVRFFQGMPEKPTTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGAKNLQSVVLSKMNFESFVKDLLLVRQYRVEVYKNRAGNKASKENDWYLAYKASPGNLSQFEDILFGNNDMSASIGVVGVKMSAVDGQRQVGVGYVDSIQRKLGLCEFPDNDQFSNLEALLIQIGPKECVLPGGETAGDMGKLRQIIQRGGILITERKKADFSTKDIYQDLNRLLKGKKGEQMNSAVLPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELTTFDFSQYMKLDIAAVRALNLFQGSVEDTTGSQSLAALLNKCKTPQGQRLVNQWIKQPLMDKNRIEERLNLVEAFVEDAELRQTLQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPNVIQALEKHEGKHQKLLLAVFVTPLTDLRSDFSKFQEMIETTLDMDQVENHEFLVKPSFDPNLSELREIMNDLEKKMQSTLISAARDLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSKLTSLNEEYTKNKTEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAQLDAVVSFAHVSNGAPVPYVRPAILEKGQGRIILKASRHACVEVQDEIAFIPNDVYFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISEYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPKHVIECAKQKALELEEFQYIGESQGYDIMEPAAKKCYLEREQGEKIIQEFLSKVKQMPFTEMSEENITIKLKQLKAEVIAKNNSFVNEIISRIKVTT TTCAWRT TT Literature-reported TTX1ISF ID TTX1ISF TTX1ISF TN DNA mismatch repair protein PMS1 (PMS1) TTX1ISF UP P54277 TTX1ISF UC PMS1_HUMAN TTX1ISF SN PMSL1; PMS1 protein homolog 1 TTX1ISF GN PMS1 TTX1ISF FC Probably involved in the repair of mismatches in DNA. TTX1ISF PD 2CS1 TTX1ISF SQ MKQLPAATVRLLSSSQIITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTSKINSHEDLENLTTYGFRGEALGSICCIAEVLITTRTAADNFSTQYVLDGSGHILSQKPSHLGQGTTVTALRLFKNLPVRKQFYSTAKKCKDEIKKIQDLLMSFGILKPDLRIVFVHNKAVIWQKSRVSDHKMALMSVLGTAVMNNMESFQYHSEESQIYLSGFLPKCDADHSFTSLSTPERSFIFINSRPVHQKDILKLIRHHYNLKCLKESTRLYPVFFLKIDVPTADVDVNLTPDKSQVLLQNKESVLIALENLMTTCYGPLPSTNSYENNKTDVSAADIVLSKTAETDVLFNKVESSGKNYSNVDTSVIPFQNDMHNDESGKNTDDCLNHQISIGDFGYGHCSSEISNIDKNTKNAFQDISMSNVSWENSQTEYSKTCFISSVKHTQSENGNKDHIDESGENEEEAGLENSSEISADEWSRGNILKNSVGENIEPVKILVPEKSLPCKVSNNNYPIPEQMNLNEDSCNKKSNVIDNKSGKVTAYDLLSNRVIKKPMSASALFVQDHRPQFLIENPKTSLEDATLQIEELWKTLSEEEKLKYEEKATKDLERYNSQMKRAIEQESQMSLKDGRKKIKPTSAWNLAQKHKLKTSLSNQPKLDELLQSQIEKRRSQNIKMVQIPFSMKNLKINFKKQNKVDLEEKDEPCLIHNLRFPDAWLMTSKTEVMLLNPYRVEEALLFKRLLENHKLPAEPLEKPIMLTESLFNGSHYLDVLYKMTADDQRYSGSTYLSDPRLTANGFKIKLIPGVSITENYLEIEGMANCLPFYGVADLKEILNAILNRNAKEVYECRPRKVISYLEGEAVRLSRQLPMYLSKEDIQDIIYRMKHQFGNEIKECVHGRPFFHHLTYLPETT TTX1ISF TT Literature-reported TTGT87E ID TTGT87E TTGT87E TN DNA repair protein complementing XP-A cells (XPA) TTGT87E UP P23025 TTGT87E UC XPA_HUMAN TTGT87E SN Xeroderma pigmentosum group A-complementing protein; XPAC; XPA protein TTGT87E GN XPA TTGT87E FC Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation. Involved in DNA excision repair. TTGT87E PD 2JNW; 1XPA; 1D4U TTGT87E SQ MAAADGALPEAAALEQPAELPASVRASIERKRQRALMLRQARLAARPYSATAAAATGGMANVKAAPKIIDTGGGFILEEEEEEEQKIGKVVHQPGPVMEFDYVICEECGKEFMDSYLMNHFDLPTCDNCRDADDKHKLITKTEAKQEYLLKDCDLEKREPPLKFIVKKNPHHSQWGDMKLYLKLQIVKRSLEVWGSQEALEEAKEVRQENREKMKQKKFDKKVKELRRAVRSSVWKRETIVHQHEYGPEENLEDDMYRKTCTMCGHELTYEKM TTGT87E TT Literature-reported TTW8A5N ID TTW8A5N TTW8A5N TN DNA-binding protein inhibitor ID-2 (ID2) TTW8A5N UP Q02363 TTW8A5N UC ID2_HUMAN TTW8A5N SN bHLHb26; Inhibitor of differentiation 2; Inhibitor of DNA binding 2; Id2; Class B basic helix-loop-helix protein 26 TTW8A5N GN ID2 TTW8A5N FC Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Restricts the CLOCK and ARNTL/BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism. Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. TTW8A5N PD 4AYA TTW8A5N SQ MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQASRTPLTTLNTDISILSLQASEFPSELMSNDSKALCG TTW8A5N TT Literature-reported TTHMYB1 ID TTHMYB1 TTHMYB1 TN E2A-Pbx1 messenger RNA (E2A-Pbx1 mRNA) TTHMYB1 UP P15923-P40424 TTHMYB1 UC TFE2_HUMAN-PBX1_HUMAN TTHMYB1 BC mRNA target TTHMYB1 SN Transcription factor 3-Homeobox protein PRL (mRNA) TTHMYB1 GN TCF3-PBX1 TTHMYB1 FC E2A-PBX1 perturbs signaling pathways upstream of PLC2 and renders leukemias amenable to targeted therapeutic inhibition. TTHMYB1 SQ MNQPQRMAPVGTDKELSDLLDFSMMFPLPVTNGKGRPASLAGAQFGGSGLEDRPSSGSWGSGDQSSSSFDPSRTFSEGTHFTESHSSLSSSTFLGPGLGGKSGERGAYASFGRDAGVGGLTQAGFLSGELALNSPGPLSPSGMKGTSQYYPSYSGSSRRRAADGSLDTQPKKVRKVPPGLPSSVYPPSSGEDYGRDATAYPSAKTPSSTYPAPFYVADGSLHPSAELWSPPGQAGFGPMLGGGSSPLPLPPGSGPVGSSGSSSTFGGLHQHERMGYQLHGAEVNGGLPSASSFSSAPGATYGGVSSHTPPVSGADSLLGSRGTTAGSSGDALGKALASIYSPDHSSNNFSSSPSTPVGSPQGLAGTSQWPRAGAPGALSPSYDGGLHGLQSKIEDHLDEAIHVLRSHAVGTAGDMHTLLPGHGALASGFTGPMSLGGRHAGLVGGSHPEDGLAGSTSLMHNHAALPSQPGTLPDLSRPPDSYSGLGRAGATAAASEIKREEKEDEENTSAADHSEEEKKELKAPRARTSPDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLNSEKPQTKLLILHQAVSVILNLEQQVRERNLNPKAACLKRREEEKVSGVVGDPQMVLSAPHPGLSEAHNPAGHMMDEQPRLMHSHAGVGMAGHPGLSQHLQDGAGGTEGEGGRKQDIGDILQQIMTITDQSLDEAQARKHALNCHRMKPALFNVLCEIKEKTVLSIRGAQEEEPTDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGAGSDNSVEHSDYRAKLSQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVSIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFNKQATEILNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAAKTAVTATNVSAHGSQANSPSTPNSAGSSSSFNMSNSGDLFMSVQSLNGDSYQGAQVGANVQSQVDTLRHVISQTGGYSDGLAASQMYSPQGISANGGWQDATTPSSVTSPTEGPGSVHSDTSN TTHMYB1 TT Literature-reported TTHMYB1 FM mRNA target TTPQE9F ID TTPQE9F TTPQE9F TN Early activation antigen CD69 (CD69) TTPQE9F UP Q07108 TTPQE9F UC CD69_HUMAN TTPQE9F SN MLR3; Leukocyte surface antigen Leu23; GP32/28; Early Tcell activation antigen p60; EA1; Ctype lectin domain family 2 member C; CD69; BLAC/P26; Activation inducer molecule TTPQE9F GN CD69 TTPQE9F FC Involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets. TTPQE9F PD 3HUP; 3CCK; 1FM5; 1E8I; 1.00E+87 TTPQE9F SQ MSSENCFVAENSSLHPESGQENDATSPHFSTRHEGSFQVPVLCAVMNVVFITILIIALIALSVGQYNCPGQYTFSMPSDSHVSSCSEDWVGYQRKCYFISTVKRSWTSAQNACSEHGATLAVIDSEKDMNFLKRYAGREEHWVGLKKEPGHPWKWSNGKEFNNWFNVTGSDKCVFLKNTEVSSMECEKNLYWICNKPYK TTPQE9F TT Literature-reported TT92GY4 ID TT92GY4 TT92GY4 TN Echinoderm microtubule-associated protein-like 4 (EMAP-4) TT92GY4 UP Q9HC35 TT92GY4 UC EMAL4_HUMAN TT92GY4 SN Ropp 120; Restrictedly overexpressed proliferation-associated protein; EMAPL4; EMAP-4; C2orf2 TT92GY4 GN EML4 TT92GY4 FC May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. TT92GY4 PD 4CGC TT92GY4 SQ MDGFAGSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKKSVSSKGQPSPRAVIPMSCITNGSGANRKPSHTSAVSIAGKETLSSAAKSGTEKKKEKPQGQREKKEESHSNDQSPQIRASPSPQPSSQPLQIHRQTPESKNATPTKSIKRPSPAEKSHNSWENSDDSRNKLSKIPSTPKLIPKVTKTADKHKDVIINQEGEYIKMFMRGRPITMFIPSDVDNYDDIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGKIVYFIASVVVLFNYEERTQRHYLGHTDCVKCLAIHPDKIRIATGQIAGVDKDGRPLQPHVRVWDSVTLSTLQIIGLGTFERGVGCLDFSKADSGVHLCIIDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKYEKPKFVQCLAFLGNGDVLTGDSGGVMLIWSKTTVEPTPGKGPKGVYQISKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNPEREIEVPDQYGTIRAVAEGKADQFLVGTSRNFILRGTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTRLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLYVVSENGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEILYWDIPNGCKLIRNRSDCKDIDWTTYTCVLGFQVFGVWPEGSDGTDINALVRSHNRKVIAVADDFCKVHLFQYPCSKAKAPSHKYSAHSSHVTNVSFTHNDSHLISTGGKDMSIIQWKLVEKLSLPQNETVADTTLTKAPVSSTESVIQSNTPTPPPSQPLNETAEEESRISSSPTLLENSLEQTVEPSEDHSEEESEEGSGDLGEPLYEEPCNEISKEQAKATLLEDQQDPSPSS TT92GY4 TT Literature-reported TTFYBZ3 ID TTFYBZ3 TTFYBZ3 TN EIF protein kinase messenger RNA (EIFK mRNA) TTFYBZ3 UP Q9BQI3; P19525; P19525; Q9P2K8 TTFYBZ3 UC E2AK1_HUMAN; E2AK2_HUMAN; E2AK3_HUMAN; E2AK4_HUMAN TTFYBZ3 BC mRNA target TTFYBZ3 SN eIF-2A kinase; Eukaryotic translation initiation factor 2-alpha kinase TTFYBZ3 GN EIF2AK1; EIF2AK2; EIF2AK3; EIF2AK4 TTFYBZ3 FC A kinase enzyme that phosphorylates eIF-2. These are all responsible for the phosphorylation of the alpha subunit of eIF-2 at serine 51, one of the best-characterized mechanisms for down-regulating protein synthesis in eukaryotes in response to various cellular stress response's. TTFYBZ3 SQ MQGGNSGVRKREEEGDGAGAVAAPPAIDFPAEGPDPEYDESDVPAEIQVLKEPLQQPTFPFAVANQLLLVSLLEHLSHVHEPNPLRSRQVFKLLCQTFIKMGLLSSFTCSDEFSSLRLHHNRAITHLMRSAKERVRQDPCEDISRIQKIRSREVALEAQTSRYLNEFEELAILGKGGYGRVYKVRNKLDGQYYAIKKILIKGATKTVCMKVLREVKVLAGLQHPNIVGYHTAWIEHVHVIQPRADRAAIELPSLEVLSDQEEDREQCGVKNDESSSSSIIFAEPTPEKEKRFGESDTENQNNKSVKYTTNLVIRESGELESTLELQENGLAGLSASSIVEQQLPLRRNSHLEESFTSTEESSEENVNFLGQTEAQYHLMLHIQMQLCELSLWDWIVERNKRGREYVDESACPYVMANVATKIFQELVEGVFYIHNMGIVHRDLKPRNIFLHGPDQQVKIGDFGLACTDILQKNTDWTNRNGKRTPTHTSRVGTCLYASPEQLEGSEYDAKSDMYSLGVVLLELFQPFGTEMERAEVLTGLRTGQLPESLRKRCPVQAKYIQHLTRRNSSQRPSAIQLLQSELFQNSGNVNLTLQMKIIEQEKEIAELKKQLNLLSQDKGVRDDGKDGGVG TTFYBZ3 TT Literature-reported TTFYBZ3 FM mRNA target TTMJ862 ID TTMJ862 TTMJ862 TN Eimeria tenella Telomerase reverse transcriptase (EIMTE TERT) TTMJ862 UP D2Y0P7 TTMJ862 UC D2Y0P7_EIMTE TTMJ862 SN EIMTE Telomerase reverse transcriptase; EIMTE Telomerase catalytic subunit TTMJ862 GN EIMTE TERT TTMJ862 FC Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. TTMJ862 EC EC 2.7.7.49 TTMJ862 SQ MVLSKAGLVALKQMELVTGELYLEKQRKRIVKFEELGYNDSSGLERRLEELLITLDPSEPKAILEGFKLGRELLFNTSLDNLSDNGIDRKLRLINGEKLILWSSIELQNGYSSFPNQRSMSSSGRSRKNEYNTELSPTSFITDQIKNIIPDSEKDSLTYQVQDFELLLRKHFPRIRIFHSGSYSGLRTSFDTIKPKKYSFCNSTLYKFQNLHAWNTLLSKIGPIEILFLFVCCIIFRILGDHSEILIQQAGRMLTNDFLEELARLYETGPKTKNKFVSSSSVLTSPLTTIIEKEEVKPELDETERQVNKREPGGIIKSEDRLSKSIYILDIKPYLSTRFLCDHFYSRGGLPCKSLVRLLPPLLLGANRTLRFILQTDHIFIDHNRQSKLGLLGISEMTKYSRVFKKLASACMEEFQMNLLLIRNTNSPVNFLDQICPIEPKLIDDLSLQFNNKLPPCFEITSTRVVNFLSRYLIKVLPKNILLGTFKNFKTFINKKIPIIVNLHIRETFKIQHAMNGIEVSNWVNRLEIESYQFKIKSKNELNESINRSKKQPNNVTRSKSKKSLISLGIKYLATRENIYFLIYLVFPVILRRHYATEIEGFSKVRYFNRPVWIKIVHRQADKWYLESLKGIIQLKDSYMLNLSISQIISKELDKNISFSEENIPKIRWVPKSKGLRPLINSKLVSGQIGLVQNLQEDHTVREEKKCKGFCDICSVWCTNGDCLPTGSCINNNWYYNYYFSYNGNNNGIVNNHYNYGHIYNNGGGIKFTSFSNSQCTQIMTNPPGRGVGLGFGNLNIGIGYISGSSVPTNTPINVMRRPSSNRKIIDIRPSTNNRMLFYPSILRSFKLLRMGKNHTLASLVGQGDIYKFIIKNWIKNWRDKQQFRQMNEFYQNDKQGKMSHVIYIIKADLVNCKFENINKSKIFEFLDVISLPNIESLSLYLSRALKTTSIPPFDNMNRDSYIQDELRSCGITSKGKLNMIVIFEKDHDPEDQKVVKSKIKIIGPRDLDELWNLKLNSCLSKDLSINLGQKAEIFTFKLSRRVINNWLVKEIIKIHKLNTSFRLRTCSFKSLRLISKQLGNSKIKFGRFLSLFKQDFGIKPQGSSSYILCICLYYNFLDLNPEIQNLLGHSFSSSYFISSFLNPIKLQEVQLLDKPTEDLFSQHKDLEGLSRTYPEKENEIFNIYNTSSKTRRLEISEYNINAKSVKLLQPEEFNNNSINQNCQNIRANLSYDQESPKSSNKQQESLLRWVDDLFLLTSDLESFAKKFLKLYIQLLWGSNVKSKDKINSNPWIDHNNEIIFILEDDVLLSSPSSSECSSSCSSSSSSSSSSSSSSSSSSSFPPSTECSSPVTEKRNTNKISEKDCNEKEMINKQAKIASQFHKQVSWTGMKFKSSEYSYNCMVSLPWKNEFICVMLDTVTLTKHQFTTSNYNFHRFKSSTISENLQTKSNYWSVLGMIKLIRYDFRIKFNGLLYCKINSLFTDVSFYNSTNNTEIKN TTMJ862 TT Literature-reported TTPC9D0 ID TTPC9D0 TTPC9D0 TN ELAV-like protein 1 (ELAVL1) TTPC9D0 UP Q15717 TTPC9D0 UC ELAV1_HUMAN TTPC9D0 SN HuR; Hu-antigen R TTPC9D0 GN ELAVL1 TTPC9D0 FC Involved in embryonic stem cells (ESCs) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESCs differentiation. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro. With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind with ZNF385A the CCNB1 mRNA. Increases the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR. RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. TTPC9D0 PD 6GD3; 6GD2; 6GD1; 6GC5; 6G2K TTPC9D0 SQ MSNGYEDHMAEDCRGDIGRTNLIVNYLPQNMTQDELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAINTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANPNQNKNVALLSQLYHSPARRFGGPVHHQAQRFRFSPMGVDHMSGLSGVNVPGNASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKILQVSFKTNKSHK TTPC9D0 TT Literature-reported TTPC9D0 FM RNA recognition motif TTYVR8M ID TTYVR8M TTYVR8M TN Endocytic receptor Endo180 (MRC2) TTYVR8M UP Q9Y5P9 TTYVR8M UC MRC2_HUMAN TTYVR8M SN Urokinase-type plasminogen activator receptor-associated protein; Urokinase receptor-associated protein; UPARAP; UPAR-associated protein; Macrophage mannose receptor 2; KIAA0709; Endocytic receptor 180; ENDO180; CLEC13E; CD280; C-type mannose receptor 2; C-type lectin domain family 13 member E TTYVR8M GN MRC2 TTYVR8M FC May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). TTYVR8M PD 5EW6; 5E4L; 5E4K; 5AO6; 5AO5 TTYVR8M SQ MGPGRPAPAPWPRHLLRCVLLLGCLHLGRPGAPGDAALPEPNVFLIFSHGLQGCLEAQGGQVRVTPACNTSLPAQRWKWVSRNRLFNLGTMQCLGTGWPGTNTTASLGMYECDREALNLRWHCRTLGDQLSLLLGARTSNISKPGTLERGDQTRSGQWRIYGSEEDLCALPYHEVYTIQGNSHGKPCTIPFKYDNQWFHGCTSTGREDGHLWCATTQDYGKDERWGFCPIKSNDCETFWDKDQLTDSCYQFNFQSTLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSSTLWIGLNDLDTSGGWQWSDNSPLKYLNWESDQPDNPSEENCGVIRTESSGGWQNRDCSIALPYVCKKKPNATAEPTPPDRWANVKVECEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDGSLVSFTHWHPFEPNNFRDSLEDCVTIWGPEGRWNDSPCNQSLPSICKKAGQLSQGAAEEDHGCRKGWTWHSPSCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNWEGEYFWTALQDLNSTGSFFWLSGDEVMYTHWNRDQPGYSRGGCVALATGSAMGLWEVKNCTSFRARYICRQSLGTPVTPELPGPDPTPSLTGSCPQGWASDTKLRYCYKVFSSERLQDKKSWVQAQGACQELGAQLLSLASYEEEHFVANMLNKIFGESEPEIHEQHWFWIGLNRRDPRGGQSWRWSDGVGFSYHNFDRSRHDDDDIRGCAVLDLASLQWVAMQCDTQLDWICKIPRGTDVREPDDSPQGRREWLRFQEAEYKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSRAQEQHWWIGLHTSESDGRFRWTDGSIINFISWAPGKPRPVGKDKKCVYMTASREDWGDQRCLTALPYICKRSNVTKETQPPDLPTTALGGCPSDWIQFLNKCFQVQGQEPQSRVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFDLWIGLHASQRDFQWVEQEPLMYANWAPGEPSGPSPAPSGNKPTSCAVVLHSPSAHFTGRWDDRSCTEETHGFICQKGTDPSLSPSPAALPPAPGTELSYLNGTFRLLQKPLRWHDALLLCESRNASLAYVPDPYTQAFLTQAARGLRTPLWIGLAGEEGSRRYSWVSEEPLNYVGWQDGEPQQPGGCTYVDVDGAWRTTSCDTKLQGAVCGVSSGPPPPRRISYHGSCPQGLADSAWIPFREHCYSFHMELLLGHKEARQRCQRAGGAVLSILDEMENVFVWEHLQSYEGQSRGAWLGMNFNPKGGTLVWQDNTAVNYSNWGPPGLGPSMLSHNSCYWIQSNSGLWRPGACTNITMGVVCKLPRAEQSSFSPSALPENPAALVVVLMAVLLLLALLTAALILYRRRQSIERGAFEGARYSRSSSSPTEATEKNILVSDMEMNEQQE TTYVR8M TT Literature-reported TTMR0OP ID TTMR0OP TTMR0OP TN Endothelin (EDN) TTMR0OP UP P20800 TTMR0OP UC EDN2_HUMAN TTMR0OP BC Endothelin/sarafotoxin TTMR0OP SN Preproendothelin-2; PPET2; Endothelin-2; ET-2 TTMR0OP GN EDN2 TTMR0OP FC Endothelins are endothelium-derived vasoconstrictor peptides. TTMR0OP SQ MVSVPTTWCSVALALLVALHEGKGQAAATLEQPASSSHAQGTHLRLRRCSCSSWLDKECVYFCHLDIIWVNTPEQTAPYGLGNPPRRRRRSLPRRCQCSSARDPACATFCLRRPWTEAGAVPSRKSPADVFQTGKTGATTGELLQRLRDISTVKSLFAKRQQEAMREPRSTHSRWRKR TTMR0OP TT Literature-reported TT1UREA ID TT1UREA TT1UREA TN Enhancer of filamentation 1 (NEDD9) TT1UREA UP Q14511 TT1UREA UC CASL_HUMAN TT1UREA SN p105; hEF1; Renal carcinoma antigen NY-REN-12; Neural precursor cell expressed developmentally down-regulated protein 9; NEDD-9; CasL; Cas scaffolding protein family member 2; CRK-associated substrate-related protein; CASS2; CAS-L TT1UREA GN NEDD9 TT1UREA FC May function in transmitting growth control signals between focal adhesions at the cell periphery and the mitotic spindle in response to adhesion or growth factor signals initiating cell proliferation. May play an important role in integrin beta-1 or B cell antigen receptor (BCR) mediated signaling in B- and T-cells. Integrin beta-1 stimulation leads to recruitment of various proteins including CRK, NCK and SHPTP2 to the tyrosine phosphorylated form. Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. TT1UREA PD 5X3S; 2L81 TT1UREA SQ MKYKNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPMQETASSHEQPASGLMQQTFGQQKLYQVPNPQAAPRDTIYQVPPSYQNQGIYQVPTGHGTQEQEVYQVPPSVQRSIGGTSGPHVGKKVITPVRTGHGYVYEYPSRYQKDVYDIPPSHTTQGVYDIPPSSAKGPVFSVPVGEIKPQGVYDIPPTKGVYAIPPSACRDEAGLREKDYDFPPPMRQAGRPDLRPEGVYDIPPTCTKPAGKDLHVKYNCDIPGAAEPVARRHQSLSPNHPPPQLGQSVGSQNDAYDVPRGVQFLEPPAETSEKANPQERDGVYDVPLHNPPDAKGSRDLVDGINRLSFSSTGSTRSNMSTSSTSSKESSLSASPAQDKRLFLDPDTAIERLQRLQQALEMGVSSLMALVTTDWRCYGYMERHINEIRTAVDKVELFLKEYLHFVKGAVANAACLPELILHNKMKRELQRVEDSHQILSQTSHDLNECSWSLNILAINKPQNKCDDLDRFVMVAKTVPDDAKQLTTTINTNAEALFRPGPGSLHLKNGPESIMNSTEYPHGGSQGQLLHPGDHKAQAHNKALPPGLSKEQAPDCSSSDGSERSWMDDYDYVHLQGKEEFERQQKELLEKENIMKQNKMQLEHHQLSQFQLLEQEITKPVENDISKWKPSQSLPTTNSGVSAQDRQLLCFYYDQCETHFISLLNAIDALFSCVSSAQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVTAQDIRNKVMNSSNQLCEQLKTIVMATKMAALHYPSTTALQEMVHQVTDLSRNAQLFKRSLLEMATF TT1UREA TT Literature-reported TTPXTVS ID TTPXTVS TTPXTVS TN Entamoeba Cysteine proteinase CP4 (Eh CP4) TTPXTVS UP Q27641 TTPXTVS UC Q27641_ENTDI TTPXTVS SN Entamoeba Cysteine proteinase CP4; Cysteine proteinase TTPXTVS GN Eh CP4 TTPXTVS FC Plays a key role in disrupting the colonic epithelial barrier and the innate host immune response during invasion of E. histolytica, the protozoan cause of human amebiasis. TTPXTVS EC EC 3.4.22.35 TTPXTVS SQ FVAAATAIDFKSWAAKNNKHFTAVEALRRRAIFNMNAKFVAKFNKANSFELSVDGPFAAMTNEEYNHLLRVHETEAAADSVYDNTIITASSKDWRAEGKVTPVRDQGNCGSCYSFSSLAVLESRLLIAGSKYNQNNQDLSEQQIVDCSTANNGCNGGSLSATYLYVKNNGVTDEASYPYTATKGTCKAFTPKVQTTGLTHVTPNEDALTSALEQGPVAVCIDAGKASFQLYKSGVYDEPKCSKTVNHGVAAVGYGTQDGKDYYIVKNSWGTSWGDKGYILMSRNKNNQCAIASVAYFPNGAHDAN TTPXTVS TT Literature-reported TTZEMUY ID TTZEMUY TTZEMUY TN Ephrin type-B receptor 6 (EPHB6) TTZEMUY UP O15197 TTZEMUY UC EPHB6_HUMAN TTZEMUY BC Kinase TTZEMUY SN Tyrosine-protein kinase-defective receptor EPH-6; HEP TTZEMUY GN EPHB6 TTZEMUY FC Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2. Kinase-defective receptor for members of the ephrin-B family. TTZEMUY SQ MATEGAAQLGNRVAGMVCSLWVLLLVSSVLALEEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEACHVAGAPPGTGQDNWLQTHFVERRGAQRAHIRLHFSVRACSSLGVSGGTCRETFTLYYRQAEEPDSPDSVSSWHLKRWTKVDTIAADESFPSSSSSSSSSSSAAWAVGPHGAGQRAGLQLNVKERSFGPLTQRGFYVAFQDTGACLALVAVRLFSYTCPAVLRSFASFPETQASGAGGASLVAAVGTCVAHAEPEEDGVGGQAGGSPPRLHCNGEGKWMVAVGGCRCQPGYQPARGDKACQACPRGLYKSSAGNAPCSPCPARSHAPNPAAPVCPCLEGFYRASSDPPEAPCTGPPSAPQELWFEVQGSALMLHWRLPRELGGRGDLLFNVVCKECEGRQEPASGGGGTCHRCRDEVHFDPRQRGLTESRVLVGGLRAHVPYILEVQAVNGVSELSPDPPQAAAINVSTSHEVPSAVPVVHQVSRASNSITVSWPQPDQTNGNILDYQLRYYDQAEDESHSFTLTSETNTATVTQLSPGHIYGFQVRARTAAGHGPYGGKVYFQTLPQGELSSQLPERLSLVIGSILGALAFLLLAAITVLAVVFQRKRRGTGYTEQLQQYSSPGLGVKYYIDPSTYEDPCQAIRELAREVDPAYIKIEEVIGTGSFGEVRQGRLQPRGRREQTVAIQALWAGGAESLQMTFLGRAAVLGQFQHPNILRLEGVVTKSRPLMVLTEFMELGPLDSFLRQREGQFSSLQLVAMQRGVAAAMQYLSSFAFVHRSLSAHSVLVNSHLVCKVARLGHSPQGPSCLLRWAAPEVIAHGKHTTSSDVWSFGILMWEVMSYGERPYWDMSEQEVLNAIEQEFRLPPPPGCPPGLHLLMLDTWQKDRARRPHFDQLVAAFDKMIRKPDTLQAGGDPGERPSQALLTPVALDFPCLDSPQAWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLLQQHLRQQGSVEV TTZEMUY TT Literature-reported TTXJGAR ID TTXJGAR TTXJGAR TN Epidermal growth factor-like protein 6 (EGFL6) TTXJGAR UP Q8IUX8 TTXJGAR UC EGFL6_HUMAN TTXJGAR BC Growth factor TTXJGAR SN MAM and EGF domains-containing gene protein; EGFL6; EGF-like protein 6 TTXJGAR GN EGFL6 TTXJGAR FC May bind integrin alpha-8/beta-1 and play a role in hair follicle morphogenesis. Promotes matrix assembly. TTXJGAR SQ MPLPWSLALPLLLSWVAGGFGNAASARHHGLLASARQPGVCHYGTKLACCYGWRRNSKGVCEATCEPGCKFGECVGPNKCRCFPGYTGKTCSQDVNECGMKPRPCQHRCVNTHGSYKCFCLSGHMLMPDATCVNSRTCAMINCQYSCEDTEEGPQCLCPSSGLRLAPNGRDCLDIDECASGKVICPYNRRCVNTFGSYYCKCHIGFELQYISGRYDCIDINECTMDSHTCSHHANCFNTQGSFKCKCKQGYKGNGLRCSAIPENSVKEVLRAPGTIKDRIKKLLAHKNSMKKKAKIKNVTPEPTRTPTPKVNLQPFNYEEIVSRGGNSHGGKKGNEEKMKEGLEDEKREEKALKNDIEERSLRGDVFFPKVNEAGEFGLILVQRKALTSKLEHKDLNISVDCSFNHGICDWKQDREDDFDWNPADRDNAIGFYMAVPALAGHKKDIGRLKLLLPDLQPQSNFCLLFDYRLAGDKVGKLRVFVKNSNNALAWEKTTSEDEKWKTGKIQLYQGTDATKSIIFEAERGKGKTGEIAVDGVLLVSGLCPDSLLSVDD TTXJGAR TT Literature-reported TTLAWO6 ID TTLAWO6 TTLAWO6 TN Epithelial cadherin (CDH1) TTLAWO6 UP P12830 TTLAWO6 UC CADH1_HUMAN TTLAWO6 SN Uvomorulin; UVO; E-cadherin gene; E-cadherin; Cadherin-1; CDHE; CD324; CAM 120/80 TTLAWO6 GN CDH1 TTLAWO6 FC Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. TTLAWO6 PD 6CXY; 4ZTE; 4ZT1; 3L6Y; 3L6X TTLAWO6 SQ MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD TTLAWO6 TT Literature-reported TTLAWO6 FM Transmembrane protein TT5OJMV ID TT5OJMV TT5OJMV TN ETS domain-containing protein Elk-3 (ELK3) TT5OJMV UP P41970 TT5OJMV UC ELK3_HUMAN TT5OJMV BC E26 transformation-specific ETS TT5OJMV SN Serum response factor accessory protein 2; SRF accessory protein 2; SAP2; SAP-2; ETS-related protein NET; ETS-related protein ERP TT5OJMV GN ELK3 TT5OJMV FC Forms a ternary complex with the serum response factor and the ETS and SRF motifs of the Fos serum response element. May be a negative regulator of transcription, but can activate transcription when coexpressed with Ras, Src or Mos. TT5OJMV SQ MESAITLWQFLLQLLLDQKHEHLICWTSNDGEFKLLKAEEVAKLWGLRKNKTNMNYDKLSRALRYYYDKNIIKKVIGQKFVYKFVSFPEILKMDPHAVEISRESLLLQDSDCKASPEGREAHKHGLAALRSTSRNEYIHSGLYSSFTINSLQNPPDAFKAIKTEKLEEPPEDSPPVEEVRTVIRFVTNKTDKHVTRPVVSLPSTSEAAAASAFLASSVSAKISSLMLPNAASISSASPFSSRSPSLSPNSPLPSEHRSLFLEAACHDSDSLEPLNLSSGSKTKSPSLPPKAKKPKGLEISAPPLVLSGTDIGSIALNSPALPSGSLTPAFFTAQTPNGLLLTPSPLLSSIHFWSSLSPVAPLSPARLQGPSTLFQFPTLLNGHMPVPIPSLDRAASPVLLSSNSQKS TT5OJMV TT Literature-reported TTGXULC ID TTGXULC TTGXULC TN ETS-domain transcription factor ERF (ERF) TTGXULC UP P50548 TTGXULC UC ERF_HUMAN TTGXULC BC E26 transformation-specific ETS TTGXULC SN Transcription factor Ets2; PE-2; Ets2 repressor factor; ETS domain-containing transcription factor ERF TTGXULC GN ERF TTGXULC FC May regulate other genes involved in cellular proliferation. Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment. May be important for regulating trophoblast stem cell differentiation. Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. TTGXULC SQ MKTPADTGFAFPDWAYKPESSPGSRQIQLWHFILELLRKEEYQGVIAWQGDYGEFVIKDPDEVARLWGVRKCKPQMNYDKLSRALRYYYNKRILHKTKGKRFTYKFNFNKLVLVNYPFIDVGLAGGAVPQSAPPVPSGGSHFRFPPSTPSEVLSPTEDPRSPPACSSSSSSLFSAVVARRLGRGSVSDCSDGTSELEEPLGEDPRARPPGPPDLGAFRGPPLARLPHDPGVFRVYPRPRGGPEPLSPFPVSPLAGPGSLLPPQLSPALPMTPTHLAYTPSPTLSPMYPSGGGGPSGSGGGSHFSFSPEDMKRYLQAHTQSVYNYHLSPRAFLHYPGLVVPQPQRPDKCPLPPMAPETPPVPSSASSSSSSSSSPFKFKLQPPPLGRRQRAAGEKAVAGADKSGGSAGGLAEGAGALAPPPPPPQIKVEPISEGESEEVEVTDISDEDEEDGEVFKTPRAPPAPPKPEPGEAPGASQCMPLKLRFKRRWSEDCRLEGGGGPAGGFEDEGEDKKVRGEGPGEAGGPLTPRRVSSDLQHATAQLSLEHRDS TTGXULC TT Literature-reported TTUF10B ID TTUF10B TTUF10B TN Eukaryotic initiation factor 4E (EIF4E) TTUF10B UP P06730 TTUF10B UC IF4E_HUMAN TTUF10B SN eIF4F 25 kDa subunit; eIF4E; eIF-4F 25 kDa subunit; eIF-4E; Eukaryotic translation initiation factor 4E; EIF4F; EIF4EL1 TTUF10B GN EIF4E TTUF10B FC Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates the binding to the mRNA cap. Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. TTUF10B PD 5ZML; 5ZK9; 5ZK7; 5ZK5; 5ZJZ TTUF10B SQ MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV TTUF10B TT Literature-reported TTH53G9 ID TTH53G9 TTH53G9 TN Eukaryotic initiation factor 5A2 (EIF5A2) TTH53G9 UP Q9GZV4 TTH53G9 UC IF5A2_HUMAN TTH53G9 BC Eukaryotic nuclear pore complex TTH53G9 SN eIF5A2; eIF-5A2; eIF-5A-2; Eukaryotic translation initiation factor 5A-2; Eukaryotic initiation factor 5A isoform 2 TTH53G9 GN EIF5A2 TTH53G9 FC Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation. mRNA-binding protein involved in translation elongation. TTH53G9 SQ MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK TTH53G9 TT Literature-reported TTRUJBV ID TTRUJBV TTRUJBV TN Eukaryotic translation initiation factor 2-alpha kinase 1 (EIF2AK1) TTRUJBV UP Q9BQI3 TTRUJBV UC E2AK1_HUMAN TTRUJBV SN PRO1362; KIAA1369; Hemin-sensitive initiation factor 2-alpha kinase; Heme-regulated inhibitor; Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase; HRI TTRUJBV GN EIF2AK1 TTRUJBV FC Inhibits protein synthesis at the translation initiation level, in response to various stress conditions, including oxidative stress, heme deficiency, osmotic shock and heat shock. Exerts its function through the phosphorylation of EIF2S1 at 'Ser-48' and 'Ser-51', thus preventing its recycling. Binds hemin forming a 1:1 complex through a cysteine thiolate and histidine nitrogenous coordination. This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell. Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties. Thus plays an essential protective role for RBC survival in anemias of iron deficiency. Similarly, in hepatocytes, involved in heme-mediated translational control of CYP2B and CYP3A and possibly other hepatic P450 cytochromes. May also contain ER stress during acute heme-deficient conditions (By similarity). TTRUJBV EC EC 2.7.11.1 TTRUJBV SQ MQGGNSGVRKREEEGDGAGAVAAPPAIDFPAEGPDPEYDESDVPAEIQVLKEPLQQPTFPFAVANQLLLVSLLEHLSHVHEPNPLRSRQVFKLLCQTFIKMGLLSSFTCSDEFSSLRLHHNRAITHLMRSAKERVRQDPCEDISRIQKIRSREVALEAQTSRYLNEFEELAILGKGGYGRVYKVRNKLDGQYYAIKKILIKGATKTVCMKVLREVKVLAGLQHPNIVGYHTAWIEHVHVIQPRADRAAIELPSLEVLSDQEEDREQCGVKNDESSSSSIIFAEPTPEKEKRFGESDTENQNNKSVKYTTNLVIRESGELESTLELQENGLAGLSASSIVEQQLPLRRNSHLEESFTSTEESSEENVNFLGQTEAQYHLMLHIQMQLCELSLWDWIVERNKRGREYVDESACPYVMANVATKIFQELVEGVFYIHNMGIVHRDLKPRNIFLHGPDQQVKIGDFGLACTDILQKNTDWTNRNGKRTPTHTSRVGTCLYASPEQLEGSEYDAKSDMYSLGVVLLELFQPFGTEMERAEVLTGLRTGQLPESLRKRCPVQAKYIQHLTRRNSSQRPSAIQLLQSELFQNSGNVNLTLQMKIIEQEKEIAELKKQLNLLSQDKGVRDDGKDGGVG TTRUJBV TT Literature-reported TT9U4EP ID TT9U4EP TT9U4EP TN Eukaryotic translation initiation factor 2-alpha kinase 4 (EIF2AK4) TT9U4EP UP Q9P2K8 TT9U4EP UC E2AK4_HUMAN TT9U4EP SN eIF-2-alpha kinase GCN2; KIAA1338; GCN2-like protein; GCN2 TT9U4EP GN EIF2AK4 TT9U4EP FC Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' in response to low amino acid availability. Plays a role as an activator of the integrated stress response (ISR) required for adapatation to amino acid starvation. Converts phosphorylated eIF-2-alpha/EIF2S1 either to a competitive inhibitor of the translation initiation factor eIF-2B, leading to a global protein synthesis repression, and thus to a reduced overall utilization of amino acids, or to a translational initiation activation of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. Binds uncharged tRNAs (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation. Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory. Plays a role in neurite outgrowth inhibition. Plays a proapoptotic role in response to glucose deprivation. Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (By similarity). Plays a role in the antiviral response against alphavirus infection; impairs early viral mRNA translation of the incoming genomic virus RNA, thus preventing alphavirus replication (By similarity). TT9U4EP EC EC 2.7.11.1 TT9U4EP SQ MAGGRGAPGRGRDEPPESYPQRQDHELQALEAIYGADFQDLRPDACGPVKEPPEINLVLYPQGLTGEEVYVKVDLRVKCPPTYPDVVPEIELKNAKGLSNESVNLLKSRLEELAKKHCGEVMIFELAYHVQSFLSEHNKPPPKSFHEEMLERRAQEEQQRLLEAKRKEEQEQREILHEIQRRKEEIKEEKKRKEMAKQERLEIASLSNQDHTSKKDPGGHRTAAILHGGSPDFVGNGKHRANSSGRSRRERQYSVCNSEDSPGSCEILYFNMGSPDQLMVHKGKCIGSDEQLGKLVYNALETATGGFVLLYEWVLQWQKKMGPFLTSQEKEKIDKCKKQIQGTETEFNSLVKLSHPNVVRYLAMNLKEQDDSIVVDILVEHISGVSLAAHLSHSGPIPVHQLRRYTAQLLSGLDYLHSNSVVHKVLSASNVLVDAEGTVKITDYSISKRLADICKEDVFEQTRVRFSDNALPYKTGKKGDVWRLGLLLLSLSQGQECGEYPVTIPSDLPADFQDFLKKCVCLDDKERWSPQQLLKHSFINPQPKMPLVEQSPEDSEGQDYVETVIPSNRLPSAAFFSETQRQFSRYFIEFEELQLLGKGAFGAVIKVQNKLDGCCYAVKRIPINPASRQFRRIKGEVTLLSRLHHENIVRYYNAWIERHERPAGPGTPPPDSGPLAKDDRAARGQPASDTDGLDSVEAAAPPPILSSSVEWSTSGERSASARFPATGPGSSDDEDDDEDEHGGVFSQSFLPASDSESDIIFDNEDENSKSQNQDEDCNEKNGCHESEPSVTTEAVHYLYIQMEYCEKSTLRDTIDQGLYRDTVRLWRLFREILDGLAYIHEKGMIHRDLKPVNIFLDSDDHVKIGDFGLATDHLAFSADSKQDDQTGDLIKSDPSGHLTGMVGTALYVSPEVQGSTKSAYNQKVDLFSLGIIFFEMSYHPMVTASERIFVLNQLRDPTSPKFPEDFDDGEHAKQKSVISWLLNHDPAKRPTATELLKSELLPPPQMEESELHEVLHHTLTNVDGKAYRTMMAQIFSQRISPAIDYTYDSDILKGNFSIRTAKMQQHVCETIIRIFKRHGAVQLCTPLLLPRNRQIYEHNEAALFMDHSGMLVMLPFDLRIPFARYVARNNILNLKRYCIERVFRPRKLDRFHPKELLECAFDIVTSTTNSFLPTAEIIYTIYEIIQEFPALQERNYSIYLNHTMLLKAILLHCGIPEDKLSQVYIILYDAVTEKLTRREVEAKFCNLSLSSNSLCRLYKFIEQKGDLQDLMPTINSLIKQKTGIAQLVKYGLKDLEEVVGLLKKLGIKLQVLINLGLVYKVQQHNGIIFQFVAFIKRRQRAVPEILAAGGRYDLLIPQFRGPQALGPVPTAIGVSIAIDKISAAVLNMEESVTISSCDLLVVSVGQMSMSRAINLTQKLWTAGITAEIMYDWSQSQEELQEYCRHHEITYVALVSDKEGSHVKVKSFEKERQTEKRVLETELVDHVLQKLRTKVTDERNGREASDNLAVQNLKGSFSNASGLFEIHGATVVPIVSVLAPEKLSASTRRRYETQVQTRLQTSLANLHQKSSEIEILAVDLPKETILQFLSLEWDADEQAFNTTVKQLLSRLPKQRYLKLVCDEIYNIKVEKKVSVLFLYSYRDDYYRILF TT9U4EP TT Literature-reported TTKGEBL ID TTKGEBL TTKGEBL TN Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) TTKGEBL UP Q13541 TTKGEBL UC 4EBP1_HUMAN TTKGEBL SN eIF4E-binding protein 1; Phosphorylated heat- andacid-stable protein regulated by insulin 1; Phosphorylated heat- and acid-stable protein regulated by insulin 1; PHAS-I; 4E-BP1 TTKGEBL GN EIF4EBP1 TTKGEBL FC In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. TTKGEBL PD 6BCX; 6BCU; 5WBJ; 5NVN; 5EKV TTKGEBL SQ MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI TTKGEBL TT Literature-reported TTIVCNR ID TTIVCNR TTIVCNR TN Eukaryotic translation initiation factor 5A-1 (EIF5A) TTIVCNR UP P63241 TTIVCNR UC IF5A1_HUMAN TTIVCNR SN eIF-5A1; eIF-5A-1; eIF-5A; eIF-4D; Rev-binding factor; Eukaryotic initiation factor 5A isoform 1 TTIVCNR GN EIF5A TTIVCNR FC A GTPase-activating protein, which helps the large ribosomal subunit associate with the small subunit. Involved in the initiation phase of eukaryotic translation. Stabilize the formation of ribosomal preinitiation complexes around the start codon and are an important input for post-transcription gene regulation. Helps with elongation and also plays a role in termination. TTIVCNR PD 5DLQ; 3CPF; 1FH4 TTIVCNR SQ MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVREDLRLPEGDLGKEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK TTIVCNR TT Literature-reported TT8WRDA ID TT8WRDA TT8WRDA TN Excitatory amino acid transporter 1 (SLC1A3) TT8WRDA UP P43003 TT8WRDA UC EAA1_HUMAN TT8WRDA SN Solute carrier family 1 member 3; Sodium-dependent glutamate/aspartate transporter 1; GLAST-1; EAAT1 TT8WRDA GN SLC1A3 TT8WRDA FC Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (By similarity). TT8WRDA PD 5MJU; 5LM4; 5LLU; 5LLM TT8WRDA SQ MTKSNGEEPKMGGRMERFQQGVRKRTLLAKKKVQNITKEDVKSYLFRNAFVLLTVTAVIVGTILGFTLRPYRMSYREVKYFSFPGELLMRMLQMLVLPLIISSLVTGMAALDSKASGKMGMRAVVYYMTTTIIAVVIGIIIVIIIHPGKGTKENMHREGKIVRVTAADAFLDLIRNMFPPNLVEACFKQFKTNYEKRSFKVPIQANETLVGAVINNVSEAMETLTRITEELVPVPGSVNGVNALGLVVFSMCFGFVIGNMKEQGQALREFFDSLNEAIMRLVAVIMWYAPVGILFLIAGKIVEMEDMGVIGGQLAMYTVTVIVGLLIHAVIVLPLLYFLVTRKNPWVFIGGLLQALITALGTSSSSATLPITFKCLEENNGVDKRVTRFVLPVGATINMDGTALYEALAAIFIAQVNNFELNFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWFLDRLRTTTNVLGDSLGAGIVEHLSRHELKNRDVEMGNSVIEENEMKKPYQLIAQDNETEKPIDSETKM TT8WRDA TT Literature-reported TTG2A6F ID TTG2A6F TTG2A6F TN Excitatory amino acid transporter 3 (SLC1A1) TTG2A6F UP P43005 TTG2A6F UC EAA3_HUMAN TTG2A6F BC Dicarboxylate/amino acid:cation symporter TTG2A6F SN Solute carrier family 1 member 1; Sodium-dependent glutamate/aspartate transporter 3; Neuronal and epithelial glutamate transporter; Excitatory amino-acid carrier 1; EAAT3; EAAC1 TTG2A6F GN SLC1A1 TTG2A6F FC Can also transport L-cysteine. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Plays an important role in L-glutamate and L-aspartate reabsorption in renal tubuli. Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate. Negatively regulated by ARL6IP5. Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. TTG2A6F SQ MGKPARKGCEWKRFLKNNWVLLSTVAAVVLGITTGVLVREHSNLSTLEKFYFAFPGEILMRMLKLIILPLIISSMITGVAALDSNVSGKIGLRAVVYYFCTTLIAVILGIVLVVSIKPGVTQKVGEIARTGSTPEVSTVDAMLDLIRNMFPENLVQACFQQYKTKREEVKPPSDPEMNMTEESFTAVMTTAISKNKTKEYKIVGMYSDGINVLGLIVFCLVFGLVIGKMGEKGQILVDFFNALSDATMKIVQIIMCYMPLGILFLIAGKIIEVEDWEIFRKLGLYMATVLTGLAIHSIVILPLIYFIVVRKNPFRFAMGMAQALLTALMISSSSATLPVTFRCAEENNQVDKRITRFVLPVGATINMDGTALYEAVAAVFIAQLNDLDLGIGQIITISITATSASIGAAGVPQAGLVTMVIVLSAVGLPAEDVTLIIAVDWLLDRFRTMVNVLGDAFGTGIVEKLSKKELEQMDVSSEVNIVNPFALESTILDNEDSDTKKSYVNGGFAVDKSDTISFTQTSQF TTG2A6F TT Literature-reported TTNZKFJ ID TTNZKFJ TTNZKFJ TN Fanconi anemia group F protein (FANCF) TTNZKFJ UP Q9NPI8 TTNZKFJ UC FANCF_HUMAN TTNZKFJ SN Protein FACF TTNZKFJ GN FANCF TTNZKFJ FC May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. TTNZKFJ PD 2IQC TTNZKFJ SQ MESLLQHLDRFSELLAVSSTTYVSTWDPATVRRALQWARYLRHIHRRFGRHGPIRTALERRLHNQWRQEGGFGRGPVPGLANFQALGHCDVLLSLRLLENRALGDAARYHLVQQLFPGPGVRDADEETLQESLARLARRRSAVHMLRFNGYRENPNLQEDSLMKTQAELLLERLQEVGKAEAERPARFLSSLWERLPQNNFLKVIAVALLQPPLSRRPQEELEPGIHKSPGEGSQVLVHWLLGNSEVFAAFCRALPAGLLTLVTSRHPALSPVYLGLLTDWGQRLHYDLQKGIWVGTESQDVPWEELHNRFQSLCQAPPPLKDKVLTALETCKAQDGDFEVPGLSIWTDLLLALRSGAFRKRQVLGLSAGLSSV TTNZKFJ TT Literature-reported TTNZKFJ FM DNA repair TT29KY7 ID TT29KY7 TT29KY7 TN F-box and WD-40 domain protein 7 (Fbxw7) TT29KY7 UP Q969H0 TT29KY7 UC FBXW7_HUMAN TT29KY7 SN hCdc4; hAgo; SEL10; SEL-10; FBX30; FBW7; F-box/WD repeat-containing protein 7; F-box-WD40 repeat protein 6; F-box protein Fbxw6; F-box protein FBX30; F-box protein FBW7; F-box and WD-40 domain-containing protein 7; Archipelago homolog TT29KY7 GN FBXW7 TT29KY7 FC Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter bring them to the SCF complex for ubiquitination. Identified substrates include cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1, and probably PSEN1. Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation. SCF(FBXW7) complex mediates the ubiquitination and subsequent degradation of NFE2L1. Involved in bone homeostasis and negative regulation of osteoclast differentiation. Regulates the amplitude of the cyclic expression of hepatic core clock genes and genes involved in lipid and glucose metabolism via ubiquitination and proteasomal degradation of their transcriptional repressor NR1D1; CDK1-dependent phosphorylation of NR1D1 is necessary for SCF(FBXW7)-mediated ubiquitination. Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. TT29KY7 PD 5V4B; 5IBK; 2OVR; 2OVQ; 2OVP TT29KY7 SQ MNQELLSVGSKRRRTGGSLRGNPSSSQVDEEQMNRVVEEEQQQQLRQQEEEHTARNGEVVGVEPRPGGQNDSQQGQLEENNNRFISVDEDSSGNQEEQEEDEEHAGEQDEEDEEEEEMDQESDDFDQSDDSSREDEHTHTNSVTNSSSIVDLPVHQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSEYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKEEGIDEPLHIKRRKVIKPGFIHSPWKSAYIRQHRIDTNWRRGELKSPKVLKGHDDHVITCLQFCGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWSSQMRDNIIISGSTDRTLKVWNAETGECIHTLYGHTSTVRCMHLHEKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQYDGRRVVSGAYDFMVKVWDPETETCLHTLQGHTNRVYSLQFDGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMELKDNILVSGNADSTVKIWDIKTGQCLQTLQGPNKHQSAVTCLQFNKNFVITSSDDGTVKLWDLKTGEFIRNLVTLESGGSGGVVWRIRASNTKLVCAVGSRNGTEETKLLVLDFDVDMK TT29KY7 TT Literature-reported TTKJX1V ID TTKJX1V TTKJX1V TN Fibroblast growth factor-14 (FGF14) TTKJX1V UP Q92915 TTKJX1V UC FGF14_HUMAN TTKJX1V BC Growth factor TTKJX1V SN Fibroblast growth factor homologous factor 4; Fibroblast growth factor 14; FHF4; FGF14 TTKJX1V GN FGF14 TTKJX1V FC Probably involved in nervous system development and function. TTKJX1V SQ MAAAIASGLIRQKRQAREQHWDRPSASRRRSSPSKNRGLCNGNLVDIFSKVRIFGLKKRRLRRQDPQLKGIVTRLYCRQGYYLQMHPDGALDGTKDDSTNSTLFNLIPVGLRVVAIQGVKTGLYIAMNGEGYLYPSELFTPECKFKESVFENYYVIYSSMLYRQQESGRAWFLGLNKEGQAMKGNRVKKTKPAAHFLPKPLEVAMYREPSLHDVGETVPKPGVTPSKSTSASAIMNGGKPVNKSKTT TTKJX1V TT Literature-reported TTYBS89 ID TTYBS89 TTYBS89 TN Fibroleukin (FGL2) TTYBS89 UP Q14314 TTYBS89 UC FGL2_HUMAN TTYBS89 BC Fibrinogen TTYBS89 SN PT49; Hfgl2; Fibrinogen-like protein 2; FGL2 TTYBS89 GN FGL2 TTYBS89 FC May play a role in physiologic lymphocyte functions at mucosal sites. TTYBS89 SQ MKLANWYWLSSAVLATYGFLVVANNETEEIKDERAKDVCPVRLESRGKCEEAGECPYQVSLPPLTIQLPKQFSRIEEVFKEVQNLKEIVNSLKKSCQDCKLQADDNGDPGRNGLLLPSTGAPGEVGDNRVRELESEVNKLSSELKNAKEEINVLHGRLEKLNLVNMNNIENYVDSKVANLTFVVNSLDGKCSKCPSQEQIQSRPVQHLIYKDCSDYYAIGKRSSETYRVTPDPKNSSFEVYCDMETMGGGWTVLQARLDGSTNFTRTWQDYKAGFGNLRREFWLGNDKIHLLTKSKEMILRIDLEDFNGVELYALYDQFYVANEFLKYRLHVGNYNGTAGDALRFNKHYNHDLKFFTTPDKDNDRYPSGNCGLYYSSGWWFDACLSANLNGKYYHQKYRGVRNGIFWGTWPGVSEAHPGGYKSSFKEAKMMIRPKHFKP TTYBS89 TT Literature-reported TT2UV5C ID TT2UV5C TT2UV5C TN FKBP-associated protein (FAP48) TT2UV5C UP Q92990 TT2UV5C UC GLMN_HUMAN TT2UV5C SN Glomulin; FK506-binding protein-associated protein; FAP48 TT2UV5C GN GLMN TT2UV5C FC Isoform 1: Regulatory component of cullin-RING-based SCF (SKP1-Cullin-F-box protein) E3 ubiquitin-protein ligase complexes. Inhibits E3 ubiquitin ligase activity by binding to RBX1 (via RING domain) and inhibiting its interaction with the E2 ubiquitin-conjugating enzyme CDC34. Inhibits RBX1-mediated neddylation of CUL1. Required for normal stability and normal cellular levels of key components of SCF ubiquitin ligase complexes, including FBXW7, RBX1, CUL1, CUL2, CUL3, CUL4A, and thereby contributes to the regulation of CCNE1 and MYC levels (By similarity). Essential for normal development of the vasculature. Contributes to the regulation of RPS6KB1 phosphorylation. TT2UV5C PD 4F52 TT2UV5C SQ MAVEELQSIIKRCQILEEQDFKEEDFGLFQLAGQRCIEEGHTDQLLEIIQNEKNKVIIKNMGWNLVGPVVRCLLCKDKEDSKRKVYFLIFDLLVKLCNPKELLLGLLELIEEPSGKQISQSILLLLQPLQTVIQKLHNKAYSIGLALSTLWNQLSLLPVPYSKEQIQMDDYGLCQCCKALIEFTKPFVEEVIDNKENSLENEKLKDELLKFCFKSLKCPLLTAQFFEQSEEGGNDPFRYFASEIIGFLSAIGHPFPKMIFNHGRKKRTWNYLEFEEEENKQLADSMASLAYLVFVQGIHIDQLPMVLSPLYLLQFNMGHIEVFLQRTEESVISKGLELLENSLLRIEDNSLLYQYLEIKSFLTVPQGLVKVMTLCPIETLRKKSLAMLQLYINKLDSQGKYTLFRCLLNTSNHSGVEAFIIQNIKNQIDMSLKRTRNNKWFTGPQLISLLDLVLFLPEGAETDLLQNSDRIMASLNLLRYLVIKDNENDNQTGLWTELGNIENNFLKPLHIGLNMSKAHYEAEIKNSQEAQKSKDLCSITVSGEEIPNMPPEMQLKVLHSALFTFDLIESVLARVEELIEIKTKSTSEENIGIK TT2UV5C TT Literature-reported TTYLZ71 ID TTYLZ71 TTYLZ71 TN Flavivirus Serine protease NS2B-NS3 (FlaV NS2B-NS3) TTYLZ71 UP P03314 (1355-2107) TTYLZ71 UC POLG_YEFV1 TTYLZ71 SN FlavivirusNon-structural protein 2B-Non-structural protein 3; Flavivirus Flavivirin protease NS2B regulatory subunit-Flavivirin protease NS3 catalytic subunit Non-structural protein 3 TTYLZ71 GN FlaV NS2B-NS3 TTYLZ71 FC Capsid protein C: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. TTYLZ71 PD 6IW4; 6IW2; 6IW1; 6IW0; 6EPK TTYLZ71 SQ SIPVNEALAAAGLVGVLAGLAFQEMENFLGPIAVGGLLMMLVSVAGRVDGLELKKLGEVSWEEEAEISGSSARYDVALSEQGEFKLLSEEKVPWDQVVMTSLALVGAALHPFALLLVLAGWLFHVRGARRSGDVLWDIPTPKIIEECEHLEDGIYGIFQSTFLGASQRGVGVAQGGVFHTMWHVTRGAFLVRNGKKLIPSWASVKEDLVAYGGSWKLEGRWDGEEEVQLIAAVPGKNVVNVQTKPSLFKVRNGGEIGAVALDYPSGTSGSPIVNRNGEVIGLYGNGILVGDNSFVSAISQTEVKEEGKEELQEIPTMLKKGMTTVLDFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGREVIDAMCHATLTYRMLEPTRVVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWNTGHDWILADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEREYPTIKQKKPDFILATDIAEMGANLCVERVLDCRTAFKPVLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSENNAHHVCWLEASMLLDNMEVRGGMVAPLYGVEGTKTPVSPGEMRLRDDQRKVFRELVRNCDLPVWLSWQVAKAGLKTNDRKWCFEGPEEHEILNDSGETVKCRAPGGAKKPLRPRWCDERVSSDQSALSEFIKFAEGRR TTYLZ71 TT Literature-reported TTSM9YR ID TTSM9YR TTSM9YR TN Folate receptor gamma (FOLR3) TTSM9YR UP P41439 TTSM9YR UC FOLR3_HUMAN TTSM9YR BC Folate receptor TTSM9YR SN Folate receptor 3; FRgamma; FOLR3 TTSM9YR GN FOLR3 TTSM9YR FC Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate to the interior of cells. Isoform Short does not bind folate. TTSM9YR SQ MDMAWQMMQLLLLALVTAAGSAQPRSARARTDLLNVCMNAKHHKTQPSPEDELYGQCSPWKKNACCTASTSQELHKDTSRLYNFNWDHCGKMEPTCKRHFIQDSCLYECSPNLGPWIRQVNQSWRKERILNVPLCKEDCERWWEDCRTSYTCKSNWHKGWNWTSGINECPAGALCSTFESYFPTPAALCEGLWSHSFKVSNYSRGSGRCIQMWFDSAQGNPNEEVAKFYAAAMNAGAPSRGIIDS TTSM9YR TT Literature-reported TTDNM9W ID TTDNM9W TTDNM9W TN Follistatin (FST) TTDNM9W UP P19883 TTDNM9W UC FST_HUMAN TTDNM9W SN FST; FS; Activinbinding protein TTDNM9W GN FST TTDNM9W FC Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH). TTDNM9W PD 5JHW; 3HH2; 2P6A; 2B0U TTDNM9W SQ MVRARHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEDTEEEEEDEDQDYSFPISSILEW TTDNM9W TT Literature-reported TTWRPM8 ID TTWRPM8 TTWRPM8 TN Follistatin-related protein 3 (FSTL3) TTWRPM8 UP O95633 TTWRPM8 UC FSTL3_HUMAN TTWRPM8 SN UNQ674/PRO1308; Follistatin-related gene protein; Follistatin-related gene; Follistatin-like 3; FSTL3; FLRG TTWRPM8 GN FSTL3 TTWRPM8 FC Isoform 1 or the secreted form is a binding and antagonizing protein for members of the TGF-beta family, such us activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin Athan on activin B. Involved in bone formation; inhibits osteoclast differentiationc. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. Isoform 2 or the nuclear form is probably involved in transcriptional regulation via interaction with MLLT10. TTWRPM8 PD 3SEK; 3B4V; 2KCX TTWRPM8 SQ MRPGAPGPLWPLPWGALAWAVGFVSSMGSGNPAPGGVCWLQQGQEATCSLVLQTDVTRAECCASGNIDTAWSNLTHPGNKINLLGFLGLVHCLPCKDSCDGVECGPGKACRMLGGRPRCECAPDCSGLPARLQVCGSDGATYRDECELRAARCRGHPDLSVMYRGRCRKSCEHVVCPRPQSCVVDQTGSAHCVVCRAAPCPVPSSPGQELCGNNNVTYISSCHMRQATCFLGRSIGVRHAGSCAGTPEEPPGGESAEEEENFV TTWRPM8 TT Literature-reported TTJQ08V ID TTJQ08V TTJQ08V TN Foot-and-mouth disease virus Capsid VP1 (FMDV VP1) TTJQ08V UP P03305 (725-935) TTJQ08V UC POLG_FMDVO TTJQ08V SN Foot-and-mouth disease virus P1D; Foot-and-mouth disease virus Virion protein 1 TTJQ08V GN FMDV VP1 TTJQ08V FC Leader protease: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Cleaves also the host translation initiation factors EIF4G1 and EIF4G3, in order to shutoff the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechanisms. Possesses a deubiquitinase activity acting on both 'Lys'-48 and 'Lys'-63-linked polyubiquitin chains. In turn, inhibits the ubiquitination and subsequent activation of key signaling molecules of type I IFN response such as host DDX58, TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by inducing a decrease in RELA mRNA levels. Cleaves a peptide bond in the C-terminus of host ISG15, resulting in the damaging of this mofidier that can no longer be attached to target proteins. Cleaves also host G3BP1 and G3BP2 in order to inhibit cytoplasmic stress granules assembly. TTJQ08V PD 6FFA; 4QBB; 2JQG; 2JQF; 1QQP TTJQ08V SQ TTSAGESADPVTTTVENYGGETQIQRRQHTDVSFIMDRFVKVTPQNQINILDLMQIPSHTLVGALLRASTYYFSDLEIAVKHEGDLTWVPNGAPEKALDNTTNPTAYHKAPLTRLALPYTAPHRVLATVYNGECRYNRNAVPNLRGDLQVLAQKVARTLPTSFNYGAIKATRVTELLYRMKRAETYCPRPLLAIHPTEARHKQKIVAPVKQ TTJQ08V TT Literature-reported TTD9KFV ID TTD9KFV TTD9KFV TN Foot-and-mouth disease virus Capsid VP2 (FMDV VP2) TTD9KFV UP P03305 (287-504) TTD9KFV UC POLG_FMDVO TTD9KFV SN Foot-and-mouth disease virus P1B; Foot-and-mouth disease virus Virion protein 2 TTD9KFV GN FMDV VP2 TTD9KFV FC Leader protease: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Cleaves also the host translation initiation factors EIF4G1 and EIF4G3, in order to shutoff the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechanisms. Possesses a deubiquitinase activity acting on both 'Lys'-48 and 'Lys'-63-linked polyubiquitin chains. In turn, inhibits the ubiquitination and subsequent activation of key signaling molecules of type I IFN response such as host DDX58, TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by inducing a decrease in RELA mRNA levels. Cleaves a peptide bond in the C-terminus of host ISG15, resulting in the damaging of this mofidier that can no longer be attached to target proteins. Cleaves also host G3BP1 and G3BP2 in order to inhibit cytoplasmic stress granules assembly. TTD9KFV PD 6FFA; 4QBB; 2JQG; 2JQF; 1QQP TTD9KFV SQ DKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTYGYATAEDFVSGPNTSGLETRVVQAERFFKTHLFDWVTSDSFGRCHLLELPTDHKGVYGSLTDSYAYMRNGWDVEVTAVGNQFNGGCLLVAMVPELYSIQKRELYQLTLFPHQFINPRTNMTAHITVPFVGVNRYDQYKVHKPWTLVVMVVAPLTVNTEGAPQIKVYANIAPTNVHVAGEFPSKE TTD9KFV TT Literature-reported TTB27Y5 ID TTB27Y5 TTB27Y5 TN Foot-and-mouth disease virus Capsid VP3 (FMDV VP3) TTB27Y5 UP P03305 (505-724) TTB27Y5 UC POLG_FMDVO TTB27Y5 SN Foot-and-mouth disease virus P1C; Foot-and-mouth disease virus Virion protein 3 TTB27Y5 GN FMDV VP3 TTB27Y5 FC Leader protease: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Cleaves also the host translation initiation factors EIF4G1 and EIF4G3, in order to shutoff the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechanisms. Possesses a deubiquitinase activity acting on both 'Lys'-48 and 'Lys'-63-linked polyubiquitin chains. In turn, inhibits the ubiquitination and subsequent activation of key signaling molecules of type I IFN response such as host DDX58, TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by inducing a decrease in RELA mRNA levels. Cleaves a peptide bond in the C-terminus of host ISG15, resulting in the damaging of this mofidier that can no longer be attached to target proteins. Cleaves also host G3BP1 and G3BP2 in order to inhibit cytoplasmic stress granules assembly. TTB27Y5 PD 6FFA; 4QBB; 2JQG; 2JQF; 1QQP TTB27Y5 SQ GIFPVACSDGYGGLVTTDPKTADPVYGKVFNPPRNQLPGRFTNLLDVAEACPTFLRFEGGVPYVTTKTDSDRVLAQFDMSLAAKQMSNTFLAGLAQYYTQYSGTINLHFMFTGPTDAKARYMVAYAPPGMEPPKTPEAAAHCIHAEWDTGLNSKFTFSIPYLSAADYAYTASGVAETTNVQGWVCLFQITHGKADGDALVVLASAGKDFELRLPVDA TTB27Y5 TT Literature-reported TTLBAP1 ID TTLBAP1 TTLBAP1 TN Forkhead box protein C2 (FOXC2) TTLBAP1 UP Q99958 TTLBAP1 UC FOXC2_HUMAN TTLBAP1 SN Transcription factor FKH14; Mesenchyme fork head protein 1; MFH1 protein; Forkheadrelated protein FKHL14; FOXC2 TTLBAP1 GN FOXC2 TTLBAP1 FC Transcriptional activator. Might be involved in the formation of special mesenchymal tissues. TTLBAP1 PD 6AKP; 6AKO; 1D5V TTLBAP1 SQ MQARYSVSDPNALGVVPYLSEQNYYRAAGSYGGMASPMGVYSGHPEQYSAGMGRSYAPYHHHQPAAPKDLVKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVSKEKEERAHLKEPPPAASKGAPATPHLADAPKEAEKKVVIKSEAASPALPVITKVETLSPESALQGSPRSAASTPAGSPDGSLPEHHAAAPNGLPGFSVENIMTLRTSPPGGELSPGAGRAGLVVPPLALPYAAAPPAAYGQPCAQGLEAGAAGGYQCSMRAMSLYTGAERPAHMCVPPALDEALSDHPSGPTSPLSALNLAAGQEGALAATGHHHQHHGHHHPQAPPPPPAPQPQPTPQPGAAAAQAASWYLNHSGDLNHLPGHTFAAQQQTFPNVREMFNSHRLGIENSTLGESQVSGNASCQLPYRSTPPLYRHAAPYSYDCTKY TTLBAP1 TT Literature-reported TTY8LZG ID TTY8LZG TTY8LZG TN Fos-related antigen 1 (FOSL1) TTY8LZG UP P15407 TTY8LZG UC FOSL1_HUMAN TTY8LZG BC Basic leucine zipper bZIP TTY8LZG SN Fra-1; FRA1 TTY8LZG GN FOSL1 TTY8LZG FC DNA-binding transcription factor activity, DNA-binding transcription factor activity, RNA polymerase II-specific, RNA polymerase II proximal promoter sequence-specific DNA binding, cellular defense response, chemotaxis, positive regulation of cell population proliferation, positive regulation of DNA-templated transcription, initiation, pri-miRNA transcription by RNA polymerase II. TTY8LZG SQ MFRDFGEPGPSSGNGGGYGGPAQPPAAAQAAQQKFHLVPSINTMSGSQELQWMVQPHFLGPSSYPRPLTYPQYSPPQPRPGVIRALGPPPGVRRRPCEQISPEEEERRRVRRERNKLAAAKCRNRRKELTDFLQAETDKLEDEKSGLQREIEELQKQKERLELVLEAHRPICKIPEGAKEGDTGSTSGTSSPPAPCRPVPCISLSPGPVLEPEALHTPTLMTTPSLTPFTPSLVFTYPSTPEPCASAHRKSSSSSGDPSSDPLGSPTLLAL TTY8LZG TT Literature-reported TT689IR ID TT689IR TT689IR TN Fos-related antigen 2 (FOSL2) TT689IR UP P15408 TT689IR UC FOSL2_HUMAN TT689IR BC Basic leucine zipper bZIP TT689IR SN FRA2; FRA-2 TT689IR GN FOSL2 TT689IR FC As a dimer with JUN, activates LIF transcription. Activates CEBPB transcription in PGE2-activated osteoblasts. Controls osteoclast survival and size. TT689IR SQ MYQDYPGNFDTSSRGSSGSPAHAESYSSGGGGQQKFRVDMPGSGSAFIPTINAITTSQDLQWMVQPTVITSMSNPYPRSHPYSPLPGLASVPGHMALPRPGVIKTIGTTVGRRRRDEQLSPEEEEKRRIRRERNKLAAAKCRNRRRELTEKLQAETEELEEEKSGLQKEIAELQKEKEKLEFMLVAHGPVCKISPEERRSPPAPGLQPMRSGGGSVGAVVVKQEPLEEDSPSSSSAGLDKAQRSVIKPISIAGGFYGEEPLHTPIVVTSTPAVTPGTSNLVFTYPSVLEQESPASPSESCSKAHRRSSSSGDQSSDSLNSPTLLAL TT689IR TT Literature-reported TT1OFBQ ID TT1OFBQ TT1OFBQ TN Fractalkine (CX3CL1) TT1OFBQ UP P78423 TT1OFBQ UC X3CL1_HUMAN TT1OFBQ SN Small-inducible cytokine D1; Small inducible cytokine D1; SCYD1; Neurotactin; NTT; FKN; CX3C membrane-anchored chemokine; C-X3-C motif chemokine 1; A-152E5.2 TT1OFBQ GN CX3CL1 TT1OFBQ FC Binds to CX3CR1. Binds to integrins ITGAV:ITGB3 and ITGA4:ITGB1. Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner. In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins. In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1. The soluble form is chemotactic for T-cells and monocytes and not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Acts as a ligand for both CX3CR1 and integrins. TT1OFBQ PD 5WB2; 4XT3; 4XT1; 3ONA; 1F2L TT1OFBQ SQ MAPISLSWLLRLATFCHLTVLLAGQHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQWVKDAMQHLDRQAAALTRNGGTFEKQIGEVKPRTTPAAGGMDESVVLEPEATGESSSLEPTPSSQEAQRALGTSPELPTGVTGSSGTRLPPTPKAQDGGPVGTELFRVPPVSTAATWQSSAPHQPGPSLWAEAKTSEAPSTQDPSTQASTASSPAPEENAPSEGQRVWGQGQSPRPENSLEREEMGPVPAHTDAFQDWGPGSMAHVSVVPVSSEGTPSREPVASGSWTPKAEEPIHATMDPQRLGVLITPVPDAQAATRRQAVGLLAFLGLLFCLGVAMFTYQSLQGCPRKMAGEMAEGLRYIPRSCGSNSYVLVPV TT1OFBQ TT Literature-reported TT1OFBQ FM Transmembrane protein TTXDOHN ID TTXDOHN TTXDOHN TN Free fatty acid receptor 3 (FFAR3) TTXDOHN UP O14843 TTXDOHN UC FFAR3_HUMAN TTXDOHN BC GPCR rhodopsin TTXDOHN SN GPR41; G-protein coupled receptor 41 TTXDOHN GN FFAR3 TTXDOHN FC G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins. Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. Activated by SCFAs and by beta-hydroxybutyrate, a ketone body produced by the liver upon starvation, it inhibits N-type calcium channels and modulates the activity of sympathetic neurons through a signaling cascade involving the beta and gamma subunits of its coupled G protein, phospholipase C and MAP kinases. Thereby, it may regulate energy expenditure through the control of the sympathetic nervous system that controls for instance heart rate. Upon activation by SCFAs accumulating in the intestine, it may also signal to the brain via neural circuits which in turn would regulate intestinal gluconeogenesis. May also control the production of hormones involved in whole-body energy homeostasis. May for instance, regulate blood pressure through renin secretion. May also regulate secretion of the PYY peptide by enteroendocrine cells and control gut motility, intestinal transit rate, and the harvesting of energy from SCFAs produced by gut microbiota. May also indirectly regulate the production of LEP/Leptin, a hormone acting on the CNS to inhibit food intake, in response to the presence of short-chain fatty acids in the intestine. Finally, may also play a role in glucose homeostasis. Besides its role in energy homeostasis, may play a role in intestinal immunity. May mediate the activation of the inflammatory and immune response by SCFAs in the gut, regulating the rapid production of chemokines and cytokines by intestinal epithelial cells. Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably propionate, butyrate and pentanoate while acetate is a poor activator. TTXDOHN SQ MDTGPDQSYFSGNHWFVFSVYLLTFLVGLPLNLLALVVFVGKLQRRPVAVDVLLLNLTASDLLLLLFLPFRMVEAANGMHWPLPFILCPLSGFIFFTTIYLTALFLAAVSIERFLSVAHPLWYKTRPRLGQAGLVSVACWLLASAHCSVVYVIEFSGDISHSQGTNGTCYLEFRKDQLAILLPVRLEMAVVLFVVPLIITSYCYSRLVWILGRGGSHRRQRRVAGLLAATLLNFLVCFGPYNVSHVVGYICGESPAWRIYVTLLSTLNSCVDPFVYYFSSSGFQADFHELLRRLCGLWGQWQQESSMELKEQKGGEEQRADRPAERKTSEHSQGCGTGGQVACAES TTXDOHN TT Literature-reported TTBZG7K ID TTBZG7K TTBZG7K TN Fungal cAMP-dependent protein kinase (Fung pka1) TTBZG7K UP P40376 TTBZG7K UC KAPB_SCHPO TTBZG7K BC Kinase TTBZG7K SN cAMP-dependent protein kinase catalytic subunit TTBZG7K GN Fung pka1 TTBZG7K FC Has cAMP-dependent protein kinase and protein serine/threonine kinase activity. TTBZG7K SQ MDTTAVASKGSTNVGSSTDTLSTSASLHPSMNAGSVNEYSEQQRHGTNSFNGKPSVHDSVGSDASVSNGHNNHNESSLWTSGIPKALEEATKSKKPDSLVSTSTSGCASAHSVGYQNIDNLIPSPLPESASRSSSQSSHQRHSRDGRGELGSEHGERRSAMDGLRDRHIRKVRVSQLLDLQRRRIRPADHTTKDRYGIQDFNFLQTLGTGSFGRVHLVQSNHNRLYYAIKVLEKKKIVDMKQIEHTCDERYILSRVQHPFITILWGTFQDAKNLFMVMDFAEGGELFSLLRKCHRFPEKVAKFYAAEVILALDYLHHNQIVYRDLKPENLLLDRFGHLKIVDFGFAKRVSTSNCCTLCGTPDYLAPEIISLKPYNKAADWWSLGILIFEMLAGYPPFYSENPMKLYENILEGKVNYPSYFSPASIDLLSHLLQRDITCRYGNLKDGSMDIIMHPWFRDISWDKILTRKIEVPYVPPIQAGMGDSSQFDAYADVATDYGTSEDPEFTSIFKDF TTBZG7K TT Literature-reported TTH567K ID TTH567K TTH567K TN Fungal GDP-mannose transporter (Fung VRG4) TTH567K UP P40107 TTH567K UC GMT1_YEAST TTH567K SN VRG4 gene; VRG4; Golgi GDP-mannose transporter TTH567K GN Fung VRG4 TTH567K FC Involved in the import of GDP-mannose from the cytoplasminto the Golgi lumen. Defective copy causes severe glycosylation defect and abnormal retention of soluble endoplasmic reticulum proteins. Involved in vanadate sensitivity. TTH567K PD 5OGK; 5OGE TTH567K SQ MSELKTGHAGHNPWASVANSGPISILSYCGSSILMTVTNKFVVNLKDFNMNFVMLFVQSLVCTITLIILRILGYAKFRSLNKTDAKNWFPISFLLVLMIYTSSKALQYLAVPIYTIFKNLTIILIAYGEVLFFGGSVTSMELSSFLLMVLSSVVATWGDQQAVAAKAASLAEGAAGAVASFNPGYFWMFTNCITSALFVLIMRKRIKLTNFKDFDTMFYNNVLALPILLLFSFCVEDWSSVNLTNNFSNDSLTAMIISGVASVGISYCSGWCVRVTSSTTYSMVGALNKLPIALSGLIFFDAPRNFLSILSIFIGFLSGIIYAVAKQKKQQAQPLRK TTH567K TT Literature-reported TT0K7WC ID TT0K7WC TT0K7WC TN Fungal Glycosylphosphatidylinositol-aspartyl-protease (Fung MKC7) TT0K7WC UP P53379 TT0K7WC UC MKC7_YEAST TT0K7WC BC Peptidase TT0K7WC SN Yapsin 2; MKC7; Glycosylphosphatidylinositol-anchored protein; GPI-anchored aspartyl protease TT0K7WC GN Fung MKC7 TT0K7WC FC Cleaves proteins C-terminally to the most C-terminal basic residue. Can process the alpha-mating factor precursor. Required for cell wall integrity. TT0K7WC SQ MKLSVLTFVVDALLVCSSIVDAGVTDFPSLPSNEVYVKMNFQKKYGSSFENALDDTKGRTRLMTRDDDYELVELTNQNSFYSVELDIGTPPQKVTVLVDTGSSDLWVTGSDNPYCSTKKKDTTGSSFKQVNKDALASVVESVFTEISYDTTIVTSEATATFDSTASTSQLIDCATYGTFNTSKSSTFNSNNTEFSIAYGDTTFASGTWGHDQLSLNDLNITGLSFAVANETNSTVGVLGIGLPGLESTYSGVSLSSVQKSYTYNNFPMVLKNSGVIKSTAYSLFANDSDSKHGTILFGAVDHGKYAGDLYTIPIINTLQHRGYKDPIQFQVTLQGLGTSKGDKEDNLTTLTTTKIPVLLDSGTTISYMPTELVKMLADQVGATYSSAYGYYIMDCIKEMEEESSIIFDFGGFYLSNWLSDFQLVTDSRSNICILGIAPQSDPTIILGDNFLANTYVVYDLDNMEISMAQANFSDDGEYIEIIESAVPSALKAPGYSSTWSTYESIVSGGNMFSTAANSSISYFASTSHSATSSSSSKGQKTQTSTTALSISKSTSSTSSTGMLSPTSSSSTRKENGGHNLNPPFFARFITAIFHHI TT0K7WC TT Literature-reported TTSA20Z ID TTSA20Z TTSA20Z TN Fungal Kexin-like serine endoprotease (Fung klse) TTSA20Z UP Q9UVD0 TTSA20Z UC Q9UVD0_PNECA TTSA20Z BC Peptidase TTSA20Z SN Kexin-like serine endoprotease TTSA20Z GN Fung klse TTSA20Z FC Cleave secretory proproteins to their active forms. Required for N-Glycan processing, morphogenesis and virulence TTSA20Z SQ EPPAPPSQPEPPAPQPQPEPPAPPPQPEPPAPPPQPEPPAPPPQPEPPAPPSQPEPPAPPPQPEPPAPPPQPEPPAPPPKPQPEQKPTSITSSTFTTSSSKTKISTIRKASSTKTSSTTKTSTRPSPTEGTFTGSSASYLSFFEKRHLLLQMILLLFFFLFLSYSF TTSA20Z TT Literature-reported TT9XT7G ID TT9XT7G TT9XT7G TN Fungal Pre-mRNA splicing factor PRP8 (Fung PRP8) TT9XT7G UP P33334 TT9XT7G UC PRP8_YEAST TT9XT7G SN Prp8 intein; PRP8; Intein (PRP8) TT9XT7G GN Fung PRP8 TT9XT7G FC Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for association of BRR2 with the spliceosomal U5 snRNP, and the subsequent assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold thatpositions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site, as well as the branch region. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region. Also has a role in cell cycle. TT9XT7G PD 6J6Q; 6J6N; 6J6H; 6J6G; 6EXN TT9XT7G SQ MSGLPPPPPGFEEDSDLALPPPPPPPPGYEIEELDNPMVPSSVNEDTFLPPPPPPPSNFEINAEEIVDFTLPPPPPPPGLDELETKAEKKVELHGKRKLDIGKDTFVTRKSRKRAKKMTKKAKRSNLYTPKAEMPPEHLRKIINTHSDMASKMYNTDKKAFLGALKYLPHAILKLLENMPHPWEQAKEVKVLYHTSGAITFVNETPRVIEPVYTAQWSATWIAMRREKRDRTHFKRMRFPPFDDDEPPLSYEQHIENIEPLDPINLPLDSQDDEYVKDWLYDSRPLEEDSKKVNGTSYKKWSFDLPEMSNLYRLSTPLRDEVTDKNYYYLFDKKSFFNGKALNNAIPGGPKFEPLYPREEEEDYNEFNSIDRVIFRVPIRSEYKVAFPHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTPALFFDPSLNPIPHFIDNNSSLNVSNTKENGDFTLPEDFAPLLAEEEELILPNTKDAMSLYHSPFPFNRTKGKMVRAQDVALAKKWFLQHPDEEYPVKVKVSYQKLLKNYVLNELHPTLPTNHNKTKLLKSLKNTKYFQQTTIDWVEAGLQLCRQGHNMLNLLIHRKGLTYLHLDYNFNLKPTKTLTTKERKKSRLGNSFHLMRELLKMMKLIVDTHVQFRLGNVDAFQLADGIHYILNHIGQLTGIYRYKYKVMHQIRACKDLKHIIYYKFNKNLGKGPGCGFWQPAWRVWLNFLRGTIPLLERYIGNLITRQFEGRSNEIVKTTTKQRLDAYYDLELRNSVMDDILEMMPESIRQKKARTILQHLSEAWRCWKANIPWDVPGMPAPIKKIIERYIKSKADAWVSAAHYNRERIKRGAHVEKTMVKKNLGRLTRLWIKNEQERQRQIQKNGPEITPEEATTIFSVMVEWLESRSFSPIPFPPLTYKNDTKILVLALEDLKDVYASKVRLNASEREELALIEEAYDNPHDTLNRIKKYLLTQRVFKPVDITMMENYQNISPVYSVDPLEKITDAYLDQYLWYEADQRKLFPNWIKPSDSEIPPLLVYKWTQGINNLSEIWDVSRGQSAVLLETTLGEMAEKIDFTLLNRLLRLIVDPNIADYITAKNNVVINFKDMSHVNKYGLIRGLKFASFIFQYYGLVIDLLLLGQERATDLAGPANNPNEFMQFKSKEVEKAHPIRLYTRYLDRIYMLFHFEEDEGEELTDEYLAENPDPNFENSIGYNNRKCWPKDSRMRLIRQDVNLGRAVFWEIQSRVPTSLTSIKWENAFVSVYSKNNPNLLFSMCGFEVRILPRQRMEEVVSNDEGVWDLVDERTKQRTAKAYLKVSEEEIKKFDSRIRGILMASGSTTFTKVAAKWNTSLISLFTYFREAIVATEPLLDILVKGETRIQNRVKLGLNSKMPTRFPPAVFYTPKELGGLGMISASHILIPASDLSWSKQTDTGITHFRAGMTHEDEKLIPTIFRYITTWENEFLDSQRVWAEYATKRQEAIQQNRRLAFEELEGSWDRGIPRISTLFQRDRHTLAYDRGHRIRREFKQYSLERNSPFWWTNSHHDGKLWNLNAYRTDVIQALGGIETILEHTLFKGTGFNSWEGLFWEKASGFEDSMQFKKLTHAQRTGLSQIPNRRFTLWWSPTINRANVYVGFLVQLDLTGIFLHGKIPTLKISLIQIFRAHLWQKIHESIVFDICQILDGELDVLQIESVTKETVHPRKSYKMNSSAADITMESVHEWEVSKPSLLHETNDSFKGLITNKMWFDVQLRYGDYDSHDISRYVRAKFLDYTTDNVSMYPSPTGVMIGIDLAYNMYDAYGNWFNGLKPLIQNSMRTIMKANPALYVLRERIRKGLQIYQSSVQEPFLNSSNYAELFNNDIKLFVDDTNVYRVTVHKTFEGNVATKAINGCIFTLNPKTGHLFLKIIHTSVWAGQKRLSQLAKWKTAEEVSALVRSLPKEEQPKQIIVTRKAMLDPLEVHMLDFPNIAIRPTELRLPFSAAMSIDKLSDVVMKATEPQMVLFNIYDDWLDRISSYTAFSRLTLLLRALKTNEESAKMILLSDPTITIKSYHLWPSFTDEQWITIESQMRDLILTEYGRKYNVNISALTQTEIKDIILGQNIKAPSVKRQKMAELEAARSEKQNDEEAAGASTVMKTKTINAQGEEIVVVASADYESQTFSSKNEWRKSAIANTLLYLRLKNIYVSADDFVEEQNVYVLPKNLLKKFIEISDVKIQVAAFIYGMSAKDHPKVKEIKTVVLVPQLGHVGSVQISNIPDIGDLPDTEGLELLGWIHTQTEELKFMAASEVATHSKLFADKKRDCIDISIFSTPGSVSLSAYNLTDEGYQWGEENKDIMNVLSEGFEPTFSTHAQLLLSDRITGNFIIPSGNVWNYTFMGTAFNQEGDYNFKYGIPLEFYNEMHRPVHFLQFSELAGDEELEAEQIDVFS TT9XT7G TT Literature-reported TTC4SOT ID TTC4SOT TTC4SOT TN Fungal Pyridoxin biosynthesis pyroA (Fung pyroA) TTC4SOT UP Q9UW83 TTC4SOT UC PDX1_EMENI TTC4SOT SN pyroA; Pdx1 homolog TTC4SOT GN Fung pyroA TTC4SOT FC Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen- generating photosensitizers. TTC4SOT EC EC 4.3.3.6 TTC4SOT SQ MAATNGASNDFTVKAGLAQMLKGGVIMDVVNAEQARIAEEAGAAAVMALERVPADIRAQGGVARMSDPSMIKEIMEAVTIPVMAKARIGHFVECQILEAIGVDYIDESEVLTPADNLYHVTKHNFKAPFVCGCRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVKHMRTVNAEIARARAILQSSPDPEPELRAYARELEAPYELLREAAEKGRLPVVNFAAGGVATPADAALMMQLGCDGVFVGSGIFKSGDAKKRAKAIVQAVTHYKDPKVLAEVSQGLGEAMVGINVSHMKDEDKLAKRGW TTC4SOT TT Literature-reported TTUKZVG ID TTUKZVG TTUKZVG TN G protein coupled receptor 101 (GPR101) TTUKZVG UP Q96P66 TTUKZVG UC GP101_HUMAN TTUKZVG BC GPCR rhodopsin TTUKZVG SN Probable Gprotein coupled receptor 101; GPR101 TTUKZVG GN GPR101 TTUKZVG FC Orphan receptor. TTUKZVG SQ MTSTCTNSTRESNSSHTCMPLSKMPISLAHGIIRSTVLVIFLAASFVGNIVLALVLQRKPQLLQVTNRFIFNLLVTDLLQISLVAPWVVATSVPLFWPLNSHFCTALVSLTHLFAFASVNTIVVVSVDRYLSIIHPLSYPSKMTQRRGYLLLYGTWIVAILQSTPPLYGWGQAAFDERNALCSMIWGASPSYTILSVVSFIVIPLIVMIACYSVVFCAARRQHALLYNVKRHSLEVRVKDCVENEDEEGAEKKEEFQDESEFRRQHEGEVKAKEGRMEAKDGSLKAKEGSTGTSESSVEARGSEEVRESSTVASDGSMEGKEGSTKVEENSMKADKGRTEVNQCSIDLGEDDMEFGEDDINFSEDDVEAVNIPESLPPSRRNSNSNPPLPRCYQCKAAKVIFIIIFSYVLSLGPYCFLAVLAVWVDVETQVPQWVITIIIWLFFLQCCIHPYVYGYMHKTIKKEIQDMLKKFFCKEKPPKEDSHPDLPGTEGGTEGKIVPSYDSATFP TTUKZVG TT Literature-reported TTT23CG ID TTT23CG TTT23CG TN G protein coupled receptor 182 (GPR182) TTT23CG UP O15218 TTT23CG UC GP182_HUMAN TTT23CG BC GPCR rhodopsin TTT23CG SN Gprotein coupled receptor 182; GPR182 TTT23CG GN GPR182 TTT23CG FC Orphan receptor. TTT23CG SQ MSVKPSWGPGPSEGVTAVPTSDLGEIHNWTELLDLFNHTLSECHVELSQSTKRVVLFALYLAMFVVGLVENLLVICVNWRGSGRAGLMNLYILNMAIADLGIVLSLPVWMLEVTLDYTWLWGSFSCRFTHYFYFVNMYSSIFFLVCLSVDRYVTLTSASPSWQRYQHRVRRAMCAGIWVLSAIIPLPEVVHIQLVEGPEPMCLFMAPFETYSTWALAVALSTTILGFLLPFPLITVFNVLTACRLRQPGQPKSRRHCLLLCAYVAVFVMCWLPYHVTLLLLTLHGTHISLHCHLVHLLYFFYDVIDCFSMLHCVINPILYNFLSPHFRGRLLNAVVHYLPKDQTKAGTCASSSSCSTQHSIIITKGDSQPAAAAPHPEPSLSFQAHHLLPNTSPISPTQPLTPS TTT23CG TT Literature-reported TTKB7T3 ID TTKB7T3 TTKB7T3 TN G0/G1 switch regulatory protein 8 (RGS2) TTKB7T3 UP P41220 TTKB7T3 UC RGS2_HUMAN TTKB7T3 SN Regulator of G-protein signaling 2; GIG31; G0S8; Cell growth-inhibiting gene 31 protein TTKB7T3 GN RGS2 TTKB7T3 FC Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. It is involved in the negative regulation of the angiotensin-activated signaling pathway. Plays a role in the regulation of blood pressure in response to signaling via G protein-coupled receptors and GNAQ. Plays a role in regulating the constriction and relaxation of vascular smooth muscle. Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein. Regulates G protein-coupled receptor signaling cascades. TTKB7T3 PD 4EKD; 4EKC; 2V4Z; 2AF0 TTKB7T3 SQ MQSAMFLAVQHDCRPMDKSAGSGHKSEEKREKMKRTLLKDWKTRLSYFLQNSSTPGKPKTGKKSKQQAFIKPSPEEAQLWSEAFDELLASKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSSKARKIYTDFIEKEAPKEINIDFQTKTLIAQNIQEATSGCFTTAQKRVYSLMENNSYPRFLESEFYQDLCKKPQITTEPHAT TTKB7T3 TT Literature-reported TTXZAJ5 ID TTXZAJ5 TTXZAJ5 TN Galanin (GAL) TTXZAJ5 UP P22466 TTXZAJ5 UC GALA_HUMAN TTXZAJ5 BC Galanin family TTXZAJ5 SN Galanin peptides; Galanin messageassociated peptide; GMAP; GAL TTXZAJ5 GN GAL TTXZAJ5 FC Contracts smooth muscle of the gastrointestinal and genitourinary tract, regulates growth hormone release, modulates insulin release, and may be involved in the control of adrenal secretion. TTXZAJ5 SQ MARGSALLLASLLLAAALSASAGLWSPAKEKRGWTLNSAGYLLGPHAVGNHRSFSDKNGLTSKRELRPEDDMKPGSFDRSIPENNIMRTIIEFLSFLHLKEAGALDRLLDLPAAASSEDIERS TTXZAJ5 TT Literature-reported TTO3NYT ID TTO3NYT TTO3NYT TN Galectin-1 (LGALS1) TTO3NYT UP P09382 TTO3NYT UC LEG1_HUMAN TTO3NYT SN SLac lectin 1; S-Lac lectin 1; Putative MAPKactivating protein PM12; Putative MAPK-activating protein PM12; Lectin galactosidebinding soluble 1; Lectin galactoside-binding soluble 1; Lactosebinding lectin 1; Lactose-binding lectin 1; HPL; HLBP14; HBL; Galaptin; Gal1; Gal-1; Betagalactosidebinding lectin L14I; Beta-galactoside-binding lectin L-14-I; 14 kDa lectin; 14 kDa lamininbinding protein; 14 kDa laminin-binding protein TTO3NYT GN LGALS1 TTO3NYT FC Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. Lectin that binds beta-galactoside and a wide array of complex carbohydrates. TTO3NYT PD 6F83; 6B94; 5MWX; 5MWT; 4Y24 TTO3NYT SQ MACGLVASNLNLKPGECLRVRGEVAPDAKSFVLNLGKDSNNLCLHFNPRFNAHGDANTIVCNSKDGGAWGTEQREAVFPFQPGSVAEVCITFDQANLTVKLPDGYEFKFPNRLNLEAINYMAADGDFKIKCVAFD TTO3NYT TT Patented-recorded TTRHK90 ID TTRHK90 TTRHK90 TN Galectin-2 (LGALS2) TTRHK90 UP P05162 TTRHK90 UC LEG2_HUMAN TTRHK90 SN SLac lectin 2; Lactosebinding lectin 2; LGALS2; HL14; Gal2; Betagalactosidebinding lectin L14II TTRHK90 GN LGALS2 TTRHK90 FC This protein binds beta-galactoside. Its physiological function is not yet known. TTRHK90 PD 5EWS; 5DG2; 5DG1; 1HLC TTRHK90 SQ MTGELEVKNMDMKPGSTLKITGSIADGTDGFVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGSEVKFTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKLKE TTRHK90 TT Literature-reported TTGAZF9 ID TTGAZF9 TTGAZF9 TN Gamma-actin (ACTG) TTGAZF9 UP P63261 TTGAZF9 UC ACTG_HUMAN TTGAZF9 SN Actin, cytoplasmic 2; ACTG TTGAZF9 GN ACTG1 TTGAZF9 FC Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. TTGAZF9 PD 6G2T; 6CXJ; 6CXI; 5JLH TTGAZF9 SQ MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF TTGAZF9 TT Literature-reported TTHVBOC ID TTHVBOC TTHVBOC TN Gamma-aminobutyric acid transporter 4 (SLC6A11) TTHVBOC UP P48066 TTHVBOC UC S6A11_HUMAN TTHVBOC BC Neurotransmitter:sodium symporter TTHVBOC SN Sodium- and chloride-dependent GABA transporter 4; Slc6a11; GAT4; GABA transporter 4 TTHVBOC GN Slc6a11 TTHVBOC FC Terminates the action of GABA by its high affinity sodium-dependent reuptake into presynaptic terminals. Can also transport beta-alanine and taurine. TTHVBOC SQ MTAEKALPLGNGKAAEEARESEAPGGGCSSGGAAPARHPRVKRDKAVHERGHWNNKVEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFLIPYVVFFICCGIPVFFLETALGQFTSEGGITCWRKVCPLFEGIGYATQVIEAHLNVYYIIILAWAIFYLSNCFTTELPWATCGHEWNTENCVEFQKLNVSNYSHVSLQNATSPVMEFWEHRVLAISDGIEHIGNLRWELALCLLAAWTICYFCIWKGTKSTGKVVYVTATFPYIMLLILLIRGVTLPGASEGIKFYLYPDLSRLSDPQVWVDAGTQIFFSYAICLGCLTALGSYNNYNNNCYRDCIMLCCLNSGTSFVAGFAIFSVLGFMAYEQGVPIAEVAESGPGLAFIAYPKAVTMMPLSPLWATLFFMMLIFLGLDSQFVCVESLVTAVVDMYPKVFRRGYRRELLILALSVISYFLGLVMLTEGGMYIFQLFDSYAASGMCLLFVAIFECICIGWVYGSNRFYDNIEDMIGYRPPSLIKWCWMIMTPGICAGIFIFFLIKYKPLKYNNIYTYPAWGYGIGWLMALSSMLCIPLWICITVWKTEGTLPEKLQKLTTPSTDLKMRGKLGVSPRMVTVNDCDAKLKSDGTIAAITEKETHF TTHVBOC TT Literature-reported TTNQTLJ ID TTNQTLJ TTNQTLJ TN Gamma-Histone H2AX (H2AFX) TTNQTLJ UP P16104 TTNQTLJ UC H2AX_HUMAN TTNQTLJ SN Phosphorylation of H2AX; Histone H2AX; Histone H2A.x; H2a/x; H2AX TTNQTLJ GN H2AFX TTNQTLJ FC Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation. Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. TTNQTLJ PD 3U3Z; 3SZM; 3SQD; 3SHV; 2DYP TTNQTLJ SQ MSGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTSATVGPKAPSGGKKATQASQEY TTNQTLJ TT Literature-reported TT5TQNZ ID TT5TQNZ TT5TQNZ TN Gamma-synuclein (SNCG) TT5TQNZ UP O76070 TT5TQNZ UC SYUG_HUMAN TT5TQNZ BC Synuclein TT5TQNZ SN Synoretin; Persyn; PRSN; Breast cancer-specific gene 1 protein; BCSG1 TT5TQNZ GN SNCG TT5TQNZ FC May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases. May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway. Plays a role in neurofilament network integrity. TT5TQNZ SQ MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGAKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVATKTVEEAENIAVTSGVVRKEDLRPSAPQQEGEASKEKEEVAEEAQSGGD TT5TQNZ TT Literature-reported TT2H4LN ID TT2H4LN TT2H4LN TN Gankyrin (PSMD10) TT2H4LN UP O75832 TT2H4LN UC PSD10_HUMAN TT2H4LN SN p28(GANK); 26S proteasome regulatory subunit p28; 26S proteasome non-ATPase regulatory subunit 10 TT2H4LN GN PSMD10 TT2H4LN FC In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis. Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). TT2H4LN PD 5VHR; 5VHQ; 5VHP; 5VHO; 5VHN TT2H4LN SQ MEGCVSNLMVCNLAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAKGGLGLILKRMVEG TT2H4LN TT Literature-reported TTFZRG0 ID TTFZRG0 TTFZRG0 TN Gap junction alpha-3 protein (Cx46) TTFZRG0 UP Q9Y6H8 TTFZRG0 UC CXA3_HUMAN TTFZRG0 BC Gap junction-forming connexin TTFZRG0 SN Connexin-46 TTFZRG0 GN GJA3 TTFZRG0 FC Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore. Structural component of lens fiber gap junctions. TTFZRG0 SQ MGDWSFLGRLLENAQEHSTVIGKVWLTVLFIFRILVLGAAAEDVWGDEQSDFTCNTQQPGCENVCYDRAFPISHIRFWALQIIFVSTPTLIYLGHVLHIVRMEEKKKEREEEEQLKRESPSPKEPPQDNPSSRDDRGRVRMAGALLRTYVFNIIFKTLFEVGFIAGQYFLYGFELKPLYRCDRWPCPNTVDCFISRPTEKTIFIIFMLAVACASLLLNMLEIYHLGWKKLKQGVTSRLGPDASEAPLGTADPPPLPPSSRPPAVAIGFPPYYAHTAAPLGQARAVGYPGAPPPAADFKLLALTEARGKGQSAKLYNGHHHLLMTEQNWANQAAERQPPALKAYPAASTPAAPSPVGSSSPPLAHEAEAGAAPLLLDGSGSSLEGSALAGTPEEEEQAVTTAAQMHQPPLPLGDPGRASKASRASSGRARPEDLAI TTFZRG0 TT Literature-reported TTQO1VY ID TTQO1VY TTQO1VY TN Gap junction alpha-4 protein (Cx37) TTQO1VY UP P35212 TTQO1VY UC CXA4_HUMAN TTQO1VY BC Gap junction-forming connexin TTQO1VY SN Connexin-37 TTQO1VY GN GJA4 TTQO1VY FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTQO1VY SQ MGDWGFLEKLLDQVQEHSTVVGKIWLTVLFIFRILILGLAGESVWGDEQSDFECNTAQPGCTNVCYDQAFPISHIRYWVLQFLFVSTPTLVYLGHVIYLSRREERLRQKEGELRALPAKDPQVERALAAVERQMAKISVAEDGRLRIRGALMGTYVASVLCKSVLEAGFLYGQWRLYGWTMEPVFVCQRAPCPYLVDCFVSRPTEKTIFIIFMLVVGLISLVLNLLELVHLLCRCLSRGMRARQGQDAPPTQGTSSDPYTDQVFFYLPVGQGPSSPPCPTYNGLSSSEQNWANLTTEERLASSRPPLFLDPPPQNGQKPPSRPSSSASKKQYV TTQO1VY TT Literature-reported TTFQKZ7 ID TTFQKZ7 TTFQKZ7 TN Gap junction alpha-5 protein (Cx40) TTFQKZ7 UP P36382 TTFQKZ7 UC CXA5_HUMAN TTFQKZ7 BC Gap junction-forming connexin TTFQKZ7 SN Connexin-40 TTFQKZ7 GN GJA5 TTFQKZ7 FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTFQKZ7 SQ MGDWSFLGNFLEEVHKHSTVVGKVWLTVLFIFRMLVLGTAAESSWGDEQADFRCDTIQPGCQNVCYDQAFPISHIRYWVLQIIFVSTPSLVYMGHAMHTVRMQEKRKLREAERAKEVRGSGSYEYPVAEKAELSCWEEGNGRIALQGTLLNTYVCSILIRTTMEVGFIVGQYFIYGIFLTTLHVCRRSPCPHPVNCYVSRPTEKNVFIVFMLAVAALSLLLSLAELYHLGWKKIRQRFVKPRQHMAKCQLSGPSVGIVQSCTPPPDFNQCLENGPGGKFFNPFSNNMASQQNTDNLVTEQVRGQEQTPGEGFIQVRYGQKPEVPNGVSPGHRLPHGYHSDKRRLSKASSKARSDDLSV TTFQKZ7 TT Literature-reported TTJ7ATH ID TTJ7ATH TTJ7ATH TN Gap junction alpha-8 protein (Cx50) TTJ7ATH UP P48165 TTJ7ATH UC CXA8_HUMAN TTJ7ATH BC Gap junction-forming connexin TTJ7ATH SN Lens fiber protein MP70; GJA8; Cx50; Connexin50 TTJ7ATH GN GJA8 TTJ7ATH FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTJ7ATH SQ MGDWSFLGNILEEVNEHSTVIGRVWLTVLFIFRILILGTAAEFVWGDEQSDFVCNTQQPGCENVCYDEAFPISHIRLWVLQIIFVSTPSLMYVGHAVHYVRMEEKRKSREAEELGQQAGTNGGPDQGSVKKSSGSKGTKKFRLEGTLLRTYICHIIFKTLFEVGFIVGHYFLYGFRILPLYRCSRWPCPNVVDCFVSRPTEKTIFILFMLSVASVSLFLNVMELGHLGLKGIRSALKRPVEQPLGEIPEKSLHSIAVSSIQKAKGYQLLEEEKIVSHYFPLTEVGMVETSPLPAKPFNQFEEKISTGPLGDLSRGYQETLPSYAQVGAQEVEGEGPPAEEGAEPEVGEKKEEAERLTTEEQEKVAVPEGEKVETPGVDKEGEKEEPQSEKVSKQGLPAEKTPSLCPELTTDDARPLSRLSKASSRARSDDLTV TTJ7ATH TT Literature-reported TTVRQ8L ID TTVRQ8L TTVRQ8L TN Gap junction beta-3 protein (Cx31) TTVRQ8L UP O75712 TTVRQ8L UC CXB3_HUMAN TTVRQ8L BC Gap junction-forming connexin TTVRQ8L SN Connexin-31; CX31 TTVRQ8L GN GJB3 TTVRQ8L FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTVRQ8L SQ MDWKTLQALLSGVNKYSTAFGRIWLSVVFVFRVLVYVVAAERVWGDEQKDFDCNTKQPGCTNVCYDNYFPISNIRLWALQLIFVTCPSLLVILHVAYREERERRHRQKHGDQCAKLYDNAGKKHGGLWWTYLFSLIFKLIIEFLFLYLLHTLWHGFNMPRLVQCANVAPCPNIVDCYIARPTEKKIFTYFMVGASAVCIVLTICELCYLICHRVLRGLHKDKPRGGCSPSSSASRASTCRCHHKLVEAGEVDPDPGNNKLQASAPNLTPI TTVRQ8L TT Literature-reported TTBRDFI ID TTBRDFI TTBRDFI TN Gap junction beta-4 protein (Cx30.3) TTBRDFI UP Q9NTQ9 TTBRDFI UC CXB4_HUMAN TTBRDFI BC Gap junction-forming connexin TTBRDFI SN Connexin-30.3 TTBRDFI GN GJB4 TTBRDFI FC Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore. Structural component of gap junctions. TTBRDFI SQ MNWAFLQGLLSGVNKYSTVLSRIWLSVVFIFRVLVYVVAAEEVWDDEQKDFVCNTKQPGCPNVCYDEFFPVSHVRLWALQLILVTCPSLLVVMHVAYREERERKHHLKHGPNAPSLYDNLSKKRGGLWWTYLLSLIFKAAVDAGFLYIFHRLYKDYDMPRVVACSVEPCPHTVDCYISRPTEKKVFTYFMVTTAAICILLNLSEVFYLVGKRCMEIFGPRHRRPRCRECLPDTCPPYVLSQGGHPEDGNSVLMKAGSAPVDAGGYP TTBRDFI TT Literature-reported TTL9MHP ID TTL9MHP TTL9MHP TN Gap junction beta-5 protein (Cx31.1) TTL9MHP UP O95377 TTL9MHP UC CXB5_HUMAN TTL9MHP BC Gap junction-forming connexin TTL9MHP SN Connexin-31.1 TTL9MHP GN GJB5 TTL9MHP FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTL9MHP SQ MNWSIFEGLLSGVNKYSTAFGRIWLSLVFIFRVLVYLVTAERVWSDDHKDFDCNTRQPGCSNVCFDEFFPVSHVRLWALQLILVTCPSLLVVMHVAYREVQEKRHREAHGENSGRLYLNPGKKRGGLWWTYVCSLVFKASVDIAFLYVFHSFYPKYILPPVVKCHADPCPNIVDCFISKPSEKNIFTLFMVATAAICILLNLVELIYLVSKRCHECLAARKAQAMCTGHHPHGTTSSCKQDDLLSGDLIFLGSDSHPPLLPDRPRDHVKKTIL TTL9MHP TT Literature-reported TT7C18W ID TT7C18W TT7C18W TN Gap junction delta-3 protein (Cx31.9) TT7C18W UP Q8N144 TT7C18W UC CXD3_HUMAN TT7C18W BC Gap junction-forming connexin TT7C18W SN Gap junction chi-1 protein; Gap junction alpha-11 protein; GJC1; GJA11; Connexin-31.9 TT7C18W GN GJD3 TT7C18W FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TT7C18W SQ MGEWAFLGSLLDAVQLQSPLVGRLWLVVMLIFRILVLATVGGAVFEDEQEEFVCNTLQPGCRQTCYDRAFPVSHYRFWLFHILLLSAPPVLFVVYSMHRAGKEAGGAEAAAQCAPGLPEAQCAPCALRARRARRCYLLSVALRLLAELTFLGGQALLYGFRVAPHFACAGPPCPHTVDCFVSRPTEKTVFVLFYFAVGLLSALLSVAELGHLLWKGRPRAGERDNRCNRAHEEAQKLLPPPPPPPPPPALPSRRPGPEPCAPPAYAHPAPASLRECGSGRGKASPATGRRDLAI TT7C18W TT Literature-reported TTL07NQ ID TTL07NQ TTL07NQ TN Gap junction delta-4 protein (Cx40.1) TTL07NQ UP Q96KN9 TTL07NQ UC CXD4_HUMAN TTL07NQ BC Gap junction-forming connexin TTL07NQ SN Connexin-40.1; CX40.1 TTL07NQ GN GJD4 TTL07NQ FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTL07NQ SQ MEGVDLLGFLIITLNCNVTMVGKLWFVLTMLLRMLVIVLAGRPVYQDEQERFVCNTLQPGCANVCYDVFSPVSHLRFWLIQGVCVLLPSAVFSVYVLHRGATLAALGPRRCPDPREPASGQRRCPRPFGERGGLQVPDFSAGYIIHLLLRTLLEAAFGALHYFLFGFLAPKKFPCTRPPCTGVVDCYVSRPTEKSLLMLFLWAVSALSFLLGLADLVCSLRRRMRRRPGPPTSPSIRKQSGASGHAEGRRTDEEGGREEEGAPAPPGARAGGEGAGSPRRTSRVSGHTKIPDEDESEVTSSASEKLGRQPRGRPHREAAQDPRGSGSEEQPSAAPSRLAAPPSCSSLQPPDPPASSSGAPHLRARKSEWV TTL07NQ TT Literature-reported TTPOCAL ID TTPOCAL TTPOCAL TN Gap junction gamma-2 protein (Cx47) TTPOCAL UP Q5T442 TTPOCAL UC CXG2_HUMAN TTPOCAL BC Gap junction-forming connexin TTPOCAL SN Gap junction alpha-12 protein; GJA12; Cx46.6; Connexin-47; Connexin-46.6 TTPOCAL GN GJC2 TTPOCAL FC May play a role in myelination in central and peripheral nervous systems. One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTPOCAL SQ MTNMSWSFLTRLLEEIHNHSTFVGKVWLTVLVVFRIVLTAVGGEAIYSDEQAKFTCNTRQPGCDNVCYDAFAPLSHVRFWVFQIVVISTPSVMYLGYAVHRLARASEQERRRALRRRPGPRRAPRAHLPPPHAGWPEPADLGEEEPMLGLGEEEEEEETGAAEGAGEEAEEAGAEEACTKAVGADGKAAGTPGPTGQHDGRRRIQREGLMRVYVAQLVARAAFEVAFLVGQYLLYGFEVRPFFPCSRQPCPHVVDCFVSRPTEKTVFLLVMYVVSCLCLLLNLCEMAHLGLGSAQDAVRGRRGPPASAPAPAPRPPPCAFPAAAAGLACPPDYSLVVRAAERARAHDQNLANLALQALRDGAAAGDRDRDSSPCVGLPAASRGPPRAGAPASRTGSATSAGTVGEQGRPGTHERPGAKPRAGSEKGSASSRDGKTTVWI TTPOCAL TT Literature-reported TTUW608 ID TTUW608 TTUW608 TN Gap junction gamma-3 protein (Cx30.2) TTUW608 UP Q8NFK1 TTUW608 UC CXG3_HUMAN TTUW608 BC Gap junction-forming connexin TTUW608 SN Gap junction epsilon-1 protein; GJE1; Cx31.3; Connexin-31.3; Connexin-30.2 TTUW608 GN GJC3 TTUW608 FC One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. TTUW608 SQ MCGRFLRRLLAEESRRSTPVGRLLLPVLLGFRLVLLAASGPGVYGDEQSEFVCHTQQPGCKAACFDAFHPLSPLRFWVFQVILVAVPSALYMGFTLYHVIWHWELSGKGKEEETLIQGREGNTDVPGAGSLRLLWAYVAQLGARLVLEGAALGLQYHLYGFQMPSSFACRREPCLGSITCNLSRPSEKTIFLKTMFGVSGFCLLFTFLELVLLGLGRWWRTWKHKSSSSKYFLTSESTRRHKKATDSLPVVETKEQFQEAVPGRSLAQEKQRPVGPRDA TTUW608 TT Literature-reported TTAT6C7 ID TTAT6C7 TTAT6C7 TN GAP-associated tyrosine phosphoprotein p62 (KHDRBS1) TTAT6C7 UP Q07666 TTAT6C7 UC KHDR1_HUMAN TTAT6C7 SN p68; p21 Ras GTPaseactivating proteinassociated p62; p21 Ras GTPase-activating protein-associated p62; Srcassociated in mitosis 68 kDa protein; Src-associated in mitosis 68 kDa protein; Sam68; KH domaincontaining, RNAbinding, signal transductionassociated protein 1; KH domain-containing, RNA-binding, signal transduction-associated protein 1; GAPassociated tyrosine phosphoprotein p62 TTAT6C7 GN KHDRBS1 TTAT6C7 FC Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to. RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner. In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1. Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4. Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. TTAT6C7 PD 3QHE; 2XA6 TTAT6C7 SQ MQRRDDPAARMSRSSGRSGSMDPSGAHPSVRQTPSRQPPLPHRSRGGGGGSRGGARASPATQPPPLLPPSATGPDATVGGPAPTPLLPPSATASVKMEPENKYLPELMAEKDSLDPSFTHAMQLLTAEIEKIQKGDSKKDDEENYLDLFSHKNMKLKERVLIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFIEVFGPPCEAYALMAHAMEEVKKFLVPDMMDDICQEQFLELSYLNGVPEPSRGRGVPVRGRGAAPPPPPVPRGRGVGPPRGALVRGTPVRGAITRGATVTRGVPPPPTVRGAPAPRARTAGIQRIPLPPPPAPETYEEYGYDDTYAEQSYEGYEGYYSQSQGDSEYYDYGHGEVQDSYEAYGQDDWNGTRPSLKAPPARPVKGAYREHPYGRY TTAT6C7 TT Literature-reported TT390KA ID TT390KA TT390KA TN Geminin (GMNN) TT390KA UP O75496 TT390KA UC GEMI_HUMAN TT390KA SN geminin DNA replication inhibitor; MGORS6 TT390KA GN GMNN TT390KA FC It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle. Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC). TT390KA PD 4BRY; 2WVR; 2LP0; 1UII; 1T6F TT390KA SQ MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI TT390KA TT Literature-reported TT390KA FM Geminin family TTPZ5IQ ID TTPZ5IQ TTPZ5IQ TN Geranylgeranyl transferase II (GGTase-II) TTPZ5IQ UP Q92696; P53611 TTPZ5IQ UC PGTA_HUMAN; PGTB2_HUMAN TTPZ5IQ BC Alkyl aryl transferase TTPZ5IQ SN Rab geranylgeranyltransferase; Rab geranyl-geranyltransferase; Rab GGTase; Rab GG transferase; Geranylgeranyl transferase type-2; Geranylgeranyl transferase type II TTPZ5IQ GN RABGGTA; RABGGTB TTPZ5IQ FC Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. TTPZ5IQ SQ MHGRLKVKTSEEQAEAKRLEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQQLETQKSPEELAALVKAELGFLESCLRVNPKSYGTWHHRCWLLGRLPEPNWTRELELCARFLEVDERNFHCWDYRRFVATQAAVPPAEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPEDVLLKELELVQNAFFTDPNDQSAWFYHRWLLGRADPQDALRCLHVSRDEACLTVSFSRPLLVGSRMEILLLMVDDSPLIVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWTAGDVQKECVLLKGRQEGWCRDSTTDEQLFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLQYFQTLKAVDPMRATYLDDLRSKFLLENSVLKMEYAEVRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRTLPPALAALRCLEVLQASDNAIESLDGVTNLPRLQELLLCNNRLQQPAVLQPLASCPRLVLLNLQGNPLCQAVGILEQLAELLPSVSSVLT TTPZ5IQ TT Literature-reported TT045OH ID TT045OH TT045OH TN GLI2 messenger RNA (GLI2 mRNA) TT045OH UP P10070 TT045OH UC GLI2_HUMAN TT045OH BC mRNA target TT045OH SN Zinc finger protein GLI2 (mRNA); Tax helper protein (mRNA); THP (mRNA); GLI family zinc finger protein 2 (mRNA) TT045OH GN GLI2 TT045OH FC Functions as transcriptional activator. May also function as transcriptional repressor. Requires STK36 for full transcriptional activator activity. Required for normal embryonic development. Functions as transcription regulator in the hedgehog (Hh) pathway. TT045OH SQ METSASATASEKQEAKSGILEAAGFPDPGKKASPLVVAAAAAAAVAAQGVPQHLLPPFHAPLPIDMRHQEGRYHYEPHSVHGVHGPPALSGSPVISDISLIRLSPHPAGPGESPFNAPHPYVNPHMEHYLRSVHSSPTLSMISAARGLSPADVAQEHLKERGLFGLPAPGTTPSDYYHQMTLVAGHPAPYGDLLMQSGGAASAPHLHDYLNPVDVSRFSSPRVTPRLSRKRALSISPLSDASLDLQRMIRTSPNSLVAYINNSRSSSAASGSYGHLSAGALSPAFTFPHPINPVAYQQILSQQRGLGSAFGHTPPLIQPSPTFLAQQPMALTSINATPTQLSSSSNCLSDTNQNKQSSESAVSSTVNPVAIHKRSKVKTEPEGLRPASPLALTQGQVSGHGSCGCALPLSQEQLADLKEDLDRDDCKQEAEVVIYETNCHWEDCTKEYDTQEQLVHHINNEHIHGEKKEFVCRWQACTREQKPFKAQYMLVVHMRRHTGEKPHKCTFEGCSKAYSRLENLKTHLRSHTGEKPYVCEHEGCNKAFSNASDRAKHQNRTHSNEKPYICKIPGCTKRYTDPSSLRKHVKTVHGPDAHVTKKQRNDVHLRTPLLKENGDSEAGTEPGGPESTEASSTSQAVEDCLHVRAIKTESSGLCQSSPGAQSSCSSEPSPLGSAPNNDSGVEMPGTGPGSLGDLTALDDTPPGADTSALAAPSAGGLQLRKHMTTMHRFEQLKKEKLKSLKDSCSWAGPTPHTRNTKLPPLPGSGSILENFSGSGGGGPAGLLPNPRLSELSASEVTMLSQLQERRDSSTSTVSSAYTVSRRSSGISPYFSSRRSSEASPLGAGRPHNASSADSYDPISTDASRRSSEASQCSGGSGLLNLTPAQQYSLRAKYAAATGGPPPTPLPGLERMSLRTRLALLDAPERTLPAGCPRPLGPRRGSDGPTYGHGHAGAAPAFPHEAPGGGARRASDPVRRPDALSLPRVQRFHSTHNVNPGPLPPCADRRGLRLQSHPSTDGGLARGAYSPRPPSISENVAMEAVAAGVDGAGPEADLGLPEDDLVLPDDVVQYIKAHASGALDEGTGQVYPTESTGFSDNPRLPSPGLHGQRRMVAADSNVGPSAPMLGGCQLGFGAPSSLNKNNMPVQWNEVSSGTVDALASQVKPPPFPQGNLAVVQQKPAFGQYPGYSPQGLQASPGGLDSTQPHLQPRSGAPSQGIPRVNYMQQLRQPVAGSQCPGMTTTMSPHACYGQVHPQLSPSTISGALNQFPQSCSNMPAKPGHLGHPQQTEVAPDPTTMGNRHRELGVPDSALAGVPPPHPVQSYPQQSHHLAASMSQEGYHQVPSLLPARQPGFMEPQTGPMGVATAGFGLVQPRPPLEPSPTGRHRGVRAVQQQLAYARATGHAMAAMPSSQETAEAVPKGAMGNMGSVPPQPPPQDAGGAPDHSMLYYYGQIHMYEQDGGLENLGSCQVMRSQPPQPQACQDSIQPQPLPSPGVNQVSSTVDSQLLEAPQIDFDAIMDDGDHSSLFSGALSPSLLHSLSQNSSRLTTPRNSLTLPSIPAGISNMAVGDMSSMLTSLAEESKFLNMMT TT045OH TT Literature-reported TT045OH FM mRNA target TTZO36H ID TTZO36H TTZO36H TN Glucose transporter type 12 (GLUT12) TTZO36H UP Q8TD20 TTZO36H UC GTR12_HUMAN TTZO36H BC Major facilitator superfamily TTZO36H SN Solute carrier family 2, facilitated glucose transporter member 12; SLC2A12 TTZO36H GN SLC2A12 TTZO36H FC Facilitative glucose transporter. TTZO36H SQ MVPVENTEGPSLLNQKGTAVETEGSGSRHPPWARGCGMFTFLSSVTAAVSGLLVGYELGIISGALLQIKTLLALSCHEQEMVVSSLVIGALLASLTGGVLIDRYGRRTAIILSSCLLGLGSLVLILSLSYTVLIVGRIAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVIGILSAYISNYAFANVFHGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEGAASKVLGRLRALSDTTEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAASLASTGVGVVKVISTIPATLLVDHVGSKTFLCIGSSVMAASLVTMGIVNLNIHMNFTHICRSHNSINQSLDESVIYGPGNLSTNNNTLRDHFKGISSHSRSSLMPLRNDVDKRGETTSASLLNAGLSHTEYQIVTDPGDVPAFLKWLSLASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTDLIGLPWVCFIYTIMSLASLLFVVMFIPETKGCSLEQISMELAKVNYVKNNICFMSHHQEELVPKQPQKRKPQEQLLECNKLCGRGQSRQLSPET TTZO36H TT Literature-reported TTO6LI7 ID TTO6LI7 TTO6LI7 TN Glutamate receptor ionotropic kainate 5 (GRIK5) TTO6LI7 UP Q16478 TTO6LI7 UC GRIK5_HUMAN TTO6LI7 BC Glutamate-gated ion channel TTO6LI7 SN KA2; Glutamate receptor ionotropic, kainate 5; Glutamate receptor KA-2; GluK5; GRIK2; Excitatory amino acid receptor 2; EAA2 TTO6LI7 GN GRIK5 TTO6LI7 FC L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > domoate > L-glutamate >> AMPA >> NMDA = 1S,3R-ACPD. Receptor for glutamate. TTO6LI7 SQ MPAELLLLLIVAFASPSCQVLSSLRMAAILDDQTVCGRGERLALALAREQINGIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPASASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAECLLRLEELVRGFLISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLILRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILGFSMFNTSHPFYPEFVRSLNMSWRENCEASTYLGPALSAALMFDAVHVVVSAVRELNRSQEIGVKPLACTSANIWPHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNATTLDINLSQTLANKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPAVWLFMLLAYLAVSCVLFLAARLSPYEWYNPHPCLRARPHILENQYTLGNSLWFPVGGFMQQGSEIMPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMEVPVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWEGGRCPKEEDHRAKGLGMENIGGIFIVLICGLIIAVFVAVMEFIWSTRRSAESEEVSVCQEMLQELRHAVSCRKTSRSRRRRRPGGPSRALLSLRAVREMRLSNGKLYSAGAGGDAGSAHGGPQRLLDDPGPPSGARPAAPTPCTHVRVCQECRRIQALRASGAGAPPRGLGVPAEATSPPRPRPGPAGPRELAEHE TTO6LI7 TT Literature-reported TTRJCNG ID TTRJCNG TTRJCNG TN Glutaredoxin-1 (GLRX) TTRJCNG UP P35754 TTRJCNG UC GLRX1_HUMAN TTRJCNG SN Thioltransferase-1; TTase-1; GRX TTRJCNG GN GLRX TTRJCNG FC Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. TTRJCNG PD 4RQR; 1JHB; 1B4Q TTRJCNG SQ MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGELLTRLKQIGALQ TTRJCNG TT Literature-reported TTESHRV ID TTESHRV TTESHRV TN Glutaredoxin-2 (GLRX2) TTESHRV UP Q9NS18 TTESHRV UC GLRX2_HUMAN TTESHRV SN Glutaredoxin-2, mitochondrial; GRX2; CGI-133 TTESHRV GN GLRX2 TTESHRV FC Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release. TTESHRV PD 2HT9; 2FLS; 2CQ9 TTESHRV SQ MIWRRAALAGTRLVWSRSGSAGWLDRAAGAAGAAAAAASGMESNTSSSLENLATAPVNQIQETISDNCVVIFSKTSCSYCTMAKKLFHDMNVNYKVVELDLLEYGNQFQDALYKMTGERTVPRIFVNGTFIGGATDTHRLHKEGKLLPLVHQCYLKKSKRKEFQ TTESHRV TT Literature-reported TT9VL2N ID TT9VL2N TT9VL2N TN Gp100[209-217] peptide (PMEL) TT9VL2N UP P40967 TT9VL2N UC PMEL_HUMAN TT9VL2N SN Silver locus protein homolog (209-217); SILV (209-217); Premelanosome protein (209-217); PMEL17 (209-217); P100 (209-217); P1 (209-217); Melanomaassociated ME20 antigen (209-217); Melanoma-associated ME20 antigen (209-217); Melanocyte protein Pmel 17 (209-217); Melanocyte protein PMEL (209-217); Mbeta (209-217); ME20S (209-217); ME20M (209-217); ME20-M (209-217); D12S53E (209-217) TT9VL2N GN PMEL TT9VL2N FC Involved in the maturation of melanosomes from stage I to II. The transition from stage I melanosomes to stage II melanosomes involves an elongation of the vesicle, and the appearance within of distinct fibrillar structures. Release of the soluble form, ME20-S, could protect tumor cells from antibody mediated immunity. Plays a central role in the biogenesis of melanosomes. TT9VL2N PD 5EU6; 5EU5; 5EU4; 5EU3; 4IS6 TT9VL2N SQ MDLVLKRCLLHLAVIGALLAVGATKVPRNQDWLGVSRQLRTKAWNRQLYPEWTEAQRLDCWRGGQVSLKVSNDGPTLIGANASFSIALNFPGSQKVLPDGQVIWVNNTIINGSQVWGGQPVYPQETDDACIFPDGGPCPSGSWSQKRSFVYVWKTWGQYWQVLGGPVSGLSIGTGRAMLGTHTMEVTVYHRRGSRSYVPLAHSSSAFTITDQVPFSVSVSQLRALDGGNKHFLRNQPLTFALQLHDPSGYLAEADLSYTWDFGDSSGTLISRALVVTHTYLEPGPVTAQVVLQAAIPLTSCGSSPVPGTTDGHRPTAEAPNTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEVISTAPVQMPTAESTGMTPEKVPVSEVMGTTLAEMSTPEATGMTPAEVSIVVLSGTTAAQVTTTEWVETTARELPIPEPEGPDASSIMSTESITGSLGPLLDGTATLRLVKRQVPLDCVLYRYGSFSVTLDIVQGIESAEILQAVPSGEGDAFELTVSCQGGLPKEACMEISSPGCQPPAQRLCQPVLPSPACQLVLHQILKGGSGTYCLNVSLADTNSLAVVSTQLIMPGQEAGLGQVPLIVGILLVLMAVVLASLIYRRRLMKQDFSVPQLPHSSSHWLRLPRIFCSCPIGENSPLLSGQQV TT9VL2N TT Literature-reported TTUGH4C ID TTUGH4C TTUGH4C TN Grainyhead-like 2 (GRHL2) TTUGH4C UP Q6ISB3 TTUGH4C UC GRHL2_HUMAN TTUGH4C SN Transcription factor CP2like 3; Grainyheadlike protein 2 homolog; GRHL2; Brother of mammalian grainyhead TTUGH4C GN GRHL2 TTUGH4C FC Transcription factor playing an important role in primary neurulationand in epithelial development (PubMed:25152456). Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes. During embryogenesis, plays unique and cooperative roles with GRHL3 in establishing distinct zones of primary neurulation. Essential for closure 3 (rostral end of the forebrain), functions cooperatively with GRHL3 in closure 2 (forebrain/midbrain boundary) and posterior neuropore closure. Regulates epithelial morphogenesis acting as a target gene-associated transcriptional activator of apicaljunctional complex components. Up-regulates of CLDN3 and CLDN4, as well as of RAB25, which increases the CLDN4 protein and its localization at tight junctions. Comprises an essential component of the transcriptional machinery that establishes appropriate expression levels of CLDN4 and CDH1 in different types of epithelia. Exhibits functional redundancy with GRHL3 in epidermal morphogenetic events and epidermal wound repair. In lung, forms a regulatory loop with NKX2-1 that coordinates lung epithelial cell morphogenesis and differentiation. In keratinocytes, plays a role in telomerase activation during cellular proliferation, regulates TERT expression by binding to TERT promoter region and inhibiting DNA methylation at the 5'-CpG island, possibly by interfering with DNMT1 enzyme activity (PubMed:19015635, PubMed:20938050). In addition, impairs keratinocyte differentiation and epidermal function by inhibiting the expression of genes clustered at the epidermal differentiation complex (EDC) as well as GRHL1 and GRHL3 through epigenetic mechanisms (PubMed:23254293). TTUGH4C PD 5MR7 TTUGH4C SQ MSQESDNNKRLVALVPMPSDPPFNTRRAYTSEDEAWKSYLENPLTAATKAMMSINGDEDSAAALGLLYDYYKVPRDKRLLSVSKASDSQEDQEKRNCLGTSEAQSNLSGGENRVQVLKTVPVNLSLNQDHLENSKREQYSISFPESSAIIPVSGITVVKAEDFTPVFMAPPVHYPRGDGEEQRVVIFEQTQYDVPSLATHSAYLKDDQRSTPDSTYSESFKDAATEKFRSASVGAEEYMYDQTSSGTFQYTLEATKSLRQKQGEGPMTYLNKGQFYAITLSETGDNKCFRHPISKVRSVVMVVFSEDKNRDEQLKYWKYWHSRQHTAKQRVLDIADYKESFNTIGNIEEIAYNAVSFTWDVNEEAKIFITVNCLSTDFSSQKGVKGLPLMIQIDTYSYNNRSNKPIHRAYCQIKVFCDKGAERKIRDEERKQNRKKGKGQASQTQCNSSSDGKLAAIPLQKKSDITYFKTMPDLHSQPVLFIPDVHFANLQRTGQVYYNTDDEREGGSVLVKRMFRPMEEEFGPVPSKQMKEEGTKRVLLYVRKETDDVFDALMLKSPTVKGLMEAISEKYGLPVEKIAKLYKKSKKGILVNMDDNIIEHYSNEDTFILNMESMVEGFKVTLMEI TTUGH4C TT Literature-reported TT0LWE3 ID TT0LWE3 TT0LWE3 TN Granulin (GRN) TT0LWE3 UP P28799 (58-573) TT0LWE3 UC GRN_HUMAN TT0LWE3 SN Progranulin (58-573); Proepithelin (58-573); PGRN (58-573); PEPI (58-573); PCDGF (58-573); PC cell-derived growth factor (58-573); Granulin-epithelin; Granulin precursor (58-573); Glycoprotein of 88 Kda (58-573); Glycoprotein 88 (58-573); GP88 (58-573); Epithelin precursor (58-573); Acrogranin (58-573) TT0LWE3 GN GRN TT0LWE3 FC Functions as regulator of proteins trafficking to lysosome and activity of lysosomal enzymes. Facilitates also the acidification of lysosomes, causing degradation of mature CTSD by CTSB. In addition, functions as wound-related growth factor that acts directly on dermal fibroblasts and endothelial cells to promote division, migration and the formation of capillary-like tubule structure. Also promotes epithelial cell proliferation by blocking TNF-mediated neutrophil activation preventing release of oxidants and proteases. Moreover, modulates inflammation in neuron by preserving neuron survival, axonal outgrowth and neuronal integrity. Secreted proteins that act as key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation. TT0LWE3 PD 2JYV; 2JYU; 2JYT; 2JYE; 1G26 TT0LWE3 SQ GGPCQVDAHCSAGHSCIFTVSGTSSCCPFPEAVACGDGHHCCPRGFHCSADGRSCFQRSGNNSVGAIQCPDSQFECPDFSTCCVMVDGSWGCCPMPQASCCEDRVHCCPHGAFCDLVHTRCITPTGTHPLAKKLPAQRTNRAVALSSSVMCPDARSRCPDGSTCCELPSGKYGCCPMPNATCCSDHLHCCPQDTVCDLIQSKCLSKENATTDLLTKLPAHTVGDVKCDMEVSCPDGYTCCRLQSGAWGCCPFTQAVCCEDHIHCCPAGFTCDTQKGTCEQGPHQVPWMEKAPAHLSLPDPQALKRDVPCDNVSSCPSSDTCCQLTSGEWGCCPIPEAVCCSDHQHCCPQGYTCVAEGQCQRGSEIVAGLEKMPARRASLSHPRDIGCDQHTSCPVGQTCCPSLGGSWACCQLPHAVCCEDRQHCCPAGYTCNVKARSCEKEVVSAQPATFLARSPHVGVKDVECGEGHFCHDNQTCCRDNRQGWACCPYRQGVCCADRRHCCPAGFRCAARGTKCL TT0LWE3 TT Literature-reported TTPNZ1F ID TTPNZ1F TTPNZ1F TN GTPase activating protein (RASA1) TTPNZ1F UP P20936 TTPNZ1F UC RASA1_HUMAN TTPNZ1F SN p120GAP; RasGAP; Ras p21 protein activator; Ras GTPase-activating protein 1; RASA; GTPase-activating protein; GAP TTPNZ1F GN RASA1 TTPNZ1F FC Stimulates the GTPase of normal but not oncogenic Ras p21; this stimulation may be further increased in the presence of NCK1. Inhibitory regulator of the Ras-cyclic AMP pathway. TTPNZ1F PD 4FSS; 2M51; 2J06; 2J05; 2GSB TTPNZ1F SQ MMAAEAGSEEGGPVTAGAGGGGAAAGSSAYPAVCRVKIPAALPVAAAPYPGLVETGVAGTLGGGAALGSEFLGAGSVAGALGGAGLTGGGTAAGVAGAAAGVAGAAVAGPSGDMALTKLPTSLLAETLGPGGGFPPLPPPPYLPPLGAGLGTVDEGDSLDGPEYEEEEVAIPLTAPPTNQWYHGKLDRTIAEERLRQAGKSGSYLIRESDRRPGSFVLSFLSQMNVVNHFRIIAMCGDYYIGGRRFSSLSDLIGYYSHVSCLLKGEKLLYPVAPPEPVEDRRRVRAILPYTKVPDTDEISFLKGDMFIVHNELEDGWMWVTNLRTDEQGLIVEDLVEEVGREEDPHEGKIWFHGKISKQEAYNLLMTVGQVCSFLVRPSDNTPGDYSLYFRTNENIQRFKICPTPNNQFMMGGRYYNSIGDIIDHYRKEQIVEGYYLKEPVPMQDQEQVLNDTVDGKEIYNTIRRKTKDAFYKNIVKKGYLLKKGKGKRWKNLYFILEGSDAQLIYFESEKRATKPKGLIDLSVCSVYVVHDSLFGRPNCFQIVVQHFSEEHYIFYFAGETPEQAEDWMKGLQAFCNLRKSSPGTSNKRLRQVSSLVLHIEEAHKLPVKHFTNPYCNIYLNSVQVAKTHAREGQNPVWSEEFVFDDLPPDINRFEITLSNKTKKSKDPDILFMRCQLSRLQKGHATDEWFLLSSHIPLKGIEPGSLRVRARYSMEKIMPEEEYSEFKELILQKELHVVYALSHVCGQDRTLLASILLRIFLHEKLESLLLCTLNDREISMEDEATTLFRATTLASTLMEQYMKATATQFVHHALKDSILKIMESKQSCELSPSKLEKNEDVNTNLTHLLNILSELVEKIFMASEILPPTLRYIYGCLQKSVQHKWPTNTTMRTRVVSGFVFLRLICPAILNPRMFNIISDSPSPIAARTLILVAKSVQNLANLVEFGAKEPYMEGVNPFIKSNKHRMIMFLDELGNVPELPDTTEHSRTDLSRDLAALHEICVAHSDELRTLSNERGAQQHVLKKLLAITELLQQKQNQYTKTNDVR TTPNZ1F TT Literature-reported TTAI9ZQ ID TTAI9ZQ TTAI9ZQ TN Heat shock protein A 12B (HSPA12B) TTAI9ZQ UP Q96MM6 TTAI9ZQ UC HS12B_HUMAN TTAI9ZQ BC Heat shock protein TTAI9ZQ SN Heat shock 70 kDa protein 12B; C20orf60 TTAI9ZQ GN HSPA12B TTAI9ZQ FC Interacts with extended peptide segments of proteins as well as partially folded proteins to prevent aggregation, remodel folding pathways, and regulate activity. When not interacting with a substrate peptide, usually in an ATP bound state. Hsp70 by itself is characterized by a very weak ATPase activity. As newly synthesized proteins emerge from the ribosomes, the substrate binding domain of Hsp70 recognizes sequences of hydrophobic amino acid residues, and interacts with them. This spontaneous interaction is reversible, and in the ATP bound state Hsp70 may relatively freely bind and release peptides. TTAI9ZQ SQ MLAVPEMGLQGLYIGSSPERSPVPSPPGSPRTQESCGIAPLTPSQSPKPEVRAPQQASFSVVVAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGAFHSFGYTARDYYHDLDPEEARDWLYFEKFKMKIHSATDLTLKTQLEAVNGKTMPALEVFAHALRFFREHALQELREQSPSLPEKDTVRWVLTVPAIWKQPAKQFMREAAYLAGLVSRENAEQLLIALEPEAASVYCRKLRLHQLLDLSGRAPGGGRLGERRSIDSSFRQAREQLRRSRHSRTFLVESGVGELWAEMQAGDRYVVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIATFKRQRPAAWVDLTIAFEARKRTAGPHRAGALNISLPFSFIDFYRKQRGHNVETALRRSSVNFVKWSSQGMLRMSCEAMNELFQPTVSGIIQHIEALLARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARGLRVVVPHDVGLTILKGAVLFGQAPGVVRVRRSPLTYGVGVLNRFVPGRHPPEKLLVRDGRRWCTDVFERFVAAEQSVALGEEVRRSYCPARPGQRRVLINLYCCAAEDARFITDPGVRKCGALSLELEPADCGQDTAGAPPGRREIRAAMQFGDTEIKVTAVDVSTNRSVRASIDFLSN TTAI9ZQ TT Literature-reported TTY0OJN ID TTY0OJN TTY0OJN TN Heat shock protein beta-8 (HSPB8) TTY0OJN UP Q9UJY1 TTY0OJN UC HSPB8_HUMAN TTY0OJN BC Heat shock protein TTY0OJN SN Small stress proteinlike protein HSP22; Small stress protein-like protein HSP22; Protein kinase H11; PP1629; HspB8; Heat shock protein beta8; HSP22; E2induced gene 1 protein; E2IG1; E2-induced gene 1 protein; CRYAC; Alphacrystallin C chain; Alpha-crystallin C chain TTY0OJN GN HSPB8 TTY0OJN FC Displays temperature-dependent chaperone activity. TTY0OJN SQ MADGQMPFSCHYPSRLRRDPFRDSPLSSRLLDDGFGMDPFPDDLTASWPDWALPRLSSAWPGTLRSGMVPRGPTATARFGVPAEGRTPPPFPGEPWKVCVNVHSFKPEELMVKTKDGYVEVSGKHEEKQQEGGIVSKNFTKKIQLPAEVDPVTVFASLSPEGLLIIEAPQVPPYSTFGESSFNNELPQDSQEVTCT TTY0OJN TT Literature-reported TTY0OJN FM Heat shock protein TT5OG9E ID TT5OG9E TT5OG9E TN Helicobacter pylori Methylthioadenosine nucleosidase (HELPY mtnN) TT5OG9E UP O24915 TT5OG9E UC MQMTN_HELPY TT5OG9E SN MTAN; MTA/SAH nucleosidase; Aminofutalosine nucleosidase; Aminodeoxyfutalosine nucleosidase; AFL nucleosidase; 6-amino-6-deoxyfutalosine N-ribosylhydrolase; 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase TT5OG9E GN HELPY mtnN TT5OG9E FC Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Can also probably catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2. Does not act on futalosine (FL) as substrate. TT5OG9E PD 4BN0; 4BMZ; 4BMY; 4BMX TT5OG9E SQ MVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAGSLVKDLKINDLLVAIQLVQHDVDLSAFDHPLGFIPESAIFIETSESLNALAKEVANEQHIVLKEGVIASGDQFVHSKERKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISDNADEEANMSFDAFLEKSAQTSAKFLKSMVDEL TT5OG9E TT Literature-reported TT5BYHP ID TT5BYHP TT5BYHP TN Heme-controlled repressor (HCR) TT5BYHP UP Q9BQI3 TT5BYHP UC E2AK1_HUMAN TT5BYHP SN HCR TT5BYHP GN EIF2AK1 TT5BYHP FC Inhibits protein synthesis at the translation initiation level, in response to various stress conditions, including oxidative stress, heme deficiency, osmotic shock and heat shock. Exerts its function through the phosphorylation of EIF2S1 at 'Ser-48' and 'Ser-51', thus preventing its recycling. Binds hemin forming a 1:1 complex through a cysteine thiolate and histidine nitrogenous coordination. This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell. Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties. Thus plays an essential protective role for RBC survival in anemias of iron deficiency. Similarly, in hepatocytes, involved in heme-mediated translational control of CYP2B and CYP3A and possibly other hepatic P450 cytochromes. May also contain ER stress during acute heme-deficient conditions (By similarity). TT5BYHP EC EC 2.7.11.1 TT5BYHP SQ MQGGNSGVRKREEEGDGAGAVAAPPAIDFPAEGPDPEYDESDVPAEIQVLKEPLQQPTFPFAVANQLLLVSLLEHLSHVHEPNPLRSRQVFKLLCQTFIKMGLLSSFTCSDEFSSLRLHHNRAITHLMRSAKERVRQDPCEDISRIQKIRSREVALEAQTSRYLNEFEELAILGKGGYGRVYKVRNKLDGQYYAIKKILIKGATKTVCMKVLREVKVLAGLQHPNIVGYHTAWIEHVHVIQPRADRAAIELPSLEVLSDQEEDREQCGVKNDESSSSSIIFAEPTPEKEKRFGESDTENQNNKSVKYTTNLVIRESGELESTLELQENGLAGLSASSIVEQQLPLRRNSHLEESFTSTEESSEENVNFLGQTEAQYHLMLHIQMQLCELSLWDWIVERNKRGREYVDESACPYVMANVATKIFQELVEGVFYIHNMGIVHRDLKPRNIFLHGPDQQVKIGDFGLACTDILQKNTDWTNRNGKRTPTHTSRVGTCLYASPEQLEGSEYDAKSDMYSLGVVLLELFQPFGTEMERAEVLTGLRTGQLPESLRKRCPVQAKYIQHLTRRNSSQRPSAIQLLQSELFQNSGNVNLTLQMKIIEQEKEIAELKKQLNLLSQDKGVRDDGKDGGVG TT5BYHP TT Literature-reported TTS6LBM ID TTS6LBM TTS6LBM TN Heparan sulfate 6-O-sulfotransferase-2 (HS6ST2) TTS6LBM UP Q96MM7 TTS6LBM UC H6ST2_HUMAN TTS6LBM SN Heparan-sulfate 6-O-sulfotransferase 2; HS6ST-2 TTS6LBM GN HS6ST2 TTS6LBM FC 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. TTS6LBM EC EC 2.8.2.- TTS6LBM SQ MALPACAVREFEPPRQPERGAPVRTTCPRRHSRVEAELAASRPGSVAASVRAGPPRGVSHGFHTRPLLDKPRKASSSLAGAACAPLFALLSRGRRRRMHVLRRRWDLGSLCRALLTRGLAALGHSLKHVLGAIFSKIFGPMASVGNMDEKSNKLLLALVMLFLFAVIVLQYVCPGTECQLLRLQAFSSPVPDPYRSEDESSARFVPRYNFTRGDLLRKVDFDIKGDDLIVFLHIQKTGGTTFGRHLVRNIQLEQPCECRVGQKKCTCHRPGKRETWLFSRFSTGWSCGLHADWTELTSCVPSVVDGKRDARLRPSRNFHYITILRDPVSRYLSEWRHVQRGATWKASLHVCDGRPPTSEELPSCYTGDDWSGCPLKEFMDCPYNLANNRQVRMLSDLTLVGCYNLSVMPEKQRNKVLLESAKSNLKHMAFFGLTEFQRKTQYLFEKTFNMNFISPFTQYNTTRASSVEINEEIQKRIEGLNFLDMELYSYAKDLFLQRYQFMRQKEHQEARRKRQEQRKFLKGRLLQTHFQSQGQGQSQNPNQNQSQNPNPNANQNLTQNLMQNLTQSLSQKENRESPKQNSGKEQNDNTSNGTNDYIGSVEKWR TTS6LBM TT Literature-reported TTV1YFT ID TTV1YFT TTV1YFT TN Heparin binding protein (FGFBP1) TTV1YFT UP Q14512 TTV1YFT UC FGFP1_HUMAN TTV1YFT BC Fibroblast growth factor-binding TTV1YFT SN HBp17; HBP17 heparin-binding and FGF-binding protein; Fibroblast growth factor binding protein 1; FGFBP1; FGF-binding protein HBp17; FGF-BP TTV1YFT GN FGFBP1 TTV1YFT FC Acts as a carrier protein that release fibroblast- binding factors (FGFs) from the extracellular matrix (EM) storage and thus enhance the mitogenic activity of FGFs. Enhances FGF2 signaling during tissue repair, angiogenesis and in tumor growth. TTV1YFT SQ MKICSLTLLSFLLLAAQVLLVEGKKKVKNGLHSKVVSEQKDTLGNTQIKQKSRPGNKGKFVTKDQANCRWAATEQEEGISLKVECTQLDHEFSCVFAGNPTSCLKLKDERVYWKQVARNLRSQKDICRYSKTAVKTRVCRKDFPESSLKLVSSTLFGNTKPRKEKTEMSPREHIKGKETTPSSLAVTQTMATKAPECVEDPDMANQRKTALEFCGETWSSLCTFFLSIVQDTSC TTV1YFT TT Literature-reported TTLJWK4 ID TTLJWK4 TTLJWK4 TN Hepatitis C virus Protein p7 (HCV p7) TTLJWK4 UP P26664 (747-809) TTLJWK4 UC POLG_HCV1 TTLJWK4 SN HCV p7 TTLJWK4 GN HCV p7 TTLJWK4 FC Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). TTLJWK4 PD 3SU4; 3RC5; 3RC4; 3QGI; 3QGH TTLJWK4 SQ ALENLVILNAASLAGTHGLVSFLVFFCFAWYLKGKWVPGAVYTFYGMWPLLLLLLALPQRAYA TTLJWK4 TT Literature-reported TTKGV26 ID TTKGV26 TTKGV26 TN Hepatoma-derived growth factor (HDGF) TTKGV26 UP P51858 TTKGV26 UC HDGF_HUMAN TTKGV26 SN High-mobility group protein 1-like 2; High mobility group protein 1-like 2; HMG1L2; HMG-1L2 TTKGV26 GN HDGF TTKGV26 FC Acts as a transcriptional repressor. Heparin-binding protein, with mitogenic activity for fibroblasts. TTKGV26 PD 2NLU; 1RI0 TTKGV26 SQ MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCVEEPEPEPEAAEGDGDKKGNAEGSSDEEGKLVIDEPAKEKNEKGALKRRAGDLLEDSPKRPKEAENPEGEEKEAATLEVERPLPMEVEKNSTPSEPGSGRGPPQEEEEEEDEEEEATKEDAEAPGIRDHESL TTKGV26 TT Literature-reported TT51ZGC ID TT51ZGC TT51ZGC TN Herpes simplex virus DNA polymerase POL (HSV POL) TT51ZGC UP P04293-P10226 TT51ZGC UC DPOL_HHV21-PAP_HHV11 TT51ZGC BC DNA polymerase type-B family TT51ZGC SN Complex of DNA polymerase processivity factor and DNA polymerase catalytic subunit TT51ZGC GN HSV POL TT51ZGC FC Synthesize herpes simplex virus DNA from deoxyribonucleotides, the building blocks of DNA. TT51ZGC SQ MTDSPGGVAPASPVEDASDASLGQPEEGAPCQVVLQGAELNGILQAFAPLRTSLLDSLLVMGDRGILIHNTIFGEQVFLPLEHSQFSRYRWRGPTAAFLSLVDQKRSLLSVFRANQYPDLRRVELAITGQAPFRTLVQRIWTTTSDGEAVELASETLMKRELTSFVVLVPQGTPDVQLRLTRPQLTKVLNATGADSATPTTFELGVNGKFSVFTTSTCVTFAAREEGVSSSTSTQVQILSNALTKAGQAAANAKTVYGENTHRTFSVVVDDCSMRAVLRRLQVGGGTLKFFLTTPVPSLCVTATGPNAVSAVFLLKPQKICLDWLGHSQGSPSAGSSASRASGSEPTDSQDSASDAVSHGDPEDLDGAARAGEAGALHACPMPSSTTRVTPTTKRGRSGGEDARADTALKKPKTGSPTAPPPADPVPLDTEDDSDAADGTAARPAAPDARSGSRYACYFRDLPTGEASPGAFSAFRGGPQTPYGFGFPMFCAAGGPASPGGKSAARAASGFFAPHNPRGATQTAPPPCRRQNFYNPHLAQTGTQPKAPGPAQRHTYYSECDEFRFIAPRSLDEDAPAEQRTGVHDGRLRRAPKVYCGGDERDVLRVGPEGFWPRRLRLWGGADHAPEGFDPTVTVFHVYDILEHVEHAYSMRAAQLHERFMDAITPAGTVITLLGLTPEGHRVAVHVYGTRQYFYMNKAEVDRHLQCRAPRDLCERLAAALRESPGASFRGISADHFEAEVVERADVYYYETRPTLYYRVFVRSGRALAYLCDNFCPAIRKYEGGVDATTRFILDNPGFVTFGWYRLKPGRGNAPAQPRPPTAFGTSSDVEFNCTADNLAVEGAMCDLPAYKLMCFDIECKAGGEDELAFPVAERPEDLVIQISCLLYDLSTTALEHILLFSLGSCDLPESHLSDLASRGLPAPVVLEFDSEFEMLLAFMTFVKQYGPEFVTGYNIINFDWPFVLTKLTEIYKVPLDGYGRMNGRGVFRVWDIGQSHFQKRSKIKVNGMVNIDMYGIITDKVKLSSYKLNAVAEAVLKDKKKDLSYRDIPAYYASGPAQRGVIGEYCVQDSLLVGQLFFKFLPHLELSAVARLAGINITRTIYDGQQIRVFTCLLRLAGQKGFILPDTQGRFRGLDKEAPKRPAVPRGEGERPGDGNGDEDKDDDEDGDEDGDEREEVARETGGRHVGYQGARVLDPTSGFHVDPVVVFDFASLYPSIIQAHNLCFSTLSLRPEAVAHLEADRDYLEIEVGGRRLFFVKAHVRESLLSILLRDWLAMRKQIRSRIPQSPPEEAVLLDKQQAAIKVVCNSVYGFTGVQHGLLPCLHVAATVTTIGREMLLATRAYVHARWAEFDQLLADFPEAAGMRAPGPYSMRIIYGDTDSIFVLCRGLTGEALVAMGDKMASHISRALFLPPIKLECEKTFTKLLLIAKKKYIGVICGGKMLIKGVDLVRKNNCAFINRTSRALVDLLFYDDTVSGAAAALAERPAEEWLARPLPEGLQAFGAVLVDAHRRITDPERDIQDFVLTAELSRHPRAYTNKRLAHLTVYYKLMARRAQVPSIKDRIPYVIVAQTREVEETVARLAALRELDAAAPGDEPAPPAALPSPAKRPRETPSHADPPGGASKPRKLLVSELAEDPGYAIARGVPLNTDYYFSHLLGAACVTFKALFGNNAKITESLLKRFIPETWHPPDDVAARLRAAGFGPAGAGATAEETRRMLHRAFDTLA TT51ZGC TT Literature-reported TTFOKAH ID TTFOKAH TTFOKAH TN Hexamethylene bis-acetamide-inducible protein 1 (HEXIM1) TTFOKAH UP O94992 TTFOKAH UC HEXI1_HUMAN TTFOKAH SN Protein HEXIM1; Menage a quatre protein 1; MAQ1; HIS1; Estrogen down-regulated gene 1 protein; EDG1; Cardiac lineage protein 1; CLP1 TTFOKAH GN HEXIM1 TTFOKAH FC Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. TTFOKAH PD 3S9G; 2GD7 TTFOKAH SQ MAEPFLSEYQHQPQTSNCTGAAAVQEELNPERPPGAEERVPEEDSRWQSRAFPQLGGRPGPEGEGSLESQPPPLQTQACPESSCLREGEKGQNGDDSSAGGDFPPPAEVEPTPEAELLAQPCHDSEASKLGAPAAGGEEEWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRIRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYSKRAAAKSDDTSDDDFMEEGGEEDGGSDGMGGDGSEFLQRDFSETYERYHTESLQNMSKQELIKEYLELEKCLSRMEDENNRLRLESKRLGGDDARVRELELELDRLRAENLQLLTENELHRQQERAPLSKFGD TTFOKAH TT Literature-reported TTBA219 ID TTBA219 TTBA219 TN High mobility group protein HMG-I/Y (HMGA1) TTBA219 UP P17096 TTBA219 UC HMGA1_HUMAN TTBA219 SN High mobility group protein R; High mobility group protein HMG-I/HMG-Y; High mobility group protein A1; High mobility group AT-hook protein 1; HMGIY; HMG-I(Y) TTBA219 GN HMGA1 TTBA219 FC It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions. HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. TTBA219 PD 2EZG; 2EZF; 2EZE; 2EZD TTBA219 SQ MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ TTBA219 TT Literature-reported TT4S150 ID TT4S150 TT4S150 TN High-affinity cationic amino acid transporter-1 (SLC7A1) TT4S150 UP P30825 TT4S150 UC CTR1_HUMAN TT4S150 BC Amino acid-polyamine-organocation TT4S150 SN System Y+ basic amino acid transporter; Solute carrier family 7 member 1; REC1L; High affinity cationic amino acid transporter 1; Ecotropic retrovirus receptor homolog; Ecotropic retroviral leukemia receptor homolog; CAT-1; ATRC1 TT4S150 GN SLC7A1 TT4S150 FC High-affinity, low capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine) in non-hepatic tissues. TT4S150 SQ MGCKVLLNIGQQMLRRKVVDCSREETRLSRCLNTFDLVALGVGSTLGAGVYVLAGAVARENAGPAIVISFLIAALASVLAGLCYGEFGARVPKTGSAYLYSYVTVGELWAFITGWNLILSYIIGTSSVARAWSATFDELIGRPIGEFSRTHMTLNAPGVLAENPDIFAVIIILILTGLLTLGVKESAMVNKIFTCINVLVLGFIMVSGFVKGSVKNWQLTEEDFGNTSGRLCLNNDTKEGKPGVGGFMPFGFSGVLSGAATCFYAFVGFDCIATTGEEVKNPQKAIPVGIVASLLICFIAYFGVSAALTLMMPYFCLDNNSPLPDAFKHVGWEGAKYAVAVGSLCALSASLLGSMFPMPRVIYAMAEDGLLFKFLANVNDRTKTPIIATLASGAVAAVMAFLFDLKDLVDLMSIGTLLAYSLVAACVLVLRYQPEQPNLVYQMASTSDELDPADQNELASTNDSQLGFLPEAEMFSLKTILSPKNMEPSKISGLIVNISTSLIAVLIITFCIVTVLGREALTKGALWAVFLLAGSALLCAVVTGVIWRQPESKTKLSFKVPFLPVLPILSIFVNVYLMMQLDQGTWVRFAVWMLIGFIIYFGYGLWHSEEASLDADQARTPDGNLDQCK TT4S150 TT Literature-reported TT4S150 FM Amino acid-polyamine-organocation TTQZ1TP ID TTQZ1TP TTQZ1TP TN Histone variant H2A.Z (H2AFZ) TTQZ1TP UP P0C0S5 TTQZ1TP UC H2AZ_HUMAN TTQZ1TP SN Histone H2A.Z; H2AZ; H2A/z TTQZ1TP GN H2AFZ TTQZ1TP FC Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. TTQZ1TP PD 5Z30; 5FUG; 5CHL; 5B33; 5B32 TTQZ1TP SQ MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV TTQZ1TP TT Literature-reported TTN26OM ID TTN26OM TTN26OM TN Homeobox protein Hox-A13 (HOXA13) TTN26OM UP P31271 TTN26OM UC HXA13_HUMAN TTN26OM SN Homeobox protein HoxA13; Homeobox protein Hox1J; HOXA13 TTN26OM GN HOXA13 TTN26OM FC Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. TTN26OM PD 2L7Z TTN26OM SQ MTASVLLHPRWIEPTVMFLYDNGGGLVADELNKNMEGAAAAAAAAAAAAAAGAGGGGFPHPAAAAAGGNFSVAAAAAAAAAAAANQCRNLMAHPAPLAPGAASAYSSAPGEAPPSAAAAAAAAAAAAAAAAAASSSGGPGPAGPAGAEAAKQCSPCSAAAQSSSGPAALPYGYFGSGYYPCARMGPHPNAIKSCAQPASAAAAAAFADKYMDTAGPAAEEFSSRAKEFAFYHQGYAAGPYHHHQPMPGYLDMPVVPGLGGPGESRHEPLGLPMESYQPWALPNGWNGQMYCPKEQAQPPHLWKSTLPDVVSHPSDASSYRRGRKKRVPYTKVQLKELEREYATNKFITKDKRRRISATTNLSERQVTIWFQNRRVKEKKVINKLKTTS TTN26OM TT Literature-reported TTXSVQP ID TTXSVQP TTXSVQP TN Homeobox protein Hox-A5 (HOXA5) TTXSVQP UP P20719 TTXSVQP UC HXA5_HUMAN TTXSVQP BC Antp homeobox TTXSVQP SN Homeobox protein HoxA5; Homeobox protein Hox1C; Homeobox protein Hox-1C; HOX1C TTXSVQP GN HOXA5 TTXSVQP FC Binds to its own promoter. Binds specifically to the motif 5'-CYYNATTA[TG]Y-3'. Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. TTXSVQP SQ MSSYFVNSFCGRYPNGPDYQLHNYGDHSSVSEQFRDSASMHSGRYGYGYNGMDLSVGRSGSGHFGSGERARSYAASASAAPAEPRYSQPATSTHSPQPDPLPCSAVAPSPGSDSHHGGKNSLSNSSGASADAGSTHISSREGVGTASGAEEDAPASSEQASAQSEPSPAPPAQPQIYPWMRKLHISHDNIGGPEGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMSMAAAGGAFRP TTXSVQP TT Literature-reported TTXSVQP FM Antp homeobox family TTMRE4Q ID TTMRE4Q TTMRE4Q TN Homeobox protein Hox-A7 (HOXA7) TTMRE4Q UP P31268 TTMRE4Q UC HXA7_HUMAN TTMRE4Q BC Antp homeobox TTMRE4Q SN HoxA7; Hox-1A; Hox 1.1; Homeobox protein Hox-1A; Homeobox protein Hox 1.1; HOX1A TTMRE4Q GN HOXA7 TTMRE4Q FC Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. TTMRE4Q SQ MSSSYYVNALFSKYTAGASLFQNAEPTSCSFAPNSQRSGYGAGAGAFASTVPGLYNVNSPLYQSPFASGYGLGADAYGNLPCASYDQNIPGLCSDLAKGACDKTDEGALHGAAEANFRIYPWMRSSGPDRKRGRQTYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKEHKDEGPTAAAAPEGAVPSAAATAAADKADEEDDDEEEEDEEE TTMRE4Q TT Literature-reported TTMRE4Q FM Antp homeobox family TTZ6I58 ID TTZ6I58 TTZ6I58 TN Homeobox protein Hox-B13 (HOXB13) TTZ6I58 UP Q92826 TTZ6I58 UC HXB13_HUMAN TTZ6I58 SN Hoxb-13; HOXB13 TTZ6I58 GN HOXB13 TTZ6I58 FC Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. TTZ6I58 PD 5NO6; 5EGO; 5EG0; 5EF6; 5EEA TTZ6I58 SQ MEPGNYATLDGAKDIEGLLGAGGGRNLVAHSPLTSHPAAPTLMPAVNYAPLDLPGSAEPPKQCHPCPGVPQGTSPAPVPYGYFGGGYYSCRVSRSSLKPCAQAATLAAYPAETPTAGEEYPSRPTEFAFYPGYPGTYQPMASYLDVSVVQTLGAPGEPRHDSLLPVDSYQSWALAGGWNSQMCCQGEQNPPGPFWKAAFADSSGQHPPDACAFRRGRKKRIPYSKGQLRELEREYAANKFITKDKRRKISAATSLSERQITIWFQNRRVKEKKVLAKVKNSATP TTZ6I58 TT Literature-reported TT1E0JK ID TT1E0JK TT1E0JK TN Homeobox protein Nkx-3.1 (NKX3-1) TT1E0JK UP Q99801 TT1E0JK UC NKX31_HUMAN TT1E0JK SN NKX3A; NKX31; NKX3.1; Homeobox protein Nkx3.1; Homeobox protein NK3 homolog A; Homeobox protein NK-3 homolog A TT1E0JK GN NKX3-1 TT1E0JK FC Plays an important role in normal prostate development, regulating proliferation of glandular epithelium and in the formation of ducts in prostate. Acts as a tumor suppressor controlling prostate carcinogenesis, as shown by the ability to inhibit proliferation and invasion activities of PC-3 prostate cancer cells. Transcription factor, which binds preferentially the consensus sequence 5'-TAAGT[AG]-3' and can behave as a transcriptional repressor. TT1E0JK PD 2L9R TT1E0JK SQ MLRVPEPRPGEAKAEGAAPPTPSKPLTSFLIQDILRDGAQRQGGRTSSQRQRDPEPEPEPEPEGGRSRAGAQNDQLSTGPRAAPEEAETLAETEPERHLGSYLLDSENTSGALPRLPQTPKQPQKRSRAAFSHTQVIELERKFSHQKYLSAPERAHLAKNLKLTETQVKIWFQNRRYKTKRKQLSSELGDLEKHSSLPALKEEAFSRASLVSVYNSYPYYPYLYCVGSWSPAFW TT1E0JK TT Literature-reported TT74D0S ID TT74D0S TT74D0S TN Human immunodeficiency virus Virion infectivity factor (HIV vif) TT74D0S UP P03402 TT74D0S UC VIF_HV1A2 TT74D0S BC Primate lentivirus group Vif protein TT74D0S SN Virion infectivity factor; Vif; SOR protein TT74D0S GN HIV vif TT74D0S FC Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells. TT74D0S SQ MENRWQVMIVWQVDRMRIRTWKSLVKHHMYISKKAKGWFYRHHYESTHPRVSSEVHIPLGDAKLVITTYWGLHTGEREWHLGQGVAIEWRKKKYSTQVDPGLADQLIHLHYFDCFSESAIKNAILGYRVSPRCEYQAGHNKVGSLQYLALAALITPKKTKPPLPSVKKLTEDRWNKPQKTKGHRGSHTMNGH TT74D0S TT Literature-reported TTWMK2G ID TTWMK2G TTWMK2G TN Human papillomavirus-18 E7 region messenger RNA (HPV-18 E7 mRNA) TTWMK2G UP P06788 TTWMK2G UC VE7_HPV18 TTWMK2G BC mRNA target TTWMK2G SN HPV-18 protein E7 (mRNA); HPV-18 E7 (mRNA) TTWMK2G GN HPV-18 E7 mRNA TTWMK2G FC Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Plays also a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. TTWMK2G SQ MHGPKATLQDIVLHLEPQNEIPVDLLCHEQLSDSEEENDEIDGVNHQHLPARRAEPQRHTMLCMCCKCEARIKLVVESSADDLRAFQQLFLNTLSFVCPWCASQQ TTWMK2G TT Literature-reported TTWMK2G FM mRNA target TTBXVDE ID TTBXVDE TTBXVDE TN ID1 messenger RNA (ID1 mRNA) TTBXVDE UP P41134 TTBXVDE UC ID1_HUMAN TTBXVDE BC mRNA target TTBXVDE SN bHLHb24 (mRNA); Inhibitor of differentiation 1 (mRNA); Inhibitor of DNA binding 1 (mRNA); ID (mRNA); DNA-binding protein inhibitor ID-1 (mRNA); Class B basic helix-loop-helix protein 24 (mRNA) TTBXVDE GN ID1 TTBXVDE FC Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. TTBXVDE SQ MKVASGSTATAAAGPSCALKAGKTASGAGEVVRCLSEQSVAISRCAGGAGARLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTPGGRGLPVRAPLSTLNGEISALTAEAACVPADDRILCR TTBXVDE TT Literature-reported TTBXVDE FM mRNA target TTY2XZ0 ID TTY2XZ0 TTY2XZ0 TN IKK complex-associated protein (IKBKAP) TTY2XZ0 UP O95163 TTY2XZ0 UC ELP1_HUMAN TTY2XZ0 SN IkappaB kinase complexassociated protein; IkappaB kinase complex-associated protein; IKK complexassociated protein; IKAP; Elongator complex protein 1; ELP1 TTY2XZ0 GN IKBKAP TTY2XZ0 FC May act as a scaffold protein that may assemble active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK). TTY2XZ0 PD 5CQR TTY2XZ0 SQ MRNLKLFRTLEFRDIQGPGNPQCFSLRTEQGTVLIGSEHGLIEVDPVSREVKNEVSLVAEGFLPEDGSGRIVGVQDLLDQESVCVATASGDVILCSLSTQQLECVGSVASGISVMSWSPDQELVLLATGQQTLIMMTKDFEPILEQQIHQDDFGESKFITVGWGRKETQFHGSEGRQAAFQMQMHESALPWDDHRPQVTWRGDGQFFAVSVVCPETGARKVRVWNREFALQSTSEPVAGLGPALAWKPSGSLIASTQDKPNQQDIVFFEKNGLLHGHFTLPFLKDEVKVNDLLWNADSSVLAVWLEDLQREESSIPKTCVQLWTVGNYHWYLKQSLSFSTCGKSKIVSLMWDPVTPYRLHVLCQGWHYLAYDWHWTTDRSVGDNSSDLSNVAVIDGNRVLVTVFRQTVVPPPMCTYQLLFPHPVNQVTFLAHPQKSNDLAVLDASNQISVYKCGDCPSADPTVKLGAVGGSGFKVCLRTPHLEKRYKIQFENNEDQDVNPLKLGLLTWIEEDVFLAVSHSEFSPRSVIHHLTAASSEMDEEHGQLNVSSSAAVDGVIISLCCNSKTKSVVLQLADGQIFKYLWESPSLAIKPWKNSGGFPVRFPYPCTQTELAMIGEEECVLGLTDRCRFFINDIEVASNITSFAVYDEFLLLTTHSHTCQCFCLRDASFKTLQAGLSSNHVSHGEVLRKVERGSRIVTVVPQDTKLVLQMPRGNLEVVHHRALVLAQIRKWLDKLMFKEAFECMRKLRINLNLIYDHNPKVFLGNVETFIKQIDSVNHINLFFTELKEEDVTKTMYPAPVTSSVYLSRDPDGNKIDLVCDAMRAVMESINPHKYCLSILTSHVKKTTPELEIVLQKVHELQGNAPSDPDAVSAEEALKYLLHLVDVNELYDHSLGTYDFDLVLMVAEKSQKDPKEYLPFLNTLKKMETNYQRFTIDKYLKRYEKAIGHLSKCGPEYFPECLNLIKDKNLYNEALKLYSPSSQQYQDISIAYGEHLMQEHMYEPAGLMFARCGAHEKALSAFLTCGNWKQALCVAAQLNFTKDQLVGLGRTLAGKLVEQRKHIDAAMVLEECAQDYEEAVLLLLEGAAWEEALRLVYKYNRLDIIETNVKPSILEAQKNYMAFLDSQTATFSRHKKRLLVVRELKEQAQQAGLDDEVPHGQESDLFSETSSVVSGSEMSGKYSHSNSRISARSSKNRRKAERKKHSLKEGSPLEDLALLEALSEVVQNTENLKDEVYHILKVLFLFEFDEQGRELQKAFEDTLQLMERSLPEIWTLTYQQNSATPVLGPNSTANSIMASYQQQKTSVPVLDAELFIPPKINRRTQWKLSLLD TTY2XZ0 TT Literature-reported TTUN4L1 ID TTUN4L1 TTUN4L1 TN Imidazoline receptor 1 (IR1) TTUN4L1 UP Q9Y2I1 TTUN4L1 UC NISCH_HUMAN TTUN4L1 SN hIRAS; KIAA0975; Imidazoline-1 receptor candidate protein; Imidazoline-1 receptor; Imidazoline receptor antisera-selected protein; IRAS; IR1; I1R candidate protein; I-1 receptor candidate protein; I-1 TTUN4L1 GN NISCH TTUN4L1 FC Acts either as the functional imidazoline-1 receptor (I1R) candidate or as a membrane-associated mediator of the I1R signaling. Binds numerous imidazoline ligands that induces initiation of cell-signaling cascades triggering to cell survival, growth and migration. Its activation by the agonist rilmenidine induces an increase in phosphorylation of mitogen-activated protein kinases MAPK1 and MAPK3 in rostral ventrolateral medulla (RVLM) neurons that exhibited rilmenidine-evoked hypotension (By similarity). Blocking its activation with efaroxan abolished rilmenidine-induced mitogen-activated protein kinase phosphorylation in RVLM neurons (By similarity). Acts as a modulator of Rac-regulated signal transduction pathways (By similarity). Suppresses Rac1-stimulated cell migration by interacting with PAK1 and inhibiting its kinase activity (By similarity). Also blocks Pak-independent Rac signaling by interacting with RAC1 and inhibiting Rac1-stimulated NF-kB response element and cyclin D1 promoter activation (By similarity). Inhibits also LIMK1 kinase activity by reducing LIMK1 'Tyr-508' phosphorylation (By similarity). Inhibits Rac-induced cell migration and invasion in breast and colon epithelial cells (By similarity). Inhibits lamellipodia formation, when overexpressed (By similarity). Plays a role in protection against apoptosis. Involved in association with IRS4 in the enhancement of insulin activation of MAPK1 and MAPK3. When overexpressed, induces a redistribution of cell surface ITGA5 integrin to intracellular endosomal structures. TTUN4L1 PD 3P0C TTUN4L1 SQ MATARTFGPEREAEPAKEARVVGSELVDTYTVYIIQVTDGSHEWTVKHRYSDFHDLHEKLVAERKIDKNLLPPKKIIGKNSRSLVEKREKDLEVYLQKLLAAFPGVTPRVLAHFLHFHFYEINGITAALAEELFEKGEQLLGAGEVFAIGPLQLYAVTEQLQQGKPTCASGDAKTDLGHILDFTCRLKYLKVSGTEGPFGTSNIQEQLLPFDLSIFKSLHQVEISHCDAKHIRGLVASKPTLATLSVRFSATSMKEVLVPEASEFDEWEPEGTTLEGPVTAVIPTWQALTTLDLSHNSVSEIDESVKLIPKIEFLDLSHNGLLVVDNLQHLYNLVHLDLSYNKLSSLEGLHTKLGNIKTLNLAGNLLESLSGLHKLYSLVNLDLRDNRIEQMEEVRSIGSLPCLEHVSLLNNPLSIIPDYRTKVLAQFGERASEVCLDDTVTTEKELDTVEVLKAIQKAKEVKSKLSNPEKKGGEDSRLSAAPCIRPSSSPPTVAPASASLPQPILSNQGIMFVQEEALASSLSSTDSLTPEHQPIAQGCSDSLESIPAGQAASDDLRDVPGAVGGASPEHAEPEVQVVPGSGQIIFLPFTCIGYTATNQDFIQRLSTLIRQAIERQLPAWIEAANQREEGQGEQGEEEDEEEEEEEDVAENRYFEMGPPDVEEEEGGGQGEEEEEEEEDEEAEEERLALEWALGADEDFLLEHIRILKVLWCFLIHVQGSIRQFAACLVLTDFGIAVFEIPHQESRGSSQHILSSLRFVFCFPHGDLTEFGFLMPELCLVLKVRHSENTLFIISDAANLHEFHADLRSCFAPQHMAMLCSPILYGSHTSLQEFLRQLLTFYKVAGGCQERSQGCFPVYLVYSDKRMVQTAAGDYSGNIEWASCTLCSAVRRSCCAPSEAVKSAAIPYWLLLTPQHLNVIKADFNPMPNRGTHNCRNRNSFKLSRVPLSTVLLDPTRSCTQPRGAFADGHVLELLVGYRFVTAIFVLPHEKFHFLRVYNQLRASLQDLKTVVIAKTPGTGGSPQGSFADGQPAERRASNDQRPQEVPAEALAPAPAEVPAPAPAAASASGPAKTPAPAEASTSALVPEETPVEAPAPPPAEAPAQYPSEHLIQATSEENQIPSHLPACPSLRHVASLRGSAIIELFHSSIAEVENEELRHLMWSSVVFYQTPGLEVTACVLLSTKAVYFVLHDGLRRYFSEPLQDFWHQKNTDYNNSPFHISQCFVLKLSDLQSVNVGLFDQHFRLTGSTPMQVVTCLTRDSYLTHCFLQHLMVVLSSLERTPSPEPVDKDFYSEFGNKTTGKMENYELIHSSRVKFTYPSEEEIGDLTFTVAQKMAEPEKAPALSILLYVQAFQVGMPPPGCCRGPLRPKTLLLTSSEIFLLDEDCVHYPLPEFAKEPPQRDRYRLDDGRRVRDLDRVLMGYQTYPQALTLVFDDVQGHDLMGSVTLDHFGEVPGGPARASQGREVQWQVFVPSAESREKLISLLARQWEALCGRELPVELTG TTUN4L1 TT Literature-reported TTST6IQ ID TTST6IQ TTST6IQ TN Immunoglobulin gamma Fc receptor II (FCGR2) TTST6IQ UP P12318; P31994; P31995 TTST6IQ UC FCG2A_HUMAN; FCG2B_HUMAN; FCG2C_HUMAN TTST6IQ BC Immunoglobulin TTST6IQ SN Low affinity immunoglobulin gamma Fc region receptor II; IgG Fc receptor II; IGFR2; FcRII; Fc-gamma-RII; Fc-gamma RII; FCG2; CDw32; CD32 TTST6IQ GN FCGR2A; FCGR2B; FCGR2C TTST6IQ FC Inhibits the functions of activating FcRs, such as phagocytosis and pro-inflammatory cytokine release, mainly by clustering of FCGR2B with different activating FCGR receptors or with the BCR by immune complexes. TTST6IQ SQ MTMETQMSQNVCPRNLWLLQPLTVLLLLASADSQAAAPPKAVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQVPSMGSSSPMGIIVAVVIATAVAAIVAAVVALIYCRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQLEETNNDYETADGGYMTLNPRAPTDDDKNIYLTLPPNDHVNSNN TTST6IQ TT Literature-reported TTH1ZOP ID TTH1ZOP TTH1ZOP TN Inactive rhomboid protein 2 (RHBDF2) TTH1ZOP UP Q6PJF5 TTH1ZOP UC RHDF2_HUMAN TTH1ZOP BC Peptidase S54 family TTH1ZOP SN iRhom2; Rhomboid veinlet-like protein 6; Rhomboid veinlet-like protein 5; Rhomboid family member 2; Rhomboid 5 homolog 2; RHBDL6; RHBDL5 TTH1ZOP GN RHBDF2 TTH1ZOP FC Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration. TTH1ZOP SQ MASADKNGGSVSSVSSSRLQSRKPPNLSITIPPPEKETQAPGEQDSMLPEGFQNRRLKKSQPRTWAAHTTACPPSFLPKRKNPAYLKSVSLQEPRSRWQESSEKRPGFRRQASLSQSIRKGAAQWFGVSGDWEGQRQQWQRRSLHHCSMRYGRLKASCQRDLELPSQEAPSFQGTESPKPCKMPKIVDPLARGRAFRHPEEMDRPHAPHPPLTPGVLSLTSFTSVRSGYSHLPRRKRMSVAHMSLQAAAALLKGRSVLDATGQRCRVVKRSFAFPSFLEEDVVDGADTFDSSFFSKEEMSSMPDDVFESPPLSASYFRGIPHSASPVSPDGVQIPLKEYGRAPVPGPRRGKRIASKVKHFAFDRKKRHYGLGVVGNWLNRSYRRSISSTVQRQLESFDSHRPYFTYWLTFVHVIITLLVICTYGIAPVGFAQHVTTQLVLRNKGVYESVKYIQQENFWVGPSSIDLIHLGAKFSPCIRKDGQIEQLVLRERDLERDSGCCVQNDHSGCIQTQRKDCSETLATFVKWQDDTGPPMDKSDLGQKRTSGAVCHQDPRTCEEPASSGAHIWPDDITKWPICTEQARSNHTGFLHMDCEIKGRPCCIGTKGSCEITTREYCEFMHGYFHEEATLCSQVHCLDKVCGLLPFLNPEVPDQFYRLWLSLFLHAGVVHCLVSVVFQMTILRDLEKLAGWHRIAIIFILSGITGNLASAIFLPYRAEVGPAGSQFGLLACLFVELFQSWPLLERPWKAFLNLSAIVLFLFICGLLPWIDNIAHIFGFLSGLLLAFAFLPYITFGTSDKYRKRALILVSLLAFAGLFAALVLWLYIYPINWPWIEHLTCFPFTSRFCEKYELDQVLH TTH1ZOP TT Literature-reported TTASGP0 ID TTASGP0 TTASGP0 TN Influenza Env messenger RNA (Influ Env mRNA) TTASGP0 UP O70902 TTASGP0 UC ENV_HV190 TTASGP0 BC mRNA target TTASGP0 SN HIV-1 90CF056 envelope glycoprotein gp160 (mRNA); HIV-1 90CF056 env polyprotein (mRNA) TTASGP0 GN Influ Env mRNA TTASGP0 FC Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. TTASGP0 SQ METQRNYPSLWRWGTLILGMLLICSAAQNLWVTVYYGVPVWKEAKTTLFCASDAKAYETEKHNVWATHACVPTDPNPQEMVMENVTESFNMWENNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLNCTNVRNNTSNSTSSMEAGGELTNCSFNVTTVLRDKQQKVHALFYRLDVVPIDNNSTQYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGLCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEQIIIRTKNISDNTKNIIVQLKTPVNITCTRPNNNTRTSIHLGPGRAFYATGDIIGDIRQAHCNISRTDWNKTLHQVVTQLGIHLNNRTISFKPNSGGDMEVRTHSFNCRGEFFYCNTSGLFNSSWEMHTNYTSNDTKGNENITLPCRIKQIVNMWQRVGRAMYAPPIQGNIMCVSNITGLILTIDEGNASAENYTFRPGGGDMRDNWRSELYKYKVVKIEPLGIAPTKTRRRVVEREKRAVGMGASFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIQARQHMLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTNVPWNSSWSNKSQSEIWDNMTWMEWDKQISNYTEEIYRLLEVSQTQQEKNEQDLLALDKWASLWTWFDISHWLWYIKIFIMIVGGLIGLRIIFAVLSIVNRVRQGYSPLSFQTLVPNPRGPDRPEGTEEGGGEQDRDRSVRLVNGFLPVVWDDLRSLSLFSYRLLRDLLLIVVRTVELLGRRGREALKYLWNLLQYWGQELKNSAIDLLNTTAIAVAEGTDGIIVIVQRAWRAILHIPRRIRQGFERSLL TTASGP0 TT Literature-reported TTASGP0 FM mRNA target TTZSY8Q ID TTZSY8Q TTZSY8Q TN Influenza HA messenger RNA (Influ HA mRNA) TTZSY8Q UP O56140 TTZSY8Q UC HEMA_I97A1 TTZSY8Q BC mRNA target TTZSY8Q SN Hemagglutinin (mRNA); HA of influenza (mRNA) TTZSY8Q GN Influ HA mRNA TTZSY8Q FC Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic speptide. Several trimers are required to form a competent fusion pore. TTZSY8Q SQ MEKTVLLLATVSLVKSDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILERTHNGKLCDLNGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIVEKASPANDLCYPGNFNDYEELKHLLSRINHFEKIQIIPKSSWSNHDASSGVSSACPYLGRSSFFRNVVWLIKKNSAYPTIKRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPEIATRPKVNGQSGRMEFFWTILKPNDAINFESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNTPQRERRRKKRGLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIINKMNTQFEAVGREFNNLERRIENLNKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVKNGTYDYPQYSEEARLNREEISGVKLESMGTYQILSIYSTVASSLALAIMVAGLSLWMCSNGSLQCRICI TTZSY8Q TT Literature-reported TTZSY8Q FM mRNA target TTRG72O ID TTRG72O TTRG72O TN Influenza NP messenger RNA (Influ NP mRNA) TTRG72O UP O92784 TTRG72O UC NCAP_I97A1 TTRG72O BC mRNA target TTRG72O SN Influenza nucleoprotein (mRNA); Influenza nucleocapsid protein (mRNA) TTRG72O GN Influ NP mRNA TTRG72O FC The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus. Encapsidates the negative strand viral RNA, protecting it from nucleases. TTRG72O SQ MASQGTKRSYEQMETGGERQNATEIRASVGRMVGGIGRFYIQMCTELKLSDQEGRLIQNSITIERMVLSAFDERRNRYLEEHPSAGKDPKKTGGPIYRRRDGKWVRELILYDKEEIRRIWRQANNGEDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAIKGVGTMVMELIRMIKRGINDRNFWRGENGRRTRIAYERMCNILKGKFQTAAQKAMMDQVRESRNPGNAEIEDLIFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEREGYSLVGIDPFRLLQNSQVFSLIRPKENPAHKSQLVWMACHSAAFEDLRVSSFIRGTRVIPRGQLSTRGVQIASNENVEAMDSTTLELRSRYWAIRTRSGGNTNQQRASAGQISVQPTFSVQRNLPFERVTIMAAFKGNTEGRTSDMRTEIIRMMESARPEDVSFQGRGVFELSDEKATNPIVPSFDMSNEGSYFFGDNAEEYDN TTRG72O TT Literature-reported TTRG72O FM mRNA target TTQI726 ID TTQI726 TTQI726 TN Influenza Nucleoprotein (Influ NP) TTQI726 UP P03466 TTQI726 UC NCAP_I34A1 TTQI726 SN Influ Protein N; Influ Nucleoprotein; Influ Nucleocapsid protein TTQI726 GN Influ NP TTQI726 FC Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus. TTQI726 PD 5V5O; 5NQ3; 5NPZ; 4ZDU; 4NQV TTQI726 SQ MASQGTKRSYEQMETDGERQNATEIRASVGKMIGGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVNGKWMRELILYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELVRMIKRGINDRNFWRGENGRKTRIAYERMCNILKGKFQTAAQKAMMDQVRESRNPGNAEFEDLTFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEREGYSLVGIDPFRLLQNSQVYSLIRPNENPAHKSQLVWMACHSAAFEDLRVLSFIKGTKVLPRGKLSTRGVQIASNENMETMESSTLELRSRYWAIRTRSGGNTNQQRASAGQISIQPTFSVQRNLPFDRTTIMAAFNGNTEGRTSDMRTEIIRMMESARPEDVSFQGRGVFELSDEKAASPIVPSFDMSNEGSYFFGDNAEEYDN TTQI726 TT Literature-reported TTSC4OM ID TTSC4OM TTSC4OM TN Influenza PB2 messenger RNA (Influ PB2 mRNA) TTSC4OM UP O56266 TTSC4OM UC PB2_I97A1 TTSC4OM BC mRNA target TTSC4OM SN RNA-directed RNA polymerase subunit P3 (mRNA); Polymerase basic protein 2 (mRNA); PB2 (mRNA) TTSC4OM GN Influ PB2 mRNA TTSC4OM FC Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. TTSC4OM SQ MERIKELRDLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRIMEMIPERNEQGQTLWSKTNDAGSDRVMVSPLAVTWWNRNGPTTSTVHYPKVYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDMNPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKREELKNCNISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRATVSADPLASLLEMCHSTQIGGVRMVDILKQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTKGFSVKREEEVLTGNLQTLKIKVHEGYEEFTMVGRRATAILRKATRRMIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGIEPIDNVMGMIGILPDMTPSTEMSLRGVRVSKMGVDEYSSTERVVVSIDRFLRVRDQQGNVLLSPEEVSETQGMEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQEPTMLYNKMEFEPFQSLVPKAARSQYSGFVRTLFQQMRDVLGTFDTVQIIKLLPFAAAPPEQSRMQFSSLTVNVRGSGMRILVRGNSPAFNYNKTTKRLTILGKDAGALTEDPDEGTAGVESAVLRGFLILGKEDKRYGPALSINELSNLTKGEKANVLIRQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN TTSC4OM TT Literature-reported TTSC4OM FM mRNA target TTKIAT3 ID TTKIAT3 TTKIAT3 TN Inositol-requiring protein 1 (IRE1a) TTKIAT3 UP O75460 TTKIAT3 UC ERN1_HUMAN TTKIAT3 SN hIRE1p; Serine/threonine-protein kinase/endoribonuclease IRE1; Ire1-alpha; IRE1a; IRE1; Endoplasmic reticulum-to-nucleus signaling 1 TTKIAT3 GN ERN1 TTKIAT3 FC Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity. The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA. The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes. Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A. TTKIAT3 PD 6HX1; 6HV0; 5HGI; 4Z7H; 4Z7G TTKIAT3 SQ MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL TTKIAT3 TT Literature-reported TTADRX7 ID TTADRX7 TTADRX7 TN Insulin receptor substrate-1 (IRS1) TTADRX7 UP P35568 TTADRX7 UC IRS1_HUMAN TTADRX7 SN Insulin receptor substrate 1; IRS-1 TTADRX7 GN IRS1 TTADRX7 FC When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit. May mediate the control of various cellular processes by insulin. TTADRX7 PD 6BNT; 5U1M; 2Z8C; 1QQG; 1K3A TTADRX7 SQ MASPPESDGFSDVRKVGYLRKPKSMHKRFFVLRAASEAGGPARLEYYENEKKWRHKSSAPKRSIPLESCFNINKRADSKNKHLVALYTRDEHFAIAADSEAEQDSWYQALLQLHNRAKGHHDGAAALGAGGGGGSCSGSSGLGEAGEDLSYGDVPPGPAFKEVWQVILKPKGLGQTKNLIGIYRLCLTSKTISFVKLNSEAAAVVLQLMNIRRCGHSENFFFIEVGRSAVTGPGEFWMQVDDSVVAQNMHETILEAMRAMSDEFRPRSKSQSSSNCSNPISVPLRRHHLNNPPPSQVGLTRRSRTESITATSPASMVGGKPGSFRVRASSDGEGTMSRPASVDGSPVSPSTNRTHAHRHRGSARLHPPLNHSRSIPMPASRCSPSATSPVSLSSSSTSGHGSTSDCLFPRRSSASVSGSPSDGGFISSDEYGSSPCDFRSSFRSVTPDSLGHTPPARGEEELSNYICMGGKGPSTLTAPNGHYILSRGGNGHRCTPGTGLGTSPALAGDEAASAADLDNRFRKRTHSAGTSPTITHQKTPSQSSVASIEEYTEMMPAYPPGGGSGGRLPGHRHSAFVPTRSYPEEGLEMHPLERRGGHHRPDSSTLHTDDGYMPMSPGVAPVPSGRKGSGDYMPMSPKSVSAPQQIINPIRRHPQRVDPNGYMMMSPSGGCSPDIGGGPSSSSSSSNAVPSGTSYGKLWTNGVGGHHSHVLPHPKPPVESSGGKLLPCTGDYMNMSPVGDSNTSSPSDCYYGPEDPQHKPVLSYYSLPRSFKHTQRPGEPEEGARHQHLRLSTSSGRLLYAATADDSSSSTSSDSLGGGYCGARLEPSLPHPHHQVLQPHLPRKVDTAAQTNSRLARPTRLSLGDPKASTLPRAREQQQQQQPLLHPPEPKSPGEYVNIEFGSDQSGYLSGPVAFHSSPSVRCPSQLQPAPREEETGTEEYMKMDLGPGRRAAWQESTGVEMGRLGPAPPGAASICRPTRAVPSSRGDYMTMQMSCPRQSYVDTSPAAPVSYADMRTGIAAEEVSLPRATMAAASSSSAASASPTGPQGAAELAAHSSLLGGPQGPGGMSAFTRVNLSPNRNQSAKVIRADPQGCRRRHSSETFSSTPSATRVGNTVPFGAGAAVGGGGGSSSSSEDVKRHSSASFENVWLRPGELGGAPKEPAKLCGAAGGLENGLNYIDLDLVKDFKQCPQECTPEPQPPPPPPPHQPLGSGESSSTRRSSEDLSAYASISFQKQPEDRQ TTADRX7 TT Clinical trial TTZHNQA ID TTZHNQA TTZHNQA TN Insulin-like growth factor-binding protein 3 (IGFBP3) TTZHNQA UP P17936 TTZHNQA UC IBP3_HUMAN TTZHNQA BC Insulin-like growth factor binding TTZHNQA SN IGFBP-3; IGF-binding protein 3; IBP3; IBP-3 TTZHNQA GN IGFBP3 TTZHNQA FC IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R. TTZHNQA SQ MQRARPTLWAAALTLLVLLRGPPVARAGASSAGLGPVVRCEPCDARALAQCAPPPAVCAELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVNASAVSRLRAYLLPAPPAPGNASESEEDRSAGSVESPSVSSTHRVSDPKFHPLHSKIIIIKKGHAKDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNHLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVHCYSMQSK TTZHNQA TT Clinical trial TTZHNQA FM Insulin-like growth factor binding TTUQ01B ID TTUQ01B TTUQ01B TN Insulin-like growth factor-binding protein 7 (IGFBP7) TTUQ01B UP Q16270 TTUQ01B UC IBP7_HUMAN TTUQ01B BC Immunoglobulin TTUQ01B SN Tumorderived adhesion factor; Tumor-derived adhesion factor; TAF; Prostacyclinstimulating factor; Prostacyclin-stimulating factor; PSF; PGI2stimulating factor; PGI2-stimulating factor; MAC25 protein; MAC25; Insulinlike growth factorbinding protein 7; IGFbinding protein 7; IGFBPrP1; IGFBP-rP1; IGFBP-7; IGF-binding protein 7; IBP7; IBP-7 TTUQ01B GN IGFBP7 TTUQ01B FC Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion. Binds IGF-I and IGF-II with a relatively low affinity. TTUQ01B SQ MERPSLRALLLGAAGLLLLLLPLSSSSSSDTCGPCEPASCPPLPPLGCLLGETRDACGCCPMCARGEGEPCGGGGAGRGYCAPGMECVKSRKRRKGKAGAAAGGPGVSGVCVCKSRYPVCGSDGTTYPSGCQLRAASQRAESRGEKAITQVSKGTCEQGPSIVTPPKDIWNVTGAQVYLSCEVIGIPTPVLIWNKVKRGHYGVQRTELLPGDRDNLAIQTRGGPEKHEVTGWVLVSPLSKEDAGEYECHASNSQGQASASAKITVVDALHEIPVKKGEGAEL TTUQ01B TT Literature-reported TT6NV8L ID TT6NV8L TT6NV8L TN Integrin alpha-1/beta-1 (ITGA1/B1) TT6NV8L UP P56199-P05556 TT6NV8L UC ITA1_HUMAN-ITB1_HUMAN TT6NV8L BC Integrin TT6NV8L SN alpha(1)beta(1) integrin; Alpha 1 beta 1 integrin TT6NV8L GN ITGA1-ITGB1 TT6NV8L FC Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G- E-R in collagen. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. TT6NV8L SQ MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGKMAPRPRARPGVAVACCWLLTVVLRCCVSFNVDVKNSMTFSGPVEDMFGYTVQQYENEEGKWVLIGSPLVGQPKNRTGDVYKCPVGRGESLPCVKLDLPVNTSIPNVTEVKENMTFGSTLVTNPNGGFLACGPLYAYRCGHLHYTTGICSDVSPTFQVVNSIAPVQECSTQLDIVIVLDGSNSIYPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTMTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRGNLSTEKFVEEIKSIASEPTEKHFFNVSDELALVTIVKTLGERIFALEATADQSAASFEMEMSQTGFSAHYSQDWVMLGAVGAYDWNGTVVMQKASQIIIPRNTTFNVESTKKNEPLASYLGYTVNSATASSGDVLYIAGQPRYNHTGQVIIYRMEDGNIKILQTLSGEQIGSYFGSILTTTDIDKDSNTDILLVGAPMYMGTEKEEQGKVYVYALNQTRFEYQMSLEPIKQTCCSSRQHNSCTTENKNEPCGARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHGGAVYIYHGSGKTIRKEYAQRIPSGGDGKTLKFFGQSIHGEMDLNGDGLTDVTIGGLGGAALFWSRDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSKEDTIYEADLQYRVTLDSLRQISRSFFSGTQERKVQRNITVRKSECTKHSFYMLDKHDFQDSVRITLDFNLTDPENGPVLDDSLPNSVHEYIPFAKDCGNKEKCISDLSLHVATTEKDLLIVRSQNDKFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKDSCESNHNITCKVGYPFLRRGEMVTFKILFQFNTSYLMENVTIYLSATSDSEEPPETLSDNVVNISIPVKYEVGLQFYSSASEYHISIAANETVPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSENANCRPHIFEDPFSINSGKKMTTSTDHLKRGTILDCNTCKFATITCNLTSSDISQVNVSLILWKPTFIKSYFSSLNLTIRGELRSENASLVLSSSNQKRELAIQISKDGLPGRVPLWVILLSAFAGLLLLMLLILALWKIGFFKRPLKKKMEK TT6NV8L TT Literature-reported TTKPR4W ID TTKPR4W TTKPR4W TN Integrin alpha-1/beta-3 (ITGA1/B3) TTKPR4W UP P56199-P05106 TTKPR4W UC ITA1_HUMAN-ITB3_HUMAN TTKPR4W BC Integrin TTKPR4W SN alpha(1)beta(3) integrin; Alpha 1 beta 3 integrin TTKPR4W GN ITGA1-ITGB3 TTKPR4W FC The heterodimeric receptor is involved in cell-cell adhesion and may play a role in inflammation and fibrosis. The alpha 1 subunit contains an inserted (I) von Willebrand factor type I domain which is thought to be involved in collagen binding. TTKPR4W SQ MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGTMAPRPRARPGVAVACCWLLTVVLRCCVSFNVDVKNSMTFSGPVEDMFGYTVQQYENEEGKWVLIGSPLVGQPKNRTGDVYKCPVGRGESLPCVKLDLPVNTSIPNVTEVKENMTFGSTLVTNPNGGFLACGPLYAYRCGHLHYTTGICSDVSPTFQVVNSIAPVQECSTQLDIVIVLDGSNSIYPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTMTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRGNLSTEKFVEEIKSIASEPTEKHFFNVSDELALVTIVKTLGERIFALEATADQSAASFEMEMSQTGFSAHYSQDWVMLGAVGAYDWNGTVVMQKASQIIIPRNTTFNVESTKKNEPLASYLGYTVNSATASSGDVLYIAGQPRYNHTGQVIIYRMEDGNIKILQTLSGEQIGSYFGSILTTTDIDKDSNTDILLVGAPMYMGTEKEEQGKVYVYALNQTRFEYQMSLEPIKQTCCSSRQHNSCTTENKNEPCGARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHGGAVYIYHGSGKTIRKEYAQRIPSGGDGKTLKFFGQSIHGEMDLNGDGLTDVTIGGLGGAALFWSRDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSKEDTIYEADLQYRVTLDSLRQISRSFFSGTQERKVQRNITVRKSECTKHSFYMLDKHDFQDSVRITLDFNLTDPENGPVLDDSLPNSVHEYIPFAKDCGNKEKCISDLSLHVATTEKDLLIVRSQNDKFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKDSCESNHNITCKVGYPFLRRGEMVTFKILFQFNTSYLMENVTIYLSATSDSEEPPETLSDNVVNISIPVKYEVGLQFYSSASEYHISIAANETVPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSENANCRPHIFEDPFSINSGKKMTTSTDHLKRGTILDCNTCKFATITCNLTSSDISQVNVSLILWKPTFIKSYFSSLNLTIRGELRSENASLVLSSSNQKRELAIQISKDGLPGRVPLWVILLSAFAGLLLLMLLILALWKIGFFKRPLKKKMEK TTKPR4W TT Literature-reported TTANXZ7 ID TTANXZ7 TTANXZ7 TN Integrin alpha-11 (ITGA11) TTANXZ7 UP Q9UKX5 TTANXZ7 UC ITA11_HUMAN TTANXZ7 BC Integrin TTANXZ7 SN MSTP018 TTANXZ7 GN ITGA11 TTANXZ7 FC Integrin alpha-11/beta-1 is a receptor for collagen. TTANXZ7 SQ MDLPRGLVVAWALSLWPGFTDTFNMDTRKPRVIPGSRTAFFGYTVQQHDISGNKWLVVGAPLETNGYQKTGDVYKCPVIHGNCTKLNLGRVTLSNVSERKDNMRLGLSLATNPKDNSFLACSPLWSHECGSSYYTTGMCSRVNSNFRFSKTVAPALQRCQTYMDIVIVLDGSNSIYPWVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETRTAFGIEFARSEAFQKGGRKGAKKVMIVITDGESHDSPDLEKVIQQSERDNVTRYAVAVLGYYNRRGINPETFLNEIKYIASDPDDKHFFNVTDEAALKDIVDALGDRIFSLEGTNKNETSFGLEMSQTGFSSHVVEDGVLLGAVGAYDWNGAVLKETSAGKVIPLRESYLKEFPEELKNHGAYLGYTVTSVVSSRQGRVYVAGAPRFNHTGKVILFTMHNNRSLTIHQAMRGQQIGSYFGSEITSVDIDGDGVTDVLLVGAPMYFNEGRERGKVYVYELRQNLFVYNGTLKDSHSYQNARFGSSIASVRDLNQDSYNDVVVGAPLEDNHAGAIYIFHGFRGSILKTPKQRITASELATGLQYFGCSIHGQLDLNEDGLIDLAVGALGNAVILWSRPVVQINASLHFEPSKINIFHRDCKRSGRDATCLAAFLCFTPIFLAPHFQTTTVGIRYNATMDERRYTPRAHLDEGGDRFTNRAVLLSSGQELCERINFHVLDTADYVKPVTFSVEYSLEDPDHGPMLDDGWPTTLRVSVPFWNGCNEDEHCVPDLVLDARSDLPTAMEYCQRVLRKPAQDCSAYTLSFDTTVFIIESTRQRVAVEATLENRGENAYSTVLNISQSANLQFASLIQKEDSDGSIECVNEERRLQKQVCNVSYPFFRAKAKVAFRLDFEFSKSIFLHHLEIELAAGSDSNERDSTKEDNVAPLRFHLKYEADVLFTRSSSLSHYEVKPNSSLERYDGIGPPFSCIFRIQNLGLFPIHGMMMKITIPIATRSGNRLLKLRDFLTDEANTSCNIWGNSTEYRPTPVEEDLRRAPQLNHSNSDVVSINCNIRLVPNQEINFHLLGNLWLRSLKALKYKSMKIMVNAALQRQFHSPFIFREEDPSRQIVFEISKQEDWQVPIWIIVGSTLGGLLLLALLVLALWKLGFFRSARRRREPGLDPTPKVLE TTANXZ7 TT Literature-reported TTANXZ7 FM Integrin TT0LHGI ID TT0LHGI TT0LHGI TN Integrin alpha-4/beta-4 (ITGA4/B4) TT0LHGI UP P13612-P16144 TT0LHGI UC ITA4_HUMAN-ITB4_HUMAN TT0LHGI BC Integrin TT0LHGI SN alpha(4)beta(4) integrin; Alpha 4 beta 4 integrin TT0LHGI GN ITGA4-ITGB4 TT0LHGI FC Heterodimeric integral membrane proteins composed of an alpha chain and a beta chain that function in cell surface adhesion and signaling. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha 4 subunit. TT0LHGI SQ MAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDDMAGPRPSPWARLLLAALISVSLSGTLANRCKKAPVKSCTECVRVDKDCAYCTDEMFRDRRCNTQAELLAAGCQRESIVVMESSFQITEETQIDTTLRRSQMSPQGLRVRLRPGEERHFELEVFEPLESPVDLYILMDFSNSMSDDLDNLKKMGQNLARVLSQLTSDYTIGFGKFVDKVSVPQTDMRPEKLKEPWPNSDPPFSFKNVISLTEDVDEFRNKLQGERISGNLDAPEGGFDAILQTAVCTRDIGWRPDSTHLLVFSTESAFHYEADGANVLAGIMSRNDERCHLDTTGTYTQYRTQDYPSVPTLVRLLAKHNIIPIFAVTNYSYSYYEKLHTYFPVSSLGVLQEDSSNIVELLEEAFNRIRSNLDIRALDSPRGLRTEVTSKMFQKTRTGSFHIRRGEVGIYQVQLRALEHVDGTHVCQLPEDQKGNIHLKPSFSDGLKMDAGIICDVCTCELQKEVRSARCSFNGDFVCGQCVCSEGWSGQTCNCSTGSLSDIQPCLREGEDKPCSGRGECQCGHCVCYGEGRYEGQFCEYDNFQCPRTSGFLCNDRGRCSMGQCVCEPGWTGPSCDCPLSNATCIDSNGGICNGRGHCECGRCHCHQQSLYTDTICEINYSAIHPGLCEDLRSCVQCQAWGTGEKKGRTCEECNFKVKMVDELKRAEEVVVRCSFRDEDDDCTYSYTMEGDGAPGPNSTVLVHKKKDCPPGSFWWLIPLLLLLLPLLALLLLLCWKYCACCKACLALLPCCNRGHMVGFKEDHYMLRENLMASDHLDTPMLRSGNLKGRDVVRWKVTNNMQRPGFATHAASINPTELVPYGLSLRLARLCTENLLKPDTRECAQLRQEVEENLNEVYRQISGVHKLQQTKFRQQPNAGKKQDHTIVDTVLMAPRSAKPALLKLTEKQVEQRAFHDLKVAPGYYTLTADQDARGMVEFQEGVELVDVRVPLFIRPEDDDEKQLLVEAIDVPAGTATLGRRLVNITIIKEQARDVVSFEQPEFSVSRGDQVARIPVIRRVLDGGKSQVSYRTQDGTAQGNRDYIPVEGELLFQPGEAWKELQVKLLELQEVDSLLRGRQVRRFHVQLSNPKFGAHLGQPHSTTIIIRDPDELDRSFTSQMLSSQPPPHGDLGAPQNPNAKAAGSRKIHFNWLPPSGKPMGYRVKYWIQGDSESEAHLLDSKVPSVELTNLYPYCDYEMKVCAYGAQGEGPYSSLVSCRTHQEVPSEPGRLAFNVVSSTVTQLSWAEPAETNGEITAYEVCYGLVNDDNRPIGPMKKVLVDNPKNRMLLIENLRESQPYRYTVKARNGAGWGPEREAIINLATQPKRPMSIPIIPDIPIVDAQSGEDYDSFLMYSDDVLRSPSGSQRPSVSDDTGCGWKFEPLLGEELDLRRVTWRLPPELIPRLSASSGRSSDAEAPHGPPDDGGAGGKGGSLPRSATPGPPGEHLVNGRMDFAFPGSTNSLHRMTTTSAAAYGTHLSPHVPHRVLSTSSTLTRDYNSLTRSEHSHSTTLPRDYSTLTSVSSHDSRLTAGVPDTPTRLVFSALGPTSLRVSWQEPRCERPLQGYSVEYQLLNGGELHRLNIPNPAQTSVVVEDLLPNHSYVFRVRAQSQEGWGREREGVITIESQVHPQSPLCPLPGSAFTLSTPSAPGPLVFTALSPDSLQLSWERPRRPNGDIVGYLVTCEMAQGGGPATAFRVDGDSPESRLTVPGLSENVPYKFKVQARTTEGFGPEREGIITIESQDGGPFPQLGSRAGLFQHPLQSEYSSITTTHTSATEPFLVDGLTLGAQHLEAGGSLTRHVTQEFVSRTLTTSGTLSTHMDQQFFQT TT0LHGI TT Literature-reported TT0LHGI FM Integrin TT165T3 ID TT165T3 TT165T3 TN Integrin alpha-6 (ITGA6) TT165T3 UP P23229 TT165T3 UC ITA6_HUMAN TT165T3 BC Integrin TT165T3 SN VLA-6 integrin; VLA-6; CD49f; CD49 antigen-like family member F; Alpha6 beta1 integrin TT165T3 GN ITGA6 TT165T3 FC Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion. Integrin alpha-6/beta-4 (ITGA6:ITGB4) is a receptor for laminin in epithelial cells and it plays a critical structural role in the hemidesmosome. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling. ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is a receptor for laminin on platelets. TT165T3 SQ MAAAGQLCLLYLSAGLLSRLGAAFNLDTREDNVIRKYGDPGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEALPLQRANRTGGLYSCDITARGPCTRIEFDNDADPTSESKEDQWMGVTVQSQGPGGKVVTCAHRYEKRQHVNTKQESRDIFGRCYVLSQNLRIEDDMDGGDWSFCDGRLRGHEKFGSCQQGVAATFTKDFHYIVFGAPGTYNWKGIVRVEQKNNTFFDMNIFEDGPYEVGGETEHDESLVPVPANSYLGLLFLTSVSYTDPDQFVYKTRPPREQPDTFPDVMMNSYLGFSLDSGKGIVSKDEITFVSGAPRANHSGAVVLLKRDMKSAHLLPEHIFDGEGLASSFGYDVAVVDLNKDGWQDIVIGAPQYFDRDGEVGGAVYVYMNQQGRWNNVKPIRLNGTKDSMFGIAVKNIGDINQDGYPDIAVGAPYDDLGKVFIYHGSANGINTKPTQVLKGISPYFGYSIAGNMDLDRNSYPDVAVGSLSDSVTIFRSRPVINIQKTITVTPNRIDLRQKTACGAPSGICLQVKSCFEYTANPAGYNPSISIVGTLEAEKERRKSGLSSRVQFRNQGSEPKYTQELTLKRQKQKVCMEETLWLQDNIRDKLRPIPITASVEIQEPSSRRRVNSLPEVLPILNSDEPKTAHIDVHFLKEGCGDDNVCNSNLKLEYKFCTREGNQDKFSYLPIQKGVPELVLKDQKDIALEITVTNSPSNPRNPTKDGDDAHEAKLIATFPDTLTYSAYRELRAFPEKQLSCVANQNGSQADCELGNPFKRNSNVTFYLVLSTTEVTFDTPDLDINLKLETTSNQDNLAPITAKAKVVIELLLSVSGVAKPSQVYFGGTVVGEQAMKSEDEVGSLIEYEFRVINLGKPLTNLGTATLNIQWPKEISNGKWLLYLVKVESKGLEKVTCEPQKEINSLNLTESHNSRKKREITEKQIDDNRKFSLFAERKYQTLNCSVNVNCVNIRCPLRGLDSKASLILRSRLWNSTFLEEYSKLNYLDILMRAFIDVTAAAENIRLPNAGTQVRVTVFPSKTVAQYSGVPWWIILVAILAGILMLALLVFILWKCGFFKRSRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS TT165T3 TT Literature-reported TT165T3 FM Integrin TT1FW8B ID TT1FW8B TT1FW8B TN Integrin alpha-8 (ITGA8) TT1FW8B UP P53708 TT1FW8B UC ITA8_HUMAN TT1FW8B BC Integrin TT1FW8B SN Integrin alpha-8 light chain; Integrin alpha-8 heavy chain TT1FW8B GN ITGA8 TT1FW8B FC It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney genesis. Neuronal receptor for TNC it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons. Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. TT1FW8B SQ MSPGASRGPRGSQAPLIAPLCCAAAALGMLLWSPACQAFNLDVEKLTVYSGPKGSYFGYAVDFHIPDARTASVLVGAPKANTSQPDIVEGGAVYYCPWPAEGSAQCRQIPFDTTNNRKIRVNGTKEPIEFKSNQWFGATVKAHKGKVVACAPLYHWRTLKPTPEKDPVGTCYVAIQNFSAYAEFSPCRNSNADPEGQGYCQAGFSLDFYKNGDLIVGGPGSFYWQGQVITASVADIIANYSFKDILRKLAGEKQTEVAPASYDDSYLGYSVAAGEFTGDSQQELVAGIPRGAQNFGYVSIINSTDMTFIQNFTGEQMASYFGYTVVVSDVNSDGLDDVLVGAPLFMEREFESNPREVGQIYLYLQVSSLLFRDPQILTGTETFGRFGSAMAHLGDLNQDGYNDIAIGVPFAGKDQRGKVLIYNGNKDGLNTKPSQVLQGVWASHAVPSGFGFTLRGDSDIDKNDYPDLIVGAFGTGKVAVYRARPVVTVDAQLLLHPMIINLENKTCQVPDSMTSAACFSLRVCASVTGQSIANTIVLMAEVQLDSLKQKGAIKRTLFLDNHQAHRVFPLVIKRQKSHQCQDFIVYLRDETEFRDKLSPINISLNYSLDESTFKEGLEVKPILNYYRENIVSEQAHILVDCGEDNLCVPDLKLSARPDKHQVIIGDENHLMLIINARNEGEGAYEAELFVMIPEEADYVGIERNNKGFRPLSCEYKMENVTRMVVCDLGNPMVSGTNYSLGLRFAVPRLEKTNMSINFDLQIRSSNKDNPDSNFVSLQINITAVAQVEIRGVSHPPQIVLPIHNWEPEEEPHKEEEVGPLVEHIYELHNIGPSTISDTILEVGWPFSARDEFLLYIFHIQTLGPLQCQPNPNINPQDIKPAASPEDTPELSAFLRNSTIPHLVRKRDVHVVEFHRQSPAKILNCTNIECLQISCAVGRLEGGESAVLKVRSRLWAHTFLQRKNDPYALASLVSFEVKKMPYTDQPAKLPEGSIVIKTSVIWATPNVSFSIPLWVIILAILLGLLVLAILTLALWKCGFFDRARPPQEDMTDREQLTNDKTPEA TT1FW8B TT Literature-reported TTH0Z37 ID TTH0Z37 TTH0Z37 TN Integrin alpha-E (ITGAE) TTH0Z37 UP P38570 TTH0Z37 UC ITAE_HUMAN TTH0Z37 BC Integrin TTH0Z37 SN Mucosal lymphocyte 1 antigen; Integrin alphaIEL; Integrin alphaE heavy chain; Integrin alpha-IEL; HML1 antigen; HML-1 antigen; CD103 TTH0Z37 GN ITGAE TTH0Z37 FC It mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell monolayers. Integrin alpha-E/beta-7 is a receptor for E-cadherin. TTH0Z37 SQ MWLFHTLLCIASLALLAAFNVDVARPWLTPKGGAPFVLSSLLHQDPSTNQTWLLVTSPRTKRTPGPLHRCSLVQDEILCHPVEHVPIPKGRHRGVTVVRSHHGVLICIQVLVRRPHSLSSELTGTCSLLGPDLRPQAQANFFDLENLLDPDARVDTGDCYSNKEGGGEDDVNTARQRRALEKEEEEDKEEEEDEEEEEAGTEIAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNITQVGSVTKTASAMQHVLDSIFTSSHGSRRKASKVMVVLTDGGIFEDPLNLTTVINSPKMQGVERFAIGVGEEFKSARTARELNLIASDPDETHAFKVTNYMALDGLLSKLRYNIISMEGTVGDALHYQLAQIGFSAQILDERQVLLGAVGAFDWSGGALLYDTRSRRGRFLNQTAAAAADAEAAQYSYLGYAVAVLHKTCSLSYIAGAPRYKHHGAVFELQKEGREASFLPVLEGEQMGSYFGSELCPVDIDMDGSTDFLLVAAPFYHVHGEEGRVYVYRLSEQDGSFSLARILSGHPGFTNARFGFAMAAMGDLSQDKLTDVAIGAPLEGFGADDGASFGSVYIYNGHWDGLSASPSQRIRASTVAPGLQYFGMSMAGGFDISGDGLADITVGTLGQAVVFRSRPVVRLKVSMAFTPSALPIGFNGVVNVRLCFEISSVTTASESGLREALLNFTLDVDVGKQRRRLQCSDVRSCLGCLREWSSGSQLCEDLLLMPTEGELCEEDCFSNASVKVSYQLQTPEGQTDHPQPILDRYTEPFAIFQLPYEKACKNKLFCVAELQLATTVSQQELVVGLTKELTLNINLTNSGEDSYMTSMALNYPRNLQLKRMQKPPSPNIQCDDPQPVASVLIMNCRIGHPVLKRSSAHVSVVWQLEENAFPNRTADITVTVTNSNERRSLANETHTLQFRHGFVAVLSKPSIMYVNTGQGLSHHKEFLFHVHGENLFGAEYQLQICVPTKLRGLQVVAVKKLTRTQASTVCTWSQERACAYSSVQHVEEWHSVSCVIASDKENVTVAAEISWDHSEELLKDVTELQILGEISFNKSLYEGLNAENHRTKITVVFLKDEKYHSLPIIIKGSVGGLLVLIVILVILFKCGFFKRKYQQLNLESIRKAQLKSENLLEEEN TTH0Z37 TT Literature-reported TT4SWR8 ID TT4SWR8 TT4SWR8 TN Interleukin 12 receptor beta-2 (IL12RB2) TT4SWR8 UP Q99665 TT4SWR8 UC I12R2_HUMAN TT4SWR8 BC Cytokine receptor TT4SWR8 SN Interleukin-12 receptor subunit beta-2; IL-12RB2; IL-12R-beta2; IL-12R-beta-2; IL-12R subunit beta-2; IL-12R beta 2; IL-12 receptor subunit beta-2; IL-12 receptor beta-2 TT4SWR8 GN IL12RB2 TT4SWR8 FC Receptor for interleukin-12. This subunit is the signaling component coupling to the JAK2/STAT4 pathway. Promotes the proliferation of T-cells as well as NK cells. Induces the promotion of T-cells towards the Th1 phenotype by strongly enhancing IFN-gamma production. TT4SWR8 SQ MAHTFRGCSLAFMFIITWLLIKAKIDACKRGDVTVKPSHVILLGSTVNITCSLKPRQGCFHYSRRNKLILYKFDRRINFHHGHSLNSQVTGLPLGTTLFVCKLACINSDEIQICGAEIFVGVAPEQPQNLSCIQKGEQGTVACTWERGRDTHLYTEYTLQLSGPKNLTWQKQCKDIYCDYLDFGINLTPESPESNFTAKVTAVNSLGSSSSLPSTFTFLDIVRPLPPWDIRIKFQKASVSRCTLYWRDEGLVLLNRLRYRPSNSRLWNMVNVTKAKGRHDLLDLKPFTEYEFQISSKLHLYKGSWSDWSESLRAQTPEEEPTGMLDVWYMKRHIDYSRQQISLFWKNLSVSEARGKILHYQVTLQELTGGKAMTQNITGHTSWTTVIPRTGNWAVAVSAANSKGSSLPTRINIMNLCEAGLLAPRQVSANSEGMDNILVTWQPPRKDPSAVQEYVVEWRELHPGGDTQVPLNWLRSRPYNVSALISENIKSYICYEIRVYALSGDQGGCSSILGNSKHKAPLSGPHINAITEEKGSILISWNSIPVQEQMGCLLHYRIYWKERDSNSQPQLCEIPYRVSQNSHPINSLQPRVTYVLWMTALTAAGESSHGNEREFCLQGKANWMAFVAPSICIAIIMVGIFSTHYFQQKVFVLLAALRPQWCSREIPDPANSTCAKKYPIAEEKTQLPLDRLLIDWPTPEDPEPLVISEVLHQVTPVFRHPPCSNWPQREKGIQGHQASEKDMMHSASSPPPPRALQAESRQLVDLYKVLESRGSDPKPENPACPWTVLPAGDLPTHDGYLPSNIDDLPSHEAPLADSLEELEPQHISLSVFPSSSLHPLTFSCGDKLTLDQLKMRCDSLML TT4SWR8 TT Literature-reported TT4SWR8 FM Transmembrane protein TT4PH9E ID TT4PH9E TT4PH9E TN Interleukin 8 receptor (IL8R) TT4PH9E UP P25024; P25025 TT4PH9E UC CXCR1_HUMAN; CXCR2_HUMAN TT4PH9E BC Cytokine receptor TT4PH9E SN IL8R; IL-8R; IL-8 receptor; High affinity interleukin-8 receptor; CXCR; CXC-R; CDw128 TT4PH9E GN CXCR1; CXCR2 TT4PH9E FC This receptor binds to IL-8 with a high affinity and to MGSA (GRO) with a low affinity. Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activate a phosphatidylinositol-calcium second messenger system. TT4PH9E SQ MSNITDPQMWDFDDLNFTGMPPADEDYSPCMLETETLNKYVVIIAYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMNLSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNIGRALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL TT4PH9E TT Literature-reported TTC5LTG ID TTC5LTG TTC5LTG TN Interleukin-27 (IL27) TTC5LTG UP Q8TAD2 TTC5LTG UC IL17D_HUMAN TTC5LTG BC Cytokine: interleukin TTC5LTG SN UNQ3096/PRO21175; Interleukin27; Interleukin17D; Interleukin-17D; IL-27; IL-17D TTC5LTG GN IL17D TTC5LTG FC Induces expression of IL6, CXCL8/IL8, and CSF2/GM-CSF from endothelial cells. TTC5LTG SQ MLVAGFLLALPPSWAAGAPRAGRRPARPRGCADRPEELLEQLYGRLAAGVLSAFHHTLQLGPREQARNASCPAGGRPADRRFRPPTNLRSVSPWAYRISYDPARYPRYLPEAYCLCRGCLTGLFGEEDVRFRSAPVYMPTVVLRRTPACAGGRSVYTEAYVTIPVGCTCVPEPEKDADSINSSIDKQGAKLLLGPNDAPAGP TTC5LTG TT Clinical trial TTJF68X ID TTJF68X TTJF68X TN Interleukin-35 (IL35) TTJF68X UP Q14213 TTJF68X UC IL27B_HUMAN TTJF68X BC Cytokine: interleukin TTJF68X SN Interleukin-27 subunit beta; IL27B; IL-27B; IL-27 subunit beta; Epstein-Barr virus-induced gene 3 protein; EBV-induced gene 3 protein TTJF68X GN EBI3 TTJF68X FC IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines. Associates with IL27 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. TTJF68X SQ MTPQLLLALVLWASCPPCSGRKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSFIATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVLNVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQVQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSFILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK TTJF68X TT Literature-reported TTH7UO3 ID TTH7UO3 TTH7UO3 TN Inward rectifier potassium channel Kir2.1 (KCNJ2) TTH7UO3 UP P63252 TTH7UO3 UC KCNJ2_HUMAN TTH7UO3 BC Inward rectifier potassium channel TTH7UO3 SN hIRK1; Potassium channel, inwardly rectifying subfamily J member 2; Inward rectifier K(+) channel Kir2.1; IRK1; IRK-1; Cardiac inward rectifier potassium channel TTH7UO3 GN KCNJ2 TTH7UO3 FC Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium or cesium. Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. TTH7UO3 SQ MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKEGKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEDDSENGVPESTSTDTPPDIDLHNQASVPLEPRPLRRESEI TTH7UO3 TT Literature-reported TTVW8QH ID TTVW8QH TTVW8QH TN Inward rectifier potassium channel Kir2.6 (KCNJ18) TTVW8QH UP B7U540 TTVW8QH UC KCJ18_HUMAN TTVW8QH BC Inward rectifier potassium channel TTVW8QH SN Potassium channel, inwardly rectifying subfamily J member 18; KCNJ18; Inward rectifier potassium channel 18; Inward rectifier K(+) channel Kir2.6 TTVW8QH GN KCNJ18 TTVW8QH FC Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised,the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. TTVW8QH SQ MTAASRANPYSIVSLEEDGLHLVTMSGANGFGNGKVHTRRRCRNRFVKKNGQCNIAFANMDEKSQRYLADMFTTCVDIRWRYMLLIFSLAFLASWLLFGVIFWVIAVAHGDLEPAEGHGRTPCVMQVHGFMAAFLFSIETQTTIGYGLRCVTEECLVAVFMVVAQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVALRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRVTEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEIDEASPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLANEILWGHRFEPVLFEEKNQYKIDYSHFHKTYEVPSTPRCSAKDLVENKFLLPSANSFCYENELAFLSRDEEDEADGDQDGRSRDGLSPQARHDFDRLQAGGGVLEQRPYRRGSEI TTVW8QH TT Literature-reported TTTIBVP ID TTTIBVP TTTIBVP TN Inward rectifier potassium channel Kir3.2 (KCNJ6) TTTIBVP UP P48051 TTTIBVP UC KCNJ6_HUMAN TTTIBVP BC Inward rectifier potassium channel TTTIBVP SN Potassium channel, inwardly rectifying subfamily J member 6; KCNJ7; KATP2; KATP-2; Inward rectifier K(+) channel Kir3.2; GIRK2; GIRK-2; G protein-activated inward rectifier potassium channel 2; BIR1 TTTIBVP GN KCNJ6 TTTIBVP FC This potassium channel may be involved in the regulation of insulin secretion by glucose and/or neurotransmitters acting through G-protein-coupled receptors. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. TTTIBVP SQ MAKLTESMTNVLEGDSMDQDVESPVAIHQPKLPKQARDDLPRHISRDRTKRKIQRYVRKDGKCNVHHGNVRETYRYLTDIFTTLVDLKWRFNLLIFVMVYTVTWLFFGMIWWLIAYIRGDMDHIEDPSWTPCVTNLNGFVSAFLFSIETETTIGYGYRVITDKCPEGIILLLIQSVLGSIVNAFMVGCMFVKISQPKKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAKLIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKEELEIVVILEGMVEATGMTCQARSSYITSEILWGYRFTPVLTLEDGFYEVDYNSFHETYETSTPSLSAKELAELASRAELPLSWSVSSKLNQHAELETEEEEKNLEEQTERNGDVANLENESKV TTTIBVP TT Literature-reported TT4VHL6 ID TT4VHL6 TT4VHL6 TN Inward rectifier potassium channel Kir3.3 (KCNJ9) TT4VHL6 UP Q92806 TT4VHL6 UC KCNJ9_HUMAN TT4VHL6 BC Inward rectifier potassium channel TT4VHL6 SN Potassium channel, inwardly rectifying subfamily J member 9; Inward rectifier K(+) channel Kir3.3; GIRK3; GIRK-3; G protein-activated inward rectifier potassium channel 3 TT4VHL6 GN KCNJ9 TT4VHL6 FC This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium (By similarity). TT4VHL6 SQ MAQENAAFSPGQEEPPRRRGRQRYVEKDGRCNVQQGNVRETYRYLTDLFTTLVDLQWRLSLLFFVLAYALTWLFFGAIWWLIAYGRGDLEHLEDTAWTPCVNNLNGFVAAFLFSIETETTIGYGHRVITDQCPEGIVLLLLQAILGSMVNAFMVGCMFVKISQPNKRAATLVFSSHAVVSLRDGRLCLMFRVGDLRSSHIVEASIRAKLIRSRQTLEGEFIPLHQTDLSVGFDTGDDRLFLVSPLVISHEIDAASPFWEASRRALERDDFEIVVILEGMVEATGMTCQARSSYLVDEVLWGHRFTSVLTLEDGFYEVDYASFHETFEVPTPSCSARELAEAAARLDAHLYWSIPSRLDEKVEEEGAGEGAGGEAGADKEQNGCLPPPESESKV TT4VHL6 TT Literature-reported TT5HWAT ID TT5HWAT TT5HWAT TN IP3 receptor isoform 1 (ITPR1) TT5HWAT UP Q14643 TT5HWAT UC ITPR1_HUMAN TT5HWAT BC Ryanodine-inositol triphosphate calcium channel TT5HWAT SN Type 1 inositol 1,4,5-trisphosphate receptor; Type 1 InsP3 receptor; InsP3R1; Inositol 1,4,5-trisphosphate receptor type 1; IP3R 1 TT5HWAT GN ITPR1 TT5HWAT FC Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1. Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways. Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. TT5HWAT SQ MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENATEELEPSPPLRQLEDHKRGEALRQVLVNRYYGNVRPSGRRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPREELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA TT5HWAT TT Literature-reported TTHN8EM ID TTHN8EM TTHN8EM TN Islet amyloid polypeptide (IAPP) TTHN8EM UP P10997 TTHN8EM UC IAPP_HUMAN TTHN8EM SN Insulinoma amyloid peptide; IAPP; Diabetes-associated peptide; Amylin TTHN8EM GN IAPP TTHN8EM FC Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. TTHN8EM PD 5MGQ; 5KO0; 5KNZ; 5K5G; 3HGZ TTHN8EM SQ MGILKLQVFLIVLSVALNHLKATPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGKRNAVEVLKREPLNYLPL TTHN8EM TT Literature-reported TTUBIOW ID TTUBIOW TTUBIOW TN Jagged-2 protein (JAG2) TTUBIOW UP Q9Y219 TTUBIOW UC JAG2_HUMAN TTUBIOW SN hJ2; Protein jagged-2; Jagged2 TTUBIOW GN JAG2 TTUBIOW FC Involved in limb development. Putative Notch ligand involved in the mediation of Notch signaling. TTUBIOW PD 5MWF; 5MW7; 5MW5 TTUBIOW SQ MRAQGRGRLPRRLLLLLALWVQAARPMGYFELQLSALRNVNGELLSGACCDGDGRTTRAGGCGHDECDTYVRVCLKEYQAKVTPTGPCSYGHGATPVLGGNSFYLPPAGAAGDRARARARAGGDQDPGLVVIPFQFAWPRSFTLIVEAWDWDNDTTPNEELLIERVSHAGMINPEDRWKSLHFSGHVAHLELQIRVRCDENYYSATCNKFCRPRNDFFGHYTCDQYGNKACMDGWMGKECKEAVCKQGCNLLHGGCTVPGECRCSYGWQGRFCDECVPYPGCVHGSCVEPWQCNCETNWGGLLCDKDLNYCGSHHPCTNGGTCINAEPDQYRCTCPDGYSGRNCEKAEHACTSNPCANGGSCHEVPSGFECHCPSGWSGPTCALDIDECASNPCAAGGTCVDQVDGFECICPEQWVGATCQLDANECEGKPCLNAFSCKNLIGGYYCDCIPGWKGINCHINVNDCRGQCQHGGTCKDLVNGYQCVCPRGFGGRHCELERDECASSPCHSGGLCEDLADGFHCHCPQGFSGPLCEVDVDLCEPSPCRNGARCYNLEGDYYCACPDDFGGKNCSVPREPCPGGACRVIDGCGSDAGPGMPGTAASGVCGPHGRCVSQPGGNFSCICDSGFTGTYCHENIDDCLGQPCRNGGTCIDEVDAFRCFCPSGWEGELCDTNPNDCLPDPCHSRGRCYDLVNDFYCACDDGWKGKTCHSREFQCDAYTCSNGGTCYDSGDTFRCACPPGWKGSTCAVAKNSSCLPNPCVNGGTCVGSGASFSCICRDGWEGRTCTHNTNDCNPLPCYNGGICVDGVNWFRCECAPGFAGPDCRINIDECQSSPCAYGATCVDEINGYRCSCPPGRAGPRCQEVIGFGRSCWSRGTPFPHGSSWVEDCNSCRCLDGRRDCSKVWCGWKPCLLAGQPEALSAQCPLGQRCLEKAPGQCLRPPCEAWGECGAEEPPSTPCLPRSGHLDNNCARLTLHFNRDHVPQGTTVGAICSGIRSLPATRAVARDRLLVLLCDRASSGASAVEVAVSFSPARDLPDSSLIQGAAHAIVAAITQRGNSSLLLAVTEVKVETVVTGGSSTGLLVPVLCGAFSVLWLACVVLCVWWTRKRRKERERSRLPREESANNQWAPLNPIRNPIERPGGHKDVLYQCKNFTPPPRRADEALPGPAGHAAVREDEEDEDLGRGEEDSLEAEKFLSHKFTKDPGRSPGRPAHWASGPKVDNRAVRSINEARYAGKE TTUBIOW TT Literature-reported TTKV0EC ID TTKV0EC TTKV0EC TN Keratin type I cytoskeletal 17 (KRT17) TTKV0EC UP Q04695 TTKV0EC UC K1C17_HUMAN TTKV0EC BC Intermediate filament family TTKV0EC SN Keratin-17; KRT17; K17; Cytokeratin-17; CK-17 TTKV0EC GN KRT17 TTKV0EC FC May play a role in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair. May be a marker of basal cell differentiation in complex epithelia and therefore indicative of a certain type of epithelial stem cells". May act as an autoantigen in the immunopathogenesis of psoriasis with certain peptide regions being a major target for autoreactive T-cells and hence causing their proliferation. Required for the correct growth of hair follicles in particular for the persistence of the anagen (growth) state. Modulates the function of TNF-alpha in the specific context of hair cycling. Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway. Involved in tissue repair. TTKV0EC SQ MTTSIRQFTSSSSIKGSSGLGGGSSRTSCRLSGGLGAGSCRLGSAGGLGSTLGGSSYSSCYSFGSGGGYGSSFGGVDGLLAGGEKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQRQAPGPARDYSQYYRTIEELQNKILTATVDNANILLQIDNARLAADDFRTKFETEQALRLSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGGEINVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGNLAETENRYCVQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLTQYKKEPVTTRQVRTIVEEVQDGKVISSREQVHQTTR TTKV0EC TT Literature-reported TT3JF9E ID TT3JF9E TT3JF9E TN Keratin type I cytoskeletal 19 (KRT19) TT3JF9E UP P08727 TT3JF9E UC K1C19_HUMAN TT3JF9E BC Intermediate filament family TT3JF9E SN Keratin19; Keratin, type I cytoskeletal 19; KRT19; K19; Cytokeratin19; CK19 TT3JF9E GN KRT19 TT3JF9E FC Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}. TT3JF9E SQ MTSYSYRQSSATSSFGGLGGGSVRFGPGVAFRAPSIHGGSGGRGVSVSSARFVSSSSSGAYGGGYGGVLTASDGLLAGNEKLTMQNLNDRLASYLDKVRALEAANGELEVKIRDWYQKQGPGPSRDYSHYYTTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVGGQVSVEVDSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDHYNNLSASKVL TT3JF9E TT Literature-reported TTQECT2 ID TTQECT2 TTQECT2 TN Kinesin-like protein KIF20B (MPHOSPH1) TTQECT2 UP Q96Q89 TTQECT2 UC KI20B_HUMAN TTQECT2 BC Myosin-kinesin ATPase TTQECT2 SN Mphase phosphoprotein 1; MPP1; M-phase phosphoprotein 1; Kinesinrelated motor interacting with PIN1; Kinesinlike protein KIF20B; Kinesin-related motor interacting with PIN1; Kinesin family member 20B; KRMP1; Cancer/testis antigen 90; CT90 TTQECT2 GN KIF20B TTQECT2 FC Required for proper midbody organization and abscission in polarized cortical stem cells. Plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. Participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in cerebral cortex growth. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression. Plus-end-directed motor enzyme that is required for completion of cytokinesis. TTQECT2 SQ MESNFNQEGVPRPSYVFSADPIARPSEINFDGIKLDLSHEFSLVAPNTEANSFESKDYLQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLYTKMNLKPHRSREYLRLSSEQEKEEIASKSALLRQIKEVTVHNDSDDTLYGSLTNSLNISEFEESIKDYEQANLNMANSIKFSVWVSFFEIYNEYIYDLFVPVSSKFQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIAQKVCVPDTLNSSQEKLFGPVKSSQDVSLDSNSNSKILNVKRATISWENSLEDLMEDEDLVEELENAEETQNVETKLLDEDLDKTLEENKAFISHEEKRKLLDLIEDLKKKLINEKKEKLTLEFKIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICATKVETEETHNYVGFEDIIDSLQDNVADIKKQAEIAHLYIASLPDPQEATACLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKSHMENTFKCNDKADTSSLIINNKLICNETVEVPKDSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDSVSQISNIDLLNLRDLSNGSEEDNLPNTQLDLLGNDYLVSKQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPDKLQTEPLSTSFEISRNKIEDGSVVLDSCEVSTENDQSTRFPKPELEIQFTPLQPNKMAVKHPGCTTPVTVKIPKARKRKSNEMEEDLVKCENKKNATPRTNLKFPISDDRNSSVKKEQKVAIRPSSKKTYSLRSQASIIGVNLATKKKEGTLQKFGDFLQHSPSILQSKAKKIIETMSSSKLSNVEASKENVSQPKRAKRKLYTSEISSPIDISGQVILMDQKMKESDHQIIKRRLRTKTAK TTQECT2 TT Literature-reported TTQECT2 FM Kinesin-like protein family TTQWICZ ID TTQWICZ TTQWICZ TN Kinesin-like protein KIF26B (KIF26B) TTQWICZ UP Q2KJY2 TTQWICZ UC KI26B_HUMAN TTQWICZ BC Myosin-kinesin ATPase TTQWICZ SN Kinesinlike protein KIF26B TTQWICZ GN KIF26B TTQWICZ FC Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds, possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8, which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules. Essential for embryonic kidney development. TTQWICZ SQ MNSVAGNKERLAVSTRGKKYGVNEVCSPTKPAAPFSPESWYRKAYEESRAGSRPTPEGAGSALGSSGTPSPGSGTSSPSSFTGSPGPASPGIGTSSPGSLGGSPGFGTGSPGSGSGGGSSPGSDRGVWCENCNARLVELKRQALRLLLPGPFPGKDPAFSAVIHDKLQVPNTIRKAWNDRDNRCDICATHLNQLKQEAIQMVLTLEQAAGSEHYDASPCSPPPLSNIPTLVGSRHVGGLQQPRDWAFVPAPCATSNYTGFANKHGSKPSSLGVSNGAEKKSGSPTHQAKVSLQMATSPSNGNILNSVAIQAHQYLDGTWSLSRTNGVTLYPYQISQLMTESSREGLTEAVLNRYNADKPSACSVPASQGSCVASETSTGTSVAASFFARAAQKLNLSSKKKKHRPSTSSAAEPPLFATSFSGILQTSPPPAPPCLLRAVNKVKDTPGLGKVKVMLRICSTLARDTSESSSFLKVDPRKKQITLYDPLTCGGQNAFQKRGNQVPPKMFAFDAVFPQDASQAEVCAGTVAEVIQSVVNGADGCVFCFGHAKLGKSYTMIGKDDSMQNLGIIPCAISWLFKLINERKEKTGARFSVRVSAVEVWGKEENLRDLLSEVATGSLQDGQSPGVYLCEDPICGTQLQNQSELRAPTAEKAAFFLDAAIASRRSHQQDCDEDDHRNSHVFFTLHIYQYRMEKSGKGGMSGGRSRLHLIDLGSCVKALSKNREGGSGLCLSLSALGNVILALVNGSKHIPYKESKLAMLLRESLGNMNCRTTMIAHISAAVGSYAETLSTIQIASRVLRMKKKKTKYTSSSSGGESSCEEGRMRRPTQLRPFHTRATVDPDFPIAHLSSDPDYSSSSEQSCDTVIYIGPNGTALSDKELTDNEGPPDFVPIVPALQKTRGDSRPAEAGEAAAGKSERDCLKCNTFAELQERLDCIDGSEEPSSFPFEELPAQFGPEQASRGPRLSQAAGASPLSESDKEDNGSEGQLTNREGPELPASKMQRSHSPVPAAAPAHSPSPASPRSVPGSSSQHSASPLVQSPSLQSSRESLNSCGFVEGKPRPMGSPRLGIASLSKTSEYKPPSSPSQRCKVYTQKGVLPSPAPLPPSSKDSGVASRESLLQPEVRTPPVGMSPQVLKKSMSAGSEGFPETPVDDEQQAATPSESKKEILSTTMVTVQQPLELNGEDELVFTLVEELTISGVLDSGRPTSIISFNSDCSARALASGSRPVSIISSISEDLECYSSTAPVSEVSITQFLPLPKMSLDEKAQDAGSRRSSISSWLSEMSAGSEGEQSCHSFIAQTCFGHGEAMAEPVASEFVSSLQNTAVVCREKPKASPDNLLILSEMGDDSFNKAAPIKGCKISTVSKAMVTISNTANLSSCEGYIPMKTNITVYPCIAMSPRNIQEPEAPTATPKAGPTLAQSRESKENSAKKEMKFEDPWLKREEEVKKETAHPNEEGMMRCETATGPSNAETRAEQEQDGKPSPGDRLSSSSGEVSASPVTDNFRRVVDGCEMALPGLATQSPVHPNKSVKSSSLPRAFQKASRQEEPDSLSYYCAAETNGVGAASGTPPSKATLEGKVASPKHCVLARPKGTPPLPPVRKSSLDQKNRASPQHSASGSGTSSPLNQPAAFPAGLPDEPSGKTKDASSSSKLFSAKLEQLASRSNSLGRATVSHYECLSLERAESLSSVSSRLHAGKDGTMPRAGRSLGRSAGTSPPSSGASPKAGQSKISAVSRLLLASPRARGPSASTTKTLSFSTKSLPQAVGQGSSSPPGGKHTPWSTQSLSRNRSSGLASKLPLRAVSGRISELLQGGAGARGLQLRAGPEAEARGGALAEDEPAAAHLLPSPYSKITPPRRPHRCSSGHGSDNSSVLSGELPPAMGKTALFYHSGGSSGYESVMRDSEATGSASSAQDSTSENSSSVGGRCRSLKTPKKRSNPGSQRRRLIPALSLDTSSPVRKPPNSTGVRWVDGPLRSSPRGLGEPFEIKVYEIDDVERLQRRRGGASKEAMCFNAKLKILEHRQQRIAEVRAKYEWLMKELEATKQYLMLDPNKWLSEFDLEQVWELDSLEYLEALECVTERLESRVNFCKAHLMMITCFDITSRRR TTQWICZ TT Literature-reported TTQWICZ FM Kinesin-like protein family TTIXBFP ID TTIXBFP TTIXBFP TN Kinetochore protein Nuf2 (NUF2) TTIXBFP UP Q9BZD4 TTIXBFP UC NUF2_HUMAN TTIXBFP SN hsNuf2; hNuf2R; hNuf2; NUF2R; Cell division cycleassociated protein 1; Cell division cycle-associated protein 1; CDCA1 TTIXBFP GN NUF2 TTIXBFP FC Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. TTIXBFP PD 3IZ0; 2VE7 TTIXBFP SQ METLSFPRYNVAEIVIHIRNKILTGADGKNLTKNDLYPNPKPEVLHMIYMRALQIVYGIRLEHFYMMPVNSEVMYPHLMEGFLPFSNLVTHLDSFLPICRVNDFETADILCPKAKRTSRFLSGIINFIHFREACRETYMEFLWQYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQEGNSQKKSNISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYERVTTINQEIQKIKLGIQQLKDAAEREKLKSQEIFLNLKTALEKYHDGIEKAAEDSYAKIDEKTAELKRKMFKMST TTIXBFP TT Literature-reported TTHDS05 ID TTHDS05 TTHDS05 TN Klebsiella Fimbrial subunit type 3 (Klebsiella mrkA) TTHDS05 UP P12267 TTHDS05 UC FM3_KLEPN TTHDS05 GN Klebsiella mrkA TTHDS05 SQ MKKVLLSAAMATAFFGMAAANAADTNVGGGQVNFFGKVTDVSCTVSVNGQGSDANVYLSPVTLTEVKAAAADTYLKPKSFTIDVSDCQAADGTKQDDVSKLGVNWTGGNLLAGATAKQQGYLANTEAAGAQNIQLVLSTDNATALTNKIIPGDSTQPKAAGDASAVQDGARFTYYVGYATSTPTTVTTGVVNSYATYEITYQ TTHDS05 TT Preclinical TT1GLAJ ID TT1GLAJ TT1GLAJ TN Lactadherin (MFGE8) TT1GLAJ UP Q08431 TT1GLAJ UC MFGM_HUMAN TT1GLAJ BC Growth factor TT1GLAJ SN Milk fat globule-EGF factor 8; MFGM; MFGE8; MFG-E8; Human milk fat globule membrane protein BA46; HMFG; Breast epithelial antigen BA46 TT1GLAJ GN MFGE8 TT1GLAJ FC Medin is the main constituent of aortic medial amyloid. TT1GLAJ SQ MPRPRLLAALCGALLCAPSLLVALDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCETKCVEPLGLENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPSSNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFETPILARYVRILPVAWHNRIALRLELLGC TT1GLAJ TT Literature-reported TTBRLU3 ID TTBRLU3 TTBRLU3 TN Lactalbumin alpha (LALBA) TTBRLU3 UP P00709 TTBRLU3 UC LALBA_HUMAN TTBRLU3 SN Lysozyme-like protein 7; Lactose synthase B protein; LYZL7; Alpha-lactalbumin TTBRLU3 GN LALBA TTBRLU3 FC Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins. TTBRLU3 PD 4L41; 3B0O; 3B0I; 1HML; 1CB3 TTBRLU3 SQ MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL TTBRLU3 TT Literature-reported TTNS7H3 ID TTNS7H3 TTNS7H3 TN Laminin gamma-2 subunit (LAMC2) TTNS7H3 UP Q13753 TTNS7H3 UC LAMC2_HUMAN TTNS7H3 SN Nicein subunit gamma; Large adhesive scatter factor 140 kDa subunit; Laminin5 subunit gamma; Laminin-5 subunit gamma; Laminin subunit gamma2; Laminin subunit gamma-2; Laminin B2t chain; Ladsin 140 kDa subunit; LAMNB2; LAMB2T; Kalinin/nicein/epiligrin 100 kDa subunit; Kalinin subunit gamma; Epiligrin subunit gamma; Cellscattering factor 140 kDa subunit; Cell-scattering factor 140 kDa subunit; CSF 140 kDa subunit TTNS7H3 GN LAMC2 TTNS7H3 FC Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells. Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. TTNS7H3 SQ MPALWLGCCLCFSLLLPAARATSRREVCDCNGKSRQCIFDRELHRQTGNGFRCLNCNDNTDGIHCEKCKNGFYRHRERDRCLPCNCNSKGSLSARCDNSGRCSCKPGVTGARCDRCLPGFHMLTDAGCTQDQRLLDSKCDCDPAGIAGPCDAGRCVCKPAVTGERCDRCRSGYYNLDGGNPEGCTQCFCYGHSASCRSSAEYSVHKITSTFHQDVDGWKAVQRNGSPAKLQWSQRHQDVFSSAQRLDPVYFVAPAKFLGNQQVSYGQSLSFDYRVDRGGRHPSAHDVILEGAGLRITAPLMPLGKTLPCGLTKTYTFRLNEHPSNNWSPQLSYFEYRRLLRNLTALRIRATYGEYSTGYIDNVTLISARPVSGAPAPWVEQCICPVGYKGQFCQDCASGYKRDSARLGPFGTCIPCNCQGGGACDPDTGDCYSGDENPDIECADCPIGFYNDPHDPRSCKPCPCHNGFSCSVMPETEEVVCNNCPPGVTGARCELCADGYFGDPFGEHGPVRPCQPCQCNNNVDPSASGNCDRLTGRCLKCIHNTAGIYCDQCKAGYFGDPLAPNPADKCRACNCNPMGSEPVGCRSDGTCVCKPGFGGPNCEHGAFSCPACYNQVKIQMDQFMQQLQRMEALISKAQGGDGVVPDTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDTHRLITQMQLSLAESEASLGNTNIPASDHYVGPNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRKALHEGVGSGSGSPDGAVVQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMDQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ TTNS7H3 TT Literature-reported TTNS7H3 KE hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05200:Pathways in cancer; hsa05222:Small cell lung cancer TTNS7H3 RC R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-2022090:Assembly of collagen fibrils and other multimeric structures; R-HSA-2214320:Anchoring fibril formation; R-HSA-3000157:Laminin interactions; R-HSA-3000171:Non-integrin membrane-ECM interactions TTQRVC9 ID TTQRVC9 TTQRVC9 TN Large ribosomal subunit protein eL15 (RPL15) TTQRVC9 UP P61313 TTQRVC9 UC RL15_HUMAN TTQRVC9 SN TCBAP0781; EC45; 60S ribosomal protein L15 TTQRVC9 GN RPL15 TTQRVC9 FC Up-regulated in gastric cancer tissues. Also highly expressed in gastric cancer cell lines AGS, MKN45, MKN28, SGC7901 and KATOIII. TTQRVC9 PD 6QZP; 6EK0; 5T2C; 5LKS; 5AJ0 TTQRVC9 SQ MGAYKYIQELWRKKQSDVMRFLLRVRCWQYRQLSALHRAPRPTRPDKARRLGYKAKQGYVIYRIRVRRGGRKRPVPKGATYGKPVHHGVNQLKFARSLQSVAEERAGRHCGALRVLNSYWVGEDSTYKFFEVILIDPFHKAIRRNPDTQWITKPVHKHREMRGLTSAGRKSRGLGKGHKFHHTIGGSRRAAWRRRNTLQLHRYR TTQRVC9 TT Literature-reported TTZ840V ID TTZ840V TTZ840V TN Leishmania 65kD membrane-associated NADH-fumarate reductase (Leishm nfr65) TTZ840V UP Q8ITL2 TTZ840V UC Q8ITL2_9TRYP TTZ840V BC CH-CH donor oxidoreductase TTZ840V SN NADH-dependent fumarate reductase TTZ840V GN Leishm nfr65 TTZ840V FC An obligatory component of the respiratory chain of the parasite. Important in the intermediate metabolism in the Leishmania parasite and is absent in mammalian cells. TTZ840V SQ MVDGRSSASIVAVDPERAARERDAAARALLQDSPLHTTMQYATSGLELTVPYALKVVASADTFDRAKEVADEVLRCAWQLADTVLNSFNPNSEVSLVGRLPVGQKHQMSAPLKRVMACCQRVYNSSAGCFDPSTAPVAKALREIALGKERNNACLEALTQACTLPNSFVIDFEAGTISRKHEHASLDLGGVSKGYIVDYVIDNINAAGFQNVFFDWGGDCRASGMNARNTPWVVGITRPPSLDMLPNPPKEASYISVISLDNEALATSGDYENLIYTADDKPLTCTYDWKGKELMKPSQSNIAQVSVKCYSAMYADALATACFIKRDPAKVRQLLDGWRYVRDTVRDYRVYVRENERVAKMFEIATEDAEMRKRRISNTLPARVIVVGGGLAGLSAAIEAAGCGAQVVLMEKEAKLGGNSAKATSGINGWGTRAQAKASIVDGGKYFERDTYKSGIGGNTDPALVKTLSMKSADAIGWLTSLGVPLTVLSQLGGHSRKRTHRAPDKKDGTPLPIGFTIMKTLEDHVRGNLSGRITIMENCSVTSLLSETKERPDGTKQIRVTGVEFTQAGSGKTTILADAVILATGGFSNDKTADSLLREHAPHLVNFPTTNGPWATGDGVKLAQRLGAQLVDMDKVQLHPTGLINPKDPANPTKFLGPEALRGSGGVLLNKQGKRFVNELDLRSVVSKAIMEQGAEYPGSGGSMFAYCVLNAAAQKLFGVSSHEFYWKKMGLFVKADTMRDLAALIGCPVESVQQTLEEYERLSISQRSCPITRKSVYPCVLGTKGPYYVAFVTPSIHYTMGGCLISPSAEIQMKNTSSRAPLSHSNPILGLFGAGEVTGGVHGGNRLGGNSLLECVVFGRIAGDRASTILQRKSSALSFKVWTTVVLREVREGGVYGAGSRVLRFNLPGALQRSGLSLGQFIAIRGDWDGQQLIGYYSPITLPDDLGMIDILARSDKGTLREWISALEPGDAVEMKACGGLVIERRLSDKHFVFMGHIINKLCLIAGGTGVAPMLQIIKAAFMKPFIDTLESVHLIYAAEDVTELTYREVLEERRRESRGKFKKTFVLNRPPPLWTDGVGFIDRGILTNHVQPPSDNLLVAICGPPVMQRIVKATLKTLGYNMNLVRTVDETEPSGSSKI TTZ840V TT Literature-reported TTW3AMG ID TTW3AMG TTW3AMG TN Leishmania Cdc2-related kinase 3 (Leishmania CRK3) TTW3AMG UP O15851 TTW3AMG UC O15851_LEIME TTW3AMG BC Kinase TTW3AMG SN Cdc2-related kinase 3; CRK3 cyclin-dependent kinase; CRK3 TTW3AMG GN Leishmania CRK3 TTW3AMG FC Form an active protein kinase complex with Leishmania cyclins CYCA and CYC6. TTW3AMG SQ MSSFGRVTARSGDAGTRDSLDRYNRLDVLGEGTYGVVYRAVDKITGQYVALKKVRLDRTEEGIPQTALREVSILQEFDHPNIVNLLDVICSDGKLYLVFEYVEADLKKAIEKQEGGYSGMDLKRLIYQLLDGLYFCHRHRIIHRDLKPANILLTSGNVLKLADFGLARAFQVPMHTYTHEVVTLWYRAPEILLGEKHYTPAVDMWSVGCIFAELARRKVLFRGDSEIGQLFEIFQVLGTPTDTEGSWPGVSRLPDYRDVFPKWTAKRLGQVLPELHPDAIDLLSKMLKYDPRERISAKEALQHPWFSDLRW TTW3AMG TT Literature-reported TTT1LHV ID TTT1LHV TTT1LHV TN Leishmania Glutathionylspermidine synthase (Leishm GSP) TTT1LHV UP E9BI04 TTT1LHV UC E9BI04_LEIDB TTT1LHV BC Carbon-nitrogen ligase TTT1LHV SN GspS; Glutathionylspermidine synthetase; Glutathione:spermidine ligase [ADP-forming]; GSP synthetase; GSP TTT1LHV GN Leishm GSP TTT1LHV FC Conjugates glutathione (gamma-Glu-Cys-Gly) and spermidine to form glutathionylspermidine in the biosynthesis trypanothione (N(1),N(8)-bis(glutathionyl)spermidine), which is involved in maintaining intracellular thiol redox and in defense againstoxidants. TTT1LHV SQ MLSLPRDHHYHTHHRGTELVPFDQVIGITPDGVPVISNGNEFHFTNLESVTPFYQALCSFDRKAPVTVSYKKLGVKWQCVEFARRYLASRKAVWTASMPIAADMWRAETPFVRVQDGTPVEFTRIANRSHGPAPAMSDIIVWGQSEETPFGHVAVVTEVLPEAVRVAEQNQGFERWPQGMLYSREIPVQRSSAGTVELVDEDPVLGWVTLHCPYYDFRDGDLADKFRIVTGPGCIVRQPFPKHVELPWLQPEERCDFYLKRSLAIGGNVGDDARAKECDVPSAFYFLDYNIWCRLGRAAHSLHRIAMTATAQVLDDADSAYLLEHYFGLPPEIHPLLRRSWEMMPPMSGRFDFGYDGNKVAMLEYNCDSSGALLECCNTQEKMANYYGVSQGMSTGSFLGAKCVSHFARLMSNEKVCPKHKLIHFMIDDDDEERYTAMCMMNFAEKAGFRTKLCVKLIDFRYRDGAPANAAPLSVTCDHPIIVDSDGDEVLLVWKTWSWDTVLREYHRQCSATDSVSSPTLSDILLNNNICVIEPLWKAVTGSKALLPFMHALAPDHEHLLAADFVPTKDIISHHYVSKPINGRAGQNIMMFDPVTDAAELNAAPQEMLSESSSQLFSIKPPAASCSALQSQSIDRTNECSTGTFFDSAVVYQKRFFLKKFEGKYFPIFCGWMIDDEFGGVVVREDTSKITKLDSIVIPARVVRENVSLGGAYTDEGET TTT1LHV TT Literature-reported TTBJEZ5 ID TTBJEZ5 TTBJEZ5 TN Leptin (LEP) TTBJEZ5 UP P41159 TTBJEZ5 UC LEP_HUMAN TTBJEZ5 SN Obesity factor; Obese protein; LEP TTBJEZ5 GN LEP TTBJEZ5 FC May function as part of a signaling pathway that acts to regulate the size of the body fat depot. An increase in the level of LEP may act directly or indirectly on the CNS to inhibit food intake and/or regulate energy expenditure as part of a homeostatic mechanism to maintain constancy of the adipose mass. TTBJEZ5 PD 1AX8 TTBJEZ5 SQ MHWGTLCGFLWLWPYLFYVQAVPIQKVQDDTKTLIKTIVTRINDISHTQSVSSKQKVTGLDFIPGLHPILTLSKMDQTLAVYQQILTSMPSRNVIQISNDLENLRDLLHVLAFSKSCHLPWASGLETLDSLGGVLEASGYSTEVVALSRLQGSLQDMLWQLDLSPGC TTBJEZ5 TT Literature-reported TTQDMJN ID TTQDMJN TTQDMJN TN Lethal(3)malignant brain tumor-like 3 (L3MBTL3) TTQDMJN UP Q96JM7 TTQDMJN UC LMBL3_HUMAN TTQDMJN SN MBT1; MBT-1; Lethal(3)malignant brain tumor-like protein 3; L(3)mbt-like protein 3; KIAA1798; H-l(3)mbt-like protein 3 TTQDMJN GN L3MBTL3 TTQDMJN FC Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Required for normal maturation of myeloid progenitor cells (By similarity). TTQDMJN PD 4L59; 4FL6; 3UT1; 1WJS; 1WJQ TTQDMJN SQ MTESASSTSGQEFDVFSVMDWKDGVGTLPGSDLKFRVNEFGALEVITDENEMENVKKATATTTWMVPTAQEAPTSPPSSRPVFPPAYWTSPPGCPTVFSEKTGMPFRLKDPVKVEGLQFCENCCQYGNVDECLSGGNYCSQNCARHIKDKDQKEERDVEEDNEEEDPKCSRKKKPKLSLKADTKEDGEERDDEMENKQDVRILRGSQRARRKRRGDSAVLKQGLPPKGKKAWCWASYLEEEKAVAVPAKLFKEHQSFPYNKNGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKGYKEEEFNWQTYLKTCKAQAAPKSLFENQNITVIPSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPNVKHFSWDKYLEETNSLPAPARAFKVKPPHGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPPLSPLELMEASEHGGCSTPGCKGIGHFKRARHLGPHSAANCPYSEINLNKDRIFPDRLSGEMPPASPSFPRNKRTDANESSSSPEIRDQHADDVKEDFEERTESEMRTSHEARGAREEPTVQQAQRRSAVFLSFKSPIPCLPLRWEQQSKLLPTVAGIPASKVSKWSTDEVSEFIQSLPGCEEHGKVFKDEQIDGEAFLLMTQTDIVKIMSIKLGPALKIFNSILMFKAAEKNSHNEL TTQDMJN TT Literature-reported TTGZ5WN ID TTGZ5WN TTGZ5WN TN Leukemia inhibitory factor (LIF) TTGZ5WN UP P15018 TTGZ5WN UC LIF_HUMAN TTGZ5WN SN Melanoma-derived LPL inhibitor; MLPLI; HILDA; Emfilermin; Differentiation-stimulating factor; D factor TTGZ5WN GN LIF TTGZ5WN FC Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes. LIF has the capacity to induce terminal differentiation in leukemic cells. TTGZ5WN PD 2Q7N; 1PVH; 1EMR TTGZ5WN SQ MKVLAAGVVPLLLVLHWKHGAGSPLPITPVNATCAIRHPCHNNLMNQIRSQLAQLNGSANALFILYYTAQGEPFPNNLDKLCGPNVTDFPPFHANGTEKAKLVELYRIVVYLGTSLGNITRDQKILNPSALSLHSKLNATADILRGLLSNVLCRLCSKYHVGHVDVTYGPDTSGKDVFQKKKLGCQLLGKYKQIIAVLAQAF TTGZ5WN TT Clinical trial TTZEIBV ID TTZEIBV TTZEIBV TN Leukocyte antigen MIC3 (CD9) TTZEIBV UP P21926 TTZEIBV UC CD9_HUMAN TTZEIBV BC Tetraspanin TTZEIBV SN p24; Tspan29; Tspan-29; Tetraspanin29; Tetraspanin-29; Motilityrelated protein; Motility-related protein; MRP-1; MIC3; GIG2; Cell growthinhibiting gene 2 protein; Cell growth-inhibiting gene 2 protein; CD9 antigen; 5H9 antigen TTZEIBV GN CD9 TTZEIBV FC Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis. Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. TTZEIBV SQ MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV TTZEIBV TT Literature-reported TTZEIBV FM Tetraspanin family TTZJA87 ID TTZJA87 TTZJA87 TN LIM and SH3 domain protein 1 (LASP1) TTZJA87 UP Q14847 TTZJA87 UC LASP1_HUMAN TTZJA87 SN Metastatic lymph node gene 50 protein; MLN50; MLN 50; LASP-1 TTZJA87 GN LASP1 TTZJA87 FC Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types. TTZJA87 PD 3I35 TTZJA87 SQ MNPNCARCGKIVYPTEKVNCLDKFWHKACFHCETCKMTLNMKNYKGYEKKPYCNAHYPKQSFTMVADTPENLRLKQQSELQSQVRYKEEFEKNKGKGFSVVADTPELQRIKKTQDQISNIKYHEEFEKSRMGPSGGEGMEPERRDSQDGSSYRRPLEQQQPHHIPTSAPVYQQPQQQPVAQSYGGYKEPAAPVSIQRSAPGGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGMLPANYVEAI TTZJA87 TT Literature-reported TT5D314 ID TT5D314 TT5D314 TN Lipophilin-B (SCGB1D2) TT5D314 UP O95969 TT5D314 UC SG1D2_HUMAN TT5D314 BC Secretoglobin family TT5D314 SN Secretoglobin family 1D member 2; SCGB1D2 TT5D314 GN SCGB1D2 TT5D314 FC May bind androgens and other steroids, may also bind estramustine, a chemotherapeutic agent used for prostate cancer. May be under transcriptional regulation of steroid hormones. TT5D314 SQ MKLSVCLLLVTLALCCYQANAEFCPALVSELLDFFFISEPLFKLSLAKFDAPPEAVAAKLGVKRCTDQMSLQKRSLIAEVLVKILKKCSV TT5D314 TT Literature-reported TTVQJLY ID TTVQJLY TTVQJLY TN Lipopolysaccharide-binding protein (LBP) TTVQJLY UP P18428 TTVQJLY UC LBP_HUMAN TTVQJLY BC Bactericidal permeability increasing protein TTVQJLY SN LBP TTVQJLY GN LBP TTVQJLY FC Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. Acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide. TTVQJLY SQ MGALARALPSILLALLLTSTPEALGANPGLVARITDKGLQYAAQEGLLALQSELLRITLPDFTGDLRIPHVGRGRYEFHSLNIHSCELLHSALRPVPGQGLSLSISDSSIRVQGRWKVRKSFFKLQGSFDVSVKGISISVNLLLGSESSGRPTVTASSCSSDIADVEVDMSGDLGWLLNLFHNQIESKFQKVLESRICEMIQKSVSSDLQPYLQTLPVTTEIDSFADIDYSLVEAPRATAQMLEVMFKGEIFHRNHRSPVTLLAAVMSLPEEHNKMVYFAISDYVFNTASLVYHEEGYLNFSITDDMIPPDSNIRLTTKSFRPFVPRLARLYPNMNLELQGSVPSAPLLNFSPGNLSVDPYMEIDAFVLLPSSSKEPVFRLSVATNVSATLTFNTSKITGFLKPGKVKVELKESKVGLFNAELLEALLNYYILNTFYPKFNDKLAEGFPLPLLKRVQLYDLGLQIHKDFLFLGANVQYMRV TTVQJLY TT Literature-reported TTFGXEB ID TTFGXEB TTFGXEB TN Liver organic anion transporter 1 (SLCO1B1) TTFGXEB UP Q9Y6L6 TTFGXEB UC SO1B1_HUMAN TTFGXEB BC Organo anion transporter TTFGXEB SN Solute carrier organic anion transporter family member 1B1; Solute carrier family 21 member 6; Sodium-independent organic anion-transporting polypeptide 2; SLC21A6; OATPC; OATP2; OATP-C; OATP-2; Liver-specific organic anion transporter 1; LST1; LST-1 TTFGXEB GN SLCO1B1 TTFGXEB FC Involved in the clearance of bile acids and organic anions from the liver. Mediates the Na(+)-independent uptake of organic anions such as pravastatin, taurocholate, methotrexate, dehydroepiandrosterone sulfate, 17-beta-glucuronosyl estradiol, estrone sulfate, prostaglandin E2, thromboxane B2, leukotriene C3, leukotriene E4, thyroxine and triiodothyronine. TTFGXEB SQ MDQNQHLNKTAEAQPSENKKTRYCNGLKMFLAALSLSFIAKTLGAIIMKSSIIHIERRFEISSSLVGFIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGGVLTALPHFFMGYYRYSKETNINSSENSTSTLSTCLINQILSLNRASPEIVGKGCLKESGSYMWIYVFMGNMLRGIGETPIVPLGLSYIDDFAKEGHSSLYLGILNAIAMIGPIIGFTLGSLFSKMYVDIGYVDLSTIRITPTDSRWVGAWWLNFLVSGLFSIISSIPFFFLPQTPNKPQKERKASLSLHVLETNDEKDQTANLTNQGKNITKNVTGFFQSFKSILTNPLYVMFVLLTLLQVSSYIGAFTYVFKYVEQQYGQPSSKANILLGVITIPIFASGMFLGGYIIKKFKLNTVGIAKFSCFTAVMSLSFYLLYFFILCENKSVAGLTMTYDGNNPVTSHRDVPLSYCNSDCNCDESQWEPVCGNNGITYISPCLAGCKSSSGNKKPIVFYNCSCLEVTGLQNRNYSAHLGECPRDDACTRKFYFFVAIQVLNLFFSALGGTSHVMLIVKIVQPELKSLALGFHSMVIRALGGILAPIYFGALIDTTCIKWSTNNCGTRGSCRTYNSTSFSRVYLGLSSMLRVSSLVLYIILIYAMKKKYQEKDINASENGSVMDEANLESLNKNKHFVPSAGADSETHC TTFGXEB TT Literature-reported TTAZHU0 ID TTAZHU0 TTAZHU0 TN L-lactate dehydrogenase (LDH) TTAZHU0 UP P00338; P07195; P07864 TTAZHU0 UC LDHA_HUMAN; LDHB_HUMAN; LDHC_HUMAN TTAZHU0 BC Short-chain dehydrogenases reductase TTAZHU0 SN Renal carcinoma antigen NY-REN; LDH TTAZHU0 GN LDHA; LDHB; LDHC TTAZHU0 FC Catalyzes the conversion of lactate to pyruvate and back, as it converts NAD+ to NADH and back. Expressed extensively in body tissues, such as blood cells and heart muscle. Functions asa marker of common injuries and disease such as heart failure because it is released during tissue damage TTAZHU0 SQ MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF TTAZHU0 TT Literature-reported TTTDAI9 ID TTTDAI9 TTTDAI9 TN Long transient receptor potential channel 1 (TRPM1) TTTDAI9 UP Q7Z4N2 TTTDAI9 UC TRPM1_HUMAN TTTDAI9 BC Transient receptor potential catioin channel TTTDAI9 SN Transient receptor potential cation channel subfamily M member 1; Melastatin-1; MLSN; LTRPC1 TTTDAI9 GN TRPM1 TTTDAI9 FC Cation channel essential for the depolarizing photoresponse of retinal ON bipolar cells. It is part of the GRM6 signaling cascade. May play a role in metastasis suppression (By similarity). May act as a spontaneously active, calcium-permeable plasma membrane channel. TTTDAI9 SQ MKDSNRCCCGQFTNQHIPPLPSATPSKNEEESKQVETQPEKWSVAKHTQSYPTDSYGVLEFQGGGYSNKAMYIRVSYDTKPDSLLHLMVKDWQLELPKLLISVHGGLQNFEMQPKLKQVFGKGLIKAAMTTGAWIFTGGVSTGVISHVGDALKDHSSKSRGRVCAIGIAPWGIVENKEDLVGKDVTRVYQTMSNPLSKLSVLNNSHTHFILADNGTLGKYGAEVKLRRLLEKHISLQKINTRLGQGVPLVGLVVEGGPNVVSIVLEYLQEEPPIPVVICDGSGRASDILSFAHKYCEEGGIINESLREQLLVTIQKTFNYNKAQSHQLFAIIMECMKKKELVTVFRMGSEGQQDIEMAILTALLKGTNVSAPDQLSLALAWNRVDIARSQIFVFGPHWPPLGSLAPPTDSKATEKEKKPPMATTKGGRGKGKGKKKGKVKEEVEEETDPRKIELLNWVNALEQAMLDALVLDRVDFVKLLIENGVNMQHFLTIPRLEELYNTRLGPPNTLHLLVRDVKKSNLPPDYHISLIDIGLVLEYLMGGAYRCNYTRKNFRTLYNNLFGPKRPKALKLLGMEDDEPPAKGKKKKKKKKEEEIDIDVDDPAVSRFQYPFHELMVWAVLMKRQKMAVFLWQRGEESMAKALVACKLYKAMAHESSESDLVDDISQDLDNNSKDFGQLALELLDQSYKHDEQIAMKLLTYELKNWSNSTCLKLAVAAKHRDFIAHTCSQMLLTDMWMGRLRMRKNPGLKVIMGILLPPTILFLEFRTYDDFSYQTSKENEDGKEKEEENTDANADAGSRKGDEENEHKKQRSIPIGTKICEFYNAPIVKFWFYTISYLGYLLLFNYVILVRMDGWPSLQEWIVISYIVSLALEKIREILMSEPGKLSQKIKVWLQEYWNITDLVAISTFMIGAILRLQNQPYMGYGRVIYCVDIIFWYIRVLDIFGVNKYLGPYVMMIGKMMIDMLYFVVIMLVVLMSFGVARQAILHPEEKPSWKLARNIFYMPYWMIYGEVFADQIDLYAMEINPPCGENLYDEEGKRLPPCIPGAWLTPALMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIMTFHDRPVLPPPMIILSHIYIIIMRLSGRCRKKREGDQEERDRGLKLFLSDEELKRLHEFEEQCVQEHFREKEDEQQSSSDERIRVTSERVENMSMRLEEINERETFMKTSLQTVDLRLAQLEELSNRMVNALENLAGIDRSDLIQARSRASSECEATYLLRQSSINSADGYSLYRYHFNGEELLFEDTSLSTSPGTGVRKKTCSFRIKEEKDVKTHLVPECQNSLHLSLGTSTSATPDGSHLAVDDLKNAEESKLGPDIGISKEDDERQTDSKKEETISPSLNKTDVIHGQDKSDVQNTQLTVETTNIEGTISYPLEETKITRYFPDETINACKTMKSRSFVYSRGRKLVGGVNQDVEYSSITDQQLTTEWQCQVQKITRSHSTDIPYIVSEAAVQAEHKEQFADMQDEHHVAEAIPRIPRLSLTITDRNGMENLLSVKPDQTLGFPSLRSKSLHGHPRNVKSIQGKLDRSGHASSVSSLVIVSGMTAEEKKVKKEKASTETEC TTTDAI9 TT Literature-reported TTO3TD8 ID TTO3TD8 TTO3TD8 TN Long transient receptor potential channel 3 (TRPM3) TTO3TD8 UP Q9HCF6 TTO3TD8 UC TRPM3_HUMAN TTO3TD8 BC Transient receptor potential catioin channel TTO3TD8 SN Transient receptor potential cation channel subfamily M member 3; Melastatin-2; MLSN2; LTrpC3; LTrpC-3; KIAA1616 TTO3TD8 GN TRPM3 TTO3TD8 FC Its activity is increased by reduction in extracellular osmolarity, by store depletion and muscarinic receptor activation. Calcium channel mediating constitutive calcium ion entry. TTO3TD8 SQ MPEPWGTVYFLGIAQVFSFLFSWWNLEGVMNQADAPRPLNWTIRKLCHAAFLPSVRLLKAQKSWIERAFYKRECVHIIPSTKDPHRCCCGRLIGQHVGLTPSISVLQNEKNESRLSRNDIQSEKWSISKHTQLSPTDAFGTIEFQGGGHSNKAMYVRVSFDTKPDLLLHLMTKEWQLELPKLLISVHGGLQNFELQPKLKQVFGKGLIKAAMTTGAWIFTGGVNTGVIRHVGDALKDHASKSRGKICTIGIAPWGIVENQEDLIGRDVVRPYQTMSNPMSKLTVLNSMHSHFILADNGTTGKYGAEVKLRRQLEKHISLQKINTRCLPFFSLDSRLFYSFWGSCQLDSVGIGQGVPVVALIVEGGPNVISIVLEYLRDTPPVPVVVCDGSGRASDILAFGHKYSEEGGLINESLRDQLLVTIQKTFTYTRTQAQHLFIILMECMKKKELITVFRMGSEGHQDIDLAILTALLKGANASAPDQLSLALAWNRVDIARSQIFIYGQQWPVGSLEQAMLDALVLDRVDFVKLLIENGVSMHRFLTISRLEELYNTRHGPSNTLYHLVRDVKKGNLPPDYRISLIDIGLVIEYLMGGAYRCNYTRKRFRTLYHNLFGPKRPKALKLLGMEDDIPLRRGRKTTKKREEEVDIDLDDPEINHFPFPFHELMVWAVLMKRQKMALFFWQHGEEAMAKALVACKLCKAMAHEASENDMVDDISQELNHNSRDFGQLAVELLDQSYKQDEQLAMKLLTYELKNWSNATCLQLAVAAKHRDFIAHTCSQMLLTDMWMGRLRMRKNSGLKVILGILLPPSILSLEFKNKDDMPYMSQAQEIHLQEKEAEEPEKPTKEKEEEDMELTAMLGRNNGESSRKKDEEEVQSKHRLIPLGRKIYEFYNAPIVKFWFYTLAYIGYLMLFNYIVLVKMERWPSTQEWIVISYIFTLGIEKMREILMSEPGKLLQKVKVWLQEYWNVTDLIAILLFSVGMILRLQDQPFRSDGRVIYCVNIIYWYIRLLDIFGVNKYLGPYVMMIGKMMIDMMYFVIIMLVVLMSFGVARQAILFPNEEPSWKLAKNIFYMPYWMIYGEVFADQIDPPCGQNETREDGKIIQLPPCKTGAWIVPAIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIMTFHERPVLPPPLIIFSHMTMIFQHLCCRWRKHESDPDERDYGLKLFITDDELKKVHDFEEQCIEEYFREKDDRFNSSNDERIRVTSERVENMSMRLEEVNEREHSMKASLQTVDIRLAQLEDLIGRMATALERLTGLERAESNKIRSRTSSDCTDAAYIVRQSSFNSQEGNTFKLQESIDPAGEETMSPTSPTLMPRMRSHSFYSVNMKDKGGIEKLESIFKERSLSLHRATSSHSVAKEPKAPAAPANTLAIVPDSRRPSSCIDIYVSAMDELHCDIDPLDNSVNILGLGEPSFSTPVPSTAPSSSAYATLAPTDRPPSRSIDFEDITSMDTRSFSSDYTHLPECQNPWDSEPPMYHTIERSKSSRYLATTPFLLEEAPIVKSHSFMFSPSRSYYANFGVPVKTAEYTSITDCIDTRCVNAPQAIADRAAFPGGLGDKVEDLTCCHPEREAELSHPSSDSEENEAKGRRATIAISSQEGDNSERTLSNNITVPKIERANSYSAEEPSAPYAHTRKSFSISDKLDRQRNTASLRNPFQRSKSSKPEGRGDSLSMRRLSRTSAFQSFESKHN TTO3TD8 TT Literature-reported TT1N8F3 ID TT1N8F3 TT1N8F3 TN Long transient receptor potential channel 5 (TRPM5) TT1N8F3 UP Q9NZQ8 TT1N8F3 UC TRPM5_HUMAN TT1N8F3 BC Transient receptor potential catioin channel TT1N8F3 SN Transient receptor potential cation channelsubfamily M member 5; TRPM5; MLSN1- and TRP-related gene 1 protein; LTrpC5; LTrpC-5 TT1N8F3 GN TRPM5 TT1N8F3 FC Voltage-modulated Ca(2+)-activated, monovalent cation channel (VCAM) that mediates a transient membrane depolarization and plays a central role in taste transduction. Monovalent- specific, non-selective cation channel that mediates the transport of Na(+), K(+) and Cs(+) ions equally well. Activated directly by increases in intracellular Ca(2+), but is impermeable to it. Gating is voltage-dependent and displays rapid activation and deactivation kinetics upon channel stimulation even during sustained elevations in Ca(2+). Also activated by a fast intracellular Ca(2+) increase in response to inositol 1,4,5- triphosphate-producing receptoragonists. The channel is blocked by extracellular acidification. External acidification has 2 effects, a fast reversible block of the current and a slower irreversible enhancement of current inactivation. Is a highly temperature-sensitive, heat activated channel showing a steep increase of inward currents at temperatures between 15 and 35 degrees Celsius. Heat activation is due to a shift of the voltage- dependent activation curve to negative potentials. Activated by arachidonic acid in vitro. May be involved in perception of bitter, sweet and umami tastes. May also be involved in sensing semiochemicals. TT1N8F3 SQ MQDVQGPRPGSPGDAEDRRELGLHRGEVNFGGSGKKRGKFVRVPSGVAPSVLFDLLLAEWHLPAPNLVVSLVGEEQPFAMKSWLRDVLRKGLVKAAQSTGAWILTSALRVGLARHVGQAVRDHSLASTSTKVRVVAVGMASLGRVLHRRILEEAQEDFPVHYPEDDGGSQGPLCSLDSNLSHFILVEPGPPGKGDGLTELRLRLEKHISEQRAGYGGTGSIEIPVLCLLVNGDPNTLERISRAVEQAAPWLILVGSGGIADVLAALVNQPHLLVPKVAEKQFKEKFPSKHFSWEDIVRWTKLLQNITSHQHLLTVYDFEQEGSEELDTVILKALVKACKSHSQEPQDYLDELKLAVAWDRVDIAKSEIFNGDVEWKSCDLEEVMVDALVSNKPEFVRLFVDNGADVADFLTYGRLQELYRSVSRKSLLFDLLQRKQEEARLTLAGLGTQQAREPPAGPPAFSLHEVSRVLKDFLQDACRGFYQDGRPGDRRRAEKGPAKRPTGQKWLLDLNQKSENPWRDLFLWAVLQNRHEMATYFWAMGQEGVAAALAACKILKEMSHLETEAEAARATREAKYERLALDLFSECYSNSEARAFALLVRRNRCWSKTTCLHLATEADAKAFFAHDGVQAFLTRIWWGDMAAGTPILRLLGAFLCPALVYTNLITFSEEAPLRTGLEDLQDLDSLDTEKSPLYGLQSRVEELVEAPRAQGDRGPRAVFLLTRWRKFWGAPVTVFLGNVVMYFAFLFLFTYVLLVDFRPPPQGPSGPEVTLYFWVFTLVLEEIRQGFFTDEDTHLVKKFTLYVGDNWNKCDMVAIFLFIVGVTCRMLPSAFEAGRTVLAMDFMVFTLRLIHIFAIHKQLGPKIIVVERMMKDVFFFLFFLSVWLVAYGVTTQALLHPHDGRLEWIFRRVLYRPYLQIFGQIPLDEIDEARVNCSTHPLLLEDSPSCPSLYANWLVILLLVTFLLVTNVLLMNLLIAMFSYTFQVVQGNADMFWKFQRYNLIVEYHERPALAPPFILLSHLSLTLRRVFKKEAEHKREHLERDLPDPLDQKVVTWETVQKENFLSKMEKRRRDSEGEVLRKTAHRVDFIAKYLGGLREQEKRIKCLESQINYCSVLVSSVADVLAQGGGPRSSQHCGEGSQLVAADHRGGLDGWEQPGAGQPPSDT TT1N8F3 TT Literature-reported TTGLMU7 ID TTGLMU7 TTGLMU7 TN Lung surfactant protein D (SFTPD) TTGLMU7 UP P35247 TTGLMU7 UC SFTPD_HUMAN TTGLMU7 SN SP-D; SFTP4; Pulmonary surfactant-associated protein D; PSPD; PSP-D; Collectin-7; COLEC7 TTGLMU7 GN SFTPD TTGLMU7 FC Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties. TTGLMU7 PD 5OXS; 5OXR; 4M18; 4M17; 4.00E+52 TTGLMU7 SQ MLLFLLSALVLLTQPLGYLEAEMKTYSHRTMPSACTLVMCSSVESGLPGRDGRDGREGPRGEKGDPGLPGAAGQAGMPGQAGPVGPKGDNGSVGEPGPKGDTGPSGPPGPPGVPGPAGREGPLGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSAGARGLAGPKGERGVPGERGVPGNTGAAGSAGAMGPQGSPGARGPPGLKGDKGIPGDKGAKGESGLPDVASLRQQVEALQGQVQHLQAAFSQYKKVELFPNGQSVGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVCEF TTGLMU7 TT Literature-reported TTG180Q ID TTG180Q TTG180Q TN Lymphocyte antigen 75 (LY75) TTG180Q UP O60449 TTG180Q UC LY75_HUMAN TTG180Q BC C-type lectin TTG180Q SN gp200MR6; Ly75; DEC205; Ctype lectin domain family 13 member B; CD205 TTG180Q GN LY75 TTG180Q FC Acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen- processing compartment. Causes reduced proliferation of B-lymphocytes. TTG180Q SQ MRTGWATPRRPAGLLMLLFWFFDLAEPSGRAANDPFTIVHGNTGKCIKPVYGWIVADDCDETEDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDSSAMLWWKCEHHSLYGAARYRLALKDGHGTAISNASDVWKKGGSEESLCDQPYHEIYTRDGNSYGRPCEFPFLIDGTWHHDCILDEDHSGPWCATTLNYEYDRKWGICLKPENGCEDNWEKNEQFGSCYQFNTQTALSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGIAKIFWIGLNQLYSARGWEWSDHKPLNFLNWDPDRPSAPTIGGSSCARMDAESGLWQSFSCEAQLPYVCRKPLNNTVELTDVWTYSDTRCDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDIKEEVWIGLKNINIPTLFQWSDGTEVTLTYWDENEPNVPYNKTPNCVSYLGELGQWKVQSCEEKLKYVCKRKGEKLNDASSDKMCPPDEGWKRHGETCYKIYEDEVPFGTNCNLTITSRFEQEYLNDLMKKYDKSLRKYFWTGLRDVDSCGEYNWATVGGRRRAVTFSNWNFLEPASPGGCVAMSTGKSVGKWEVKDCRSFKALSICKKMSGPLGPEEASPKPDDPCPEGWQSFPASLSCYKVFHAERIVRKRNWEEAERFCQALGAHLSSFSHVDEIKEFLHFLTDQFSGQHWLWIGLNKRSPDLQGSWQWSDRTPVSTIIMPNEFQQDYDIRDCAAVKVFHRPWRRGWHFYDDREFIYLRPFACDTKLEWVCQIPKGRTPKTPDWYNPDRAGIHGPPLIIEGSEYWFVADLHLNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANISGDGQKWWIRISEWPIDDHFTYSRYPWHRFPVTFGEECLYMSAKTWLIDLGKPTDCSTKLPFICEKYNVSSLEKYSPDSAAKVQCSEQWIPFQNKCFLKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEATLWIGLRWTAYEKINKWTDNRELTYSNFHPLLVSGRLRIPENFFEEESRYHCALILNLQKSPFTGTWNFTSCSERHFVSLCQKYSEVKSRQTLQNASETVKYLNNLYKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSSLWIGLFSQDDELNFGWSDGKRLHFSRWAETNGQLEDCVVLDTDGFWKTVDCNDNQPGAICYYSGNETEKEVKPVDSVKCPSPVLNTPWIPFQNCCYNFIITKNRHMATTQDEVHTKCQKLNPKSHILSIRDEKENNFVLEQLLYFNYMASWVMLGITYRNKSLMWFDKTPLSYTHWRAGRPTIKNEKFLAGLSTDGFWDIQTFKVIEEAVYFHQHSILACKIEMVDYKEEYNTTLPQFMPYEDGIYSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFPLWVGLSSHDGSESSFEWSDGSTFDYIPWKGQTSPGNCVLLDPKGTWKHEKCNSVKDGAICYKPTKSKKLSRLTYSSRCPAAKENGSRWIQYKGHCYKSDQALHSFSEAKKLCSKHDHSATIVSIKDEDENKFVSRLMRENNNITMRVWLGLSQHSVDQSWSWLDGSEVTFVKWENKSKSGVGRCSMLIASNETWKKVECEHGFGRVVCKVPLGPDYTAIAIIVATLSILVLMGGLIWFLFQRHRLHLAGFSSVRYAQGVNEDEIMLPSFHD TTG180Q TT Clinical trial TTC214J ID TTC214J TTC214J TN Lysosome-associated membrane glycoprotein 1 (CD107a) TTC214J UP P11279 TTC214J UC LAMP1_HUMAN TTC214J BC Lysosomal protein import TTC214J SN Lysosomeassociated membrane protein 1; Lysosomeassociated membrane glycoprotein 1; Lysosome-associated membrane protein 1; LAMP-1; CD107 antigenlike family member A; CD107 antigen-like family member A TTC214J GN LAMP1 TTC214J FC Implicated in tumor cell metastasis. Presents carbohydrate ligands to selectins. TTC214J SQ MAAPGSARRPLLLLLLLLLLGLMHCASAAMFMVKNGNGTACIMANFSAAFSVNYDTKSGPKNMTFDLPSDATVVLNRSSCGKENTSDPSLVIAFGRGHTLTLNFTRNATRYSVQLMSFVYNLSDTHLFPNASSKEIKTVESITDIRADIDKKYRCVSGTQVHMNNVTVTLHDATIQAYLSNSSFSRGETRCEQDRPSPTTAPPAPPSPSPSPVPKSPSVDKYNVSGTNGTCLLASMGLQLNLTYERKDNTTVTRLLNINPNKTSASGSCGAHLVTLELHSEGTTVLLFQFGMNASSSRFFLQGIQLNTILPDARDPAFKAANGSLRALQATVGNSYKCNAEEHVRVTKAFSVNIFKVWVQAFKVEGGQFGSVEECLLDENSMLIPIAVGGALAGLVLIVLIAYLVGRKRSHAGYQTI TTC214J TT Literature-reported TTC214J FM Lysosomal protein import TT84HCW ID TT84HCW TT84HCW TN M1-specific T cell receptor beta chain (TRB) TT84HCW UP P0DSE2 TT84HCW UC TRBR1_HUMAN TT84HCW SN TR beta chain TRBV19*01J2S7*01C*02 TT84HCW GN TRB TT84HCW FC The beta chain of TRAV27*01J42*01C*01/TRBV19*01J2S7*01C*02 alpha-beta T cell receptor (TR) clonotype that is specific for HLA-A*02:01-restricted M/matrix protein 1 immunodominant epitope GILGFVFTL of influenza A virus (IAV). Classified as a public TCR clonotype, it is preferentially selected in effector memory CD8-positive T cells among multiple HLA-A*02:01 carriers/individuals and confers long-lived immunity against IAV infection. Can cross-recognize sporadically emerging IAV variants by molecular mimicry, inducing immunity toward different influenza strains. Antigen recognition initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell differentiation into effector/memory T cells (By similarity). TT84HCW PD 5HHO; 5HHM; 2VLR; 2VLK; 2VLJ TT84HCW SQ MSNQVLCCVVLCLLGANTVDGGITQSPKYLFRKEGQNVTLSCEQNLNHDAMYWYRQDPGQGLRLIYYSQIVNDFQKGDIAEGYSVSREKKESFPLTVTSAQKNPTAFYLCASSIRSSYEQYFGPGTRLTVTEDLKNVFPPKVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRADCGFTSESYQQGVLSATILYEILLGKATLYAVLVSALVLMAMVKRKDSRG TT84HCW TT Literature-reported TTBTWI1 ID TTBTWI1 TTBTWI1 TN Macrophage-derived chemokine (MDC) TTBTWI1 UP O00626 TTBTWI1 UC CCL22_HUMAN TTBTWI1 BC Cytokine: CC chemokine TTBTWI1 SN Stimulated T-cell chemotactic protein 1; Stimulated T cell chemotactic protein1; Small-inducible cytokine A22; SCYA22; MDC(1-69); CC chemokine STCP-1; C-C motif chemokine 22; A-152E5.1 TTBTWI1 GN CCL22 TTBTWI1 FC Chemotactic for monocytes, dendritic cells and natural killer cells. Mild chemoattractant for primary activated T-lymphocytes and a potent chemoattractant for chronically activated T-lymphocytes but has no chemoattractant activity for neutrophils, eosinophils, and resting T-lymphocytes. Binds to CCR4. Processed forms MDC(3-69), MDC(5-69) and MDC(7-69) seem not be active. May play a role in the trafficking of activated/effector T-lymphocytes to inflammatory sites and other aspects of activated T-lymphocyte physiology. TTBTWI1 SQ MDRLQTALLVVLVLLAVALQATEAGPYGANMEDSVCCRDYVRYRLPLRVVKHFYWTSDSCPRPGVVLLTFRDKEICADPRVPWVKMILNKLSQ TTBTWI1 TT Literature-reported TTBTWI1 FM Cytokine: intecrine/chemokine TTY5F9C ID TTY5F9C TTY5F9C TN Major prion protein (PRNP) TTY5F9C UP P04156 TTY5F9C UC PRIO_HUMAN TTY5F9C SN Prion protein PrP(C); Prion protein; PrP33-35C; PrP27-30; PrP; PRNP; CD230 antigen; ASCR TTY5F9C GN PRNP TTY5F9C FC The physiological function of prp is not known. TTY5F9C PD 5YJ5; 5YJ4; 5L6R; 4N9O; 4KML TTY5F9C SQ MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG TTY5F9C TT Literature-reported TT1W3RE ID TT1W3RE TT1W3RE TN Mammaglobin A (SCGB2A2) TT1W3RE UP Q13296 TT1W3RE UC SG2A2_HUMAN TT1W3RE BC Secretoglobin family TT1W3RE SN UGB2; Secretoglobin family 2A member 2; Mammaglobin-A; Mammaglobin-1; MGB1 TT1W3RE GN SCGB2A2 TT1W3RE FC Expressed mainly in mucosa. Involved in cell signalling, immune response, and chemotaxis, and may also serve as transporters for steroid hormones in humans. TT1W3RE SQ MKLLMVLMLAALSQHCYAGSGCPLLENVISKTINPQVSKTEYKELLQEFIDDNATTNAIDELKECFLNQTDETLSNVEVFMQLIYDSSLCDLF TT1W3RE TT Literature-reported TTMQDZ5 ID TTMQDZ5 TTMQDZ5 TN Mannose binding protein (MBL2) TTMQDZ5 UP P11226 TTMQDZ5 UC MBL2_HUMAN TTMQDZ5 SN Mannosebinding protein C; Mannosebinding lectin; Mannanbinding protein; MBPC; MBP1; MBL2; Collectin1 TTMQDZ5 GN MBL2 TTMQDZ5 FC Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages. May bind DNA. {ECO:0000269|PubMed:14515269}. TTMQDZ5 PD 1HUP TTMQDZ5 SQ MSLFPSLPLLLLSMVAASYSETVTCEDAQKTCPAVIACSSPGINGFPGKDGRDGTKGEKGEPGQGLRGLQGPPGKLGPPGNPGPSGSPGPKGQKGDPGKSPDGDSSLAASERKALQTEMARIKKWLTFSLGKQVGNKFFLTNGEIMTFEKVKALCVKFQASVATPRNAAENGAIQNLIKEEAFLGITDEKTEGQFVDLTGNRLTYTNWNEGEPNNAGSDEDCVLLLKNGQWNDVPCSTSHLAVCEFPI TTMQDZ5 TT Literature-reported TTDJ51N ID TTDJ51N TTDJ51N TN Mast cell growth factor (MGF) TTDJ51N UP P21583 TTDJ51N UC SCF_HUMAN TTDJ51N SN sKITLG; cKit ligand; c-Kit ligand; Stem cell factor; Soluble KIT ligand; SCF; Kit ligand TTDJ51N GN KITLG TTDJ51N FC Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins. Ligand for the receptor-type protein-tyrosine kinase KIT. TTDJ51N PD 2E9W; 1SCF; 1EXZ TTDJ51N SQ MKKTQTWILTCIYLQLLLFNPLVKTEGICRNRVTNNVKDVTKLVANLPKDYMITLKYVPGMDVLPSHCWISEMVVQLSDSLTDLLDKFSNISEGLSNYSIIDKLVNIVDDLVECVKENSSKDLKKSFKSPEPRLFTPEEFFRIFNRSIDAFKDFVVASETSDCVVSSTLSPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKAKNPPGDSSLHWAAMALPALFSLIIGFAFGALYWKKRQPSLTRAVENIQINEEDNEISMLQEKEREFQEV TTDJ51N TT Literature-reported TT5HNVS ID TT5HNVS TT5HNVS TN Melanoma derived growth regulator (MIA) TT5HNVS UP Q16674 TT5HNVS UC MIA_HUMAN TT5HNVS SN Melanoma-derived growth regulatory protein; Melanoma inhibitory activity protein TT5HNVS GN MIA TT5HNVS FC Elicits growth inhibition on melanoma cells in vitro as well as some other neuroectodermal tumors, including gliomas. TT5HNVS PD 5IXB; 1K0X; 1I1J; 1HJD TT5HNVS SQ MARSLVCLGVIILLSAFSGPGVRGGPMPKLADRKLCADQECSHPISMAVALQDYMAPDCRFLTIHRGQVVYVFSKLKGRGRLFWGGSVQGDYYGDLAARLGYFPSSIVREDQTLKPGKVDVKTDKWDFYCQ TT5HNVS TT Literature-reported TT9GUW0 ID TT9GUW0 TT9GUW0 TN Melanoma differentiation-associated protein 6 (CDKN1A) TT9GUW0 UP P38936 TT9GUW0 UC CDN1A_HUMAN TT9GUW0 SN WAF1; SDI1; PIC1; P21(WAF1); P21; Melanoma differentiation associated protein 6; MDA6; MDA-6; Cyclin-dependent kinase inhibitor 1; CIP1; CDK-interacting protein 1; CAP20 TT9GUW0 GN CDKN1A TT9GUW0 FC Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex. Inhibits DNA synthesis by DNA polymerase delta by competing with POLD3 for PCNA binding. May be involved in p53/TP53 mediated inhibition of cellular proliferation in response to DNA damage. TT9GUW0 PD 6CIX; 6CIV; 6CEJ; 6CBI; 5E0U TT9GUW0 SQ MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP TT9GUW0 TT Literature-reported TTMS7DF ID TTMS7DF TTMS7DF TN Membrane cofactor protein (CD46) TTMS7DF UP P15529 TTMS7DF UC MCP_HUMAN TTMS7DF SN Trophoblast leukocyte common antigen; TLX; MIC10; MCP TTMS7DF GN CD46 TTMS7DF FC May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity. Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. TTMS7DF PD 5FO8; 3O8E; 3L89; 3INB; 2O39 TTMS7DF SQ MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNYPGYPKPEEGILDSLDVWVIAVIVIAIVVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL TTMS7DF TT Clinical trial TTBGTEJ ID TTBGTEJ TTBGTEJ TN Membrane inhibitor of reactive lysis (CD59) TTBGTEJ UP P13987 TTBGTEJ UC CD59_HUMAN TTBGTEJ SN Protectin; Membrane attack complex inhibition factor; MSK21; MIRL; MIN3; MIN2; MIN1; MIC11; MEM43 antigen; MACinhibitory protein; MACIP; MACIF; MAC-inhibitory protein; MAC-IP; HRF20; HRF-20; CD59 glycoprotein; 20 kDa homologous restriction factor; 1F5 antigen TTBGTEJ GN CD59 TTBGTEJ FC Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase. Potent inhibitor of the complement membrane attack complex (MAC) action. TTBGTEJ PD 5IMY; 5IMT; 4BIK; 2UX2; 2UWR TTBGTEJ SQ MGIQGGSVLFGLLLVLAVFCHSGHSLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLCNFNEQLENGGTSLSEKTVLLLVTPFLAAAWSLHP TTBGTEJ TT Clinical trial TT56RYE ID TT56RYE TT56RYE TN Mesencephalic astrocyte-derived neurotrophic factor (ARMET) TT56RYE UP P55145 TT56RYE UC MANF_HUMAN TT56RYE SN Mesencephalic astrocytederived neurotrophic factor; MANF; Argininerich protein TT56RYE GN MANF TT56RYE FC Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. TT56RYE PD 2W51; 2KVE; 2KVD TT56RYE SQ MRRMWATQGLAVALALSVLPGSRALRPGDCEVCISYLGRFYQDLKDRDVTFSPATIENELIKFCREARGKENRLCYYIGATDDAATKIINEVSKPLAHHIPVEKICEKLKKKDSQICELKYDKQIDLSTVDLKKLRVKELKKILDDWGETCKGCAEKSDYIRKINELMPKYAPKAASARTDL TT56RYE TT Literature-reported TTWRP2F ID TTWRP2F TTWRP2F TN Metabotropic glutamate receptor 6 (mGluR6) TTWRP2F UP O15303 TTWRP2F UC GRM6_HUMAN TTWRP2F BC GPCR glutamate TTWRP2F SN MGLUR6; GPRC1F TTWRP2F GN GRM6 TTWRP2F FC G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity (By similarity). Signaling stimulates TRPM1 channel activity and Ca(2+) uptake. Required for normal vision. TTWRP2F SQ MARPRRAREPLLVALLPLAWLAQAGLARAAGSVRLAGGLTLGGLFPVHARGAAGRACGQLKKEQGVHRLEAMLYALDRVNADPELLPGVRLGARLLDTCSRDTYALEQALSFVQALIRGRGDGDEVGVRCPGGVPPLRPAPPERVVAVVGASASSVSIMVANVLRLFAIPQISYASTAPELSDSTRYDFFSRVVPPDSYQAQAMVDIVRALGWNYVSTLASEGNYGESGVEAFVQISREAGGVCIAQSIKIPREPKPGEFSKVIRRLMETPNARGIIIFANEDDIRRVLEAARQANLTGHFLWVGSDSWGAKTSPILSLEDVAVGAITILPKRASIDGFDQYFMTRSLENNRRNIWFAEFWEENFNCKLTSSGTQSDDSTRKCTGEERIGRDSTYEQEGKVQFVIDAVYAIAHALHSMHQALCPGHTGLCPAMEPTDGRMLLQYIRAVRFNGSAGTPVMFNENGDAPGRYDIFQYQATNGSASSGGYQAVGQWAETLRLDVEALQWSGDPHEVPSSLCSLPCGPGERKKMVKGVPCCWHCEACDGYRFQVDEFTCEACPGDMRPTPNHTGCRPTPVVRLSWSSPWAAPPLLLAVLGIVATTTVVATFVRYNNTPIVRASGRELSYVLLTGIFLIYAITFLMVAEPGAAVCAARRLFLGLGTTLSYSALLTKTNRIYRIFEQGKRSVTPPPFISPTSQLVITFSLTSLQVVGMIAWLGARPPHSVIDYEEQRTVDPEQARGVLKCDMSDLSLIGCLGYSLLLMVTCTVYAIKARGVPETFNEAKPIGFTMYTTCIIWLAFVPIFFGTAQSAEKIYIQTTTLTVSLSLSASVSLGMLYVPKTYVILFHPEQNVQKRKRSLKATSTVAAPPKGEDAEAHK TTWRP2F TT Literature-reported TTTQDEO ID TTTQDEO TTTQDEO TN Metal regulatory transcription factor 1 (MTF1) TTTQDEO UP Q14872 TTTQDEO UC MTF1_HUMAN TTTQDEO BC Zinc-finger TTTQDEO SN Transcription factor MTF1; MTF1; MREbinding transcription factor TTTQDEO GN MTF1 TTTQDEO FC Activates the metallothionein I promoter. Binds to the metal responsive element (MRE). TTTQDEO SQ MGEHSPDNNIIYFEAEEDELTPDDKMLRFVDKNGLVPSSSGTVYDRTTVLIEQDPGTLEDEDDDGQCGEHLPFLVGGEEGFHLIDHEAMSQGYVQHIISPDQIHLTINPGSTPMPRNIEGATLTLQSECPETKRKEVKRYQCTFEGCPRTYSTAGNLRTHQKTHRGEYTFVCNQEGCGKAFLTSYSLRIHVRVHTKEKPFECDVQGCEKAFNTLYRLKAHQRLHTGKTFNCESEGCSKYFTTLSDLRKHIRTHTGEKPFRCDHDGCGKAFAASHHLKTHVRTHTGERPFFCPSNGCEKTFSTQYSLKSHMKGHDNKGHSYNALPQHNGSEDTNHSLCLSDLSLLSTDSELRENSSTTQGQDLSTISPAIIFESMFQNSDDTAIQEDPQQTASLTESFNGDAESVSDVPPSTGNSASLSLPLVLQPGLSEPPQPLLPASAPSAPPPAPSLGPGSQQAAFGNPPALLQPPEVPVPHSTQFAANHQEFLPHPQAPQPIVPGLSVVAGASASAAAVASAVAAPAPPQSTTEPLPAMVQTLPLGANSVLTNNPTITITPTPNTAILQSSLVMGEQNLQWILNGATSSPQNQEQIQQASKVEKVFFTTAVPVASSPGSSVQQIGLSVPVIIIKQEEACQCQCACRDSAKERASSRRKGCSSPPPPEPSPQAPDGPSLQLPAQTFSSAPVPGSSSSTLPSSCEQSRQAETPSDPQTETLSAMDVSEFLSLQSLDTPSNLIPIEALLQGEEEMGLTSSFSK TTTQDEO TT Literature-reported TTH6SA5 ID TTH6SA5 TTH6SA5 TN Metastasis adhesion protein (MTDH) TTH6SA5 UP Q86UE4 TTH6SA5 UC LYRIC_HUMAN TTH6SA5 SN Protein LYRIC; Metadherin; Lysine-rich CEACAM1 co-isolated protein; LYRIC; Astrocyte elevated gene-1 protein; AEG1; AEG-1; 3D3/LYRIC TTH6SA5 GN MTDH TTH6SA5 FC Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. Downregulates SLC1A2/EAAT2 promoter activity when expressed ectopically. TTH6SA5 PD 4QMG TTH6SA5 SQ MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPSAWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEEWGNWVDEERASLLKSQEPIPDDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKTRPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPILQETDKSKSNTKQNSVPPSQTKSETSWESPKQIKKKKKARRET TTH6SA5 TT Literature-reported TTTAU9R ID TTTAU9R TTTAU9R TN Methyl cpg binding protein 2 (MECP2) TTTAU9R UP P51608 TTTAU9R UC MECP2_HUMAN TTTAU9R SN MethylCpGbinding protein 2; Methyl-CpG-binding protein 2; MeCp2 protein; MeCp2; MeCp-2 protein TTTAU9R GN MECP2 TTTAU9R FC It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference for 5-methylcytosine (5mC). Chromosomal protein that binds to methylated DNA. TTTAU9R PD 6OGK; 6OGJ; 6C1Y; 5BT2; 3C2I TTTAU9R SQ MVAGMLGLREEKSEDQDLQGLKDKPLKFKKVKKDKKEEKEGKHEPVQPSAHHSAEPAEAGKAETSEGSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAGKYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGTGRGRGRPKGSGTTRPKAATSEGVQVKRVLEKSPGKLLVKMPFQTSPGGKAEGGGATTSTQVMVIKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVQETVLPIKKRKTRETVSIEVKEVVKPLLVSTLGEKSGKGLKTCKSPGRKSKESSPKGRSSSASSPPKKEHHHHHHHSESPKAPVPLLPPLPPPPPEPESSEDPTSPPEPQDLSSSVCKEEKMPRGGSLESDGCPKEPAKTQPAVATAATAAEKYKHRGEGERKDIVSSSMPRPNREEPVDSRTPVTERVS TTTAU9R TT Literature-reported TTHONFT ID TTHONFT TTHONFT TN MHC class I antigen A*33 (HLA-A) TTHONFT UP P16190 TTHONFT UC 1A33_HUMAN TTHONFT BC MHC class I TTHONFT SN HLAA; HLA-A; HLA class I histocompatibility antigen, A33 alpha chain; Aw33; Aw19 TTHONFT GN HLA-A TTHONFT FC Involved in the presentation of foreign antigens to the immune system. TTHONFT SQ MAVMAPRTLLLLLSGALALTQTWAGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDQETRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQIMYGCDVGSDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAAHEAEQLRAYLDGTCVEWLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWELSSQPTIPIVGIIAGLVLLGAVITGAVVAAVMWRRKSSDRKGGSYTQAASSDSAQGSDVSLTACKV TTHONFT TT Literature-reported TTV8UE7 ID TTV8UE7 TTV8UE7 TN Midgestation and kidney protein (Midkine) TTV8UE7 UP P21741 TTV8UE7 UC MK_HUMAN TTV8UE7 SN Neurite outgrowth-promoting protein; Neurite outgrowth-promoting factor 2; NEGF2; MK1; MK; Amphiregulin-associated protein; ARAP TTV8UE7 GN MDK TTV8UE7 FC Binds cell-surface proteoglycan receptors via their chondroitin sulfate (CS) groups. Thereby regulates many processes like inflammatory response, cell proliferation, cell adhesion, cell growth, cell survival, tissue regeneration, cell differentiation and cell migration. Participates in inflammatory processes by exerting two different activities. Firstly, mediates neutrophils and macrophages recruitment to the sites of inflammation both by direct action by cooperating namely with ITGB2 via LRP1 and by inducing chemokine expression. This inflammation can be accompanied by epithelial cell survival and smooth muscle cell migration after renal and vessel damage, respectively. Secondly, suppresses the development of tolerogenic dendric cells thereby inhibiting the differentiation of regulatory T cells and also promote T cell expansion through NFAT signaling and Th1 cell differentiation. Promotes tissue regeneration after injury or trauma. After heart damage negatively regulates the recruitment of inflammatory cells and mediates cell survival through activation of anti-apoptotic signaling pathways via MAPKs and AKT pathways through the activation of angiogenesis. Also facilites liver regeneration as well as bone repair by recruiting macrophage at trauma site and by promoting cartilage development by facilitating chondrocyte differentiation. Plays a role in brain by promoting neural precursor cells survival and growth through interaction with heparan sulfate proteoglycans. Binds PTPRZ1 and promotes neuronal migration and embryonic neurons survival. Binds SDC3 or GPC2 and mediates neurite outgrowth and cell adhesion. Binds chondroitin sulfate E and heparin leading to inhibition of neuronal cell adhesion induced by binding with GPC2. Binds CSPG5 and promotes elongation of oligodendroglial precursor-like cells. Also binds ITGA6:ITGB1 complex; this interaction mediates MDK-induced neurite outgrowth. Binds LRP1; promotes neuronal survival. Binds ITGA4:ITGB1 complex; this interaction mediates MDK-induced osteoblast cells migration through PXN phosphorylation. Binds anaplastic lymphoma kinase (ALK) which induces ALK activation and subsequent phosphorylation of the insulin receptor substrate (IRS1), followed by the activation of mitogen-activated protein kinase (MAPK) and PI3-kinase, and the induction of cell proliferation. Promotes epithelial to mesenchymal transition through interaction with NOTCH2. During arteriogenesis, plays a role in vascular endothelial cell proliferation by inducing VEGFA expression and release which in turn induces nitric oxide synthase expression. Moreover activates vasodilation through nitric oxide synthase activation. Negatively regulates bone formation in response to mechanical load by inhibiting Wnt/beta-catenin signaling in osteoblasts. In addition plays a role in hippocampal development, working memory, auditory response, early fetal adrenal gland development and the female reproductive system. Secreted protein that functions as cytokine and growth factor and mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors. TTV8UE7 PD 1MKN; 1MKC TTV8UE7 SQ MQHRGFLLLTLLALLALTSAVAKKKDKVKKGGPGSECAEWAWGPCTPSSKDCGVGFREGTCGAQTQRIRCRVPCNWKKEFGADCKYKFENWGACDGGTGTKVRQGTLKKARYNAQCQETIRVTKPCTPKTKAKAKAKKGKGKD TTV8UE7 TT Literature-reported TTNE9U7 ID TTNE9U7 TTNE9U7 TN Mitotic checkpoint protein (MAD1L1) TTNE9U7 UP Q9UNH0 TTNE9U7 UC MD1L1_HUMAN TTNE9U7 SN hMAD1; Tax-binding protein 181; TXBP181; Mitotic spindle assembly checkpoint protein MAD1; Mitotic checkpoint gene hMAD1; Mitotic checkpoint MAD1 protein homolog; Mitotic arrest deficient 1-like protein 1; MAD1-like protein 1; MAD1 (Mitotic arrest deficient, yeast, homolog)-like 1; MAD1; HsMAD1 TTNE9U7 GN MAD1L1 TTNE9U7 FC May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding. Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. TTNE9U7 PD 4DZO; 1GO4 TTNE9U7 SQ MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA TTNE9U7 TT Literature-reported TTN1J82 ID TTN1J82 TTN1J82 TN Monocarboxylate transporter 1 (SLC16A1) TTN1J82 UP P53985 TTN1J82 UC MOT1_HUMAN TTN1J82 BC Major facilitator TTN1J82 SN Solute carrier family 16 member 1; MCT1; MCT 1 TTN1J82 GN SLC16A1 TTN1J82 FC Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Depending on the tissue and on cicumstances, mediates the import or export of lactic acid and ketone bodies. Required for normal nutrient assimilation, increase of white adipose tissue and body weight gain when on a high-fat diet. Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate, small molecules that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis. Proton-coupled monocarboxylate transporter. TTN1J82 SQ MPPAVGGPVGYTPPDGGWGWAVVIGAFISIGFSYAFPKSITVFFKEIEGIFHATTSEVSWISSIMLAVMYGGGPISSILVNKYGSRIVMIVGGCLSGCGLIAASFCNTVQQLYVCIGVIGGLGLAFNLNPALTMIGKYFYKRRPLANGLAMAGSPVFLCTLAPLNQVFFGIFGWRGSFLILGGLLLNCCVAGALMRPIGPKPTKAGKDKSKASLEKAGKSGVKKDLHDANTDLIGRHPKQEKRSVFQTINQFLDLTLFTHRGFLLYLSGNVIMFFGLFAPLVFLSSYGKSQHYSSEKSAFLLSILAFVDMVARPSMGLVANTKPIRPRIQYFFAASVVANGVCHMLAPLSTTYVGFCVYAGFFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVVLIISGIYLFIGMGINYRLLAKEQKANEQKKESKEEETSIDVAGKPNEVTKAAESPDQKDTDGGPKEEESPV TTN1J82 TT Literature-reported TTN1J82 FM Major facilitator superfamily TTG6VD5 ID TTG6VD5 TTG6VD5 TN Monocarboxylate transporter 4 (SLC16A3) TTG6VD5 UP O15427 TTG6VD5 UC MOT4_HUMAN TTG6VD5 BC Major facilitator TTG6VD5 SN Solute carrier family 16 member 3; MCT4; MCT 4 TTG6VD5 GN SLC16A3 TTG6VD5 FC Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Proton-linked monocarboxylate transporter. TTG6VD5 SQ MGGAVVDEGPTGVKAPDGGWGWAVLFGCFVITGFSYAFPKAVSVFFKELIQEFGIGYSDTAWISSILLAMLYGTGPLCSVCVNRFGCRPVMLVGGLFASLGMVAASFCRSIIQVYLTTGVITGLGLALNFQPSLIMLNRYFSKRRPMANGLAAAGSPVFLCALSPLGQLLQDRYGWRGGFLILGGLLLNCCVCAALMRPLVVTAQPGSGPPRPSRRLLDLSVFRDRGFVLYAVAASVMVLGLFVPPVFVVSYAKDLGVPDTKAAFLLTILGFIDIFARPAAGFVAGLGKVRPYSVYLFSFSMFFNGLADLAGSTAGDYGGLVVFCIFFGISYGMVGALQFEVLMAIVGTHKFSSAIGLVLLMEAVAVLVGPPSGGKLLDATHVYMYVFILAGAEVLTSSLILLLGNFFCIRKKPKEPQPEVAAAEEEKLHKPPADSGVDLREVEHFLKAEPEKNGEVVHTPETSV TTG6VD5 TT Literature-reported TTX8EBV ID TTX8EBV TTX8EBV TN Mothers against decapentaplegic homolog 9 (SMAD9) TTX8EBV UP O15198 TTX8EBV UC SMAD9_HUMAN TTX8EBV BC Dwarfin SMAD family TTX8EBV SN Smad9; Smad8; SMAD 9; SMAD 8; Mothers against DPP homolog 9 TTX8EBV GN Smad9 TTX8EBV FC Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD). Has been shown to be activated by activin type I receptor-like kinases (ALK-2, ALK-3, ALK-6) which stimulate heteromerization between SMAD9 and SMAD4. May play a role in osteoblast differentiation and maturation. TTX8EBV SQ MHSTTPISSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMDELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVETPVLPPVLVPRHSEYNPQLSLLAKFRSASLHSEPLMPHNATYPDSFQQPPCSALPPSPSHAFSQSPCTASYPHSPGSPSEPESPYQHSVDTPPLPYHATEASETQSGQPVDATADRHVVLSIPNGDFRPVCYEEPQHWCSVAYYELNNRVGETFQASSRSVLIDGFTDPSNNRNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKVFNNQLFAQLLAQSVHHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS TTX8EBV TT Literature-reported TT143WL ID TT143WL TT143WL TN MTOR complex 2 (RICTOR) TT143WL UP Q6R327 TT143WL UC RICTR_HUMAN TT143WL SN hAVO3; Rapamycin-insensitive companion of mTOR; KIAA1999; AVO3 homolog TT143WL GN RICTOR TT143WL FC mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Plays an essential role in embryonic growth and development. Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. TT143WL PD 5ZCS TT143WL SQ MAAIGRGRSLKNLRVRGRNDSGEENVPLDLTREPSDNLREILQNVARLQGVSNMRKLGHLNNFTKLLCDIGHSEEKLGFHYEDIIICLRLALLNEAKEVRAAGLRALRYLIQDSSILQKVLKLKVDYLIARCIDIQQSNEVERTQALRLVRKMITVNASLFPSSVTNSLIAVGNDGLQERDRMVRACIAIICELALQNPEVVALRGGLNTILKNVIDCQLSRINEALITTILHLLNHPKTRQYVRADVELERILAPYTDFHYRHSPDTAEGQLKEDREARFLASKMGIIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTEEFIEALLSVDPGRFQDSWRLSDGFVAAEAKTILPHRARSRPDLMDNYLALILSAFIRNGLLEGLVEVITNSDDHISVRATILLGELLHMANTILPHSHSHHLHCLPTLMNMAASFDIPKEKRLRASAALNCLKRFHEMKKRGPKPYSLHLDHIIQKAIATHQKRDQYLRVQKDIFILKDTEEALLINLRDSQVLQHKENLEWNWNLIGTILKWPNVNLRNYKDEQLHRFVRRLLYFYKPSSKLYANLDLDFAKAKQLTVVGCQFTEFLLESEEDGQGYLEDLVKDIVQWLNASSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVILSKILTAATDACRLYATKHLRVLLRANVEFFNNWGIELLVTQLHDKNKTISSEALDILDEACEDKANLHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAKQLEKWHREYNSKYVDLIEEQLNEALTTYRKPVDGDNYVRRSNQRLQRPHVYLPIHLYGQLVHHKTGCHLLEVQNIITELCRNVRTPDLDKWEEIKKLKASLWALGNIGSSNWGLNLLQEENVIPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHNWDAVRHSRKHLWPVVPDDVEQLCNELSSIPSTLSLNSESTSSRHNSESESVPSSMFILEDDRFGSSSTSTFFLDINEDTEPTFYDRSGPIKDKNSFPFFASSKLVKNRILNSLTLPNKKHRSSSDPKGGKLSSESKTSNRRIRTLTEPSVDFNHSDDFTPISTVQKTLQLETSFMGNKHIEDTGSTPSIGENDLKFTKNFGTENHRENTSRERLVVESSTSSHMKIRSQSFNTDTTTSGISSMSSSPSRETVGVDATTMDTDCGSMSTVVSTKTIKTSHYLTPQSNHLSLSKSNSVSLVPPGSSHTLPRRAQSLKAPSIATIKSLADCNFSYTSSRDAFGYATLKRLQQQRMHPSLSHSEALASPAKDVLFTDTITMKANSFESRLTPSRFMKALSYASLDKEDLLSPINQNTLQRSSSVRSMVSSATYGGSDDYIGLALPVDINDIFQVKDIPYFQTKNIPPHDDRGARAFAHDAGGLPSGTGGLVKNSFHLLRQQMSLTEIMNSIHSDASLFLESTEDTGLQEHTDDNCLYCVCIEILGFQPSNQLSAICSHSDFQDIPYSDWCEQTIHNPLEVVPSKFSGISGCSDGVSQEGSASSTKSTELLLGVKTIPDDTPMCRILLRKEVLRLVINLSSSVSTKCHETGLLTIKEKYPQTFDDICLYSEVSHLLSHCTFRLPCRRFIQELFQDVQFLQMHEEAEAVLATPPKQPIVDTSAES TT143WL TT Literature-reported TTGQ6MI ID TTGQ6MI TTGQ6MI TN Mucin-15 (MUC15) TTGQ6MI UP Q8N387 TTGQ6MI UC MUC15_HUMAN TTGQ6MI BC Mucin TTGQ6MI SN Mucin15; MUC15 TTGQ6MI GN MUC15 TTGQ6MI FC May play a role in the cell adhesion to the extracellular matrix. TTGQ6MI SQ MLALAKILLISTLFYSLLSGSHGKENQDINTTQNIAEVFKTMENKPISLESEANLNSDKENITTSNLKASHSPPLNLPNNSHGITDFSSNSSAEHSLGSLKPTSTISTSPPLIHSFVSKVPWNAPIADEDLLPISAHPNATPALSSENFTWSLVNDTVKTPDNSSITVSILSSEPTSPSVTPLIVEPSGWLTTNSDSFTGFTPYQEKTTLQPTLKFTNNSKLFPNTSDPQKENRNTGIVFGAILGAILGVSLLTLVGYLLCGKRKTDSFSHRRLYDDRNEPVLRLDNAPEPYDVSFGNSSYYNPTLNDSAMPESEENARDGIPMDDIPPLRTSV TTGQ6MI TT Literature-reported TT9XBVO ID TT9XBVO TT9XBVO TN Mucolipin-1 (TRPML1) TT9XBVO UP Q9GZU1 TT9XBVO UC MCLN1_HUMAN TT9XBVO SN Transient receptor potential channel mucolipin 1; TRPML1; Mucolipidin; MSTP080; ML4; ML1; MG-2 TT9XBVO GN MCOLN1 TT9XBVO FC Nonselective cation channel probably playing a role in the regulation of membrane trafficking events and of metal homeostasis. Proposed to play a major role in Ca(2+) release from late endosome and lysosome vesicles to the cytoplasm, which is important for many lysosome-dependent cellular events, including the fusion and trafficking of these organelles, exocytosis and autophagy. Required for efficient uptake of large particles in macrophages in which Ca(2+) release from the lysosomes triggers lysosomal exocytosis. May also play a role in phagosome-lysosome fusion (By similarity). Involved in lactosylceramide trafficking indicative for a role in the regulation of late endocytic membrane fusion/fission events. By mediating lysosomal Ca(2+) release is involved in regulation of mTORC1 signaling and in mTOR/TFEB-dependent lysosomal adaptation to environmental cues such as nutrient levels. Seems to act as lysosomal active oxygen species (ROS) sensor involved in ROS-induced TFEB activation and autophagy. Functions as a Fe(2+) permeable channel in late endosomes and lysosomes. Proposed to play a role in zinc homeostasis probably implicating its association with TMEM163 In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells (By similarity). TT9XBVO PD 6E7Z; 6E7Y; 6E7P; 5WJ9; 5WJ5 TT9XBVO SQ MTAPAGPRGSETERLLTPNPGYGTQAGPSPAPPTPPEEEDLRRRLKYFFMSPCDKFRAKGRKPCKLMLQVVKILVVTVQLILFGLSNQLAVTFREENTIAFRHLFLLGYSDGADDTFAAYTREQLYQAIFHAVDQYLALPDVSLGRYAYVRGGGDPWTNGSGLALCQRYYHRGHVDPANDTFDIDPMVVTDCIQVDPPERPPPPPSDDLTLLESSSSYKNLTLKFHKLVNVTIHFRLKTINLQSLINNEIPDCYTFSVLITFDNKAHSGRIPISLETQAHIQECKHPSVFQHGDNSFRLLFDVVVILTCSLSFLLCARSLLRGFLLQNEFVGFMWRQRGRVISLWERLEFVNGWYILLVTSDVLTISGTIMKIGIEAKNLASYDVCSILLGTSTLLVWVGVIRYLTFFHNYNILIATLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFAAMQAQQGRSSLVWLFSQLYLYSFISLFIYMVLSLFIALITGAYDTIKHPGGAGAEESELQAYIAQCQDSPTSGKFRRGSGSACSLLCCCGRDPSEEHSLLVN TT9XBVO TT Preclinical TT0NLAQ ID TT0NLAQ TT0NLAQ TN Mucolipin-3 (TRPML3) TT0NLAQ UP Q8TDD5 TT0NLAQ UC MCLN3_HUMAN TT0NLAQ SN Transient receptor potential channel mucolipin 3; TRPML3 TT0NLAQ GN MCOLN3 TT0NLAQ FC Nonselective ligand-gated cation channel probably playing a role in the regulation of membrane trafficking events. Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity. Mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal acidification and is involved in the regulation of membrane trafficking and fusion in the endosomal pathway. Does not seem to act as mechanosensory transduction channel in inner ear sensory hair cells. Proposed to play a critical role at the cochlear stereocilia ankle-link region during hair-bundle growth (By similarity). Involved in the regulation of autophagy. Through association with GABARAPL2 may be involved in autophagosome formation possibly providing Ca(2+) for the fusion process (By similarity). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Possible heteromeric ion channel assemblies with TRPV5 show pharmacological similarity with TRPML3. TT0NLAQ PD 6AYG; 6AYF; 6AYE TT0NLAQ SQ MADPEVVVSSCSSHEEENRCNFNQQTSPSEELLLEDQMRRKLKFFFMNPCEKFWARGRKPWKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTIAFKHLFLKGYMDRMDDTYAVYTQSDVYDQLIFAVNQYLQLYNVSVGNHAYENKGTKQSAMAICQHFYKRGNIYPGNDTFDIDPEIETECFFVEPDEPFHIGTPAENKLNLTLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIRECKDWHVSGSIQKNTHYMMIFDAFVILTCLVSLILCIRSVIRGLQLQQEFVNFFLLHYKKEVSVSDQMEFVNGWYIMIIISDILTIIGSILKMEIQAKSLTSYDVCSILLGTSTMLVWLGVIRYLGFFAKYNLLILTLQAALPNVIRFCCCAAMIYLGYCFCGWIVLGPYHDKFRSLNMVSECLFSLINGDDMFATFAKMQQKSYLVWLFSRIYLYSFISLFIYMILSLFIALITDTYETIKQYQQDGFPETELRTFISECKDLPNSGKYRLEDDPPVSLFCCCKK TT0NLAQ TT Literature-reported TTUEAFL ID TTUEAFL TTUEAFL TN Multidrug resistance protein 4 (ABCC4) TTUEAFL UP O15439 TTUEAFL UC MRP4_HUMAN TTUEAFL BC ABC transporter TTUEAFL SN Multispecific organic anion transporter B; Multidrug resistanceassociated protein 4; MRP/cMOATrelated ABC transporter; MOATB; ATPbinding cassette subfamily C member 4; ABCC4 TTUEAFL GN ABCC4 TTUEAFL FC May be an organic anion pump relevant to cellular detoxification. TTUEAFL SQ MLPVYQEVKPNPLQDANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKEVLRAENDAQKPSLTRAIIKCYWKSYLVLGIFTLIEESAKVIQPIFLGKIINYFENYDPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRIQTFLLLDEISQRNRQLPSDGKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKKDNEESEQPPVPGTPTLRNRTFSESSVWSQQSSRPSLKDGALESQDTENVPVTLSEENRSEGKVGFQAYKNYFRAGAHWIVFIFLILLNTAAQVAYVLQDWWLSYWANKQSMLNVTVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYTDLEKEAPWEYQKRPPPAWPHEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESLFYKMVQQLGKAEAAALTETAKQVYFKRNYPHIGHTDHMVTNTSNGQPSTLTIFETAL TTUEAFL TT Literature-reported TTFTWQ8 ID TTFTWQ8 TTFTWQ8 TN Multiple tumor suppressor 1 (CDKN2A) TTFTWQ8 UP P42771 TTFTWQ8 UC CDN2A_HUMAN TTFTWQ8 SN p16INK4A; Tumour suppressor gene p16; P16-INK4a; P16-INK4; P16 gene; MTS-1; Cyclin-dependent kinase inhibitor 2A; Cyclin-dependent kinase 4 inhibitor A; CDK4I TTFTWQ8 GN CDKN2A TTFTWQ8 FC Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein. TTFTWQ8 PD 2A5E; 1DC2; 1BI7; 1A5E TTFTWQ8 SQ MEPAAGSSMEPSADWLATAAARGRVEEVRALLEAGALPNAPNSYGRRPIQVMMMGSARVAELLLLHGAEPNCADPATLTRPVHDAAREGFLDTLVVLHRAGARLDVRDAWGRLPVDLAEELGHRDVARYLRAAAGGTRGSNHARIDAAEGPSDIPD TTFTWQ8 TT Literature-reported TTFTWQ8 FM CDKN2 cyclin-dependent kinase inhibitor TTH9OLG ID TTH9OLG TTH9OLG TN Muscleblind-like protein 1 (MBNL2) TTH9OLG UP Q5VZF2 TTH9OLG UC MBNL2_HUMAN TTH9OLG SN Muscleblindlike proteinlike 39; Muscleblindlike proteinlike; Muscleblindlike protein 2; Muscleblindlike protein 1; Muscleblind-like protein-like 39; Muscleblind-like protein-like; Muscleblind-like protein 2; MLP1; MBLL39; MBLL TTH9OLG GN MBNL2 TTH9OLG FC Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. RNA-binding protein that binds to 5'ACACCC-3' core sequence, termed zipcode, within the 3'UTR of ITGA3. Binds to CUG triplet repeat expansion in myotonic dystrophy muscle cells by sequestering the target RNAs. Seems to regulate expression and localization of ITGA3 by transporting it from the nucleus to cytoplasm at adhesion plaques. May play a role in myotonic dystrophy pathophysiology (DM). Mediates pre-mRNA alternative splicing regulation. TTH9OLG PD 2RPP; 2E5S TTH9OLG SQ MALNVAPVRDTKWLTLEVCRQFQRGTCSRSDEECKFAHPPKSCQVENGRVIACFDSLKGRCSRENCKYLHPPTHLKTQLEINGRNNLIQQKTAAAMLAQQMQFMFPGTPLHPVPTFPVGPAIGTNTAISFAPYLAPVTPGVGLVPTEILPTTPVIVPGSPPVTVPGSTATQKLLRTDKLEVCREFQRGNCARGETDCRFAHPADSTMIDTSDNTVTVCMDYIKGRCMREKCKYFHPPAHLQAKIKAAQHQANQAAVAAQAAAAAATVMAFPPGALHPLPKRQALEKSNGTSAVFNPSVLHYQQALTSAQLQQHAAFIPTGSVLCMTPATSIDNSEIISRNGMECQESALRITKHCYCTYYPVSSSIELPQTAC TTH9OLG TT Literature-reported TTH9OLG FM Muscleblind family TT6SA0X ID TT6SA0X TT6SA0X TN Muscle-specific kinase receptor (MUSK) TT6SA0X UP O15146 TT6SA0X UC MUSK_HUMAN TT6SA0X SN Muscle-specific tyrosine-protein kinase receptor; Muscle, skeletal receptor tyrosine-protein kinase; MuSK TT6SA0X GN MUSK TT6SA0X FC Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle. Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUSK, the kinase of the complex. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. May regulate AChR phosphorylation and clustering through activation of ABL1 and Src family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a ternary complex with MUSK are also important for MUSK-dependent regulation of AChR clustering. May positively regulate Rho family GTPases through FNTA. Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. Other effectors of the MUSK signaling include DNAJA3 which functions downstream of MUSK. May also play a role within the central nervous system by mediating cholinergic responses, synaptic plasticity and memory formation (By similarity). TT6SA0X EC EC 2.7.10.1 TT6SA0X SQ MRELVNIPLVHILTLVAFSGTEKLPKAPVITTPLETVDALVEEVATFMCAVESYPQPEISWTRNKILIKLFDTRYSIRENGQLLTILSVEDSDDGIYCCTANNGVGGAVESCGALQVKMKPKITRPPINVKIIEGLKAVLPCTTMGNPKPSVSWIKGDSPLRENSRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGTAYSKVVKLEVEVFARILRAPESHNVTFGSFVTLHCTATGIPVPTITWIENGNAVSSGSIQESVKDRVIDSRLQLFITKPGLYTCIATNKHGEKFSTAKAAATISIAEWSKPQKDNKGYCAQYRGEVCNAVLAKDALVFLNTSYADPEEAQELLVHTAWNELKVVSPVCRPAAEALLCNHIFQECSPGVVPTPIPICREYCLAVKELFCAKEWLVMEEKTHRGLYRSEMHLLSVPECSKLPSMHWDPTACARLPHLDYNKENLKTFPPMTSSKPSVDIPNLPSSSSSSFSVSPTYSMTVIISIMSSFAIFVLLTITTLYCCRRRKQWKNKKRESAAVTLTTLPSELLLDRLHPNPMYQRMPLLLNPKLLSLEYPRNNIEYVRDIGEGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDNPNIVKLLGVCAVGKPMCLLFEYMAYGDLNEFLRSMSPHTVCSLSHSDLSMRAQVSSPGPPPLSCAEQLCIARQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKIADFGLSRNIYSADYYKANENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGLQPYYGMAHEEVIYYVRDGNILSCPENCPVELYNLMRLCWSKLPADRPSFTSIHRILERMCERAEGTVSV TT6SA0X TT Literature-reported TT16NHT ID TT16NHT TT16NHT TN Mutated Histone H3.3 (H3F3A) TT16NHT UP P84243 TT16NHT UC H33_HUMAN TT16NHT SN PP781; Histone H3.3; H3F3; H3.3B; H3.3A TT16NHT GN H3F3A TT16NHT FC Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. TT16NHT PD 6J51; 6J50; 6J4Z; 6J4Y; 6J4X TT16NHT SQ MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA TT16NHT TT Literature-reported TTKQU18 ID TTKQU18 TTKQU18 TN Mycobacterium 27kDa antigen Cfp30B (MycB cfp32) TTKQU18 UP O53774 TTKQU18 UC CF30_MYCTU TTKQU18 SN MycB Putative glyoxylase CF30 TTKQU18 GN MycB cfp32 TTKQU18 FC May function as a glyoxylase involved in the methylglyoxal detoxification pathway. Induces maturation of dendritic cells in a TLR2-dependent manner, causing increased expression of cell-surface molecules (CD80, CD86, MHC class I and II) and proinflammatory cytokines (TNF-alpha, IL-6, IL-1 beta and IL-12p70). Acts via both the NF-kappa-B and MAPK signaling pathways. Induces Th1-polarized immune responses. TTKQU18 PD 3OXH TTKQU18 SQ MPKRSEYRQGTPNWVDLQTTDQSAAKKFYTSLFGWGYDDNPVPGGGGVYSMATLNGEAVAAIAPMPPGAPEGMPPIWNTYIAVDDVDAVVDKVVPGGGQVMMPAFDIGDAGRMSFITDPTGAAVGLWQANRHIGATLVNETGTLIWNELLTDKPDLALAFYEAVVGLTHSSMEIAAGQNYRVLKAGDAEVGGCMEPPMPGVPNHWHVYFAVDDADATAAKAAAAGGQVIAEPADIPSVGRFAVLSDPQGAIFSVLKPAPQQ TTKQU18 TT Literature-reported TTHP87B ID TTHP87B TTHP87B TN Mycobacterium 6kDa early secretory antigenic target (MycB esxA) TTHP87B UP P9WNK7 TTHP87B UC ESXA_MYCTU TTHP87B SN ESAT-6; 6 kDa early secretory antigenic target TTHP87B GN MycB esxA TTHP87B FC A secreted protein that plays a number of roles in modulating the host's immune response to infection as well as being responsible for bacterial escape into the host cytoplasm. Acts as a strong host (human) T-cell antigen. Inhibits IL-12 p40 (IL12B) and TNF-alpha expression by infected host (mouse) macrophages, reduces the nitric oxide response by about 75%. In mice previously exposed to the bacterium, elicits high level of IFN-gamma production by T-cells upon subsequent challenge by M.tuberculosis, in the first phase of a protective immune response. Higher levels (1.6-3.3 uM) of recombinant protein inhibit IFN-gamma production by host (human) T-cells and also IL-17 and TNF-alpha production but not IL-2; decreases expression of host ATF-2 and JUN transcription factors by affecting T-cell receptors signaling downstream of ZAP70, without cytotoxicity or apoptosis. EsxA inhibits IFN-gamma production in human T-cells by activating p38 MAPK (MAPK14), p38 MAPK is not responsible for IL-17 decrease. Binds host (mouse) Toll-like receptor 2 (TLR2) and decreases host MYD88-dependent signaling; binding to TLR2 activates host kinase AKT and subsequently inhibits downstream activation of NF-kappa-B; the C-terminal 20 residues (76-95) are necessary and sufficient for the TLR2 inhibitory effect. Required for induction of host (human) IL-1B maturation and release by activating the host NLRP3/ASC inflammasome; may also promote access of other tuberculosis proteins to the host cells cytoplasm. Induces IL-8 (CXCL8) expression in host (human) lung epithelial cells. Exogenously applied protein, or protein expressed in host (human and mouse), binds beta-2-microglobulin (B2M) and decreases its export to the cell surface, probably leading to defects in class I antigen presentation by the host cell. Responsible for mitochondrial fragmention, redistribution around the cell nucleus and decreased mitochondrial mass; this effect is not seen until 48 hours post-infection. Able to disrupt artificial planar bilayers in the absence of EsxB (CFP-10). Native protein binds artificial liposomes in the absence but not presence of EsxB and is able to rigidify and lyse them; the EsxA-EsxB complex dissociates at acidic pH, EsxB might serve as a chaperone to prevent membrane lysis. Recombinant protein induces leakage of phosphocholine liposomes at acidic pH in the absence of ExsB, undergoes conformational change, becoming more alpha-helical at acidic pH. The study using recombinant protein did not find dissociation of EsxA-EsxB complex at acidic pH. Involved in translocation of bacteria from the host (human) phagolysosome to the host cytoplasm. Translocation into host cytoplasm is visible 3 days post-infection using cultured human cells and precedes host cell death. Recombinant protein induces apoptosis in host (human) differentiated cell lines, which is cell-line dependent; bacteria missing the ESX-1 locus do not induce apoptosis. Host (human) cells treated with EsxA become permeable to extracellular dye. EsxA and EsxA-EsxB are cytotoxic to pneumocytes. ESX-1 secretion system-induced host (mouse) cell apoptosis, which is probably responsible for infection of new host cells, might be due to EsxA. EsxA induces necrosis in aged neutrophils. May help regulate assembly and function of the type VII secretion system (T7SS) (By similarity). EsxA disassembles pre-formed EccC-EsxB multimers, possibly by making EccC-EsxA-EsxB trimers instead of EccC-EsxB-EsxB-EccC tetramers (By similarity). TTHP87B PD 3FAV; 1WA8 TTHP87B SQ MTEQQWNFAGIEAAASAIQGNVTSIHSLLDEGKQSLTKLAAAWGGSGSEAYQGVQQKWDATATELNNALQNLARTISEAGQAMASTEGNVTGMFA TTHP87B TT Literature-reported TTGDAE5 ID TTGDAE5 TTGDAE5 TN Mycobacterium Alkylhydroperoxidase AhpD (MycB ahpD) TTGDAE5 UP Q57353 TTGDAE5 UC AHPD_MYCTU TTGDAE5 SN Alkylhydroperoxidase AhpD; Alkyl hydroperoxide reductase AhpD TTGDAE5 GN MycB ahpD TTGDAE5 FC Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity. TTGDAE5 PD 1ME5; 1LW1; 1KNC; 1GU9 TTGDAE5 SQ MSIEKLKAALPEYAKDIKLNLSSITRSSVLDQEQLWGTLLASAAATRNPQVLADIGAEATDHLSAAARHAALGAAAIMGMNNVFYRGRGFLEGRYDDLRPGLRMNIIANPGIPKANFELWSFAVSAINGCSHCLVAHEHTLRTVGVDREAIFEALKAAAIVSGVAQALATIEALSPS TTGDAE5 TT Literature-reported TTTO9MF ID TTTO9MF TTTO9MF TN Mycobacterium Alpha-glucan:maltose-phosphate maltosyltransferase (MycB glgE) TTTO9MF UP P9WQ17 TTTO9MF UC GLGE_MYCTU TTTO9MF BC Glycosyl transferase TTTO9MF SN GMPMT; Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase; (1->4)-alpha-D-glucan:phosphate alpha-D-maltosyltransferase; (1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase TTTO9MF GN MycB glgE TTTO9MF FC Essential maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP5 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Exhibits an alpha-retaining catalytic mechanism. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB. TTTO9MF SQ MSGRAIGTETEWWVPGRVEIDDVAPVVSCGVYPAKAVVGEVVPVSAAVWREGHEAVAATLVVRYLGVRYPHLTDRPRARVLPTPSEPQQRVKPLLIPMTSGQEPFVFHGQFTPDRVGLWTFRVDGWGDPIHTWRHGLIAKLDAGQGETELSNDLLVGAVLLERAATGVPRGLRDPLLAAAAALRTPGDPVTRTALALTPEIEELLADYPLRDLVTRGEQFGVWVDRPLARFGAWYEMFPRSTGGWDDDGNPVHGTFATAAAELPRIAGMGFDVVYLPPIHPIGKVHRKGRNNSPTAAPTDVGSPWAIGSDEGGHDTVHPSLGTIDDFDDFVSAARDLGMEVALDLALQCAPDHPWAREHRQWFTELPDGTIAYAENPPKKYQDIYPLNFDNDPEGLYDEVLRVVQHWVNHGVKFFRVDNPHTKPPNFWAWLIAQVKTVDPDVLFLSEAFTPPARQYGLAKLGFTQSYSYFTWRTTKWELTEFGNQIAELADYRRPNLFVNTPDILHAVLQHNGPGMFAIRAVLAATMSPAWGMYCGYELFEHRAVREGSEEYLDSEKYELRPRDFASALDQGRSLQPFITRLNIIRRLHPAFQQLRTIHFHHVDNDALLAYSKFDPATGDCVLVVVTLNAFGPEEATLWLDMAALGMEDYDRFWVRDEITGEEYQWGQANYIRIDPARAVAHIINMPAVPYESRNTLLRRR TTTO9MF TT Literature-reported TTB91WX ID TTB91WX TTB91WX TN Mycobacterium Arabinosyltransferase A (MycB embA) TTB91WX UP P71485 TTB91WX UC EMBA_MYCAV TTB91WX SN Probable arabinosyltransferase A TTB91WX GN MycB embA TTB91WX FC Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan. TTB91WX EC EC 2.4.2.- TTB91WX SQ MPHDGKQRSQRIPRSVAAVAGIAGLLLCLAVPLLPVRQTTATVLWPQGTVDGHVSQITAPLVSGAPRALDISIPCPAVATLPADGGLVVSTLPPGGMDAGKNGLFVRANKDVVVVAFRDTVAAVAQRPAVAAGACSVLHAWADAGAAGAEFVGIPGAAGTLPAEKKPQVGGIFTDLKVPAGPGLSARVDIDTRFITAPTVLKQIVMVLGTLAVLTAIVALAVLDRRSRGGGTLINWRSPIAWLSRYRPGTHLANWRRVGLATWIADAAVLATLLLWHVVGATSSDDGYNLTIARVAPKAGYLVDYYRYFGTTDAPFDWYLGLLSRLASVSTAGVWMRLPATLAGIGCWLIISHWVLRRLGPGRGGLAANRVAVFTAGAVFVAAWLPFNNGLRPEPLIALGVLVTWMLVERAIALQRLAPAAVAVVVALLTATLAPQGLIAVAALLTGARAVAQAIRRRRASDGLLAPLAVLAAALSLILVVVFRSQTVATVLESARIKYKVGPTIAWYQDWLRYYFLTVESNPDGSMARRFAVLVMLLCLFGMLVILLRRGHVPGVASGPRWRLIGTTAVGLLLLTFTPTKWAVQFGAFAGLAGALGALTAFACSRIGLHNRRNLTLYVTALLFVLAWATSGINGWFYVGNYGVPWYDIQPVIASHPVTSMFLTLSIITGLLAAWQHFRMDYAGHTEVKDSRRNRVLASTPLLVVATIMVVGEVASLTKGAVFRYPLYTTGKANLAAIASGLSPTSCAMADDVLAEPDANAGMLQPLPGQTFGPDGPLGGVNPVGFKPDGVGDDLQSDPVVTKPGLVNSDASPNKPNVAYSDSAGTAGGKGPVGVNGSHAALPFGLDPARTPVMGSYGENSLAATATSAWYQLPPRTPDRPLVVVSAAGAIWSYKEDGTFTYGQSLKLQWGVARPDGSTVPLAEVQPIDIGPQPAWRNLRFPLAWAPPEANVARIVAYDPNLSSEQWFAFTPPRVPVTETLQQLIGSQTPVMMDIATAANFPCQRPFSEHLGVAELPAYRILPDRKQTAASSNLWQSSEAGGPFLFLQALLRTSTIPTYLRGDWYRDWGSVEQYFRLVPADQAPDAAIEQGVMTVHGWSRQGPIRALP TTB91WX TT Literature-reported TTSBUH3 ID TTSBUH3 TTSBUH3 TN Mycobacterium Arabinosyltransferase B (MycB embB) TTSBUH3 UP P71486 TTSBUH3 UC EMBB_MYCAV TTSBUH3 SN Probable arabinosyltransferase B TTSBUH3 GN MycB embB TTSBUH3 FC Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan. TTSBUH3 EC EC 2.4.2.- TTSBUH3 SQ MSVSTVGGDVRVTRWVATIAGLIGFVLSVATPLLPVVQTTATLNWPQGGQLNSVTAPLISLTPVDLTATVPCSLVRDLPPGGGVILSTGPKKGKDAALNALFVVAHGKRVDVTDRNVVIASASRDQVAGAGCSRIEIASTRAGTFATFVGLTDPAGKPLGGGFPDPNLRPQIVGVFTDLTGPAPAGLKLSATIDTRFSTTPTTLKLAAMVTAILATIVALVALWRLDQLDGHRMRRLIPANWRTFTLADVAVIFGFVLWHVIGANSSDDGYILGMARVADRAGYMSNYFRWFGSPEDPFGWYYNLLALMTHVSDASLWMRLPDLFAGIVCWLLLSREVLPRLGPAVAASRPANWAAGMVLLTAWMPFDNGLRPEPIIALGSLVTYVLIERSMRYSRLTPAALAVITAAFTLGVQPTGLIAVAALVAGGRPILRILVRRHRVVGTWPLVAPMLAAGTVILTVVFADQTLATVLEATRIRTAIGPSQAWYTENLRYYYLILPTVDGSLSRRFGFLITALCLFTAVFIMLRRKRIPGVARGPAWRLMGVIFGTMFFLMFTPTKWVHHFGLFAAVGAAMAALTTVLVSPAVLGWSRNRMAFLAALLFMMALCFATTNGWWYVSSYGVPFNSTMPKIGGITVSTVFFSMFVAAALYAIWLHFASREHGEGRLARALTAAPVPLAAGFMALVFIASMVAGIVRQYPTYSNAWDNLREFSGGCGLADDVLVEPDSNVGYMTPLGGDYGPLGPLGGQHPVGFSPNGVPEHTVAEAIRITPNQPGTDYDWDAPTKLSAPGINGSTVPLPYGLDAARVPLAGSYTTGAQQQSRLTSAWYRLPAPDDGHPLVVVTAAGKIAGNSVLHHHTDGQTVVLEYGRPGPGGDIVPAGRLVPYDLYGEQPKAWRNLRFARSDMPADTVAVRVVAEDLSLTPEDWIAVTPPRVPEMRSLQEYVGSTQPVLMDWAVGLAFPCQQPMLHVNGVTEIPKFRITPDYTAKKMDTDTWEDGTNGGLLGITDLLLRAHVMSTYLSHDWGRDWGSLRRFETIADAHPAQLDLGTATRTGWWSPGPIRIKP TTSBUH3 TT Literature-reported TTB859L ID TTB859L TTB859L TN Mycobacterium Beta-ketoacyl-ACP reductase (MycB fabG1) TTB859L UP P9WGT3 TTB859L UC FABG_MYCTU TTB859L SN Beta-ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; 3-oxoacyl-[acyl-carrier-protein] reductase FabG1; 3-ketoacyl-acyl carrier protein reductase TTB859L GN MycB fabG1 TTB859L FC Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. MabA preferentially metabolizes long-chain substrates (C8-C20) and has a poor affinity for the C4 substrate. TTB859L PD 2NTN; 1UZN; 1UZM; 1UZL TTB859L SQ MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH TTB859L TT Literature-reported TT8R2M4 ID TT8R2M4 TT8R2M4 TN Mycobacterium Bifunctional protein GlmU (MycB glmU) TT8R2M4 UP P9WMN3 TT8R2M4 UC GLMU_MYCTU TT8R2M4 SN Bifunctional protein GlmU TT8R2M4 GN MycB glmU TT8R2M4 FC Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. TT8R2M4 PD 4HCQ; 4G87; 4G3S; 4G3Q; 4G3P TT8R2M4 SQ MTFPGDTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTLGRTIDVALQDRPLGTGHAVLCGLSALPDDYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIVEQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLAELASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVRTHGSSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKRPGSPAAQASKRASEMACQQPTQPPDADQTP TT8R2M4 TT Literature-reported TT0S4IF ID TT0S4IF TT0S4IF TN Mycobacterium Glyoxylase CFP32 (MycB cfp32) TT0S4IF UP P9WIR3 TT0S4IF UC CFP32_MYCTU TT0S4IF SN MycB Putative glyoxylase CFP32; 27 kDa antigen Cfp30B TT0S4IF GN MycB cfp32 TT0S4IF FC May function as a glyoxylase involved in the methylglyoxal detoxification pathway. Induces maturation of dendritic cells in a TLR2-dependent manner, causing increased expression of cell-surface molecules (CD80, CD86, MHC class I and II) and proinflammatory cytokines (TNF-alpha, IL-6, IL-1 beta and IL-12p70). Acts via both the NF-kappa-B and MAPK signaling pathways. Induces Th1-polarized immune responses. TT0S4IF PD 3OXH TT0S4IF SQ MPKRSEYRQGTPNWVDLQTTDQSAAKKFYTSLFGWGYDDNPVPGGGGVYSMATLNGEAVAAIAPMPPGAPEGMPPIWNTYIAVDDVDAVVDKVVPGGGQVMMPAFDIGDAGRMSFITDPTGAAVGLWQANRHIGATLVNETGTLIWNELLTDKPDLALAFYEAVVGLTHSSMEIAAGQNYRVLKAGDAEVGGCMEPPMPGVPNHWHVYFAVDDADATAAKAAAAGGQVIAEPADIPSVGRFAVLSDPQGAIFSVLKPAPQQ TT0S4IF TT Literature-reported TTLYJGT ID TTLYJGT TTLYJGT TN Mycobacterium Immunogenic protein MPT63/MPB63 (MycB mpt63) TTLYJGT UP P97175 TTLYJGT UC MP63_MYCTU TTLYJGT SN Immunogenic protein MPT63; Antigen MPT63; 16 kDa immunoprotective extracellular protein TTLYJGT GN MycB mpt63 TTLYJGT FC A secreted protein of unknown function that is specific to mycobacteria. TTLYJGT PD 1LMI TTLYJGT SQ MKLTTMIKTAVAVVAMAAIATFAAPVALAAYPITGKLGSELTMTDTVGQVVLGWKVSDLKSSTAVIPGYPVAGQVWEATATVNAIRGSVTPAVSQFNARTADGINYRVLWQAAGPDTISGATIPQGEQSTGKIYFDVTGPSPTIVAMNNGMEDLLIWEP TTLYJGT TT Literature-reported TTFZAYL ID TTFZAYL TTFZAYL TN Mycobacterium Phosphopantetheinyl transferase (MycB pptT) TTFZAYL UP O33336 TTFZAYL UC O33336_MYCTU TTFZAYL SN Phosphopantetheinyl transferase PptT (CoA:APO-[ACP]pantetheinephosphotransferase) (CoA:APO-[acyl-carrier protein]pantetheinephosphotransferase) TTFZAYL GN MycB pptT TTFZAYL FC Invovled in the assembly-line production of complex molecules such as fatty acids, polyketides and polypeptides, where they activate acyl or peptidyl carrier proteins, transferring a 4'-phosphopantetheinyl moiety from coenzyme A (CoA) to a reactive serine residue on the carrier protein. TTFZAYL PD 4U89; 4QVH; 4QJK TTFZAYL SQ MTVGTLVASVLPATVFEDLAYAELYSDPPGLTPLPEEAPLIARSVAKRRNEFITVRHCARIALDQLGVPPAPILKGDKGEPCWPDGMVGSLTHCAGYRGAVVGRRDAVRSVGIDAEPHDVLPNGVLDAISLPAERADMPRTMPAALHWDRILFCAKEATYKAWFPLTKRWLGFEDAHITFETDSTGWTGRFVSRILIDGSTLSGPPLTTLRGRWSVERGLVLTAIVL TTFZAYL TT Literature-reported TT7MHK2 ID TT7MHK2 TT7MHK2 TN Mycobacterium Polyketide synthase (MycB pks2) TT7MHK2 UP P9WQE9 TT7MHK2 UC PHAS_MYCTU TT7MHK2 SN Polyketide synthase pks2; Phthioceranic/hydroxyphthioceranic acid synthase TT7MHK2 GN MycB pks2 TT7MHK2 FC Catalyzes the synthesis of the hepta- and octamethyl phthioceranic acids and/or hydroxyphthioceranic acids that are the major acyl constituents of sulfolipids. TT7MHK2 EC EC 2.3.1.- TT7MHK2 SQ MGLGSAASGTGADRGAWTLAEPRVTPVAVIGMACRLPGGIDSPELLWKALLRGDDLITEVPPDRWDCDEFYDPQPGVPGRTVCKWGGFLDNPADFDCEFFGIGEREAIAIDPQQRLLLETSWEAMEHAGLTQQTLAGSATGVFAGVTHGDYTMVAADAKQLEEPYGYLGNSFSMASGRVAYAMRLHGPAITVDTACSSGLTAVHMACRSLHEGESDVALAGGVALMLEPRKAAAGSALGMLSPTGRCRAFDVAADGFVSGEGCAVVVLKRLPDALADGDRILAVIRGTSANQDGHTVNIATPSQPAQVAAYRAALAAGGVDAATVGMVEAHGPGTPIGDPIEYASVSEVYGVDGPCALASVKTNFGHTQSTAGVLGLIKVVLALKHGVVPRNLHFTRLPDEIAGITTNLFVPEVTTPWPTNGRQVPRRAAVSSYGFSGTNVHAVVEQAPQTEAQPHAASTPPTGTPALFTLSASSADALRQTAQRLTDWIQQHADSLVLSDLAYTLARRRTHRSVRTAVIASSVDELIAGLGEVADGDTVYQPAVGQDDRGPVWLFSGQGSQWAAMGADLLTNESVFAATVAELEPLIAAESGFSVTEAMTAPETVTGIDRVQPTIFAMQVALAATMAAYGVRPGAVIGHSMGESAAAVVAGVLSAEDGVRVICRRSKLMATIAGSAAMASVELPALAVQSELTALGIDDVVVAVVTAPQSTVIAGGTESVRKLVDIWERRDVLARAVAVDVASHSPQVDPILDELIAALADLNPKAPEIPYYSATLFDPREAPACDARYWADNLRHTVRFSAAVRSALDDGYRVFAELSPHPLLTHAVDQIAGSVGMPVAALAGMRREQPLPLGLRRLLTDLHNAGAAVDFSVLCPQGRLVDAPLPAWSHRFLFYDREGVDNRSPGGSTVAVHPLLGAHVRLPEEPERHAWQADVGTATLPWLGDHRIHNVAALPGAAYCEMALSAARAVLGEQSEVRDMRFEAMLLLDDQTPVSTVATVTSPGVVDFAVEALQEGVGHHLRRASAVLQQVSGECEPPAYDMASLLEAHPCRVDGEDLRRQFDKHGVQYGPAFTGLAVAYVAEDATATMLAEVALPGSIRSQQGLYAIHPALLDACFQSVGAHPDSQSVGSGLLVPLGVRRVRAYAPVRTARYCYTRVTKVELVGVEADIDVLDAHGTVLLAVCGLRIGTGVSERDKHNRVLNERLLTIEWHQRELPEMDPSGAGKWLLISDCAASDVTATRLADAFREHSAACTTMRWPLHDDQLAAADQLRDQVGSDEFSGVVVLTGSNTGTPHQGSADRGAEYVRRLVGIARELSDLPGAVPRMYVVTRGAQRVLADDCVNLEQGGLRGLLRTIGAEHPHLRATQIDVDEQTGVEQLARQLLATSEEDETAWRDNEWYVARLCPTPLRPQERRTIVADHQQSGMRLQIRTPGDMQTIELAAFHRVPPGPGQIEVAVRASSVNFADVLIAFGRYPSFEGHLPQLGTDFAGVVTAVGPGVTDHKVGDHVGGMSPNGCWGTFVTCDARLAATLPPGLGDAQAAAVTTAHATAWYGLHELARIRAGDTVLIHSGTGGVGQAAIAIARAAGAEIFATAGTPQRRELLRNMGIEHVYDSRSIEFAEQIRRDTNGRGVDVVLNSVTGAAQLAGLKLLAFRGRFVEIGKRDIYGDTKLGLFPFRRNLSFYAVDLGLLSATHPEELRDLLGTVYRLTAAGELPMPQSTHYPLVEAATAIRVMGNAEHTGKLVLHIPQTGKSLVTLPPEQAQVFRPDGSYIITGGLGGLGLFLAEKMAAAGCGRIVLNSRTQPTQKMRETIEAIAAMGSEVVVECGDIAQPGTAERLVATAVATGLPVRGVLHAAAVVEDATLANITDELLARDWAPKVHGAWELHEATSGQPLDWFCLFSSAAALTGSPGQSAYSAANSWLDAFAHWRQAQGLPATAIAWGAWSDIGQLGWWSASPARASALEESNYTAITPDEGAYAFEALLRHNRVYTGYAPVIGAPWLVAFAERSRFFEVFSSSNGSGTSKFRVELNELPRDEWPARLRQLVAEQVSLILRRTVDPDRPLPEYGLDSLGALELRTRIETETGIRLAPKNVSATVRGLADHLYEQLAPDDAPAAALSSQ TT7MHK2 TT Literature-reported TT19LDW ID TT19LDW TT19LDW TN Mycobacterium Polyphosphate kinase (MycB ppk) TT19LDW UP O33127 TT19LDW UC PPK1_MYCLE TT19LDW BC Kinase TT19LDW SN Polyphosphoric acid kinase; PPK; ATP-polyphosphate phosphotransferase TT19LDW GN MycB ppk TT19LDW FC Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). TT19LDW SQ MMSNDLLVTDIEAEARTEENIWHSDNSALAAPPAATTSASQDQLPDDRYLNRESSWLDFNARVLALAADNSLPLLERAKFLAIFASNLDEFYMVRVAGLKRRDEMDLSVRSADGLTPREQLSRIGEQTQWIASRHARVFLDSVLPALGEEGIYIVTWTDLDQAERDQLSTYFNEQVFPVLTPLAVDPAHPFPFVSGLSLNLAVTVKQPEDGTQHFARVKVPNNVDRFVELANRGAVRDTSAGDEGQLIHRFLPMEELIAAFLPVLFPGTEIVEHHAFRITRNADFEVEEDRDEDLLQALERELARRRFGSPVRLEIADDMTESMLELLLRELDVHPSDVIEVPGLLDLSSLWQIYGLDRPALKDRAFIPDTHPAFAERETPKSIFATLREGDVLVHHPYHSFATSVQRFIEQATADPDVLAIKQTLYRTSGDSPIVLALIEAAEAGKQVVALVEIKARFDEQANIRWARALEHAGVHVVYGIVGLKTHCKTCLVVRREGPTIRRYCHIGTGNYNSKTARLYEDVGLLTAAPDIGADLTDLFNSLTGYSRKLAYRNLLVAPYGIRRGIIERVEREVAAHRESGPQTGKGLIRLKMNALVDEQVIDALYRASQAGVRVEVVVRGICALRPGTEGFSENIFVRSILGRFLEHSRIIHFRAIDEFWIGSADMMHRNLDRRVEVLAQVKDSRLTAQLDELLKSALDPFTRCWELRPDGQWTASPQKGQQVRDHQESLMERHRSR TT19LDW TT Literature-reported TTTU2LD ID TTTU2LD TTTU2LD TN Mycobacterium Primase (MycB ligD) TTTU2LD UP P9WNV3 TTTU2LD UC LIGD_MYCTU TTTU2LD SN NHEJ DNA repair protein D; NHEJ DNA polymerase; Multifunctional non-homologous end joining DNA repair protein LigD; Mt-Lig TTTU2LD GN MycB ligD TTTU2LD FC With Ku forms a non-homologous end joining (NHEJ) repair enzyme which repairs DNA double-strand breaks (DSB) with reduced fidelity. Recognizes, processes and reseals DSBs, including repairs on incompatible DSB which require 3'-resection, gap filling and ligation. Anneals the 3' overhanging strands from opposing breaks to form a gapped intermediate, which then can be extended in trans by using the termini as primers for extension of the annealed break. Binds to the recessed 5'-phosphate moiety of the downstream DNA strand forming a stable synaptic complex even when the 3'-protruding ends of the template DNA strands are not complementary. Has numerous activites; gap filling copies the template strand, and prefers a 5'-phosphate in the gap and rNTPS, DNA-directed DNA or RNA polymerase on 5'-overhangs, terminal transferase (extending ssDNA or blunt dsDNA in a non-templated fashion, preferentially with rNTPs), DNA-dependent RNA primase (synthesizes short RNAs on unprimed closed ssDNA) and 3'- to 5'-exonuclease on ssDNA. Isolated Pol domain (and presumably the holoenzyme) is able to form complexes between 2 noncompatible protruding 3'-ends DNA ends via microhomologous DNA strands, in a end-bridging function to which it adds a templated nucleotide. Minimal primer length is 2 nucleotides. TTTU2LD PD 4MKY; 3PKY; 2R9L; 2IRY; 2IRX TTTU2LD SQ MGSASEQRVTLTNADKVLYPATGTTKSDIFDYYAGVAEVMLGHIAGRPATRKRWPNGVDQPAFFEKQLALSAPPWLSRATVAHRSGTTTYPIIDSATGLAWIAQQAALEVHVPQWRFVAEPGSGELNPGPATRLVFDLDPGEGVMMAQLAEVARAVRDLLADIGLVTFPVTSGSKGLHLYTPLDEPVSSRGATVLAKRVAQRLEQAMPALVTSTMTKSLRAGKVFVDWSQNSGSKTTIAPYSLRGRTHPTVAAPRTWAELDDPALRQLSYDEVLTRIARDGDLLERLDADAPVADRLTRYRRMRDASKTPEPIPTAKPVTGDGNTFVIQEHHARRPHYDFRLECDGVLVSWAVPKNLPDNTSVNHLAIHTEDHPLEYATFEGAIPSGEYGAGKVIIWDSGTYDTEKFHDDPHTGEVIVNLHGGRISGRYALIRTNGDRWLAHRLKNQKDQKVFEFDNLAPMLATHGTVAGLKASQWAFEGKWDGYRLLVEADHGAVRLRSRSGRDVTAEYPQLRALAEDLADHHVVLDGEAVVLDSSGVPSFSQMQNRGRDTRVEFWAFDLLYLDGRALLGTRYQDRRKLLETLANATSLTVPELLPGDGAQAFACSRKHGWEGVIAKRRDSRYQPGRRCASWVKDKHWNTQEVVIGGWRAGEGGRSSGVGSLLMGIPGPGGLQFAGRVGTGLSERELANLKEMLAPLHTDESPFDVPLPARDAKGITYVKPALVAEVRYSEWTPEGRLRQSSWRGLRPDKKPSEVVRE TTTU2LD TT Literature-reported TTYVRWD ID TTYVRWD TTYVRWD TN Mycobacterium Sensor-like histidine kinase senX3 (MycB senX3) TTYVRWD UP Q11155 TTYVRWD UC SENX3_MYCTU TTYVRWD SN SenX3; Rv0490; MTCY20G9.16 TTYVRWD GN MycB senX3 TTYVRWD FC Probably forms part of a two-component regulatory system senx3/regx3. Phosphorylates regx3. TTYVRWD EC EC 2.7.13.3 TTYVRWD SQ MTVFSALLLAGVLSALALAVGGAVGMRLTSRVVEQRQRVATEWSGITVSQMLQCIVTLMPLGAAVVDTHRDVVYLNERAKELGLVRDRQLDDQAWRAARQALGGEDVEFDLSPRKRSATGRSGLSVHGHARLLSEEDRRFAVVFVHDQSDYARMEAARRDFVANVSHELKTPVGAMALLAEALLASADDSETVRRFAEKVLIEANRLGDMVAELIELSRLQGAERLPNMTDVDVDTIVSEAISRHKVAADNADIEVRTDAPSNLRVLGDQTLLVTALANLVSNAIAYSPRGSLVSISRRRRGANIEIAVTDRGIGIAPEDQERVFERFFRGDKARSRATGGSGLGLAIVKHVAANHDGTIRVWSKPGTGSTFTLALPALIEAYHDDERPEQAREPELRSNRSQREEELSR TTYVRWD TT Literature-reported TTS6XJE ID TTS6XJE TTS6XJE TN Mycobacterium Serine/threonine-protein kinase PknB (MycB pknB) TTS6XJE UP P9WI81 TTS6XJE UC PKNB_MYCTU TTS6XJE SN pknB; Serine/threonineprotein kinase PknB TTS6XJE GN MycB pknB TTS6XJE FC Key component of a signal transduction pathway that regulates cell growth and cell division via phosphorylation of target proteins such as GarA, GlmU, PapA5, PbpA, FhaB (Rv0019c), FhaA(Rv0020c), MviN, PstP, EmbR, Rv1422, Rv1747 and RseA. Shows a strong preference for Thr versus Ser as the phosphoacceptor. TTS6XJE PD 6I2P; 6B2P; 5U94; 5E0Z; 5E0Y TTS6XJE SQ MTTPSHLSDRYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPAGPLPYIVMEYVDGVTLRDIVHTEGPMTPKRAIEVIADACQALNFSHQNGIIHRDVKPANIMISATNAVKVMDFGIARAIADSGNSVTQTAAVIGTAQYLSPEQARGDSVDARSDVYSLGCVLYEVLTGEPPFTGDSPVSVAYQHVREDPIPPSARHEGLSADLDAVVLKALAKNPENRYQTAAEMRADLVRVHNGEPPEAPKVLTDAERTSLLSSAAGNLSGPRTDPLPRQDLDDTDRDRSIGSVGRWVAVVAVLAVLTVVVTIAINTFGGITRDVQVPDVRGQSSADAIATLQNRGFKIRTLQKPDSTIPPDHVIGTDPAANTSVSAGDEITVNVSTGPEQREIPDVSTLTYAEAVKKLTAAGFGRFKQANSPSTPELVGKVIGTNPPANQTSAITNVVIIIVGSGPATKDIPDVAGQTVDVAQKNLNVYGFTKFSQASVDSPRPAGEVTGTNPPAGTTVPVDSVIELQVSKGNQFVMPDLSGMFWVDAEPRLRALGWTGMLDKGADVDAGGSQHNRVVYQNPPAGTGVNRDGIITLRFGQ TTS6XJE TT Literature-reported TTBIL13 ID TTBIL13 TTBIL13 TN Myosin-2 (MYH2) TTBIL13 UP Q9UKX2 TTBIL13 UC MYH2_HUMAN TTBIL13 BC Myosin-kinesin ATPase TTBIL13 SN Myosin heavy chain, skeletal muscle, adult 2; Myosin heavy chain IIa; Myosin heavy chain 2a; Myosin heavy chain 2; MyHCIIa; MyHC2a; MyHC-IIa; MyHC-2a; MYHSA2 TTBIL13 GN MYH2 TTBIL13 FC Required for cytoskeleton organization. Muscle contraction. TTBIL13 SQ MSSDSELAVFGEAAPFLRKSERERIEAQNRPFDAKTSVFVAEPKESFVKGTIQSREGGKVTVKTEGGATLTVKDDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQARCRGFLARVEYQRMVERREAIFCIQYNIRSFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE TTBIL13 TT Literature-reported TTYJRN5 ID TTYJRN5 TTYJRN5 TN N-acetylglucosaminyltransferase I (NAGAT1) TTYJRN5 UP P26572 TTYJRN5 UC MGAT1_HUMAN TTYJRN5 SN N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; MGAT; GlcNAc-T I; GNT-I; GLCT1; GGNT1; Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase TTYJRN5 GN MGAT1 TTYJRN5 FC Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans. TTYJRN5 EC EC 2.4.1.101 TTYJRN5 SQ MLKKQSAGLVLWGAILFVAWNALLLLFFWTRPAPGRPPSVSALDGDPASLTREVIRLAQDAEVELERQRGLLQQIGDALSSQRGRVPTAAPPAQPRVPVTPAPAVIPILVIACDRSTVRRCLDKLLHYRPSAELFPIIVSQDCGHEETAQAIASYGSAVTHIRQPDLSSIAVPPDHRKFQGYYKIARHYRWALGQVFRQFRFPAAVVVEDDLEVAPDFFEYFRATYPLLKADPSLWCVSAWNDNGKEQMVDASRPELLYRTDFFPGLGWLLLAELWAELEPKWPKAFWDDWMRRPEQRQGRACIRPEISRTMTFGRKGVSHGQFFDQHLKFIKLNQQFVHFTQLDLSYLQREAYDRDFLARVYGAPQLQVEKVRTNDRKELGEVRVQYTGRDSFKAFAKALGVMDDLKSGVPRAGYRGIVTFQFRGRRVHLAPPLTWEGYDPSWN TTYJRN5 TT Patented-recorded TTQNRJM ID TTQNRJM TTQNRJM TN Natural cytotoxic triggering receptor 1 (NCR1) TTQNRJM UP O76036 TTQNRJM UC NCTR1_HUMAN TTQNRJM SN hNKp46; Natural killer cell p46-related protein; Natural cytotoxicity triggering receptor 1; NKp46; NK-p46; NK cell-activating receptor; Lymphocyte antigen 94 homolog; LY94; CD335 TTQNRJM GN NCR1 TTQNRJM FC Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis. TTQNRJM PD 1P6F; 1OLL TTQNRJM SQ MSSTLPALLCVGLCLSQRISAQQQTLPKPFIWAEPHFMVPKEKQVTICCQGNYGAVEYQLHFEGSLFAVDRPKPPERINKVKFYIPDMNSRMAGQYSCIYRVGELWSEPSNLLDLVVTEMYDTPTLSVHPGPEVISGEKVTFYCRLDTATSMFLLLKEGRSSHVQRGYGKVQAEFPLGPVTTAHRGTYRCFGSYNNHAWSFPSEPVKLLVTGDIENTSLAPEDPTFPADTWGTYLLTTETGLQKDHALWDHTAQNLLRMGLAFLVLVALVWFLVEDWLSRKRTRERASRASTWEGRRRLNTQTL TTQNRJM TT Literature-reported TTMDW9L ID TTMDW9L TTMDW9L TN Negative growth-regulatory protein MyD118 (GADD45B) TTMDW9L UP O75293 TTMDW9L UC GA45B_HUMAN TTMDW9L BC Ribosomal protein TTMDW9L SN Myeloid differentiation primary response protein MyD118; GADD45beta; GADD45B; DNA damage-inducible gene 45beta TTMDW9L GN GADD45B TTMDW9L FC Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK. TTMDW9L SQ MTLEELVACDNAAQKMQTVTAAVEELLVAAQRQDRLTVGVYESAKLMNVDPDSVVLCLLAIDEEEEDDIALQIHFTLIQSFCCDNDINIVRVSGMQRLAQLLGEPAETQGTTEARDLHCLLVTNPHTDAWKSHGLVEVASYCEESRGNNQWVPYISLQER TTMDW9L TT Literature-reported TT7YXGM ID TT7YXGM TT7YXGM TN Neurite outgrowth inhibitor NOGO-A (RTN4) TT7YXGM UP Q9NQC3 TT7YXGM UC RTN4_HUMAN TT7YXGM SN Reticulon-5; RTN-x; Nogo protein; Neuroendocrine-specific protein C homolog; Neuroendocrine-specific protein; Neurite outgrowth inhibitor; NSP; NOGO; KIAA0886; Foocen TT7YXGM GN RTN4 TT7YXGM FC Required to induce the formation and stabilization of endoplasmic reticulum (ER) tubules. They regulate membrane morphogenesis in the ER by promoting tubular ER production. They influence nuclear envelope expansion, nuclear pore complex formation and proper localization of inner nuclear membrane proteins. However each isoform have specific functions mainly depending on their tissue expression specificities (Probable). TT7YXGM PD 2JV5; 2G31 TT7YXGM SQ MEDLDQSPLVSSSDSPPRPQPAFKYQFVREPEDEEEEEEEEEEDEDEDLEELEVLERKPAAGLSAAPVPTAPAAGAPLMDFGNDFVPPAPRGPLPAAPPVAPERQPSWDPSPVSSTVPAPSPLSAAAVSPSKLPEDDEPPARPPPPPPASVSPQAEPVWTPPAPAPAAPPSTPAAPKRRGSSGSVDETLFALPAASEPVIRSSAENMDLKEQPGNTISAGQEDFPSVLLETAASLPSLSPLSAASFKEHEYLGNLSTVLPTEGTLQENVSEASKEVSEKAKTLLIDRDLTEFSELEYSEMGSSFSVSPKAESAVIVANPREEIIVKNKDEEEKLVSNNILHNQQELPTALTKLVKEDEVVSSEKAKDSFNEKRVAVEAPMREEYADFKPFERVWEVKDSKEDSDMLAAGGKIESNLESKVDKKCFADSLEQTNHEKDSESSNDDTSFPSTPEGIKDRSGAYITCAPFNPAATESIATNIFPLLGDPTSENKTDEKKIEEKKAQIVTEKNTSTKTSNPFLVAAQDSETDYVTTDNLTKVTEEVVANMPEGLTPDLVQEACESELNEVTGTKIAYETKMDLVQTSEVMQESLYPAAQLCPSFEESEATPSPVLPDIVMEAPLNSAVPSAGASVIQPSSSPLEASSVNYESIKHEPENPPPYEEAMSVSLKKVSGIKEEIKEPENINAALQETEAPYISIACDLIKETKLSAEPAPDFSDYSEMAKVEQPVPDHSELVEDSSPDSEPVDLFSDDSIPDVPQKQDETVMLVKESLTETSFESMIEYENKEKLSALPPEGGKPYLESFKLSLDNTKDTLLPDEVSTLSKKEKIPLQMEELSTAVYSNDDLFISKEAQIRETETFSDSSPIEIIDEFPTLISSKTDSFSKLAREYTDLEVSHKSEIANAPDGAGSLPCTELPHDLSLKNIQPKVEEKISFSDDFSKNGSATSKVLLLPPDVSALATQAEIESIVKPKVLVKEAEKKLPSDTEKEDRSPSAIFSAELSKTSVVDLLYWRDIKKTGVVFGASLFLLLSLTVFSIVSVTAYIALALLSVTISFRIYKGVIQAIQKSDEGHPFRAYLESEVAISEELVQKYSNSALGHVNCTIKELRRLFLVDDLVDSLKFAVLMWVFTYVGALFNGLTLLILALISLFSVPVIYERHQAQIDHYLGLANKNVKDAMAKIQAKIPGLKRKAE TT7YXGM TT Literature-reported TTZIK7P ID TTZIK7P TTZIK7P TN Neurofibromin-2 (NF2) TTZIK7P UP P35240 TTZIK7P UC MERL_HUMAN TTZIK7P SN Schwannomin; Schwannomerlin; SCH; Moesin-ezrin-radixin-like protein; Merlin TTZIK7P GN NF2 TTZIK7P FC Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. TTZIK7P PD 6CDS; 4ZRJ; 4ZRI; 3U8Z; 1H4R TTZIK7P SQ MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSDRGGSSKHNTIKKLTLQSAKSRVAFFEEL TTZIK7P TT Literature-reported TTSGLN5 ID TTSGLN5 TTSGLN5 TN Neuromodulin (GAP43) TTSGLN5 UP P17677 TTSGLN5 UC NEUM_HUMAN TTSGLN5 BC Neuromodulin family TTSGLN5 SN pp46; Neural phosphoprotein B-50; Growth-associated protein 43; Axonal membrane protein GAP-43 TTSGLN5 GN GAP43 TTSGLN5 FC This protein is associated with nerve growth. It is a major component of the motile "growth cones" that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction. TTSGLN5 SQ MLCCMRRTKQVEKNDDDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKDDVQAAEAEANKKDEAPVADGVEKKGEGTTTAEAAPATGSKPDEPGKAGETPSEEKKGEGDAATEQAAPQAPASSEEKAGSAETESATKASTDNSPSSKAEDAPAKEEPKQADVPAAVTAAAATTPAAEDAAAKATAQPPTETGESSQAEENIEAVDETKPKESARQDEGKEEEPEADQEHA TTSGLN5 TT Literature-reported TTZ4JC3 ID TTZ4JC3 TTZ4JC3 TN Neutrophil cytosol factor 1 (NCF1) TTZ4JC3 UP P14598 TTZ4JC3 UC NCF1_HUMAN TTZ4JC3 SN SH3PXD1A; SH3 and PX domain-containing protein 1A; P47-phox; P47(phox) NAD(P)H oxidase; Nox-organizing protein 2; Nox organizer 2; Neutrophil NADPH oxidase factor 1; NOXO2; NCF-47K; NCF-1; 47 kDa neutrophil oxidase factor; 47 kDa autosomal chronic granulomatous disease protein TTZ4JC3 GN NCF1 TTZ4JC3 FC NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). TTZ4JC3 PD 1WLP; 1W70; 1UEC; 1OV3; 1O7K TTZ4JC3 SQ MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRRFTEIYEFHKTLKEMFPIEAGAINPENRIIPHLPAPKWFDGQRAAENRQGTLTEYCSTLMSLPTKISRCPHLLDFFKVRPDDLKLPTDNQTKKPETYLMPKDGKSTATDITGPIILQTYRAIANYEKTSGSEMALSTGDVVEVVEKSESGWWFCQMKAKRGWIPASFLEPLDSPDETEDPEPNYAGEPYVAIKAYTAVEGDEVSLLEGEAVEVIHKLLDGWWVIRKDDVTGYFPSMYLQKSGQDVSQAQRQIKRGAPPRRSSIRNAHSIHQRSRKRLSQDAYRRNSVRFLQQRRRQARPGPQSPGSPLEEERQTQRSKPQPAVPPRPSADLILNRCSESTKRKLASAV TTZ4JC3 TT Literature-reported TT789FN ID TT789FN TT789FN TN Nischarin (NISCH) TT789FN UP Q9Y2I1 TT789FN UC NISCH_HUMAN TT789FN SN NISCH; I1R TT789FN GN NISCH TT789FN FC Acts either as the functional imidazoline-1 receptor (I1R) candidate or as amembrane-associated mediator of the I1R signaling. Binds numerous imidazoline ligands that induces initiation of cell-signaling cascades triggering to cell survival, growth and migration. Its activation by the agonist rilmenidine induces an increase in phosphorylation of mitogen-activated protein kinases MAPK1 and MAPK3 in rostral ventrolateral medulla (RVLM) neurons that exhibited rilmenidine-evoked hypotension. Blocking its activation with efaroxan abolished rilmenidine-induced mitogen-activated protein kinase phosphorylation in RVLM neurons. Acts as a modulator of Rac-regulated signal transduction pathways. Suppresses Rac1-stimulated cell migration by interacting with PAK1 and inhibiting its kinase activity. Also blocks Pak-independent Rac signaling by interacting with RAC1 and inhibiting Rac1-stimulated NF-kB response element and cyclin D1 promoter activation. Inhibits also LIMK1 kinase activity by reducing LIMK1 'Tyr-508' phosphorylation. Inhibits Rac-induced cell migration and invasion in breast and colon epithelial cells. Inhibits lamellipodia formation, when overexpressed. Plays a role in protection against apoptosis. Involved in association with IRS4 in the enhancement of insulin activation of MAPK1 and MAPK3. When overexpressed, induces a redistribution of cell surface ITGA5 integrin to intracellular endosomal structures. . TT789FN PD 3P0C TT789FN SQ MATARTFGPEREAEPAKEARVVGSELVDTYTVYIIQVTDGSHEWTVKHRYSDFHDLHEKLVAERKIDKNLLPPKKIIGKNSRSLVEKREKDLEVYLQKLLAAFPGVTPRVLAHFLHFHFYEINGITAALAEELFEKGEQLLGAGEVFAIGPLQLYAVTEQLQQGKPTCASGDAKTDLGHILDFTCRLKYLKVSGTEGPFGTSNIQEQLLPFDLSIFKSLHQVEISHCDAKHIRGLVASKPTLATLSVRFSATSMKEVLVPEASEFDEWEPEGTTLEGPVTAVIPTWQALTTLDLSHNSVSEIDESVKLIPKIEFLDLSHNGLLVVDNLQHLYNLVHLDLSYNKLSSLEGLHTKLGNIKTLNLAGNLLESLSGLHKLYSLVNLDLRDNRIEQMEEVRSIGSLPCLEHVSLLNNPLSIIPDYRTKVLAQFGERASEVCLDDTVTTEKELDTVEVLKAIQKAKEVKSKLSNPEKKGGEDSRLSAAPCIRPSSSPPTVAPASASLPQPILSNQGIMFVQEEALASSLSSTDSLTPEHQPIAQGCSDSLESIPAGQAASDDLRDVPGAVGGASPEHAEPEVQVVPGSGQIIFLPFTCIGYTATNQDFIQRLSTLIRQAIERQLPAWIEAANQREEGQGEQGEEEDEEEEEEEDVAENRYFEMGPPDVEEEEGGGQGEEEEEEEEDEEAEEERLALEWALGADEDFLLEHIRILKVLWCFLIHVQGSIRQFAACLVLTDFGIAVFEIPHQESRGSSQHILSSLRFVFCFPHGDLTEFGFLMPELCLVLKVRHSENTLFIISDAANLHEFHADLRSCFAPQHMAMLCSPILYGSHTSLQEFLRQLLTFYKVAGGCQERSQGCFPVYLVYSDKRMVQTAAGDYSGNIEWASCTLCSAVRRSCCAPSEAVKSAAIPYWLLLTPQHLNVIKADFNPMPNRGTHNCRNRNSFKLSRVPLSTVLLDPTRSCTQPRGAFADGHVLELLVGYRFVTAIFVLPHEKFHFLRVYNQLRASLQDLKTVVIAKTPGTGGSPQGSFADGQPAERRASNDQRPQEVPAEALAPAPAEVPAPAPAAASASGPAKTPAPAEASTSALVPEETPVEAPAPPPAEAPAQYPSEHLIQATSEENQIPSHLPACPSLRHVASLRGSAIIELFHSSIAEVENEELRHLMWSSVVFYQTPGLEVTACVLLSTKAVYFVLHDGLRRYFSEPLQDFWHQKNTDYNNSPFHISQCFVLKLSDLQSVNVGLFDQHFRLTGSTPMQVVTCLTRDSYLTHCFLQHLMVVLSSLERTPSPEPVDKDFYSEFGNKTTGKMENYELIHSSRVKFTYPSEEEIGDLTFTVAQKMAEPEKAPALSILLYVQAFQVGMPPPGCCRGPLRPKTLLLTSSEIFLLDEDCVHYPLPEFAKEPPQRDRYRLDDGRRVRDLDRVLMGYQTYPQALTLVFDDVQGHDLMGSVTLDHFGEVPGGPARASQGREVQWQVFVPSAESREKLISLLARQWEALCGRELPVELTG TT789FN TT Literature-reported TTQX29T ID TTQX29T TTQX29T TN NLR pyrin domain containing 1 (NLRP1) TTQX29T UP Q9C000 TTQX29T UC NLRP1_HUMAN TTQX29T SN Nucleotide-binding domain and caspase recruitment domain; NACHT, LRR and PYD domains-containing protein 1; NAC; KIAA0926; Death effector filament-forming ced-4-like apoptosis protein; DEFCAP; Caspase recruitment domain-containing protein 7; CARD7 TTQX29T GN NLRP1 TTQX29T FC As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP1, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. May be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner. Contrary to its mouse ortholog, not activated by Bacillus anthracis lethal toxin. It is unclear whether isoform 2 is involved in inflammasome formation. It is not cleaved within the FIIND domain, does not assemble into specks, nor promote IL1B release. However, in an vitro cell-free system, it has been shown to be activated by MDP. Binds ATP. TTQX29T PD 5Y3S; 4IM6; 4IFP; 3KAT; 1PN5 TTQX29T SQ MAGGAWGRLACYLEFLKKEELKEFQLLLANKAHSRSSSGETPAQPEKTSGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCAQAQEGAGHSPSFPYSPSEPHLGSPSQPTSTAVLMPWIHELPAGCTQGSERRVLRQLPDTSGRRWREISASLLYQALPSSPDHESPSQESPNAPTSTAVLGSWGSPPQPSLAPREQEAPGTQWPLDETSGIYYTEIREREREKSEKGRPPWAAVVGTPPQAHTSLQPHHHPWEPSVRESLCSTWPWKNEDFNQKFTQLLLLQRPHPRSQDPLVKRSWPDYVEENRGHLIEIRDLFGPGLDTQEPRIVILQGAAGIGKSTLARQVKEAWGRGQLYGDRFQHVFYFSCRELAQSKVVSLAELIGKDGTATPAPIRQILSRPERLLFILDGVDEPGWVLQEPSSELCLHWSQPQPADALLGSLLGKTILPEASFLITARTTALQNLIPSLEQARWVEVLGFSESSRKEYFYRYFTDERQAIRAFRLVKSNKELWALCLVPWVSWLACTCLMQQMKRKEKLTLTSKTTTTLCLHYLAQALQAQPLGPQLRDLCSLAAEGIWQKKTLFSPDDLRKHGLDGAIISTFLKMGILQEHPIPLSYSFIHLCFQEFFAAMSYVLEDEKGRGKHSNCIIDLEKTLEAYGIHGLFGASTTRFLLGLLSDEGEREMENIFHCRLSQGRNLMQWVPSLQLLLQPHSLESLHCLYETRNKTFLTQVMAHFEEMGMCVETDMELLVCTFCIKFSRHVKKLQLIEGRQHRSTWSPTMVVLFRWVPVTDAYWQILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLLETLRLAGCGLTAEDCKDLAFGLRANQTLTELDLSFNVLTDAGAKHLCQRLRQPSCKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHPACKLIRLGLDQTTLSDEMRQELRALEQEKPQLLIFSRRKPSVMTPTEGLDTGEMSNSTSSLKRQRLGSERAASHVAQANLKLLDVSKIFPIAEIAEESSPEVVPVELLCVPSPASQGDLHTKPLGTDDDFWGPTGPVATEVVDKEKNLYRVHFPVAGSYRWPNTGLCFVMREAVTVEIEFCVWDQFLGEINPQHSWMVAGPLLDIKAEPGAVEAVHLPHFVALQGGHVDTSLFQMAHFKEEGMLLEKPARVELHHIVLENPSFSPLGVLLKMIHNALRFIPVTSVVLLYHRVHPEEVTFHLYLIPSDCSIRKAIDDLEMKFQFVRIHKPPPLTPLYMGCRYTVSGSGSGMLEILPKELELCYRSPGEDQLFSEFYVGHLGSGIRLQVKDKKDETLVWEALVKPGDLMPATTLIPPARIAVPSPLDAPQLLHFVDQYREQLIARVTSVEVVLDKLHGQVLSQEQYERVLAENTRPSQMRKLFSLSQSWDRKCKDGLYQALKETHPHLIMELWEKGSKKGLLPLSS TTQX29T TT Literature-reported TT9JBY5 ID TT9JBY5 TT9JBY5 TN N-myc proto-oncogene protein (MYCN) TT9JBY5 UP P04198 TT9JBY5 UC MYCN_HUMAN TT9JBY5 SN bHLHe37; NMYC; N-myc; Class E basic helix-loop-helix protein 37 TT9JBY5 GN MYCN TT9JBY5 FC Positively regulates the transcription of MYCNOS in neuroblastoma cells. TT9JBY5 PD 5G1X TT9JBY5 SQ MPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC TT9JBY5 TT Literature-reported TTWS7I3 ID TTWS7I3 TTWS7I3 TN Non-receptor tyrosine-protein kinase TNK1 (TNK1) TTWS7I3 UP Q13470 TTWS7I3 UC TNK1_HUMAN TTWS7I3 SN CD38 negative kinase 1 TTWS7I3 GN TNK1 TTWS7I3 FC Involved in negative regulation of cell growth. Has tumor suppressor properties. Plays a negative regulatory role in the Ras-MAPK pathway. May function in signaling pathways utilized broadly during fetal development and more selectively in adult tissues and in cells of the lymphohematopoietic system. Could specifically be involved in phospholipid signal transduction. TTWS7I3 EC EC 2.7.10.2 TTWS7I3 SQ MLPEAGSLWLLKLLRDIQLAQFYWPILEELNVTRPEHFDFVKPEDLDGIGMGRPAQRRLSEALKRLRSGPKSKNWVYKILGGFAPEHKEPTLPSDSPRHLPEPEGGLKCLIPEGAVCRGELLGSGCFGVVHRGLWTLPSGKSVPVAVKSLRVGPEGPMGTELGDFLREVSVMMNLEHPHVLRLHGLVLGQPLQMVMELAPLGSLHARLTAPAPTPPLLVALLCLFLRQLAGAMAYLGARGLVHRDLATRNLLLASPRTIKVADFGLVRPLGGARGRYVMGGPRPIPYAWCAPESLRHGAFSSASDVWMFGVTLWEMFSGGEEPWAGVPPYLILQRLEDRARLPRPPLCSRALYSLALRCWAPHPADRPSFSHLEGLLQEAGPSEACCVRDVTEPGALRMETGDPITVIEGSSSFHSPDSTIWKGQNGRTFKVGSFPASAVTLADAGGLPATRPVHRGTPARGDQHPGSIDGDRKKANLWDAPPARGQRRNMPLERMKGISRSLESVLSLGPRPTGGGSSPPEIRQARAVPQGPPGLPPRPPLSSSSPQPSQPSRERLPWPKRKPPHNHPMGMPGARKAAALSGGLLSDPELQRKIMEVELSVHGVTHQECQTALGATGGDVVSAIRNLKVDQLFHLSSRSRADCWRILEHYQWDLSAASRYVLARP TTWS7I3 TT Literature-reported TTHVOTQ ID TTHVOTQ TTHVOTQ TN NUAK family SNF1-like kinase 2 (NUAK2) TTHVOTQ UP Q9H093 TTHVOTQ UC NUAK2_HUMAN TTHVOTQ SN SNF1/AMP kinase-related kinase; SNARK; Omphalocele kinase 2; OMPHK2 TTHVOTQ GN NUAK2 TTHVOTQ FC Stress-activated kinase involved in tolerance to glucose starvation. Induces cell-cell detachment by increasing F-actin conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required for the increased motility and invasiveness of CD95-activated tumor cells. Able to phosphorylate 'Ser-464' of LATS1. TTHVOTQ EC EC 2.7.11.1 TTHVOTQ SQ MESLVFARRSGPTPSAAELARPLAEGLIKSPKPLMKKQAVKRHHHKHNLRHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLMHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLYDYISERQQLSEREARHFFRQIVSAVHYCHQNRVVHRDLKLENILLDANGNIKIADFGLSNLYHQGKFLQTFCGSPLYASPEIVNGKPYTGPEVDSWSLGVLLYILVHGTMPFDGHDHKILVKQISNGAYREPPKPSDACGLIRWLLMVNPTRRATLEDVASHWWVNWGYATRVGEQEAPHEGGHPGSDSARASMADWLRRSSRPLLENGAKVCSFFKQHAPGGGSTTPGLERQHSLKKSRKENDMAQSLHSDTADDTAHRPGKSNLKLPKGILKKKVSASAEGVQEDPPELSPIPASPGQAAPLLPKKGILKKPRQRESGYYSSPEPSESGELLDAGDVFVSGDPKEQKPPQASGLLLHRKGILKLNGKFSQTALELAAPTTFGSLDELAPPRPLARASRPSGAVSEDSILSSESFDQLDLPERLPEPPLRGCVSVDNLTGLEEPPSEGPGSCLRRWRQDPLGDSCFSLTDCQEVTATYRQALRVCSKLT TTHVOTQ TT Literature-reported TT39EZT ID TT39EZT TT39EZT TN Nuclear receptor coactivator 4 (NCOA4) TT39EZT UP Q13772 TT39EZT UC NCOA4_HUMAN TT39EZT SN Ret-activating protein ELE1; RFG; NCoA-4; ELE1; Androgen receptor-associated protein of 70 kDa; Androgen receptor coactivator 70 kDa protein; ARA70 (dARA70N); ARA70; 70 kDa androgen receptor coactivator; 70 kDa AR-activator TT39EZT GN NCOA4 TT39EZT FC Ligand-independent coactivator of the peroxisome proliferator-activated receptor (PPAR) gamma. Enhances the androgen receptor transcriptional activity in prostate cancer cells. TT39EZT PD 1T5Z TT39EZT SQ MNTFQDQSGSSSNREPLLRCSDARRDLELAIGGVLRAEQQIKDNLREVKAQIHSCISRHLECLRSREVWLYEQVDLIYQLKEETLQQQAQQLYSLLGQFNCLTHQLECTQNKDLANQVSVCLERLGSLTLKPEDSTVLLFEADTITLRQTITTFGSLKTIQIPEHLMAHASSANIGPFLEKRGCISMPEQKSASGIVAVPFSEWLLGSKPASGYQAPYIPSTDPQDWLTQKQTLENSQTSSRACNFFNNVGGNLKGLENWLLKSEKSSYQKCNSHSTTSSFSIEMEKVGDQELPDQDEMDLSDWLVTPQESHKLRKPENGSRETSEKFKLLFQSYNVNDWLVKTDSCTNCQGNQPKGVEIENLGNLKCLNDHLEAKKPLSTPSMVTEDWLVQNHQDPCKVEEVCRANEPCTSFAECVCDENCEKEALYKWLLKKEGKDKNGMPVEPKPEPEKHKDSLNMWLCPRKEVIEQTKAPKAMTPSRIADSFQVIKNSPLSEWLIRPPYKEGSPKEVPGTEDRAGKQKFKSPMNTSWCSFNTADWVLPGKKMGNLSQLSSGEDKWLLRKKAQEVLLNSPLQEEHNFPPDHYGLPAVCDLFACMQLKVDKEKWLYRTPLQM TT39EZT TT Literature-reported TT4AQ5F ID TT4AQ5F TT4AQ5F TN Nucleus accumbens-associated protein 1 (NACC1) TT4AQ5F UP Q96RE7 TT4AQ5F UC NACC1_HUMAN TT4AQ5F SN NAC1; NAC-1; BTBD14B; BTB/POZ domain-containing protein 14B TT4AQ5F GN NACC1 TT4AQ5F FC Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines. Functions as a transcriptional repressor. TT4AQ5F PD 4U2N; 3GA1 TT4AQ5F SQ MAQTLQMEIPNFGNSILECLNEQRLQGLYCDVSVVVKGHAFKAHRAVLAASSSYFRDLFNNSRSAVVELPAAVQPQSFQQILSFCYTGRLSMNVGDQFLLMYTAGFLQIQEIMEKGTEFFLKVSSPSCDSQGLHAEEAPSSEPQSPVAQTSGWPACSTPLPLVSRVKTEQQESDSVQCMPVAKRLWDSGQKEAGGGGNGSRKMAKFSTPDLAANRPHQPPPPQQAPVVAAAQPAVAAGAGQPAGGVAAAGGVVSGPSTSERTSPGTSSAYTSDSPGSYHNEEDEEEDGGEEGMDEQYRQICNMYTMYSMMNVGQTAEKVEALPEQVAPESRNRIRVRQDLASLPAELINQIGNRCHPKLYDEGDPSEKLELVTGTNVYITRAQLMNCHVSAGTRHKVLLRRLLASFFDRNTLANSCGTGIRSSTNDPRRKPLDSRVLHAVKYYCQNFAPNFKESEMNAIAADMCTNARRVVRKSWMPKVKVLKAEDDAYTTFISETGKIEPDMMGVEHGFETASHEGEAGPSAEALQ TT4AQ5F TT Literature-reported TTZRE3C ID TTZRE3C TTZRE3C TN Olfactory receptor 51E2 (OR51E2) TTZRE3C UP Q9H255 TTZRE3C UC O51E2_HUMAN TTZRE3C BC GPCR rhodopsin TTZRE3C SN Prostate specific G-protein coupled receptor; PSGR; OR51E2; HPRAJ TTZRE3C GN OR51E2 TTZRE3C FC Probable G protein-coupled receptor that is activated bythe short chain fatty acids (SCFA) acetate and propionate. In response to SCFA, may positively regulate renin secretion and increase blood pressure (PubMed:23401498). May also be activated by steroidhormones and regulate cell proliferation (PubMed:19389702). May also function as an olfactory receptor being activated by beta-ionone (PubMed:19389702). TTZRE3C SQ MSSCNFTHATFVLIGIPGLEKAHFWVGFPLLSMYVVAMFGNCIVVFIVRTERSLHAPMYLFLCMLAAIDLALSTSTMPKILALFWFDSREISFEACLTQMFFIHALSAIESTILLAMAFDRYVAICHPLRHAAVLNNTVTAQIGIVAVVRGSLFFFPLPLLIKRLAFCHSNVLSHSYCVHQDVMKLAYADTLPNVVYGLTAILLVMGVDVMFISLSYFLIIRTVLQLPSKSERAKAFGTCVSHIGVVLAFYVPLIGLSVVHRFGNSLHPIVRVVMGDIYLLLPPVINPIIYGAKTKQIRTRVLAMFKISCDKDLQAVGGK TTZRE3C TT Literature-reported TTAH0KM ID TTAH0KM TTAH0KM TN Oncostatin-M-specific receptor beta (OSMR) TTAH0KM UP Q99650 TTAH0KM UC OSMR_HUMAN TTAH0KM BC Cytokine receptor TTAH0KM SN Oncostatin-M-specific receptor subunit beta; OSMRB; Interleukin-31 receptor subunit beta; IL-31RB; IL-31R-beta; IL-31R subunit beta; IL-31 receptor subunit beta TTAH0KM GN OSMR TTAH0KM FC Binds IL31 to activate STAT3 and possibly STAT1 and STAT5. Capable of transducing OSM-specific signaling events. Associates with IL31RA to form the IL31 receptor. TTAH0KM SQ MALFAVFQTTFFLTLLSLRTYQSEVLAERLPLTPVSLKVSTNSTRQSLHLQWTVHNLPYHQELKMVFQIQISRIETSNVIWVGNYSTTVKWNQVLHWSWESELPLECATHFVRIKSLVDDAKFPEPNFWSNWSSWEEVSVQDSTGQDILFVFPKDKLVEEGTNVTICYVSRNIQNNVSCYLEGKQIHGEQLDPHVTAFNLNSVPFIRNKGTNIYCEASQGNVSEGMKGIVLFVSKVLEEPKDFSCETEDFKTLHCTWDPGTDTALGWSKQPSQSYTLFESFSGEKKLCTHKNWCNWQITQDSQETYNFTLIAENYLRKRSVNILFNLTHRVYLMNPFSVNFENVNATNAIMTWKVHSIRNNFTYLCQIELHGEGKMMQYNVSIKVNGEYFLSELEPATEYMARVRCADASHFWKWSEWSGQNFTTLEAAPSEAPDVWRIVSLEPGNHTVTLFWKPLSKLHANGKILFYNVVVENLDKPSSSELHSIPAPANSTKLILDRCSYQICVIANNSVGASPASVIVISADPENKEVEEERIAGTEGGFSLSWKPQPGDVIGYVVDWCDHTQDVLGDFQWKNVGPNTTSTVISTDAFRPGVRYDFRIYGLSTKRIACLLEKKTGYSQELAPSDNPHVLVDTLTSHSFTLSWKDYSTESQPGFIQGYHVYLKSKARQCHPRFEKAVLSDGSECCKYKIDNPEEKALIVDNLKPESFYEFFITPFTSAGEGPSATFTKVTTPDEHSSMLIHILLPMVFCVLLIMVMCYLKSQWIKETCYPDIPDPYKSSILSLIKFKENPHLIIMNVSDCIPDAIEVVSKPEGTKIQFLGTRKSLTETELTKPNYLYLLPTEKNHSGPGPCICFENLTYNQAASDSGSCGHVPVSPKAPSMLGLMTSPENVLKALEKNYMNSLGEIPAGETSLNYVSQLASPMFGDKDSLPTNPVEAPHCSEYKMQMAVSLRLALPPPTENSSLSSITLLDPGEHYC TTAH0KM TT Literature-reported TTAH0KM FM Type I cytokine receptor TTK9HGZ ID TTK9HGZ TTK9HGZ TN Osteoclast differentiation factor receptor (ODFR) TTK9HGZ UP Q9Y6Q6 TTK9HGZ UC TNR11_HUMAN TTK9HGZ SN Tumor necrosis factor receptor superfamily member 11A; Receptor activator of NF-KB; RANK; ODFR; CD265 TTK9HGZ GN TNFRSF11A TTK9HGZ FC Involved in the regulation of interactions between T-cells and dendritic cells. Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis. TTK9HGZ PD 1LB5 TTK9HGZ SQ MAPRARRRRPLFALLLLCALLARLQVALQIAPPCTSEKHYEHLGRCCNKCEPGKYMSSKCTTTSDSVCLPCGPDEYLDSWNEEDKCLLHKVCDTGKALVAVVAGNSTTPRRCACTAGYHWSQDCECCRRNTECAPGLGAQHPLQLNKDTVCKPCLAGYFSDAFSSTDKCRPWTNCTFLGKRVEHHGTEKSDAVCSSSLPARKPPNEPHVYLPGLIILLLFASVALVAAIIFGVCYRKKGKALTANLWHWINEACGRLSGDKESSGDSCVSTHTANFGQQGACEGVLLLTLEEKTFPEDMCYPDQGGVCQGTCVGGGPYAQGEDARMLSLVSKTEIEEDSFRQMPTEDEYMDRPSQPTDQLLFLTEPGSKSTPPFSEPLEVGENDSLSQCFTGTQSTVGSESCNCTEPLCRTDWTPMSSENYLQKEVDSGHCPHWAASPSPNWADVCTGCRNPPGEDCEPLVGSPKRGPLPQCAYGMGLPPEEEASRTEARDQPEDGADGRLPSSARAGAGSGSSPGGQSPASGNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGAAAAAEPMGRPVQEETLARRDSFAGNGPRFPDPCGGPEGLREPEKASRPVQEQGGAKA TTK9HGZ TT Literature-reported TT2CJ75 ID TT2CJ75 TT2CJ75 TN Osteoclastogenesis inhibitory factor (TNFRSF11B) TT2CJ75 UP O00300 TT2CJ75 UC TR11B_HUMAN TT2CJ75 SN Tumor necrosis factor receptor superfamily member 11B; Osteoprotegerin; Osteoclastogenesis inhibitoryfactor; OPG; OCIF TT2CJ75 GN TNFRSF11B TT2CJ75 FC Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. TT2CJ75 PD 3URF TT2CJ75 SQ MNNLLCCALVFLDISIKWTTQETFPPKYLHYDEETSHQLLCDKCPPGTYLKQHCTAKWKTVCAPCPDHYYTDSWHTSDECLYCSPVCKELQYVKQECNRTHNRVCECKEGRYLEIEFCLKHRSCPPGFGVVQAGTPERNTVCKRCPDGFFSNETSSKAPCRKHTNCSVFGLLLTQKGNATHDNICSGNSESTQKCGIDVTLCEEAFFRFAVPTKFTPNWLSVLVDNLPGTKVNAESVERIKRQHSSQEQTFQLLKLWKHQNKDQDIVKKIIQDIDLCENSVQRHIGHANLTFEQLRSLMESLPGKKVGAEDIEKTIKACKPSDQILKLLSLWRIKNGDQDTLKGLMHALKHSKTYHFPKTVTQSLKKTIRFLHSFTMYKLYQKLFLEMIGNQVQSVKISCL TT2CJ75 TT Literature-reported TTBQFM7 ID TTBQFM7 TTBQFM7 TN Osteonectin (SPARC) TTBQFM7 UP P09486 TTBQFM7 UC SPRC_HUMAN TTBQFM7 SN Secreted protein acidic and rich in cysteine; ON; Basement-membrane protein 40; Basement membrane protein BM-40; BM-40 TTBQFM7 GN SPARC TTBQFM7 FC Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity. Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. TTBQFM7 PD 2V53; 1SRA; 1NUB; 1BMO TTBQFM7 SQ MRAWIFFLLCLAGRALAAPQQEALPDETEVVEETVAEVTEVSVGANPVQVEVGEFDDGAEETEEEVVAENPCQNHHCKHGKVCELDENNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIPPCLDSELTEFPLRMRDWLKNVLVTLYERDEDNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALDEWAGCFGIKQKDIDKDLVI TTBQFM7 TT Literature-reported TT8ME6I ID TT8ME6I TT8ME6I TN Osteopontin (SPP1) TT8ME6I UP P10451 TT8ME6I UC OSTP_HUMAN TT8ME6I SN Uropontin; Urinary stone protein; Secreted phosphoprotein 1; SPP-1; PSEC0156; OPN; Nephropontin; Bone sialoprotein 1; BNSP TT8ME6I GN SPP1 TT8ME6I FC Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Binds tightly to hydroxyapatite. TT8ME6I PD 3DSF; 3CXD TT8ME6I SQ MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN TT8ME6I TT Literature-reported TT1FE3L ID TT1FE3L TT1FE3L TN P2Y purinoceptor 13 (P2RY13) TT1FE3L UP Q9BPV8 TT1FE3L UC P2Y13_HUMAN TT1FE3L SN P2Y13; GPR94; GPR86; G-protein coupled receptor 94; G-protein coupled receptor 86; FKSG77 TT1FE3L GN P2RY13 TT1FE3L FC Receptor for ADP. Coupled to G(i)-proteins. May play a role in hematopoiesis and the immune system. TT1FE3L PD 2B6U TT1FE3L SQ MTAAIRRQRELSILPKVTLEAMNTTVMQGFNRSERCPRDTRIVQLVFPALYTVVFLTGILLNTLALWVFVHIPSSSTFIIYLKNTLVADLIMTLMLPFKILSDSHLAPWQLRAFVCRFSSVIFYETMYVGIVLLGLIAFDRFLKIIRPLRNIFLKKPVFAKTVSIFIWFFLFFISLPNTILSNKEATPSSVKKCASLKGPLGLKWHQMVNNICQFIFWTVFILMLVFYVVIAKKVYDSYRKSKSKDRKNNKKLEGKVFVVVAVFFVCFAPFHFARVPYTHSQTNNKTDCRLQNQLFIAKETTLFLAATNICMDPLIYIFLCKKFTEKLPCMQGRKTTASSQENHSSQTDNITLG TT1FE3L TT Literature-reported TT72OKI ID TT72OKI TT72OKI TN P2Y purinoceptor 14 (P2RY14) TT72OKI UP Q15391 TT72OKI UC P2Y14_HUMAN TT72OKI SN UDP-glucose receptor; P2Y14; KIAA0001; GPR105; G-protein coupled receptor 105 TT72OKI GN P2RY14 TT72OKI FC Receptor for UDP-glucose and other UDP-sugar coupled to G-proteins. Not activated by ATP, ADP, UTP or ATP. TT72OKI PD 2B6V TT72OKI SQ MINSTSTQPPDESCSQNLLITQQIIPVLYCMVFIAGILLNGVSGWIFFYVPSSKSFIIYLKNIVIADFVMSLTFPFKILGDSGLGPWQLNVFVCRVSAVLFYVNMYVSIVFFGLISFDRYYKIVKPLWTSFIQSVSYSKLLSVIVWMLMLLLAVPNIILTNQSVREVTQIKCIELKSELGRKWHKASNYIFVAIFWIVFLLLIVFYTAITKKIFKSHLKSSRNSTSVKKKSSRNIFSIVFVFFVCFVPYHIARIPYTKSQTEAHYSCQSKEILRYMKEFTLLLSAANVCLDPIIYFFLCQPFREILCKKLHIPLKAQNDLDISRIKRGNTTLESTDTL TT72OKI TT Literature-reported TT84EWY ID TT84EWY TT84EWY TN P2Y purinoceptor 8 (P2RY8) TT84EWY UP Q86VZ1 TT84EWY UC P2RY8_HUMAN TT84EWY BC GPCR rhodopsin TT84EWY SN P2Y8; P2RY8 TT84EWY GN P2RY8 TT84EWY FC Probable receptor for purines coupled to G-proteins. TT84EWY SQ MQVPNSTGPDNATLQMLRNPAIAVALPVVYSLVAAVSIPGNLFSLWVLCRRMGPRSPSVIFMINLSVTDLMLASVLPFQIYYHCNRHHWVFGVLLCNVVTVAFYANMYSSILTMTCISVERFLGVLYPLSSKRWRRRRYAVAACAGTWLLLLTALSPLARTDLTYPVHALGIITCFDVLKWTMLPSVAMWAVFLFTIFILLFLIPFVITVACYTATILKLLRTEEAHGREQRRRAVGLAAVVLLAFVTCFAPNNFVLLAHIVSRLFYGKSYYHVYKLTLCLSCLNNCLDPFVYYFASREFQLRLREYLGCRRVPRDTLDTRRESLFSARTTSVRSEAGAHPEGMEGATRPGLQRQESVF TT84EWY TT Literature-reported TTA4REJ ID TTA4REJ TTA4REJ TN Paired box protein Pax-5 (PAX5) TTA4REJ UP Q02548 TTA4REJ UC PAX5_HUMAN TTA4REJ SN PAX5; BSAP; B-cell specific transcription factor TTA4REJ GN PAX5 TTA4REJ FC May play an important role in b-cell differentiation as well as neural development and spermatogenesis. Involved in the regulation of the cd19 gene, a b-lymphoid-specific target gene. TTA4REJ PD 1MDM; 1K78 TTA4REJ SQ MDLEKNYPTPRTSRTGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAERVCDNDTVPSVSSINRIIRTKVQQPPNQPVPASSHSIVSTGSVTQVSSVSTDSAGSSYSISGILGITSPSADTNKRKRDEGIQESPVPNGHSLPGRDFLRKQMRGDLFTQQQLEVLDRVFERQHYSDIFTTTEPIKPEQTTEYSAMASLAGGLDDMKANLASPTPADIGSSVPGPQSYPIVTGRDLASTTLPGYPPHVPPAGQGSYSAPTLTGMVPGSEFSGSPYSHPQYSSYNDSWRFPNPGLLGSPYYYSAAARGAAPPAAATAYDRH TTA4REJ TT Literature-reported TTIFD98 ID TTIFD98 TTIFD98 TN Palmdelphin (PALMD) TTIFD98 UP Q9NP74 TTIFD98 UC PALMD_HUMAN TTIFD98 BC Paralemmin family TTIFD98 SN Paralemmin-like protein; PALML; C1orf11 TTIFD98 GN PALMD TTIFD98 FC cytoplasm. TTIFD98 SQ MEEAELVKGRLQAITDKRKIQEEISQKRLKIEEDKLKHQHLKKKALREKWLLDGISSGKEQEEMKKQNQQDQHQIQVLEQSILRLEKEIQDLEKAELQISTKEEAILKKLKSIERTTEDIIRSVKVEREERAEESIEDIYANIPDLPKSYIPSRLRKEINEEKEDDEQNRKALYAMEIKVEKDLKTGESTVLSSIPLPSDDFKGTGIKVYDDGQKSVYAVSSNHSAAYNGTDGLAPVEVEELLRQASERNSKSPTEYHEPVYANPFYRPTTPQRETVTPGPNFQERIKIKTNGLGIGVNESIHNMGNGLSEERGNNFNHISPIPPVPHPRSVIQQAEEKLHTPQKRLMTPWEESNVMQDKDAPSPKPRLSPRETIFGKSEHQNSSPTCQEDEEDVRYNIVHSLPPDINDTEPVTMIFMGYQQAEDSEEDKKFLTGYDGIIHAELVVIDDEEEEDEGEAEKPSYHPIAPHSQVYQPAKPTPLPRKRSEASPHENTNHKSPHKNSISLKEQEESLGSPVHHSPFDAQTTGDGTEDPSLTALRMRMAKLGKKVI TTIFD98 TT Literature-reported TT8SGZK ID TT8SGZK TT8SGZK TN Pancreas duodenum homeobox 1 (PDX1) TT8SGZK UP P52945 TT8SGZK UC PDX1_HUMAN TT8SGZK SN Somatostatin-transactivating factor 1; STF1; STF-1; Pancreas/duodenum homeobox protein 1; PDX-1; Islet/duodenum homeobox-1; Insulin upstream factor 1; Insulin promoter factor 1; IUF-1; IPF1; IPF-1; IDX-1; Glucose-sensitive factor; GSF TT8SGZK GN PDX1 TT8SGZK FC Activates insulin, somatostatin, glucokinase, islet amyloid polypeptide and glucose transporter type 2 gene transcription. Particularly involved in glucose-dependent regulation of insulin gene transcription. As part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Binds preferentially the DNA motif 5'-[CT]TAAT[TG]-3'. During development, specifies the early pancreatic epithelium, permitting its proliferation, branching and subsequent differentiation. At adult stage, required for maintaining the hormone-producing phenotype of the beta-cell. TT8SGZK PD 6F8F TT8SGZK SQ MNGEEQYYAATQLYKDPCAFQRGPAPEFSASPPACLYMGRQPPPPPPHPFPGALGALEQGSPPDISPYEVPPLADDPAVAHLHHHLPAQLALPHPPAGPFPEGAEPGVLEEPNRVQLPFPWMKSTKAHAWKGQWAGGAYAAEPEENKRTRTAYTRAQLLELEKEFLFNKYISRPRRVELAVMLNLTERHIKIWFQNRRMKWKKEEDKKRGGGTAVGGGGVAEPEQDCAVTSGEELLALPPPPPPGGAVPPAAPVAAREGRLPPGLSASPQPSSVAPRRPQEPR TT8SGZK TT Literature-reported TTA258K ID TTA258K TTA258K TN Parainfluenza Hemagglutinin-neuraminidase glycoprotein (HPIV HN) TTA258K UP P16071 TTA258K UC HN_PI1HW TTA258K SN Hemagglutinin-neuraminidase TTA258K GN HPIV HN TTA258K FC Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity). TTA258K EC EC 3.2.1.18 TTA258K SQ MAEKGKTNSSYWSTTRNDNSTVNTYIDTPAGKTHIWLLIATTMHTILSFIIMILCIDLIIKQDTCMKTNIMTVSSMNESAKTIKETITELIRQEVISRTINIQSSVQSGIPILLNKQSRDLTQLIEKSCNRQELAQICENTIAIHHADGISPLDPHDFWRCPVGEPLLSNNPNISLLPGPSLLSGSTTISGCVRLPSLSIGDAIYAYSSNLITQGCADIGKSYQVLQLGYISLNSDMYPDLKPVISHTYDINDNRKSCSVIAAGTRGYQLCSLPTVNETTDYSSEGIEDLVFDILDLKGKTKSHRYKNEDITFDHPFSAMYPSVGSGIKIENTLIFLGYGGLTTPLQGDTKCVTNRCANVNQSVCNDALKITWLKKRQVVNVLIRINNYLSDRPKIVVETIPITQNYLGAEGRLLKLGKKIYIYTRSSGWHSHLQIGSLDINNPMTIKWAPHEVLSRPGNQDCNWYNRCPRECISGVYTDAYPLSPDAVNVATTTLYANTSRVNPTIMYSNTSEIINMLRLKNVQLEAAYTTTSCITHFGKGYCFHIVEINQTSLNTLQPMLFKTSIPKICKITS TTA258K TT Literature-reported TTYSRXM ID TTYSRXM TTYSRXM TN Pattern recognition receptor NOD1 (NOD1) TTYSRXM UP Q9Y239 TTYSRXM UC NOD1_HUMAN TTYSRXM SN Nucleotide-binding oligomerization domain-containing protein 1; Caspase recruitment domain-containing protein 4; CARD4 TTYSRXM GN NOD1 TTYSRXM FC Induces NF-kappa-B activity via RIPK2 and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS). Forms an intracellular sensing system along with ARHGEF2 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIPK2 dependent NF-kappa-B signaling pathway activation upon S. flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides but also in the activation of NF-kappa-B by Shigella effector proteins IpgB2 and OspB. Recruits NLRP10 to the cell membrane following bacterial infection. Enhances caspase-9-mediated apoptosis. TTYSRXM PD 4JQW; 4E9M; 2NZ7; 2NSN; 2DBD TTYSRXM SQ MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAYARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRGYLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAKVYEDEKRIICF TTYSRXM TT Literature-reported TTH9LDP ID TTH9LDP TTH9LDP TN PC4 and SFRS1-interacting protein (PSIP1) TTH9LDP UP O75475 TTH9LDP UC PSIP1_HUMAN TTH9LDP SN Transcriptional coactivator p75/p52; PSIP2; Lens epithelium-derived growth factor; LEDGF; Dense fine speckles 70 kDa protein; DFS70; DFS 70; CLL-associated antigen KW-7 TTH9LDP GN PSIP1 TTH9LDP FC Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis. Isoform 2 is a more general and stronger transcriptional coactivator. Isoform 2 may also act as an adapter to coordinate pre-mRNA splicing. Cellular cofactor for lentiviral integration. TTH9LDP PD 6EMR; 6EMQ; 6EMP; 6EMO; 5YI9 TTH9LDP SQ MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQAATKQSNASSDVEVEEKETSVSKEDTDHEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVETEEAGVVTTATASVNLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN TTH9LDP TT Patented-recorded TTDTBLM ID TTDTBLM TTDTBLM TN PDZ domain containing-protein (PDZK1) TTDTBLM UP O60450 TTDTBLM UC NHRF3_HUMAN TTDTBLM SN Sodium-hydrogen exchanger regulatory factor 3; PDZD1; PDZ domain-containing protein 1; NaPi-Cap1; Na/Pi cotransporter C-terminal-associated protein 1; Na(+)/H(+) exchanger regulatory factor 3; Na(+)/H(+) exchange regulatory cofactor NHE-RF3; NHERF3; NHERF-3; Multi-PDZ domain containing adaptor protein; CFTR-associated protein of 70 kDa; CAP70 TTDTBLM GN PDZK1 TTDTBLM FC May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. Required for normal cell-surface expression of SCARB1. Plays a role in maintaining normal plasma cholesterol levels via its effects on SCARB1. Plays a role in the normal localization and function of the chloride-anion exchanger SLC26A6 to the plasma membrane in the brush border of the proximal tubule of the kidney. May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function. A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. TTDTBLM PD 6EZI; 4Q2P; 3TMH; 2VSP; 2EEJ TTDTBLM SQ MTSTFNPRECKLSKQEGQNYGFFLRIEKDTEGHLVRVVEKCSPAEKAGLQDGDRVLRINGVFVDKEEHMQVVDLVRKSGNSVTLLVLDGDSYEKAVKTRVDLKELGQSQKEQGLSDNILSPVMNGGVQTWTQPRLCYLVKEGGSYGFSLKTVQGKKGVYMTDITPQGVAMRAGVLADDHLIEVNGENVEDASHEEVVEKVKKSGSRVMFLLVDKETDKRHVEQKIQFKRETASLKLLPHQPRIVEMKKGSNGYGFYLRAGSEQKGQIIKDIDSGSPAEEAGLKNNDLVVAVNGESVETLDHDSVVEMIRKGGDQTSLLVVDKETDNMYRLAHFSPFLYYQSQELPNGSVKEAPAPTPTSLEVSSPPDTTEEVDHKPKLCRLAKGENGYGFHLNAIRGLPGSFIKEVQKGGPADLAGLEDEDVIIEVNGVNVLDEPYEKVVDRIQSSGKNVTLLVCGKKAYDYFQAKKIPIVSSLADPLDTPPDSKEGIVVESNHDSHMAKERAHSTASHSSSNSEDTEM TTDTBLM TT Literature-reported TTKZ864 ID TTKZ864 TTKZ864 TN Pepsinogen-5 (PGA5) TTKZ864 UP P0DJD9 TTKZ864 UC PEPA5_HUMAN TTKZ864 SN Pepsin A-5 TTKZ864 GN PGA5 TTKZ864 FC Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. TTKZ864 EC EC 3.4.23.1 TTKZ864 SQ MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWEAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDKSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGETIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNVPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA TTKZ864 TT Literature-reported TT8ALTZ ID TT8ALTZ TT8ALTZ TN Periostin (POSTN) TT8ALTZ UP Q15063 TT8ALTZ UC POSTN_HUMAN TT8ALTZ SN POSTN; PN; Osteoblastspecific factor 2 TT8ALTZ GN POSTN TT8ALTZ FC Enhances incorporation of BMP1 in the fibronectin matrix ofconnective tissues, and subsequent proteolytic activation of lysyl oxidase LOX. Induces cell attachment and spreading and plays a role in cell adhesion. May play a role in extracellular matrix mineralization. {ECO:0000250, ECO:0000269|PubMed:12235007, ECO:0000269|PubMed:18450759}. TT8ALTZ PD 5YJH; 5YJG; 5WT7 TT8ALTZ SQ MIPFLPMFSLLLLLIVNPINANNHYDKILAHSRIRGRDQGPNVCALQQILGTKKKYFSTCKNWYKKSICGQKTTVLYECCPGYMRMEGMKGCPAVLPIDHVYGTLGIVGATTTQRYSDASKLREEIEGKGSFTYFAPSNEAWDNLDSDIRRGLESNVNVELLNALHSHMINKRMLTKDLKNGMIIPSMYNNLGLFINHYPNGVVTVNCARIIHGNQIATNGVVHVIDRVLTQIGTSIQDFIEAEDDLSSFRAAAITSDILEALGRDGHFTLFAPTNEAFEKLPRGVLERIMGDKVASEALMKYHILNTLQCSESIMGGAVFETLEGNTIEIGCDGDSITVNGIKMVNKKDIVTNNGVIHLIDQVLIPDSAKQVIELAGKQQTTFTDLVAQLGLASALRPDGEYTLLAPVNNAFSDDTLSMDQRLLKLILQNHILKVKVGLNELYNGQILETIGGKQLRVFVYRTAVCIENSCMEKGSKQGRNGAIHIFREIIKPAEKSLHEKLKQDKRFSTFLSLLEAADLKELLTQPGDWTLFVPTNDAFKGMTSEEKEILIRDKNALQNIILYHLTPGVFIGKGFEPGVTNILKTTQGSKIFLKEVNDTLLVNELKSKESDIMTTNGVIHVVDKLLYPADTPVGNDQLLEILNKLIKYIQIKFVRGSTFKEIPVTVYTTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPEFRLIKEGETITEVIHGEPIIKKYTKIIDGVPVEITEKETREERIITGPEIKYTRISTGGGETEETLKKLLQEEVTKVTKFIEGGDGHLFEDEEIKRLLQGDTPVRKLQANKKVQGSRRRLREGRSQ TT8ALTZ TT Literature-reported TTRPJQ1 ID TTRPJQ1 TTRPJQ1 TN Phospholipase C-gamma (PPCG) TTRPJQ1 UP P19174; P16885 TTRPJQ1 UC PLCG1_HUMAN; PLCG2_HUMAN TTRPJQ1 BC Phosphoric diester hydrolase TTRPJQ1 SN Phospholipase C gamma; Phosphoinositide phospholipase C-gamma; PLC-gamma; PLC; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma TTRPJQ1 GN PLCG1; PLCG2 TTRPJQ1 FC Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration. TTRPJQ1 SQ MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRAGERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVTFLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQYFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSSSTELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLWFPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSISMASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCAISIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDLELASLLIKIDIFPAKENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFEDFRISQEHLADHFDSRERRAPRRTRVNGDNRL TTRPJQ1 TT Literature-reported TTZF6SN ID TTZF6SN TTZF6SN TN Phospholipid transfer protein (PLTP) TTZF6SN UP P55058 TTZF6SN UC PLTP_HUMAN TTZF6SN BC Bactericidal permeability increasing protein TTZF6SN SN Plasma phospholipid transfer protein; Lipid transfer protein II; Lipid II precursor TTZF6SN GN PLTP TTZF6SN FC Essential for the transfer of excess surface lipids from triglyceride-rich lipoproteins to HDL, thereby facilitating the formation of smaller lipoprotein remnants, contributing to the formation of LDL, and assisting in the maturation of HDL particles. PLTP also plays a key role in the uptake of cholesterol from peripheral cells and tissues that is subsequently transported to the liver for degradation and excretion. Two distinct forms of PLTP exist in plasma: an active form that can transfer PC from phospholipid vesicles to high-density lipoproteins (HDL), and an inactive form that lacks this capability. Facilitates the transfer of a spectrum of different lipid molecules, including diacylglycerol, phosphatidic acid, sphingomyelin, phosphatidylcholine, phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine. TTZF6SN SQ MALFGALFLALLAGAHAEFPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGHFYYNISEVKVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFFYDGGYINASAEGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFKKVYDFLSTFITSGMRFLLNQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLMKDPVASTSNLDMDFRGAFFPLTERNWSLPNRAVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALQLLLVGDKVPHDLDMLLRATYFGSIVLLSPAVIDSPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQPEVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQIGVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLREVIEKNRPADVRASTAPTPSTAAV TTZF6SN TT Literature-reported TTZF6SN FM Bactericidal permeability increasing protein TTWM461 ID TTWM461 TTWM461 TN Phosphorylated GluA2 (pGluA2) TTWM461 UP P42262 (phosphorylated) TTWM461 UC GRIA2_HUMAN TTWM461 SN Glutamate receptor ionotropic, AMPA 2 (phosphorylated); Glutamate receptor 2 (phosphorylated); GluR-K2 (phosphorylated); GluR-B (phosphorylated); GluR-2 (phosphorylated); GluA2 (phosphorylated); GLUR2 (phosphorylated); AMPA-selective glutamate receptor 2 (phosphorylated) TTWM461 GN GRIA2 TTWM461 FC Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity). TTWM461 PD 5ZG3; 5ZG2; 5ZG1; 5ZG0; 5YBG TTWM461 SQ MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDEMYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI TTWM461 TT Literature-reported TTF1Z4J ID TTF1Z4J TTF1Z4J TN Plasmodium Apicoplast ribosome (Malaria RPL18) TTF1Z4J UP Q6LFD5 TTF1Z4J UC RK18_PLAF7 TTF1Z4J BC Ribosomal protein TTF1Z4J SN Putative 50S ribosomal protein L18, apicoplastic TTF1Z4J GN Malaria RPL18 TTF1Z4J FC Has a unique composition, resulting from the loss of several large and small subunit proteins accompanied by significant sequence and size divergences in parasite orthologues of ribosomal proteins. Many more ribosomal proteins with apicoplast and mitochondrial targeting sequences that are post-translationally processed for targeting to organelles. TTF1Z4J SQ MYISFILFSIIFIFLGVIENFIINKRVLYKPNFLLYSEKKNKKKSTPEQVTTRVNKDLKEKKRKRPRSKILECLLKEKVEKVEKVEKNSDENQCSNVDKEIREGKRVPRLRVRNTNNHIYASIIDDYKKYVLCSTCSRDATLSKILGTYRRKATNRVINNGRTIKSAWEIGKIIGKKALSKGIFKVRFDRARHPYAGKVEALAEGARAVGLLL TTF1Z4J TT Literature-reported TTCS8WB ID TTCS8WB TTCS8WB TN Plasmodium Choline transporter (Malaria CT) TTCS8WB UP Q8I5S7 TTCS8WB UC Q8I5S7_PLAF7 TTCS8WB SN Glycerol-3-phosphate 1-O-acyltransferase TTCS8WB GN Malaria CT TTCS8WB FC Mediates the delivery of these compounds to the intracellular parasite TTCS8WB EC EC 2.3.1.15 TTCS8WB SQ MPDFYFLIRWLCKVIVKSVFRDVNVINPENVPLYGSVIFVGNHNNQFIDACVLIANIPRQVKFIVAEKSMRRAVIGKLASVIGCISVKRPQDLKFKGIGHICWNEGDVKITGINTRFRLDVQIGDKLLIQNKMFPVVKIESETELLIQEVINIECEDKMNGVPFKIIPKINQTEVYNLVTNSLKNGDTIGIFPEGGSHDRTNLLPLKPGVAIMTLCALADGIEDVSIIPVGLSYSKLYQLQGCATLFYGNAIIISQDLCKEYNNNNREAISKLLSKIEEGMRSCMLTSKDHETSRCIELCVSLYTPERMTISKNKIYNNLQLFCKMFWKFGNSKVIENLSYELKCYEKLLQANKIKDDEVWMLKQSTSAATLKFIEHICTFIFCVIFGMTFSLLWLPLVLISIYLAERHRKAALRNSTIKIQGGDVVSSYKVLVLIVLLPTFNIVYGLLFSIYLYHSWLKRILFVFLSMCILPICYYINLNYAVQIPSLLRQMKILLKVICGKINVWRDNERELISTRHELQLKVRDLVSTLGPDVSDDFLEQLYRNIPKFVVDVDTKRLIRGKDEFLPILQRSQLEYKEEIL TTCS8WB TT Literature-reported TTT4WBH ID TTT4WBH TTT4WBH TN Plasmodium Folylpolyglutamate synthase (Malaria dhfs-fpgs) TTT4WBH UP Q9U738 TTT4WBH UC Q9U738_PLAFA TTT4WBH BC Carbon-nitrogen ligase TTT4WBH SN dhfs-fpgs; Folylpolyglutamate synthetase; Folylpoly-gamma-glutamate synthetase; FPGS TTT4WBH GN Malaria dhfs-fpgs TTT4WBH FC Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Unsubstitued reduced folates are the preferred substrates. Metabolizes methotrexate (MTX) to polyglutamates. TTT4WBH SQ MEKNQNDKSNKNDIIHMNDKSGNYDKNNINNFIDKNDEHDMSDILHKINNEEKKYEEIKSYSECLELLYKTHALKLGLDNPKKLNESFGHPCDKYKTIHIAGTNGKGSVCYKIYTCLKIKKFKVGLFSSPHIFSLRERIIVNDEPISEKELIHLVNEVLNKAKKLYINPSFFEIITLVAFLHFLNKKVDYAIIETGIGGRLDATNILTKPEVIVITSIGYDHLNILGDNLPIICNEKIGIFKKDANVVIGPSVAIYKNVFDKAKELNCTIHTVVPEPRGERYNEENSRIALRTLEILNISIDYFLKSIIPIKPPLRIQYLATEQIQHIKKKFSPDNLEHNVQYPLAVILDVGHNETAIDRLCTDINYFHKGQNIRICISITKPRNLSVFHPFIAQFGDTLKDIFYLPSLNERTYDFEEIVEMLNNEEEIKNEIKELILSSSKKVGKWLAHEKQGNINEEDALKLYKRGCIPLIIKNAFLECCKDNSILLVCGTFFVFDEVLNVFDIHSDMQDTIFMNEPSLV TTT4WBH TT Literature-reported TTOY91U ID TTOY91U TTOY91U TN Plasmodium Hypoxanthine-guanine-xanthine phosphoribosyltransferase (Malaria LACZ) TTOY91U UP P07833 TTOY91U UC HGXR_PLAFK TTOY91U BC Pentosyltransferase TTOY91U SN LACZ of Plasmodium falciparum (isolate K1 / Thailand); HGXPRTase; HGXPRT; HGPRT of Plasmodium falciparum (isolate K1 / Thailand) TTOY91U GN Malaria LACZ TTOY91U FC Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5- phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Works with guanine, hypoxanthine and xanthine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway. TTOY91U SQ MPIPNNPGAGENAFDPVFVKDDDGYDLDSFMIPAHYKKYLTKVLVPNGVIKNRIEKLAYDIKKVYNNEEFHILCLLKGSRGFFTALLKHLSRIHNYSAVEMSKPLFGEHYVRVKSYCNDQSTGTLEIVSEDLSCLKGKHVLIVEDIIDTGKTLVKFCEYLKKFEIKTVAIACLFIKRTPLWNGFKADFVGFSIPDHFVVGYSLDYNEIFRDLDHCCLVNDEGKKKYKATSL TTOY91U TT Literature-reported TT7PLWT ID TT7PLWT TT7PLWT TN Plasmodium Plasmepsin 5 (Malaria PLA5) TT7PLWT UP Q8I6Z5 TT7PLWT UC Q8I6Z5_PLAF7 TT7PLWT SN Plasmepsin V TT7PLWT GN Malaria PLA5 TT7PLWT FC endoplasmic reticulum, integral component of membrane, aspartic-type endopeptidase activity, protein catabolic process, proteolysis TT7PLWT EC EC 3.4.23.- TT7PLWT SQ MNNYFLRKENFFILFCFVFVSIFFVSNVTIIKCNNVENKIDNVGKKIENVGKKIGDMENKNDNVENKNDNVGNKNDNVKNASSDLYKYKLYGDIDEYAYYFLDIDIGKPSQRISLILDTGSSSLSFPCNGCKDCGIHMEKPYNLNYSKTSSILYCNKSNCPYGLKCVGNKCEYLQSYCEGSQIYGFYFSDIVTLPSYNNKNKISFEKLMGCHMHEESLFLHQQATGVLGFSLTKPNGVPTFVDLLFKHTPSLKPIYSICVSEHGGELIIGGYEPDYFLSNQKEKQKMDKSDNNSSNKGNVSIKLKNNDKNDDEENNSKDVIVSNNVEDIVWQAITRKYYYYIKIYGLDLYGTNIMDKKELDMLVDSGSTFTHIPENIYNQINYYLDILCIHDMTNIYEINKRLKLTNESLNKPLVYFEDFKTALKNIIQNENLCIKIVDGVQCWKSLENLPNLYITLSNNYKMIWKPSSYLYKKESFWCKGLEKQVNNKPILGLTFFKNKQVIFDLQQNQIAFIESKCPSNLTSSRPRTFNEYREKENIFLKVSYINLYCLWLLLALTILLSLILYVRKMFYMDYFPLSDQNKSPIQEST TT7PLWT TT Literature-reported TT7UPN3 ID TT7UPN3 TT7UPN3 TN Plasmodium Subtilisin-like protease (Malaria sub-1) TT7UPN3 UP O61142 TT7UPN3 UC O61142_PLAFA TT7UPN3 BC Protease TT7UPN3 SN Subtilisin-like protease TT7UPN3 GN Malaria sub-1 TT7UPN3 FC Plays a dual role at the blood stage by enabling egress of the progeny merozoites from the infected erythrocyte and priming merozoites for subsequent erythrocyte invasion. TT7UPN3 SQ MMLNKKVVALCTLTLHLFCIFLCLGKEVRSEENGKIQDDAKKIVSELRFLEKVEDVIEKSNIGGNEVDADENSFNPDTEVPIEEIEEIKMRELKDVKEEKNKNDNHNNNNNNNNISSSSSSSSNTFGEEKEEVSKKKKKLRLIVSENHATTPSFFQESLLEPDVLSFLESKGNLSNLKNINSMIIELKEDTTDDELISYIKILEEKGALIESDKLVSADNIDISGIKDAIRRGEENIDVNDYKSMLEVENDAEDYDKMFGMFNESHAATSKRKRHSTNERGYDTFSSPSYKTYSKSDYLYDDDNNNNNYYYSHSSNGHNSSSRNSSSSRSRPGKYHFNDEFRNLQWGLDLSRLDETQELINEHQVMSTRICVIDSGIDYNHPDLKDNIELNLKELHGRKGFDDDNNGIVDDIYGANFVNNSGNPMDDNYHGTHVSGIISAIGNNNIGVVGVDVNSKLIICKALDEHKLGRLGDMFKCLDYCISRNAHMINGSFSFDEYSGIFNSSVEYLQRKGILFFVSASNCSHPKSSTPDIRKCDLSINAKYPPILSTVYDNVISVANLKKNDNNNHYSLSINSFYSNKYCQLAAPGTNIYSTAPHNSYRKLNGTSMAAPHVAAIASLIFSINPDLSYKKVIQILKDSIVYLPSLKNMVAWAGYADINKAVNLAIKSKKTYINSNISNKWKKKSRYLH TT7UPN3 TT Literature-reported TT3B9JV ID TT3B9JV TT3B9JV TN Plasmodium Subtilisin-like protease 2 (Malaria sub2) TT3B9JV UP Q9NG20 TT3B9JV UC Q9NG20_PLABE TT3B9JV BC Protease TT3B9JV SN Subtilisin-like protease 2 TT3B9JV GN Malaria sub2 TT3B9JV FC Essential for red cell invasion. TT3B9JV SQ MLRTFYVLSLMLIEFILHNGQYNKHICSKNSKKYNFVGKKHRILVSDIEDRENHIEGIADIYKPIFNIYEISAEFHKKKNIADKKKKRKYGINQSIEKRRIAEENERRQLNKTEGTQFLELSNRYPNIGKQNSQQNKVNEINNQNAASNSNDNIGNDNIGNDNIGNDEDDDEDDDEDLIEGRKDNLEEDDLIEKNDSNLPRGKMHEKEEKNKNINTTPGNESSNKNVNDKKKNGISLKDKIDNKQNNGGLKEKGNNLDDNIKTYTFDHYKIITNSDNILNDIKVDASDISKLSINSINIEYNEKNKAEYTHQRHIVLSNNGNRRYKIFLMTKNPKFTKTEDIEEPGMSFIQTETGENEDEKEDEENYLNENLYSGFGTIDYENDYSKKKKKIESEHASGLNDKISNSQNIEKSGSHENEKYNHGYIEKIRSFFSFLSMPSSKKDDSIGSEKKTEERSNTDSKAKLNKKTNDMAKKNNSNAFLSVDKIIDQYLLNLKNKNMKEQELIFIFHGNLDLHSKEMKTVINEANAKFTKYINMHFKDVKNIRYDISSPINFVCFFIPIIFDMSNLKILKEALIILNNELKDYIDNWNFSNTYVAFDNNYENEDIDNVMNKLNENMEKYIKKPKKLYNIKYSFLRKIWGLKSIISLSKNQDKKDAEIEEKILSALPKELKEYSTWNLSFIRVFNAWLLSGYGNKNVKICVIDSGIDKNHIDLANNIYTPKYSDRYEMTDELFDFMVKNPIDTSGHGTHVSGIAAASANSLGMVGVAPNINLISLRFIDGDNYGGSFHVIKAINICILNKSPIINASWGSRNYDTNMFLAIERLKYTFKGKGTVFIAAAGNENKNNDLYPIYPASYKLQNVYSVGSINKFLQISPFSNYGANSVHILAPGHHIYSTTPMNTYKMNTGTSMAAPHVSGVAGLIYSVCYKQGFIPDADEVLEIITRTSIKIVSKDKKTIHNSLINAEAAVLTTLLGGLWIQMDCHFAKFYLNENKQKSVPIVFSAYKDGVYESDIIIGIQPEDANSKEYGEIVIPIKILTNPKLKDFSLSPRVGKKIRIDENESNDDILSYICENALYNLYEHDNSFLISSLILFFIGIILIVLASIVFFLKHHQSKQRDGEKYMHQKMVDRTYNVKYNFKDSGTDGIKRINTLDDNINNHRNTQRFTIVQNEDNMYVLKKKSSIQAKYEPRNELVKRSLVKRPIVKHADINVNFSNVDVLYEPKNNSSE TT3B9JV TT Literature-reported TTN8WFB ID TTN8WFB TTN8WFB TN Plasmodium Trophozoite cysteine proteinase (Malaria TCP) TTN8WFB UP P25805 TTN8WFB UC CYSP_PLAFA TTN8WFB SN Trophozoite cysteine proteinase; TCP TTN8WFB GN Malaria TCP TTN8WFB FC Probably degrades erythrocyte hemoglobin. TTN8WFB EC EC 3.4.22.- TTN8WFB SQ MVAIKEMKELAFARPSLVETLNKKKKFLKKKEKRTFVLSIYAFITFIIFCIGILYFTNKSSAHNNNNNKNEHSLKKEEIELLRVLLEKYKKQKDGILNESSNEEDEEKYTLNSETYNNKNNVSNIKNDSIKSKKEEYINLERILLEKYKKFINENNEENRKELSNILHKLLEINKLILREEKDDKKVYLINDNYDEKGALEIGMNEEMKYKKEDPINNIKYASKFFKFMKEHNKVYKNIDEQMRKFEIFKINYISIKNHNKLNKNAMYKKKVNQFSDYSEEELKEYFKTLLHVPNHMIEKYSKPFENHLKDNILISEFYTNGKRNEKDIFSKVPEILDYREKGIVHEPKDQGLCGSCWAFASVGNIESVFAKKNKNILSFSEQEVVDCSKDNFGCDGGHPFYSFLYVLQNELCLGDEYKYKAKDDMFCLNYRCKRKVSLSSIGAVKENQLILALNEVGPLSVNVGVNNDFVAYSEGVYNGTCSEELNHSVLLVGYGQVEKTKLNYNNKIQTYNTKENSNQPDDNIIYYWIIKNSWSKKWGENGFMRLSRNKNGDNVFCGIGEEVFYPIL TTN8WFB TT Literature-reported TT4EZB2 ID TT4EZB2 TT4EZB2 TN Platelet endothelial cell adhesion molecule (PECAM1) TT4EZB2 UP P16284 TT4EZB2 UC PECA1_HUMAN TT4EZB2 SN PECAM-1; PECA1; GPIIA'; EndoCAM; ECAM; CD31 antigen; CD31 TT4EZB2 GN PECAM1 TT4EZB2 FC Tyr-690 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions. Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils. Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal. Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes. Modulates bradykinin receptor BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells. Induces susceptibility to atherosclerosis. Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. TT4EZB2 PD 5GNI; 5C14; 2KY5 TT4EZB2 SQ MQPRWAQGATMWLGVLLTLLLCSSLEGQENSFTINSVDMKSLPDWTVQNGKNLTLQCFADVSTTSHVKPQHQMLFYKDDVLFYNISSMKSTESYFIPEVRIYDSGTYKCTVIVNNKEKTTAEYQVLVEGVPSPRVTLDKKEAIQGGIVRVNCSVPEEKAPIHFTIEKLELNEKMVKLKREKNSRDQNFVILEFPVEEQDRVLSFRCQARIISGIHMQTSESTKSELVTVTESFSTPKFHISPTGMIMEGAQLHIKCTIQVTHLAQEFPEIIIQKDKAIVAHNRHGNKAVYSVMAMVEHSGNYTCKVESSRISKVSSIVVNITELFSKPELESSFTHLDQGERLNLSCSIPGAPPANFTIQKEDTIVSQTQDFTKIASKSDSGTYICTAGIDKVVKKSNTVQIVVCEMLSQPRISYDAQFEVIKGQTIEVRCESISGTLPISYQLLKTSKVLENSTKNSNDPAVFKDNPTEDVEYQCVADNCHSHAKMLSEVLRVKVIAPVDEVQISILSSKVVESGEDIVLQCAVNEGSGPITYKFYREKEGKPFYQMTSNATQAFWTKQKASKEQEGEYYCTAFNRANHASSVPRSKILTVRVILAPWKKGLIAVVIIGVIIALLIIAAKCYFLRKAKAKQMPVEMSRPAVPLLNSNNEKMSDPNMEANSHYGHNDDVRNHAMKPINDNKEPLNSDVQYTEVQVSSAESHKDLGKKDTETVYSEVRKAVPDAVESRYSRTEGSLDGT TT4EZB2 TT Literature-reported TT4EZB2 FM Transmembrane protein TTOABM9 ID TTOABM9 TTOABM9 TN Platelet-derived growth factor C (PDGFC) TTOABM9 UP Q9NRA1 TTOABM9 UC PDGFC_HUMAN TTOABM9 BC Growth factor TTOABM9 SN VEGF-E; UNQ174/PRO200; Spinal cord-derived growth factor; SCDGF; PDGF-C; Fallotein TTOABM9 GN PDGFC TTOABM9 FC Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function. TTOABM9 SQ MSLFGLLLLTSALAGQRQGTQAESNLSSKFQFSSNKEQNGVQDPQHERIITVSTNGSIHSPRFPHTYPRNTVLVWRLVAVEENVWIQLTFDERFGLEDPEDDICKYDFVEVEEPSDGTILGRWCGSGTVPGKQISKGNQIRIRFVSDEYFPSEPGFCIHYNIVMPQFTEAVSPSVLPPSALPLDLLNNAITAFSTLEDLIRYLEPERWQLDLEDLYRPTWQLLGKAFVFGRKSRVVDLNLLTEEVRLYSCTPRNFSVSIREELKRTDTIFWPGCLLVKRCGGNCACCLHNCNECQCVPSKVTKKYHEVLQLRPKTGVRGLHKSLTDVALEHHEECDCVCRGSTGG TTOABM9 TT Literature-reported TTSN0GA ID TTSN0GA TTSN0GA TN Platelet-derived growth factor D (PDGFD) TTSN0GA UP Q9GZP0 TTSN0GA UC PDGFD_HUMAN TTSN0GA BC Growth factor TTSN0GA SN Spinal cordderived growth factor B; SCDGFB; Plateletderived growth factor D, receptorbinding form; PDGFD receptorbinding form; PDGFD latent form; PDGFD; Irisexpressed growth factor TTSN0GA GN PDGFD TTSN0GA FC Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix. TTSN0GA SQ MHRLIFVYTLICANFCSCRDTSATPQSASIKALRNANLRRDESNHLTDLYRRDETIQVKGNGYVQSPRFPNSYPRNLLLTWRLHSQENTRIQLVFDNQFGLEEAENDICRYDFVEVEDISETSTIIRGRWCGHKEVPPRIKSRTNQIKITFKSDDYFVAKPGFKIYYSLLEDFQPAAASETNWESVTSSISGVSYNSPSVTDPTLIADALDKKIAEFDTVEDLLKYFNPESWQEDLENMYLDTPRYRGRSYHDRKSKVDLDRLNDDAKRYSCTPRNYSVNIREELKLANVVFFPRCLLVQRCGGNCGCGTVNWRSCTCNSGKTVKKYHEVLQFEPGHIKRRGRAKTMALVDIQLDHHERCDCICSSRPPR TTSN0GA TT Literature-reported TTCDZMO ID TTCDZMO TTCDZMO TN Pleckstrin homology domain-containing A5 (PLEKHA5) TTCDZMO UP Q9HAU0 TTCDZMO UC PKHA5_HUMAN TTCDZMO SN Pleckstrin homology domain-containing family A member 5; Phosphoinositol 3-phosphate-binding protein 2; PH domain-containing family A member 5; PEPP2; PEPP-2; KIAA1686 TTCDZMO GN PLEKHA5 TTCDZMO FC Involved in the mechanism of CNS homing of metastatic disease. Functions as a regulator of brain metastasis in melanoma. TTCDZMO PD 2DKP TTCDZMO SQ MAADLNLEWISLPRSWTYGITRGGRVFFINEEAKSTTWLHPVTGEAVVTGHRRQSTDLPTGWEEAYTFEGARYYINHNERKVTCKHPVTGQPSQDNCIFVVNEQTVATMTSEEKKERPISMINEASNYNVTSDYAVHPMSPVGRTSRASKKVHNFGKRSNSIKRNPNAPVVRRGWLYKQDSTGMKLWKKRWFVLSDLCLFYYRDEKEEGILGSILLPSFQIALLTSEDHINRKYAFKAAHPNMRTYYFCTDTGKEMELWMKAMLDAALVQTEPVKRVDKITSENAPTKETNNIPNHRVLIKPEIQNNQKNKEMSKIEEKKALEAEKYGFQKDGQDRPLTKINSVKLNSLPSEYESGSACPAQTVHYRPINLSSSENKIVNVSLADLRGGNRPNTGPLYTEADRVIQRTNSMQQLEQWIKIQKGRGHEEETRGVISYQTLPRNMPSHRAQIMARYPEGYRTLPRNSKTRPESICSVTPSTHDKTLGPGAEEKRRSMRDDTMWQLYEWQQRQFYNKQSTLPRHSTLSSPKTMVNISDQTMHSIPTSPSHGSIAAYQGYSPQRTYRSEVSSPIQRGDVTIDRRHRAHHPKHVYVPDRRSVPAGLTLQSVSPQSLQGKTLSQDEGRGTLYKYRPEEVDIDAKLSRLCEQDKVVHALEEKLQQLHKEKYTLEQALLSASQEIEMHADNPAAIQTVVLQRDDLQNGLLSTCRELSRATAELERAWREYDKLEYDVTVTRNQMQEQLDHLGEVQTESAGIQRAQIQKELWRIQDVMEGLSKHKQQRGTTEIGMIGSKPFSTVKYKNEGPDYRLYKSEPELTTVAEVDESNGEEKSEPVSEIETSVVKGSHFPVGVVPPRAKSPTPESSTIASYVTLRKTKKMMDLRTERPRSAVEQLCLAESTRPRMTVEEQMERIRRHQQACLREKKKGLNVIGASDQSPLQSPSNLRDNPFRTTQTRRRDDKELDTAIRENDVKPDHETPATEIVQLKETEPQNVDFSKELKKTENISYEMLFEPEPNGVNSVEMMDKERNKDKMPEDVTFSPQDETQTANHKPEEHPEENTKNSVDEQEETVISYESTPEVSRGNQTMAVKSLSPSPESSASPVPSTQPQLTEGSHFMCV TTCDZMO TT Literature-reported TTA9EJK ID TTA9EJK TTA9EJK TN Pleiotrophin (PTN) TTA9EJK UP P21246 TTA9EJK UC PTN_HUMAN TTA9EJK SN Osteoblast-specific factor 1; Osteoblast specific factor 1; OSF-1; NEGF1; Heparin-binding neurite outgrowth-promoting factor 1; Heparin-binding neurite outgrowth-promoting factor; Heparin-binding neurite outgrowth promoting factor 1; Heparin-binding growth-associated molecule; Heparin-binding brain mitogen; HBNF1; HBNF-1; HBNF; HBBM; HB-GAM TTA9EJK GN PTN TTA9EJK FC Binds cell-surface proteoglycan receptor via their chondroitin sulfate (CS) groups. Thereby regulates many processes like cell proliferation, cell survival, cell growth, cell differentiation and cell migration in several tissues namely neuron and bone. Also plays a role in synaptic plasticity and learning-related behavior by inhibiting long-term synaptic potentiation. Binds PTPRZ1, leading to neutralization of the negative charges of the CS chains of PTPRZ1, inducing PTPRZ1 clustering, thereby causing the dimerization and inactivation of its phosphatase activity leading to increased tyrosine phosphorylation of each of the PTPRZ1 substrates like ALK, CTNNB1 or AFAP1L2 in order to activate the PI3K-AKT pathway. Through PTPRZ1 binding controls oligodendrocyte precursor cell differentiation by enhancing the phosphorylation of AFAP1L2 in order to activate the PI3K-AKT pathway. Forms a complex with PTPRZ1 and integrin alpha-V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell migration through SRC dephosphorylation and activation that consequently leads to ITGB3 'Tyr-773' phosphorylation. In adult hippocampus promotes dendritic arborization, spine development, and functional integration and connectivity of newborn granule neurons through ALK by activating AKT signaling pathway. Binds GPC2 and chondroitin sulfate proteoglycans (CSPGs) at the neuron surface, leading to abrogation of binding between PTPRS and CSPGs and neurite outgrowth promotion. Binds SDC3 and mediates bone formation by recruiting and attaching osteoblasts/osteoblast precursors to the sites for new bone deposition. Binds ALK and promotes cell survival and cell proliferation through MAPK pathway activation. Inhibits proliferation and enhances differentiation of neural stem cells by inhibiting FGF2-induced fibroblast growth factor receptor signaling pathway. Mediates regulatory mechanisms in normal hemostasis and in hematopoietic regeneration and in maintaining the balance of myeloid and lymphoid regeneration. In addition may play a role in the female reproductive system, auditory response and the progesterone-induced decidualization pathway. Secreted growth factor that mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors. TTA9EJK PD 2N6F TTA9EJK SQ MQAQQYQQQRRKFAAAFLAFIFILAAVDTAEAGKKEKPEKKVKKSDCGEWQWSVCVPTSGDCGLGTREGTRTGAECKQTMKTQRCKIPCNWKKQFGAECKYQFQAWGECDLNTALKTRTGSLKRALHNAECQKTVTISKPCGKLTKPKPQAESKKKKKEGKKQEKMLD TTA9EJK TT Literature-reported TTPSK7A ID TTPSK7A TTPSK7A TN Plexin domain-containing protein 1 (PLXDC1) TTPSK7A UP Q8IUK5 TTPSK7A UC PLDX1_HUMAN TTPSK7A BC Plexin family TTPSK7A SN Tumor endothelial marker 7; Tumor endothelial marker 3; PLXDC1 TTPSK7A GN PLXDC1 TTPSK7A FC Plays a critical role in endothelial cell capillarymorphogenesis. TTPSK7A SQ MRGELWLLVLVLREAARALSPQPGAGHDEGPGSGWAAKGTVRGWNRRARESPGHVSEPDRTQLSQDLGGGTLAMDTLPDNRTRVVEDNHSYYVSRLYGPSEPHSRELWVDVAEANRSQVKIHTILSNTHRQASRVVLSFDFPFYGHPLRQITIATGGFIFMGDVIHRMLTATQYVAPLMANFNPGYSDNSTVVYFDNGTVFVVQWDHVYLQGWEDKGSFTFQAALHHDGRIVFAYKEIPMSVPEISSSQHPVKTGLSDAFMILNPSPDVPESRRRSIFEYHRIELDPSKVTSMSAVEFTPLPTCLQHRSCDACMSSDLTFNCSWCHVLQRCSSGFDRYRQEWMDYGCAQEAEGRMCEDFQDEDHDSASPDTSFSPYDGDLTTTSSSLFIDSLTTEDDTKLNPYAGGDGLQNNLSPKTKGTPVHLGTIVGIVLAVLLVAAIILAGIYINGHPTSNAALFFIERRPHHWPAMKFRSHPDHSTYAEVEPSGHEKEGFMEAEQC TTPSK7A TT Literature-reported TTH8ZRL ID TTH8ZRL TTH8ZRL TN Polybromo-1 (PBRM1) TTH8ZRL UP Q86U86 TTH8ZRL UC PB1_HUMAN TTH8ZRL SN hPB1; Protein polybromo-1; Polybromo-1D; PB1; BRG1-associated factor 180; BAF180 TTH8ZRL GN PBRM1 TTH8ZRL FC Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). Acts as a negative regulator of cell proliferation. Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). TTH8ZRL PD 5IID; 5II2; 5II1; 5HRX; 5HRW TTH8ZRL SQ MGSKRRRATSPSSSVSGDFDDGHHSVSTPGPSRKRRRLSNLPTVDPIAVCHELYNTIRDYKDEQGRLLCELFIRAPKRRNQPDYYEVVSQPIDLMKIQQKLKMEEYDDVNLLTADFQLLFNNAKSYYKPDSPEYKAACKLWDLYLRTRNEFVQKGEADDEDDDEDGQDNQGTVTEGSSPAYLKEILEQLLEAIVVATNPSGRLISELFQKLPSKVQYPDYYAIIKEPIDLKTIAQRIQNGSYKSIHAMAKDIDLLAKNAKTYNEPGSQVFKDANSIKKIFYMKKAEIEHHEMAKSSLRMRTPSNLAAARLTGPSHSKGSLGEERNPTSKYYRNKRAVQGGRLSAITMALQYGSESEEDAALAAARYEEGESEAESITSFMDVSNPFYQLYDTVRSCRNNQGQLIAEPFYHLPSKKKYPDYYQQIKMPISLQQIRTKLKNQEYETLDHLECDLNLMFENAKRYNVPNSAIYKRVLKLQQVMQAKKKELARRDDIEDGDSMISSATSDTGSAKRKSKKNIRKQRMKILFNVVLEAREPGSGRRLCDLFMVKPSKKDYPDYYKIILEPMDLKIIEHNIRNDKYAGEEGMIEDMKLMFRNARHYNEEGSQVYNDAHILEKLLKEKRKELGPLPDDDDMASPKLKLSRKSGISPKKSKYMTPMQQKLNEVYEAVKNYTDKRGRRLSAIFLRLPSRSELPDYYLTIKKPMDMEKIRSHMMANKYQDIDSMVEDFVMMFNNACTYNEPESLIYKDALVLHKVLLETRRDLEGDEDSHVPNVTLLIQELIHNLFVSVMSHQDDEGRCYSDSLAEIPAVDPNFPNKPPLTFDIIRKNVENNRYRRLDLFQEHMFEVLERARRMNRTDSEIYEDAVELQQFFIKIRDELCKNGEILLSPALSYTTKHLHNDVEKERKEKLPKEIEEDKLKREEEKREAEKSEDSSGAAGLSGLHRTYSQDCSFKNSMYHVGDYVYVEPAEANLQPHIVCIERLWEDSAGEKWLYGCWFYRPNETFHLATRKFLEKEVFKSDYYNKVPVSKILGKCVVMFVKEYFKLCPENFRDEDVFVCESRYSAKTKSFKKIKLWTMPISSVRFVPRDVPLPVVRVASVFANADKGDDEKNTDNSEDSRAEDNFNLEKEKEDVPVEMSNGEPGCHYFEQLHYNDMWLKVGDCVFIKSHGLVRPRVGRIEKVWVRDGAAYFYGPIFIHPEETEHEPTKMFYKKEVFLSNLEETCPMTCILGKCAVLSFKDFLSCRPTEIPENDILLCESRYNESDKQMKKFKGLKRFSLSAKVVDDEIYYFRKPIVPQKEPSPLLEKKIQLLEAKFAELEGGDDDIEEMGEEDSEVIEPPSLPQLQTPLASELDLMPYTPPQSTPKSAKGSAKKEGSKRKINMSGYILFSSEMRAVIKAQHPDYSFGELSRLVGTEWRNLETAKKAEYEERAAKVAEQQERERAAQQQQPSASPRAGTPVGALMGVVPPPTPMGMLNQQLTPVAGMMGGYPPGLPPLQGPVDGLVSMGSMQPLHPGGPPPHHLPPGVPGLPGIPPPGVMNQGVAPMVGTPAPGGSPYGQQVGVLGPPGQQAPPPYPGPHPAGPPVIQQPTTPMFVAPPPKTQRLLHSEAYLKYIEGLSAESNSISKWDQTLAARRRDVHLSKEQESRLPSHWLKSKGAHTTMADALWRLRDLMLRDTLNIRQAYNLENV TTH8ZRL TT Literature-reported TTAHD89 ID TTAHD89 TTAHD89 TN Polycystic kidney disease 2-like 1 (TRPP2) TTAHD89 UP Q9P0L9 TTAHD89 UC PK2L1_HUMAN TTAHD89 SN Polycystin-L1; Polycystin-L; Polycystin-2L1; Polycystin-2 homolog; Polycystic kidney disease 2-like 1 protein; PKDL; PKD2L TTAHD89 GN PKD2L1 TTAHD89 FC Pore-forming subunit of a heterotetrameric, non-selective cation channel that is permeable to Ca(2+). Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in primary cilia, where it controls cilium calcium concentration, but does not affect cytoplasmic calcium concentration. The channel formed by PKD1L2 and PKD1L1 in primary cilia regulates sonic hedgehog/SHH signaling and GLI2 transcription. Pore-forming subunit of a channel formed by PKD1L2 and PKD1L3 that contributes to sour taste perception in gustatory cells. The heteromeric channel formed by PKD1L2 and PKD1L3 is activated by low pH, but opens only when the extracellular pH rises again. May play a role in the perception of carbonation taste (By similarity). May play a role in the sensory perception of water, via a mechanism that activates the channel in response to dilution of salivary bicarbonate and changes in salivary pH (By similarity). TTAHD89 PD 6DU8; 4GIF; 3TE3 TTAHD89 SQ MNAVGSPEGQELQKLGSGAWDNPAYSGPPSPHGTLRVCTISSTGPLQPQPKKPEDEPQETAYRTQVSSCCLHICQGIRGLWGTTLTENTAENRELYIKTTLRELLVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDTGVSFQAISSMADFWDFAQGPLLDSLYWTKWYNNQSLGHGSHSFIYYENMLLGVPRLRQLKVRNDSCVVHEDFREDILSCYDVYSPDKEEQLPFGPFNGTAWTYHSQDELGGFSHWGRLTSYSGGGYYLDLPGSRQGSAEALRALQEGLWLDRGTRVVFIDFSVYNANINLFCVLRLVVEFPATGGAIPSWQIRTVKLIRYVSNWDFFIVGCEVIFCVFIFYYVVEEILELHIHRLRYLSSIWNILDLVVILLSIVAVGFHIFRTLEVNRLMGKLLQQPNTYADFEFLAFWQTQYNNMNAVNLFFAWIKIFKYISFNKTMTQLSSTLARCAKDILGFAVMFFIVFFAYAQLGYLLFGTQVENFSTFIKCIFTQFRIILGDFDYNAIDNANRILGPAYFVTYVFFVFFVLLNMFLAIINDTYSEVKEELAGQKDELQLSDLLKQGYNKTLLRLRLRKERVSDVQKVLQGGEQEIQFEDFTNTLRELGHAEHEITELTATFTKFDRDGNRILDEKEQEKMRQDLEEERVALNTEIEKLGRSIVSSPQGKSGPEAARAGGWVSGEEFYMLTRRVLQLETVLEGVVSQIDAVGSKLKMLERKGWLAPSPGVKEQAIWKHPQPAPAVTPDPWGVQGGQESEVPYKREEEALEERRLSRGEIPTLQRS TTAHD89 TT Literature-reported TTHR3IE ID TTHR3IE TTHR3IE TN Polynucleotide kinase-3'-phosphatase (PNKP) TTHR3IE UP Q96T60 TTHR3IE UC PNKP_HUMAN TTHR3IE SN DNA 5'-kinase/3'-phosphatase; Bifunctional polynucleotide phosphatase/kinase TTHR3IE GN PNKP TTHR3IE FC Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. TTHR3IE PD 2W3O; 2BRF TTHR3IE SQ MGEVEAPGRLWLESPPGGAPPIFLPSDGQALVLGRGPLTQVTDRKCSRTQVELVADPETRTVAVKQLGVNPSTTGTQELKPGLEGSLGVGDTLYLVNGLHPLTLRWEETRTPESQPDTPPGTPLVSQDEKRDAELPKKRMRKSNPGWENLEKLLVFTAAGVKPQGKVAGFDLDGTLITTRSGKVFPTGPSDWRILYPEIPRKLRELEAEGYKLVIFTNQMSIGRGKLPAEEFKAKVEAVVEKLGVPFQVLVATHAGLYRKPVTGMWDHLQEQANDGTPISIGDSIFVGDAAGRPANWAPGRKKKDFSCADRLFALNLGLPFATPEEFFLKWPAAGFELPAFDPRTVSRSGPLCLPESRALLSASPEVVVAVGFPGAGKSTFLKKHLVSAGYVHVNRDTLGSWQRCVTTCETALKQGKRVAIDNTNPDAASRARYVQCARAAGVPCRCFLFTATLEQARHNNRFREMTDSSHIPVSDMVMYGYRKQFEAPTLAEGFSAILEIPFRLWVEPRLGRLYCQFSEG TTHR3IE TT Literature-reported TTWMX0U ID TTWMX0U TTWMX0U TN Polypyrimidine tract-binding protein (PTBP1) TTWMX0U UP P26599 TTWMX0U UC PTBP1_HUMAN TTWMX0U SN hnRNP I; Polypyrimidine tractbinding protein 1; Polypyrimidine tract-binding protein 1; PTB; Heterogeneous nuclear ribonucleoprotein I; 57 kDa RNAbinding protein PPTB1; 57 kDa RNA-binding protein PPTB-1 TTWMX0U GN PTBP1 TTWMX0U FC Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10. In case of infection by picornaviruses, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation. Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. TTWMX0U PD 3ZZZ; 3ZZY; 2N3O; 2EVZ; 2ADC TTWMX0U SQ MDGIVPDIAVGTKRGSDELFSTCVTNGPFIMSSNSASAANGNDSKKFKGDSRSAGVPSRVIHIRKLPIDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVTPVLRGQPIYIQFSNHKELKTDSSPNQARAQAALQAVNSVQSGNLALAASAAAVDAGMAMAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDYTRPDLPSGDSQPSLDQTMAAAFGLSVPNVHGALAPLAIPSAAAAAAAAGRIAIPGLAGAGNSVLLVSNLNPERVTPQSLFILFGVYGDVQRVKILFNKKENALVQMADGNQAQLAMSHLNGHKLHGKPIRITLSKHQNVQLPREGQEDQGLTKDYGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVSEEDLKVLFSSNGGVVKGFKFFQKDRKMALIQMGSVEEAVQALIDLHNHDLGENHHLRVSFSKSTI TTWMX0U TT Literature-reported TTWMX0U FM RNA recognition motif TTLONKX ID TTLONKX TTLONKX TN PP2A B subunit isoform R5-alpha (PPP2R5A) TTLONKX UP Q15172 TTLONKX UC 2A5A_HUMAN TTLONKX SN Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform; Protein phosphatase-2A; PR61alpha; PP2A, B subunit, R5 alpha isoform; PP2A, B subunit, PR61 alpha isoform; PP2A, B subunit, B56 alpha isoform; PP2A, B subunit, B' alpha isoform; PP2A B subunit isoform PR61-alpha; PP2A B subunit isoform B56-alpha; PP2A B subunit isoform B'-alpha TTLONKX GN PPP2R5A TTLONKX FC The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. TTLONKX SQ MSSSSPPAGAASAAISASEKVDGFTRKSVRKAQRQKRSQGSSQFRSQGSQAELHPLPQLKDATSNEQQELFCQKLQQCCILFDFMDSVSDLKSKEIKRATLNELVEYVSTNRGVIVESAYSDIVKMISANIFRTLPPSDNPDFDPEEDEPTLEASWPHIQLVYEFFLRFLESPDFQPSIAKRYIDQKFVQQLLELFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNIFLRFIYETEHFNGVAELLEILGSIINGFALPLKAEHKQFLMKVLIPMHTAKGLALFHAQLAYCVVQFLEKDTTLTEPVIRGLLKFWPKTCSQKEVMFLGEIEEILDVIEPTQFKKIEEPLFKQISKCVSSSHFQVAERALYFWNNEYILSLIEENIDKILPIMFASLYKISKEHWNPTIVALVYNVLKTLMEMNGKLFDDLTSSYKAERQREKKKELEREELWKKLEELKLKKALEKQNSAYNMHSILSNTSAE TTLONKX TT Literature-reported TTLONKX KE hsa03015:mRNA surveillance pathway; hsa04071:Sphingolipid signaling pathway; hsa04114:Oocyte meiosis; hsa04151:PI3K-Akt signaling pathway; hsa04152:AMPK signaling pathway; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04728:Dopaminergic synapse TTLONKX RC R-HSA-195253:Degradation of beta-catenin by the destruction complex; R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-389513:CTLA4 inhibitory signaling; R-HSA-432142:Platelet sensitization by LDL; R-HSA-4641262:Disassembly of the destruction complex and recruitment of AXIN to the membrane; R-HSA-5358747:S33 mutants of beta-catenin aren't phosphorylated; R-HSA-5358749:S37 mutants of beta-catenin aren't phosphorylated; R-HSA-5358751:S45 mutants of beta-catenin aren't phosphorylated; R-HSA-5358752:T41 mutants of beta-catenin aren't phosphorylated; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-5673000:RAF activation; R-HSA-5675221:Negative regulation of MAPK pathway; R-HSA-68877:Mitotic Prometaphase TT4LM0E ID TT4LM0E TT4LM0E TN Progranulin (PGRN) TT4LM0E UP P28799 TT4LM0E UC GRN_HUMAN TT4LM0E SN Proepithelin; PGRN; PEPI; PCDGF; PC cell-derived growth factor; Granulin precursor; Glycoprotein of 88 Kda; Glycoprotein 88; GP88; Epithelin precursor; Acrogranin TT4LM0E GN GRN TT4LM0E FC Secreted proteins that act as key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation. Functions as regulator of proteins trafficking to lysosome and activity of lysosomal enzymes. Facilitates also the acidification of lysosomes, causing degradation of mature CTSD by CTSB. In addition, functions as wound-related growth factor that acts directly on dermal fibroblasts and endothelial cells to promote division, migration and the formation of capillary-like tubule structure (By similarity). Also promotes epithelial cell proliferation by blocking TNF-mediated neutrophil activation preventing release of oxidants and proteases. Moreover, modulates inflammation in neuron by preserving neuron survival, axonal outgrowth and neuronal integrity. TT4LM0E PD 2JYV; 2JYU; 2JYT; 2JYE; 1G26 TT4LM0E SQ MWTLVSWVALTAGLVAGTRCPDGQFCPVACCLDPGGASYSCCRPLLDKWPTTLSRHLGGPCQVDAHCSAGHSCIFTVSGTSSCCPFPEAVACGDGHHCCPRGFHCSADGRSCFQRSGNNSVGAIQCPDSQFECPDFSTCCVMVDGSWGCCPMPQASCCEDRVHCCPHGAFCDLVHTRCITPTGTHPLAKKLPAQRTNRAVALSSSVMCPDARSRCPDGSTCCELPSGKYGCCPMPNATCCSDHLHCCPQDTVCDLIQSKCLSKENATTDLLTKLPAHTVGDVKCDMEVSCPDGYTCCRLQSGAWGCCPFTQAVCCEDHIHCCPAGFTCDTQKGTCEQGPHQVPWMEKAPAHLSLPDPQALKRDVPCDNVSSCPSSDTCCQLTSGEWGCCPIPEAVCCSDHQHCCPQGYTCVAEGQCQRGSEIVAGLEKMPARRASLSHPRDIGCDQHTSCPVGQTCCPSLGGSWACCQLPHAVCCEDRQHCCPAGYTCNVKARSCEKEVVSAQPATFLARSPHVGVKDVECGEGHFCHDNQTCCRDNRQGWACCPYRQGVCCADRRHCCPAGFRCAARGTKCLRREAPRWDAPLRDPALRQLL TT4LM0E TT Literature-reported TT6U071 ID TT6U071 TT6U071 TN Prohibitin (PHB) TT6U071 UP P35232 TT6U071 UC PHB_HUMAN TT6U071 SN PHB1; HEL-S-54e; HEL-215 TT6U071 GN PHB TT6U071 FC It has a role in regulating proliferation. As yet it is unclear if the protein or the mRNA exhibits this effect. May play a role in regulating mitochondrial respiration activity and in aging. Prohibitin inhibits DNA synthesis. TT6U071 PD 1LU7 TT6U071 SQ MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIFTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ TT6U071 TT Literature-reported TT6U071 FM Prohibitin family TTVXTZ4 ID TTVXTZ4 TTVXTZ4 TN Proliferation marker protein Ki-67 (MKI67) TTVXTZ4 UP P46013 TTVXTZ4 UC KI67_HUMAN TTVXTZ4 SN Antigen identified by monoclonal antibody Ki-67; Antigen Ki67; Antigen KI-67 TTVXTZ4 GN MKI67 TTVXTZ4 FC Associates with the surface of the mitotic chromosome, the perichromosomal layer, and covers a substantial fraction of the chromosome surface. Prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility. Binds DNA, with a preference for supercoiled DNA and AT-rich DNA. Does not contribute to the internal structure of mitotic chromosomes. May play a role in chromatin organization. It is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in maintaining mitotic chromosomes dispersed. Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. TTVXTZ4 PD 5J28; 2AFF; 1R21 TTVXTZ4 SQ MWPTRRLVTIKRSGVDGPHFPLSLSTCLFGRGIECDIRIQLPVVSKQHCKIEIHEQEAILHNFSSTNPTQVNGSVIDEPVRLKHGDVITIIDRSFRYENESLQNGRKSTEFPRKIREQEPARRVSRSSFSSDPDEKAQDSKAYSKITEGKVSGNPQVHIKNVKEDSTADDSKDSVAQGTTNVHSSEHAGRNGRNAADPISGDFKEISSVKLVSRYGELKSVPTTQCLDNSKKNESPFWKLYESVKKELDVKSQKENVLQYCRKSGLQTDYATEKESADGLQGETQLLVSRKSRPKSGGSGHAVAEPASPEQELDQNKGKGRDVESVQTPSKAVGASFPLYEPAKMKTPVQYSQQQNSPQKHKNKDLYTTGRRESVNLGKSEGFKAGDKTLTPRKLSTRNRTPAKVEDAADSATKPENLSSKTRGSIPTDVEVLPTETEIHNEPFLTLWLTQVERKIQKDSLSKPEKLGTTAGQMCSGLPGLSSVDINNFGDSINESEGIPLKRRRVSFGGHLRPELFDENLPPNTPLKRGEAPTKRKSLVMHTPPVLKKIIKEQPQPSGKQESGSEIHVEVKAQSLVISPPAPSPRKTPVASDQRRRSCKTAPASSSKSQTEVPKRGGRKSGNLPSKRVSISRSQHDILQMICSKRRSGASEANLIVAKSWADVVKLGAKQTQTKVIKHGPQRSMNKRQRRPATPKKPVGEVHSQFSTGHANSPCTIIIGKAHTEKVHVPARPYRVLNNFISNQKMDFKEDLSGIAEMFKTPVKEQPQLTSTCHIAISNSENLLGKQFQGTDSGEEPLLPTSESFGGNVFFSAQNAAKQPSDKCSASPPLRRQCIRENGNVAKTPRNTYKMTSLETKTSDTETEPSKTVSTANRSGRSTEFRNIQKLPVESKSEETNTEIVECILKRGQKATLLQQRREGEMKEIERPFETYKENIELKENDEKMKAMKRSRTWGQKCAPMSDLTDLKSLPDTELMKDTARGQNLLQTQDHAKAPKSEKGKITKMPCQSLQPEPINTPTHTKQQLKASLGKVGVKEELLAVGKFTRTSGETTHTHREPAGDGKSIRTFKESPKQILDPAARVTGMKKWPRTPKEEAQSLEDLAGFKELFQTPGPSEESMTDEKTTKIACKSPPPESVDTPTSTKQWPKRSLRKADVEEEFLALRKLTPSAGKAMLTPKPAGGDEKDIKAFMGTPVQKLDLAGTLPGSKRQLQTPKEKAQALEDLAGFKELFQTPGHTEELVAAGKTTKIPCDSPQSDPVDTPTSTKQRPKRSIRKADVEGELLACRNLMPSAGKAMHTPKPSVGEEKDIIIFVGTPVQKLDLTENLTGSKRRPQTPKEEAQALEDLTGFKELFQTPGHTEEAVAAGKTTKMPCESSPPESADTPTSTRRQPKTPLEKRDVQKELSALKKLTQTSGETTHTDKVPGGEDKSINAFRETAKQKLDPAASVTGSKRHPKTKEKAQPLEDLAGLKELFQTPVCTDKPTTHEKTTKIACRSQPDPVDTPTSSKPQSKRSLRKVDVEEEFFALRKRTPSAGKAMHTPKPAVSGEKNIYAFMGTPVQKLDLTENLTGSKRRLQTPKEKAQALEDLAGFKELFQTRGHTEESMTNDKTAKVACKSSQPDPDKNPASSKRRLKTSLGKVGVKEELLAVGKLTQTSGETTHTHTEPTGDGKSMKAFMESPKQILDSAASLTGSKRQLRTPKGKSEVPEDLAGFIELFQTPSHTKESMTNEKTTKVSYRASQPDLVDTPTSSKPQPKRSLRKADTEEEFLAFRKQTPSAGKAMHTPKPAVGEEKDINTFLGTPVQKLDQPGNLPGSNRRLQTRKEKAQALEELTGFRELFQTPCTDNPTTDEKTTKKILCKSPQSDPADTPTNTKQRPKRSLKKADVEEEFLAFRKLTPSAGKAMHTPKAAVGEEKDINTFVGTPVEKLDLLGNLPGSKRRPQTPKEKAKALEDLAGFKELFQTPGHTEESMTDDKITEVSCKSPQPDPVKTPTSSKQRLKISLGKVGVKEEVLPVGKLTQTSGKTTQTHRETAGDGKSIKAFKESAKQMLDPANYGTGMERWPRTPKEEAQSLEDLAGFKELFQTPDHTEESTTDDKTTKIACKSPPPESMDTPTSTRRRPKTPLGKRDIVEELSALKQLTQTTHTDKVPGDEDKGINVFRETAKQKLDPAASVTGSKRQPRTPKGKAQPLEDLAGLKELFQTPICTDKPTTHEKTTKIACRSPQPDPVGTPTIFKPQSKRSLRKADVEEESLALRKRTPSVGKAMDTPKPAGGDEKDMKAFMGTPVQKLDLPGNLPGSKRWPQTPKEKAQALEDLAGFKELFQTPGTDKPTTDEKTTKIACKSPQPDPVDTPASTKQRPKRNLRKADVEEEFLALRKRTPSAGKAMDTPKPAVSDEKNINTFVETPVQKLDLLGNLPGSKRQPQTPKEKAEALEDLVGFKELFQTPGHTEESMTDDKITEVSCKSPQPESFKTSRSSKQRLKIPLVKVDMKEEPLAVSKLTRTSGETTQTHTEPTGDSKSIKAFKESPKQILDPAASVTGSRRQLRTRKEKARALEDLVDFKELFSAPGHTEESMTIDKNTKIPCKSPPPELTDTATSTKRCPKTRPRKEVKEELSAVERLTQTSGQSTHTHKEPASGDEGIKVLKQRAKKKPNPVEEEPSRRRPRAPKEKAQPLEDLAGFTELSETSGHTQESLTAGKATKIPCESPPLEVVDTTASTKRHLRTRVQKVQVKEEPSAVKFTQTSGETTDADKEPAGEDKGIKALKESAKQTPAPAASVTGSRRRPRAPRESAQAIEDLAGFKDPAAGHTEESMTDDKTTKIPCKSSPELEDTATSSKRRPRTRAQKVEVKEELLAVGKLTQTSGETTHTDKEPVGEGKGTKAFKQPAKRKLDAEDVIGSRRQPRAPKEKAQPLEDLASFQELSQTPGHTEELANGAADSFTSAPKQTPDSGKPLKISRRVLRAPKVEPVGDVVSTRDPVKSQSKSNTSLPPLPFKRGGGKDGSVTGTKRLRCMPAPEEIVEELPASKKQRVAPRARGKSSEPVVIMKRSLRTSAKRIEPAEELNSNDMKTNKEEHKLQDSVPENKGISLRSRRQNKTEAEQQITEVFVLAERIEINRNEKKPMKTSPEMDIQNPDDGARKPIPRDKVTENKRCLRSARQNESSQPKVAEESGGQKSAKVLMQNQKGKGEAGNSDSMCLRSRKTKSQPAASTLESKSVQRVTRSVKRCAENPKKAEDNVCVKKIRTRSHRDSEDI TTVXTZ4 TT Literature-reported TT3HYDO ID TT3HYDO TT3HYDO TN Prolyl endopeptidase-like (PREPL) TT3HYDO UP Q4J6C6 TT3HYDO UC PPCEL_HUMAN TT3HYDO SN Prolylendopeptidase-like; KIAA0436 TT3HYDO GN PREPL TT3HYDO FC Probable serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. May play a role in the regulation of synaptic vesiscle exocytosis. TT3HYDO EC EC 3.4.21.- TT3HYDO SQ MQQKTKLFLQALKYSIPHLGKCMQKQHLNHYNFADHCYNRIKLKKYHLTKCLQNKPKISELARNIPSRSFSCKDLQPVKQENEKPLPENMDAFEKVRTKLETQPQEEYEIINVEVKHGGFVYYQEGCCLVRSKDEEADNDNYEVLFNLEELKLDQPFIDCIRVAPDEKYVAAKIRTEDSEASTCVIIKLSDQPVMEASFPNVSSFEWVKDEEDEDVLFYTFQRNLRCHDVYRATFGDNKRNERFYTEKDPSYFVFLYLTKDSRFLTINIMNKTTSEVWLIDGLSPWDPPVLIQKRIHGVLYYVEHRDDELYILTNVGEPTEFKLMRTAADTPAIMNWDLFFTMKRNTKVIDLDMFKDHCVLFLKHSNLLYVNVIGLADDSVRSLKLPPWACGFIMDTNSDPKNCPFQLCSPIRPPKYYTYKFAEGKLFEETGHEDPITKTSRVLRLEAKSKDGKLVPMTVFHKTDSEDLQKKPLLVHVYGAYGMDLKMNFRPERRVLVDDGWILAYCHVRGGGELGLQWHADGRLTKKLNGLADLEACIKTLHGQGFSQPSLTTLTAFSAGGVLAGALCNSNPELVRAVTLEAPFLDVLNTMMDTTLPLTLEELEEWGNPSSDEKHKNYIKRYCPYQNIKPQHYPSIHITAYENDERVPLKGIVSYTEKLKEAIAEHAKDTGEGYQTPNIILDIQPGGNHVIEDSHKKITAQIKFLYEELGLDSTSVFEDLKKYLKF TT3HYDO TT Literature-reported TTLH9NY ID TTLH9NY TTLH9NY TN Promyelocytic leukemia protein (PML) TTLH9NY UP P29590 TTLH9NY UC PML_HUMAN TTLH9NY SN Tripartite motif-containing protein 19; TRIM19; RNF71; RING finger protein 71; Protein PML; PP8675; MYL TTLH9NY GN PML TTLH9NY FC Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Isoform PML-4 has a multifaceted role in the regulation of apoptosis and growth suppression: activates RB1 and inhibits AKT1 via interactions with PP1 and PP2A phosphatases respectively, negatively affects the PI3K pathway by inhibiting MTOR and activating PTEN, and positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Isoform PML-4 also: acts as a transcriptional repressor of TBX2 during cellular senescence and the repression is dependent on a functional RBL2/E2F4 repressor complex, regulates double-strand break repair in gamma-irradiation-induced DNA damage responses via its interaction with WRN, acts as a negative regulator of telomerase by interacting with TERT, and regulates PER2 nuclear localization and circadian function. Isoform PML-6 inhibits specifically the activity of the tetrameric form of PKM. The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in concert with SATB1 are involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Isoform PML-2 is required for efficient IFN-gamma induced MHC II gene transcription via regulation of CIITA. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. PML also regulates transcription activity of ELF4 and can act as an important mediator for TNF-alpha- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration. TTLH9NY PD 5YUF; 4WJO; 4WJN; 2MWX; 2MVW TTLH9NY SQ MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS TTLH9NY TT Literature-reported TTK3VYC ID TTK3VYC TTK3VYC TN Proprotein convertase subtilisin/kexin type 4 (PCSK4) TTK3VYC UP Q6UW60 TTK3VYC UC PCSK4_HUMAN TTK3VYC SN UNQ2757/PRO6496; Proprotein convertase 4; PC4 TTK3VYC GN PCSK4 TTK3VYC FC Proprotein convertase involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues (By similarity). In males, important for ADAM2 processing as well as other acrosomal proteins with roles in fertilization and critical for normal fertilization events such as sperm capacitation, acrosome reaction and binding of sperm to zona pellucida (By similarity). Plays also a role in female fertility, involved in the regulation of trophoblast migration and placental development, may be through the proteolytical processing and activation of proteins such as IGF2. May also participate in folliculogenesis in the ovaries (By similarity). TTK3VYC EC EC 3.4.21.- TTK3VYC SQ MRPAPIALWLRLVLALALVRPRAVGWAPVRAPIYVSSWAVQVSQGNREVERLARKFGFVNLGPIFPDGQYFHLRHRGVVQQSLTPHWGHRLHLKKNPKVQWFQQQTLQRRVKRSVVVPTDPWFSKQWYMNSEAQPDLSILQAWSQGLSGQGIVVSVLDDGIEKDHPDLWANYDPLASYDFNDYDPDPQPRYTPSKENRHGTRCAGEVAAMANNGFCGVGVAFNARIGGVRMLDGTITDVIEAQSLSLQPQHIHIYSASWGPEDDGRTVDGPGILTREAFRRGVTKGRGGLGTLFIWASGNGGLHYDNCNCDGYTNSIHTLSVGSTTQQGRVPWYSEACASTLTTTYSSGVATDPQIVTTDLHHGCTDQHTGTSASAPLAAGMIALALEANPFLTWRDMQHLVVRASKPAHLQAEDWRTNGVGRQVSHHYGYGLLDAGLLVDTARTWLPTQPQRKCAVRVQSRPTPILPLIYIRENVSACAGLHNSIRSLEHVQAQLTLSYSRRGDLEISLTSPMGTRSTLVAIRPLDVSTEGYNNWVFMSTHFWDENPQGVWTLGLENKGYYFNTGTLYRYTLLLYGTAEDMTARPTGPQVTSSACVQRDTEGLCQACDGPAYILGQLCLAYCPPRFFNHTRLVTAGPGHTAAPALRVCSSCHASCYTCRGGSPRDCTSCPPSSTLDQQQGSCMGPTTPDSRPRLRAAACPHHRCPASAMVLSLLAVTLGGPVLCGMSMDLPLYAWLSRARATPTKPQVWLPAGT TTK3VYC TT Literature-reported TT75LN9 ID TT75LN9 TT75LN9 TN Proprotein convertase subtilisin/kexin type 6 (PCSK6) TT75LN9 UP P29122 TT75LN9 UC PCSK6_HUMAN TT75LN9 SN Subtilisin/kexin-like protease PACE4; Subtilisin-like proprotein convertase 4; SPC4; Paired basic amino acid cleaving enzyme 4; PACE4 TT75LN9 GN PCSK6 TT75LN9 FC Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway, with unique restricted distribution in both neuroendocrine and non-neuroendocrine tissues. TT75LN9 EC EC 3.4.21.- TT75LN9 SQ MPPRAPPAPGPRPPPRAAAATDTAAGAGGAGGAGGAGGPGFRPLAPRPWRWLLLLALPAACSAPPPRPVYTNHWAVQVLGGPAEADRVAAAHGYLNLGQIGNLEDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKRQVRSDPQALYFNDPIWSNMWYLHCGDKNSRCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRYDASNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGPGRLAKQAFEYGIKKGRQGLGSIFVWASGNGGREGDYCSCDGYTNSIYTISVSSATENGYKPWYLEECASTLATTYSSGAFYERKIVTTDLRQRCTDGHTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSRPAHLKASDWKVNGAGHKVSHFYGFGLVDAEALVVEAKKWTAVPSQHMCVAASDKRPRSIPLVQVLRTTALTSACAEHSDQRVVYLEHVVVRTSISHPRRGDLQIYLVSPSGTKSQLLAKRLLDLSNEGFTNWEFMTVHCWGEKAEGQWTLEIQDLPSQVRNPEKQGKLKEWSLILYGTAEHPYHTFSAHQSRSRMLELSAPELEPPKAALSPSQVEVPEDEEDYTAQSTPGSANILQTSVCHPECGDKGCDGPNADQCLNCVHFSLGSVKTSRKCVSVCPLGYFGDTAARRCRRCHKGCETCSSRAATQCLSCRRGFYHHQEMNTCVTLCPAGFYADESQKNCLKCHPSCKKCVDEPEKCTVCKEGFSLARGSCIPDCEPGTYFDSELIRCGECHHTCGTCVGPGREECIHCAKNFHFHDWKCVPACGEGFYPEEMPGLPHKVCRRCDENCLSCAGSSRNCSRCKTGFTQLGTSCITNHTCSNADETFCEMVKSNRLCERKLFIQFCCRTCLLAG TT75LN9 TT Literature-reported TTD30LY ID TTD30LY TTD30LY TN Proprotein convertase subtilisin/kexin type 7 (PCSK7) TTD30LY UP Q16549 TTD30LY UC PCSK7_HUMAN TTD30LY SN Subtilisin/kexin-like protease PC7; SPC7; Proprotein convertase 8; Proprotein convertase 7; Prohormone convertase 7; PC8; PC7; Lymphoma proprotein convertase; LPC TTD30LY GN PCSK7 TTD30LY FC Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway. TTD30LY EC EC 3.4.21.- TTD30LY SQ MPKGRQKVPHLDAPLGLPTCLWLELAGLFLLVPWVMGLAGTGGPDGQGTGGPSWAVHLESLEGDGEEETLEQQADALAQAAGLVNAGRIGELQGHYLFVQPAGHRPALEVEAIRQQVEAVLAGHEAVRWHSEQRLLRRAKRSVHFNDPKYPQQWHLNNRRSPGRDINVTGVWERNVTGRGVTVVVVDDGVEHTIQDIAPNYSPEGSYDLNSNDPDPMPHPDVENGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGPLTDSMEAVAFNKHYQINDIYSCSWGPDDDGKTVDGPHQLGKAALQHGVIAGRQGFGSIFVVASGNGGQHNDNCNYDGYANSIYTVTIGAVDEEGRMPFYAEECASMLAVTFSGGDKMLRSIVTTDWDLQKGTGCTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTATRYEDRRAEWVTNEAGFSHSHQHGFGLLNAWRLVNAAKIWTSVPYLASYVSPVLKENKAIPQSPRSLEVLWNVSRMDLEMSGLKTLEHVAVTVSITHPRRGSLELKLFCPSGMMSLIGAPRSMDSDPNGFNDWTFSTVRCWGERARGTYRLVIRDVGDESFQVGILRQWQLTLYGSVWSAVDIRDRQRLLESAMSGKYLHDDFALPCPPGLKIPEEDGYTITPNTLKTLVLVGCFTVFWTVYYMLEVYLSQRNVASNQVCRSGPCHWPHRSRKAKEEGTELESVPLCSSKDPDEVETESRGPPTTSDLLAPDLLEQGDWSLSQNKSALDCPHQHLDVPHGKEEQIC TTD30LY TT Literature-reported TT3I4WV ID TT3I4WV TT3I4WV TN Prostate apoptosis response-4 (PAWR) TT3I4WV UP Q96IZ0 TT3I4WV UC PAWR_HUMAN TT3I4WV SN Prostate apoptosis response 4 protein; PRKC apoptosis WT1 regulator protein; PAR4 TT3I4WV GN PAWR TT3I4WV FC Pro-apoptopic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1. TT3I4WV PD 2JK9 TT3I4WV SQ MATGGYRTSSGLGGSTTDFLEEWKAKREKMRAKQNPPGPAPPGGGSSDAAGKPPAGALGTPAAAAANELNNNLPGGAPAAPAVPGPGGVNCAVGSAMLTRAAPGPRRSEDEPPAASASAAPPPQRDEEEPDGVPEKGKSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAVNLLDPGSSYLLQEPPRTVSGRYKSTTSVSEEDVSSRYSRTDRSGFPRYNRDANVSGTLVSSSTLEKKIEDLEKEVVRERQENLRLVRLMQDKEEMIGKLKEEIDLLNRDLDDIEDENEQLKQENKTLLKVVGQLTR TT3I4WV TT Clinical trial TTAR2P0 ID TTAR2P0 TTAR2P0 TN Protein arginine methyltransferase 7 (PRMT7) TTAR2P0 UP Q9NVM4 TTAR2P0 UC ANM7_HUMAN TTAR2P0 SN Protein arginine N-methyltransferase 7; KIAA1933; Histone-arginine N-methyltransferase PRMT7; [Myelin basic protein]-arginine N-methyltransferase PRMT7 TTAR2P0 GN PRMT7 TTAR2P0 FC Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo. TTAR2P0 EC EC 2.1.1.321 TTAR2P0 SQ MKIFCSRANPTTGSVEWLEEDEHYDYHQEIARSSYADMLHDKDRNVKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIKVINKHSTEVTVGPEGDMPCRANILVTELFDTELIGEGALPSYEHAHRHLVEENCEAVPHRATVYAQLVESGRMWSWNKLFPIHVQTSLGEQVIVPPVDVESCPGAPSVCDIQLNQVSPADFTVLSDVLPMFSIDFSKQVSSSAACHSRRFEPLTSGRAQVVLSWWDIEMDPEGKIKCTMAPFWAHSDPEEMQWRDHWMQCVYFLPQEEPVVQGSALYLVAHHDDYCVWYSLQRTSPEKNERVRQMRPVCDCQAHLLWNRPRFGEINDQDRTDRYVQALRTVLKPDSVCLCVSDGSLLSVLAHHLGVEQVFTVESSAASHKLLRKIFKANHLEDKINIIEKRPELLTNEDLQGRKVSLLLGEPFFTTSLLPWHNLYFWYVRTAVDQHLGPGAMVMPQAASLHAVVVEFRDLWRIRSPCGDCEGFDVHIMDDMIKRALDFRESREAEPHPLWEYPCRSLSEPWQILTFDFQQPVPLQPLCAEGTVELRRPGQSHAAVLWMEYHLTPECTLSTGLLEPADPEGGCCWNPHCKQAVYFFSPAPDPRALLGGPRTVSYAVEFHPDTGDIIMEFRHADTPD TTAR2P0 TT Literature-reported TT1Q347 ID TT1Q347 TT1Q347 TN Protein FAM83B (FA83B) TT1Q347 UP Q5T0W9 TT1Q347 UC FA83B_HUMAN TT1Q347 SN C6orf143 TT1Q347 GN FAM83B TT1Q347 FC Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. May activate both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. TT1Q347 PD 5QHS; 5QHR; 5QHQ; 5QHP; 5QHO TT1Q347 SQ METSSMLSSLNDECKSDNYIEPHYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVAQSTAHGTDDSCDDTLSSGTYWPVESDVEAPNLDLGWPYVMPGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAHLSMVQIITGQLVESFDEEFRTLYARSCVPSSFAQEESARVKHGKALWENGTYQHSVSSLASVSSQRNLFGRQDKIHKLDSSYFKNRGIYTLNEHDKYNIRSHGYKPHFVPNFNGPNAIRQFQPNQINENWKRHSYAGEQPETVPYLLLNRALNRTNNPPGNWKKPSDSLSVASSSREGYVSHHNTPAQSFANRLAQRKTTNLADRNSNVRRSFNGTDNHIRFLQQRMPTLEHTTKSFLRNWRIESYLNDHSEATPDSNGSALGDRFEGYDNPENLKANALYTHSRLRSSLVFKPTLPEQKEVNSCTTGSSNSTIIGSQGSETPKEVPDTPTNVQHLTDKPLPESIPKLPLQSEAPKMHTLQVPENHSVALNQTTNGHTESNNYIYKTLGVNKQTENLKNQQTENLLKRRSFPLFDNSKANLDPGNSKHYVYSTLTRNRVRQPEKPKEDLLKSSKSMHNVTHNLEEDEEEVTKRNSPSGTTTKSVSIAALLDVNKEESNKELASKKEVKGSPSFLKKGSQKLRSLLSLTPDKKENLSKNKAPAFYRLCSSSDTLVSEGEENQKPKKSDTKVDSSPRRKHSSSSNSQGSIHKSKEDVTVSPSQEINAPPDENKRTPSPGPVESKFLERAGDASAPRFNTEQIQYRDSREINAVVTPERRPTSSPRPTSSELLRSHSTDRRVYSRFEPFCKIESSIQPTSNMPNTSINRPEIKSATMGNSYGRSSPLLNYNTGVYRSYQPNENKFRGFMQKFGNFIHKNK TT1Q347 TT Literature-reported TTVSEBF ID TTVSEBF TTVSEBF TN Proteinase activated receptor 3 (F2RL2) TTVSEBF UP O00254 TTVSEBF UC PAR3_HUMAN TTVSEBF BC GPCR rhodopsin TTVSEBF SN Thrombin receptor-like 2; Protease activated receptor 3; PAR-3; F2RL2; Coagulation factor II receptor-like 2 TTVSEBF GN F2RL2 TTVSEBF FC Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. TTVSEBF SQ MKALIFAAAGLLLLLPTFCQSGMENDTNNLAKPTLPIKTFRGAPPNSFEEFPFSALEGWTGATITVKIKCPEESASHLHVKNATMGYLTSSLSTKLIPAIYLLVFVVGVPANAVTLWMLFFRTRSICTTVFYTNLAIADFLFCVTLPFKIAYHLNGNNWVFGEVLCRATTVIFYGNMYCSILLLACISINRYLAIVHPFTYRGLPKHTYALVTCGLVWATVFLYMLPFFILKQEYYLVQPDITTCHDVHNTCESSSPFQLYYFISLAFFGFLIPFVLIIYCYAAIIRTLNAYDHRWLWYVKASLLILVIFTICFAPSNIILIIHHANYYYNNTDGLYFIYLIALCLGSLNSCLDPFLYFLMSKTRNHSTAYLTK TTVSEBF TT Literature-reported TTK5OG6 ID TTK5OG6 TTK5OG6 TN Proteolipid protein 2 (PLP2) TTK5OG6 UP Q04941 TTK5OG6 UC PLP2_HUMAN TTK5OG6 BC Plasmolipin family TTK5OG6 SN PLP2; Intestinal membrane A4 protein; Differentiation-dependent protein A4 TTK5OG6 GN PLP2 TTK5OG6 FC May play a role in cell differentiation in the intestinal epithelium. TTK5OG6 SQ MADSERLSAPGCWAACTNFSRTRKGILLFAEIILCLVILICFSASTPGYSSLSVIEMILAAIFFVVYMCDLHTKIPFINWPWSDFFRTLIAAILYLITSIVVLVERGNHSKIVAGVLGLIATCLFGYDAYVTFPVRQPRHTAAPTDPADGPV TTK5OG6 TT Literature-reported TT59Z6T ID TT59Z6T TT59Z6T TN Pseudomonas Aeruginosa Psl (Pseudo pslG) TT59Z6T UP Q9I1N2 TT59Z6T UC Q9I1N2_PSEAE TT59Z6T SN Pseudo PslG TT59Z6T GN Pseudo pslG TT59Z6T FC Involved in the synthesis of a key biofilm matrix exopolysaccharide Psl in Pseudomonas aeruginosa. Prevents biofilm formation and disassembles existing biofilms within minutes at nanomolar concentrations when supplied exogenously. TT59Z6T PD 5BXA; 5BX9; 4ZN2 TT59Z6T SQ MARKGLYLGGSALLLAVVLLLVFWGRPADAEIQVLKAPRAVVWKDFLGVNAQFLWFSPERYNKQIDRLQDLGLEWVRLDLHWDRLETAEDQYQLASLDQLVKDLEARQLKSVFYLVGSARFITTAPFYSPFQDQYPPRDPEVFARRMAMLSQRYPSVAAWQVWNEPNLIGFWRPKADPEGYAKLLQASTIALRMVDPEKPVVSAGMAFFSEMPDGRTMFDALGHLGVESLGTIATYHPYTQLPEGNYPWNLDFVSHANQINRALRNAGVPAIWSTEWGWSAYKGPKELQDIIGVEGQADYVLRRLALMSALDYDRIFLFTLSDLDQRASVRDRDYGLLDLDANPKPVYLALQRFLKVTGPKLRPADPPVTEDLPDGSFSIGWTREDGRNVWLFWSARGGNVRLPKLKEATLHDPLSGKVTPLSGSDGLEVPVKSSLQMLVWE TT59Z6T TT Literature-reported TTYA3NK ID TTYA3NK TTYA3NK TN Pseudomonas Amidotransferase (Pseudo yafJ) TTYA3NK UP A0A072ZJB2 TTYA3NK UC A0A072ZJB2_PSEAI TTYA3NK SN Putative glutamine amidotransferase yafJ; Putative glutamine amidotransferase; Glutamine amidotransferases class-II; Class II glutamine amidotransferase TTYA3NK GN Pseudo yafJ TTYA3NK FC Catalyses the removal of the ammonia group from a glutamine molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. TTYA3NK EC EC 2.4.2.- TTYA3NK SQ MCELLGMSANVPTDIVFSFTGLMQRGGGTGPHRDGWGIAFYEGRGVRLFQDPLASVDSEVARLVQRFPIKSETVIGHIRQANVGKVGLSNTHPFIRELGGRYWTFAHNGQLADFQPKPGFYRPVGETDSEAAFCDLLNRVRRAFPEPVPVEVLLPVLISACDEYRKKGVFNALISDGDWLFTFCSSKLAYITRRAPFGPARLKDADLTVDFHAETTPDDVVTVIATEPLTDNENWTLQQSGEWVLWWGGEVLAKGRV TTYA3NK TT Literature-reported TTCZ69H ID TTCZ69H TTCZ69H TN Pseudomonas Histidine kinase AlgR1 (Pseudo algR1) TTCZ69H UP Q9WWI2 TTCZ69H UC Q9WWI2_PSESY TTCZ69H BC Kinase TTCZ69H SN Response regulator transcription factor; Alginate biosynthesis regulatory protein TTCZ69H GN Pseudo algR1 TTCZ69H FC Plays an important role in essential signal transduction for adapting to bacterial stress. TTCZ69H SQ MNVLIVDDEPLARERLSRMVNEIEGYRVLEPSASNGEEALALIETHKPDVVLLDIRMPGLDGLQVAARLCEREAPPAVVFCTAHDEFALEAFQVSAVGYLVKPVRPEHLVEALRKAERPNRVQLAALTRPAAESGSGPRSHISARTRKGIELIPLDQVIYFIADHKYVTLRHEGGEVLLDEPLKALEDEFGDRFVRIHRNALVARERIERLQRTPLGHFQLFLRGLNGDALIVSRRHVAGVRKMMQQL TTCZ69H TT Literature-reported TTYX5QR ID TTYX5QR TTYX5QR TN Pseudomonas Histidine kinase AlgR2 (Pseudo algQ) TTYX5QR UP P15275 TTYX5QR UC ALGQ_PSEAE TTYX5QR BC Kinase TTYX5QR SN algQ; Transcriptional regulatory protein AlgQ (mRNA); Alginate regulatory protein AlgR2 (mRNA) TTYX5QR GN Pseudo algQ TTYX5QR FC The promoter for a critical alginate biosynthetic gene, AlgD, encoding GDP-mannose dehydrogenase, is activated only under conditions reminiscent of the cystic fibrosis lung (i.e. under high osmolarity), and at least two regulatory genes, AlgP and AlgQ, have been implicated in this activation process. TTYX5QR SQ MLESCRNAQERWGGVHQLIDRWLHERQQLVQAFDALSGIQAPAPNAEELQHFCQLLLDYVSAGHFEVYEQLTAEGKAFGDQRGLELAKQIFPRLEAITESALNFNDRCDNGDCREGACLIAELKVLRQQLHERFELEDCLIEVLHNAHSQSGAEGSAVPV TTYX5QR TT Literature-reported TT0CXNS ID TT0CXNS TT0CXNS TN Pseudomonas Indole-3-glycerol phosphate synthase (Pseudo trpC) TT0CXNS UP P20577 TT0CXNS UC TRPC_PSEAE TT0CXNS BC Carbon-carbon lyase TT0CXNS SN Indole-3-glycerol phosphate synthase; IGPS TT0CXNS GN Pseudo trpC TT0CXNS FC Catalyzes the fifth reaction in the synthesis of tryptophan from chorismate--a reaction that is absent in mammals. TT0CXNS SQ MSVPTVLQKILARKAEEVAERRARVNLAEVERLARSADAPRGFANALLERAKRKEPAVIAEIKKASPSKGVLREHFVPAEIARSYEAGGAACLSVLTDVDFFQGADAYLKEARAACALPVIRKDFMIDPYQIVEARAIGADCILLIVSALDDVLMAELAATAKSVGLDVLVEVHDGTELERALKTLDTPLVGINNRNLHTFEVSLETTLDLLPEIPRDRLVVTESGILNRADVELMEVSEVYAFLVGEAFMRADDPGLELKRLFFQERGAVVLGADPD TT0CXNS TT Literature-reported TTLQ3OP ID TTLQ3OP TTLQ3OP TN Pseudomonas Kynureninase (Pseudo kynU) TTLQ3OP UP Q9I235 TTLQ3OP UC Q9I235_PSEAE TTLQ3OP SN L-kynurenine hydrolase TTLQ3OP GN Pseudo kynU TTLQ3OP FC Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. TTLQ3OP EC EC 3.7.1.3 TTLQ3OP SQ MTTRDDCLALDAGDPLADLRQLFALPDGVIYLDGNSLGARPRAAVERAAEVVAAEWGEGLIRSWNSADWRGLPERLGDKLAPLIGARAGEVVITDTTSINLFKVLSAALRIQEEDAPGRKVIVSESSNFPTDLYIAEGLTDMLQRGYRLRLVDDPEQLPAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTYKYLNGGPGSPAYVWVAPRLRERVWQPLSGWFGHSRQFAMEPRYQPGEGITRFLCGTQPITSLALVECGLDIFARTDMQRLRDKSLALADLFIELVESRCERFGLTLVTPREHARRGSHVSFEHAQGYAIVQALIDRGVIGDYREPGILRFGFTPLYTRFVEVWDAVQALLEILQSEAWKEPRYQVRHKVT TTLQ3OP TT Preclinical TT7L1ZX ID TT7L1ZX TT7L1ZX TN Pseudomonas Multiple virulence factor regulator MvfR (Pseudo MvfR) TT7L1ZX UP Q9I4X0 TT7L1ZX UC MVFR_PSEAE TT7L1ZX SN Transcriptional regulator MvfR TT7L1ZX GN Pseudo MvfR TT7L1ZX FC Transcription regulator that plays a critical role in virulence by positively regulating the expression of multiple quorum sensing (QS)-regulated virulence factors, genes involved in protein secretion, translation, response to oxidative stress and the phnAB operon. At the stationary phase, negatively autoregulates its function through cleavage and translocation to the extracellular space. TT7L1ZX SQ MPIHNLNHVNMFLQVIASGSISSAARILRKSHTAVSSAVSNLEIDLCVELVRRDGYKVEPTEQALRLIPYMRSLLNYQQLIGDIAFNLNKGPRNLRVLLDTAIPPSFCDTVSSVLLDDFNMVSLIRTSPADSLATIKQDNAEIDIAITIDEELKISRFNQCVLGYTKAFVVAHPQHPLCNASLHSIASLANYRQISLGSRSGQHSNLLRPVSDKVLFVENFDDMLRLVEAGVGWGIAPHYFVEERLRNGTLAVLSELYEPGGIDTKVYCYYNTALESERSFLRFLESARQRLRELGRQRFDDAPAWQPSIVETAQRRSGPKALAYRQRAAPE TT7L1ZX TT Preclinical TTOMVUW ID TTOMVUW TTOMVUW TN Pseudomonas Transcriptional activator protein LasR (Pseudo LasR) TTOMVUW UP P25084 TTOMVUW UC LASR_PSEAE TTOMVUW GN Pseudo LasR TTOMVUW FC Transcriptional activator of elastase structural gene (LasB). Binds to the PAI autoinducer. TTOMVUW SQ MALVDGFLELERSSGKLEWSAILQKMASDLGFSKILFGLLPKDSQDYENAFIVGNYPAAWREHYDRAGYARVDPTVSHCTQSVLPIFWEPSIYQTRKQHEFFEEASAAGLVYGLTMPLHGARGELGALSLSVEAENRAEANRFMESVLPTLWMLKDYALQSGAGLAFEHPVSKPVVLTSREKEVLQWCAIGKTSWEISVICNCSEANVNFHMGNIRRKFGVTSRRVAAIMAVNLGLITL TTOMVUW TT Preclinical TT50NTP ID TT50NTP TT50NTP TN Pseudomonas Type III secretion system protein PcrV (Pseudo pcrV) TT50NTP UP M4Q7H6 TT50NTP UC M4Q7H6_PSEAI TT50NTP SN Type III secretion system protein TT50NTP GN Pseudo pcrV TT50NTP FC Essential for cytotoxicity. Found both within the bacterial cytoplasm and localized extracellularly. TT50NTP PD 6CYF TT50NTP SQ MEVRNLNAARELFLDELLAASAAPASAEQEELLALLRSERIVLAHAGQPLSEAQVLKALAWLLAANPSAPPGQGLEVLREVLQARRQPGAQWDLREFLVSAYFSLHGRLDEDVIGVYKDVLQTQDGKRKALLDELKALTAELKVYSVIQSQINAALSARQGIRIDAGGIDLVDPTLYGYAVGDPRWKDSPEYALLSNLDTFSGKLSIKDFLSGSPKQSGELKGLSDEYPFEKDNNPVGNFATTVSDRSRPLNDKVNEKTTLLNDTSSRYNSAVEALNRFIQKYDSVLSDILSAI TT50NTP TT Literature-reported TTA7DU1 ID TTA7DU1 TTA7DU1 TN PtdIns(4)P-5-kinase 1 alpha (PIP5K1A) TTA7DU1 UP Q99755 TTA7DU1 UC PI51A_HUMAN TTA7DU1 SN Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha; Phosphatidylinositol 4-phosphate 5-kinase type I alpha; PIP5KIalpha; PIP5K1-alpha; 68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha TTA7DU1 GN PIP5K1A TTA7DU1 FC Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as actin cytoskeleton organization, cell adhesion, migration and phagocytosis. Required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of RAC1 to the plasma membrane. Together with PIP5K1C is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle ingestion by activating WAS that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Plays a role during calcium-induced keratinocyte differentiation. Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, diacylglycerol and inositol 1,4,5-trisphosphate that mobilize internal calcium and drive keratinocyte differentiation. Together with PIP5K1C have a role during embryogenesis. Functions also in the nucleus where acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs. Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes (By similarity). TTA7DU1 EC EC 2.7.1.68 TTA7DU1 SQ MASASSGPSSSVGFSSFDPAVPSCTLSSAASGIKRPMASEVLEARQDSYISLVPYASGMPIKKIGHRSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLMSIHNIDHAQREPLSSETQYSVDTRRPAPQKALYSTAMESIQGEARRGGTMETDDHMGGIPARNSKGERLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPLKPSPSKKFRSGSSFSRRAGSSGNSCITYQPSVSGEHKAQVTTKAEVEPGVHLGRPDVLPQTPPLEEISEGSPIPDPSFSPLVGETLQMLTTSTTLEKLEVAESEFTH TTA7DU1 TT Literature-reported TT9BQ50 ID TT9BQ50 TT9BQ50 TN Rac family small GTPase 3 (RAC3) TT9BQ50 UP P60763 TT9BQ50 UC RAC3_HUMAN TT9BQ50 SN p21-Rac3; Ras-related C3 botulinum toxin substrate 3 TT9BQ50 GN RAC3 TT9BQ50 FC Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner. TT9BQ50 PD 2QME; 2OV2; 2IC5; 2G0N; 2C2H TT9BQ50 SQ MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDLRDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKPGKKCTVF TT9BQ50 TT Literature-reported TT2AP5B ID TT2AP5B TT2AP5B TN Ras converting CAAX endopeptidase 1 (RCE1) TT2AP5B UP Q9Y256 TT2AP5B UC FACE2_HUMAN TT2AP5B SN hRCE1; RCE1B; RCE1A; RCE1 homolog; Prenyl protein-specific endoprotease 2; Farnesylated proteins-converting enzyme 2; FACE2; FACE-2; CAAX prenyl protease 2 TT2AP5B GN RCE1 TT2AP5B FC Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. Seems to be able to process K-Ras, N-Ras, H-Ras, RAP1B and G-gamma-1. TT2AP5B EC EC 3.4.22.- TT2AP5B SQ MAALGGDGLRLLSVSRPERPPESAALGGLGPGLCCWVSVFSCLSLACSYVGSLYVWKSELPRDHPAVIKRRFTSVLVVSSLSPLCVLLWRELTGIQPGTSLLTLMGFRLEGIFPAALLPLLLTMILFLGPLMQLSMDCPCDLADGLKVVLAPRSWARCLTDMRWLRNQVIAPLTEELVFRACMLPMLAPCMGLGPAVFTCPLFFGVAHFHHIIEQLRFRQSSVGNIFLSAAFQFSYTAVFGAYTAFLFIRTGHLIGPVLCHSFCNYMGFPAVCAALEHPQRRPLLAGYALGVGLFLLLLQPLTDPKLYGSLPLCVLLERAGDSEAPLCS TT2AP5B TT Literature-reported TTAJ746 ID TTAJ746 TTAJ746 TN Ras-related protein Rab-22A (Rab22a) TTAJ746 UP Q9UL26 TTAJ746 UC RB22A_HUMAN TTAJ746 BC Small GTPase TTAJ746 SN Rab-22; RAB22 TTAJ746 GN RAB22A TTAJ746 FC Mediates trafficking of TF from early endosomes to recycling endosomes. Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite outgrowth. Binds GTP and GDP and has low GTPase activity. Alternates between a GTP-bound active form and a GDP-bound inactive form. Plays a role in endocytosis and intracellular protein transport. TTAJ746 SQ MALRELKVCLLGDTGVGKSSIVWRFVEDSFDPNINPTIGASFMTKTVQYQNELHKFLIWDTAGQERFRALAPMYYRGSAAAIIVYDITKEETFSTLKNWVKELRQHGPPNIVVAIAGNKCDLIDVREVMERDAKDYADSIHAIFVETSAKNAININELFIEISRRIPSTDANLPSGGKGFKLRRQPSEPKRSCC TTAJ746 TT Literature-reported TTAJ746 FM Small GTPase superfamily TT72D4Z ID TT72D4Z TT72D4Z TN Recombining binding protein suppressor of hairless (RBPJ) TT72D4Z UP Q06330 TT72D4Z UC SUH_HUMAN TT72D4Z SN Renal carcinoma antigen NY-REN-30; RBPSUH; RBPJK; RBP-JK; RBP-J kappa; RBP-J; J kappa-recombination signal-binding protein; IGKJRB1; IGKJRB; CBF-1 TT72D4Z GN RBPJ TT72D4Z FC Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some NICD product of Notch proteins (Notch intracellular domain), it acts as a transcriptional activator that activates transcription of Notch target genes. Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively. Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence. Binds specifically to methylated DNA. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by repressing transcription of NADPH oxidase subunits. Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations. TT72D4Z PD 3V79; 3NBN; 2F8X TT72D4Z SQ MDHTEGSPAEEPPAHAPSPGKFGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNADLCIASGTKVALFNRLRSQTVSTRYLHVEGGNFHASSQQWGAFFIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQATPCPKEPNKEMINDGASWTIISTDKAEYTFYEGMGPVLAPVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLVRNDGIIYSTSLTFTYTPEPGPRPHCSAAGAILRANSSQVPPNESNTNSEGSYTNASTNSTSVTSSTATVVS TT72D4Z TT Literature-reported TTVZEHU ID TTVZEHU TTVZEHU TN Regenerating islet-derived protein IV (REG4) TTVZEHU UP Q9BYZ8 TTVZEHU UC REG4_HUMAN TTVZEHU SN Regenerating islet-derived protein 4; Regenerating islet-derived family, member 4; Reg IV; RELP; REGIV; REG-like protein; REG-4; Gastrointestinal secretory protein GISP; Gastrointestinal secretory protein; GISP TTVZEHU GN REG4 TTVZEHU FC May be involved in inflammatory and metaplastic responses of the gastrointestinal epithelium. Calcium-independent lectin displaying mannose-binding specificity and able to maintain carbohydrate recognition activity in an acidic environment. TTVZEHU PD 2KV3 TTVZEHU SQ MASRSMRLLLLLSCLAKTGVLGDIIMRPSCAPGWFYHKSNCYGYFRKLRNWSDAELECQSYGNGAHLASILSLKEASTIAEYISGYQRSQPIWIGLHDPQKRQQWQWIDGAMYLYRSWSGKSMGGNKHCAEMSSNNNFLTWSSNECNKRQHFLCKYRP TTVZEHU TT Literature-reported TTP9AV7 ID TTP9AV7 TTP9AV7 TN Regulator of G-protein signaling 12 (RGS12) TTP9AV7 UP O14924 TTP9AV7 UC RGS12_HUMAN TTP9AV7 SN RGS12 TTP9AV7 GN RGS12 TTP9AV7 FC Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. TTP9AV7 PD 2KV8; 2EBZ TTP9AV7 SQ MFRAGEASKRPLPGPSPPRVRSVEVARGRAGYGFTLSGQAPCVLSCVMRGSPADFVGLRAGDQILAVNEINVKKASHEDVVKLIGKCSGVLHMVIAEGVGRFESCSSDEEGGLYEGKGWLKPKLDSKALGINRAERVVEEMQSGGIFNMIFENPSLCASNSEPLKLKQRSLSESAATRFDVGHESINNPNPNMLSKEEISKVIHDDSVFSIGLESHDDFALDASILNVAMIVGYLGSIELPSTSSNLESDSLQAIRGCMRRLRAEQKIHSLVTMKIMHDCVQLSTDKAGVVAEYPAEKLAFSAVCPDDRRFFGLVTMQTNDDGSLAQEEEGALRTSCHVFMVDPDLFNHKIHQGIARRFGFECTADPDTNGCLEFPASSLPVLQFISVLYRDMGELIEGMRARAFLDGDADAHQNNSTSSNSDSGIGNFHQEEKSNRVLVVDLGGSSSRHGPGGSAWDGVGGRGAQPWGAPWTGPFCPDPEGSPPFEAAHQTDRFWDLNKHLGPASPVEVPPASLRSSVPPSKRGTVGAGCGFNQRWLPVHVLREWQCGHTSDQDSYTDSTDGWSSINCGTLPPPMSKIPADRYRVEGSFAQPPLNAPKREWSRKAFGMQSIFGPHRNVRKTKEDKKGSKFGRGTGLTQPSQRTSARRSFGRSKRFSITRSLDDLESATVSDGELTGADLKDCVSNNSLSSNASLPSVQSCRRLRERRVASWAVSFERLLQDPVGVRYFSDFLRKEFSEENILFWQACEYFNHVPAHDKKELSYRAREIFSKFLCSKATTPVNIDSQAQLADDVLRAPHPDMFKEQQLQIFNLMKFDSYTRFLKSPLYQECILAEVEGRALPDSQQVPSSPASKHSLGSDHSSVSTPKKLSGKSKSGRSLNEELGDEDSEKKRKGAFFSWSRTRSTGRSQKKREHGDHADDALHANGGLCRRESQGSVSSAGSLDLSEACRTLAPEKDKATKHCCIHLPDGTSCVVAVKAGFSIKDILSGLCERHGINGAAADLFLVGGDKPLVLHQDSSILESRDLRLEKRTLFRLDLVPINRSVGLKAKPTKPVTEVLRPVVARYGLDLSGLLVRLSGEKEPLDLGAPISSLDGQRVVLEEKDPSRGKASADKQKGVPVKQNTAVNSSSRNHSATGEERTLGKSNSIKIKGENGKNARDPRLSKREESIAKIGKKKYQKINLDEAEEFFELISKAQSNRADDQRGLLRKEDLVLPEFLRLPPGSTELTLPTPAAVAKGFSKRSATGNGRESASQPGEQWEPVQESSDSPSTSPGSASSPPGPPGTTPPGQKSPSGPFCTPQSPVSLAQEGTAQIWKRQSQEVEAGGIQTVEDEHVAELTLMGEGDISSPNSTLLPPPSTPQEVPGPSRPGSGTHGSRDLPVNRIIDVDLVTGSAPGRDGGIAGAQAGPGRSQASGGPPTSDLPGLGPVPGEPAKPKTSAHHATFV TTP9AV7 TT Literature-reported TTJ96M8 ID TTJ96M8 TTJ96M8 TN Regulator of G-protein signaling 6 (RGS6) TTJ96M8 UP P49758 TTJ96M8 UC RGS6_HUMAN TTJ96M8 SN S914 TTJ96M8 GN RGS6 TTJ96M8 FC Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. The RGS6/GNB5 dimer enhances GNAO1 GTPase activity. Regulates G protein-coupled receptor signaling cascades. TTJ96M8 PD 2ES0 TTJ96M8 SQ MAQGSGDQRAVGVADPEESSPNMIVYCKIEDIITKMQDDKTGGVPIRTVKSFLSKIPSVVTGTDIVQWLMKNLSIEDPVEAIHLGSLIAAQGYIFPISDHVLTMKDDGTFYRFQAPYFWPSNCWEPENTDYAIYLCKRTMQNKARLELADYEAENLARLQRAFARKWEFIFMQAEAQVKIDRKKDKTERKILDSQERAFWDVHRPVPGCVNTTEMDIRKCRRLKNPQKVKKSVYGVTEESQAQSPVHVLSQPIRKTTKEDIRKQITFLNAQIDRHCLKMSKVAESLIAYTEQYVEYDPLITPAEPSNPWISDDVALWDIEMSKEPSQQRVKRWGFSFDEILKDQVGRDQFLRFLESEFSSENLRFWLAVQDLKKQPLQDVAKRVEEIWQEFLAPGAPSAINLDSHSYEITSQNVKDGGRYTFEDAQEHIYKLMKSDSYARFLRSNAYQDLLLAKKKGKSLAGKRLTGLMQSS TTJ96M8 TT Literature-reported TTWME23 ID TTWME23 TTWME23 TN Regulator of G-protein signaling 8 (RGS8) TTWME23 UP P57771 TTWME23 UC RGS8_HUMAN TTWME23 SN RGS8 TTWME23 GN RGS8 TTWME23 FC Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to DRD2 and CHRM2 signaling (By similarity). TTWME23 PD 5DO9; 2ODE; 2IHD TTWME23 SQ MAALLMPRRNKGMRTRLGCLSHKSDSCSDFTAILPDKPNRALKRLSTEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTAKLVSKAHRIFEEFVDVQAPREVNIDFQTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLDLLSQSQRRLS TTWME23 TT Patented-recorded TTVS4C3 ID TTVS4C3 TTVS4C3 TN Retinoid-inducible nuclear factor (CXXC5) TTVS4C3 UP Q7LFL8 TTVS4C3 UC CXXC5_HUMAN TTVS4C3 SN TCCCIA00297; Retinoidinducible nuclear factor; RINF; Putative NFkappaBactivating protein 102; Putative NF-kappa-B-activating protein 102; Putative MAPKactivating protein PM08; Putative MAPK-activating protein PM08; HSPC195; CXXCtype zinc finger protein 5; CXXC-type zinc finger protein 5; CF5 TTVS4C3 GN CXXC5 TTVS4C3 FC Acts as a mediator of BMP4-mediated modulation of canonical Wnt signaling activity in neural stem cells. Required for DNA damage-induced ATM phosphorylation, p53 activation and cell cycle arrest. Involved in myelopoiesis. Transcription factor. Binds to the oxygen responsive element of COX4I2 and represses its transcription under hypoxia conditions (4% oxygen), as well as normoxia conditions (20% oxygen). May repress COX4I2 transactivation induced by CHCHD2 and RBPJ. May indirectly participate in activation of the NF-kappa-B and MAPK pathways. TTVS4C3 PD 5W9S TTVS4C3 SQ MSSLGGGSQDAGGSSSSSTNGSGGSGSSGPKAGAADKSAVVAAAAPASVADDTPPPERRNKSGIISEPLNKSLRRSRPLSHYSSFGSSGGSGGGSMMGGESADKATAAAAAASLLANGHDLAAAMAVDKSNPTSKHKSGAVASLLSKAERATELAAEGQLTLQQFAQSTEMLKRVVQEHLPLMSEAGAGLPDMEAVAGAEALNGQSDFPYLGAFPINPGLFIMTPAGVFLAESALHMAGLAEYPMQGELASAISSGKKKRKRCGMCAPCRRRINCEQCSSCRNRKTGHQICKFRKCEELKKKPSAALEKVMLPTGAAFRWFQ TTVS4C3 TT Literature-reported TTT2CZY ID TTT2CZY TTT2CZY TN Retinoschisin (RS1) TTT2CZY UP O15537 TTT2CZY UC XLRS1_HUMAN TTT2CZY SN X-linked juvenile retinoschisis protein; RS1 TTT2CZY GN RS1 TTT2CZY FC May be active in cell adhesion processes during retinal development. TTT2CZY PD 5N6W; 3JD6 TTT2CZY SQ MSRKIEGFLLLLLFGYEATLGLSSTEDEGEDPWYQKACKCDCQGGPNALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKFQDSSQWLQIDLKEIKVISGILTQGRCDIDEWMTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRTSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECVSKCA TTT2CZY TT Clinical trial TTFX379 ID TTFX379 TTFX379 TN Rhombotin-2 (LMO2) TTFX379 UP P25791 TTFX379 UC RBTN2_HUMAN TTFX379 SN TTG2; T-cell translocation protein 2; RHOM2; RBTNL1; RBTN2; LMO-2; LIM-only protein 2; LIM-domain protein Lmo2; LIM domain only protein 2; Cysteine-rich protein TTG-2; Cysteine rich protein TTG-2 TTFX379 GN LMO2 TTFX379 FC Acts with LDB1 to maintain erythroid precursors in an immature state. Acts with TAL1/SCL to regulate red blood cell development. TTFX379 PD 4KFZ; 2YPA; 2XJZ; 2XJY TTFX379 SQ MSSAIERKSLDPSEEPVDEVLQIPPSLLTCGGCQQNIGDRYFLKAIDQYWHEDCLSCDLCGCRLGEVGRRLYYKLGRKLCRRDYLRLFGQDGLCASCDKRIRAYEMTMRVKDKVYHLECFKCAACQKHFCVGDRYLLINSDIVCEQDIYEWTKINGMI TTFX379 TT Literature-reported TTY1QGP ID TTY1QGP TTY1QGP TN Rotavirus Toxin (Rota TOX) TTY1QGP UP P04512 TTY1QGP UC NSP4_ROTS1 TTY1QGP SN Non-structural glycoprotein 4; NSP4; NS28; NCVP5 TTY1QGP GN Rota TOX TTY1QGP FC Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly. TTY1QGP PD 2O1K; 1G1J; 1G1I TTY1QGP SQ MEKLTDLNYTLSVITLMNNTLHTILEDPGMAYFPYIASVLTGLFALNKASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMDRVVKEMRRQLEMIDKLTTREIEQVELLKRIYDKLTVQTTGEIDMTKEINQKNVRTLEEWESGKNPYEPREVTAAM TTY1QGP TT Literature-reported TTND1YP ID TTND1YP TTND1YP TN Roundabout homolog 1 (ROBO1) TTND1YP UP Q9Y6N7 TTND1YP UC ROBO1_HUMAN TTND1YP SN H-Robo-1; Deleted in U twenty twenty; DUTT1 TTND1YP GN ROBO1 TTND1YP FC Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1. In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA. May be required for lung development (By similarity). TTND1YP PD 6A79; 6A78; 6A77; 5OPE; 5O5I TTND1YP SQ MKWKHVPFLVMISLLSLSPNHLFLAQLIPDPEDVERGNDHGTPIPTSDNDDNSLGYTGSRLRQEDFPPRIVEHPSDLIVSKGEPATLNCKAEGRPTPTIEWYKGGERVETDKDDPRSHRMLLPSGSLFFLRIVHGRKSRPDEGVYVCVARNYLGEAVSHNASLEVAILRDDFRQNPSDVMVAVGEPAVMECQPPRGHPEPTISWKKDGSPLDDKDERITIRGGKLMITYTRKSDAGKYVCVGTNMVGERESEVAELTVLERPSFVKRPSNLAVTVDDSAEFKCEARGDPVPTVRWRKDDGELPKSRYEIRDDHTLKIRKVTAGDMGSYTCVAENMVGKAEASATLTVQEPPHFVVKPRDQVVALGRTVTFQCEATGNPQPAIFWRREGSQNLLFSYQPPQSSSRFSVSQTGDLTITNVQRSDVGYYICQTLNVAGSIITKAYLEVTDVIADRPPPVIRQGPVNQTVAVDGTFVLSCVATGSPVPTILWRKDGVLVSTQDSRIKQLENGVLQIRYAKLGDTGRYTCIASTPSGEATWSAYIEVQEFGVPVQPPRPTDPNLIPSAPSKPEVTDVSRNTVTLSWQPNLNSGATPTSYIIEAFSHASGSSWQTVAENVKTETSAIKGLKPNAIYLFLVRAANAYGISDPSQISDPVKTQDVLPTSQGVDHKQVQRELGNAVLHLHNPTVLSSSSIEVHWTVDQQSQYIQGYKILYRPSGANHGESDWLVFEVRTPAKNSVVIPDLRKGVNYEIKARPFFNEFQGADSEIKFAKTLEEAPSAPPQGVTVSKNDGNGTAILVSWQPPPEDTQNGMVQEYKVWCLGNETRYHINKTVDGSTFSVVIPFLVPGIRYSVEVAASTGAGSGVKSEPQFIQLDAHGNPVSPEDQVSLAQQISDVVKQPAFIAGIGAACWIILMVFSIWLYRHRKKRNGLTSTYAGIRKVPSFTFTPTVTYQRGGEAVSSGGRPGLLNISEPAAQPWLADTWPNTGNNHNDCSISCCTAGNGNSDSNLTTYSRPADCIANYNNQLDNKQTNLMLPESTVYGDVDLSNKINEMKTFNSPNLKDGRFVNPSGQPTPYATTQLIQSNLSNNMNNGSGDSGEKHWKPLGQQKQEVAPVQYNIVEQNKLNKDYRANDTVPPTIPYNQSYDQNTGGSYNSSDRGSSTSGSQGHKKGARTPKVPKQGGMNWADLLPPPPAHPPPHSNSEEYNISVDESYDQEMPCPVPPARMYLQQDELEEEEDERGPTPPVRGAASSPAAVSYSHQSTATLTPSPQEELQPMLQDCPEETGHMQHQPDRRRQPVSPPPPPRPISPPHTYGYISGPLVSDMDTDAPEEEEDEADMEVAKMQTRRLLLRGLEQTPASSVGDLESSVTGSMINGWGSASEEDNISSGRSSVSSSDGSFFTDADFAQAVAAAAEYAGLKVARRQMQDAAGRRHFHASQCPRPTSPVSTDSNMSAAVMQKTRPAKKLKHQPGHLRRETYTDDLPPPPVPPPAIKSPTAQSKTQLEVRPVVVPKLPSMDARTDRSSDRKGSSYKGREVLDGRQVVDMRTNPGDPREAQEQQNDGKGRGNKAAKRDLPPAKTHLIQEDILPYCRPTFPTSNNPRDPSSSSSMSSRGSGSRQREQANVGRRNIAEMQVLGGYERGEDNNEELEETES TTND1YP TT Literature-reported TT3S9TY ID TT3S9TY TT3S9TY TN Roundabout homolog 4 (ROBO4) TT3S9TY UP Q8WZ75 TT3S9TY UC ROBO4_HUMAN TT3S9TY BC Immunoglobulin TT3S9TY SN ROBO4; Magic roundabout TT3S9TY GN ROBO4 TT3S9TY FC Receptor for Slit proteins, at least for SLIT2, and seemsto be involved in angiogenesis and vascular patterning. May mediate the inhibition of primary endothelial cell migration by Slit proteins. TT3S9TY SQ MGSGGDSLLGGRGSLPLLLLLIMGGMAQDSPPQILVHPQDQLFQGPGPARMSCQASGQPPPTIRWLLNGQPLSMVPPDPHHLLPDGTLLLLQPPARGHAHDGQALSTDLGVYTCEASNRLGTAVSRGARLSVAVLREDFQIQPRDMVAVVGEQFTLECGPPWGHPEPTVSWWKDGKPLALQPGRHTVSGGSLLMARAEKSDEGTYMCVATNSAGHRESRAARVSIQEPQDYTEPVELLAVRIQLENVTLLNPDPAEGPKPRPAVWLSWKVSGPAAPAQSYTALFRTQTAPGGQGAPWAEELLAGWQSAELGGLHWGQDYEFKVRPSSGRARGPDSNVLLLRLPEKVPSAPPQEVTLKPGNGTVFVSWVPPPAENHNGIIRGYQVWSLGNTSLPPANWTVVGEQTQLEIATHMPGSYCVQVAAVTGAGAGEPSRPVCLLLEQAMERATQEPSEHGPWTLEQLRATLKRPEVIATCGVALWLLLLGTAVCIHRRRRARVHLGPGLYRYTSEDAILKHRMDHSDSQWLADTWRSTSGSRDLSSSSSLSSRLGADARDPLDCRRSLLSWDSRSPGVPLLPDTSTFYGSLIAELPSSTPARPSPQVPAVRRLPPQLAQLSSPCSSSDSLCSRRGLSSPRLSLAPAEAWKAKKKQELQHANSSPLLRGSHSLELRACELGNRGSKNLSQSPGAVPQALVAWRALGPKLLSSSNELVTRHLPPAPLFPHETPPTQSQQTQPPVAPQAPSSILLPAAPIPILSPCSPPSPQASSLSGPSPASSRLSSSSLSSLGEDQDSVLTPEEVALCLELSEGEETPRNSVSPMPRAPSPPTTYGYISVPTASEFTDMGRTGGGVGPKGGVLLCPPRPCLTPTPSEGSLANGWGSASEDNAASARASLVSSSDGSFLADAHFARALAVAVDSFGFGLEPREADCVFIDASSPPSPRDEIFLTPNLSLPLWEWRPDWLEDMEVSHTQRLGRGMPPWPPDSQISSQRSQLHCRMPKAGASPVDYS TT3S9TY TT Literature-reported TTWIN3H ID TTWIN3H TTWIN3H TN Runt-related transcription factor 1 (RUNX1) TTWIN3H UP Q01196 TTWIN3H UC RUNX1_HUMAN TTWIN3H SN SL3/AKV core-binding factor alpha B subunit; SL3-3 enhancer factor 1 alpha B subunit; Polyomavirus enhancer-binding protein 2 alpha B subunit; PEBP2-alpha B; PEA2-alpha B; Oncogene AML-1; Core-binding factor subunit alpha-2; CBFA2; CBF-alpha-2; Acute myeloid leukemia 1 protein; AML1 TTWIN3H GN RUNX1 TTWIN3H FC Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). Essential for the development of normal hematopoiesis. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter. Inhibits KAT6B-dependent transcriptional activation (By similarity). Involved in lineage commitment of immature T cell precursors. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (By similarity). Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells. Positively regulates the expression of RORC in T-helper 17 cells (By similarity). TTWIN3H PD 1LJM; 1H9D; 1CO1; 1CMO; 1.00E+50 TTWIN3H SQ MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPVTSGIGIGMSAMGSATRYHTYLPPPYPGSSQAQGGPFQASSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGSALLNPSLPNQSDVVEAEGSHSNSPTNMAPSARLEEAVWRPY TTWIN3H TT Literature-reported TTKCVO7 ID TTKCVO7 TTKCVO7 TN Runt-related transcription factor 3 (RUNX3) TTKCVO7 UP Q13761 TTKCVO7 UC RUNX3_HUMAN TTKCVO7 SN SL3/AKV core-binding factor alpha C subunit; SL3-3 enhancer factor 1 alpha C subunit; Polyomavirus enhancer-binding protein 2 alpha C subunit; PEBP2A3; PEBP2-alpha C; PEA2-alpha C; Oncogene AML-2; Core-binding factor subunit alpha-3; CBFA3; CBF-alpha-3; Acute myeloid leukemia 2 protein; AML2 TTKCVO7 GN RUNX3 TTKCVO7 FC RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. May be involved in the control of cellular proliferation and/or differentiation. In association with ZFHX3, upregulates CDKN1A promoter activity following TGF-beta stimulation. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing. Forms the heterodimeric complex core-binding factor (CBF) with CBFB. TTKCVO7 PD 5W69 TTKCVO7 SQ MRIPVDPSTSRRFTPPSPAFPCGGGGGKMGENSGALSAQAAVGPGGRARPEVRSMVDVLADHAGELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGDVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPTQVATYHRAIKVTVDGPREPRRHRQKLEDQTKPFPDRFGDLERLRMRVTPSTPSPRGSLSTTSHFSSQPQTPIQGTSELNPFSDPRQFDRSFPTLPTLTESRFPDPRMHYPGAMSAAFPYSATPSGTSISSLSVAGMPATSRFHHTYLPPPYPGAPQNQSGPFQANPSPYHLYYGTSSGSYQFSMVAGSSSGGDRSPTRMLASCTSSAASVAAGNLMNPSLGGQSDGVEADGSHSNSPTALSTPGRMDEAVWRPY TTKCVO7 TT Literature-reported TTIXUDE ID TTIXUDE TTIXUDE TN S100 calcium-binding protein G (S100G) TTIXUDE UP P29377 TTIXUDE UC S100G_HUMAN TTIXUDE BC S100 calcium-binding protein TTIXUDE SN Vitamin D-dependent calcium-binding protein, intestinal; S100D; Protein S100-G; Calbindin-D9k; CALB3; CABP9K; CABP TTIXUDE GN S100G TTIXUDE FC Vitamin D-dependent. Its expression correlates with calcium transport activity. May increase Ca2+ absorption by buffering Ca2+ in the cytoplasm and increase ATP-dependent Ca2+ transport in duodenal basolateral membrane vesicles. TTIXUDE SQ MSTKKSPEELKRIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLLKGPNTLDDLFQELDKNGDGEVSFEEFQVLVKKISQ TTIXUDE TT Literature-reported TT0Y754 ID TT0Y754 TT0Y754 TN Saccharomyces Casein Kinase I Isoform Hrr25 (Saccha HRR25) TT0Y754 UP P29295 TT0Y754 UC HRR25_YEAST TT0Y754 SN Casein kinase I homolog HRR25 TT0Y754 GN Saccha HRR25 TT0Y754 FC Associated with repair of damaged DNA and meiosis. Phosphorylates serine and threonine. Can use casein as a substrate. TT0Y754 PD 5CZO; 5CYZ; 4XHL TT0Y754 SQ MDLRVGRKFRIGRKIGSGSFGDIYHGTNLISGEEVAIKLESIRSRHPQLDYESRVYRYLSGGVGIPFIRWFGREGEYNAMVIDLLGPSLEDLFNYCHRRFSFKTVIMLALQMFCRIQYIHGRSFIHRDIKPDNFLMGVGRRGSTVHVIDFGLSKKYRDFNTHRHIPYRENKSLTGTARYASVNTHLGIEQSRRDDLESLGYVLIYFCKGSLPWQGLKATTKKQKYDRIMEKKLNVSVETLCSGLPLEFQEYMAYCKNLKFDEKPDYLFLARLFKDLSIKLEYHNDHLFDWTMLRYTKAMVEKQRDLLIEKGDLNANSNAASASNSTDNKSETFNKIKLLAMKKFPTHFHYYKNEDKHNPSPEEIKQQTILNNNAASSLPEELLNALDKGMENLRQQQPQQQVQSSQPQPQPQQLQQQPNGQRPNYYPEPLLQQQQRDSQEQQQQVPMATTRATQYPPQINSNNFNTNQASVPPQMRSNPQQPPQDKPAGQSIWL TT0Y754 TT Literature-reported TT75YK4 ID TT75YK4 TT75YK4 TN Saccharomyces Cell division control protein 28 (Saccha CDC28) TT75YK4 UP P00546 TT75YK4 UC CDK1_YEAST TT75YK4 BC Kinase TT75YK4 SN YBR160W; YBR1211; SRM5; HSL5; Cyclindependent kinase 1 of Saccharomyces cerevisiae; Cell division protein kinase 1; Cell division control protein 28; CDK1 of Saccharomyces cerevisiae; CDK1; CDC28 TT75YK4 GN Saccha CDC28 TT75YK4 FC More than 200 substrates have been identified. This protein is essential for the completion of the start, the controlling event, in the cell cycle. TT75YK4 SQ MSGELANYKRLEKVGEGTYGVVYKALDLRPGQGQRVVALKKIRLESEDEGVPSTAIREISLLKELKDDNIVRLYDIVHSDAHKLYLVFEFLDLDLKRYMEGIPKDQPLGADIVKKFMMQLCKGIAYCHSHRILHRDLKPQNLLINKDGNLKLGDFGLARAFGVPLRAYTHEIVTLWYRAPEVLLGGKQYSTGVDTWSIGCIFAEMCNRKPIFSGDSEIDQIFKIFRVLGTPNEAIWPDIVYLPDFKPSFPQWRRKDLSQVVPSLDPRGIDLLDKLLAYDPINRISARRAAIHPYFQES TT75YK4 TT Literature-reported TTSMT9W ID TTSMT9W TTSMT9W TN Sarcoglycan gamma (SGCG) TTSMT9W UP Q13326 TTSMT9W UC SGCG_HUMAN TTSMT9W BC Sarcoglycan TTSMT9W SN SGCG; Gammasarcoglycan; GammaSG; 35DAG; 35 kDa dystrophinassociated glycoprotein TTSMT9W GN SGCG TTSMT9W FC Component of the sarcoglycan complex, a subcomplexof the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. TTSMT9W SQ MVREQYTTATEGICIERPENQYVYKIGIYGWRKRCLYLFVLLLLIILVVNLALTIWILKVMWFSPAGMGHLCVTKDGLRLEGESEFLFPLYAKEIHSRVDSSLLLQSTQNVTVNARNSEGEVTGRLKVGPKMVEVQNQQFQINSNDGKPLFTVDEKEVVVGTDKLRVTGPEGALFEHSVETPLVRADPFQDLRLESPTRSLSMDAPRGVHIQAHAGKIEALSQMDILFHSSDGMLVLDAETVCLPKLVQGTWGPSGSSQSLYEICVCPDGKLYLSVAGVSTTCQEHNHICL TTSMT9W TT Literature-reported TT2TDH9 ID TT2TDH9 TT2TDH9 TN Scavenger receptor A1 (MSR1) TT2TDH9 UP P21757 TT2TDH9 UC MSRE_HUMAN TT2TDH9 SN Macrophage scavenger receptor; Macrophage acetylated LDL receptor I and II; MSR1; CD204 antigen TT2TDH9 GN MSR1 TT2TDH9 FC Membrane glycoproteins implicated in the pathologic deposition of cholesterol in arterial walls during atherogenesis. Two types of receptor subunits exist. These receptors mediate the endocytosis of a diverse group of macromolecules, including modified low density lipoproteins (LDL). Isoform III does not internalize acetylated LDL. TT2TDH9 SQ MEQWDHFHNQQEDTDSCSESVKFDARSMTALLPPNPKNSPSLQEKLKSFKAALIALYLLVFAVLIPLIGIVAAQLLKWETKNCSVSSTNANDITQSLTGKGNDSEEEMRFQEVFMEHMSNMEKRIQHILDMEANLMDTEHFQNFSMTTDQRFNDILLQLSTLFSSVQGHGNAIDEISKSLISLNTTLLDLQLNIENLNGKIQENTFKQQEEISKLEERVYNVSAEIMAMKEEQVHLEQEIKGEVKVLNNITNDLRLKDWEHSQTLRNITLIQGPPGPPGEKGDRGPTGESGPRGFPGPIGPPGLKGDRGAIGFPGSRGLPGYAGRPGNSGPKGQKGEKGSGNTLTPFTKVRLVGGSGPHEGRVEILHSGQWGTICDDRWEVRVGQVVCRSLGYPGVQAVHKAAHFGQGTGPIWLNEVFCFGRESSIEECKIRQWGTRACSHSEDAGVTCTL TT2TDH9 TT Literature-reported TT2TDH9 KE hsa04145:Phagosome TT2TDH9 RC R-HSA-3000480:Scavenging by Class A Receptors TTRE324 ID TTRE324 TTRE324 TN Scavenger receptor class B member 1 (SCARB1) TTRE324 UP Q8WTV0 TTRE324 UC SCRB1_HUMAN TTRE324 BC Long chain fatty acid translocase TTRE324 SN SRB1; SR-BI; Collagen type I receptor, thrombospondin receptor-like 1; CLA1; CLA-1; CD36L1; CD36 antigen-like 1; CD36 and LIMPII analogous 1; CD36 TTRE324 GN SCARB1 TTRE324 FC Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells. Receptor for HDL, mediating selective uptake of cholesteryl ether and HDL-dependent cholesterol efflux. Also facilitates the flux of free and esterified cholesterol between the cell surface and apoB-containing lipoproteins and modified lipoproteins, although less efficiently than HDL. May be involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity. TTRE324 SQ MGCSAKARWAAGALGVAGLLCAVLGAVMIVMVPSLIKQQVLKNVRIDPSSLSFNMWKEIPIPFYLSVYFFDVMNPSEILKGEKPQVRERGPYVYREFRHKSNITFNNNDTVSFLEYRTFQFQPSKSHGSESDYIVMPNILVLGAAVMMENKPMTLKLIMTLAFTTLGERAFMNRTVGEIMWGYKDPLVNLINKYFPGMFPFKDKFGLFAELNNSDSGLFTVFTGVQNISRIHLVDKWNGLSKVDFWHSDQCNMINGTSGQMWPPFMTPESSLEFYSPEACRSMKLMYKESGVFEGIPTYRFVAPKTLFANGSIYPPNEGFCPCLESGIQNVSTCRFSAPLFLSHPHFLNADPVLAEAVTGLHPNQEAHSLFLDIHPVTGIPMNCSVKLQLSLYMKSVAGIGQTGKIEPVVLPLLWFAESGAMEGETLHTFYTQLVLMPKVMHYAQYVLLALGCVLLLVPVICQIRSQVGAGQRAARADSHSLACWGKGASDRTLWPTAAWSPPPAAVLRLCRSGSGHCWGLRSTLASFACRVATTLPVLEGLGPSLGGGTGS TTRE324 TT Literature-reported TTRE324 FM Long chain fatty acid translocase TTAGE7U ID TTAGE7U TTAGE7U TN Septin-6 (SEPT6) TTAGE7U UP Q14141 TTAGE7U UC SEPT6_HUMAN TTAGE7U SN KIAA0128 TTAGE7U GN SEPTIN6 TTAGE7U FC Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis. May play a role in HCV RNA replication. TTAGE7U PD 2QAG TTAGE7U SQ MAATDIARQVGEGCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLQSNTYDLQESNVRLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHTYHDSRIHVCLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADAISKSELTKFKIKITSELVSNGVQIYQFPTDDESVAEINGTMNAHLPFAVIGSTEELKIGNKMMRARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQDEKKKLEDKKKSLDDEVNAFKQRKTAAELLQSQGSQAGGSQTLKRDKEKKNNPWLCTE TTAGE7U TT Literature-reported TTCHB06 ID TTCHB06 TTCHB06 TN Serglycin (SRGN) TTCHB06 UP P10124 TTCHB06 UC SRGN_HUMAN TTCHB06 BC Serglycin family TTCHB06 SN Secretory granule proteoglycan core protein; Platelet proteoglycan core protein; PRG1; PRG; P.PG; Hematopoietic proteoglycan core protein TTCHB06 GN SRGN TTCHB06 FC Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF-alpha and may also regulate protease secretion. Inhibits bone mineralization. TTCHB06 SQ MMQKLLKCSRLVLALALILVLESSVQGYPTRRARYQWVRCNPDSNSANCLEEKGPMFELLPGESNKIPRLRTDLFPKTRIQDLNRIFPLSEDYSGSGFGSGSGSGSGSGSGFLTEMEQDYQLVDESDAFHDNLRSLDRNLPSDSQDLGQHGLEEDFML TTCHB06 TT Literature-reported TTZVMA7 ID TTZVMA7 TTZVMA7 TN Serine palmitoyltransferase (SPTC) TTZVMA7 UP O15269; O15270; Q9NUV7 TTZVMA7 UC SPTC1_HUMAN; SPTC2_HUMAN; SPTC3_HUMAN TTZVMA7 BC Acyltransferase TTZVMA7 SN Serine-palmitoyl-CoA transferase; SPT; Long chain base biosynthesis protein; LCB TTZVMA7 GN SPTLC1; SPTLC2; SPTLC3 TTZVMA7 FC Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1- SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference. TTZVMA7 SQ MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEELIEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAAALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCMNRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL TTZVMA7 TT Literature-reported TT4DFM2 ID TT4DFM2 TT4DFM2 TN Serine/arginine-rich splicing factor 12 (Srrp35) TT4DFM2 UP Q8WXF0 TT4DFM2 UC SRS12_HUMAN TT4DFM2 BC Splicing factor SR family TT4DFM2 SN Splicing factor, arginine/serine-rich 19; Splicing factor, arginine/serine-rich 13B; SRSF12; 35 kDa SR repressor protein TT4DFM2 GN SRSF12 TT4DFM2 FC Splicing factor that seems to antagonize SR proteins in pre-mRNA splicing regulation. TT4DFM2 SQ MSRYTRPPNTSLFIRNVADATRPEDLRREFGRYGPIVDVYIPLDFYTRRPRGFAYVQFEDVRDAEDALYNLNRKWVCGRQIEIQFAQGDRKTPGQMKSKERHPCSPSDHRRSRSPSQRRTRSRSSSWGRNRRRSDSLKESRHRRFSYSQSKSRSKSLPRRSTSARQSRTPRRNFGSRGRSRSKSLQKRSKSIGKSQSSSPQKQTSSGTKSRSHGRHSDSIARSPCKSPKGYTNSETKVQTAKHSHFRSHSRSRSYRHKNSW TT4DFM2 TT Literature-reported TT8I2M7 ID TT8I2M7 TT8I2M7 TN Serine/threonine-protein kinase Nek6 (NEK6) TT8I2M7 UP Q9HC98 TT8I2M7 UC NEK6_HUMAN TT8I2M7 SN Protein kinase SID6-1512; NimA-related protein kinase 6; Never in mitosis A-related kinase 6 TT8I2M7 GN NEK6 TT8I2M7 FC Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence. TT8I2M7 EC EC 2.7.11.1 TT8I2M7 SQ MAGQPGHMPHGGSSNNLCHTLGPVHPPDPQRHPNTLSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPGEHYSEKLRELVSMCICPDPHQRPDIGYVHQVAKQMHIWMSST TT8I2M7 TT Literature-reported TTFS1T2 ID TTFS1T2 TTFS1T2 TN Serpin I2 (SERPINI2) TTFS1T2 UP O75830 TTFS1T2 UC SPI2_HUMAN TTFS1T2 BC Serpin protein TTFS1T2 SN Peptidase inhibitor 14; Pancreas-specific protein TSA2004; Pancpin; PI14; PI-14; Myoepithelium-derived serine protease inhibitor; MEPI TTFS1T2 GN SERPINI2 TTFS1T2 FC A member of the plasminogen activator inhibitor-1 family, a subset of the serpin superfamily whose members act as tissue-specific tPA inhibitors.Plays central roles in the regulation of a wide variety of physiological processes, including coagulation, fibrinolysis, development, malignancy and inflammation. TTFS1T2 SQ MDTIFLWSLLLLFFGSQASRCSAQKNTEFAVDLYQEVSLSHKDNIIFSPLGITLVLEMVQLGAKGKAQQQIRQTLKQQETSAGEEFFVLKSFFSAISEKKQEFTFNLANALYLQEGFTVKEQYLHGNKEFFQSAIKLVDFQDAKACAEMISTWVERKTDGKIKDMFSGEEFGPLTRLVLVNAIYFKGDWKQKFRKEDTQLINFTKKNGSTVKIPMMKALLRTKYGYFSESSLNYQVLELSYKGDEFSLIIILPAEGMDIEEVEKLITAQQILKWLSEMQEEEVEISLPRFKVEQKVDFKDVLYSLNITEIFSGGCDLSGITDSSEVYVSQVTQKVFFEINEDGSEAATSTGIHIPVIMSLAQSQFIANHPFLFIMKHNPTESILFMGRVTNPDTQEIKGRDLDSL TTFS1T2 TT Literature-reported TTY0DN9 ID TTY0DN9 TTY0DN9 TN Serum amyloid A-1 protein (SAA1) TTY0DN9 UP P0DJI8 TTY0DN9 UC SAA1_HUMAN TTY0DN9 SN SAA TTY0DN9 GN SAA1 TTY0DN9 FC Major acute phase protein. TTY0DN9 PD 6MST; 4IP9; 4IP8 TTY0DN9 SQ MKLLTGLVFCSLVLGVSSRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY TTY0DN9 TT Literature-reported TTU68X4 ID TTU68X4 TTU68X4 TN Serum-and glucocorticoid-inducible kinase SGK (SGK) TTU68X4 UP O00141; Q9HBY8; Q96BR1 TTU68X4 UC SGK1_HUMAN; SGK2_HUMAN; SGK3_HUMAN TTU68X4 BC Kinase TTU68X4 SN Serum/glucocorticoid-regulated kinase; Serine/threonine-protein kinase Sgk; SGK TTU68X4 GN SGK1; SGK2; SGK3 TTU68X4 FC Invovled in ion channel and transporter regulation, regulation of cell volume, cell proliferation and apoptosis, memory formation, transcription and metabolism. TTU68X4 SQ MTVKTEAAKGTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKISQPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEVFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNSTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFMEIKSHVFFSLINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTEEPVPNSIGKSPDSVLVTASVKEAAEAFLGFSYAPPTDSFL TTU68X4 TT Literature-reported TTSJ9E7 ID TTSJ9E7 TTSJ9E7 TN Short transient receptor potential channel 2 (TRPC2) TTSJ9E7 UP Q3C1U7 TTSJ9E7 UC Q3C1U7_HUMAN TTSJ9E7 BC Transient receptor potential catioin channel TTSJ9E7 SN Uncharacterized protein TTSJ9E7 GN TRPC2 TTSJ9E7 FC Has calcium channel activity. TTSJ9E7 SQ SCACLECSNARRYDLLKLSLSRINTYLGIASRAHLSLASEDAMLAAFQLSRELRRLARKEPEFKPEYIALESLSQDYGFQLLGMCWNQSEVTAVLNDLAEDSETEPEAEGLGLAFEEGIPSLVRPRLAVNYNQKRFVAHLICQQVLSSI TTSJ9E7 TT Literature-reported TT06GRA ID TT06GRA TT06GRA TN Short transient receptor potential channel 7 (TRPC7) TT06GRA UP Q9HCX4 TT06GRA UC TRPC7_HUMAN TT06GRA BC Transient receptor potential catioin channel TT06GRA SN hTRP7; Transient receptor protein 7; TRP7; TRP-7 TT06GRA GN TRPC7 TT06GRA FC Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) (By similarity). May also be activated by intracellular calcium store depletion. TT06GRA SQ MLRNSTFKNMQRRHTTLREKGRRQAIRGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARVGDALLLAISKGYVRIVEAILNHPAFAQGQRLTLSPLEQELRDDDFYAYDEDGTRFSHDITPIILAAHCQEYEIVHILLLKGARIERPHDYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVLTALELSNELARLANIETEFKNDYRKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVNFQVWSDHHRPSLSRIKLAIKYEVKKFVAHPNCQQQLLTMWYENLSGLRQQSIAVKFLAVFGVSIGLPFLAIAYWIAPCSKLGRTLRSPFMKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPNETFTDYPKQIFRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLSIFVASFTARFMAFLKATEAQLYVDQHVQDDTLHNVSLPPEVAYFTYARDKWWPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYRGAKYNPAFTTVEESFKTLFWSIFGLSEVISVVLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYYLIMRIKMCLIKLCKSKAKSCENDLEMGMLNSKFKKTRYQAGMRNSENLTANNTLSKPTRYQKIMKRLIKRYVLKAQVDRENDEVNEGELKEIKQDISSLRYELLEEKSQATGELADLIQQLSEKFGKNLNKDHLRVNKGKDI TT06GRA TT Literature-reported TTBPKGD ID TTBPKGD TTBPKGD TN Shugoshin-like protein 1 (SGO1) TTBPKGD UP Q5FBB7 TTBPKGD UC SGO1_HUMAN TTBPKGD SN hSgo1; Serologically defined breast cancer antigen NY-BR-85; SGOL1; SGO1 TTBPKGD GN SGO1 TTBPKGD FC Plays a central role in chromosome cohesion during mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. May act by preventing phosphorylation of the STAG2 subunit of cohesin complex at the centromere, ensuring cohesin persistence at centromere until cohesin cleavage by ESPL1/separase at anaphase. Essential for proper chromosome segregation during mitosis and this function requires interaction with PPP2R1A. Its phosphorylated form is necessary for chromosome congression and for the proper attachment of spindle microtubule to the kinetochore. Necessary for kinetochore localization of PLK1 and CENPF. May play a role in the tension sensing mechanism of the spindle-assembly checkpoint by regulating PLK1 kinetochore affinity. Isoform 3 plays a role in maintaining centriole cohesion involved in controlling spindle pole integrity. Involved in centromeric enrichment of AUKRB in prometaphase. TTBPKGD PD 4A0I; 3Q6S; 3FGA TTBPKGD SQ MAKERCLKKSFQDSLEDIKKRMKEKRNKNLAEIGKRRSFIAAPCQIITNTSTLLKNYQDNNKMLVLALENEKSKVKEAQDIILQLRKECYYLTCQLYALKGKLTSQQTVEPAQNQEICSSGMDPNSDDSSRNLFVKDLPQIPLEETELPGQGESFQIEDQIPTIPQDTLGVDFDSGEAKSTDNVLPRTVSVRSSLKKHCNSICQFDSLDDFETSHLAGKSFEFERVGFLDPLVNMHIPENVQHNACQWSKDQVNLSPKLIQPGTFTKTKEDILESKSEQTKSKQRDTQERKREEKRKANRRKSKRMSKYKENKSENKKTVPQKKMHKSVSSNDAYNFNLEEGVHLTPFRQKVSNDSNREENNESEVSLCESSGSGDDSDDLYLPTCKYIQNPTSNSDRPVTRPLAKRALKYTDEKETEGSKPTKTPTTTPPETQQSPHLSLKDITNVSLYPVVKIRRLSLSPKKNKASPAVALPKRRCTASVNYKEPTLASKLRRGDPFTDLCFLNSPIFKQKKDLRRSKKRALEVSPAKEAIFILYYVREFVSRFPDCRKCKLETHICLR TTBPKGD TT Literature-reported TTBSZPF ID TTBSZPF TTBSZPF TN Sialic acid-binding immunoglobulin-like lectin 15 (SIGLEC15) TTBSZPF UP Q6ZMC9 TTBSZPF UC SIG15_HUMAN TTBSZPF BC Immunoglobulin TTBSZPF SN Siglec-15; SIGLEC15; CD33 antigen-like 3 TTBSZPF GN SIGLEC15 TTBSZPF FC Binds sialylated glycoproteins. TTBSZPF SQ MEKSIWLLACLAWVLPTGSFVRTKIDTTENLLNTEVHSSPAQRWSMQVPPEVSAEAGDAAVLPCTFTHPHRHYDGPLTAIWRAGEPYAGPQVFRCAAARGSELCQTALSLHGRFRLLGNPRRNDLSLRVERLALADDRRYFCRVEFAGDVHDRYESRHGVRLHVTAAPRIVNISVLPSPAHAFRALCTAEGEPPPALAWSGPALGNSLAAVRSPREGHGHLVTAELPALTHDGRYTCTAANSLGRSEASVYLFRFHGASGASTVALLLGALGFKALLLLGVLAARAARRRPEHLDTPDTPPRSQAQESNYENLSQMNPRSPPATMCSP TTBSZPF TT Clinical trial TT36N7Z ID TT36N7Z TT36N7Z TN Signal transduction protein Lnk (SH2B3) TT36N7Z UP Q9UQQ2 TT36N7Z UC SH2B3_HUMAN TT36N7Z BC SH2B adapter family TT36N7Z SN SH2B3; SH2B adapter protein 3; Lymphocyte-specific adapter protein Lnk; Lymphocyte adapter protein TT36N7Z GN SH2B3 TT36N7Z FC Links T-cell receptor activation signal to phospholipaseC-gamma-1, GRB2 and phosphatidylinositol 3-kinase. TT36N7Z SQ MNGPALQPSSPSSAPSASPAAAPRGWSEFCELHAVAAARELARQYWLFAREHPQHAPLRAELVSLQFTDLFQRYFCREVRDGRAPGRDYRDTGRGPPAKAEASPEPGPGPAAPGLPKARSSEELAPPRPPGPCSFQHFRRSLRHIFRRRSAGELPAAHTAAAPGTPGEAAETPARPGLAKKFLPWSLAREPPPEALKEAVLRYSLADEASMDSGARWQRGRLALRRAPGPDGPDRVLELFDPPKSSRPKLQAACSSIQEVRWCTRLEMPDNLYTFVLKVKDRTDIIFEVGDEQQLNSWMAELSECTGRGLESTEAEMHIPSALEPSTSSSPRGSTDSLNQGASPGGLLDPACQKTDHFLSCYPWFHGPISRVKAAQLVQLQGPDAHGVFLVRQSETRRGEYVLTFNFQGIAKHLRLSLTERGQCRVQHLHFPSVVDMLHHFQRSPIPLECGAACDVRLSSYVVVVSQPPGSCNTVLFPFSLPHWDSESLPHWGSELGLPHLSSSGCPRGLSPEGLPGRSSPPEQIFHLVPSPEELANSLQHLEHEPVNRARDSDYEMDSSSRSHLRAIDNQYTPL TT36N7Z TT Literature-reported TTW6L4V ID TTW6L4V TTW6L4V TN SIK family kinase 3 (SIK3) TTW6L4V UP Q9Y2K2 TTW6L4V UC SIK3_HUMAN TTW6L4V SN Serine/threonine-protein kinase SIK3; Serine/threonine-protein kinase QSK; Salt-inducible kinase 3; SIK-3; KIAA0999 TTW6L4V GN SIK3 TTW6L4V FC Positive regulator of mTOR signaling that functions by triggering the degradation of DEPTOR, an mTOR inhibitor. Involved in the dynamic regulation of mTOR signaling in chondrocyte differentiation during skeletogenesis. Negatively regulates cAMP signaling pathway possibly by acting on CRTC2/TORC2 and CRTC3/TORC3 (Probable). Prevents HDAC4 translocation to the nucleus (By similarity). TTW6L4V EC EC 2.7.11.1 TTW6L4V SQ MAAAAASGAGGAAGAGTGGAGPAGRLLPPPAPGSPAAPAAVSPAAGQPRPPAPASRGPMPARIGYYEIDRTIGKGNFAVVKRATHLVTKAKVAIKIIDKTQLDEENLKKIFREVQIMKMLCHPHIIRLYQVMETERMIYLVTEYASGGEIFDHLVAHGRMAEKEARRKFKQIVTAVYFCHCRNIVHRDLKAENLLLDANLNIKIADFGFSNLFTPGQLLKTWCGSPPYAAPELFEGKEYDGPKVDIWSLGVVLYVLVCGALPFDGSTLQNLRARVLSGKFRIPFFMSTECEHLIRHMLVLDPNKRLSMEQICKHKWMKLGDADPNFDRLIAECQQLKEERQVDPLNEDVLLAMEDMGLDKEQTLQSLRSDAYDHYSAIYSLLCDRHKRHKTLRLGALPSMPRALAFQAPVNIQAEQAGTAMNISVPQVQLINPENQIVEPDGTLNLDSDEGEEPSPEALVRYLSMRRHTVGVADPRTEVMEDLQKLLPGFPGVNPQAPFLQVAPNVNFMHNLLPMQNLQPTGQLEYKEQSLLQPPTLQLLNGMGPLGRRASDGGANIQLHAQQLLKRPRGPSPLVTMTPAVPAVTPVDEESSDGEPDQEAVQSSTYKDSNTLHLPTERFSPVRRFSDGAASIQAFKAHLEKMGNNSSIKQLQQECEQLQKMYGGQIDERTLEKTQQQHMLYQQEQHHQILQQQIQDSICPPQPSPPLQAACENQPALLTHQLQRLRIQPSSPPPNHPNNHLFRQPSNSPPPMSSAMIQPHGAASSSQFQGLPSRSAIFQQQPENCSSPPNVALTCLGMQQPAQSQQVTIQVQEPVDMLSNMPGTAAGSSGRGISISPSAGQMQMQHRTNLMATLSYGHRPLSKQLSADSAEAHSLNVNRFSPANYDQAHLHPHLFSDQSRGSPSSYSPSTGVGFSPTQALKVPPLDQFPTFPPSAHQQPPHYTTSALQQALLSPTPPDYTRHQQVPHILQGLLSPRHSLTGHSDIRLPPTEFAQLIKRQQQQRQQQQQQQQQQEYQELFRHMNQGDAGSLAPSLGGQSMTERQALSYQNADSYHHHTSPQHLLQIRAQECVSQASSPTPPHGYAHQPALMHSESMEEDCSCEGAKDGFQDSKSSSTLTKGCHDSPLLLSTGGPGDPESLLGTVSHAQELGIHPYGHQPTAAFSKNKVPSREPVIGNCMDRSSPGQAVELPDHNGLGYPARPSVHEHHRPRALQRHHTIQNSDDAYVQLDNLPGMSLVAGKALSSARMSDAVLSQSSLMGSQQFQDGENEECGASLGGHEHPDLSDGSQHLNSSCYPSTCITDILLSYKHPEVSFSMEQAGV TTW6L4V TT Literature-reported TTI7ENL ID TTI7ENL TTI7ENL TN Skeletal muscle LIM-protein 1 (FHL1) TTI7ENL UP Q13642 TTI7ENL UC FHL1_HUMAN TTI7ENL SN Skeletal muscle LIMprotein 1; SLIM1; SLIM; Four and a half LIM domains protein 1; FHL1 TTI7ENL GN FHL1 TTI7ENL FC May have an involvement in muscle development or hypertrophy. TTI7ENL PD 2EGQ; 2CUR; 2CUP; 1X63 TTI7ENL SQ MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVTCHETKFAKHCVKCNKAITSGGITYQDQPWHADCFVCVTCSKKLAGQRFTAVEDQYYCVDCYKNFVAKKCAGCKNPITGKRTVSRVSHPVSKARKPPVCHGKRLPLTLFPSANLRGRHPGGERTCPSWVVVLYRKNRSLAAPRGPGLVKAPVWWPMKDNPGTTTASTAKNAP TTI7ENL TT Literature-reported TTCF82X ID TTCF82X TTCF82X TN Sodium calcium exchanger 1 (SLC8A1) TTCF82X UP P32418 TTCF82X UC NAC1_HUMAN TTCF82X BC Calcium:cation antiporter TTCF82X SN Solute carrier family 8 member 1; Sodium/calcium exchanger 1; Na(+)/Ca(2+)-exchange protein 1; NCX1; CNC TTCF82X GN SLC8A1 TTCF82X FC Contributes to Ca(2+) transport during excitation-contraction coupling in muscle. In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline. Required for normal embryonic heart development and the onset of heart contractions. Mediates the exchange of one Ca(2+) ion against three to four Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. TTCF82X SQ MYNMRRLSLSPTFSMGFHLLVTVSLLFSHVDHVIAETEMEGEGNETGECTGSYYCKKGVILPIWEPQDPSFGDKIARATVYFVAMVYMFLGVSIIADRFMSSIEVITSQEKEITIKKPNGETTKTTVRIWNETVSNLTLMALGSSAPEILLSVIEVCGHNFTAGDLGPSTIVGSAAFNMFIIIALCVYVVPDGETRKIKHLRVFFVTAAWSIFAYTWLYIILSVISPGVVEVWEGLLTFFFFPICVVFAWVADRRLLFYKYVYKRYRAGKQRGMIIEHEGDRPSSKTEIEMDGKVVNSHVENFLDGALVLEVDERDQDDEEARREMARILKELKQKHPDKEIEQLIELANYQVLSQQQKSRAFYRIQATRLMTGAGNILKRHAADQARKAVSMHEVNTEVTENDPVSKIFFEQGTYQCLENCGTVALTIIRRGGDLTNTVFVDFRTEDGTANAGSDYEFTEGTVVFKPGDTQKEIRVGIIDDDIFEEDENFLVHLSNVKVSSEASEDGILEANHVSTLACLGSPSTATVTIFDDDHAGIFTFEEPVTHVSESIGIMEVKVLRTSGARGNVIVPYKTIEGTARGGGEDFEDTCGELEFQNDEIVKTISVKVIDDEEYEKNKTFFLEIGEPRLVEMSEKKALLLNELGGFTITGKYLFGQPVFRKVHAREHPILSTVITIADEYDDKQPLTSKEEEERRIAEMGRPILGEHTKLEVIIEESYEFKSTVDKLIKKTNLALVVGTNSWREQFIEAITVSAGEDDDDDECGEEKLPSCFDYVMHFLTVFWKVLFAFVPPTEYWNGWACFIVSILMIGLLTAFIGDLASHFGCTIGLKDSVTAVVFVALGTSVPDTFASKVAATQDQYADASIGNVTGSNAVNVFLGIGVAWSIAAIYHAANGEQFKVSPGTLAFSVTLFTIFAFINVGVLLYRRRPEIGGELGGPRTAKLLTSCLFVLLWLLYIFFSSLEAYCHIKGF TTCF82X TT Literature-reported TTQPZTM ID TTQPZTM TTQPZTM TN Sodium/phosphate cotransporter 2B (SLC34A2) TTQPZTM UP O95436 TTQPZTM UC NPT2B_HUMAN TTQPZTM BC Phosphate:sodium symporter TTQPZTM SN Solute carrier family 34 member 2; Sodium-phosphate transport protein 2B; Sodium-dependent phosphate transport protein 2B; NaPi3b; NaPi-2b; Na(+)/Pi cotransporter 2B; Na(+)-dependent phosphate cotransporter 2B TTQPZTM GN SLC34A2 TTQPZTM FC It may be the main phosphate transport protein in the intestinal brush border membrane. May have a role in the synthesis of surfactant in lungs' alveoli. May be involved in actively transporting phosphate into cells via Na(+) cotransport. TTQPZTM SQ MAPWPELGDAQPNPDKYLEGAAGQQPTAPDKSKETNKTDNTEAPVTKIELLPSYSTATLIDEPTEVDDPWNLPTLQDSGIKWSERDTKGKILCFFQGIGRLILLLGFLYFFVCSLDILSSAFQLVGGKMAGQFFSNSSIMSNPLLGLVIGVLVTVLVQSSSTSTSIVVSMVSSSLLTVRAAIPIIMGANIGTSITNTIVALMQVGDRSEFRRAFAGATVHDFFNWLSVLVLLPVEVATHYLEIITQLIVESFHFKNGEDAPDLLKVITKPFTKLIVQLDKKVISQIAMNDEKAKNKSLVKIWCKTFTNKTQINVTVPSTANCTSPSLCWTDGIQNWTMKNVTYKENIAKCQHIFVNFHLPDLAVGTILLILSLLVLCGCLIMIVKILGSVLKGQVATVIKKTINTDFPFPFAWLTGYLAILVGAGMTFIVQSSSVFTSALTPLIGIGVITIERAYPLTLGSNIGTTTTAILAALASPGNALRSSLQIALCHFFFNISGILLWYPIPFTRLPIRMAKGLGNISAKYRWFAVFYLIIFFFLIPLTVFGLSLAGWRVLVGVGVPVVFIIILVLCLRLLQSRCPRVLPKKLQNWNFLPLWMRSLKPWDAVVSKFTGCFQMRCCCCCRVCCRACCLLCDCPKCCRCSKCCEDLEEAQEGQDVPVKAPETFDNITISREAQGEVPASDSKTECTAL TTQPZTM TT Clinical trial TT5LF3C ID TT5LF3C TT5LF3C TN Solute carrier family 15 member 1 (SLC15A1) TT5LF3C UP P46059 TT5LF3C UC S15A1_HUMAN TT5LF3C BC Proton-dependent oligopeptide transporter TT5LF3C SN PEPT1; Oligopeptide transporter, small intestine isoform; Intestinal H(+)/peptide cotransporter TT5LF3C GN SLC15A1 TT5LF3C FC May constitute a major route for the absorption of protein digestion end-products. Proton-coupled intake of oligopeptides of 2 to 4 amino acids with a preference for dipeptides. TT5LF3C SQ MGMSKSHSFFGYPLSIFFIVVNEFCERFSYYGMRAILILYFTNFISWDDNLSTAIYHTFVALCYLTPILGALIADSWLGKFKTIVSLSIVYTIGQAVTSVSSINDLTDHNHDGTPDSLPVHVVLSLIGLALIALGTGGIKPCVSAFGGDQFEEGQEKQRNRFFSIFYLAINAGSLLSTIITPMLRVQQCGIHSKQACYPLAFGVPAALMAVALIVFVLGSGMYKKFKPQGNIMGKVAKCIGFAIKNRFRHRSKAFPKREHWLDWAKEKYDERLISQIKMVTRVMFLYIPLPMFWALFDQQGSRWTLQATTMSGKIGALEIQPDQMQTVNAILIVIMVPIFDAVLYPLIAKCGFNFTSLKKMAVGMVLASMAFVVAAIVQVEIDKTLPVFPKGNEVQIKVLNIGNNTMNISLPGEMVTLGPMSQTNAFMTFDVNKLTRINISSPGSPVTAVTDDFKQGQRHTLLVWAPNHYQVVKDGLNQKPEKGENGIRFVNTFNELITITMSGKVYANISSYNASTYQFFPSGIKGFTISSTEIPPQCQPNFNTFYLEFGSAYTYIVQRKNDSCPEVKVFEDISANTVNMALQIPQYFLLTCGEVVFSVTGLEFSYSQAPSNMKSVLQAGWLLTVAVGNIIVLIVAGAGQFSKQWAEYILFAALLLVVCVIFAIMARFYTYINPAEIEAQFDEDEKKNRLEKSNPYFMSGANSQKQM TT5LF3C TT Literature-reported TT27Q3A ID TT27Q3A TT27Q3A TN Solute carrier family 15 member 2 (SLC15A2) TT27Q3A UP Q16348 TT27Q3A UC S15A2_HUMAN TT27Q3A SN Peptide transporter 2; PEPT2; Oligopeptide transporter, kidney isoform; Kidney H(+)/peptide cotransporter TT27Q3A GN SLC15A2 TT27Q3A FC Proton-coupled intake of oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Transports the dipeptide-like aminopeptidase inhibitor bestatin (By similarity). Can also transport the aminocephalosporin antibiotic cefadroxil (By similarity). TT27Q3A PD 6EZI TT27Q3A SQ MNPFQKNESKETLFSPVSIEEVPPRPPSPPKKPSPTICGSNYPLSIAFIVVNEFCERFSYYGMKAVLILYFLYFLHWNEDTSTSIYHAFSSLCYFTPILGAAIADSWLGKFKTIIYLSLVYVLGHVIKSLGALPILGGQVVHTVLSLIGLSLIALGTGGIKPCVAAFGGDQFEEKHAEERTRYFSVFYLSINAGSLISTFITPMLRGDVQCFGEDCYALAFGVPGLLMVIALVVFAMGSKIYNKPPPEGNIVAQVFKCIWFAISNRFKNRSGDIPKRQHWLDWAAEKYPKQLIMDVKALTRVLFLYIPLPMFWALLDQQGSRWTLQAIRMNRNLGFFVLQPDQMQVLNPLLVLIFIPLFDFVIYRLVSKCGINFSSLRKMAVGMILACLAFAVAAAVEIKINEMAPAQPGPQEVFLQVLNLADDEVKVTVVGNENNSLLIESIKSFQKTPHYSKLHLKTKSQDFHFHLKYHNLSLYTEHSVQEKNWYSLVIREDGNSISSMMVKDTESRTTNGMTTVRFVNTLHKDVNISLSTDTSLNVGEDYGVSAYRTVQRGEYPAVHCRTEDKNFSLNLGLLDFGAAYLFVITNNTNQGLQAWKIEDIPANKMSIAWQLPQYALVTAGEVMFSVTGLEFSYSQAPSSMKSVLQAAWLLTIAVGNIIVLVVAQFSGLVQWAEFILFSCLLLVICLIFSIMGYYYVPVKTEDMRGPADKHIPHIQGNMIKLETKKTKL TT27Q3A TT Literature-reported TT7X02I ID TT7X02I TT7X02I TN Solute carrier family 26 member 4 (SLC26A4) TT7X02I UP O43511 TT7X02I UC S26A4_HUMAN TT7X02I BC Sulfate permease TT7X02I SN Sodium-independent chloride/iodide transporter; SLC26A4 TT7X02I GN SLC26A4 TT7X02I FC Sodium-independent transporter of chloride and iodide. TT7X02I SQ MAAPGGRSEPPQLPEYSCSYMVSRPVYSELAFQQQHERRLQERKTLRESLAKCCSCSRKRAFGVLKTLVPILEWLPKYRVKEWLLSDVISGVSTGLVATLQGMAYALLAAVPVGYGLYSAFFPILTYFIFGTSRHISVGPFPVVSLMVGSVVLSMAPDEHFLVSSSNGTVLNTTMIDTAARDTARVLIASALTLLVGIIQLIFGGLQIGFIVRYLADPLVGGFTTAAAFQVLVSQLKIVLNVSTKNYNGVLSIIYTLVEIFQNIGDTNLADFTAGLLTIVVCMAVKELNDRFRHKIPVPIPIEVIVTIIATAISYGANLEKNYNAGIVKSIPRGFLPPELPPVSLFSEMLAASFSIAVVAYAIAVSVGKVYATKYDYTIDGNQEFIAFGISNIFSGFFSCFVATTALSRTAVQESTGGKTQVAGIISAAIVMIAILALGKLLEPLQKSVLAAVVIANLKGMFMQLCDIPRLWRQNKIDAVIWVFTCIVSIILGLDLGLLAGLIFGLLTVVLRVQFPSWNGLGSIPSTDIYKSTKNYKNIEEPQGVKILRFSSPIFYGNVDGFKKCIKSTVGFDAIRVYNKRLKALRKIQKLIKSGQLRATKNGIISDAVSTNNAFEPDEDIEDLEELDIPTKEIEIQVDWNSELPVKVNVPKVPIHSLVLDCGAISFLDVVGVRSLRVIVKEFQRIDVNVYFASLQDYVIEKLEQCGFFDDNIRKDTFFLTVHDAILYLQNQVKSQEGQGSILETITLIQDCKDTLELIETELTEEELDVQDEAMRTLAS TT7X02I TT Literature-reported TTKRVU0 ID TTKRVU0 TTKRVU0 TN Solute carrier family 26 member 9 (SLC26A9) TTKRVU0 UP Q7LBE3 TTKRVU0 UC S26A9_HUMAN TTKRVU0 BC Sulfate permease TTKRVU0 SN SLC26A9; Anion transporter/exchanger protein 9 TTKRVU0 GN SLC26A9 TTKRVU0 FC DIDS- and thiosulfate- sensitive anion exchanger mediating chloride, sulfate and oxalate transport. Mediates chloride/bicarbonate exchange or chloride-independent bicarbonate extrusion thus assuring bicarbonate secretion. Inhibited by ammonium and thiosulfate. TTKRVU0 SQ MSQPRPRYVVDRAAYSLTLFDDEFEKKDRTYPVGEKLRNAFRCSSAKIKAVVFGLLPVLSWLPKYKIKDYIIPDLLGGLSGGSIQVPQGMAFALLANLPAVNGLYSSFFPLLTYFFLGGVHQMVPGTFAVISILVGNICLQLAPESKFQVFNNATNESYVDTAAMEAERLHVSATLACLTAIIQMGLGFMQFGFVAIYLSESFIRGFMTAAGLQILISVLKYIFGLTIPSYTGPGSIVFTFIDICKNLPHTNIASLIFALISGAFLVLVKELNARYMHKIRFPIPTEMIVVVVATAISGGCKMPKKYHMQIVGEIQRGFPTPVSPVVSQWKDMIGTAFSLAIVSYVINLAMGRTLANKHGYDVDSNQEMIALGCSNFFGSFFKIHVICCALSVTLAVDGAGGKSQVASLCVSLVVMITMLVLGIYLYPLPKSVLGALIAVNLKNSLKQLTDPYYLWRKSKLDCCIWVVSFLSSFFLSLPYGVAVGVAFSVLVVVFQTQFRNGYALAQVMDTDIYVNPKTYNRAQDIQGIKIITYCSPLYFANSEIFRQKVIAKTGMDPQKVLLAKQKYLKKQEKRRMRPTQQRRSLFMKTKTVSLQELQQDFENAPPTDPNNNQTPANGTSVSYITFSPDSSSPAQSEPPASAEAPGEPSDMLASVPPFVTFHTLILDMSGVSFVDLMGIKALAKLSSTYGKIGVKVFLVNIHAQVYNDISHGGVFEDGSLECKHVFPSIHDAVLFAQANARDVTPGHNFQGAPGDAELSLYDSEEDIRSYWDLEQEMFGSMFHAETLTAL TTKRVU0 TT Literature-reported TTEARWC ID TTEARWC TTEARWC TN Solute carrier family 38 member 7 (SLC38A7) TTEARWC UP Q9NVC3 TTEARWC UC S38A7_HUMAN TTEARWC BC Amino acid/polyamine transporter 2 family TTEARWC SN SNAT7 TTEARWC GN SLC38A7 TTEARWC FC Mediates sodium-dependent transport of amino acids, preferentially L-glutamine. TTEARWC SQ MAQVSINNDYSEWDLSTDAGERARLLQSPCVDTAPKSEWEASPGGLDRGTTSTLGAIFIVVNACLGAGLLNFPAAFSTAGGVAAGIALQMGMLVFIISGLVILAYCSQASNERTYQEVVWAVCGKLTGVLCEVAIAVYTFGTCIAFLIIIGDQQDKIIAVMAKEPEGASGPWYTDRKFTISLTAFLFILPLSIPREIGFQKYASFLSVVGTWYVTAIVIIKYIWPDKEMTPGNILTRPASWMAVFNAMPTICFGFQCHVSSVPVFNSMQQPEVKTWGGVVTAAMVIALAVYMGTGICGFLTFGAAVDPDVLLSYPSEDMAVAVARAFIILSVLTSYPILHFCGRAVVEGLWLRYQGVPVEEDVGRERRRRVLQTLVWFLLTLLLALFIPDIGKVISVIGGLAACFIFVFPGLCLIQAKLSEMEEVKPASWWVLVSYGVLLVTLGAFIFGQTTANAIFVDLLA TTEARWC TT Literature-reported TT5B2EO ID TT5B2EO TT5B2EO TN S-phase kinase-associated protein 2 (SKP2) TT5B2EO UP Q13309 TT5B2EO UC SKP2_HUMAN TT5B2EO SN Skp2; P45skp2; FBXL1; F-box/LRR-repeat protein 1; F-box protein Skp2; Cyclin-A/CDK2-associated protein p45; Cyclin A/CDK2-associated protein p45; Cyclin A/CDK2-associated p45 TT5B2EO GN SKP2 TT5B2EO FC Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, and probably MYC, TOB1 and TAL1. Degradation of TAL1 also requires STUB1. Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destruction of CDH1 in a CK1-Dependent Manner, thereby regulating cell migration. Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. TT5B2EO PD 2AST; 2ASS; 1LDK; 1FS2; 1FS1 TT5B2EO SQ MHRKHLQEIPDLSSNVATSFTWGWDSSKTSELLSGMGVSALEKEEPDSENIPQELLSNLGHPESPPRKRLKSKGSDKDFVIVRRPKLNRENFPGVSWDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLDLTGKNLHPDVTGRLLSQGVIAFRCPRSFMDQPLAEHFSPFRVQHMDLSNSVIEVSTLHGILSQCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVQVAVAHVSETITQLNLSGYRKNLQKSDLSTLVRRCPNLVHLDLSDSVMLKNDCFQEFFQLNYLQHLSLSRCYDIIPETLLELGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKNQEIWGIKCRLTLQKPSCL TT5B2EO TT Literature-reported TTFIW7J ID TTFIW7J TTFIW7J TN Spindle protein CHICA (FAM83D) TTFIW7J UP Q9H4H8 TTFIW7J UC FA83D_HUMAN TTFIW7J SN Protein FAM83D; FAM83D TTFIW7J GN FAM83D TTFIW7J FC Probable proto-oncogene that regulates cell proliferation, growth, migration and epithelial to mesenchymal transition. Through the degradation of FBXW7, may act indirectly on the expression and downstream signaling of MTOR, JUN and MYC. May play also a role in cell proliferation through activation of the ERK1/ERK2 signaling cascade. May also be important for proper chromosome congression and alignment during mitosis through its interaction with KIF22. TTFIW7J PD 5E0M; 5E0L TTFIW7J SQ MALLSEGLDEVPAACLSPCGPPNPTELFSESRRLALEELVAGGPEAFAAFLRRERLARFLNPDEVHAILRAAERPGEEGAAAAAAAEDSFGSSHDCSSGTYFPEQSDLEPPLLELGWPAFYQGAYRGATRVETHFQPRGAGEGGPYGCKDALRQQLRSAREVIAVVMDVFTDIDIFRDLQEICRKQGVAVYILLDQALLSQFLDMCMDLKVHPEQEKLMTVRTITGNIYYARSGTKIIGKVHEKFTLIDGIRVATGSYSFTWTDGKLNSSNLVILSGQVVEHFDLEFRILYAQSKPISPKLLSHFQSSNKFDHLTNRKPQSKELTLGNLLRMRLARLSSTPRKADLDPEMPAEGKAERKPHDCESSTVSEEDYFSSHRDELQSRKAIDAATQTEPGEEMPGLSVSEVGTQTSITTACAGTQTAVITRIASSQTTIWSRSTTTQTDMDENILFPRGTQSTEGSPVSKMSVSRSSSLKSSSSVSSQGSVASSTGSPASIRTTDFHNPGYPKYLGTPHLELYLSDSLRNLNKERQFHFAGIRSRLNHMLAMLSRRTLFTENHLGLHSGNFSRVNLLAVRDVALYPSYQ TTFIW7J TT Literature-reported TT6QLPX ID TT6QLPX TT6QLPX TN Squamous cell carcinoma antigen 1 (SCCA-1) TT6QLPX UP P29508 TT6QLPX UC SPB3_HUMAN TT6QLPX SN Serpin B3; SCCA1; SCCA-1; SCCA; Protein T4-A TT6QLPX GN SERPINB3 TT6QLPX FC May act as a papain-like cysteine protease inhibitor to modulate the host immune response against tumor cells. Also functions as an inhibitor of UV-induced apoptosis via suppression of the activity of c-Jun NH(2)-terminal kinase (JNK1). TT6QLPX PD 4ZK3; 4ZK0; 2ZV6 TT6QLPX SQ MNSLSEANTKFMFDLFQQFRKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGKAATYHVDRSGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP TT6QLPX TT Literature-reported TTRQ4AP ID TTRQ4AP TTRQ4AP TN SREBP transcription factor 2 (SREBF2) TTRQ4AP UP Q12772 TTRQ4AP UC SRBP2_HUMAN TTRQ4AP SN Sterol regulatory element-binding transcription factor 2; Sterol regulatory element-binding protein 2; SREBP2; SREBP-2; Class D basic helix-loop-helix protein 2; BHLHD2 TTRQ4AP GN SREBF2 TTRQ4AP FC Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the cholesterol and to a lesser degree the fatty acid synthesis pathway (By similarity). Binds the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3') found in the flanking region of the LDRL and HMG-CoA synthase genes. TTRQ4AP PD 1UKL TTRQ4AP SQ MDDSGELGGLETMETLTELGDELTLGDIDEMLQFVSNQVGEFPDLFSEQLCSSFPGSGGSGSSSGSSGSSSSSSNGRGSSSGAVDPSVQRSFTQVTLPSFSPSAASPQAPTLQVKVSPTSVPTTPRATPILQPRPQPQPQPQTQLQQQTVMITPTFSTTPQTRIIQQPLIYQNAATSFQVLQPQVQSLVTSSQVQPVTIQQQVQTVQAQRVLTQTANGTLQTLAPATVQTVAAPQVQQVPVLVQPQIIKTDSLVLTTLKTDGSPVMAAVQNPALTALTTPIQTAALQVPTLVGSSGTILTTMPVMMGQEKVPIKQVPGGVKQLEPPKEGERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMVLKLANQKNKLLKGIDLGSLVDNEVDLKIEDFNQNVLLMSPPASDSGSQAGFSPYSIDSEPGSPLLDDAKVKDEPDSPPVALGMVDRSRILLCVLTFLCLSFNPLTSLLQWGGAHDSDQHPHSGSGRSVLSFESGSGGWFDWMMPTLLLWLVNGVIVLSVFVKLLVHGEPVIRPHSRSSVTFWRHRKQADLDLARGDFAAAAGNLQTCLAVLGRALPTSRLDLACSLSWNVIRYSLQKLRLVRWLLKKVFQCRRATPATEAGFEDEAKTSARDAALAYHRLHQLHITGKLPAGSACSDVHMALCAVNLAECAEEKIPPSTLVEIHLTAAMGLKTRCGGKLGFLASYFLSRAQSLCGPEHSAVPDSLRWLCHPLGQKFFMERSWSVKSAAKESLYCAQRNPADPIAQVHQAFCKNLLERAIESLVKPQAKKKAGDQEEESCEFSSALEYLKLLHSFVDSVGVMSPPLSRSSVLKSALGPDIICRWWTSAITVAISWLQGDDAAVRSHFTKVERIPKALEVTESPLVKAIFHACRAMHASLPGKADGQQSSFCHCERASGHLWSSLNVSGATSDPALNHVVQLLTCDLLLSLRTALWQKQASASQAVGETYHASGAELAGFQRDLGSLRRLAHSFRPAYRKVFLHEATVRLMAGASPTRTHQLLEHSLRRRTTQSTKHGEVDAWPGQRERATAILLACRHLPLSFLSSPGQRAVLLAEAARTLEKVGDRRSCNDCQQMIVKLGGGTAIAAS TTRQ4AP TT Literature-reported TTM3DAY ID TTM3DAY TTM3DAY TN Stabilin-2 (STAB2) TTM3DAY UP Q8WWQ8 TTM3DAY UC STAB2_HUMAN TTM3DAY SN STAB2; Hyaluronan receptor for endocytosis; Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 2; FEEL-2; FAS1 EGF-like and X-link domain-containing adhesion molecule 2 TTM3DAY GN STAB2 TTM3DAY FC Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed 190 kDa form also functions as an endocytosis receptor for heparin internalisation as well as HA and CS. TTM3DAY PD 5N86 TTM3DAY SQ MMLQHLVIFCLGLVVQNFCSPAETTGQARRCDRKSLLTIRTECRSCALNLGVKCPDGYTMITSGSVGVRDCRYTFEVRTYSLSLPGCRHICRKDYLQPRCCPGRWGPDCIECPGGAGSPCNGRGSCAEGMEGNGTCSCQEGFGGTACETCADDNLFGPSCSSVCNCVHGVCNSGLDGDGTCECYSAYTGPKCDKPIPECAALLCPENSRCSPSTEDENKLECKCLPNYRGDGKYCDPINPCLRKICHPHAHCTYLGPNRHSCTCQEGYRGDGQVCLPVDPCQINFGNCPTKSTVCKYDGPGQSHCECKEHYQNFVPGVGCSMTDICKSDNPCHRNANCTTVAPGRTECICQKGYVGDGLTCYGNIMERLRELNTEPRGKWQGRLTSFISLLDKAYAWPLSKLGPFTVLLPTDKGLKGFNVNELLVDNKAAQYFVKLHIIAGQMNIEYMNNTDMFYTLTGKSGEIFNSDKDNQIKLKLHGGKKKVKIIQGDIIASNGLLHILDRAMDKLEPTFESNNEQTIMTMLQPRYSKFRSLLEETNLGHALDEDGVGGPYTIFVPNNEALNNMKDGTLDYLLSPEGSRKLLELVRYHIVPFTQLEVATLISTPHIRSMANQLIQFNTTDNGQILANDVAMEEIEITAKNGRIYTLTGVLIPPSIVPILPHRCDETKREMKLGTCVSCSLVYWSRCPANSEPTALFTHRCVYSGRFGSLKSGCARYCNATVKIPKCCKGFYGPDCNQCPGGFSNPCSGNGQCADSLGGNGTCICEEGFQGSQCQFCSDPNKYGPRCNKKCLCVHGTCNNRIDSDGACLTGTCRDGSAGRLCDKQTSACGPYVQFCHIHATCEYSNGTASCICKAGYEGDGTLCSEMDPCTGLTPGGCSRNAECIKTGTGTHTCVCQQGWTGNGRDCSEINNCLLPSAGGCHDNASCLYVGPGQNECECKKGFRGNGIDCEPITSCLEQTGKCHPLASCQSTSSGVWSCVCQEGYEGDGFLCYGNAAVELSFLSEAAIFNRWINNASLQPTLSATSNLTVLVPSQQATEDMDQDEKSFWLSQSNIPALIKYHMLLGTYRVADLQTLSSSDMLATSLQGNFLHLAKVDGNITIEGASIVDGDNAATNGVIHIINKVLVPQRRLTGSLPNLLMRLEQMPDYSIFRGYIIQYNLANAIEAADAYTVFAPNNNAIENYIREKKVLSLEEDVLRYHVVLEEKLLKNDLHNGMHRETMLGFSYFLSFFLHNDQLYVNEAPINYTNVATDKGVIHGLGKVLEIQKNRCDNNDTTIIRGRCRTCSSELTCPFGTKSLGNEKRRCIYTSYFMGRRTLFIGCQPKCVRTVITRECCAGFFGPQCQPCPGNAQNVCFGNGICLDGVNGTGVCECGEGFSGTACETCTEGKYGIHCDQACSCVHGRCNQGPLGDGSCDCDVGWRGVHCDNATTEDNCNGTCHTSANCLTNSDGTASCKCAAGFQGNGTICTAINACEISNGGCSAKADCKRTTPGRRVCTCKAGYTGDGIVCLEINPCLENHGGCDKNAECTQTGPNQAACNCLPAYTGDGKVCTLINVCLTKNGGCSEFAICNHTGQVERTCTCKPNYIGDGFTCRGSIYQELPKNPKTSQYFFQLQEHFVKDLVGPGPFTVFAPLSAAFDEEARVKDWDKYGLMPQVLRYHVVACHQLLLENLKLISNATSLQGEPIVISVSQSTVYINNKAKIISSDIISTNGIVHIIDKLLSPKNLLITPKDNSGRILQNLTTLATNNGYIKFSNLIQDSGLLSVITDPIHTPVTLFWPTDQALHALPAEQQDFLFNQDNKDKLKEYLKFHVIRDAKVLAVDLPTSTAWKTLQGSELSVKCGAGRDIGDLFLNGQTCRIVQRELLFDLGVAYGIDCLLIDPTLGGRCDTFTTFDASGECGSCVNTPSCPRWSKPKGVKQKCLYNLPFKRNLEGCRERCSLVIQIPRCCKGYFGRDCQACPGGPDAPCNNRGVCLDQYSATGECKCNTGFNGTACEMCWPGRFGPDCLPCGCSDHGQCDDGITGSGQCLCETGWTGPSCDTQAVLPAVCTPPCSAHATCKENNTCECNLDYEGDGITCTVVDFCKQDNGGCAKVARCSQKGTKVSCSCQKGYKGDGHSCTEIDPCADGLNGGCHEHATCKMTGPGKHKCECKSHYVGDGLNCEPEQLPIDRCLQDNGQCHADAKCVDLHFQDTTVGVFHLRSPLGQYKLTFDKAREACANEAATMATYNQLSYAQKAKYHLCSAGWLETGRVAYPTAFASQNCGSGVVGIVDYGPRPNKSEMWDVFCYRMKDVNCTCKVGYVGDGFSCSGNLLQVLMSFPSLTNFLTEVLAYSNSSARGRAFLEHLTDLSIRGTLFVPQNSGLGENETLSGRDIEHHLANVSMFFYNDLVNGTTLQTRLGSKLLITASQDPLQPTETRFVDGRAILQWDIFASNGIIHVISRPLKAPPAPVTLTHTGLGAGIFFAIILVTGAVALAAYSYFRINRRTIGFQHFESEEDINVAALGKQQPENISNPLYESTTSAPPEPSYDPFTDSEERQLEGNDPLRTL TTM3DAY TT Literature-reported TTDLUER ID TTDLUER TTDLUER TN Stanniocalcin 1 (STC1) TTDLUER UP P52823 TTDLUER UC STC1_HUMAN TTDLUER BC Stanniocalcin family TTDLUER SN Stanniocalcin-1; STC1 TTDLUER GN STC1 TTDLUER FC Stimulates renal phosphate reabsorption, and could therefore prevent hypercalcemia. TTDLUER SQ MLQNSAVLLVLVISASATHEAEQNDSVSPRKSRVAAQNSAEVVRCLNSALQVGCGAFACLENSTCDTDGMYDICKSFLYSAAKFDTQGKAFVKESLKCIANGVTSKVFLAIRRCSTFQRMIAEVQEECYSKLNVCSIAKRNPEAITEVVQLPNHFSNRYYNRLVRSLLECDEDTVSTIRDSLMEKIGPNMASLFHILQTDHCAQTHPRADFNRRRTNEPQKLKVLLRNLRGEEDSPSHIKRTSHESA TTDLUER TT Literature-reported TTWKOF5 ID TTWKOF5 TTWKOF5 TN Staphylococcus Aminoacyltransferase FemA (Stap-coc femA) TTWKOF5 UP P14304 TTWKOF5 UC FEMA_STAAW TTWKOF5 SN Factor essential for expression of methicillin resistance TTWKOF5 GN Stap-coc femA TTWKOF5 FC May be involved in cell wall or membrane metabolism, or it might be a control element acting on expression of genes involved in cell wall or membrane biosynthesis. It is involved in resistance to the antibiotic methicillin. TTWKOF5 EC EC 2.3.2.17 TTWKOF5 SQ MKFTNLTAKEFGAFTDSMPYSHFTQTVGHYELKLAEGYETHLVGIKNNNNEVIAACLLTAVPVMKVFKYFYSNRGPVIDYENQELVHFFFNELSKYVKKHRCLYLHIDPYLPYQYLNHDGEITGNAGNDWFFDKMSNLGFEHTGFHKGFDPVLQIRYHSVLDLKDKTADDIIKNMDGLRKRNTKKVKKNGVKVRFLSEEELPIFRSFMEDTSESKAFADRDDKFYYNRLKYYKDRVLVPLAYINFDEYIKELNEERDILNKDLNKALKDIEKRPENKKAHNKRDNLQQQLDANEQKIEEGKRLQEEHGNELPISAGFFFINPFEVVYYAGGTSNAFRHFAGSYAVQWEMINYALNHGIDRYNFYGVSGKFTEDAEDAGVVKFKKGYNAEIIEYVGDFIKPINKPVYAAYTALKKVKDRIF TTWKOF5 TT Literature-reported TTKA90F ID TTKA90F TTKA90F TN Staphylococcus Aminoacyltransferase FemB (Stap-coc femB) TTKA90F UP P0A0A6 TTKA90F UC FEMB_STAAM TTKA90F SN Possible protein femB; ORF 419 TTKA90F GN Stap-coc femB TTKA90F FC Its function is unknown but its expression is needed for attaining the full level of resistance to the antibiotic methicillin. TTKA90F EC EC 2.3.2.18 TTKA90F SQ MKFTELTVTEFDNFVQNPSLESHYFQVKENIVTRENDGFEVVLLGIKDDNNKVIAASLFSKIPTMGSYVYYSNRGPVMDFSDLGLVDYYLKELDKYLQQHQCLYVKLDPYWLYHLYDKDIVPFEGREKNDALVNLFKSHGYEHHGFTTEYDTSSQVRWMGVLNLEGKTPETLKKTFDSQRKRNINKAINYGVKVRFLERDEFNLFLDLYRETEERAGFVSKTDDYFYNFIDTYGDKVLVPLAYIDLDEYVLKLQQELNDKENRRDQMMAKENKSDKQMKKIAELDKQIDHDQHELLNASELSKTDGPILNLASGVYFANAYEVNYFSGGSSEKYNQFMGPYMMHWFMINYCFDNGYDRYNFYGLSGDFTENSEDYGVYRFKRGFNVQIEELIGDFYKPIHKVKYWLFTTLDKLRKKLKK TTKA90F TT Literature-reported TTR5YAZ ID TTR5YAZ TTR5YAZ TN Staphylococcus Dehydrosqualene desaturase (Stap-coc crtN) TTR5YAZ UP O07855 TTR5YAZ UC CRTN_STAAE TTR5YAZ SN Dehydrosqualene desaturase; 4,4'-diapophytoene desaturase (4,4'-diaponeurosporene-forming) TTR5YAZ GN Stap-coc crtN TTR5YAZ FC Involved in the biosynthesis of the yellow-orange carotenoid staphyloxanthin, which plays a role in the virulence via its protective function against oxidative stress. Catalyzes three successive dehydrogenation reactions that lead to the introduction of three double bonds into 4,4'-diapophytoene (dehydrosqualene), with 4,4'-diapophytofluene and 4,4'-diapo-zeta-carotene as intermediates, and 4,4'-diaponeurosporene (the major deep-yellow pigment in staphylococci strains) as the end product. TTR5YAZ EC EC 1.3.8.- TTR5YAZ SQ MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNNNVGGRMNQLKKDGFTFDMGPTIVMMPDVYKDVFTACGKNYEDYIELRQLRYIYDVYFDHDDRITVPTDLAELQQMLESIEPGSTHGFMSFLTDVYKKYEIARRYFLERTYRKPSDFYNMTSLVQGAKLKTLNHADQLIEHYIDNEKIQKLLAFQTLYIGIDPKRGPSLYSIIPMIEMMFGVHFIKGGMYGMAQGLAQLNKDLGVNIELNAEIEQIIIDPKFKRADAIKVNGDIRKFDKILCTADFPSVAESLMPDFAPIKKYPPHKIADLDYSCSAFLMYIGIDIDVTDQVRLHNVIFSDDFRGNIEEIFEGRLSYDPSIYVYVPAVADKSLAPEGKTGIYVLMPTPELKTGSGIDWSDEALTQQIKEIIYRKLATIEVFEDIKSHIVSETIFTPNDFEQTYHAKFGSAFGLMPTLAQSNYYRPQNVSRDYKDLYFAGASTHPGAGVPIVLTSAKITVDEMIKDIERGV TTR5YAZ TT Literature-reported TTCIJ5S ID TTCIJ5S TTCIJ5S TN Staphylococcus Enterotoxin B (Stap-coc entB) TTCIJ5S UP P01552 TTCIJ5S UC ETXB_STAAU TTCIJ5S SN SEB; Enterotoxin type B TTCIJ5S GN Stap-coc entB TTCIJ5S FC Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death. TTCIJ5S PD 4RGO; 4RGN; 4RGM; 4C56; 3W2D TTCIJ5S SQ MYKRLFISHVILIFALILVISTPNVLAESQPDPKPDELHKSSKFTGLMENMKVLYDDNHVSAINVKSIDQFLYFDLIYSIKDTKLGNYDNVRVEFKNKDLADKYKDKYVDVFGANYYYQCYFSKKTNDINSHQTDKRKTCMYGGVTEHNGNQLDKYRSITVRVFEDGKNLLSFDVQTNKKKVTAQELDYLTRHYLVKNKKLYEFNNSPYETGYIKFIENENSFWYDMMPAPGDKFDQSKYLMMYNDNKMVDSKDVKIEVYLTTKKK TTCIJ5S TT Literature-reported TTKFESN ID TTKFESN TTKFESN TN Staphylococcus Lipid II:glycine glycyltransferase (Stap-coc femX) TTKFESN UP Q6GEH2 TTKFESN UC FEMX_STAAR TTKFESN SN femX; Lipid II:glycine glycyltransferase; Factor essential for expression of methicillin resistance X TTKFESN GN Stap-coc femX TTKFESN FC Catalyzes the incorporation of the first glycine of the pentaglycine interpeptide bridge, which is characteristic of the S.aureus peptidoglycan. This glycine is added to the epsilon-amino group of the L-lysine of the membrane-bound lipid II intermediate (GlcNAc-(beta-1,4)-N-acetylmuramic acid(-L-Ala-D-iGln-L-Lys-D-Ala- D-Ala)-pyrophosphoryl-undecaprenol), using glycyl-tRNA(Gly) as donor, in a ribosome-independent mechanism. Involved in methicillin resistance. TTKFESN EC EC 2.3.2.16 TTKFESN SQ MEKMHITNQEHDAFVKSNPNGDLLQLTKWAETKKLTGWYARRIAVGRDGEIQGVAQLLFKKVPKLPYTLCYISRGFVVDYSNKEALNALLDSAKEIAKAEKAYAIKIDPDVEVDKGTDALQNLKALGFKHKGFKEGLSKDYIQPRMTMITPIDKNDDELLNSFERRNRSKVRLALKRGTTVERSDREGLKTFAELMKITGERDGFLTRDISYFENIYDALHEDGDAELFLVKLDPKENIAKVNQELNELHAEIAKWQQKMETSEKQAKKAQNMINDAQNKIAKNEDLKRDLEALEKEHPEGIYLSGALLMFAGSKSYYLYGASSNEFRDFLPNHHMQYTMMKYAREHGATTYDFGGTDNDPDKDSEHYGLWAFKKVWGTYLSEKIGEFDYVLNQPLYQLIEQVKPRLTKAKIKISRKLKRK TTKFESN TT Literature-reported TTMQBO3 ID TTMQBO3 TTMQBO3 TN Staphylococcus Lysostaphin (Stap-coc lss) TTMQBO3 UP P10548 TTMQBO3 UC LSTP_STAST TTMQBO3 SN Lysostaphin; Glycyl-glycine endopeptidase TTMQBO3 GN Stap-coc lss TTMQBO3 FC Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan. TTMQBO3 EC EC 3.4.24.75 TTMQBO3 SQ MKKTKNNYYTTPLAIGLSTFALASIVYGGIQNETHASEKSNMDVSKKVAEVETSKPPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKALVQNRTALRAATHEHSAQWLNNYKKGYGYGPYPLGINGGIHYGVDFFMNIGTPVKAISSGKIVEAGWSNYGGGNQIGLIENDGVHRQWYMHLSKYNVKVGDYVKAGQIIGWSGSTGYSTAPHLHFQRMVNSFSNSTAQDPMPFLKSAGYGKAGGTVTPTPNTGWKTNKYGTLYKSESASFTPNTDIITRTTGPFRSMPQSGVLKAGQTIHYDEVMKQDGHVWVGYTGNSGQRIYLPVRTWNKSTNTLGVLWGTIK TTMQBO3 TT Literature-reported TTEN986 ID TTEN986 TTEN986 TN Staphylococcus Sortase A (Stap-coc srtA) TTEN986 UP Q2FV99 TTEN986 UC SRTA_STAA8 TTEN986 SN Surface protein sorting A TTEN986 GN Stap-coc srtA TTEN986 FC Transpeptidase that anchors surface proteins to the cell wall. Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall. This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues. Utilizes lipid II as the peptidoglycan substrate for the sorting reaction. Responsible for the display of important virulence factors. Important for interactions with the host and host colonization during infection. TTEN986 EC EC 3.4.22.70 TTEN986 SQ MKKWTNRLMTIAGVVLILVAAYLFAKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAKPQIPKDKSKVAGYIEIPDADIKEPVYPGPATPEQLNRGVSFAEENESLDDQNISIAGHTFIDRPNYQFTNLKAAKKGSMVYFKVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKQLTLITCDDYNEKTGVWEKRKIFVATEVK TTEN986 TT Preclinical TTR5GXT ID TTR5GXT TTR5GXT TN Staphylococcus Toxic shock syndrome toxin-1 (Stap-coc tst) TTR5GXT UP P06886 TTR5GXT UC TSST_STAAU TTR5GXT SN Toxic shock syndrome toxin-1; TSST-1 TTR5GXT GN Stap-coc tst TTR5GXT FC Responsible for the symptoms of toxic shock syndrome. TTR5GXT PD 5TSS; 4TSS; 4OHJ; 3TSS; 2TSS TTR5GXT SQ MNKKLLMNFFIVSPLLLATTATDFTPVPLSSNQIIKTAKASTNDNIKDLLDWYSSGSDTFTNSEVLDNSLGSMRIKNTDGSISLIIFPSPYYSPAFTKGEKVDLNTKRTKKSQHTSEGTYIHFQISGVTNTEKLPTPIELPLKVKVHGKDSPLKYGPKFDKKQLAISTLDFEIRHQLTQIHGLYRSSDKTGGYWKITMNDGSTYQSDLSKKFEYNTEKPPINIDEIKTIEAEIN TTR5GXT TT Literature-reported TTYQTIU ID TTYQTIU TTYQTIU TN Ste-20-related kinase (STK39) TTYQTIU UP Q9UEW8 TTYQTIU UC STK39_HUMAN TTYQTIU SN Serine/threonine-protein kinase 39; STE20/SPS1-related proline-alanine-rich protein kinase; SPAK; DCHT TTYQTIU GN STK39 TTYQTIU FC May act as a mediator of stress-activated signals. Mediates the inhibition of SLC4A4, SLC26A6 as well as CFTR activities by the WNK scaffolds, probably through phosphorylation. Phosphorylates RELT. TTYQTIU EC EC 2.7.11.1 TTYQTIU SQ MAEPSGSPVHVQLPQQAAPVTAAAAAAPAAATAAPAPAAPAAPAPAPAPAAQAVGWPICRDAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPNVVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGLDYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDKEMMKKYGKSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEKLLTRTPDIAQRAKKVRRVPGSSGHLHKTEDGDWEWSDDEMDEKSEEGKAAFSQEKSRRVKEENPEIAVSASTIPEQIQSLSVHDSQGPPNANEDYREASSCAVNLVLRLRNSRKELNDIRFEFTPGRDTADGVSQELFSAGLVDGHDVVIVAANLQKIVDDPKALKTLTFKLASGCDGSEIPDEVKLIGFAQLSVS TTYQTIU TT Literature-reported TTEI40H ID TTEI40H TTEI40H TN Steroidogenic acute regulatory protein (STAR) TTEI40H UP P49675 TTEI40H UC STAR_HUMAN TTEI40H SN Steroidogenic acute regulatory protein, mitochondrial; StARD1; START domain-containing protein 1 TTEI40H GN STAR TTEI40H FC Plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone. Mediates the transfer of cholesterol from the outer mitochondrial membrane to the inner mitochondrial membrane where it is cleaved to pregnenolone. TTEI40H PD 5OMA; 3P0L; 2I93; 1IMG TTEI40H SQ MLLATFKLCAGSSYRHMRNMKGLRQQAVMAISQELNRRALGGPTPSTWINQVRRRSSLLGSRLEETLYSDQELAYLQQGEEAMQKALGILSNQEGWKKESQQDNGDKVMSKVVPDVGKVFRLEVVVDQPMERLYEELVERMEAMGEWNPNVKEIKVLQKIGKDTFITHELAAEAAGNLVGPRDFVSVRCAKRRGSTCVLAGMATDFGNMPEQKGVIRAEHGPTCMVLHPLAGSPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRKRLESHPASEARC TTEI40H TT Literature-reported TTER0UB ID TTER0UB TTER0UB TN Sterol regulatory element binding protein-1 (SREBF1) TTER0UB UP P36956 TTER0UB UC SRBP1_HUMAN TTER0UB SN bHLHd1; Sterol regulatory element-binding transcription factor 1; Sterol regulatory element-binding protein 1; SREBP1; SREBP-1; SREBP 1; Class D basic helix-loop-helix protein 1 TTER0UB GN SREBF1 TTER0UB FC Regulates transcription of the LDL receptor gene as well as the fatty acid and to a lesser degree the cholesterol synthesis pathway. Binds to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3'). Transcriptional activator required for lipid homeostasis. TTER0UB PD 1AM9 TTER0UB SQ MDEPPFSEAALEQALGEPCDLDAALLTDIEDMLQLINNQDSDFPGLFDPPYAGSGAGGTDPASPDTSSPGSLSPPPATLSSSLEAFLSGPQAAPSPLSPPQPAPTPLKMYPSMPAFSPGPGIKEESVPLSILQTPTPQPLPGALLPQSFPAPAPPQFSSTPVLGYPSPPGGFSTGSPPGNTQQPLPGLPLASPPGVPPVSLHTQVQSVVPQQLLTVTAAPTAAPVTTTVTSQIQQVPVLLQPHFIKADSLLLTAMKTDGATVKAAGLSPLVSGTTVQTGPLPTLVSGGTILATVPLVVDAEKLPINRLAAGSKAPASAQSRGEKRTAHNAIEKRYRSSINDKIIELKDLVVGTEAKLNKSAVLRKAIDYIRFLQHSNQKLKQENLSLRTAVHKSKSLKDLVSACGSGGNTDVLMEGVKTEVEDTLTPPPSDAGSPFQSSPLSLGSRGSGSGGSGSDSEPDSPVFEDSKAKPEQRPSLHSRGMLDRSRLALCTLVFLCLSCNPLASLLGARGLPSPSDTTSVYHSPGRNVLGTESRDGPGWAQWLLPPVVWLLNGLLVLVSLVLLFVYGEPVTRPHSGPAVYFWRHRKQADLDLARGDFAQAAQQLWLALRALGRPLPTSHLDLACSLLWNLIRHLLQRLWVGRWLAGRAGGLQQDCALRVDASASARDAALVYHKLHQLHTMGKHTGGHLTATNLALSALNLAECAGDAVSVATLAEIYVAAALRVKTSLPRALHFLTRFFLSSARQACLAQSGSVPPAMQWLCHPVGHRFFVDGDWSVLSTPWESLYSLAGNPVDPLAQVTQLFREHLLERALNCVTQPNPSPGSADGDKEFSDALGYLQLLNSCSDAAGAPAYSFSISSSMATTTGVDPVAKWWASLTAVVIHWLRRDEEAAERLCPLVEHLPRVLQESERPLPRAALHSFKAARALLGCAKAESGPASLTICEKASGYLQDSLATTPASSSIDKAVQLFLCDLLLVVRTSLWRQQQPPAPAPAAQGTSSRPQASALELRGFQRDLSSLRRLAQSFRPAMRRVFLHEATARLMAGASPTRTHQLLDRSLRRRAGPGGKGGAVAELEPRPTRREHAEALLLASCYLPPGFLSAPGQRVGMLAEAARTLEKLGDRRLLHDCQQMLMRLGGGTTVTSS TTER0UB TT Literature-reported TTDHKNP ID TTDHKNP TTDHKNP TN Streptococcus Glycerol-3-phosphate oxidase (Stre-coc glpO) TTDHKNP UP Q99YI8 TTDHKNP UC GLPO_STRP1 TTDHKNP BC Short-chain dehydrogenases reductase TTDHKNP SN Glycerol-3-phosphate oxidase; Alpha-glycerophosphate oxidase TTDHKNP GN Stre-coc glpO TTDHKNP FC A FAD-dependent -glycerophosphate oxidase and catalyzes the formation of dihydroxyacetonephosphate. Used in the kinetic assay to study gluconeogenesis in liver and in immobilization studies on pencil graphite (PG) electrode. TTDHKNP SQ MEFSRETRRLALQKMQERDLDLLIIGGGITGAGVALQAAASGLDTGLIEMQDFAQGTSSRSTKLVHGGLRYLKQFDVEVVSDTVSERAVVQQIAPHIPKPDPMLLPVYDEPGSTFSMFRLKVAMDLYDLLAGVSNTPAANKVLTKEEVLKREPDLKQEGLLGGGVYLDFRNNDARLVIENIKRANRDGALIASHVKAEDFLLDDNGKIIGVKARDLLSDQEIIIKAKLVINTTGPWSDEIRQFSHKGQPIHQMRPTKGVHLVVDRQKLPVSQPVYVDTGLNDGRMVFVLPREEKTYFGTTDTDYTGDLEHPQVTQEDVDYLLGVVNNRFPNANVTIDDIESSWAGLRPLLSGNSASDYNGGNSGKVSDDSFDHLVDTVKAYINHEDSREAVEKAIKQVETSTSEKELDPSAVSRGSSFERDENGLFTLAGGKITDYRKMAEGALTGIIQILKEEFGKSFKLINSKTYPVSGGEINPANVDSEIEAYAQLGTLSGLSMDDARYLANLYGSNAPKVFALTRQLTAAEGLSLAETLSLHYAMDYEMALKPTDYFLRRTNHLLFMRDSLDALIDPVINEMAKHFEWSDQERVAQEDDLRRVIADNDLSALKGHQEG TTDHKNP TT Literature-reported TTK6ZND ID TTK6ZND TTK6ZND TN Streptococcus Pneumococcal surface adhesin A (Stre-coc psaA) TTK6ZND UP P0A4G2 TTK6ZND UC MTSA1_STRPN TTK6ZND SN PsaA TTK6ZND GN Stre-coc psaA TTK6ZND FC Part of an atp-driven transport system for manganese. Also act as an adhesin which is involved on adherence to extracellular matrix. It is an important factor in pathogenesis and infection. TTK6ZND PD 4UTP; 4UTO; 3ZTT; 3ZKA; 3ZK9 TTK6ZND SQ MKKLGTLLVLFLSAIILVACASGKKDTTSGQKLKVVATNSIIADITKNIAGDKIDLHSIVPIGQDPHEYEPLPEDVKKTSEADLIFYNGINLETGGNAWFTKLVENAKKTENKDYFAVSDGVDVIYLEGQNEKGKEDPHAWLNLENGIIFAKNIAKQLSAKDPNNKEFYEKNLKEYTDKLDKLDKESKDKFNKIPAEKKLIVTSEGAFKYFSKAYGVPSAYIWEINTEEEGTPEQIKTLVEKLRQTKVPSLFVESSVDDRPMKTVSQDTNIPIYAQIFTDSIAEQGKEGDSYYSMMKYNLDKIAEGLAK TTK6ZND TT Literature-reported TTYOAVU ID TTYOAVU TTYOAVU TN Streptococcus UPF0090 protein SP0552 (Stre-coc rimP) TTYOAVU UP Q97S61 TTYOAVU UC RIMP_STRPN TTYOAVU SN rimP; SP14.3; Hypothetical protein SP14.3 TTYOAVU GN Stre-coc rimP TTYOAVU FC Required for maturation of 30S ribosomal subunits. TTYOAVU PD 1IB8 TTYOAVU SQ MDAIATIVELVREVVEPVIEAPFELVDIEYGKIGSDMILSIFVDKPEGITLNDTADLTEIISPVLDTIKPDPFPEQYFLEITSPGLERPLKTKDAVAGAVGKYIHVGLYQAIDKQKVFEGTLLAFEEDELTMEYMDKTRKKTVQIPYSLVSKARLAVKL TTYOAVU TT Literature-reported TTLW798 ID TTLW798 TTLW798 TN Stromelysin (SL) TTLW798 UP P08254; P09238; P24347 TTLW798 UC MMP3_HUMAN; MMP10_HUMAN; MMP11_HUMAN TTLW798 BC Peptidase TTLW798 SN Transin; STMY; SL; Matrix metalloproteinase SL TTLW798 GN MMP3; MMP10; MMP11 TTLW798 FC Plays an important role in tissue remodeling associated with various physiological or pathological processes such as morphogenesis, angiogenesis, tissue repair, cirrhosis, arthritis, and metastasis. Excess MMPs degrade the structural proteins of the aortic wall. Disregulation of the balance between MMPs and TIMPs is also a characteristic of acute and chronic cardiovascular diseases. TTLW798 SQ MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC TTLW798 TT Literature-reported TTS8D17 ID TTS8D17 TTS8D17 TN Structural maintenance of chromosomes protein 2 (SMC2) TTS8D17 UP O95347 TTS8D17 UC SMC2_HUMAN TTS8D17 SN hCAP-E; XCAP-E homolog; SMC2L1; SMC-2; SMC protein 2; PRO0324; Chromosome-associated protein E; CAPE TTS8D17 GN SMC2 TTS8D17 FC The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. TTS8D17 PD 4U4P TTS8D17 SQ MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGKKLLERGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNNPKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFVDGVSTVARFTQCQNGKISKEAKSKAKPPKGAHVEV TTS8D17 TT Literature-reported TTYNM3X ID TTYNM3X TTYNM3X TN Sugen kinase 110 (SBK3) TTYNM3X UP P0C264 TTYNM3X UC SBK3_HUMAN TTYNM3X SN Uncharacterized serine/threonine-protein kinase SBK3; SH3-binding domain kinase family member 3; SGK110 TTYNM3X GN SBK3 TTYNM3X FC A serine/threonine protein kinase that does not have an activating compound and are either non-specific or their specificity has not been analyzed to date. TTYNM3X EC EC 2.7.11.1 TTYNM3X SQ MERRASETPEDGDPEEDTATALQRLVELTTSRVTPVRSLRDQYHLIRKLGSGSYGRVLLAQPHQGGPAVALKLLRRDLVLRSTFLREFCVGRCVSAHPGLLQTLAGPLQTPRYFAFAQEYAPCGDLSGMLQERGLPELLVKRVVAQLAGALDFLHSRGLVHADVKPDNVLVFDPVCSRVALGDLGLTRPEGSPTPAPPVPLPTAPPELCLLLPPDTLPLRPAVDSWGLGVLLFCAATACFPWDVALAPNPEFEAFAGWVTTKPQPPQPPPPWDQFAPPALALLQGLLDLDPETRSPPLAVLDFLGDDWGLQGNREGPGVLGSAVSYEDREEGGSSLEEWTDEGDDSKSGGRTGTDGGAP TTYNM3X TT Literature-reported TTNRQJ3 ID TTNRQJ3 TTNRQJ3 TN Super conserved receptor brain 2 (GPR85) TTNRQJ3 UP P60893 TTNRQJ3 UC GPR85_HUMAN TTNRQJ3 BC GPCR rhodopsin TTNRQJ3 SN Super conserved receptor expressed in brain 2; SREB2; Probable Gprotein coupled receptor 85; Probable G-protein coupled receptor 85 TTNRQJ3 GN GPR85 TTNRQJ3 FC Orphan receptor. TTNRQJ3 SQ MANYSHAADNILQNLSPLTAFLKLTSLGFIIGVSVVGNLLISILLVKDKTLHRAPYYFLLDLCCSDILRSAICFPFVFNSVKNGSTWTYGTLTCKVIAFLGVLSCFHTAFMLFCISVTRYLAIAHHRFYTKRLTFWTCLAVICMVWTLSVAMAFPPVLDVGTYSFIREEDQCTFQHRSFRANDSLGFMLLLALILLATQLVYLKLIFFVHDRRKMKPVQFVAAVSQNWTFHGPGASGQAAANWLAGFGRGPTPPTLLGIRQNANTTGRRRLLVLDEFKMEKRISRMFYIMTFLFLTLWGPYLVACYWRVFARGPVVPGGFLTAAVWMSFAQAGINPFVCIFSNRELRRCFSTTLLYCRKSRLPREPYCVI TTNRQJ3 TT Literature-reported TTNRQJ3 FM GPCR rhodopsin TTBLQS5 ID TTBLQS5 TTBLQS5 TN Supervillin (SVIL) TTBLQS5 UP Q9H1R7 TTBLQS5 UC SVIL_HUMAN TTBLQS5 SN p205/p250; Archvillin TTBLQS5 GN SVIL TTBLQS5 FC Isoform 1: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function. TTBLQS5 PD 2K6N; 2K6M TTBLQS5 SQ MKRKERIARRLEGIENDTQPILLQSCTGLVTHRLLEEDTPRYMRASDPASPHIGRSNEEEETSDSSLEKQTRSKYCTETSGVHGDSPYGSGTMDTHSLESKAERIARYKAERRRQLAEKYGLTLDPEADSEYLSRYTKSRKEPDAVEKRGGKSDKQEESSRDASSLYPGTETMGLRTCAGESKDYALHVGDGSSDPEVLLNIENQRRGQELSATRQAHDLSPAAESSSTFSFSGRDSSFTEVPRSPKHAHSSSLQQAASRSPSFGDPQLSPEARPSTGKPKHEWFLQKDSEGDTPSLINWPSRVKVREKLVKEESARNSPELASESVTQRRHQPAPVHYVSFQSEHSAFDRVPSKAAGSTRQPIRGYVQPADTGHTAKLVTPETPENASECSWVASATQNVPKPPSLTVLEGDGRDSPVLHVCESKAEEEEGEGEGEEKEEDVCFTEALEQSKKTLLALEGDGLVRSPEDPSRNEDFGKPAVSTVTLEHQKELENVAQPPQAPHQPTERTGRSEMVLYIQSEPVSQDAKPTGHNREASKKRKVRTRSLSDFTGPPQLQALKYKDPASRRELELPSSKTEGPYGEISMLDTKVSVAQLRSAFLASANACRRPELKSRVERSAEGPGLPTGVERERGSRKPRRYFSPGESRKTSERFRTQPITSAERKESDRCTSHSETPTVDDEEKVDERAKLSVAAKRLLFREMEKSFDEQNVPKRRSRNTAVEQRLRRLQDRSLTQPITTEEVVIAATEPIPASCSGGTHPVMARLPSPTVARSAVQPARLQASAHQKALAKDQTNEGKELAEQGEPDSSTLSLAEKLALFNKLSQPVSKAISTRNRIDTRQRRMNARYQTQPVTLGEVEQVQSGKLIPFSPAVNTSVSTVASTVAPMYAGDLRTKPPLDHNASATDYKFSSSIENSDSPVRSILKSQAWQPLVEGSENKGMLREYGETESKRALTGRDSGMEKYGSFEEAEASYPILNRAREGDSHKESKYAVPRRGSLERANPPITHLGDEPKEFSMAKMNAQGNLDLRDRLPFEEKVEVENVMKRKFSLRAAEFGEPTSEQTGTAAGKTIAQTTAPVSWKPQDSSEQPQEKLCKNPCAMFAAGEIKTPTGEGLLDSPSKTMSIKERLALLKKSGEEDWRNRLSRRQEGGKAPASSLHTQEAGRSLIKKRVTESRESQMTIEERKQLITVREEAWKTRGRGAANDSTQFTVAGRMVKKGLASPTAITPVASPICGKTRGTTPVSKPLEDIEARPDMQLESDLKLDRLETFLRRLNNKVGGMHETVLTVTGKSVKEVMKPDDDETFAKFYRSVDYNMPRSPVEMDEDFDVIFDPYAPKLTSSVAEHKRAVRPKRRVQASKNPLKMLAAREDLLQEYTEQRLNVAFMESKRMKVEKMSSNSNFSEVTLAGLASKENFSNVSLRSVNLTEQNSNNSAVPYKRLMLLQIKGRRHVQTRLVEPRASALNSGDCFLLLSPHCCFLWVGEFANVIEKAKASELATLIQTKRELGCRATYIQTIEEGINTHTHAAKDFWKLLGGQTSYQSAGDPKEDELYEAAIIETNCIYRLMDDKLVPDDDYWGKIPKCSLLQPKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGTFDYENCDINPLDPGECNPLIPRKGQGRPDWAIFGRLTEHNETILFKEKFLDWTELKRSNEKNPGELAQHKEDPRTDVKAYDVTRMVSMPQTTAGTILDGVNVGRGYGLVEGHDRRQFEITSVSVDVWHILEFDYSRLPKQSIGQFHEGDAYVVKWKFMVSTAVGSRQKGEHSVRAAGKEKCVYFFWQGRHSTVSEKGTSALMTVELDEERGAQVQVLQGKEPPCFLQCFQGGMVVHSGRREEEEENVQSEWRLYCVRGEVPVEGNLLEVACHCSSLRSRTSMVVLNVNKALIYLWHGCKAQAHTKEVGRTAANKIKEQCPLEAGLHSSSKVTIHECDEGSEPLGFWDALGRRDRKAYDCMLQDPGSFNFAPRLFILSSSSGDFAATEFVYPARAPSVVSSMPFLQEDLYSAPQPALFLVDNHHEVYLWQGWWPIENKITGSARIRWASDRKSAMETVLQYCKGKNLKKPAPKSYLIHAGLEPLTFTNMFPSWEHREDIAEITEMDTEVSNQITLVEDVLAKLCKTIYPLADLLARPLPEGVDPLKLEIYLTDEDFEFALDMTRDEYNALPAWKQVNLKKAKGLF TTBLQS5 TT Literature-reported TT7Q9WR ID TT7Q9WR TT7Q9WR TN Suppressor of G2 allele of SKP1 homolog (Sgt1) TT7Q9WR UP Q9Y2Z0 TT7Q9WR UC SGT1_HUMAN TT7Q9WR SN Protein SGT1 homolog; Protein 40-6-3 TT7Q9WR GN SUGT1 TT7Q9WR FC May play a role in ubiquitination and subsequent proteasomal degradation of target proteins. TT7Q9WR PD 1RL1 TT7Q9WR SQ MAAAAAGTATSQRFFQSFSDALIDEDPQAALEELTKALEQKPDDAQYYCQRAYCHILLGNYCVAVADAKKSLELNPNNSTAMLRKGICEYHEKNYAAALETFTEGQKLDIETGFHRVGQAGLQLLTSSDPPALDSQSAGITGADANFSVWIKRCQEAQNGSESEVWTHQSKIKYDWYQTESQVVITLMIKNVQKNDVNVEFSEKELSALVKLPSGEDYNLKLELLHPIIPEQSTFKVLSTKIEIKLKKPEAVRWEKLEGQGDVPTPKQFVADVKNLYPSSSPYTRNWDKLVGEIKEEEKNEKLEGDAALNRLFQQIYSDGSDEVKRAMNKSFMESGGTVLSTNWSDVGKRKVEINPPDDMEWKKY TT7Q9WR TT Literature-reported TTDFTJG ID TTDFTJG TTDFTJG TN Synembryn-A (RIC8A) TTDFTJG UP Q9NPQ8 TTDFTJG UC RIC8A_HUMAN TTDFTJG BC Synembryn TTDFTJG SN Protein Ric-8A TTDFTJG GN RIC8A TTDFTJG FC Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation. Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. TTDFTJG SQ MEPRAVAEAVETGEEDVIMEALRSYNQEHSQSFTFDDAQQEDRKRLAELLVSVLEQGLPPSHRVIWLQSVRILSRDRNCLDPFTSRQSLQALACYADISVSEGSVPESADMDVVLESLKCLCNLVLSSPVAQMLAAEARLVVKLTERVGLYRERSFPHDVQFFDLRLLFLLTALRTDVRQQLFQELKGVRLLTDTLELTLGVTPEGNPPPTLLPSQETERAMEILKVLFNITLDSIKGEVDEEDAALYRHLGTLLRHCVMIATAGDRTEEFHGHAVNLLGNLPLKCLDVLLTLEPHGDSTEFMGVNMDVIRALLIFLEKRLHKTHRLKESVAPVLSVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGEMLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSEDEDTDTDEYKEAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVTMFDKLSRNRVIQPMGMSPRGHLTSLQDAMCETMEQQLSSDPDSDPD TTDFTJG TT Literature-reported TTDFTJG FM Synembryn family TT26BHC ID TT26BHC TT26BHC TN Synembryn-B (RIC8B) TT26BHC UP Q9NVN3 TT26BHC UC RIC8B_HUMAN TT26BHC BC Synembryn TT26BHC SN hSyn; Protein Ric-8B; Brain synembryn TT26BHC GN RIC8B TT26BHC FC Able to potentiate G(olf)-alpha-dependent cAMP accumulation suggesting that it may be an important component for odorant signal transduction. Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins by exchanging bound GDP for free GTP. TT26BHC SQ MDEERALYIVRAGEAGAIERVLRDYSDKHRATFKFESTDEDKRKKLCEGIFKVLIKDIPTTCQVSCLEVLRILSRDKKVLVPVTTKENMQILLRLAKLNELDDSLEKVSEFPVIVESLKCLCNIVFNSQMAQQLSLELNLAAKLCNLLRKCKDRKFINDIKCFDLRLLFLLSLLHTDIRSQLRYELQGLPLLTQILESAFSIKWTDEYESAIDHNGPPLSPQETDCAIEALKALFNVTVDSWKVHKESDSHQFRVMAAVLRHCLLIVGPTEDKTEELHSNAVNLLSNVPVSCLDVLICPLTHEETAQEATTLDELPSNKTAEKETVLKNNTMVYNGMNMEAIHVLLNFMEKRIDKGSSYREGLTPVLSLLTECSRAHRNIRKFLKDQVLPPLRDVTNRPEVGSTVRNKLVRLMTHVDLGVKQIAAEFLFVLCKERVDSLLKYTGYGNAAGLLAARGLLAGGRGDNWYSEDEDTDTEEYKNAKPKEELLKPMGLKPDGTITPLEEALNQYSVIEETSSDTD TT26BHC TT Literature-reported TT26BHC FM Synembryn family TTQY9DH ID TTQY9DH TTQY9DH TN TAO kinase 1 (TAOK1) TTQY9DH UP Q7L7X3 TTQY9DH UC TAOK1_HUMAN TTQY9DH SN hTAOK1; hKFC-B; Thousand and one amino acid protein kinase 1; TAOK1; Serine/threonine-protein kinase TAO1; Prostate-derived sterile 20-like kinase 2; Prostate-derived STE20-like kinase 2; PSK2; PSK-2; MARKK; MARK Kinase; MAP3K16; Kinase from chicken homolog B; KIAA1361 TTQY9DH GN TAOK1 TTQY9DH FC Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade. TTQY9DH EC EC 2.7.11.1 TTQY9DH SQ MPSTNRAGSLKDPEIAELFFKEDPEKLFTDLREIGHGSFGAVYFARDVRTNEVVAIKKMSYSGKQSTEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHTMIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHIFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQEAHNGPAVEAQEEEEEQDHGVGRTGTVNSVGSNQSIPSMSISASSQSSSVNSLPDVSDDKSELDMMEGDHTVMSNSSVIHLKPEEENYREEGDPRTRASDPQSPPQVSRHKSHYRNREHFATIRTASLVTRQMQEHEQDSELREQMSGYKRMRRQHQKQLMTLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQAAMEKEAKVMSNEEKKFQQHIQAQQKKELNSFLESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHLLETTPKSEHKAVLKRLKEEQTRKLAILAEQYDHSINEMLSTQALRLDEAQEAECQVLKMQLQQELELLNAYQSKIKMQAEAQHDRELRELEQRVSLRRALLEQKIEEEMLALQNERTERIRSLLERQAREIEAFDSESMRLGFSNMVLSNLSPEAFSHSYPGASGWSHNPTGGPGPHWGHPMGGPPQAWGHPMQGGPQPWGHPSGPMQGVPRGSSMGVRNSPQALRRTASGGRTEQGMSRSTSVTSQISNGSHMSYT TTQY9DH TT Literature-reported TT1GES9 ID TT1GES9 TT1GES9 TN T-cell leukemia virus Type-1 proteinase (TLV pro) TT1GES9 UP Q82443 TT1GES9 UC Q82443_9DELA TT1GES9 BC Protease TT1GES9 SN Protease TT1GES9 GN TLV pro TT1GES9 FC Critical for virion replication. TT1GES9 SQ KEFNMGGGLTSPPTLQQVLLNQDPASILPVIPLDPARRPVIKAQVDTQTSHPKTIEALLDTGADMTVLPIALFSSNTPLKNTSVLGAGGQTQDHFKLTSLPVLIRLPFRTTPIVLTSCLVDTKNNWAIIGRDALQQCQGVLYLPEAKGPPVILPIQAPAVLGLEHLPRPPEISQFPLNQNASRPCNTWSERPWRQAISNPTPDQEITQYSQLKRPMEPGDSSTTCGPLTL TT1GES9 TT Literature-reported TTUKRDV ID TTUKRDV TTUKRDV TN T-cell leukemia/lymphoma protein 1A (TCL1A) TTUKRDV UP P56279 TTUKRDV UC TCL1A_HUMAN TTUKRDV SN TCL1 oncogene; TCL1; TCL-1 protein; T-cell leukemia/lymphoma 1 oncogene; Protein p14 TCL1; P14 TCL1 protein; Oncogene TCL1; Oncogene TCL-1 TTUKRDV GN TCL1A TTUKRDV FC Promotes nuclear translocation of AKT1. Enhances cell proliferation, stabilizes mitochondrial membrane potential and promotes cell survival. Enhances the phosphorylation and activation of AKT1, AKT2 and AKT3. TTUKRDV PD 1JSG TTUKRDV SQ MAECPTLGEAVTDHPDRLWAWEKFVYLDEKQHAWLPLTIEIKDRLQLRVLLRREDVVLGRPMTPTQIGPSLLPIMWQLYPDGRYRSSDSSFWRLVYHIKIDGVEDMLLELLPDD TTUKRDV TT Literature-reported TTRBJ8C ID TTRBJ8C TTRBJ8C TN T-cell receptor beta chain V region CTL-L17 (TCRB) TTRBJ8C UP P04435 TTRBJ8C UC TVB79_HUMAN TTRBJ8C BC Immunoglobulin TTRBJ8C SN V beta 17 T-cell receptor; TRBV7-9; T cell receptor beta variable 7-9 TTRBJ8C GN TCRB TTRBJ8C FC Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens. Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation. The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity. V region of the variable domain of T cell receptor (TR) beta chain that participates in the antigen recognition. TTRBJ8C SQ MGTSLLCWMALCLLGADHADTGVSQNPRHKITKRGQNVTFRCDPISEHNRLYWYRQTLGQGPEFLTYFQNEAQLEKSRLLSDRFSAERPKGSFSTLEIQRTEQGDSAMYLCASSL TTRBJ8C TT Literature-reported TTEGYK1 ID TTEGYK1 TTEGYK1 TN T-cell surface glycoprotein CD5 (CD5) TTEGYK1 UP P06127 TTEGYK1 UC CD5_HUMAN TTEGYK1 SN Lymphocyte antigen T1/Leu-1; LEU1 TTEGYK1 GN CD5 TTEGYK1 FC May act as a receptor in regulating T-cell proliferation. TTEGYK1 PD 2OTT; 2JP0; 2JOP; 2JA4 TTEGYK1 SQ MPMGSLQPLATLYLLGMLVASCLGRLSWYDPDFQARLTRSNSKCQGQLEVYLKDGWHMVCSQSWGRSSKQWEDPSQASKVCQRLNCGVPLSLGPFLVTYTPQSSIICYGQLGSFSNCSHSRNDMCHSLGLTCLEPQKTTPPTTRPPPTTTPEPTAPPRLQLVAQSGGQHCAGVVEFYSGSLGGTISYEAQDKTQDLENFLCNNLQCGSFLKHLPETEAGRAQDPGEPREHQPLPIQWKIQNSSCTSLEHCFRKIKPQKSGRVLALLCSGFQPKVQSRLVGGSSICEGTVEVRQGAQWAALCDSSSARSSLRWEEVCREQQCGSVNSYRVLDAGDPTSRGLFCPHQKLSQCHELWERNSYCKKVFVTCQDPNPAGLAAGTVASIILALVLLVVLLVVCGPLAYKKLVKKFRQKKQRQWIGPTGMNQNMSFHRNHTATVRSHAENPTASHVDNEYSQPPRNSHLSAYPALEGALHRSSMQPDNSSDSDYDLHGAQRL TTEGYK1 TT Literature-reported TT1Y6J2 ID TT1Y6J2 TT1Y6J2 TN Telomeric repeat-binding factor 1 (TERF1) TT1Y6J2 UP P54274 TT1Y6J2 UC TERF1_HUMAN TT1Y6J2 SN Telomeric protein Pin2/TRF1; TTAGGG repeat-binding factor 1; TRF1; TRF; TRBF1; PIN2; NIMA-interacting protein 2 TT1Y6J2 GN TERF1 TT1Y6J2 FC Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. TT1Y6J2 PD 5XUP; 5WIR; 5HKP; 3L82; 3BQO TT1Y6J2 SQ MAEDVSSAAPSPRGCADGRDADPTEEQMAETERNDEEQFECQELLECQVQVGAPEEEEEEEEDAGLVAEAEAVAAGWMLDFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESALMIWGSIEKEHDKLHEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHMPFKSKLLMIISQKDTFHSFFQHFSYNHMMEKIKSYVNYVLSEKSSTFLMKAAAKVVESKRTRTITSQDKPSGNDVEMETEANLDTRKSVSDKQSAVTESSEGTVSLLRSHKNLFLSKLQHGTQQQDLNKKERRVGTPQSTKKKKESRRATESRIPVSKSQPVTPEKHRARKRQAWLWEEDKNLRSGVRKYGEGNWSKILLHYKFNNRTSVMLKDRWRTMKKLKLISSDSED TT1Y6J2 TT Literature-reported TT5XSLT ID TT5XSLT TT5XSLT TN Telomeric repeat-binding factor 2 (TERF2) TT5XSLT UP Q15554 TT5XSLT UC TERF2_HUMAN TT5XSLT SN Telomeric DNA-binding protein; TTAGGG repeat-binding factor 2; TRF2; TRBF2 TT5XSLT GN TERF2 TT5XSLT FC Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length. TT5XSLT PD 6J67; 5XYF; 5WQD; 4RQI; 4M7C TT5XSLT SQ MAAGAGTAGPASGPGVVRDPAASQPRKRPGREGGEGARRSDTMAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAAVIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKMLRFLESHLDDAEPYLLTMAKKALKSESAASSTGKEDKQPAPGPVEKPPREPARQLRNPPTTIGMMTLKAAFKTLSGAQDSEAAFAKLDQKDLVLPTQALPASPALKNKRPRKDENESSAPADGEGGSELQPKNKRMTISRLVLEEDSQSTEPSAGLNSSQEAASAPPSKPTVLNQPLPGEKNPKVPKGKWNSSNGVEEKETWVEEDELFQVQAAPDEDSTTNITKKQKWTVEESEWVKAGVQKYGEGNWAAISKNYPFVNRTAVMIKDRWRTMKRLGMN TT5XSLT TT Literature-reported TTWKT3Y ID TTWKT3Y TTWKT3Y TN Testis-specific kinase 1 (TESK1) TTWKT3Y UP Q15569 TTWKT3Y UC TESK1_HUMAN TTWKT3Y SN Testicular protein kinase 1; Dual specificity testis-specific protein kinase 1 TTWKT3Y GN TESK1 TTWKT3Y FC Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity). TTWKT3Y EC EC 2.7.12.1 TTWKT3Y SQ MAGERPPLRGPGPGPGEVPGEGPPGPGGTGGGPGRGRPSSYRALRSAVSSLARVDDFHCAEKIGAGFFSEVYKVRHRQSGQVMVLKMNKLPSNRGNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIARGLRYLHSKGVFHRDLTSKNCLVRREDRGFTAVVGDFGLAEKIPVYREGARKEPLAVVGSPYWMAPEVLRGELYDEKADVFAFGIVLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGDDCPLPFLLLAIHCCNLEPSTRAPFTEITQHLEWILEQLPEPAPLTRTALTHNQGSVARGGPSATLPRPDPRLSRSRSDLFLPPSPESPPNWGDNLTRVNPFSLREDLRGGKIKLLDTPSKPVLPLVPPSPFPSTQLPLVTTPETLVQPGTPARRCRSLPSSPELPRRMETALPGPGPPAVGPSAEEKMECEGSSPEPEPPGPAPQLPLAVATDNFISTCSSASQPWSPRSGPVLNNNPPAVVVNSPQGWAGEPWNRAQHSLPRAAALERTEPSPPPSAPREPDEGLPCPGCCLGPFSFGFLSMCPRPTPAVARYRNLNCEAGSLLCHRGHHAKPPTPSLQLPGARS TTWKT3Y TT Literature-reported TTRMD8U ID TTRMD8U TTRMD8U TN Testis-specific kinase 2 (TESK2) TTRMD8U UP Q96S53 TTRMD8U UC TESK2_HUMAN TTRMD8U SN Testicular protein kinase 2; Dual specificity testis-specific protein kinase 2 TTRMD8U GN TESK2 TTRMD8U FC Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser-3'. May play an important role in spermatogenesis. TTRMD8U EC EC 2.7.12.1 TTRMD8U SQ MDRSKRNSIAGFPPRVERLEEFEGGGGGEGNVSQVGRVWPSSYRALISAFSRLTRLDDFTCEKIGSGFFSEVFKVRHRASGQVMALKMNTLSSNRANMLKEVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINSGNLEQLLDSNLHLPWTVRVKLAYDIAVGLSYLHFKGIFHRDLTSKNCLIKRDENGYSAVVADFGLAEKIPDVSMGSEKLAVVGSPFWMAPEVLRDEPYNEKADVFSYGIILCEIIARIQADPDYLPRTENFGLDYDAFQHMVGDCPPDFLQLTFNCCNMDPKLRPSFVEIGKTLEEILSRLQEEEQERDRKLQPTARGLLEKAPGVKRLSSLDDKIPHKSPCPRRTIWLSRSQSDIFSRKPPRTVSVLDPYYRPRDGAARTPKVNPFSARQDLMGGKIKFFDLPSKSVISLVFDLDAPGPGTMPLADWQEPLAPPIRRWRSLPGSPEFLHQEACPFVGREESLSDGPPPRLSSLKYRVKEIPPFRASALPAAQAHEAMDCSILQEENGFGSRPQGTSPCPAGASEEMEVEERPAGSTPATFSTSGIGLQTQGKQDG TTRMD8U TT Literature-reported TTA3Z2W ID TTA3Z2W TTA3Z2W TN Testis-specific serine kinase 2 (TSSK2) TTA3Z2W UP Q96PF2 TTA3Z2W UC TSSK2_HUMAN TTA3Z2W SN Testis-specific serine/threonine-protein kinase 2; TSSK-2; TSK2; TSK-2; Serine/threonine-protein kinase 22B; STK22B; SPOGA2; DiGeorge syndrome protein G; DGSG; DGS-G TTA3Z2W GN TSSK2 TTA3Z2W FC Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates TSKS at 'Ser-288' and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body. TTA3Z2W EC EC 2.7.11.1 TTA3Z2W SQ MDDATVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHGSIIKTYEIFETSDGRIYIIMELGVQGDLLEFIKCQGALHEDVARKMFRQLSSAVKYCHDLDIVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDSNGRIILSKTFCGSAAYAAPEVLQSIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIRKMLRIQKEHRVDFPRSKNLTCECKDLIYRMLQPDVSQRLHIDEILSHSWLQPPKPKATSSASFKREGEGKYRAECKLDTKTGLRPDHRPDHKLGAKTQHRLLVVPENENRMEDRLAETSRAKDHHISGAEVGKAST TTA3Z2W TT Literature-reported TTMT6VE ID TTMT6VE TTMT6VE TN Tetraspanin-7 (TSPAN7) TTMT6VE UP P41732 TTMT6VE UC TSN7_HUMAN TTMT6VE BC Tetraspanin family TTMT6VE SN TSPAN7; TALLA-1; T-cell acute lymphoblastic leukemia-associated antigen 1; T-cell acute lymphoblastic leukemia associated antigen 1; Membrane component, X chromosome, surface marker 1; Cell surface glycoprotein A15; CD231 antigen TTMT6VE GN TSPAN7 TTMT6VE FC May be involved in cell proliferation and cell motility. TTMT6VE SQ MASRRMETKPVITCLKTLLIIYSFVFWITGVILLAVGVWGKLTLGTYISLIAENSTNAPYVLIGTGTTIVVFGLFGCFATCRGSPWMLKLYAMFLSLVFLAELVAGISGFVFRHEIKDTFLRTYTDAMQTYNGNDERSRAVDHVQRSLSCCGVQNYTNWSTSPYFLEHGIPPSCCMNETDCNPQDLHNLTVAATKVNQKGCYDLVTSFMETNMGIIAGVAFGIAFSQLIGMLLACCLSRFITANQYEMV TTMT6VE TT Literature-reported TTNU6I5 ID TTNU6I5 TTNU6I5 TN T-lymphoma invasion and metastasis 1 (TIAM1) TTNU6I5 UP Q13009 TTNU6I5 UC TIAM1_HUMAN TTNU6I5 SN TIAM-1; T-lymphoma invasion and metastasis-inducing protein 1 TTNU6I5 GN TIAM1 TTNU6I5 FC Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates RAC1, CDC42, and to a lesser extent RHOA. Required for normal cell adhesion and cell migration. Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. TTNU6I5 PD 4NXR; 4NXQ; 4NXP; 4K2P; 4K2O TTNU6I5 SQ MGNAESQHVEHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKVIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQDGTLEDFGSPIWVDRVDMGLRPVSYTDSSVTPSVDSSIVLTAASVQSMPDTEESRLYGDDATYLAEGGRRQHSYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETRASPRQLSTCQRANSLGDLYAQKNSGVTANGGPGSKFAGYCRNLVSDIPNLANHKMPPAAAEETPPYSNYNTLPCRKSHCLSEGATNPQISHSNSMQGRRAKTTQDVNAGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPTTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSIPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACATAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAMGRLGIFSVSSFHALVAARTGETGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPSINQVFGEGTEAVKKSLEGIFDDIVPDGKREKEVVLPNVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLIENKMQLYVPQPEEDIYELLYKEIEICPKVTQSIHIEKSDTAADTYGFSLSSVEEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAADALNSSMLKDFLSQPSLGLLVRTYPELEEGVELLESPPHRVDGPADLGESPLAFLTSNPGHSLCSEQGSSAETAPEETEGPDLESSDETDHSSKSTEQVAAFCRSLHEMNPSDQSPSPQDSTGPQLATMRQLSDADKLRKVICELLETERTYVKDLNCLMERYLKPLQKETFLTQDELDVLFGNLTEMVEFQVEFLKTLEDGVRLVPDLEKLEKVDQFKKVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPKQQHSSTLESYLIKPIQRILKYPLLLRELFALTDAESEEHYHLDVAIKTMNKVASHINEMQKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLLHTTVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKLVGSHRLSIYEDWDPFRFRHMIPTEALQVRALASADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKAVHSILRDKHRRQLLKTESLPSSQQYVPFGGKRLCALKGARPAMSRAVSAPSKSLGRRRRRLARNRFTIDSDAVSASSPEKESQQPPGGGDTDRWVEEQFDLAQYEEQDDIKETDILSDDDEFCESVKGASVDRDLQERLQATSISQRERGRKTLDSHASRMAQLKKQAALSGINGGLESASEEVIWVRREDFAPSRKLNTEI TTNU6I5 TT Literature-reported TTFE091 ID TTFE091 TTFE091 TN Toxoplasma Calcium-dependent protein kinase 1 (Tg CDPK1) TTFE091 UP A0A0F7UUA6 TTFE091 UC A0A0F7UUA6_TOXGV TTFE091 SN CAM kinase, CDPK family TgCDPK1 TTFE091 GN Tg CDPK1 TTFE091 FC Provides the mechanistic link between calcium signalling and motility, differentiation and invasion. Required for the microneme secretion at the apical complex and parasite proliferation. TTFE091 PD 6BFA TTFE091 SQ MGQQESTLGGAAGEPRSRGHAAGTSGGPGDHLHATPGMFVQHSTAIFSDRYKGQRVLGKGSFGEVILCKDKITGQECAVKVISKRQVKQKTDKESLLREVQLLKQLDHPNIMKLYEFFEDKGYFYLVGEVYTGGELFDEIISRKRFSEVDAARIIRQVLSGITYMHKNKIVHRDLKPENLLLESKSKDANIRIIDFGLSTHFEASKKMKDKIGTAYYIAPEVLHGTYDEKCDVWSTGVILYILLSGCPPFNGANEYDILKKVEKGKYTFELPQWKKVSESAKDLIRKMLTYVPSMRISARDALDHEWIQTYTKEQISVDVPSLDNAILNIRQFQGTQKLAQAALLYMGSKLTSQDETKELTAIFHKMDKNGDGQLDRAELIEGYKELMRMKGQDASMLDASAVEHEVDQVLDAVDFDKNGYIEYSEFVTVAMDRKTLLSRERLERAFRMFDSDNSGKISSTELATIFGVSDVDSETWKSVLSEVDKNNDGEVDFDEFQQMLLKLCGN TTFE091 TT Literature-reported TT1XW7U ID TT1XW7U TT1XW7U TN Toxoplasma Toxopain-1 (Tg cp1) TT1XW7U UP Q8MTU2 TT1XW7U UC Q8MTU2_TOXGO TT1XW7U BC Protease TT1XW7U SN Toxoplasma Cysteine proteinase TT1XW7U GN Tg cp1 TT1XW7U FC A cathepsin B, play a critical role in the pathogenesis of toxoplasmosis. Secreted in the parasitophorous vacuole, where it may be involved in the degradation of host cell peptides, a process extensively studied in the related apicomplexan Plasmodium falciparum TT1XW7U SQ MEGRKSFRVLGTPLPFAALAAILLLGCMYTRAAGTPDDSLFPLSEDTSVDPRESFSAEDVLNAFVSPESVESLFDSIVAEQVVATSGNLTESAPRDRDSAPERRSDGGTLRGHPEDAGELLRLLLADSEDMELWKANFFRHLTHSMRHIVRDSVLVSEKAFPSEQAGEAGRDPGDLKKALEETGEDVFWESRPASSNAAVALIKKKMEKQAGKTGEGAGHTWEPEVSLRFRYLSLKDAKKLMGTFLVNTKVEGFPTPKGMPLPAKEFENATEPVPAHFDARTAFPACKDVVGHVRDQGDCGSCWAFASTEAFNDRLCIRSQGKRLMPLSAQHTTSCCNAIHCASFGCNGGQPGMAWRWFERKGVVTGGDFDALGKGTTCWPYEVPFCAHHAKAPFPDCDATLVPRKTPKCRKDCEEQAYADNVHPFDQDTHKATSAYSLRSRDDVKRDMMTHGPVSGAFMVYEDFLSYKSGVYKHVSGLPVGGHAIKIIGWGTENGEEYWHAVNSWNTYWGDGGQFKIAMGQCGIDGEMVAGEAAWQETEGVVNGEEELPGQRAAGARAGAHAEEEREM TT1XW7U TT Literature-reported TTEL90S ID TTEL90S TTEL90S TN Tracheobronchial mucin 5A (MUC5AC) TTEL90S UP P98088 TTEL90S UC MUC5A_HUMAN TTEL90S SN Tracheobronchial mucin; TBM; Mucin5AC; Mucin5 subtype AC, tracheobronchial; Mucin-5AC; Mucin-5 subtype AC, tracheobronchial; Major airway glycoprotein; MUC5; MUC-5AC; Lewis B blood group antigen; LeB; Gastric mucin TTEL90S GN MUC5AC TTEL90S FC Gel-forming glycoprotein of gastric and respiratoy tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microrganisms and particles that are subsequently removed by the mucocilary system. TTEL90S PD 5AJP; 5AJO; 5AJN TTEL90S SQ MSVGRRKLALLWALALALACTRHTGHAQDGSSESSYKHHPALSPIARGPSGVPLRGATVFPSLRTIPVVRASNPAHNGRVCSTWGSFHYKTFDGDVFRFPGLCNYVFSEHCGAAYEDFNIQLRRSQESAAPTLSRVLMKVDGVVIQLTKGSVLVNGHPVLLPFSQSGVLIQQSSSYTKVEARLGLVLMWNHDDSLLLELDTKYANKTCGLCGDFNGMPVVSELLSHNTKLTPMEFGNLQKMDDPTDQCQDPVPEPPRNCSTGFGICEELLHGQLFSGCVALVDVGSYLEACRQDLCFCEDTDLLSCVCHTLAEYSRQCTHAGGLPQDWRGPDFCPQKCPNNMQYHECRSPCADTCSNQEHSRACEDHCVAGCFCPEGTVLDDIGQTGCVPVSKCACVYNGAAYAPGATYSTDCTNCTCSGGRWSCQEVPCPGTCSVLGGAHFSTFDGKQYTVHGDCSYVLTKPCDSSAFTVLAELRRCGLTDSETCLKSVTLSLDGAQTVVVIKASGEVFLNQIYTQLPISAANVTIFRPSTFFIIAQTSLGLQLNLQLVPTMQLFMQLAPKLRGQTCGLCGNFNSIQADDFRTLSGVVEATAAAFFNTFKTQAACPNIRNSFEDPCSLSVENEKYAQHWCSQLTDADGPFGRCHAAVKPGTYYSNCMFDTCNCERSEDCLCAALSSYVHACAAKGVQLGGWRDGVCTKPMTTCPKSMTYHYHVSTCQPTCRSLSEGDITCSVGFIPVDGCICPKGTFLDDTGKCVQASNCPCYHRGSMIPNGESVHDSGAICTCTHGKLSCIGGQAPAPVCAAPMVFFDCRNATPGDTGAGCQKSCHTLDMTCYSPQCVPGCVCPDGLVADGEGGCITAEDCPCVHNEASYRAGQTIRVGCNTCTCDSRMWRCTDDPCLATCAVYGDGHYLTFDGQSYSFNGDCEYTLVQNHCGGKDSTQDSFRVVTENVPCGTTGTTCSKAIKIFLGGFELKLSHGKVEVIGTDESQEVPYTIRQMGIYLVVDTDIGLVLLWDKKTSIFINLSPEFKGRVCGLCGNFDDIAVNDFATRSRSVVGDVLEFGNSWKLSPSCPDALAPKDPCTANPFRKSWAQKQCSILHGPTFAACHAHVEPARYYEACVNDACACDSGGDCECFCTAVAAYAQACHEVGLCVSWRTPSICPLFCDYYNPEGQCEWHYQPCGVPCLRTCRNPRGDCLRDVRGLEGCYPKCPPEAPIFDEDKMQCVATCPTPPLPPRCHVHGKSYRPGAVVPSDKNCQSCLCTERGVECTYKAEACVCTYNGQRFHPGDVIYHTTDGTGGCISARCGANGTIERRVYPCSPTTPVPPTTFSFSTPPLVVSSTHTPSNGPSSAHTGPPSSAWPTTAGTSPRTRLPTASASLPPVCGEKCLWSPWMDVSRPGRGTDSGDFDTLENLRAHGYRVCESPRSVECRAEDAPGVPLRALGQRVQCSPDVGLTCRNREQASGLCYNYQIRVQCCTPLPCSTSSSPAQTTPPTTSKTTETRASGSSAPSSTPGTVSLSTARTTPAPGTATSVKKTFSTPSPPPVPATSTSSMSTTAPGTSVVSSKPTPTEPSTSSCLQELCTWTEWIDGSYPAPGINGGDFDTFQNLRDEGYTFCESPRSVQCRAESFPNTPLADLGQDVICSHTEGLICLNKNQLPPICYNYEIRIQCCETVNVCRDITRLPKTVATTRPTPHPTGAQTQTTFTTHMPSASTEQPTATSRGGPTATSVTQGTHTTLVTRNCHPRCTWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAKSHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPRGCHMTSTPGSTSSSPAQTTPSTTSKTTETQASGSSAPSSTPGTVSLSTARTTPAPGTATSVKKTFSTPSPPPVPATSTSSMSTTAPGTSVVSSKPTPTEPSTSSCLQELCTWTEWIDGSYPAPGINGGDFDTFQNLRDEGYTFCESPRSVQCRAESFPNTPLADLGQDVICSHTEGLICLNKNQLPPICYNYEIRIQCCETVNVCRDITRPPKTVATTRPTPHPTGAQTQTTFTTHMPSASTEQPTATSRGGPTATSVTQGTHTTPVTRNCHPRCTWTTWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAKSHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTPVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTTSTTSTPQTSTTYAHTTSTTSAPTARTTSAPTTRTTSASPASTTSGPGNTPSPVPTTSTISAPTTSITSAPTTSTTSAPTSSTTSGPGTTPSPVPTTSITSAPTTSTTSAPTTSTTSARTSSTTSATTTSRISGPETTPSPVPTTSTTSATTTSTTSAPTTSTTSAPTSSTTSSPQTSTTSAPTTSTTSGPGTTPSPVPTTSTTSAPTTRTTSAPKSSTTSAATTSTTSGPETTPRPVPTTSTTSSPTTSTTSAPTTSTTSASTTSTTSGAGTTPSPVPTTSTTSAPTTSTTSAPISSTTSATTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSGPGTTPSAVPTTSITSAPTTSTNSAPISSTTSATTTSRISGPETTPSPVPTASTTSASTTSTTSGPGTTPSPVPTTSTISVPTTSTTSASTTSTTSASTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSAPTTSTISAPTTSTTSATTTSTTSAPTPRRTSAPTTSTISASTTSTTSATTTSTTSATTTSTISAPTTSTTLSPTTSTTSTTITSTTSAPISSTTSTPQTSTTSAPTTSTTSGPGTTSSPVPTTSTTSAPTTSTTSAPTTRTTSVPTSSTTSTATTSTTSGPGTTPSPVPTTSTTSAPTTRTTSAPTTSTTSAPTTSTTSAPTSSTTSATTTSTISVPTTSTTSVPGTTPSPVPTTSTISVPTTSTTSASTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSAPTTSTISAPTTSTPSAPTTSTTLAPTTSTTSAPTTSTTSTPTSSTTSSPQTSTTSASTTSITSGPGTTPSPVPTTSTTSAPTTSTTSAATTSTISAPTTSTTSAPTTSTTSASTASKTSGLGTTPSPIPTTSTTSPPTTSTTSASTASKTSGPGTTPSPVPTTSTIFAPRTSTTSASTTSTTPGPGTTPSPVPTTSTASVSKTSTSHVSISKTTHSQPVTRDCHLRCTWTKWFDIDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAESHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTPVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTTSTTSTPQTSTTSAPTTSTTSAPTTSTTSAPTTSTTSTPQTSISSAPTSSTTSAPTSSTISARTTSIISAPTTSTTSSPTTSTTSATTTSTTSAPTSSTTSTPQTSKTSAATSSTTSGSGTTPSPVTTTSTASVSKTSTSHVSVSKTTHSQPVTRDCHPRCTWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAKSHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTSVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTSSITSTTQTSTTSAPTTSTTPASIPSTTSAPTTSTTSAPTTSTTSAPTTSTTSTPQTTTSSAPTSSTTSAPTTSTISAPTTSTISAPTTSTTSAPTASTTSAPTSTSSAPTTNTTSAPTTSTTSAPITSTISAPTTSTTSTPQTSTISSPTTSTTSTPQTSTTSSPTTSTTSAPTTSTTSAPTTSTTSTPQTSISSAPTSSTTSAPTASTISAPTTSTTSFHTTSTTSPPTSSTSSTPQTSKTSAATSSTTSGSGTTPSPVPTTSTASVSKTSTSHVSVSKTTHSQPVTRDCHPRCTWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAESHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTPVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTTSTTSTPQTSTTSAPTTSTIPASTPSTTSAPTTSTTSAPTTSTTSAPTHRTTSGPTTSTTLAPTTSTTSAPTTSTNSAPTTSTISASTTSTISAPTTSTISSPTSSTTSTPQTSKTSAATSSTTSGSGTTPSPVPTTSTTSASTTSTTSAPTTSTTSGPGTTPSPVPSTSTTSAATTSTTSAPTTRTTSAPTSSMTSGPGTTPSPVPTTSTTSAPTTSTTSGPGTTPSPVPTTSTTSAPITSTTSGPGSTPSPVPTTSTTSAPTTSTTSASTASTTSGPGTTPSPVPTTSTTSAPTTRTTSASTASTTSGPGSTPSPVPTTSTTSAPTTRTTPASTASTTSGPGTTPSPVPTTSTTSASTTSTISLPTTSTTSAPITSMTSGPGTTPSPVPTTSTTSAPTTSTTSASTASTTSGPGTTPSPVPTTSTTSAPTTSTTSASTASTTSGPGTSLSPVPTTSTTSAPTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSGPGTTPSPVPTTSTTPVSKTSTSHLSVSKTTHSQPVTSDCHPLCAWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAESHPEVNIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPRGCPVTSVTPYGTSPTNALYPSLSTSMVSASVASTSVASSSVASSSVAYSTQTCFCNVADRLYPAGSTIYRHRDLAGHCYYALCSQDCQVVRGVDSDCPSTTLPPAPATSPSISTSEPVTELGCPNAVPPRKKGETWATPNCSEATCEGNNVISLRPRTCPRVEKPTCANGYPAVKVADQDGCCHHYQCQCVCSGWGDPHYITFDGTYYTFLDNCTYVLVQQIVPVYGHFRVLVDNYFCGAEDGLSCPRSIILEYHQDRVVLTRKPVHGVMTNEIIFNNKVVSPGFRKNGIVVSRIGVKMYATIPELGVQVMFSGLIFSVEVPFSKFANNTEGQCGTCTNDRKDECRTPRGTVVASCSEMSGLWNVSIPDQPACHRPHPTPTTVGPTTVGSTTVGPTTVGSTTVGPTTPPAPCLPSPICQLILSKVFEPCHTVIPPLLFYEGCVFDRCHMTDLDVVCSSLELYAALCASHDICIDWRGRTGHMCPFTCPADKVYQPCGPSNPSYCYGNDSASLGALPEAGPITEGCFCPEGMTLFSTSAQVCVPTGCPRCLGPHGEPVKVGHTVGMDCQECTCEAATWTLTCRPKLCPLPPACPLPGFVPVPAAPQAGQCCPQYSCACNTSRCPAPVGCPEGARAIPTYQEGACCPVQNCSWTVCSINGTLYQPGAVVSSSLCETCRCELPGGPPSDAFVVSCETQICNTHCPVGFEYQEQSGQCCGTCVQVACVTNTSKSPAHLFYPGETWSDAGNHCVTHQCEKHQDGLVVVTTKKACPPLSCSLDEARMSKDGCCRFCPPPPPPYQNQSTCAVYHRSLIIQQQGCSSSEPVRLAYCRGNCGDSSSMYSLEGNTVEHRCQCCQELRTSLRNVTLHCTDGSSRAFSYTEVEECGCMGRRCPAPGDTQHSEEAEPEPSQEAESGSWERGVPVSPMH TTEL90S TT Literature-reported TT0KV32 ID TT0KV32 TT0KV32 TN Transcobalamin receptor (CD320) TT0KV32 UP Q9NPF0 TT0KV32 UC CD320_HUMAN TT0KV32 SN UNQ198/PRO224; TCblR; FDCsignaling molecule 8D6; FDCSM8D6; FDC-signaling molecule 8D6; FDC-SM-8D6; CD320 antigen; 8D6A; 8D6 antigen TT0KV32 GN CD320 TT0KV32 FC Plays an important role in cobalamin uptake. Plasma membrane protein that is expressed on follicular dendritic cells (FDC) and mediates interaction with germinal center B cells. Functions as costimulator to promote B cell responses to antigenic stimuli; promotes B cell differentiation and proliferation. Germinal center-B (GC-B) cells differentiate into memory B-cells and plasma cells (PC) through interaction with T-cells and follicular dendritic cells (FDC). CD320 augments the proliferation of PC precursors generated by IL-10. Receptor for transcobalamin saturated with cobalamin (TCbl). TT0KV32 PD 4ZRQ; 4ZRP TT0KV32 SQ MSGGWMAQVGAWRTGALGLALLLLLGLGLGLEAAASPLSTPTSAQAAGPSSGSCPPTKFQCRTSGLCVPLTWRCDRDLDCSDGSDEEECRIEPCTQKGQCPPPPGLPCPCTGVSDCSGGTDKKLRNCSRLACLAGELRCTLSDDCIPLTWRCDGHPDCPDSSDELGCGTNEILPEGDATTMGPPVTLESVTSLRNATTMGPPVTLESVPSVGNATSSSAGDQSGSPTAYGVIAAAAVLSASLVTATLLLLSWLRAQERLRPLGLLVAMKESLLLSEQKTSLP TT0KV32 TT Literature-reported TT80QAL ID TT80QAL TT80QAL TN Transcription factor 7-like 2 (TCF7L2) TT80QAL UP Q9NQB0 TT80QAL UC TF7L2_HUMAN TT80QAL SN TCF4; TCF-4; T-cell-specific transcription factor 4; T-cell transcription factor-4; T-cell factor 4; HTCF-4; HMG box transcription factor 4 TT80QAL GN TCF7L2 TT80QAL FC Acts as repressor in the absence of CTNNB1, and as activator in its presence. Activates transcription from promoters with several copies of the Tcf motif 5'-CCTTTGATC-3' in the presence of CTNNB1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7L2/TCF4 and CTNNB1. Expression of dominant-negative mutants results in cell-cycle arrest in G1. Necessary for the maintenance of the epithelial stem-cell compartment of the small intestine. Participates in the Wnt signaling pathway and modulates MYC expression by binding to its promoter in a sequence-specific manner. TT80QAL PD 2GL7; 1JPW; 1JDH TT80QAL SQ MPQLNGGGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESETNQNSSSDSEAERRPPPRSESFRDKSRESLEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSPTARTLHFQSGSTHYSAYKTIEHQIAVQYLQMKWPLLDVQAGSLQSRQALKDARSPSPAHIVSNKVPVVQHPHHVHPLTPLITYSNEHFTPGNPPPHLPADVDPKTGIPRPPHPPDISPYYPLSPGTVGQIPHPLGWLVPQQGQPVYPITTGGFRHPYPTALTVNASMSRFPPHMVPPHHTLHTTGIPHPAIVTPTVKQESSQSDVGSLHSSKHQDSKKEEEKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKRDKQPGETNEHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCRRKKKCVRYIQGEGSCLSPPSSDGSLLDSPPPSPNLLGSPPRDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAEATHKASALCPNGALDLPPAALQPAAPSSSIAQPSTSSLHSHSSLAGTQPQPLSLVTKSLE TT80QAL TT Literature-reported TT5FYX0 ID TT5FYX0 TT5FYX0 TN Transcription factor E2F2 (E2F2) TT5FYX0 UP Q14209 TT5FYX0 UC E2F2_HUMAN TT5FYX0 SN E2F-2 TT5FYX0 GN E2F2 TT5FYX0 FC The DRTF1/E2F complex functions in the control of cell-cycle progression from g1 to s phase. E2F2 binds specifically to RB1 in a cell-cycle dependent manner. Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. TT5FYX0 PD 1N4M TT5FYX0 SQ MLQGPRALASAAGQTPKVVPAMSPTELWPSGLSSPQLCPATATYYTPLYPQTAPPAAAPGTCLDATPHGPEGQVVRCLPAGRLPAKRKLDLEGIGRPVVPEFPTPKGKCIRVDGLPSPKTPKSPGEKTRYDTSLGLLTKKFIYLLSESEDGVLDLNWAAEVLDVQKRRIYDITNVLEGIQLIRKKAKNNIQWVGRGMFEDPTRPGKQQQLGQELKELMNTEQALDQLIQSCSLSFKHLTEDKANKRLAYVTYQDIRAVGNFKEQTVIAVKAPPQTRLEVPDRTEDNLQIYLKSTQGPIEVYLCPEEVQEPDSPSEEPLPSTSTLCPSPDSAQPSSSTDPSIMEPTASSVPAPAPTPQQAPPPPSLVPLEATDSLLELPHPLLQQTEDQFLSPTLACSSPLISFSPSLDQDDYLWGLEAGEGISDLFDSYDLGDLLIN TT5FYX0 TT Literature-reported TTCNOT6 ID TTCNOT6 TTCNOT6 TN Transcription factor SOX-2 (SOX2) TTCNOT6 UP P48431 TTCNOT6 UC SOX2_HUMAN TTCNOT6 SN SRY-box 2; MCOPS3; ANOP3 TTCNOT6 GN SOX2 TTCNOT6 FC Critical for early embryogenesis and for embryonic stem cell pluripotency. May function as a switch in neuronal development. Downstream SRRT target that mediates the promotion of neural stem cell self-renewal. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation. Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. TTCNOT6 PD 2LE4; 1O4X TTCNOT6 SQ MYNMMETELKPPGPQQTSGGGGGNSTAAAAGGNQKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSETEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGGNSMASGVGVGAGLGAGVNQRMDSYAHMNGWSNGSYSMMQDQLGYPQHPGLNAHGAAQMQPMHRYDVSALQYNSMTSSQTYMNGSPTYSMSYSQQGTPGMALGSMGSVVKSEASSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPEPAAPSRLHMSQHYQSGPVPGTAINGTLPLSHM TTCNOT6 TT Literature-reported TTYXT16 ID TTYXT16 TTYXT16 TN Transducin beta-like 1X-related protein 1 (TBL1XR1) TTYXT16 UP Q9BZK7 TTYXT16 UC TBL1R_HUMAN TTYXT16 SN Transducin betalike 1Xrelated protein 1; TBLR1; TBL1related protein 1; TBL1-related protein 1; Nuclear receptor corepressor/HDAC3 complexsubunit TBLR1; Nuclear receptor corepressor/HDAC3 complex subunit TBLR1; IRA1; Fboxlike/WD repeatcontaining protein TBL1XR1; F-box-like/WD repeat-containing protein TBL1XR1 TTYXT16 GN TBL1XR1 TTYXT16 FC Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of the N-Cor corepressor complex that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of N-Cor complex, thereby allowing cofactor exchange, and transcription activation. F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. TTYXT16 PD 4LG9 TTYXT16 SQ MSISSDEVNFLVYRYLQESGFSHSAFTFGIESHISQSNINGALVPPAALISIIQKGLQYVEAEVSINEDGTLFDGRPIESLSLIDAVMPDVVQTRQQAYRDKLAQQQAAAAAAAAAAASQQGSAKNGENTANGEENGAHTIANNHTDMMEVDGDVEIPPNKAVVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSENSTSGSTQLVLRHCIREGGQDVPSNKDVTSLDWNSEGTLLATGSYDGFARIWTKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNNTFASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYTIKWSPTGPGTNNPNANLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHSYRGTGGIFEVCWNAAGDKVGASASDGSVCVLDLRK TTYXT16 TT Literature-reported TTQ4UFD ID TTQ4UFD TTQ4UFD TN Transforming acidic coiled-coil protein 3 (TACC3) TTQ4UFD UP Q9Y6A5 TTQ4UFD UC TACC3_HUMAN TTQ4UFD SN Transforming acidic coiled-coil-containing protein 3; ERIC1; ERIC-1 TTQ4UFD GN TACC3 TTQ4UFD FC Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. May be involved in the control of cell growth and differentiation. May contribute to cancer. Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. TTQ4UFD PD 5ODT; 5ODS; 5LXO; 5LXN TTQ4UFD SQ MSLQVLNDKNVSNEKNTENCDFLFSPPEVTGRSSVLRVSQKENVPPKNLAKAMKVTFQTPLRDPQTHRILSPSMASKLEAPFTQDDTLGLENSHPVWTQKENQQLIKEVDAKTTHGILQKPVEADTDLLGDASPAFGSGSSSESGPGALADLDCSSSSQSPGSSENQMVSPGKVSGSPEQAVEENLSSYSLDRRVTPASETLEDPCRTESQHKAETPHGAEEECKAETPHGAEEECRHGGVCAPAAVATSPPGAIPKEACGGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPESTAPTNHLVAGRAMTLSPQEEVAAGQMASSSRSGPVKLEFDVSDGATSKRAPPPRRLGERSGLKPPLRKAAVRQQKAPQEVEEDDGRSGAGEDPPMPASRGSYHLDWDKMDDPNFIPFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGPCLSQQLHSASAEDTPVVQLAAETPTAESKERALNSASTSLPTSCPGSEPVPTHQQGQPALELKEESFRDPAEVLGTGAEVDYLEQFGTSSFKESALRKQSLYLKFDPLLRDSPGRPVPVATETSSMHGANETPSGRPREAKLVEFDFLGALDIPVPGPPPGVPAPGGPPLSTGPIVDLLQYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI TTQ4UFD TT Literature-reported TT6LPFO ID TT6LPFO TT6LPFO TN Transforming protein RhoB (RHOB) TT6LPFO UP P62745 TT6LPFO UC RHOB_HUMAN TT6LPFO SN RhoB TT6LPFO GN RHOB TT6LPFO FC Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. TT6LPFO PD 2FV8 TT6LPFO SQ MAAIRKKLVVVGDGACGKTCLLIVFSKDEFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSVDSPDSLENIPEKWVPEVKHFCPNVPIILVANKKDLRSDEHVRTELARMKQEPVRTDDGRAMAVRIQAYDYLECSAKTKEGVREVFETATRAALQKRYGSQNGCINCCKVL TT6LPFO TT Literature-reported TTDRZ9H ID TTDRZ9H TTDRZ9H TN Transgelin (TAGLN) TTDRZ9H UP Q01995 TTDRZ9H UC TAGL_HUMAN TTDRZ9H BC Calponin family TTDRZ9H SN TAGLN; Smooth muscle protein 22-alpha; SM22-alpha; Protein WS3-10; 22 kDa actin-binding protein TTDRZ9H GN TAGLN TTDRZ9H FC Actin cross-linking/gelling protein. Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence. TTDRZ9H SQ MANKGPSYGMSREVQSKIEKKYDEELEERLVEWIIVQCGPDVGRPDRGRLGFQVWLKNGVILSKLVNSLYPDGSKPVKVPENPPSMVFKQMEQVAQFLKAAEDYGVIKTDMFQTVDLFEGKDMAAVQRTLMALGSLAVTKNDGHYRGDPNWFMKKAQEHKREFTESQLQEGKHVIGLQMGSNRGASQAGMTGYGRPRQIIS TTDRZ9H TT Literature-reported TTE1OHM ID TTE1OHM TTE1OHM TN Transmembrane 6 superfamily member 2 (TM6SF2) TTE1OHM UP Q9BZW4 TTE1OHM UC TM6S2_HUMAN TTE1OHM BC TM6SF family TTE1OHM SN KIAA1926 TTE1OHM GN TM6SF2 TTE1OHM FC Regulator of liver fat metabolism influencing triglyceride secretion and hepatic lipid droplet content (PubMed:24531328, PubMed:24927523). May function as sterol isomerase (PubMed:25566323). TTE1OHM SQ MDIPPLAGKIAALSLSALPVSYALNHVSALSHPLWVALMSALILGLLFVAVYSLSHGEVSYDPLYAVFAVFAFTSVVDLIIALQEDSYVVGFMEFYTKEGEPYLRTAHGVFICYWDGTVHYLLYLAMAGAICRRKRYRNFGLYWLGSFAMSILVFLTGNILGKYSSEIRPAFFLTIPYLLVPCWAGMKVFSQPRALTRCTANMVQEEQRKGLLQRPADLALVIYLILAGFFTLFRGLVVLDCPTDACFVYIYQYEPYLRDPVAYPKVQMLMYMFYVLPFCGLAAYALTFPGCSWLPDWALVFAGGIGQAQFSHMGASMHLRTPFTYRVPEDTWGCFFVCNLLYALGPHLLAYRCLQWPAFFHQPPPSDPLALHKKQH TTE1OHM TT Literature-reported TTL9KE7 ID TTL9KE7 TTL9KE7 TN Transmembrane protease serine 6 (TMPRSS6) TTL9KE7 UP Q8IU80 TTL9KE7 UC TMPS6_HUMAN TTL9KE7 SN Matriptase-2 TTL9KE7 GN TMPRSS6 TTL9KE7 FC Serine protease which hydrolyzes a range of proteins including type I collagen, fibronectin and fibrinogen. Can also activate urokinase-type plasminogen activator with low efficiency. May play a specialized role in matrix remodeling processes in liver. Through the cleavage of HJV, a regulator of the expression of the iron absorption-regulating hormone hepicidin/HAMP, plays a role in iron homeostasis. TTL9KE7 EC EC 3.4.21.- TTL9KE7 SQ MLLLFHSKRMPVAEAPQVAGGQGDGGDGEEAEPEGMFKACEDSKRKARGYLRLVPLFVLLALLVLASAGVLLWYFLGYKAEVMVSQVYSGSLRVLNRHFSQDLTRRESSAFRSETAKAQKMLKELITSTRLGTYYNSSSVYSFGEGPLTCFFWFILQIPEHRRLMLSPEVVQALLVEELLSTVNSSAAVPYRAEYEVDPEGLVILEASVKDIAALNSTLGCYRYSYVGQGQVLRLKGPDHLASSCLWHLQGPKDLMLKLRLEWTLAECRDRLAMYDVAGPLEKRLITSVYGCSRQEPVVEVLASGAIMAVVWKKGLHSYYDPFVLSVQPVVFQACEVNLTLDNRLDSQGVLSTPYFPSYYSPQTHCSWHLTVPSLDYGLALWFDAYALRRQKYDLPCTQGQWTIQNRRLCGLRILQPYAERIPVVATAGITINFTSQISLTGPGVRVHYGLYNQSDPCPGEFLCSVNGLCVPACDGVKDCPNGLDERNCVCRATFQCKEDSTCISLPKVCDGQPDCLNGSDEEQCQEGVPCGTFTFQCEDRSCVKKPNPQCDGRPDCRDGSDEEHCDCGLQGPSSRIVGGAVSSEGEWPWQASLQVRGRHICGGALIADRWVITAAHCFQEDSMASTVLWTVFLGKVWQNSRWPGEVSFKVSRLLLHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPISNALQKVDVQLIPQDLCSEVYRYQVTPRMLCAGYRKGKKDACQGDSGGPLVCKALSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVISWIQQVVT TTL9KE7 TT Literature-reported TTHZQP0 ID TTHZQP0 TTHZQP0 TN Triggering receptor expressed on monocytes 1 (TREM1) TTHZQP0 UP Q9NP99 TTHZQP0 UC TREM1_HUMAN TTHZQP0 SN Trem1; TREM-1 TTHZQP0 GN Trem1 TTHZQP0 FC Stimulates neutrophil and monocyte-mediated inflammatory responses. Triggers release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a crucial mediator of septic shock. TTHZQP0 PD 1SMO; 1Q8M TTHZQP0 SQ MRKTRLWGLLWMLFVSELRAATKLTEEKYELKEGQTLDVKCDYTLEKFASSQKAWQIIRDGEMPKTLACTERPSKNSHPVQVGRIILEDYHDHGLLRVRMVNLQVEDSGLYQCVIYQPPKEPHMLFDRIRLVVTKGFSGTPGSNENSTQNVYKIPPTTTKALCPLYTSPRTVTQAPPKSTADVSTPDSEINLTNVTDIIRVPVFNIVILLAGGFLSKSLVFSVLFAVTLRSFVP TTHZQP0 TT Literature-reported TTQRMSJ ID TTQRMSJ TTQRMSJ TN Triggering receptor expressed on monocytes 2 (TREM2) TTQRMSJ UP Q9NZC2 TTQRMSJ UC TREM2_HUMAN TTQRMSJ SN Triggering receptor expressed on myeloid cells 2; TREM-2 TTQRMSJ GN TREM2 TTQRMSJ FC Forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding. Acts as a receptor for amyloid-beta protein 42, a cleavage product of the amyloid-beta precursor protein APP, and mediates its uptake and degradation by microglia. Binding to amyloid-beta 42 mediates microglial activation, proliferation, migration, apoptosis and expression of pro-inflammatory cytokines, such as IL6R and CCL3, and the anti-inflammatory cytokine ARG1 (By similarity). Acts as a receptor for lipoprotein particles such as LDL, VLDL, and HDL and for apolipoproteins such as APOA1, APOA2, APOB, APOE, APOE2, APOE3, APOE4, and CLU and enhances their uptake in microglia. Binds phospholipids (preferably anionic lipids) such as phosphatidylserine, phosphatidylethanolamine, phosphatidylglycerol and sphingomyelin. Regulates microglial proliferation by acting as an upstream regulator of the Wnt/beta-catenin signaling cascade (By similarity). Required for microglial phagocytosis of apoptotic neurons. Also required for microglial activation and phagocytosis of myelin debris after neuronal injury and of neuronal synapses during synapse elimination in the developing brain (By similarity). Regulates microglial chemotaxis and process outgrowth, and also the microglial response to oxidative stress and lipopolysaccharide (By similarity). It suppresses PI3K and NF-kappa-B signaling in response to lipopolysaccharide; thus promoting phagocytosis, suppressing pro-inflammatory cytokine and nitric oxide production, inhibiting apoptosis and increasing expression of IL10 and TGFB (By similarity). During oxidative stress, it promotes anti-apoptotic NF-kappa-B signaling and ERK signaling (By similarity). Plays a role in microglial MTOR activation and metabolism (By similarity). Regulates age-related changes in microglial numbers. Triggers activation of the immune responses in macrophages and dendritic cells. Mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (By similarity). In dendritic cells, it mediates up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival. Involved in the positive regulation of osteoclast differentiation. TTQRMSJ PD 6B8O; 5UD8; 5UD7; 5ELI TTQRMSJ SQ MEPLRLLILLFVTELSGAHNTTVFQGVAGQSLQVSCPYDSMKHWGRRKAWCRQLGEKGPCQRVVSTHNLWLLSFLRRWNGSTAITDDTLGGTLTITLRNLQPHDAGLYQCQSLHGSEADTLRKVLVEVLADPLDHRDAGDLWFPGESESFEDAHVEHSISRSLLEGEIPFPPTSILLLLACIFLIKILAASALWAAAWHGQKPGTHPPSELDCGHDPGYQLQTLPGLRDT TTQRMSJ TT Literature-reported TT613U4 ID TT613U4 TT613U4 TN Tripartite motif-containing 59 (TRIM59) TT613U4 UP Q8IWR1 TT613U4 UC TRI59_HUMAN TT613U4 BC TRIM/RBCC family TT613U4 SN Tumor suppressor TSBF-1; TSBF1; TRIM57; RNF104; RING finger protein 104 TT613U4 GN TRIM59 TT613U4 FC May serve as a multifunctional regulator for innate immune signaling pathways. TT613U4 SQ MHNFEEELTCPICYSIFEDPRVLPCSHTFCRNCLENILQASGNFYIWRPLRIPLKCPNCRSITEIAPTGIESLPVNFALRAIIEKYQQEDHPDIVTCPEHYRQPLNVYCLLDKKLVCGHCLTIGQHHGHPIDDLQSAYLKEKDTPQKLLEQLTDTHWTDLTHLIEKLKEQKSHSEKMIQGDKEAVLQYFKELNDTLEQKKKSFLTALCDVGNLINQEYTPQIERMKEIREQQLELMALTISLQEESPLKFLEKVDDVRQHVQILKQRPLPEVQPVEIYPRVSKILKEEWSRTEIGQIKNVLIPKMKISPKRMSCSWPGKDEKEVEFLKILNIVVVTLISVILMSILFFNQHIITFLSEITLIWFSEASLSVYQSLSNSLHKVKNILCHIFYLLKEFVWKIVSH TT613U4 TT Literature-reported TT50OG3 ID TT50OG3 TT50OG3 TN TRPV1 messenger RNA (TRPV1 mRNA) TT50OG3 UP Q8NER1 TT50OG3 UC TRPV1_HUMAN TT50OG3 BC mRNA target TT50OG3 SN Vanilloid receptor 1 (mRNA); VR1 (mRNA); TrpV1 (mRNA); Transient receptor potential cation channel subfamily V member 1 (mRNA); Osm-9-like TRP channel 1 (mRNA); OTRPC1 (mRNA); Capsaicin receptor (mRNA) TT50OG3 GN TRPV1 TT50OG3 FC Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6. 5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis. Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. TT50OG3 SQ MKKWSSTDLGAAADPLQKDTCPDPLDGDPNSRPPPAKPQLSTAKSRTRLFGKGDSEEAFPVDCPHEEGELDSCPTITVSPVITIQRPGDGPTGARLLSQDSVAASTEKTLRLYDRRSIFEAVAQNNCQDLESLLLFLQKSKKHLTDNEFKDPETGKTCLLKAMLNLHDGQNTTIPLLLEIARQTDSLKELVNASYTDSYYKGQTALHIAIERRNMALVTLLVENGADVQAAAHGDFFKKTKGRPGFYFGELPLSLAACTNQLGIVKFLLQNSWQTADISARDSVGNTVLHALVEVADNTADNTKFVTSMYNEILMLGAKLHPTLKLEELTNKKGMTPLALAAGTGKIGVLAYILQREIQEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFLVYCLYMIIFTMAAYYRPVDGLPPFKMEKTGDYFRVTGEILSVLGGVYFFFRGIQYFLQRRPSMKTLFVDSYSEMLFFLQSLFMLATVVLYFSHLKEYVASMVFSLALGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYIVFLFGFSTAVVTLIEDGKNDSLPSESTSHRWRGPACRPPDSSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGYTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSSRVSGRHWKNFALVPLLREASARDRQSAQPEEVYLRQFSGSLKPEDAEVFKSPAASGEK TT50OG3 TT Clinical trial TT50OG3 FM mRNA target TTRV8K7 ID TTRV8K7 TTRV8K7 TN Trypanosoma Ribonucleotide reductase R2 (Trypano RNR2) TTRV8K7 UP O15910 TTRV8K7 UC RIR2_TRYBB TTRV8K7 BC CH/CH(2) oxidoreductase TTRV8K7 SN Ribonucleotide reductase R2 subunit; RNR2 TTRV8K7 GN Trypano RNR2 TTRV8K7 FC Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. TTRV8K7 SQ MPPKSHKCSRKEGEVEEPLLTENPDRYVIFPIKYPDIWQKYKEAESSIWTVEEIDLGNDMTDWEKLDDGERHFIKHVLAFFAASDGIVLENLAERFMCEVQVPEVRCFYGFQIAMENIHSETYSVLIDTYVVDPDEKQRLLHAIRTIPCIEKKAKWAIEWIGSQTSFPTRLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYEKYIVNKLPRDRVLEIICNAVSIEREFICDALPVRLIGMNSQLMTQYIEFVADRLLVSLGYDRHYNSKNPFDFMDMISLQGKTNFFEKKVGEYQKAGVMSSERSSKVFSLDADF TTRV8K7 TT Literature-reported TT63WSF ID TT63WSF TT63WSF TN Tumor necrosis factor receptor type II (TNF-R2) TT63WSF UP P20333 TT63WSF UC TNR1B_HUMAN TT63WSF SN p80 TNF-alpha receptor; p75; Tumor necrosis factor receptor superfamily member 1B; Tumor necrosis factor receptor 2; TNFR2; TNFR-II; TNFBR; TNF-RII; TNF-R2; Etanercept; CD120b TT63WSF GN TNFRSF1B TT63WSF FC Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity. TT63WSF PD 3ALQ; 1CA9 TT63WSF SQ MAPVAVWAALAVGLELWAAAHALPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWVPECLSCGSRCSSDQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSDVVCKPCAPGTFSNTTSSTDICRPHQICNVVAIPGNASMDAVCTSTSPTRSMAPGAVHLPQPVSTRSQHTQPTPEPSTAPSTSFLLPMGPSPPAEGSTGDFALPVGLIVGVTALGLLIIGVVNCVIMTQVKKKPLCLQREAKVPHLPADKARGTQGPEQQHLLITAPSSSSSSLESSASALDRRAPTRNQPQAPGVEASGAGEARASTGSSDSSPGGHGTQVNVTCIVNVCSSSDHSSQCSSQASSTMGDTDSSPSESPKDEQVPFSKEECAFRSQLETPETLLGSTEEKPLPLGVPDAGMKPS TT63WSF TT Literature-reported TT63WSF FM Transmembrane protein TTX4UE9 ID TTX4UE9 TTX4UE9 TN Tumor suppressor p53-binding protein 1 (TP53BP1) TTX4UE9 UP Q12888 TTX4UE9 UC TP53B_HUMAN TTX4UE9 SN p53BP1; p53-binding protein 1; TP53-binding protein 1; 53BP1 TTX4UE9 GN TP53BP1 TTX4UE9 FC Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites. Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites. Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs. Participates to the repair and the orientation of the broken DNA ends during CSR. In contrast, it is not required for classic NHEJ and V(D)J recombination. Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1. Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis. TTX4UE9 PD 6IUA; 6IU7; 6CO2; 6CO1; 5ZCJ TTX4UE9 SQ MDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEDDSGSHFSMLSRHLPNLQTHKENPVLDVVSNPEQTAGEERGDGNSGFNEHLKENKVADPVDSSNLDTCGSISQVIEQLPQPNRTSSVLGMSVESAPAVEEEKGEELEQKEKEKEEDTSGNTTHSLGAEDTASSQLGFGVLELSQSQDVEENTVPYEVDKEQLQSVTTNSGYTRLSDVDANTAIKHEEQSNEDIPIAEQSSKDIPVTAQPSKDVHVVKEQNPPPARSEDMPFSPKASVAAMEAKEQLSAQELMESGLQIQKSPEPEVLSTQEDLFDQSNKTVSSDGCSTPSREEGGCSLASTPATTLHLLQLSGQRSLVQDSLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQEGRQDKPMDTSVLSEEGGEPFQKKLQSGEPVELENPPLLPESTVSPQASTPISQSTPVFPPGSLPIPSQPQFSHDIFIPSPSLEEQSNDGKKDGDMHSSSLTVECSKTSEIEPKNSPEDLGLSLTGDSCKLMLSTSEYSQSPKMESLSSHRIDEDGENTQIEDTEPMSPVLNSKFVPAENDSILMNPAQDGEVQLSQNDDKTKGDDTDTRDDISILATGCKGREETVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMEIKEHHPEEGSSGSEVEEIPETPCESQGEELKEENMESVPLHLSLTETQSQGLCLQKEMPKKECSEAMEVETSVISIDSPQKLAILDQELEHKEQEAWEEATSEDSSVVIVDVKEPSPRVDVSCEPLEGVEKCSDSQSWEDIAPEIEPCAENRLDTKEEKSVEYEGDLKSGTAETEPVEQDSSQPSLPLVRADDPLRLDQELQQPQTQEKTSNSLTEDSKMANAKQLSSDAEAQKLGKPSAHASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVMSESMVETHDPILGSGKGDSGAAPDVDDKLCLRMKLVSPETEASEESLQFNLEKPATGERKNGSTAVAESVASPQKTMSVLSCICEARQENEARSEDPPTTPIRGNLLHFPSSQGEEEKEKLEGDHTIRQSQQPMKPISPVKDPVSPASQKMVIQGPSSPQGEAMVTDVLEDQKEGRSTNKENPSKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEFDMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSLHRTSSGTSLSAMHSSGSSGKGAGPLRGKTSGTEPADFALPSSRGGPGKLSPRKGVSQTGTPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETAVPGPLGIEDISPNLSPDDKSFSRVVPRVPDSTRRTDVGAGALRRSDSPEIPFQAAAGPSDGLDASSPGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNVSSPATPTASSSSSTTPTRKITESPRASMGVLSGKRKLITSEEERSPAKRGRKSATVKPGAVGAGEFVSPCESGDNTGEPSALEEQRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLPDGPTGSSEEEEEFLEIPPFNKQYTESQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH TTX4UE9 TT Literature-reported TTL4FMB ID TTL4FMB TTL4FMB TN TWIK-related acid-sensitive potassium channel 3 (TASK3) TTL4FMB UP Q9NPC2 TTL4FMB UC KCNK9_HUMAN TTL4FMB SN Two pore potassium channel KT3.2; TWIK-related acid-sensitive K+ channel 3; KCNK9; Acid-sensitive potassium channel protein TASK-3 TTL4FMB GN KCNK9 TTL4FMB FC pH-dependent, voltage-insensitive, background potassium channel protein. TTL4FMB PD 6GHP; 4FR3; 3UX0; 3SPR; 3SP5 TTL4FMB SQ MKRQNVRTLSLIVCTFTYLLVGAAVFDALESDHEMREEEKLKAEEIRIKGKYNISSEDYRQLELVILQSEPHRAGVQWKFAGSFYFAITVITTIGYGHAAPGTDAGKAFCMFYAVLGIPLTLVMFQSLGERMNTFVRYLLKRIKKCCGMRNTDVSMENMVTVGFFSCMGTLCIGAAAFSQCEEWSFFHAYYYCFITLTTIGFGDYVALQTKGALQKKPLYVAFSFMYILVGLTVIGAFLNLVVLRFLTMNSEDERRDAEERASLAGNRNSMVIHIPEEPRPSRPRYKADVPDLQSVCSCTCYRSQDYGGRSVAPQNSFSAKLAPHYFHSISYKIEEISPSTLKNSLFPSPISSISPGLHSFTDHQRLMKRRKSV TTL4FMB TT Literature-reported TTZWC8B ID TTZWC8B TTZWC8B TN Two pore calcium channel protein 2 (TPC2) TTZWC8B UP Q8NHX9 TTZWC8B UC TPC2_HUMAN TTZWC8B SN Voltage-dependent calcium channel protein TPC2; TPC2 TTZWC8B GN TPCN2 TTZWC8B FC Nicotinic acid adenine dinucleotide phosphate (NAADP) receptor that may function as one of the major voltage-gated Ca(2+) channels (VDCC) across the lysosomal membrane. May be involved in smooth muscle contraction. TTZWC8B PD 6NQ2; 6NQ1; 6NQ0 TTZWC8B SQ MAEPQAESEPLLGGARGGGGDWPAGLTTYRSIQVGPGAAARWDLCIDQAVVFIEDAIQYRSINHRVDASSMWLYRRYYSNVCQRTLSFTIFLILFLAFIETPSSLTSTADVRYRAAPWEPPCGLTESVEVLCLLVFAADLSVKGYLFGWAHFQKNLWLLGYLVVLVVSLVDWTVSLSLVCHEPLRIRRLLRPFFLLQNSSMMKKTLKCIRWSLPEMASVGLLLAIHLCLFTMFGMLLFAGGKQDDGQDRERLTYFQNLPESLTSLLVLLTTANNPDVMIPAYSKNRAYAIFFIVFTVIGSLFLMNLLTAIIYSQFRGYLMKSLQTSLFRRRLGTRAAFEVLSSMVGEGGAFPQAVGVKPQNLLQVLQKVQLDSSHKQAMMEKVRSYGSVLLSAEEFQKLFNELDRSVVKEHPPRPEYQSPFLQSAQFLFGHYYFDYLGNLIALANLVSICVFLVLDADVLPAERDDFILGILNCVFIVYYLLEMLLKVFALGLRGYLSYPSNVFDGLLTVVLLVLEISTLAVYRLPHPGWRPEMVGLLSLWDMTRMLNMLIVFRFLRIIPSMKLMAVVASTVLGLVQNMRAFGGILVVVYYVFAIIGINLFRGVIVALPGNSSLAPANGSAPCGSFEQLEYWANNFDDFAAALVTLWNLMVVNNWQVFLDAYRRYSGPWSKIYFVLWWLVSSVIWVNLFLALILENFLHKWDPRSHLQPLAGTPEATYQMTVELLFRDILEEPGEDELTERLSQHPHLWLCR TTZWC8B TT Literature-reported TT7YMXZ ID TT7YMXZ TT7YMXZ TN Tyrosine-protein kinase Srms (SRMS) TT7YMXZ UP Q9H3Y6 TT7YMXZ UC SRMS_HUMAN TT7YMXZ SN C20orf148 TT7YMXZ GN SRMS TT7YMXZ FC Non-receptor tyrosine-protein kinase which phosphorylates DOK1 on tyrosine residues. Also phosphorylates KHDRBS1/SAM68 and VIM on tyrosine residues. Phosphorylation of KHDRBS1 is EGF-dependent. TT7YMXZ EC EC 2.7.10.2 TT7YMXZ SQ MEPFLRRRLAFLSFFWDKIWPAGGEPDHGTPGSLDPNTDPVPTLPAEPCSPFPQLFLALYDFTARCGGELSVRRGDRLCALEEGGGYIFARRLSGQPSAGLVPITHVAKASPETLSDQPWYFSGVSRTQAQQLLLSPPNEPGAFLIRPSESSLGGYSLSVRAQAKVCHYRVSMAADGSLYLQKGRLFPGLEELLTYYKANWKLIQNPLLQPCMPQKAPRQDVWERPHSEFALGRKLGEGYFGEVWEGLWLGSLPVAIKVIKSANMKLTDLAKEIQTLKGLRHERLIRLHAVCSGGEPVYIVTELMRKGNLQAFLGTPEGRALRLPPLLGFACQVAEGMSYLEEQRVVHRDLAARNVLVDDGLACKVADFGLARLLKDDIYSPSSSSKIPVKWTAPEAANYRVFSQKSDVWSFGVLLHEVFTYGQCPYEGMTNHETLQQIMRGYRLPRPAACPAEVYVLMLECWRSSPEERPSFATLREKLHAIHRCHP TT7YMXZ TT Literature-reported TTEJA2R ID TTEJA2R TTEJA2R TN U3 snoRNP protein IMP3 (IMP3) TTEJA2R UP Q9NV31 TTEJA2R UC IMP3_HUMAN TTEJA2R SN U3 small nucleolar ribonucleoprotein protein IMP3; MRPS4; C15orf12; BRMS2 TTEJA2R GN IMP3 TTEJA2R FC Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing. TTEJA2R PD 2CQJ TTEJA2R SQ MVRKLKFHEQKLLKQVDFLNWEVTDHNLHELRVLRRYRLQRREDYTRYNQLSRAVRELARRLRDLPERDQFRVRASAALLDKLYALGLVPTRGSLELCDFVTASSFCRRRLPTVLLKLRMAQHLQAAVAFVEQGHVRVGPDVVTDPAFLVTRSMEDFVTWVDSSKIKRHVLEYNEERDDFDLEA TTEJA2R TT Literature-reported TT9TQRP ID TT9TQRP TT9TQRP TN Uridine phosphorylase (UPP) TT9TQRP UP Q16831; O95045 TT9TQRP UC UPP1_HUMAN; UPP2_HUMAN TT9TQRP BC Pentosyltransferase TT9TQRP SN UrdPase; UPase TT9TQRP GN UPP1; UPP2 TT9TQRP FC Catalyzes the reversible phosphorylytic cleavage ofuridine and deoxyuridine to uracil and ribose- or deoxyribose-1- phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. TT9TQRP SQ MAATGANAEKAESHNDCPVRLLNPNIAKMKEDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCPGRDYPNICAGTDRYAMYKVGPVLSVSHGMGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQELLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKKKLSKA TT9TQRP TT Literature-reported TTNOSTX ID TTNOSTX TTNOSTX TN Urokinase plasminogen receptor (PLAUR) TTNOSTX UP Q03405 TTNOSTX UC UPAR_HUMAN TTNOSTX SN UPAR; U-PAR; Monocyte activation antigen Mo3; MO3 TTNOSTX GN PLAUR TTNOSTX FC Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form. TTNOSTX PD 4QTI; 4K24; 3U74; 3U73; 3BT2 TTNOSTX SQ MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTEVVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNGFHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLWT TTNOSTX TT Literature-reported TTERU0T ID TTERU0T TTERU0T TN Urotensin II (UTS2) TTERU0T UP O95399 TTERU0T UC UTS2_HUMAN TTERU0T SN Urotensin-II; UTS2; UII; U-II; HU-II TTERU0T GN UTS2 TTERU0T FC Highly potent vasoconstrictor. TTERU0T PD 6HVC; 6HVB TTERU0T SQ MYKLASCCLLFIGFLNPLLSLPLLDSREISFQLSAPHEDARLTPEELERASLLQILPEMLGAERGDILRKADSSTNIFNPRGNLRKFQDFSGQDPNILLSHLLARIWKPYKKRETPDCFWKYCV TTERU0T TT Literature-reported TTONPVW ID TTONPVW TTONPVW TN Uteroglobin (SCGB1A1) TTONPVW UP P11684 TTONPVW UC UTER_HUMAN TTONPVW BC Secretoglobin family TTONPVW SN Urine protein 1; Urinary protein 1; UP-1; Secretoglobin family 1A member 1; SCGB1A1; Clara cells 10 kDa secretory protein; Clara cell phospholipid-binding protein; CCPBP; CC10 TTONPVW GN SCGB1A1 TTONPVW FC Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2. TTONPVW SQ MKLAVTLTLVTLALCCSSASAEICPSFQRVIETLLMDTPSSYEAAMELFSPDQDMREAGAQLKKLVDTLPQKPRESIIKLMEKIAQSSLCN TTONPVW TT Literature-reported TTXLCFO ID TTXLCFO TTXLCFO TN Vascular endothelial cadherin (CDH5) TTXLCFO UP P33151 TTXLCFO UC CADH5_HUMAN TTXLCFO BC Cadherin protein TTXLCFO SN VE-cadherin; VE-cad; Cadherin-5; CD144 antigen; CD144; 7B4 antigen TTXLCFO GN CDH5 TTXLCFO FC Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. This cadherin may play a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. It associates with alpha-catenin forming a link to the cytoskeleton. Acts in concert with KRIT1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for activation of PRKCZ and for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction. TTXLCFO SQ MQRLMMLLATSGACLGLLAVAAVAAAGANPAQRDTHSLLPTHRRQKRDWIWNQMHIDEEKNTSLPHHVGKIKSSVSRKNAKYLLKGEYVGKVFRVDAETGDVFAIERLDRENISEYHLTAVIVDKDTGENLETPSSFTIKVHDVNDNWPVFTHRLFNASVPESSAVGTSVISVTAVDADDPTVGDHASVMYQILKGKEYFAIDNSGRIITITKSLDREKQARYEIVVEARDAQGLRGDSGTATVLVTLQDINDNFPFFTQTKYTFVVPEDTRVGTSVGSLFVEDPDEPQNRMTKYSILRGDYQDAFTIETNPAHNEGIIKPMKPLDYEYIQQYSFIVEATDPTIDLRYMSPPAGNRAQVIINITDVDEPPIFQQPFYHFQLKENQKKPLIGTVLAMDPDAARHSIGYSIRRTSDKGQFFRVTKKGDIYNEKELDREVYPWYNLTVEAKELDSTGTPTGKESIVQVHIEVLDENDNAPEFAKPYQPKVCENAVHGQLVLQISAIDKDITPRNVKFKFILNTENNFTLTDNHDNTANITVKYGQFDREHTKVHFLPVVISDNGMPSRTGTSTLTVAVCKCNEQGEFTFCEDMAAQVGVSIQAVVAILLCILTITVITLLIFLRRRLRKQARAHGKSVPEIHEQLVTYDEEGGGEMDTTSYDVSVLNSVRRGGAKPPRPALDARPSLYAQVQKPPRHAPGAHGGPGEMAAMIEVKKDEADHDGDGPPYDTLHIYGYEGSESIAESLSSLGTDSSDSDVDYDFLNDWGPRFKMLAELYGSDPREELLY TTXLCFO TT Literature-reported TTXLCFO FM Cadherin TTGTWLF ID TTGTWLF TTGTWLF TN Vasoactive intestinal polypeptide (VIP) TTGTWLF UP P01282 TTGTWLF UC VIP_HUMAN TTGTWLF SN Vasoactive intestinal peptide; VIP peptides; Peptide histidine valine 42; Intestinal peptide PHV-42 TTGTWLF GN VIP TTGTWLF FC VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder. TTGTWLF PD 2RRI; 2RRH TTGTWLF SQ MDTRNKAQLLVLLTLLSVLFSQTSAWPLYRAPSALRLGDRIPFEGANEPDQVSLKEDIDMLQNALAENDTPYYDVSRNARHADGVFTSDFSKLLGQLSAKKYLESLMGKRVSSNISEDPVPVKRHSDAVFTDNYTRLRKQMAVKKYLNSILNGKRSSEGESPDFPEELEK TTGTWLF TT Literature-reported TTAD1O8 ID TTAD1O8 TTAD1O8 TN V-erbA-related protein 1 (NR1D1) TTAD1O8 UP P20393 TTAD1O8 UC NR1D1_HUMAN TTAD1O8 SN THRAL; Rev-erbA-alpha; Nuclear receptor subfamily 1 group D member 1; HREV; EAR1; EAR-1 TTAD1O8 GN NR1D1 TTAD1O8 FC Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core clock components ARTNL/BMAL1, CLOCK and CRY1. Also regulates genes involved in metabolic functions, including lipid and bile acid metabolism, adipogenesis, gluconeogenesis and the macrophage inflammatory response. Acts as a receptor for heme which stimulates its interaction with the NCOR1/HDAC3 corepressor complex, enhancing transcriptional repression. Recognizes two classes of DNA response elements within the promoter of its target genes and can bind to DNA as either monomers or homodimers, depending on the nature of the response element. Binds as a monomer to a response element composed of the consensus half-site motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence (RevRE), or as a homodimer to a direct repeat of the core motif spaced by two nucleotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and regulates the levels of its ligand heme by repressing the expression of PPARGC1A, a potent inducer of heme synthesis. Regulates lipid metabolism by repressing the expression of APOC3 and by influencing the activity of sterol response element binding proteins (SREBPs); represses INSIG2 which interferes with the proteolytic activation of SREBPs which in turn govern the rhythmic expression of enzymes with key functions in sterol and fatty acid synthesis. Regulates gluconeogenesis via repression of G6PC and PEPCK and adipocyte differentiation via repression of PPARG. Regulates glucagon release in pancreatic alpha-cells via the AMPK-NAMPT-SIRT1 pathway and the proliferation, glucose-induced insulin secretion and expression of key lipogenic genes in pancreatic-beta cells. Positively regulates bile acid synthesis by increasing hepatic expression of CYP7A1 via repression of NR0B2 and NFIL3 which are negative regulators of CYP7A1. Modulates skeletal muscle oxidative capacity by regulating mitochondrial biogenesis and autophagy; controls mitochondrial biogenesis and respiration by interfering with the STK11-PRKAA1/2-SIRT1-PPARGC1A signaling pathway. Represses the expression of SERPINE1/PAI1, an important modulator of cardiovascular disease and the expression of inflammatory cytokines and chemokines in macrophages. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). Plays a role in the circadian regulation of body temperature and negatively regulates thermogenic transcriptional programs in brown adipose tissue (BAT); imposes a circadian oscillation in BAT activity, increasing body temperature when awake and depressing thermogenesis during sleep. In concert with NR2E3, regulates transcriptional networks critical for photoreceptor development and function. In addition to its activity as a repressor, can also act as a transcriptional activator. In the ovarian granulosa cells acts as a transcriptional activator of STAR which plays a role in steroid biosynthesis. In collaboration with SP1, activates GJA1 transcription in a heme-independent manner. Represses the transcription of CYP2B10, CYP4A10 and CYP4A14 (By similarity). Represses the transcription of CES2 (By similarity). Represses and regulates the circadian expression of TSHB in a NCOR1-dependent manner (By similarity). Negatively regulates the protein stability of NR3C1 and influences the time-dependent subcellular distribution of NR3C1, thereby affecting its transcriptional regulatory activity (By similarity). Plays a critical role in the circadian control of neutrophilic inflammation in the lung; under resting, non-stress conditions, acts as a rhythmic repressor to limit inflammatory activity whereas in the presence of inflammatory triggers undergoes ubiquitin-mediated degradation thereby relieving inhibition of the inflammatory response (By similarity). Plays a key role in the circadian regulation of microglial activation and neuroinflammation; suppresses microglial activation through the NF-kappaB pathway in the central nervous system (By similarity). Plays a role in the regulation of the diurnal rhythms of lipid and protein metabolism in the skeletal muscle via transcriptional repression of genes controlling lipid and amino acid metabolism in the muscle (By similarity). TTAD1O8 PD 3N00; 1HLZ; 1GA5; 1EF6; 1A6Y TTAD1O8 SQ MTTLDSNNNTGGVITYIGSSGSSPSRTSPESLYSDNSNGSFQSLTQGCPTYFPPSPTGSLTQDPARSFGSIPPSLSDDGSPSSSSSSSSSSSSFYNGSPPGSLQVAMEDSSRVSPSKSTSNITKLNGMVLLCKVCGDVASGFHYGVHACEGCKGFFRRSIQQNIQYKRCLKNENCSIVRINRNRCQQCRFKKCLSVGMSRDAVRFGRIPKREKQRMLAEMQSAMNLANNQLSSQCPLETSPTQHPTPGPMGPSPPPAPVPSPLVGFSQFPQQLTPPRSPSPEPTVEDVISQVARAHREIFTYAHDKLGSSPGNFNANHASGSPPATTPHRWENQGCPPAPNDNNTLAAQRHNEALNGLRQAPSSYPPTWPPGPAHHSCHQSNSNGHRLCPTHVYAAPEGKAPANSPRQGNSKNVLLACPMNMYPHGRSGRTVQEIWEDFSMSFTPAVREVVEFAKHIPGFRDLSQHDQVTLLKAGTFEVLMVRFASLFNVKDQTVMFLSRTTYSLQELGAMGMGDLLSAMFDFSEKLNSLALTEEELGLFTAVVLVSADRSGMENSASVEQLQETLLRALRALVLKNRPLETSRFTKLLLKLPDLRTLNNMHSEKLLSFRVDAQ TTAD1O8 TT Preclinical TTFSUIA ID TTFSUIA TTFSUIA TN Vesicular H(+)/Aspartate-glutamate cotransporter (HP59) TTFSUIA UP Q9NRA2 TTFSUIA UC S17A5_HUMAN TTFSUIA BC Major facilitator superfamily TTFSUIA SN Solute carrier family 17 member 5; Sodium/sialic acid cotransporter; SLC17A5; Membrane glycoprotein HP59; AST TTFSUIA GN SLC17A5 TTFSUIA FC Transports glucuronic acid and free sialic acid out of the lysosome after it is cleaved from sialoglycoconjugates undergoing degradation, this is required for normal CNS myelination. Mediates aspartate and glutamate membrane potential- dependent uptake into synaptic vesicles and synaptic-like microvesicles. Also functions as an electrogenic 2NO(3)(-)/H(+) cotransporter in the plasma membrane of salivary gland acinar cells, mediating the physiological nitrate efflux, 25% of the circulating nitrate ions is typically removed and secreted in saliva. TTFSUIA SQ MRSPVRDLARNDGEESTDRTPLLPGAPRAEAAPVCCSARYNLAILAFFGFFIVYALRVNLSVALVDMVDSNTTLEDNRTSKACPEHSAPIKVHHNQTGKKYQWDAETQGWILGSFFYGYIITQIPGGYVASKIGGKMLLGFGILGTAVLTLFTPIAADLGVGPLIVLRALEGLGEGVTFPAMHAMWSSWAPPLERSKLLSISYAGAQLGTVISLPLSGIICYYMNWTYVFYFFGTIGIFWFLLWIWLVSDTPQKHKRISHYEKEYILSSLRNQLSSQKSVPWVPILKSLPLWAIVVAHFSYNWTFYTLLTLLPTYMKEILRFNVQENGFLSSLPYLGSWLCMILSGQAADNLRAKWNFSTLCVRRIFSLIGMIGPAVFLVAAGFIGCDYSLAVAFLTISTTLGGFCSSGFSINHLDIAPSYAGILLGITNTFATIPGMVGPVIAKSLTPDNTVGEWQTVFYIAAAINVFGAIFFTLFAKGEVQNWALNDHHGHRH TTFSUIA TT Literature-reported TTVFR2S ID TTVFR2S TTVFR2S TN Vibrio TCP pilus virulence regulatory protein (Vibrio tcpN) TTVFR2S UP P0C6D6 TTVFR2S UC TCPN_VIBCH TTVFR2S GN Vibrio tcpN TTVFR2S FC Probable regulatory protein for the tcp operon. TTVFR2S SQ MIGKKSFQTNVYRMSKFDTYIFNNLYINDYKMFWIDSGIAKLIDKNCLVSYEINSSSIILLKKNSIQRFSLTSLSDENINVSVITISDSFIRSLKSYILGDLMIRNLYSENKDLLLWNCEHNDIAVLSEVVNGFREINYSDEFLKVFFSGFFSKVEKKYNSIFITDDLDAMEKISCLVKSDITRNWRWADICGELRTNRMILKKELESRGVKFRELINSIRISYSISLMKTGEFKIKQIAYQSGFASVSYFSTVFKSTMNVAPSEYLFMLTGVAEK TTVFR2S TT Preclinical TTVBE0F ID TTVBE0F TTVBE0F TN Virus Genome polyprotein (Viru POL) TTVBE0F UP P23008 TTVBE0F UC POLG_HRV1A TTVBE0F SN Protein VP1; Genome polyprotein of Human rhinovirus 1A TTVBE0F GN Viru POL TTVBE0F FC RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to- tail interaction called interface-I.Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomicreplication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated. TTVBE0F PD 2HWF; 2HWE; 2HWD; 1R1A; 1AYN TTVBE0F SQ MGAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASSGASRLDFSQDPSKFTDPVKDVLEKGIPTLQSPSVEACGYSDRIMQITRGDSTITSQDVANAVVGYGVWPHYLTPQDATAIDKPTQPDTSSNRFYTLESKHWNGSSKGWWWKLPDALKDMGIFGENMYYHFLGRSGYTVHVQCNASKFHQGTLLVAMIPEHQLASAKHGSVTAGYKLTHPGEAGRDVSQERDASLRQPSDDSWLNFDGTLLGNLLIFPHQFINLRSNNSATLIVPYVNAVPMDSMLRHNNWSLVIIPISPLRSETTSSNIVPITVSISPMCAEFSGARAKNIKQGLPVYITPGSGQFMTTDDMQSPCALPWYHPTKEISIPGEVKNLIEMCQVDTLIPVNNVGNNVGNVSMYTVQLGNQTGMAQKVFSIKVDITSQPLATTLIGEIASYYTHWTGSLRFSFMFCGTANTTLKLLLAYTPPGIDEPTTRKDAMLGTHVVWDVGLQSTISLVVPWVSASHFRLTADNKYSMAGYITCWYQTNLVVPPSTPQTADMLCFVSACKDFCLRMARDTDLHIQSGPIEQNPVENYIDEVLNEVLVVPNIKESHHTTSNSAPLLDAAETGHTSNVQPEDAIETRYVITSQTRDEMSIESFLGRSGCVHISRIKVDYTDYNGQDINFTKWKITLQEMAQIRRKFELFTYVRFDSEITLVPCIAGRGDDIGHIVMQYMYVPPGAPIPSKRNDFSWQSGTNMSIFWQHGQPFPRFSLPFLSIASAYYMFYDGYDGDNTSSKYGSVVTNDMGTICSRIVTEKQKHSVVITTHIYHKAKHTKAWCPRPPRAVPYTHSHVTNYMPETGDVTTAIVRRNTITTAGPSDLYVHVGNLIYRNLHLFNSEMHDSILISYSSDLIIYRTNTIGDDYIPNCNCTEATYYCRHKNRYYPIKVTPHDWYEIQESEYYPKHIQYNLLIGEGPCEPGDCGGKLLCRHGVIGIITAGGEGHVAFIDLRQFHCAEEQGITDYIHMLGEAFGNGFVDSVKEQINAINPINNISKKVIKWLLRIISAMVIIIRNSSDPQTIIATLTLIGCNGSPWRFLKEKFCKWTQLTYIHKESDSWLKKFTEMCNAARGLEWIGNKISKFIDWMKSMLPQAQLKVKYLNEIKKLSLLEKQIENLRAADSATQEKIKCEIDTLHDLSCKFLPLYAHEAKRIKVLYNKCSNIIKQRKRSEPVAVMIHGPPGTGKSITTNFLARMITNESDVYSLPPDPKYFDGYDNQSVVIMDDIMQNPDGEDMTLFCQMVSSVTFIPPMADLPDKGKPFDSRFILCSTNHSLLAPPTISSLPAMNRRFFFDLDIVVHDNYKDTQGKLDVSKAFRPCNVNTKIGNAKCCPFVCGKAVXFKDRSTCSTYTLAQVYNHILEEDKRRRQVVDVMSAIFQGPISLDXPPPPAIXDLLQSVRTPEVIKYCQDNKWVIPAECQVERDLNIANSIIAIIANIISIAGIIFVIYKLFCSLQGPYSGEPKPKTKVPERRVVAQGPEEEFGRSILKNNTCVITTGNGKFTGLGIHDRILIIPTHADPGREVQVNGVHTKVLDSYDLYNRDGVKLEITVIQLDRNEKFRDIRKYIPETEDDYPECNLALSANQDEPTIIKVGDVVSYGNILLSGNQTARMLKYNYPTKSGYCGGVLYKIGQILGIHVGGNGRDGFSAMLLRSYFTDTQGQIKVNKHATECGLPTIHTPSKTKLQPSVFYDVFPGSKEPAVLTDNDPRLEVNFKEALFSKYKGNVECNLNEHMEIAIAHYSAQLMTLDIDSRPIALEDSVFGIEGLEALDLNTSAGFPYVTMGIKKRDLINNKTKDISRLKEALDKYGVDLPMITFLKDELRKKEKISTGKTRVIEASSINDTILFRTTFGNLFSKFHLNPGVVTGSAVGCDPETFWSKIPVMLDGDCIMAFDYTNYDGSIHPVWFQALKKVLENLSFQSNLIDRLCYSKHLFKSTYYEVAGGVPSGCSGTSIFNTMINNIIIRTLVLDAYKNIDLDKLKIIAYGDDVIFSYKYTLDMEAIANEGKKYGLTITPADKSNEFKKLDYSNVTFLKRGFKQDERHTFLIHPTFPVEEIHESIRWTKKPSQMQEHVLSLCHLMWHNGRKVYEDFSSKIRSVSAGRALYIPPYDLLKHEWYEKF TTVBE0F TT Literature-reported TTU9LAT ID TTU9LAT TTU9LAT TN Virus Papain-like cysteine protease (Viru pcp) TTU9LAT UP Q9WJB2 TTU9LAT UC RPOA_PRRSR TTU9LAT BC Arteriviridae polyprotein family TTU9LAT SN rep of Porcine reproductive and respiratory syndrome virus; Pol; ORF1ab polyprotein of Porcine reproductive and respiratory syndrome virus; Nsp8; Nsp5-6-7; Nsp3; Nsp12; Nsp11; Non-structural protein 12; Hel; CP of Porcine reproductive and respiratory syndrome virus; 3CLSP TTU9LAT GN Viru pcp TTU9LAT FC The helicase chain, which contains a zinc finger structure,displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. TTU9LAT SQ MSGILDRCTCTPNARVFMAEGQVYCTRCLSARSLLPLNLQVSELGVLGLFYRPEEPLRWTLPRAFPTVECSPAGACWLSAIFPIARMTSGNLNFQQRMVRVAAELYRAGQLTPAVLKALQVYERGCRWYPIVGPVPGVAVFANSLHVSDKPFPGATHVLTNLPLPQRPKPEDFCPFECAMATVYDIGHDAVMYVAERKVSWAPRGGDEVKFEAVPGELKLIANRLRTSFPPHHTVDMSKFAFTAPGCGVSMRVERQHGCLPADTVPEGNCWWSLFDLLPLEVQNKEIRHANQFGYQTKHGVSGKYLQRRLQVNGLRAVTDLNGPIVVQYFSVKESWIRHLKLAGEPSYSGFEDLLRIRVEPNTSPLADKEEKIFRFGSHKWYGAGKRARKARSCATATVAGRALSVRETRQAKEHEVAGANKAEHLKHYSPPAEGNCGWHCISAIANRMVNSKFETTLPERVRPPDDWATDEDLVNAIQILRLPAALDRNGACTSAKYVLKLEGEHWTVTVTPGMSPSLLPLECVQGCCGHKGGLGSPDAVEVSGFDPACLDRLAEVMHLPSSAIPAALAEMSGDSDRSASPVTTVWTVSQFFARHSGGNHPDQVRLGKIISLCQVIEDCCCSQNKTNRVTPEEVAAKIDLYLRGATNLEECLARLEKARPPRVIDTSFDWDVVLPGVEAATQTIKLPQVNQCRALVPVVTQKSLDNNSVPLTAFSLANYYYRAQGDEVRHRERLTAVLSKLEKVVREEYGLMPTEPGPRPTLPRGLDELKDQMEEDLLKLANAQTTSDMMAWAVEQVDLKTWVKNYPRWTPPPPPPKVQPRKTKPVKSLPERKPVPAPRRKVGSDCGSPVSLGGDVPNSWEDLAVSSPFDLPTPPEPATPSSELVIVSSPQCIFRPATPLSEPAPIPAPRGTVSRPVTPLSEPIPVPAPRRKFQQVKRLSSAAAIPPYQDEPLDLSASSQTEYEASPPAPPQSGGVLGVEGHEAEETLSEISDMSGNIKPASVSSSSSLSSVRITRPKYSAQAIIDSGGPCSGHLQEVKETCLSVMREACDATKLDDPATQEWLSRMWDRVDMLTWRNTSVYQAICTLDGRLKFLPKMILETPPPYPCEFVMMPHTPAPSVGAESDLTIGSVATEDVPRILEKIENVGEMANQGPLAFSEDKPVDDQLVNDPRISSRRPDESTSAPSAGTGGAGSFTDLPPSDGADADGGGPFRTVKRKAERLFDQLSRQVFDLVSHLPVFFSRLFYPGGGYSPGDWGFAAFTLLCLFLCYSYPAFGIAPLLGVFSGSSRRVRMGVFGCWLAFAVGLFKPVSDPVGAACEFDSPECRNILHSFELLKPWDPVRSLVVGPVGLGLAILGRLLGGARCIWHFLLRLGIVADCILAGAYVLSQGRCKKCWGSCIRTAPNEVAFNVFPFTRATRSSLIDLCDRFCAPKGMDPIFLATGWRGCWAGRSPIEQPSEKPIAFAQLDEKKITARTVVAQPYDPNQAVKCLRVLQSGGAMVAKAVPKVVKVSAVPFRAPFFPTGVKVDPDCRVVVDPDTFTAALRSGYSTTNLVLGVGDFAQLNGLKIRQISKPSGGGPHLMAALHVACSMALHMLAGIYVTAVGSCGTGTNDPWCANPFAVPGYGPGSLCTSRLCISQHGLTLPLTALVAGFGIQEIALVVLIFVSIGGMAHRLSCKADMLCVLLAIASYVWVPLTWLLCVFPCWLRCFSLHPLTILWLVFFLISVNMPSGILAMVLLVSLWLLGRYTNVAGLVTPYDIHHYTSGPRGVAALATAPDGTYLAAVRRAALTGRTMLFTPSQLGSLLEGAFRTRKPSLNTVNVIGSSMGSGGVFTIDGKVKCVTAAHVLTGNSARVSGVGFNQMLDFDVKGDFAIADCPNWQGAAPKTQFCTDGWTGRAYWLTSSGVEPGVIGKGFAFCFTACGDSGSPVITEAGELVGVHTGSNKQGGGIVTRPSGQFCNVAPIKLSELSEFFAGPKVPLGDVKVGSHIIKDISEVPSDLCALLAAKPELEGGLSTVQLLCVFFLLWRMMGHAWTPLVAVSFFILNEVLPAVLVRSVFSFGMFVLSWLTPWSAQVLMIRLLTAALNRNRWSLAFFSLGAVTGFVADLAATQGHPLQAVMNLSTYAFLPRMMVVTSPVPVITCGVVHLLAIILYLFKYRGPHHILVGDGVFSAAFFLRYFAEGKLREGVSQSCGMNHESLTGALAMRLNDEDLDFLMKWTDFKCFVSASNMRNAAGQFIEAAYAKALRVELAQLVQVDKVRGTLAKLEAFADTVAPQLSPGDIVVALGHTPVGSIFDLKVGSTKHTLQAIETRVLAGSKMTVARVVDPTPTPPPAPVPIPLPPKVLENGPNAWGDEDRLNKKKRRRMEALGIYVMGGKKYQKFWDKNSGDVFYEEVHNNTDEWECLRVGDPADFDPEKGTLCGHVTIENKAYHVYTSPSGKKFLVPVNPENGRVQWEAAKLSVEQALGMMNVDGELTAKELEKLKRIIDKLQGLTKEQCLNCLAASDLTRCGRGGLVVTETAVKIVKFHNRTFTLGPVNLKVASEVELKDAVEHNQHPVARPIDGGVVLLRSAVPSLIDVLISGADASPKLLAHHGPGNTGIDGTLWDFESEATKEEVALSAQIIQACDIRRGDAPEIGLPYKLYPVRGNPERVKGVLQNTRFGDIPYKTPSDTGSPVHAAACLTPNATPVTDGRSVLATTMPPGFELYVPTIPASVLDYLDSRPDCPKQLTEHGCEDAALKDLSKYDLSTQGFVLPGVLRLVRKYLFAHVGKCPPVHRPSTYPAKNSMAGINGNRFPTKDIQSVPEIDVLCAQAVRENWQTVTPCTLKKQYCGKKKTRTILGTNNFIALAHRAVLSGVTQGFMKKAFNSPIALGKNKFKELQTPVLGRCLEADLASCDRSTPAIVRWFAANLLYELACAEEHLPSYVLNCCHDLLVTQSGAVTKRGGLSSGDPITSVSNTIYSLVIYAQHMVLSYFKSGHPHGLLFLQDQLKFEDMLKVQPLIVYSDDLVLYAESPTMPNYHWWVEHLNLMLGFQTDPKKTAITDSPSFLGCRIINGRQLVPNRDRILAALAYHMKASNVSEYYASAAAILMDSCACLEYDPEWFEELVVGIAQCARKDGYSFPGTPFFMSMWEKLRSNYEGKKSRVCGYCGAPAPYATACGLDVCIYHTHFHQHCPVTIWCGHPAGSGSCSECKSPVGKGTSPLDEVLEQVPYKPPRTVIMHVEQGLTPLDPGRYQTRRGLVSVRRGIRGNEVGLPDGDYASTALLPTCKEINMVAVASNVLRSRFIIGPPGAGKTYWLLQQVQDGDVIYTPTHQTMLDMIRALGTCRFNVPAGTTLQFPVPSRTGPWVRILAGGWCPGKNSFLDEAAYCNHLDVLRLLSKTTLTCLGDFKQLHPVGFDSHCYVFDIMPQTQLKTIWRFGQNICDAIQPDYRDKLMSMVNTTRVTYVEKPVRYGQVLTPYHRDREDDAITIDSSQGATFDVVTLHLPTKDSLNRQRALVAITRARHAIFVYDPHRQLQGLFDLPAKGTPVNLAVHCDGQLIVLDRNNKECTVAQALGNGDKFRATDKRVVDSLRAICADLEGSSSPLPKVAHNLGFYFSPDLTQFAKLPVELAPHWPVVSTQNNEKWPDRLVASLRPIHKYSRACIGAGYMVGPSVFLGTPGVVSYYLTKFVKGGAQVLPETVFSTGRIEVDCREYLDDREREVAASLPHGFIGDVKGTTVGGCHHVTSRYLPRVLPKESVAVVGVSSPGKAAKALCTLTDVYLPDLEAYLHPETQSKCWKMMLDFKEVRLMVWKDKTAYFQLEGRYFTWYQLASYASYIRVPVNSTVYLDPCMGPALCNRRVVGSTHWGADLAVTPYDYGAKIILSSAYHGEMPPGYKILACAEFSLDDPVKYKHTWGFESDTAYLYEFTGNGEDWEDYNDAFRARQEGKIYKATATSLKFYFPPGPVIEPTLGLN TTU9LAT TT Literature-reported TTW5I7Q ID TTW5I7Q TTW5I7Q TN Virus Pre-glycoprotein GP complex (Viru GPC) TTW5I7Q UP P03540 TTW5I7Q UC GLYC_PIARV TTW5I7Q BC Arenaviridae GPC protein TTW5I7Q SN Pre-GP-C; GPC TTW5I7Q GN Viru GPC TTW5I7Q FC Glycoprotein G2 is a viral fusion protein. Membrane fusion is mediated by conformational changes induced upon acidification in the endosome (Potential). TTW5I7Q SQ MGQIVTLIQSIPEVLQEVFNVALIIVSVLCIVKGFVNLMRCGLFQLVTFLILSGRSCDSMMIDRRHNLTHVEFNLTRMFDNLPQSCSKNNTHHYYKGPSNTTWGIELTLTNTSIANETSGNFSNIGSLGYGNISNCDRTREAGHTLKWLLNELHFNVLHVTRHIGARCKTVEGAGVLIQYNLTVGDRGGEVGRHLIASLAQIIGDPKIAWVGKCFNNCSGDTCRLTNCEGGTHYNFLIIQNTTWENHCTYTPMATIRMALQRTAYSSVSRKLLGFFTWDLSDSSGQHVPGGYCLEQWAIIWAGIKCFDNTVMAKCNKDHNEEFCDTMRLFDFNQNAIKTLQLNVENSLNLFKKTINGLISDSLVIRNSLKQLAKIPYCNYTKFWYINDTITGRHSLPQCWLVHNGSYLNETHFKNDWLWESQNLYNEMLMKEYEERQGKTPLALTDICFWSLVFYTITVFLHIVGIPTHRHIIGDGCPKPHRITRNSLCSCGYYKYQRNLTNG TTW5I7Q TT Literature-reported TTEQU6A ID TTEQU6A TTEQU6A TN Virus Protein P16 (Viru GpS) TTEQU6A UP P27392 TTEQU6A UC VP16_BPPRD TTEQU6A SN XVI; Protein S; GpS TTEQU6A GN Viru GpS TTEQU6A FC protein of the infection vertex complex, which increases the vertex stability. Anchors the vertex structure to the viral membrane. Essential for viral infectivity. TTEQU6A PD 1W8X TTEQU6A SQ MDKKKLLYWVGGGLVLILIWLWFRNRPAAQVASNWEGPPYMTYNQPQAGSVTLPVAGYTSPSPTLPNRNRSCGCNPAVSAAMAQGADLASKLTDSITSQLNDYASSLNDYLASQAGV TTEQU6A TT Literature-reported TT6G10V ID TT6G10V TT6G10V TN Vitiligo-associated protein 1 (FBXO11) TT6G10V UP Q86XK2 TT6G10V UC FBX11_HUMAN TT6G10V SN Vitiligoassociated protein 1; VIT1; VIT-1; UG063H01; Protein arginine N-methyltransferase 9; PRMT9; Fbox only protein 11; FBX11; F-box only protein 11 TT6G10V GN FBXO11 TT6G10V FC The SCF(FBXO11) complex mediates ubiquitination and degradation of BCL6, thereby playing a role in the germinal center B-cells terminal differentiation toward memory B-cells and plasma cells. The SCF(FBXO11) complex also mediates ubiquitination and degradation of DTL, an important step for the regulation of TGF-beta signaling, cell migration and the timing of the cell-cycle progression and exit. Binds to and neddylates phosphorylated p53/TP53, inhibiting its transcriptional activity. SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53. Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. TT6G10V PD 5VMD TT6G10V SQ MNSVRAANRRPRRVSRPRPVQQQQQQPPQQPPPQPPQQQPPQQQPPPPPQQQQQQQPPPPPPPPPPLPQERNNVGERDDDVPADMVAEESGPGAQNSPYQLRRKTLLPKRTACPTKNSMEGASTSTTENFGHRAKRARVSGKSQDLSAAPAEQYLQEKLPDEVVLKIFSYLLEQDLCRAACVCKRFSELANDPILWKRLYMEVFEYTRPMMHPEPGKFYQINPEEYEHPNPWKESFQQLYKGAHVKPGFAEHFYSNPARYKGRENMLYYDTIEDALGGVQEAHFDGLIFVHSGIYTDEWIYIESPITMIGAAPGKVADKVIIENTRDSTFVFMEGSEDAYVGYMTIRFNPDDKSAQHHNAHHCLEITVNCSPIIDHCIIRSTCTVGSAVCVSGQGACPTIKHCNISDCENVGLYITDHAQGIYEDNEISNNALAGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRGQFIENKIYANNFAGVWITSNSDPTIRGNSIFNGNQGGVYIFGDGRGLIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQGVIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGCIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRGLLEENDIFRNAQAGVLISTNSHPILRKNRIFDGFAAGIEITNHATATLEGNQIFNNRFGGLFLASGVNVTMKDNKIMNNQDAIEKAVSRGQCLYKISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPCTLAGEPTHDTDTLYDSAPPIESNTLQHN TT6G10V TT Literature-reported TTL213V ID TTL213V TTL213V TN Voltage-gated A-type potassium channel (A-KC) TTL213V UP P22459; Q03721; Q9NSA2; Q9NZV8; Q9UK17 TTL213V UC KCNA4_HUMAN; KCNC4_HUMAN; KCND1_HUMAN; KCND2_HUMAN; KCND3_HUMAN TTL213V BC Voltage-gated ion channel TTL213V SN Potassium voltage-gated channel TTL213V GN KCNA4; KCNC4; KCND1; KCND2; KCND3 TTL213V FC Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND1/Kv4.1 and KCND2/Kv4.2 currents. Increases the presence of KCND2 at the cell surface. TTL213V SQ MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGSGGSGGGSHHHHQSRGACTSHDPQSSRGSRRRRRQRSEKKKAHYRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEDDHGDECSYTDLLPQDEGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLVMALSAGGHGGLLNDTSAPHLENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFITLGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMRELGLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCAKEEKCQGKGDDSETDKNNCSNAKAVETDV TTL213V TT Literature-reported TTJ0SO4 ID TTJ0SO4 TTJ0SO4 TN Voltage-gated calcium channel alpha Cav1.4 (CACNA1F) TTJ0SO4 UP O60840 TTJ0SO4 UC CAC1F_HUMAN TTJ0SO4 BC Voltage-gated ion channel TTJ0SO4 SN Voltage-gated calcium channel subunit alpha Cav1.4; Voltage-dependent L-type calcium channel subunit alpha-1F; CACNAF1 TTJ0SO4 GN CACNA1F TTJ0SO4 FC Isoform 1: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1F gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines. Activates at more negative voltages and does not undergo calcium-dependent inactivation (CDI), due to incoming calcium ions, during depolarization. TTJ0SO4 SQ MSESEGGKDTTPEPSPANGAGPGPEWGLCPGPPAVEGESSGASGLGTPKRRNQHSKHKTVAVASAQRSPRALFCLTLANPLRRSCISIVEWKPFDILILLTIFANCVALGVYIPFPEDDSNTANHNLEQVEYVFLVIFTVETVLKIVAYGLVLHPSAYIRNGWNLLDFIIVVVGLFSVLLEQGPGRPGDAPHTGGKPGGFDVKALRAFRVLRPLRLVSGVPSLHIVLNSIMKALVPLLHIALLVLFVIIIYAIIGLELFLGRMHKTCYFLGSDMEAEEDPSPCASSGSGRACTLNQTECRGRWPGPNGGITNFDNFFFAMLTVFQCVTMEGWTDVLYWMQDAMGYELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKQREKQQMEEDLRGYLDWITQAEELDMEDPSADDNLGSMAEEGRAGHRPQLAELTNRRRGRLRWFSHSTRSTHSTSSHASLPASDTGSMTETQGDEDEEEGALASCTRCLNKIMKTRVCRRLRRANRVLRARCRRAVKSNACYWAVLLLVFLNTLTIASEHHGQPVWLTQIQEYANKVLLCLFTVEMLLKLYGLGPSAYVSSFFNRFDCFVVCGGILETTLVEVGAMQPLGISVLRCVRLLRIFKVTRHWASLSNLVASLLNSMKSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDQTHTKRSTFDTFPQALLTVFQILTGEDWNVVMYDGIMAYGGPFFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLASGDAGTAKDKGGEKSNEKDLPQENEGLVPGVEKEEEEGARREGADMEEEEEEEEEEEEEEEEEGAGGVELLQEVVPKEKVVPIPEGSAFFCLSQTNPLRKGCHTLIHHHVFTNLILVFIILSSVSLAAEDPIRAHSFRNHILGYFDYAFTSIFTVEILLKMTVFGAFLHRGSFCRSWFNMLDLLVVSVSLISFGIHSSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIMIVTTLLQFMFACIGVQLFKGKFYTCTDEAKHTPQECKGSFLVYPDGDVSRPLVRERLWVNSDFNFDNVLSAMMALFTVSTFEGWPALLYKAIDAYAEDHGPIYNYRVEISVFFIVYIIIIAFFMMNIFVGFVIITFRAQGEQEYQNCELDKNQRQCVEYALKAQPLRRYIPKNPHQYRVWATVNSAAFEYLMFLLILLNTVALAMQHYEQTAPFNYAMDILNMVFTGLFTIEMVLKIIAFKPKHYFTDAWNTFDALIVVGSIVDIAVTEVNNGGHLGESSEDSSRISITFFRLFRVMRLVKLLSKGEGIRTLLWTFIKSFQALPYVALLIAMIFFIYAVIGMQMFGKVALQDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEIMLASLPGNRCDPESDFGPGEEFTCGSNFAIAYFISFFMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWSEYDPGAKGRIKHLDVVALLRRIQPPLGFGKLCPHRVACKRLVAMNMPLNSDGTVTFNATLFALVRTSLKIKTEGNLEQANQELRIVIKKIWKRMKQKLLDEVIPPPDEEEVTVGKFYATFLIQDYFRKFRRRKEKGLLGNDAAPSTSSALQAGLRSLQDLGPEMRQALTCDTEEEEEEGQEGVEEEDEKDLETNKATMVSQPSARRGSGISVSLPVGDRLPDSLSFGPSDDDRGTPTSSQPSVPQAGSNTHRRGSGALIFTIPEEGNSQPKGTKGQNKQDEDEEVPDRLSYLDEQAGTPPCSVLLPPHRAQRYMDGHLVPRRRLLPPTPAGRKPSFTIQCLQRQGSCEDLPIPGTYHRGRNSGPNRAQGSWATPPQRGRLLYAPLLLVEEGAAGEGYLGRSSGPLRTFTCLHVPGTHSDPSHGKRGSADSLVEAVLISEGLGLFARDPRFVALAKQEIADACRLTLDEMDNAASDLLAQGTSSLYSDEESILSRFDEEDLGDEMACVHAL TTJ0SO4 TT Literature-reported TTVFB0O ID TTVFB0O TTVFB0O TN Voltage-gated potassium channel Kv1.2 (KCNA2) TTVFB0O UP P16389 TTVFB0O UC KCNA2_HUMAN TTVFB0O BC Voltage-gated ion channel TTVFB0O SN Voltage-gated potassium channel subunit Kv1.2; Voltage-gated potassium channel HBK5; Voltage-gated K(+) channel HuKIV; Potassium voltage-gated channel subfamily A member 2; NGK1 TTVFB0O GN KCNA2 TTVFB0O FC Prevents aberrant action potential firing and regulates neuronal output. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA2 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure. In contrast, a heteromultimer formed by KCNA2 and KCNA4 shows rapid inactivation. Regulates neuronal excitability and plays a role as pacemaker in the regulation of neuronal action potentials. KCNA2-containing channels play a presynaptic role and prevent hyperexcitability and aberrant action potential firing. Response to toxins that are selective for KCNA2-containing potassium channels suggests that in Purkinje cells, dendritic subthreshold KCNA2-containing potassium channels prevent random spontaneous calcium spikes, suppressing dendritic hyperexcitability without hindering the generation of somatic action potentials, and thereby play an important role in motor coordination. Plays a role in the induction of long-term potentiation of neuron excitability in the CA3 layer of the hippocampus. May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons. May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA). Contributes to the regulation of the axonal release of the neurotransmitter dopamine. Reduced KCNA2 expression plays a role in the perception of neuropathic pain after peripheral nerve injury, but not acute pain. Plays a role in the regulation of the time spent in non-rapid eye movement (NREM) sleep. Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the cardiovascular system. TTVFB0O SQ MTVATGDPADEAAALPGHPQDTYDPEADHECCERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGPARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGSGVTFHTYSNSTIGYQQSTSFTDPFFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYFITLGTELAEKPEDAQQGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEADERESQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQYLQVTSCPKIPSSPDLKKSRSASTISKSDYMEIQEGVNNSNEDFREENLKTANCTLANTNYVNITKMLTDV TTVFB0O TT Literature-reported TTJ2W69 ID TTJ2W69 TTJ2W69 TN Voltage-gated potassium channel Kv1.6 (KCNA6) TTJ2W69 UP P17658 TTJ2W69 UC KCNA6_HUMAN TTJ2W69 BC Voltage-gated ion channel TTJ2W69 SN Voltage-gated potassium channel subunit Kv1.6; Voltage-gated potassium channel HBK2; Potassium voltage-gated channel subfamily A member 6 TTJ2W69 GN KCNA6 TTJ2W69 FC Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (By similarity). Homotetrameric channels display rapid activation and slow inactivation. TTJ2W69 SQ MRSEKSLTLAAPGEVRGPEGEQQDAGDFPEAGGGGGCCSSERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFLEEIRFYQLGDEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPQFRVDGRGGNNGGVSRVSPVSRGSQEEEEDEDDSYTFHHGITPGEMGTGGSSSLSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKPAFFRNIMNIIDLVAIFPYFITLGTELVQQQEQQPASGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADDDDSLFPSIPDAFWWAVVTMTTVGYGDMYPMTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEQEEQGQYTHVTCGQPAPDLRATDNGLGKPDFPEANRERRPSYLPTPHRAYAEKRMLTEV TTJ2W69 TT Literature-reported TTCVBT7 ID TTCVBT7 TTCVBT7 TN Voltage-gated potassium channel Kv1.7 (KCNA7) TTCVBT7 UP Q96RP8 TTCVBT7 UC KCNA7_HUMAN TTCVBT7 BC Voltage-gated ion channel TTCVBT7 SN Voltage-gated potassium channel subunit Kv1.7; Potassium voltage-gated channel subfamily A member 7 TTCVBT7 GN KCNA7 TTCVBT7 FC Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient (By similarity). TTCVBT7 SQ MEPRCPPPCGCCERLVLNVAGLRFETRARTLGRFPDTLLGDPARRGRFYDDARREYFFDRHRPSFDAVLYYYQSGGRLRRPAHVPLDVFLEEVAFYGLGAAALARLREDEGCPVPPERPLPRRAFARQLWLLFEFPESSQAARVLAVVSVLVILVSIVVFCLETLPDFRDDRDGTGLAAAAAAGPFPAPLNGSSQMPGNPPRLPFNDPFFVVETLCICWFSFELLVRLLVCPSKAIFFKNVMNLIDFVAILPYFVALGTELARQRGVGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLRASMRELGLLIFFLFIGVVLFSSAVYFAEVDRVDSHFTSIPESFWWAVVTMTTVGYGDMAPVTVGGKIVGSLCAIAGVLTISLPVPVIVSNFSYFYHRETEGEEAGMFSHVDMQPCGPLEGKANGGLVDGEVPELPPPLWAPPGKHLVTEV TTCVBT7 TT Literature-reported TTT4Y0X ID TTT4Y0X TTT4Y0X TN Voltage-gated potassium channel Kv1.8 (KCNA10) TTT4Y0X UP Q16322 TTT4Y0X UC KCA10_HUMAN TTT4Y0X BC Voltage-gated ion channel TTT4Y0X SN Voltage-gated potassium channel subunit Kv1.8; Potassium voltage-gated channel subfamily A member 10 TTT4Y0X GN KCNA10 TTT4Y0X FC Mediates voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. The channel activity is up-regulated by cAMP. TTT4Y0X SQ MDVCGWKEMEVALVNFDNSDEIQEEPGYATDFDSTSPKGRPGGSSFSNGKILISESTNHETAFSKLPGDYADPPGPEPVVLNEGNQRVIINIAGLRFETQLRTLSQFPETLLGDREKRMQFFDSMRNEYFFDRNRPSFDGILYYYQSGGKIRRPANVPIDIFADEISFYELGSEAMDQFREDEGFIKDPETLLPTNDIHRQFWLLFEYPESSSAARAVAVVSVLVVVISITIFCLETLPEFREDRELKVVRDPNLNMSKTVLSQTMFTDPFFMVESTCIVWFTFELVLRFVVCPSKTDFFRNIMNIIDIISIIPYFATLITELVQETEPSAQQNMSLAILRIIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEVDEPESHFSSIPDGFWWAVVTMTTVGYGDMCPTTPGGKIVGTLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEKQNIPGEIERILNSVGSRMGSTDSLNKTNGGCSTEKSRK TTT4Y0X TT Literature-reported TTX8LQ0 ID TTX8LQ0 TTX8LQ0 TN Voltage-gated potassium channel Kv10.2 (KCNH5) TTX8LQ0 UP Q8NCM2 TTX8LQ0 UC KCNH5_HUMAN TTX8LQ0 BC Voltage-gated ion channel TTX8LQ0 SN hEAG2; Voltage-gated potassium channel subunit Kv10.2; Potassium voltage-gated channel subfamily H member 5; Ether-a-go-go potassium channel 2; EAG2 TTX8LQ0 GN KCNH5 TTX8LQ0 FC Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a non-inactivating outward rectifying current. Channel properties may be modulated by cAMP and subunit assembly. TTX8LQ0 SQ MPGGKRGLVAPQNTFLENIVRRSSESSFLLGNAQIVDWPVVYSNDGFCKLSGYHRADVMQKSSTCSFMYGELTDKKTIEKVRQTFDNYESNCFEVLLYKKNRTPVWFYMQIAPIRNEHEKVVLFLCTFKDITLFKQPIEDDSTKGWTKFARLTRALTNSRSVLQQLTPMNKTEVVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCAFKTTWDWVILILTFYTAIMVPYNVSFKTKQNNIAWLVLDSVVDVIFLVDIVLNFHTTFVGPGGEVISDPKLIRMNYLKTWFVIDLLSCLPYDIINAFENVDEGISSLFSSLKVVRLLRLGRVARKLDHYLEYGAAVLVLLVCVFGLVAHWLACIWYSIGDYEVIDEVTNTIQIDSWLYQLALSIGTPYRYNTSAGIWEGGPSKDSLYVSSLYFTMTSLTTIGFGNIAPTTDVEKMFSVAMMMVGSLLYATIFGNVTTIFQQMYANTNRYHEMLNNVRDFLKLYQVPKGLSERVMDYIVSTWSMSKGIDTEKVLSICPKDMRADICVHLNRKVFNEHPAFRLASDGCLRALAVEFQTIHCAPGDLIYHAGESVDALCFVVSGSLEVIQDDEVVAILGKGDVFGDIFWKETTLAHACANVRALTYCDLHIIKREALLKVLDFYTAFANSFSRNLTLTCNLRKRIIFRKISDVKKEEEERLRQKNEVTLSIPVDHPVRKLFQKFKQQKELRNQGSTQGDPERNQLQVESRSLQNGASITGTSVVTVSQITPIQTSLAYVKTSESLKQNNRDAMELKPNGGADQKCLKVNSPIRMKNGNGKGWLRLKNNMGAHEEKKEDWNNVTKAESMGLLSEDPKSSDSENSVTKNPLRKTDSCDSGITKSDLRLDKAGEARSPLEHSPIQADAKHPFYPIPEQALQTTLQEVKHELKEDIQLLSCRMTALEKQVAEILKILSEKSVPQASSPKSQMPLQVPPQIPCQDIFSVSRPESPESDKDEIHF TTX8LQ0 TT Literature-reported TTZ4MTQ ID TTZ4MTQ TTZ4MTQ TN Voltage-gated potassium channel Kv12.2 (KCNH3) TTZ4MTQ UP Q9ULD8 TTZ4MTQ UC KCNH3_HUMAN TTZ4MTQ BC Voltage-gated ion channel TTZ4MTQ SN Voltage-gated potassium channel subunit Kv12.2; Potassium voltage-gated channel subfamily H member 3; KIAA1282; Ether-a-go-go-like potassium channel 2; ELK2; ELK channel 2; Brain-specific eag-like channel 1; BEC1 TTZ4MTQ GN KCNH3 TTZ4MTQ FC Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits an outward current with fast inactivation. Channel properties may be modulated by cAMP and subunit assembly. TTZ4MTQ SQ MPAMRGLLAPQNTFLDTIATRFDGTHSNFVLGNAQVAGLFPVVYCSDGFCDLTGFSRAEVMQRGCACSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEKGEVALFLVSHKDISETKNRGGPDRWKETGGGRRRYGRARSKGFNANRRRSRAVLYHLSGHLQKQPKGKHKLNKGVFGEKPNLPEYKVAAIRKSPFILLHCGALRATWDGFILLATLYVAVTVPYSVCVSTAREPSAARGPPSVCDLAVEVLFILDIVLNFRTTFVSKSGQVVFAPKSICLHYVTTWFLLDVIAALPFDLLHAFKVNVYFGAHLLKTVRLLRLLRLLPRLDRYSQYSAVVLTLLMAVFALLAHWVACVWFYIGQREIESSESELPEIGWLQELARRLETPYYLVGRRPAGGNSSGQSDNCSSSSEANGTGLELLGGPSLRSAYITSLYFALSSLTSVGFGNVSANTDTEKIFSICTMLIGALMHAVVFGNVTAIIQRMYARRFLYHSRTRDLRDYIRIHRIPKPLKQRMLEYFQATWAVNNGIDTTELLQSLPDELRADIAMHLHKEVLQLPLFEAASRGCLRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLKGGTVLAILGKGDLIGCELPRREQVVKANADVKGLTYCVLQCLQLAGLHDSLALYPEFAPRFSRGLRGELSYNLGAGGGSAEVDTSSLSGDNTLMSTLEEKETDGEQGPTVSPAPADEPSSPLLSPGCTSSSSAAKLLSPRRTAPRPRLGGRGRPGRAGALKAEAGPSAPPRALEGLRLPPMPWNVPPDLSPRVVDGIEDGCGSDQPKFSFRVGQSGPECSSSPSPGPESGLLTVPHGPSEARNTDTLDKLRQAVTELSEQVLQMREGLQSLRQAVQLVLAPHREGPCPRASGEGPCPASTSGLLQPLCVDTGASSYCLQPPAGSVLSGTWPHPRPGPPPLMAPWPWGPPASQSSPWPRATAFWTSTSDSEPPASGDLCSEPSTPASPPPSEEGARTGPAEPVSQAEATSTGEPPPGSGGLALPWDPHSLEMVLIGCHGSGTVQWTQEEGTGV TTZ4MTQ TT Literature-reported TT5PFNG ID TT5PFNG TT5PFNG TN Voltage-gated potassium channel Kv2.2 (KCNB2) TT5PFNG UP Q92953 TT5PFNG UC KCNB2_HUMAN TT5PFNG BC Voltage-gated ion channel TT5PFNG SN Voltage-gated potassium channel subunit Kv2.2; Potassium voltage-gated channel subfamily B member 2 TT5PFNG GN KCNB2 TT5PFNG FC Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells. TT5PFNG SQ MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMREREGEEFDNTCCPDKRKKLWDLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQETDEFGQLNDNRQLAHVEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDATKFTSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVAVEKAGESANTKDSADDNHLSPSRWKWARKALSETSSNKSFENKYQEVSQKDSHEQLNNTSSSSPQHLSAQKLEMLYNEITKTQPHSHPNPDCQEKPERPSAYEEEIEMEEVVCPQEQLAVAQTEVIVDMKSTSSIDSFTSCATDFTETERSPLPPPSASHLQMKFPTDLPGTEEHQRARGPPFLTLSREKGPAARDGTLEYAPVDITVNLDASGSQCGLHSPLQSDNATDSPKSSLKGSNPLKSRSLKVNFKENRGSAPQTPPSTARPLPVTTADFSLTTPQHISTILLEETPSQGDRPLLGTEVSAPCQGPSKGLSPRFPKQKLFPFSSRERRSFTEIDTGDDEDFLELPGAREEKQVDSSPNCFADKPSDGRDPLREEGSVGSSSPQDTGHNCRQDIYHAVSEVKKDSSQEGCKMENHLFAPEIHSNPGDTGYCPTRETSM TT5PFNG TT Literature-reported TTVUWHQ ID TTVUWHQ TTVUWHQ TN Voltage-gated potassium channel Kv3.1 (KCNC1) TTVUWHQ UP P48547 TTVUWHQ UC KCNC1_HUMAN TTVUWHQ BC Voltage-gated ion channel TTVUWHQ SN Voltage-gated potassium channel subunit Kv4; Voltage-gated potassium channel subunit Kv3.1; Potassium voltage-gated channel subfamily C member 1; NGK2 TTVUWHQ GN KCNC1 TTVUWHQ FC The channel opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical gradient. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNC2, and possibly other family members as well. Contributes to fire sustained trains of very brief action potentials at high frequency in pallidal neurons. Voltage-gated potassium channel that plays an important role in the rapid repolarization of fast-firing brain neurons. TTVUWHQ SQ MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRHPGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDSFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALFEDPYSSRYARYVAFASLFFILVSITTFCLETHERFNPIVNKTEIENVRNGTQVRYYREAETEAFLTYIEGVCVVWFTFEFLMRVIFCPNKVEFIKNSLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGAQPNDPSASEHTHFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKKKHIPRPPQLGSPNYCKSVVNSPHHSTQSDTCPLAQEEILEINRAGRKPLRGMSI TTVUWHQ TT Literature-reported TTGK3ZO ID TTGK3ZO TTGK3ZO TN Voltage-gated potassium channel Kv3.2 (KCNC2) TTGK3ZO UP Q96PR1 TTGK3ZO UC KCNC2_HUMAN TTGK3ZO BC Voltage-gated ion channel TTGK3ZO SN Shaw-like potassium channel; Potassium voltage-gated channel subfamily C member 2 TTGK3ZO GN KCNC2 TTGK3ZO FC Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Contributes to the regulation of the fast action potential repolarization and in sustained high-frequency firing in neurons of the central nervous system. Homotetramer channels mediate delayed-rectifier voltage-dependent potassium currents that activate rapidly at high-threshold voltages and inactivate slowly. Forms tetrameric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNC1, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties may be modulated either by the association with ancillary subunits, such as KCNE1, KCNE2 or KCNE3 or indirectly by nitric oxide (NO) through a cGMP- and PKG-mediated signaling cascade, slowing channel activation and deactivation of delayed rectifier potassium channels (By similarity). Contributes to fire sustained trains of very brief action potentials at high frequency in retinal ganglion cells, thalamocortical and suprachiasmatic nucleus (SCN) neurons and in hippocampal and neocortical interneurons. Sustained maximal action potential firing frequency in inhibitory hippocampal interneurons is negatively modulated by histamine H2 receptor activation in a cAMP- and protein kinase (PKA) phosphorylation-dependent manner. Plays a role in maintaining the fidelity of synaptic transmission in neocortical GABAergic interneurons by generating action potential (AP) repolarization at nerve terminals, thus reducing spike-evoked calcium influx and GABA neurotransmitter release. Required for long-range synchronization of gamma oscillations over distance in the neocortex. Contributes to the modulation of the circadian rhythm of spontaneous action potential firing in suprachiasmatic nucleus (SCN) neurons in a light-dependent manner (By similarity). TTGK3ZO SQ MGKIENNERVILNVGGTRHETYRSTLKTLPGTRLALLASSEPPGDCLTTAGDKLQPSPPPLSPPPRAPPLSPGPGGCFEGGAGNCSSRGGRASDHPGGGREFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDIFETPDLIGGDPGDDEDLAAKRLGIEDAAGLGGPDGKSGRWRRLQPRMWALFEDPYSSRAARFIAFASLFFILVSITTFCLETHEAFNIVKNKTEPVINGTSVVLQYEIETDPALTYVEGVCVVWFTFEFLVRIVFSPNKLEFIKNLLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERVGAQPNDPSASEHTQFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPRKRKKHIPPAPQASSPTFCKTELNMACNSTQSDTCLGKDNRLLEHNRSVLSGDDSTGSEPPLSPPERLPIRRSSTRDKNRRGETCFLLTTGDYTCASDGGIRKGYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL TTGK3ZO TT Literature-reported TTALSY9 ID TTALSY9 TTALSY9 TN Voltage-gated potassium channel Kv3.3 (KCNC3) TTALSY9 UP Q14003 TTALSY9 UC KCNC3_HUMAN TTALSY9 BC Voltage-gated ion channel TTALSY9 SN Voltage-gated potassium channel subunit Kv3.3; Potassium voltage-gated channel subfamily C member 3; KSHIIID TTALSY9 GN KCNC3 TTALSY9 FC Voltage-gated potassium channel that plays an important role in the rapid repolarization of fast-firing brain neurons. The channel opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical gradient. The channel displays rapid activation and inactivation kinetics. It plays a role in the regulation of the frequency, shape and duration of action potentials in Purkinje cells. Required for normal survival of cerebellar neurons, probably via its role in regulating the duration and frequency of action potentials that in turn regulate the activity of voltage-gated Ca(2+) channels and cellular Ca(2+) homeostasis (By similarity). Required for normal motor function. Plays a role in the reorganization of the cortical actin cytoskeleton and the formation of actin veil structures in neuronal growth cones via its interaction with HAX1 and the Arp2/3 complex. TTALSY9 SQ MLSSVCVSSFRGRQGASKQQPAPPPQPPESPPPPPLPPQQQQPAQPGPAASPAGPPAPRGPGDRRAEPCPGLPAAAMGRHGGGGGDSGKIVINVGGVRHETYRSTLRTLPGTRLAGLTEPEAAARFDYDPGADEFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELGFWGIDETDVEACCWMTYRQHRDAEEALDSFEAPDPAGAANAANAAGAHDGGLDDEAGAGGGGLDGAGGELKRLCFQDAGGGAGGPPGGAGGAGGTWWRRWQPRVWALFEDPYSSRAARYVAFASLFFILISITTFCLETHEGFIHISNKTVTQASPIPGAPPENITNVEVETEPFLTYVEGVCVVWFTFEFLMRITFCPDKVEFLKSSLNIIDCVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGADPDDILGSNHTYFKNIPIGFWWAVVTMTTLGYGDMYPKTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKNKHIPRPPQPGSPNYCKPDPPPPPPPHPHHGSGGISPPPPITPPSMGVTVAGAYPAGPHTHPGLLRGGAGGLGIMGLPPLPAPGEPCPLAQEEVIEINRADPRPNGDPAAAALAHEDCPAIDQPAMSPEDKSPITPGSRGRYSRDRACFLLTDYAPSPDGSIRKATGAPPLPPQDWRKPGPPSFLPDLNANAAAWISP TTALSY9 TT Literature-reported TT4DI0J ID TT4DI0J TT4DI0J TN Voltage-gated potassium channel Kv4.1 (KCND1) TT4DI0J UP Q9NSA2 TT4DI0J UC KCND1_HUMAN TT4DI0J BC Voltage-gated ion channel TT4DI0J SN Voltage-gated potassium channel subunit Kv4.1; Potassium voltage-gated channel subfamily D member 1 TT4DI0J GN KCND1 TT4DI0J FC Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits. TT4DI0J SQ MAAGLATWLPFARAAAVGWLPLAQQPLPPAPGVKASRGDEVLVVNVSGRRFETWKNTLDRYPDTLLGSSEKEFFYDADSGEYFFDRDPDMFRHVLNFYRTGRLHCPRQECIQAFDEELAFYGLVPELVGDCCLEEYRDRKKENAERLAEDEEAEQAGDGPALPAGSSLRQRLWRAFENPHTSTAALVFYYVTGFFIAVSVIANVVETIPCRGSARRSSREQPCGERFPQAFFCMDTACVLIFTGEYLLRLFAAPSRCRFLRSVMSLIDVVAILPYYIGLLVPKNDDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSCASELGFLLFSLTMAIIIFATVMFYAEKGTNKTNFTSIPAAFWYTIVTMTTLGYGDMVPSTIAGKIFGSICSLSGVLVIALPVPVIVSNFSRIYHQNQRADKRRAQQKVRLARIRLAKSGTTNAFLQYKQNGGLEDSGSGEEQALCVRNRSAFEQQHHHLLHCLEKTTCHEFTDELTFSEALGAVSPGGRTSRSTSVSSQPVGPGSLLSSCCPRRAKRRAIRLANSTASVSRGSMQELDMLAGLRRSHAPQSRSSLNAKPHDSLDLNCDSRDFVAAIISIPTPPANTPDESQPSSPGGGGRAGSTLRNSSLGTPCLFPETVKISSL TT4DI0J TT Literature-reported TT7OFWB ID TT7OFWB TT7OFWB TN WD repeat-containing protein 5 (WDR5) TT7OFWB UP P61964 TT7OFWB UC WDR5_HUMAN TT7OFWB SN BMP2-induced 3-kb gene protein; BIG3 TT7OFWB GN WDR5 TT7OFWB FC May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation. Contributes to histone modification. TT7OFWB PD 6IAM; 6E1Z; 6E1Y; 6DYA; 6DY7 TT7OFWB SQ MATEEKKPETEAARAQPTPSSSATQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISGHKLGISDVAWSSDSNLLVSASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVKTGKCLKTLPAHSDPVSAVHFNRDGSLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSKGKCLKTYTGHKNEKYCIFANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALENDKTIKLWKSDC TT7OFWB TT Literature-reported TT8NARC ID TT8NARC TT8NARC TN Wnt-7a protein (WNT7A) TT8NARC UP O00755 TT8NARC UC WNT7A_HUMAN TT8NARC SN Protein Wnt-7a TT8NARC GN WNT7A TT8NARC FC Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation. Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes. Required for normal neural stem cell proliferation in the hippocampus dentate gyrus. Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation. Promotes formation of synapses via its interaction with FZD5. Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway. TT8NARC PD 4UZQ TT8NARC SQ MNRKARRCLGHLFLSLGMVYLRIGGFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK TT8NARC TT Literature-reported TTI9MBZ ID TTI9MBZ TTI9MBZ TN X-prolyl aminopeptidase 2 (XPNPEP2) TTI9MBZ UP O43895 TTI9MBZ UC XPP2_HUMAN TTI9MBZ SN mAmP; Xaa-Pro aminopeptidase 2; X-Pro aminopeptidase 2; Membrane-bound aminopeptidase P; Membrane-bound AmP; Membrane-bound APP; Aminoacylproline aminopeptidase TTI9MBZ GN XPNPEP2 TTI9MBZ FC Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin. TTI9MBZ EC EC 3.4.11.9 TTI9MBZ SQ MARAHWGCCPWLVLLCACAWGHTKPVDLGGQDVRNCSTNPPYLPVTVVNTTMSLTALRQQMQTQNLSAYIIPGTDAHMNEYIGQHDERRAWITGFTGSAGTAVVTMKKAAVWTDSRYWTQAERQMDCNWELHKEVGTTPIVTWLLTEIPAGGRVGFDPFLLSIDTWESYDLALQGSNRQLVSITTNLVDLVWGSERPPVPNQPIYALQEAFTGSTWQEKVSGVRSQMQKHQKVPTAVLLSALEETAWLFNLRASDIPYNPFFYSYTLLTDSSIRLFANKSRFSSETLSYLNSSCTGPMCVQIEDYSQVRDSIQAYSLGDVRIWIGTSYTMYGIYEMIPKEKLVTDTYSPVMMTKAVKNSKEQALLKASHVRDAVAVIRYLVWLEKNVPKGTVDEFSGAEIVDKFRGEEQFSSGPSFETISASGLNAALAHYSPTKELNRKLSSDEMYLLDSGGQYWDGTTDITRTVHWGTPSAFQKEAYTRVLIGNIDLSRLIFPAATSGRMVEAFARRALWDAGLNYGHGTGHGIGNFLCVHEWPVGFQSNNIAMAKGMFTSIEPGYYKDGEFGIRLEDVALVVEAKTKYPGSYLTFEVVSFVPYDRNLIDVSLLSPEHLQYLNRYYQTIREKVGPELQRRQLLEEFEWLQQHTEPLAARAPDTASWASVLVVSTLAILGWSV TTI9MBZ TT Literature-reported TTYGH36 ID TTYGH36 TTYGH36 TN Yersinia pestis Virulence associated V antigen (YP lcrV) TTYGH36 UP P0C7U7 TTYGH36 UC LCRV_YERPE TTYGH36 SN lcrV; YP Virulence-associated V antigen; YP Low calcium response locus protein V TTYGH36 GN YP lcrV TTYGH36 FC Possibly involved in calcium regulation of YOP expression, which includes the export process. TTYGH36 PD 4JBU; 1R6F TTYGH36 SQ MIRAYEQNPQHFIEDLEKVRVEQLTGHGSSVLEELVQLVKDKNIDISIKYDPRKDSEVFANRVITDDIELLKKILAYFLPEDAILKGGHYDNQLQNGIKRVKEFLESSPNTQWELRAFMAVMHFSLTADRIDDDILKVIVDSMNHHGDARSKLREELAELTAELKIYSVIQAEINKHLSSSGTINIHDKSINLMDKNLYGYTDEEIFKASAEYKILEKMPQTTIQVDGSEKKIVSIKDFLGSENKRTGALGNLKNSYSYNKDNNELSHFATTCSDKSRPLNDLVSQKTTQLSDITSRFNSAIEALNRFIQKYDSVMQRLLDDTSGK TTYGH36 TT Literature-reported TT8UN2D ID TT8UN2D TT8UN2D TN Yes-associated protein 1 (YAP1) TT8UN2D UP P46937 TT8UN2D UC YAP1_HUMAN TT8UN2D SN Yorkie homolog; Yes-associated protein YAP65 homolog; YAP65; Transcriptional coactivator YAP1; Protein yorkie homolog; 65 kDa Yes-associated protein TT8UN2D GN YAP1 TT8UN2D FC The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization. Plays a key role to control cell proliferation in response to cell contact. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. The presence of TEAD transcription factors are required for it to stimulate gene expression, cell growth, anchorage-independent growth, and epithelial mesenchymal transition (EMT) induction. Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. TT8UN2D PD 6HIL; 6HIK; 6GEK; 6GEI; 6GEG TT8UN2D SQ MDPGQQPPPQPAPQGQGQPPSQPPQGQGPPSGPGQPAPAATQAAPQAPPAGHQIVHVRGDSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEPKSHSRQASTDAGTAGALTPQHVRAHSSPASLQLGAVSPGTLTPTGVVSGPAATPTAQHLRQSSFEIPDDVPLPAGWEMAKTSSGQRYFLNHIDQTTTWQDPRKAMLSQMNVTAPTSPPVQQNMMNSASGPLPDGWEQAMTQDGEIYYINHKNKTTSWLDPRLDPRFAMNQRISQSAPVKQPPPLAPQSPQGGVMGGSNSNQQQQMRLQQLQMEKERLRLKQQELLRQAMRNINPSTANSPKCQELALRSQLPTLEQDGGTQNPVSSPGMSQELRTMTTNSSDPFLNSGTYHSRDESTDSGLSMSSYSVPRTPDDFLNSVDEMDTGDTINQSTLPSQQNRFPDYLEAIPGTNVDLGTLEGDGMNIEGEELMPSLQEALSSDILNDMESVLAATKLDKESFLTWL TT8UN2D TT Literature-reported TT4D2GZ ID TT4D2GZ TT4D2GZ TN Yet another novel kinase 2 (STK32B) TT4D2GZ UP Q9NY57 TT4D2GZ UC ST32B_HUMAN TT4D2GZ SN YANK2; Serine/threonine-protein kinase 32B TT4D2GZ GN STK32B TT4D2GZ FC Catalyzes the conversion of L-seryl-protein into O-phospho-L-seryl-protein. TT4D2GZ EC EC 2.7.11.1 TT4D2GZ SQ MGGNHSHKPPVFDENEEVNFDHFQILRAIGKGSFGKVCIVQKRDTKKMYAMKYMNKQKCIERDEVRNVFRELQIMQGLEHPFLVNLWYSFQDEEDMFMVVDLLLGGDLRYHLQQNVHFTEGTVKLYICELALALEYLQRYHIIHRDIKPDNILLDEHGHVHITDFNIATVVKGAERASSMAGTKPYMAPEVFQVYMDRGPGYSYPVDWWSLGITAYELLRGWRPYEIHSVTPIDEILNMFKVERVHYSSTWCKGMVALLRKLLTKDPESRVSSLHDIQSVPYLADMNWDAVFKKALMPGFVPNKGRLNCDPTFELEEMILESKPLHKKKKRLAKNRSRDGTKDSCPLNGHLQHCLETVREEFIIFNREKLRRQQGQGSQLLDTDSRGGGQAQSKLQDGCNNNLLTHTCTRGCSS TT4D2GZ TT Literature-reported TTUPYLV ID TTUPYLV TTUPYLV TN Zinc alpha-2 glycoprotein (AZGP1) TTUPYLV UP P25311 TTUPYLV UC ZA2G_HUMAN TTUPYLV SN Zn-alpha-2-glycoprotein; Zn-alpha-2-GP; Zinc-alpha-2-glycoprotein; ZNGP1; ZAG TTUPYLV GN AZGP1 TTUPYLV FC Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids. TTUPYLV PD 3ES6; 1ZAG; 1T80; 1T7Z; 1T7Y TTUPYLV SQ MVRMVPVLLSLLLLLGPAVPQENQDGRYSLTYIYTGLSKHVEDVPAFQALGSLNDLQFFRYNSKDRKSQPMGLWRQVEGMEDWKQDSQLQKAREDIFMETLKDIVEYYNDSNGSHVLQGRFGCEIENNRSSGAFWKYYYDGKDYIEFNKEIPAWVPFDPAAQITKQKWEAEPVYVQRAKAYLEEECPATLRKYLKYSKNILDRQDPPSVVVTSHQAPGEKKKLKCLAYDFYPGKIDVHWTRAGEVQEPELRGDVLHNGNGTYQSWVVVAVPPQDTAPYSCHVQHSSLAQPLVVPWEAS TTUPYLV TT Literature-reported TTO50LN ID TTO50LN TTO50LN TN Zinc finger CCHC domain-containing 1 (Lin-28A) TTO50LN UP Q9H9Z2 TTO50LN UC LN28A_HUMAN TTO50LN SN Zinc finger CCHC domain-containing protein 1; ZCCHC1; Protein lin-28 homolog A; Lin-28A; LIN28; CSDD1 TTO50LN GN LIN28A TTO50LN FC RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism. Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits TUT4 AND tut7 uridylyltransferaseS. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells. Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity). TTO50LN PD 5UDZ; 2LI8; 2CQF TTO50LN SQ MGSVSNQQFAGGCAKAAEEAPEEAPEDAARAADEPQLLHGAGICKWFNVRMGFGFLSMTARAGVALDPPVDVFVHQSKLHMEGFRSLKEGEAVEFTFKKSAKGLESIRVTGPGGVFCIGSERRPKGKSMQKRRSKGDRCYNCGGLDHHAKECKLPPQPKKCHFCQSISHMVASCPLKAQQGPSAQGKPTYFREEEEEIHSPTLLPEAQN TTO50LN TT Literature-reported TTT2WK4 ID TTT2WK4 TTT2WK4 TN Zinc finger E-box-binding homeobox 2 (ZEB2) TTT2WK4 UP O60315 TTT2WK4 UC ZEB2_HUMAN TTT2WK4 SN Zinc finger homeobox protein 1b; ZFX1B; ZFHX1B; Smad-interacting protein 1; SMADIP1; SIP1; KIAA0569; HRIHFB2411 TTT2WK4 GN ZEB2 TTT2WK4 FC Represses transcription of E-cadherin. Transcriptional inhibitor that binds to DNA sequence 5'-CACCT-3' in different promoters. TTT2WK4 PD 2DA7 TTT2WK4 SQ MKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDDGIANPLDQETSPASVPNHESSPHVSQALLPREEEEDEIREGGVEHPWHNNEILQASVDGPEEMKEDYDTMGPEATIQTAINNGTVKNANCTSDFEEYFAKRKLEERDGHAVSIEEYLQRSDTAIIYPEAPEELSRLGTPEANGQEENDLPPGTPDAFAQLLTCPYCDRGYKRLTSLKEHIKYRHEKNEENFSCPLCSYTFAYRTQLERHMVTHKPGTDQHQMLTQGAGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCIGLISVNGRMRNNIKTGSSPNSVSSSPTNSAITQLRNKLENGKPLSMSEQTGLLKIKTEPLDFNDYKVLMATHGFSGTSPFMNGGLGATSPLGVHPSAQSPMQHLGVGMEAPLLGFPTMNSNLSEVQKVLQIVDNTVSRQKMDCKAEEISKLKGYHMKDPCSQPEEQGVTSPNIPPVGLPVVSHNGATKSIIDYTLEKVNEAKACLQSLTTDSRRQISNIKKEKLRTLIDLVTDDKMIENHNISTPFSCQFCKESFPGPIPLHQHERYLCKMNEEIKAVLQPHENIVPNKAGVFVDNKALLLSSVLSEKGMTSPINPYKDHMSVLKAYYAMNMEPNSDELLKISIAVGLPQEFVKEWFEQRKVYQYSNSRSPSLERSSKPLAPNSNPPTKDSLLPRSPVKPMDSITSPSIAELHNSVTNCDPPLRLTKPSHFTNIKPVEKLDHSRSNTPSPLNLSSTSSKNSHSSSYTPNSFSSEELQAEPLDLSLPKQMKEPKSIIATKNKTKASSISLDHNSVSSSSENSDEPLNLTFIKKEFSNSNNLDNKSTNPVFSMNPFSAKPLYTALPPQSAFPPATFMPPVQTSIPGLRPYPGLDQMSFLPHMAYTYPTGAATFADMQQRRKYQRKQGFQGELLDGAQDYMSGLDDMTDSDSCLSRKKIKKTESGMYACDLCDKTFQKSSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTELLMNRAYLQSITPQGYSDSEERESMPRDGESEKEHEKEGEDGYGKLGRQDGDEEFEEEEEESENKSMDTDPETIRDEEETGDHSMDDSSEDGKMETKSDHEEDNMEDGM TTT2WK4 TT Literature-reported TTD9R62 ID TTD9R62 TTD9R62 TN Zinc finger protein 202 (ZNF202) TTD9R62 UP O95125 TTD9R62 UC ZN202_HUMAN TTD9R62 BC Zinc-finger TTD9R62 SN Zinc finger protein ZNF202; ZNF202 TTD9R62 GN ZNF202 TTD9R62 FC Transcriptional repressor that binds to elements found predominantly in genes that participate in lipid metabolism. Among its targets are structural components of lipoprotein particles (apolipoproteins AIV, CIII, and E), enzymes involved in lipidprocessing (lipoprotein lipase, lecithin cholesteryl ester transferase), transporters involved in lipid homeostasis (ABCA1, ABCG1), and several genes involved in processes related to energy metabolism and vascular disease. TTD9R62 SQ MATAVEPEDQDLWEEEGILMVKLEDDFTCRPESVLQRDDPVLETSHQNFRRFRYQEAASPREALIRLRELCHQWLRPERRTKEQILELLVLEQFLTVLPGELQSWVRGQRPESGEEAVTLVEGLQKQPRRPRRWVTVHVHGQEVLSEETVHLGVEPESPNELQDPVQSSTPEQSPEETTQSPDLGAPAEQRPHQEEELQTLQESEVPVPEDPDLPAERSSGDSEMVALLTALSQGLVTFKDVAVCFSQDQWSDLDPTQKEFYGEYVLEEDCGIVVSLSFPIPRPDEISQVREEEPWVPDIQEPQETQEPEILSFTYTGDRSKDEEECLEQEDLSLEDIHRPVLGEPEIHQTPDWEIVFEDNPGRLNERRFGTNISQVNSFVNLRETTPVHPLLGRHHDCSVCGKSFTCNSHLVRHLRTHTGEKPYKCMECGKSYTRSSHLARHQKVHKMNAPYKYPLNRKNLEETSPVTQAERTPSVEKPYRCDDCGKHFRWTSDLVRHQRTHTGEKPFFCTICGKSFSQKSVLTTHQRIHLGGKPYLCGECGEDFSEHRRYLAHRKTHAAEELYLCSECGRCFTHSAAFAKHLRGHASVRPCRCNECGKSFSRRDHLVRHQRTHTGEKPFTCPTCGKSFSRGYHLIRHQRTHSEKTS TTD9R62 TT Literature-reported TTJD1TI ID TTJD1TI TTJD1TI TN Zinc finger protein OZF (ZNF146) TTJD1TI UP Q15072 TTJD1TI UC OZF_HUMAN TTJD1TI BC Zinc-finger TTJD1TI SN Zinc finger protein 146; Only zinc finger protein; OZF TTJD1TI GN ZNF146 TTJD1TI FC A nuclear zinc finger protein consisting of a single domain of 10 zinc finger motifs of the Kruppel type, preceded by 10 amino acids. Involved in gene regulation and tumorigenesis. TTJD1TI SQ MSHLSQQRIYSGENPFACKVCGKVFSHKSNLTEHEHFHTREKPFECNECGKAFSQKQYVIKHQNTHTGEKLFECNECGKSFSQKENLLTHQKIHTGEKPFECKDCGKAFIQKSNLIRHQRTHTGEKPFVCKECGKTFSGKSNLTEHEKIHIGEKPFKCSECGTAFGQKKYLIKHQNIHTGEKPYECNECGKAFSQRTSLIVHVRIHSGDKPYECNVCGKAFSQSSSLTVHVRSHTGEKPYGCNECGKAFSQFSTLALHLRIHTGKKPYQCSECGKAFSQKSHHIRHQKIHTH TTJD1TI TT Literature-reported TTXIGT7 ID TTXIGT7 TTXIGT7 TN Zinc transporter 8 (SLC30A8) TTXIGT7 UP Q8IWU4 TTXIGT7 UC ZNT8_HUMAN TTXIGT7 BC Cation diffusion facilitator TTXIGT7 SN ZnT-8; Solute carrier family 30 member 8; SLC30A8 TTXIGT7 GN SLC30A8 TTXIGT7 FC Facilitates the accumulation of zinc from the cytoplasm into intracellular vesicles, being a zinc-efflux transporter. May be a major component for providing zinc to insulin maturation and/or storage processes in insulin-secreting pancreatic beta-cells. TTXIGT7 SQ MEFLERTYLVNDKAAKMYAFTLESVELQQKPVNKDQCPRERPEELESGGMYHCHSGSKPTEKGANEYAYAKWKLCSASAICFIFMIAEVVGGHIAGSLAVVTDAAHLLIDLTSFLLSLFSLWLSSKPPSKRLTFGWHRAEILGALLSILCIWVVTGVLVYLACERLLYPDYQIQATVMIIVSSCAVAANIVLTVVLHQRCLGHNHKEVQANASVRAAFVHALGDLFQSISVLISALIIYFKPEYKIADPICTFIFSILVLASTITILKDFSILLMEGVPKSLNYSGVKELILAVDGVLSVHSLHIWSLTMNQVILSAHVATAASRDSQVVRREIAKALSKSFTMHSLTIQMESPVDQDPDCLFCEDPCD TTXIGT7 TT Literature-reported TT19ATJ ID TT19ATJ TT19ATJ TN Abeta-binding alcohol dehydrogenase (ABAD) TT19ATJ UP Q2L8D9 TT19ATJ UC Q2L8D9_HUMAN TT19ATJ SN Amyloid beta-binding alcohol dehydrogenase TT19ATJ GN ABAD TT19ATJ FC A direct molecular link from Abeta to mitochondrial toxicity. An ABAD peptide specifically inhibits ABAD-Abeta interaction and suppresses Abeta-induced apoptosis and free-radical generation in neurons. TT19ATJ SQ MAAACRSVK TT19ATJ TT Literature-reported TTQJCV8 ID TTQJCV8 TTQJCV8 TN Activation-associated cDNA protein (FNDC1) TTQJCV8 UP Q4ZHG4 TTQJCV8 UC FNDC1_HUMAN TTQJCV8 SN MEL4B3; KIAA1866; Fibronectin type III domain-containing protein 1; FNDC2; Expressed in synovial lining protein TTQJCV8 GN FNDC1 TTQJCV8 FC May be an activator of G protein signaling. TTQJCV8 SQ MAPEAGATLRAPRRLSWAALLLLAALLPVASSAAASVDHPLKPRHVKLLSTKMGLKVTWDPPKDATSRPVEHYNIAYGKSLKSLKYIKVNAETYSFLIEDVEPGVVYFVLLTAENHSGVSRPVYRAESPPGGEWIEIDGFPIKGPGPFNETVTEKEVPNKPLRVRVRSSDDRLSVAWKAPRLSGAKSPRRSRGFLLGYGESGRKMNYVPLTRDERTHEIKKLASESVYVVSLQSMNSQGRSQPVYRAALTKRKISEEDELDVPDDISVRVMSSQSVLVSWVDPVLEKQKKVVASRQYTVRYREKGELARWDYKQIANRRVLIENLIPDTVYEFAVRISQGERDGKWSTSVFQRTPESAPTTAPENLNVWPVNGKPTVVAASWDALPETEGKVKEYILSYAPALKPFGAKSLTYPGDTTSALVDGLQPGERYLFKIRATNRRGLGPHSKAFIVAMPTTSKADVEQNTEDNGKPEKPEPSSPSPRAPASSQHPSVPASPQGRNAKDLLLDLKNKILANGGAPRKPQLRAKKAEELDLQSTEITGEEELGSREDSPMSPSDTQDQKRTLRPPSRHGHSVVAPGRTAVRARMPALPRREGVDKPGFSLATQPRPGAPPSASASPAHHASTQGTSHRPSLPASLNDNDLVDSDEDERAVGSLHPKGAFAQPRPALSPSRQSPSSVLRDRSSVHPGAKPASPARRTPHSGAAEEDSSASAPPSRLSPPHGGSSRLLPTQPHLSSPLSKGGKDGEDAPATNSNAPSRSTMSSSVSSHLSSRTQVSEGAEASDGESHGDGDREDGGRQAEATAQTLRARPASGHFHLLRHKPFAANGRSPSRFSIGRGPRLQPSSSPQSTVPSRAHPRVPSHSDSHPKLSSGIHGDEEDEKPLPATVVNDHVPSSSRQPISRGWEDLRRSPQRGASLHRKEPIPENPKSTGADTHPQGKYSSLASKAQDVQQSTDADTEGHSPKAQPGSTDRHASPARPPAARSQQHPSVPRRMTPGRAPQQQPPPPVATSQHHPGPQSRDAGRSPSQPRLSLTQAGRPRPTSQGRSHSSSDPYTASSRGMLPTALQNQDEDAQGSYDDDSTEVEAQDVRAPAHAARAKEAAASLPKHQQVESPTGAGAGGDHRSQRGHAASPARPSRPGGPQSRARVPSRAAPGKSEPPSKRPLSSKSQQSVSAEDDEEEDAGFFKGGKEDLLSSSVPKWPSSSTPRGGKDADGSLAKEEREPAIALAPRGGSLAPVKRPLPPPPGSSPRASHVPSRLPPRSAATVSPVAGTHPWPQYTTRAPPGHFSTTPMLSLRQRMMHARFRNPLSRQPARPSYRQGYNGRPNVEGKVLPGSNGKPNGQRIINGPQGTKWVVDLDRGLVLNAEGRYLQDSHGNPLRIKLGGDGRTIVDLEGTPVVSPDGLPLFGQGRHGTPLANAQDKPILSLGGKPLVGLEVIKKTTHPPTTTMQPTTTTTPLPTTTTPRPTTATTRRTTTTRRTTTRRPTTTVRTTTRTTTTTTPTPTTPIPTCPPGTLERHDDDGNLIMSSNGIPECYAEEDEFSGLETDTAVPTEEAYVIYDEDYEFETSRPPTTTEPSTTATTPRVIPEEGAISSFPEEEFDLAGRKRFVAPYVTYLNKDPSAPCSLTDALDHFQVDSLDEIIPNDLKKSDLPPQHAPRNITVVAVEGCHSFVIVDWDKATPGDVVTGYLVYSASYEDFIRNKWSTQASSVTHLPIENLKPNTRYYFKVQAQNPHGYGPISPSVSFVTESDNPLLVVRPPGGEPIWIPFAFKHDPSYTDCHGRQYVKRTWYRKFVGVVLCNSLRYKIYLSDNLKDTFYSIGDSWGRGEDHCQFVDSHLDGRTGPQSYVEALPTIQGYYRQYRQEPVRFGNIGFGTPYYYVGWYECGVSIPGKW TTQJCV8 TT Literature-reported TTSMK36 ID TTSMK36 TTSMK36 TN Adenomatous polyposis coli 2 (APC2) TTSMK36 UP O95996 TTSMK36 UC APCL_HUMAN TTSMK36 SN Adenomatous polyposis coli proteinlike; Adenomatous polyposis coli protein-like; Adenomatous polyposis coli protein 2; APClike; APCL; APC-like TTSMK36 GN APC2 TTSMK36 FC May also function in Wnt signaling by promoting the rapid degradation of CTNNB1. Stabilizes microtubules and may regulate actin fiber dynamics through the activation of Rho family GTPases. TTSMK36 SQ MASSVAPYEQLVRQVEALKAENSHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQMDITSLYNLKFQPPTLGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDRERCFLLNEIEKEEKEKLWYYSQLQGLSKRLDELPHVETQFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQALLAVKSVPVDEDPETEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQILHGTEAAAGGRAGAPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDGGPEGGGAGSAPIPIEPQICQATCAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTRDPLNLALRRYAGMTLTNLTFGDVANKATLCARRGCMEAIVAQLASDSEELHQVVSSILRNLSWRADINSKKVLREAGSVTALVQCVLRATKESTLKSVLSALWNLSAHSTENKAAICQVDGALGFLVSTLTYKCQSNSLAIIESGGGILRNVSSLVATREDYRQVLRDHNCLQTLLQHLTSHSLTIVSNACGTLWNLSARSARDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKHQAAATAVSPGSCVPSLYVRKQRALEAELDARHLAQALEHLEKQGPPAAEAATKKPLPPLRHLDGLAQDYASDSGCFDDDDAPSSLAAAAATGEPASPAALSLFLGSPFLQGQALARTPPTRRGGKEAEKDTSGEAAVAAKAKAKLALAVARIDQLVEDISALHTSSDDSFSLSSGDPGQEAPREGRAQSCSPCRGPEGGRREAGSRAHPLLRLKAAHASLSNDSLNSGSASDGYCPREHMLPCPLAALASRREDPRCGQPRPSRLDLDLPGCQAEPPAREATSADARVRTIKLSPTYQHVPLLEGASRAGAEPLAGPGISPGARKQAWLPADHLSKVPEKLAAAPLSVASKALQKLAAQEGPLSLSRCSSLSSLSSAGRPGPSEGGDLDDSDSSLEGLEEAGPSEAELDSTWRAPGATSLPVAIPAPRRNRGRGLGVEDATPSSSSENYVQETPLVLSRCSSVSSLGSFESPSIASSIPSEPCSGQGSGTISPSELPDSPGQTMPPSRSKTPPLAPAPQGPPEATQFSLQWESYVKRFLDIADCRERCRLPSELDAGSVRFTVEKPDENFSCASSLSALALHEHYVQQDVELRLLPSACPERGGGAGGAGLHFAGHRRREEGPAPTGSRPRGAADQELELLRECLGAAVPARLRKVASALVPGRRALPVPVYMLVPAPAPAQEDDSCTDSAEGTPVNFSSAASLSDETLQGPPRDQPGGPAGRQRPTGRPTSARQAMGHRHKAGGAGRSAEQSRGAGKNRAGLELPLGRPPSAPADKDGSKPGRTRGDGALQSLCLTTPTEEAVYCFYGNDSDEEPPAAAPTPTHRRTSAIPRAFTRERPQGRKEAPAPSKAAPAAPPPARTQPSLIADETPPCYSLSSSASSLSEPEPSEPPAVHPRGREPAVTKDPGPGGGRDSSPSPRAAEELLQRCISSALPRRRPPVSGLRRRKPRATRLDERPAEGSRERGEEAAGSDRASDLDSVEWRAIQEGANSIVTWLHQAAAATREASSESDSILSFVSGLSVGSTLQPPKHRKGRQAEGEMGSARRPEKRGAASVKTSGSPRSPAGPEKPRGTQKTTPGVPAVLRGRTVIYVPSPAPRAQPKGTPGPRATPRKVAPPCLAQPAAPAKVPSPGQQRSRSLHRPAKTSELATLSQPPRSATPPARLAKTPSSSSSQTSPASQPLPRKRPPVTQAAGALPGPGASPVPKTPARTLLAKQHKTQRSPVRIPFMQRPARRGPPPLARAVPEPGPRGRAGTEAGPGARGGRLGLVRVASALSSGSESSDRSGFRRQLTFIKESPGLRRRRSELSSAESAASAPQGASPRRGRPALPAVFLCSSRCEELRAAPRQGPAPARQRPPAARPSPGERPARRTTSESPSRLPVRAPAARPETVKRYASLPHISVARRPDGAVPAAPASADAARRSSDGEPRPLPRVAAPGTTWRRIRDEDVPHILRSTLPATALPLRGSTPEDAPAGPPPRKTSDAVVQTEEVAAPKTNSSTSPSLETREPPGAPAGGQLSLLGSDVDGPSLAKAPISAPFVHEGLGVAVGGFPASRHGSPSRSARVPPFNYVPSPMVVAATTDSAAEKAPATASATLLE TTSMK36 TT Literature-reported TTHGD1B ID TTHGD1B TTHGD1B TN Adiponectin receptor (ADIPOR) TTHGD1B UP Q96A54; Q86V24 TTHGD1B UC PAQR1_HUMAN; PAQR2_HUMAN TTHGD1B SN Progestin and adipoQ receptor family member; PAQR; Adiponectin receptor protein TTHGD1B GN ADIPOR1; ADIPOR2 TTHGD1B FC Receptor for globular and full-length adiponectin (APM1), an essential hormone secreted by adipocytes that acts as an antidiabetic. Probably involved in metabolic pathways that regulate lipid metabolism such as fatty acid oxidation. Mediates increased AMPK, PPARA ligand activity, fatty acid oxidation and glucose uptake by adiponectin. Has some high-affinity receptor for globular adiponectin but low-affinity receptor for full-length adiponectin. TTHGD1B SQ MSSHKGSVVAQGNGAPASNREADTVELAELGPLLEEKGKRVIANPPKAEEEQTCPVPQEEEEEVRVLTLPLQAHHAMEKMEEFVYKVWEGRWRVIPYDVLPDWLKDNDYLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGFVLFLFLGILTMLRPNMYFMAPLQEKVVFGMFFLGAVLCLSFSWLFHTVYCHSEKVSRTFSKLDYSGIALLIMGSFVPWLYYSFYCSPQPRLIYLSIVCVLGISAIIVAQWDRFATPKHRQTRAGVFLGLGLSGVVPTMHFTIAEGFVKATTVGQMGWFFLMAVMYITGAGLYAARIPERFFPGKFDIWFQSHQIFHVLVVAAAFVHFYGVSNLQEFRYGLEGGCTDDTLL TTHGD1B TT Literature-reported TTB6H2S ID TTB6H2S TTB6H2S TN Amino acid transporter ATB0+ (SLC6A14) TTB6H2S UP Q9UN76 TTB6H2S UC S6A14_HUMAN TTB6H2S SN Solute carrier family 6 member 14; Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+) TTB6H2S GN SLC6A14 TTB6H2S FC Mediates the uptake of a broad range of neutral and cationic amino acids (with the exception of proline) in a Na(+)/Cl(-)-dependent manner. TTB6H2S SQ MDKLKCPSFFKCREKEKVSASSENFHVGENDENQDRGNWSKKSDYLLSMIGYAVGLGNVWRFPYLTYSNGGGAFLIPYAIMLALAGLPLFFLECSLGQFASLGPVSVWRILPLFQGVGITMVLISIFVTIYYNVIIAYSLYYMFASFQSELPWKNCSSWSDKNCSRSPIVTHCNVSTVNKGIQEIIQMNKSWVDINNFTCINGSEIYQPGQLPSEQYWNKVALQRSSGMNETGVIVWYLALCLLLAWLIVGAALFKGIKSSGKVVYFTALFPYVVLLILLVRGATLEGASKGISYYIGAQSNFTKLKEAEVWKDAATQIFYSLSVAWGGLVALSSYNKFKNNCFSDAIVVCLTNCLTSVFAGFAIFSILGHMAHISGKEVSQVVKSGFDLAFIAYPEALAQLPGGPFWSILFFFMLLTLGLDSQFASIETITTTIQDLFPKVMKKMRVPITLGCCLVLFLLGLVCVTQAGIYWVHLIDHFCAGWGILIAAILELVGIIWIYGGNRFIEDTEMMIGAKRWIFWLWWRACWFVITPILLIAIFIWSLVQFHRPNYGAIPYPDWGVALGWCMIVFCIIWIPIMAIIKIIQAKGNIFQRLISCCRPASNWGPYLEQHRGERYKDMVDPKKEADHEIPTVSGSRKPE TTB6H2S TT Literature-reported TTVHFE8 ID TTVHFE8 TTVHFE8 TN Ammonium transporter Rh type A (RHAG) TTVHFE8 UP Q02094 TTVHFE8 UC RHAG_HUMAN TTVHFE8 SN Rhesus blood group-associated glycoprotein; Rhesus blood group-associated ammonia channel; Rhesus blood group family type A glycoprotein; Rh50A; Rh type A glycoprotein; Rh family type A glycoprotein; RH50; Erythrocyte plasma membrane 50 kDa glycoprotein; Erythrocyte membrane glycoprotein Rh50; CD241 TTVHFE8 GN RHAG TTVHFE8 FC Associated with rhesus blood group antigen expression. May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. Involved in ammonia transport across the erythrocyte membrane. Seems to act in monovalent cation transport. TTVHFE8 SQ MRFTFPLMAIVLEIAMIVLFGLFVEYETDQTVLEQLNITKPTDMGIFFELYPLFQDVHVMIFVGFGFLMTFLKKYGFSSVGINLLVAALGLQWGTIVQGILQSQGQKFNIGIKNMINADFSAATVLISFGAVLGKTSPTQMLIMTILEIVFFAHNEYLVSEIFKASDIGASMTIHAFGAYFGLAVAGILYRSGLRKGHENEESAYYSDLFAMIGTLFLWMFWPSFNSAIAEPGDKQCRAIVNTYFSLAACVLTAFAFSSLVEHRGKLNMVHIQNATLAGGVAVGTCADMAIHPFGSMIIGSIAGMVSVLGYKFLTPLFTTKLRIHDTCGVHNLHGLPGVVGGLAGIVAVAMGASNTSMAMQAAALGSSIGTAVVGGLMTGLILKLPLWGQPSDQNCYDDSVYWKVPKTR TTVHFE8 TT Literature-reported TTQEAIO ID TTQEAIO TTQEAIO TN Amyloid precursor protein secretase (Secretase) TTQEAIO UP Q9Y5Z0; Q9NZ42; Q96BI3; Q8WW43 TTQEAIO UC BACE2_HUMAN; PEN2_HUMAN; APH1A_HUMAN; APH1B_HUMAN TTQEAIO SN Secretase TTQEAIO GN BACE2; PSENEN; APH1A; APH1B TTQEAIO FC Enzymes that "snip" pieces off a longer protein that is embedded in the cell membrane. Among other roles in the cell, secretases act on the amyloid precursor protein (APP) to cleave the protein into three fragments. Sequential cleavage by -secretase (BACE) and -secretase produces the amyloid- peptide fragment that aggregates into clumps called "plaques" in the brains of Alzheimer's disease patients. TTQEAIO SQ MGALARALLLPLLAQWLLRAAPELAPAPFTLPLRVAAATNRVVAPTPGPGTPAERHADGLALALEPALASPAGAANFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLVNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARASLIPEFSDGFWTGSQLACWTNSETPWSYFPKISIYLRDENSSRSFRITILPQLYIQPMMGAGLNYECYRFGISPSTNALVIGATVMEGFYVIFDRAQKRVGFAASPCAEIAGAAVSEISGPFSTEDVASNCVPAQSLSEPILWIVSYALMSVCGAILLVLIVLLLLPFRCQRRPRDPEVVNDESSLVRHRWK TTQEAIO TT Literature-reported TTI48OS ID TTI48OS TTI48OS TN Angiomotin (AMOT) TTI48OS UP Q4VCS5 TTI48OS UC AMOT_HUMAN TTI48OS SN KIAA1071 TTI48OS GN AMOT TTI48OS FC Appears to regulate endothelial cell migration and tube formation. May also play a role in the assembly of endothelial cell-cell junctions. Plays a central role in tight junction maintenance via the complex formed with ARHGAP17, which acts by regulating the uptake of polarity proteins at tight junctions. TTI48OS SQ MRNSEEQPSGGTTVLQRLLQEQLRYGNPSENRSLLAIHQQATGNGPPFPSGSGNPGPQSDVLSPQDHHQQLVAHAARQEPQGQEIQSENLIMEKQLSPRMQNNEELPTYEEAKVQSQYFRGQQHASVGAAFYVTGVTNQKMRTEGRPSVQRLNPGKMHQDEGLRDLKQGHVRSLSERLMQMSLATSGVKAHPPVTSAPLSPPQPNDLYKNPTSSSEFYKAQGPLPNQHSLKGMEHRGPPPEYPFKGMPPQSVVCKPQEPGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARPAQDISLPLSARNSQPHSPTSSLTSGGSLPLLQSPPSTRLSPARHPLVPNQGDHSAHLPRPQQHFLPNQAHQGDHYRLSQPGLSQQQQQQQQQHHHHHHHQQQQQQQPQQQPGEAYSAMPRAQPSSASYQPVPADPFAIVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNCQPTNVSEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSCMRPAKSLMSISNAGSGLLSHSSTLTGSPIMEEKRDDKSWKGSLGILLGGDYRAEYVPSTPSPVPPSTPLLSAHSKTGSRDCSTQTERGTESNKTAAVAPISVPAPVAAAATAAAITATAATITTTMVAAAPVAVAAAAAPAAAAAPSPATAAATAAAVSPAAAGQIPAAASVASAAAVAPSAAAAAAVQVAPAAPAPVPAPALVPVPAPAAAQASAPAQTQAPTSAPAVAPTPAPTPTPAVAQAEVPASPATGPGPHRLSIPSLTCNPDKTDGPVFHSNTLERKTPIQILGQEPDAEMVEYLI TTI48OS TT Literature-reported TTTQH13 ID TTTQH13 TTTQH13 TN Angiotensin-(1-7) receptor (MAS1) TTTQH13 UP P04201 TTTQH13 UC MAS_HUMAN TTTQH13 SN MAS TTTQH13 GN MAS1 TTTQH13 FC Receptor for angiotensin 1-7 (By similarity). Acts specifically as a functional antagonist of AGTR1 (angiotensin-2 type 1 receptor), although it up-regulates AGTR1 receptor levels. Positive regulation of AGTR1 levels occurs through activation of the G-proteins GNA11 and GNAQ, and stimulation of the protein kinase C signaling cascade. The antagonist effect on AGTR1 function is probably due to AGTR1 being physically altered by MAS1. TTTQH13 SQ MDGSNVTSFVVEEPTNISTGRNASVGNAHRQIPIVHWVIMSISPVGFVENGILLWFLCFRMRRNPFTVYITHLSIADISLLFCIFILSIDYALDYELSSGHYYTIVTLSVTFLFGYNTGLYLLTAISVERCLSVLYPIWYRCHRPKYQSALVCALLWALSCLVTTMEYVMCIDREEESHSRNDCRAVIIFIAILSFLVFTPLMLVSSTILVVKIRKNTWASHSSKLYIVIMVTIIIFLIFAMPMRLLYLLYYEYWSTFGNLHHISLLFSTINSSANPFIYFFVGSSKKKRFKESLKVVLTRAFKDEMQPRRQKDNCNTVTVETVV TTTQH13 TT Literature-reported TTM7D9O ID TTM7D9O TTM7D9O TN Annexin II receptor (ANXA2R) TTM7D9O UP Q3ZCQ2 TTM7D9O UC AX2R_HUMAN TTM7D9O SN Annexin2 receptor; AXIIR; ANXA2R TTM7D9O GN ANXA2R TTM7D9O FC May act as a receptor for annexin II on marrow stromal cells to induce osteoclast formation. TTM7D9O SQ MEQHFLGCVKRAWDSAEVAPEPQPPPIVSSEDRGPWPLPLYPVLGEYSLDSCDLGLLSSPCWRLPGVYWQNGLSPGVQSTLEPSTAKPTEFSWPGTQKQQEAPVEEVGQAEEPDRLRLQQLPWSSPLHPWDRQQDTEVCDSGCLLERRHPPALQPWRHLPGFSDCLEWILRVGFAAFSVLWACCSRICGAKQP TTM7D9O TT Literature-reported TTDY4BS ID TTDY4BS TTDY4BS TN AP-2 transcription factor (TFAP2A) TTDY4BS UP P05549 TTDY4BS UC AP2A_HUMAN TTDY4BS SN Transcription factor AP-2-alpha; TFAP2; Activator protein 2; Activating enhancer-binding protein 2-alpha; AP2TF; AP2-alpha; AP-2 TTDY4BS GN TFAP2A TTDY4BS FC AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region. Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. TTDY4BS SQ MLWKLTDNIKYEDCEDRHDGTSNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHALSSGLGDLSIHSLPHAIEEVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEFLNRQHSDPNEQVTRKNMLLATKQICKEFTDLLAQDRSPLGNSRPNPILEPGIQSCLTHFNLISHGFGSPAVCAAVTALQNYLTEALKAMDKMYLSNNPNSHTDNNAKSSDKEEKHRK TTDY4BS TT Literature-reported TT87D3J ID TT87D3J TT87D3J TN APJ endogenous ligand (Apelin) TT87D3J UP Q9ULZ1 TT87D3J UC APEL_HUMAN TT87D3J SN Apelin13; APEL TT87D3J GN APLN TT87D3J FC Drives internalization of the apelin receptor. Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR. Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis. Has an inhibitory effect on cytokine production in response to T-cell receptor/CD3 cross-linking; the oral intake of apelin in the colostrum and the milk might therefore modulate immune responses in neonates. Plays a role in early coronary blood vessels formation. Mediates myocardial contractility in an ERK1/2-dependent manner. May also have a role in the central control of body fluid homeostasis by influencing vasopressin release and drinking behavior. Endogenous ligand for the apelin receptor (APLNR). TT87D3J SQ MNLRLCVQALLLLWLSLTAVCGGSLMPLPDGNGLEDGNVRHLVQPRGSRNGPGPWQGGRRKFRRQRPRLSHKGPMPF TT87D3J TT Literature-reported TT87D3J FM Apelin family TTFLIKM ID TTFLIKM TTFLIKM TN Apoptosis-related protein 3 (ATRAID) TTFLIKM UP Q6UW56 TTFLIKM UC ARAID_HUMAN TTFLIKM SN p18; C2orf28 TTFLIKM GN ATRAID TTFLIKM FC Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway. TTFLIKM SQ MAPHDPGSLTTLVPWAAALLLALGVERALALPEICTQCPGSVQNLSKVAFYCKTTRELMLHARCCLNQKGTILGLDLQNCSLEDPGPNFHQAHTTVIIDLQANPLKGDLANTFRGFTQLQTLILPQHVNCPGGINAWNTITSYIDNQICQGQKNLCNNTGDPEMCPENGSCVPDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGATTLSVSILLWATQRRKAKTS TTFLIKM TT Literature-reported TTLDNMQ ID TTLDNMQ TTLDNMQ TN Aquaporin 3 (AQP3) TTLDNMQ UP Q92482 TTLDNMQ UC AQP3_HUMAN TTLDNMQ SN Aquaporin-3; Aquaglyceroporin-3; AQP-3 TTLDNMQ GN AQP3 TTLDNMQ FC Water channel required to promote glycerol permeability and water transport across cell membranes. Acts as a glycerol transporter in skin and plays an important role in regulating SC (stratum corneum) and epidermal glycerol content. Involved in skin hydration, wound healing, and tumorigenesis. Provides kidney medullary collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. Slightly permeable to urea and may function as a water and urea exit mechanism in antidiuresis in collecting duct cells. It may play an important role in gastrointestinal tract water transport and in glycerol metabolism (By similarity). TTLDNMQ SQ MGRQKELVSRCGEMLHIRYRLLRQALAECLGTLILVMFGCGSVAQVVLSRGTHGGFLTINLAFGFAVTLGILIAGQVSGAHLNPAVTFAMCFLAREPWIKLPIYTLAQTLGAFLGAGIVFGLYYDAIWHFADNQLFVSGPNGTAGIFATYPSGHLDMINGFFDQFIGTASLIVCVLAIVDPYNNPVPRGLEAFTVGLVVLVIGTSMGFNSGYAVNPARDFGPRLFTALAGWGSAVFTTGQHWWWVPIVSPLLGSIAGVFVYQLMIGCHLEQPPPSNEEENVKLAHVKHKEQI TTLDNMQ TT Literature-reported TTS5GLJ ID TTS5GLJ TTS5GLJ TN B melanoma antigen 1 (BAGE) TTS5GLJ UP Q13072 TTS5GLJ UC BAGE1_HUMAN TTS5GLJ SN Cancer/testis antigen 2.1; CT2.1; BAGE1; B melanoma antigen; Antigen MZ2BA; Antigen MZ2-BA TTS5GLJ GN BAGE TTS5GLJ FC Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes. TTS5GLJ SQ MAARAVFLALSAQLLQARLMKEESPVVSWRLEPEDGTALCFIF TTS5GLJ TT Literature-reported TT61VIL ID TT61VIL TT61VIL TN Bacterial Cycloinulo-oligosaccharide fructanotransferase (Bact cft) TT61VIL UP Q9F0I5 TT61VIL UC Q9F0I5_PAEMA TT61VIL SN Cycloinulo-oligosaccharide fructanotransferase TT61VIL GN Bact cft TT61VIL FC Converts inulin into cyclooligosaccharides (cyclofructans) consisting of 6 to 8 molecules of (21)linked cyclic Dfructofuranose through intramolecular transfructosylation. TT61VIL SQ MRKVKRGKCWISGMVIWAMVLQLVVPGISVASENRTVAGETLIPKNDVKSSVTDAIYQIKNIPQNDMGLSVTDSVYQIRNPGFETGDLTGWTVIKGDAFGPNSVTDETTWWAEKIPYNQEGAYHLNGWKYDESATGVLRSSTFELGGSGGISFKLGGAKNPDKVFINIVEVDTGQVIARYGNSAFADVGFPDPAQGMRLANMVQYKADLSTQLGKKLYVEVVDNATSDWGVIFADAFSMYHESEPAEGIVATDIKPDFKRYEIDNPSFETGNLDGWTVEEDAFEVTDEAHASKEGNFYAKSSLQGKGSITSNTFTLQGTGTINFTVLDILKPENAYVALFDANSNTLLMKTGNVSANEKISWKVQEHYNKKLYVKVVDHSNEASIAVDSFQASDRGTIFYLNLDEGAGKKALEKVHNLRHDVNYVFNNARYMASKDPRWTPRGIKGGALLFDGSSNYIEVNANVTVPVSDALTIEAWVAPRSYEWGDGNKLSAIVNQSDQDKAEGFSLGMYRHGTWSMQVGIGGQWIQVWVKDHPLEKYKWNYVAATFSKEDGKIKLYLNGEEVASQATPVNVPITPSTESLIIGKNNKPVELAGVFSFNMFSGLLDEVKLHNKALTNQEILAGYESVKALHGGSIPKIPNADIDEDPSVFDGDQHRPQYHAMPPQNWMNEAHAPIYYNGKYHLFYQHNPQGPFWHQIHWGHWVSDDMVNWENVRPALAPEAGTLDPDGTWSGSAAYDRNGNPVLFYTAGNDSLSPNQRTGLATPADLSDPYLEKWEKYPKPVTEQNGKGIHNEFRDPFVWYDKEVDKWYQLVTSGLPDFSSGTALVYVSDDMYNWKYKGPLYVSDRIRYPELGTVWELPVLLPLGTDSTGKQKYIFMINPHEKPEHVPPANDVQRDVEVFYWIGTWDRDNFKFIPDQEAPSKMDVGDGYLTAESGLVTPDGRTVVFSMVQNVRTPQAEYQSGWAHNLSLPVSLSLDKYDKLHIEPIKELQSLRGEKWVDFSDKNLESANQLIKNVKGDMLEIVMEIDPREAQKFGLKVRRSEKGQEETLIYYDKKNGTFNVDRTKSSIDPDVRVDGIQGGYVDLEGENLKLHIFLDRSVIEAFANYKKKLTTRVYVGRYDSLGLQIWADGDINIKSMQVWDMNALTGKPAAPVYVPDKWDNSVYKDITELPNHDFATGDLTGWMTEGDAFQNVHVTNTQFFWDNIFFNPSHKIPGSYHLWGFNEQAGGDSLTGALRSQNFVLGGNGKINFLISGGRDIDRLYVALVRASDDKELFKETATNYEEYQRKIWDATDYIGEELYIKVVDHSKGGFGHINVDDFNVPVQVKKKTNN TT61VIL TT Literature-reported TTPEFM3 ID TTPEFM3 TTPEFM3 TN Bacterial Ribosomal ATPase RbbA (Bact rbbA) TTPEFM3 UP P37624 TTPEFM3 UC RBBA_ECOLI TTPEFM3 SN Ribosome-associated ATPase; Ribosomal bound ATPase TTPEFM3 GN Bact rbbA TTPEFM3 FC Exhibits an intrinsic ATPase activity that is stimulated by both 70S ribosomes and 30S ribosomal subunits. Could be involved in protein-chain elongation and in release of deacyl-tRNA from ribosomes after peptide bond synthesis. Stimulates the synthesis of polyphenylalanine in vitro. TTPEFM3 SQ MTHLELVPVPPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIAWMPQGLGKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSATLEEAFINLLPQAQRQAHQAVVIPPYQPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGAASLEEAFIAYLQEAAGQSNEAEAPPVVHDTTHAPRQGFSLRRLFSYSRREALELRRDPVRSTLALMGTVILMLIMGYGISMDVENLRFAVLDRDQTVSSQAWTLNLSGSRYFIEQPPLTSYDELDRRMRAGDITVAIEIPPNFGRDIARGTPVELGVWIDGAMPSRAETVKGYVQAMHQSWLQDVASRQSTPASQSGLMNIETRYRYNPDVKSLPAIVPAVIPLLLMMIPSMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIALGMLNFFLLCGLSVFVFGVPHKGSFLTLTLAALLYIIIATGMGLLISTFMKSQIAAIFGTAIITLIPATQFSGMIDPVASLEGPGRWIGEVYPTSHFLTIARGTFSKALDLTDLWQLFIPLLIAIPLVMGLSILLLKKQEG TTPEFM3 TT Literature-reported TTL7N2W ID TTL7N2W TTL7N2W TN B-cell translocation gene 1 protein (BTG1) TTL7N2W UP P62324 TTL7N2W UC BTG1_HUMAN TTL7N2W SN Protein BTG1 TTL7N2W GN BTG1 TTL7N2W FC Anti-proliferative protein. TTL7N2W SQ MHPFYTRAATMIGEIAAAVSFISKFLRTKGLTSERQLQTFSQSLQELLAEHYKHHWFPEKPCKGSGYRCIRINHKMDPLIGQAAQRIGLSSQELFRLLPSELTLWVDPYEVSYRIGEDGSICVLYEASPAGGSTQNSTNVQMVDSRISCKEELLLGRTSPSKNYNMMTVSG TTL7N2W TT Literature-reported TTKYEPM ID TTKYEPM TTKYEPM TN Bombesin-like receptor 3 (BRS3) TTKYEPM UP P32247 TTKYEPM UC BRS3_HUMAN TTKYEPM SN Bombesin receptor subtype-3; BRS-3 TTKYEPM GN BRS3 TTKYEPM FC Role in sperm cell division, maturation, or function. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. TTKYEPM SQ MAQRQPHSPNQTLISITNDTESSSSVVSNDNTNKGWSGDNSPGIEALCAIYITYAVIISVGILGNAILIKVFFKTKSMQTVPNIFITSLAFGDLLLLLTCVPVDATHYLAEGWLFGRIGCKVLSFIRLTSVGVSVFTLTILSADRYKAVVKPLERQPSNAILKTCVKAGCVWIVSMIFALPEAIFSNVYTFRDPNKNMTFESCTSYPVSKKLLQEIHSLLCFLVFYIIPLSIISVYYSLIARTLYKSTLNIPTEEQSHARKQIESRKRIARTVLVLVALFALCWLPNHLLYLYHSFTSQTYVDPSAMHFIFTIFSRVLAFSNSCVNPFALYWLSKSFQKHFKAQLFCCKAERPEPPVADTSLTTLAVMGTVPGTGSIQMSEISVTSFTGCSVKQAEDRF TTKYEPM TT Literature-reported TTDYAKQ ID TTDYAKQ TTDYAKQ TN Borna disease virus Glycoprotein p56 (BoDV p56) TTDYAKQ UP Q89857 TTDYAKQ UC Q89857_BDV1 TTDYAKQ SN Glycoprotein TTDYAKQ GN BoDV p56 TTDYAKQ FC Required for neuronal dissemination of Borna disease virus TTDYAKQ SQ MQPSMSFLIGFGTLVLVLSARTFDLQGLSCNTDSTPGLIDLEIRRLCHTPTENVISCEVSYLNHTTISLPAVHTSCLKYHCKTYWGFFGSYSADRIINRYTGTVKGCLNNSAPEDPFECNWFYCCSAITTEICRCSITNVTVAVQTFPPFMYCSFADCSTVSQQELESGKAMLSDGSTLTYTPYILQSEVVNKTLNGTILCNSSSKIVSFDEFRRSYSLTNGSYQSSSINVTCANYTSSCRPRLKRRRRDTQQIEYLVHKLRPTLKDAWEDCEILQSLLLGVFGTGIASASQFLRSWLNHPDIIGYIVNGVGVVWQCHRVNVTFMTWNESTYYPPVDYNGRKYFLNDEGRLQTNTPEARPGLKRVMWFGRYFLGTVGSGVKPRRIRYNKTSHDYHLEEFEASLNMTPQTSIASGHETDPINHAYGTQADLLPYTRSSNITSTDTGSGWVHIGLPSFAFLNPLGWLRDLLAWAAWLGGVLYLISLCVSLPASFARRRRLGRWQE TTDYAKQ TT Literature-reported TTI6B3F ID TTI6B3F TTI6B3F TN C3a anaphylatoxin chemotactic receptor (C3AR1) TTI6B3F UP Q16581 TTI6B3F UC C3AR_HUMAN TTI6B3F SN HNFAG09; C3a-R; C3R1; C3AR; AZ3B TTI6B3F GN C3AR1 TTI6B3F FC Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production. TTI6B3F SQ MASFSAETNSTDLLSQPWNEPPVILSMVILSLTFLLGLPGNGLVLWVAGLKMQRTVNTIWFLHLTLADLLCCLSLPFSLAHLALQGQWPYGRFLCKLIPSIIVLNMFASVFLLTAISLDRCLVVFKPIWCQNHRNVGMACSICGCIWVVAFVMCIPVFVYREIFTTDNHNRCGYKFGLSSSLDYPDFYGDPLENRSLENIVQPPGEMNDRLDPSSFQTNDHPWTVPTVFQPQTFQRPSADSLPRGSARLTSQNLYSNVFKPADVVSPKIPSGFPIEDHETSPLDNSDAFLSTHLKLFPSASSNSFYESELPQGFQDYYNLGQFTDDDQVPTPLVAITITRLVVGFLLPSVIMIACYSFIVFRMQRGRFAKSQSKTFRVAVVVVAVFLVCWTPYHIFGVLSLLTDPETPLGKTLMSWDHVCIALASANSCFNPFLYALLGKDFRKKARQSIQGILEAAFSEELTRSTHCPSNNVISERNSTTV TTI6B3F TT Literature-reported TTUZ9GV ID TTUZ9GV TTUZ9GV TN Calcitonin gene-related peptide 2 (CALCB) TTUZ9GV UP P10092 TTUZ9GV UC CALCB_HUMAN TTUZ9GV SN Calcitonin gene-related peptide II; CGRP-II; CALC2; Beta-type CGRP; Beta-CGRP TTUZ9GV GN CALCB TTUZ9GV FC CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role. TTUZ9GV SQ MGFRKFSPFLALSILVLYQAGSLQAAPFRSALESSPDPATLSKEDARLLLAALVQDYVQMKASELKQEQETQGSSSAAQKRACNTATCVTHRLAGLLSRSGGMVKSNFVPTNVGSKAFGRRRRDLQA TTUZ9GV TT Literature-reported TTR7YAT ID TTR7YAT TTR7YAT TN Candida Co-chaperone SGT1 (Candi SGT1) TTR7YAT UP A0A1D8PIG5 TTR7YAT UC A0A1D8PIG5_CANAL TTR7YAT SN orf19.4089; CAALFM_C209270CA TTR7YAT GN Candi SGT1 TTR7YAT FC Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Required for both entry into S phase and kinetochore function. Also involved in cyclic AMP (cAMP) pathway, possibly by participating in the assembly or the conformational activation of specific multiprotein complexes. TTR7YAT SQ MAIEQFITKGDDALKSKDYLGAISYYSQAIKENPQAFSPYLKRSTAYQKLKNNDKAKADISSAFSIATEKGKRVDIGLCYFKLGLVYYQEKKVKLSLTQFEKAVEYDCKEPTLSMWKAKAEYDLKNHPEWNVEGDKEEDDDIDLVLGVENEYTQSMANTEKDKSHEPKIVELDANEESSEKKSNQESTSSAPAAQATTQAPKSTNVDVINKIAPLNVKFRDDWYQSNEEVIITIYAKKVNEEKLKVEFDTNSVCISFPSAAASEYKYYLDPLFAEIVPSESKYKVYSTKLEITLKKKDANKWPELEKQAVEGVTDNQDKDKKVDPSELVYPTSSKKKINWNNFKIDDDDKEEGNENDFFRKIFKDVDEDSRRAMMKSYVQSNGTVLTTSWDEAKDKEFEVLPPDGMEVKKWDT TTR7YAT TT Literature-reported TTLAK5E ID TTLAK5E TTLAK5E TN Candida Mannan polymerase complex MNN9 (Candi MNN9) TTLAK5E UP P53697 TTLAK5E UC MNN9_CANAL TTLAK5E SN MNN9; C. albicans MNN9 TTLAK5E GN Candi MNN9 TTLAK5E FC Required for the addition of the long alpha 1,6-mannose backbone ofN-linked glycans on cell wall and periplasmic proteins. TTLAK5E SQ MVHYRNRYLNYIRRKPLALLAPITLLVVIYFYFFSAHGFSSNKQKYNYNKKSRGWFYKNRDTVILKDLPKNHISHYDLNKLTASKDALNKREEVLILTPMSKFLPEYWENINKLTYDHSLISLGFIFPRTTQGDDALKELENALKKTKREKRLNFKKITILRQDSNSLQSQLEKDRHAFKVQKERRSMMALARNSLVFSTILPSTSWVLWLDADIVETPVTLIQDLTGHNKPVVSANVHQRFINQDTKQPDIRPYDFNNWVESEEGLKLAASLPDDEIIVEGYSEMVTHRALMAHFYDPKGDPSTEMTLDGVGGGAVMVKADVHRDGAMFPSFPFYHLIETEGFAKMAKRLGYEVYGLPNYLVFHYNE TTLAK5E TT Literature-reported TTI6V13 ID TTI6V13 TTI6V13 TN Cardiotrophin-like cytokine factor 1 (CLCF1) TTI6V13 UP Q9UBD9 TTI6V13 UC CLCF1_HUMAN TTI6V13 SN Novel neurotrophin1; NNT1; CLCF1; Bcellstimulating factor 3; BSF3 TTI6V13 GN CLCF1 TTI6V13 FC Cytokine with B-cell stimulating capability. Binds to and activates the ILST/gp130 receptor. TTI6V13 SQ MDLRAGDSWGMLACLCTVLWHLPAVPALNRTGDPGPGPSIQKTYDLTRYLEHQLRSLAGTYLNYLGPPFNEPDFNPPRLGAETLPRATVDLEVWRSLNDKLRLTQNYEAYSHLLCYLRGLNRQAATAELRRSLAHFCTSLQGLLGSIAGVMAALGYPLPQPLPGTEPTWTPGPAHSDFLQKMDDFWLLKELQTWLWRSAKDFNRLKKKMQPPAAAVTLHLGAHGF TTI6V13 TT Literature-reported TT5CISB ID TT5CISB TT5CISB TN Cation channel sperm-associated protein 1 (CatSper1) TT5CISB UP Q8NEC5 TT5CISB UC CTSR1_HUMAN TT5CISB SN hCatSper; CatSper1 TT5CISB GN CATSPER1 TT5CISB FC Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte. TT5CISB SQ MDQNSVPEKAQNEADTNNADRFFRSHSSPPHHRPGHSRALHHYELHHHGVPHQRGESHHPPEFQDFHDQALSSHVHQSHHHSEARNHGRAHGPTGFGLAPSQGAVPSHRSYGEDYHDELQRDGRRHHDGSQYGGFHQQSDSHYHRGSHHGRPQYLGENLSHYSSGVPHHGEASHHGGSYLPHGPNPYSESFHHSEASHLSGLQHDESQHHQVPHRGWPHHHQVHHHGRSRHHEAHQHGKSPHHGETISPHSSVGSYQRGISDYHSEYHQGDHHPSEYHHGDHPHHTQHHYHQTHRHRDYHQHQDHHGAYHSSYLHGDYVQSTSQLSIPHTSRSLIHDAPGPAASRTGVFPYHVAHPRGSAHSMTRSSSTIRSRVTQMSKKVHTQDISTKHSEDWGKEEGQFQKRKTGRLQRTRKKGHSTNLFQWLWEKLTFLIQGFREMIRNLTQSLAFETFIFFVVCLNTVMLVAQTFAEVEIRGEWYFMALDSIFFCIYVVEALLKIIALGLSYFFDFWNNLDFFIMAMAVLDFLLMQTHSFAIYHQSLFRILKVFKSLRALRAIRVLRRLSFLTSVQEVTGTLGQSLPSIAAILILMFTCLFLFSAVLRALFRKSDPKRFQNIFTTIFTLFTLLTLDDWSLIYMDSRAQGAWYIIPILVIYIIIQYFIFLNLVITVLVDSFQTALFKGLEKAKQERAARIQEKLLEDSLTELRAAEPKEVASEGTMLKRLIEKKFGTMTEKQQELLFHYLQLVASVEQEQQKFRSQAAVIDEIVDTTFEAGEEDFRN TT5CISB TT Literature-reported TTOEGC4 ID TTOEGC4 TTOEGC4 TN Cation channel sperm-associated protein 2 (CatSper2) TTOEGC4 UP Q96P56 TTOEGC4 UC CTSR2_HUMAN TTOEGC4 SN CatSper2 TTOEGC4 GN CATSPER2 TTOEGC4 FC Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte. TTOEGC4 SQ MAAYQQEEQMQLPRADAIRSRLIDTFSLIEHLQGLSQAVPRHTIRELLDPSRQKKLVLGDQHQLVRFSIKPQRIEQISHAQRLLSRLHVRCSQRPPLSLWAGWVLECPLFKNFIIFLVFLNTIILMVEIELLESTNTKLWPLKLTLEVAAWFILLIFILEILLKWLSNFSVFWKSAWNVFDFVVTMLSLLPEVVVLVGVTGQSVWLQLLRICRVLRSLKLLAQFRQIQIIILVLVRALKSMTFLLMLLLIFFYIFAVTGVYVFSEYTRSPRQDLEYHVFFSDLPNSLVTVFILFTLDHWYALLQDVWKVPEVSRIFSSIYFILWLLLGSIIFRSIIVAMMVTNFQNIRKELNEEMARREVQLKADMFKRQIIQRRKNMSHEALTSSHSKIEDSSRGASQQRESLDLSEVSEVESNYGATEEDLITSASKTEETLSKKREYQSSSCVSSTSSSYSSSSESRFSESIGRLDWETLVHENLPGLMEMDQDDRVWPRDSLFRYFELLEKLQYNLEERKKLQEFAVQALMNLEDK TTOEGC4 TT Literature-reported TTP52ZV ID TTP52ZV TTP52ZV TN Cation channel sperm-associated protein 3 (CatSper3) TTP52ZV UP Q86XQ3 TTP52ZV UC CTSR3_HUMAN TTP52ZV SN One-repeat calcium channel-like protein; CatSper3; Ca(v)-like protein TTP52ZV GN CATSPER3 TTP52ZV FC Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte. TTP52ZV SQ MSQHRHQRHSRVISSSPVDTTSVGFCPTFKKFKRNDDECRAFVKRVIMSRFFKIIMISTVTSNAFFMALWTSYDIRYRLFRLLEFSEIFFVSICTSELSMKVYVDPINYWKNGYNLLDVIIIIVMFLPYALRQLMGKQFTYLYIADGMQSLRILKLIGYSQGIRTLITAVGQTVYTVASVLLLLFLLMYIFAILGFCLFGSPDNGDHDNWGNLAAAFFTLFSLATVDGWTDLQKQLDNREFALSRAFTIIFILLASFIFLNMFVGVMIMHTEDSIRKFERELMLEQQEMLMGEKQVILQRQQEEISRLMHIQKNADCTSFSELVENFKKTLSHTDPMVLDDFGTSLPFIDIYFSTLDYQDTTVHKLQELYYEIVHVLSLMLEDLPQEKPQSLEKVDEK TTP52ZV TT Literature-reported TTBSUAR ID TTBSUAR TTBSUAR TN CDK inhibitor 1C p57Kip2 (CDKN1C) TTBSUAR UP P49918 TTBSUAR UC CDN1C_HUMAN TTBSUAR SN P57KIP2; P57(KIP2); KIP2; Cyclin-dependent kinase inhibitor p57; Cyclin-dependent kinase inhibitor 1C TTBSUAR GN CDKN1C TTBSUAR FC Negative regulator of cell proliferation. May play a role in maintenance of the non-proliferative state throughout life. Potent tight-binding inhibitor of several G1 cyclin/CDK complexes (cyclin E-CDK2, cyclin D2-CDK4, and cyclin A-CDK2) and, to lesser extent, of the mitotic cyclin B-CDC2. TTBSUAR SQ MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR TTBSUAR TT Literature-reported TTHRE05 ID TTHRE05 TTHRE05 TN Cell surface glycoprotein MUC18 (MCAM) TTHRE05 UP P43121 TTHRE05 UC MUC18_HUMAN TTHRE05 SN S-endo 1 endothelial-associated antigen; Melanoma-associated antigen MUC18; Melanoma-associated antigen A32; Melanoma cell adhesion molecule; Melanoma adhesion molecule; MUC18; Cell surface glycoprotein P1H12; CD146 antigen; CD146 TTHRE05 GN MCAM TTHRE05 FC Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration. Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. TTHRE05 SQ MGLPRLVCAFLLAACCCCPRVAGVPGEAEQPAPELVEVEVGSTALLKCGLSQSQGNLSHVDWFSVHKEKRTLIFRVRQGQGQSEPGEYEQRLSLQDRGATLALTQVTPQDERIFLCQGKRPRSQEYRIQLRVYKAPEEPNIQVNPLGIPVNSKEPEEVATCVGRNGYPIPQVIWYKNGRPLKEEKNRVHIQSSQTVESSGLYTLQSILKAQLVKEDKDAQFYCELNYRLPSGNHMKESREVTVPVFYPTEKVWLEVEPVGMLKEGDRVEIRCLADGNPPPHFSISKQNPSTREAEEETTNDNGVLVLEPARKEHSGRYECQGLDLDTMISLLSEPQELLVNYVSDVRVSPAAPERQEGSSLTLTCEAESSQDLEFQWLREETGQVLERGPVLQLHDLKREAGGGYRCVASVPSIPGLNRTQLVNVAIFGPPWMAFKERKVWVKENMVLNLSCEASGHPRPTISWNVNGTASEQDQDPQRVLSTLNVLVTPELLETGVECTASNDLGKNTSILFLELVNLTTLTPDSNTTTGLSTSTASPHTRANSTSTERKLPEPESRGVVIVAVIVCILVLAVLGAVLYFLYKKGKLPCRRSGKQEITLPPSRKSELVVEVKSDKLPEEMGLLQGSSGDKRAPGDQGEKYIDLRH TTHRE05 TT Literature-reported TTHRE05 FM Transmembrane protein TT8MI6U ID TT8MI6U TT8MI6U TN Centrosomal protein (CNTLN) TT8MI6U UP Q9NXG0 TT8MI6U UC CNTLN_HUMAN TT8MI6U SN Centlein; C9orf39; C9orf101 TT8MI6U GN CNTLN TT8MI6U FC Required for centrosome cohesion and recruitment of CEP68 to centrosomes. TT8MI6U SQ MAARSPPSPHPSPPARQLGPRSPRVGRGAEVHAMRSEASGFAGAAREVVADESDKIWVGEEGSGGRRGPGGAAPAHAPLLSAPMGSRRLEGISVEEAMVTRTQLLEEELSSLKEELALCQADKEFVWSLWKRLQVTNPDLTQVVSLVVEREKQKSEAKDRKVLEILQVKDAKIQEFEQRESVLKQEINDLVKRKIAVDEENAFLRKEFSDLEKKFKDKSQEIKDTKECVQNKEEQNRLVIKNLEEENKKLSTRCTDLLNDLEKLRKQEAHLRKEKYSTDAKIKTFEDNLIEARKEVEVSQSKYNALSLQLSNKQTELIQKDMDITLVRKELQELQNLYKQNSTHTAQQAELIQQLQVLNMDTQKVLRNQEDVHTAESISYQKLYNELHICFETTKSNEAMLRQSVTNLQDQLLQKEQENAKLKEKLQESQGAPLPLPQESDPDYSAQVPHRPSLSSLETLMVSQKSEIEYLQEKLKIANEKLSENISANKGFSRKSIMTSAEGKHKEPPVKRSRSLSPKSSFTDSEELQKLRKAERKIENLEKALQLKSQENDELRDAHEKRKERLQMLQTNYRAVKEQLKQWEEGSGMTEIRKIKRADPQQLRQEDSDAVWNELAYFKRENQELMIQKMNLEEELDELKVHISIDKAAIQELNRCVAERREEQLFRSGEDDEVKRSTPEKNGKEMLEQTLQKVTELENRLKSFEKRSRKLKEGNKKLMKENDFLKSLLKQQQEDTETREKELEQIIKGSKDVEKENTELQVKISELETEVTSLRRQVAEANALRNENEELINPMEKSHQSADRAKSEMATMKVRSGRYDCKTTMTKVKFKAAKKNCSVGRHHTVLNHSIKVMSNVFENLSKDGWEDVSESSSDSEAQTSQTLGTIIVETSQKISPTEDGKDQKESDPTEDSQTQGKEIVQTYLNIDGKTPKDYFHDKNAKKPTFQKKNCKMQKSSHTAVPTRVNREKYKNITAQKSSSNIILLRERIISLQQQNSVLQNAKKTAELSVKEYKEVNEKLLHQQQVSDQRFQTSRQTIKKLNLDLAGLRKEKEDLLKKLESSSEITSLAEENSQVTFPRIQVTSLSPSRSMDLEMKQLQYKLKNATNELTKQSSNVKTLKFELLAKEEHIKEMHEKISRMERDITMKRHLIEDLKFRQKVNLESNKSFSEMLQNLDKKVKTLTEECSNKKVSIDSLKQRLNVAVKEKSQYEQMYQKSKEELEKKDLKLTLLVSRISETESAMAEIETAASKQLQELALQSEQVLEGAQKTLLLANEKVEEFTTFVKALAKELQNDVHVVRRQIRELKKMKKNRDACKTSTHKAQTLAASILNISRSDLEEILDTEDQVEIEKTKIDAENDKEWMLYIQKLLEGQSLTLSPRLKCNGAIVAHQNLRLPDSSSSASAS TT8MI6U TT Literature-reported TT4UGZL ID TT4UGZL TT4UGZL TN Chemerin receptor (CMKLR1) TT4UGZL UP Q99788 TT4UGZL UC CML1_HUMAN TT4UGZL SN G-protein coupled receptor DEZ; G-protein coupled receptor ChemR23; DEZ; Chemokine-like receptor 1; CHEMR23 TT4UGZL GN CMKLR1 TT4UGZL FC Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 induces activation of intracellular signaling molecules, such as SKY, MAPK1/3 (ERK1/2), MAPK14/P38MAPK and PI3K leading to multifunctional effects, like, reduction of immune responses, enhancing of adipogenesis and angionesis. Resolvin E1 down-regulates cytokine production in macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-kappa-B. Positively regulates adipogenesis and adipocyte metabolism. Acts as a coreceptor for several SIV strains (SIVMAC316, SIVMAC239, SIVMACL7E-FR and SIVSM62A), as well as a primary HIV-1 strain (92UG024-2). TT4UGZL SQ MRMEDEDYNTSISYGDEYPDYLDSIVVLEDLSPLEARVTRIFLVVVYSIVCFLGILGNGLVIIIATFKMKKTVNMVWFLNLAVADFLFNVFLPIHITYAAMDYHWVFGTAMCKISNFLLIHNMFTSVFLLTIISSDRCISVLLPVWSQNHRSVRLAYMACMVIWVLAFFLSSPSLVFRDTANLHGKISCFNNFSLSTPGSSSWPTHSQMDPVGYSRHMVVTVTRFLCGFLVPVLIITACYLTIVCKLQRNRLAKTKKPFKIIVTIIITFFLCWCPYHTLNLLELHHTAMPGSVFSLGLPLATALAIANSCMNPILYVFMGQDFKKFKVALFSRLVNALSEDTGHSSYPSHRSFTKMSSMNERTSMNERETGML TT4UGZL TT Literature-reported TT7MYXI ID TT7MYXI TT7MYXI TN Chondroitin sulfate proteoglycan 4 (CSPG4) TT7MYXI UP Q6UVK1 TT7MYXI UC CSPG4_HUMAN TT7MYXI SN Melanoma-associated chondroitin sulfate proteoglycan; Melanoma chondroitin sulfate proteoglycan; MCSP; Chondroitin sulfate proteoglycan NG2 TT7MYXI GN CSPG4 TT7MYXI FC Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades. TT7MYXI SQ MQSGPRPPLPAPGLALALTLTMLARLASAASFFGENHLEVPVATALTDIDLQLQFSTSQPEALLLLAAGPADHLLLQLYSGRLQVRLVLGQEELRLQTPAETLLSDSIPHTVVLTVVEGWATLSVDGFLNASSAVPGAPLEVPYGLFVGGTGTLGLPYLRGTSRPLRGCLHAATLNGRSLLRPLTPDVHEGCAEEFSASDDVALGFSGPHSLAAFPAWGTQDEGTLEFTLTTQSRQAPLAFQAGGRRGDFIYVDIFEGHLRAVVEKGQGTVLLHNSVPVADGQPHEVSVHINAHRLEISVDQYPTHTSNRGVLSYLEPRGSLLLGGLDAEASRHLQEHRLGLTPEATNASLLGCMEDLSVNGQRRGLREALLTRNMAAGCRLEEEEYEDDAYGHYEAFSTLAPEAWPAMELPEPCVPEPGLPPVFANFTQLLTISPLVVAEGGTAWLEWRHVQPTLDLMEAELRKSQVLFSVTRGARHGELELDIPGAQARKMFTLLDVVNRKARFIHDGSEDTSDQLVLEVSVTARVPMPSCLRRGQTYLLPIQVNPVNDPPHIIFPHGSLMVILEHTQKPLGPEVFQAYDPDSACEGLTFQVLGTSSGLPVERRDQPGEPATEFSCRELEAGSLVYVHRGGPAQDLTFRVSDGLQASPPATLKVVAIRPAIQIHRSTGLRLAQGSAMPILPANLSVETNAVGQDVSVLFRVTGALQFGELQKQGAGGVEGAEWWATQAFHQRDVEQGRVRYLSTDPQHHAYDTVENLALEVQVGQEILSNLSFPVTIQRATVWMLRLEPLHTQNTQQETLTTAHLEATLEEAGPSPPTFHYEVVQAPRKGNLQLQGTRLSDGQGFTQDDIQAGRVTYGATARASEAVEDTFRFRVTAPPYFSPLYTFPIHIGGDPDAPVLTNVLLVVPEGGEGVLSADHLFVKSLNSASYLYEVMERPRHGRLAWRGTQDKTTMVTSFTNEDLLRGRLVYQHDDSETTEDDIPFVATRQGESSGDMAWEEVRGVFRVAIQPVNDHAPVQTISRIFHVARGGRRLLTTDDVAFSDADSGFADAQLVLTRKDLLFGSIVAVDEPTRPIYRFTQEDLRKRRVLFVHSGADRGWIQLQVSDGQHQATALLEVQASEPYLRVANGSSLVVPQGGQGTIDTAVLHLDTNLDIRSGDEVHYHVTAGPRWGQLVRAGQPATAFSQQDLLDGAVLYSHNGSLSPRDTMAFSVEAGPVHTDATLQVTIALEGPLAPLKLVRHKKIYVFQGEAAEIRRDQLEAAQEAVPPADIVFSVKSPPSAGYLVMVSRGALADEPPSLDPVQSFSQEAVDTGRVLYLHSRPEAWSDAFSLDVASGLGAPLEGVLVELEVLPAAIPLEAQNFSVPEGGSLTLAPPLLRVSGPYFPTLLGLSLQVLEPPQHGALQKEDGPQARTLSAFSWRMVEEQLIRYVHDGSETLTDSFVLMANASEMDRQSHPVAFTVTVLPVNDQPPILTTNTGLQMWEGATAPIPAEALRSTDGDSGSEDLVYTIEQPSNGRVVLRGAPGTEVRSFTQAQLDGGLVLFSHRGTLDGGFRFRLSDGEHTSPGHFFRVTAQKQVLLSLKGSQTLTVCPGSVQPLSSQTLRASSSAGTDPQLLLYRVVRGPQLGRLFHAQQDSTGEALVNFTQAEVYAGNILYEHEMPPEPFWEAHDTLELQLSSPPARDVAATLAVAVSFEAACPQRPSHLWKNKGLWVPEGQRARITVAALDASNLLASVPSPQRSEHDVLFQVTQFPSRGQLLVSEEPLHAGQPHFLQSQLAAGQLVYAHGGGGTQQDGFHFRAHLQGPAGASVAGPQTSEAFAITVRDVNERPPQPQASVPLRLTRGSRAPISRAQLSVVDPDSAPGEIEYEVQRAPHNGFLSLVGGGLGPVTRFTQADVDSGRLAFVANGSSVAGIFQLSMSDGASPPLPMSLAVDILPSAIEVQLRAPLEVPQALGRSSLSQQQLRVVSDREEPEAAYRLIQGPQYGHLLVGGRPTSAFSQFQIDQGEVVFAFTNFSSSHDHFRVLALARGVNASAVVNVTVRALLHVWAGGPWPQGATLRLDPTVLDAGELANRTGSVPRFRLLEGPRHGRVVRVPRARTEPGGSQLVEQFTQQDLEDGRLGLEVGRPEGRAPGPAGDSLTLELWAQGVPPAVASLDFATEPYNAARPYSVALLSVPEAARTEAGKPESSTPTGEPGPMASSPEPAVAKGGFLSFLEANMFSVIIPMCLVLLLLALILPLLFYLRKRNKTGKHDVQVLTAKPRNGLAGDTETFRKVEPGQAIPLTAVPGQGPPPGGQPDPELLQFCRTPNPALKNGQYWV TT7MYXI TT Literature-reported TTHJVXA ID TTHJVXA TTHJVXA TN Clostridium botulinum Botulinum neurotoxin (CB bot) TTHJVXA UP P0DPI0; P10844; Q00496 TTHJVXA UC BXA1_CLOBH; BXB_CLOBO; BXE_CLOBO TTHJVXA SN Botulinum neurotoxin; Bontoxilysin; BoNT TTHJVXA GN CB botA; CB botB; CB botE TTHJVXA FC Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-|-Arg- 198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure. TTHJVXA SQ MPFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYNRQIERSSRTLGCSWEFIPVDDGWGERPL TTHJVXA TT Literature-reported TTN8T0E ID TTN8T0E TTN8T0E TN Clusterin (CLU) TTN8T0E UP P10909 TTN8T0E UC CLUS_HUMAN TTN8T0E SN Testosteronerepressed prostate message 2; Testosterone-repressed prostate message 2; TRPM-2; NA1/NA2; Ku70binding protein 1; Ku70-binding protein 1; KUB1; Complementassociated protein SP40,40; Complement-associated protein SP-40,40; Complement cytolysis inhibitor; Clusterin alpha chain; CLI; Apolipoprotein J; ApoJ; Apo-J; Agingassociated gene 4 protein; Aging-associated gene 4 protein; AAG4 TTN8T0E GN CLU TTN8T0E FC Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. TTN8T0E SQ MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE TTN8T0E TT Literature-reported TTBCOKN ID TTBCOKN TTBCOKN TN Collagen VII (COL7A1) TTBCOKN UP Q02388 TTBCOKN UC CO7A1_HUMAN TTBCOKN SN Longchain collagen; Long-chain collagen; LC collagen; Collagen alpha1(VII) chain; Collagen alpha-1(VII) chain TTBCOKN GN COL7A1 TTBCOKN FC Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen. TTBCOKN SQ MTLRLLVAALCAGILAEAPRVRAQHRERVTCTRLYAADIVFLLDGSSSIGRSNFREVRSFLEGLVLPFSGAASAQGVRFATVQYSDDPRTEFGLDALGSGGDVIRAIRELSYKGGNTRTGAAILHVADHVFLPQLARPGVPKVCILITDGKSQDLVDTAAQRLKGQGVKLFAVGIKNADPEELKRVASQPTSDFFFFVNDFSILRTLLPLVSRRVCTTAGGVPVTRPPDDSTSAPRDLVLSEPSSQSLRVQWTAASGPVTGYKVQYTPLTGLGQPLPSERQEVNVPAGETSVRLRGLRPLTEYQVTVIALYANSIGEAVSGTARTTALEGPELTIQNTTAHSLLVAWRSVPGATGYRVTWRVLSGGPTQQQELGPGQGSVLLRDLEPGTDYEVTVSTLFGRSVGPATSLMARTDASVEQTLRPVILGPTSILLSWNLVPEARGYRLEWRRETGLEPPQKVVLPSDVTRYQLDGLQPGTEYRLTLYTLLEGHEVATPATVVPTGPELPVSPVTDLQATELPGQRVRVSWSPVPGATQYRIIVRSTQGVERTLVLPGSQTAFDLDDVQAGLSYTVRVSARVGPREGSASVLTVRREPETPLAVPGLRVVVSDATRVRVAWGPVPGASGFRISWSTGSGPESSQTLPPDSTATDITGLQPGTTYQVAVSVLRGREEGPAAVIVARTDPLGPVRTVHVTQASSSSVTITWTRVPGATGYRVSWHSAHGPEKSQLVSGEATVAELDGLEPDTEYTVHVRAHVAGVDGPPASVVVRTAPEPVGRVSRLQILNASSDVLRITWVGVTGATAYRLAWGRSEGGPMRHQILPGNTDSAEIRGLEGGVSYSVRVTALVGDREGTPVSIVVTTPPEAPPALGTLHVVQRGEHSLRLRWEPVPRAQGFLLHWQPEGGQEQSRVLGPELSSYHLDGLEPATQYRVRLSVLGPAGEGPSAEVTARTESPRVPSIELRVVDTSIDSVTLAWTPVSRASSYILSWRPLRGPGQEVPGSPQTLPGISSSQRVTGLEPGVSYIFSLTPVLDGVRGPEASVTQTPVCPRGLADVVFLPHATQDNAHRAEATRRVLERLVLALGPLGPQAVQVGLLSYSHRPSPLFPLNGSHDLGIILQRIRDMPYMDPSGNNLGTAVVTAHRYMLAPDAPGRRQHVPGVMVLLVDEPLRGDIFSPIREAQASGLNVVMLGMAGADPEQLRRLAPGMDSVQTFFAVDDGPSLDQAVSGLATALCQASFTTQPRPEPCPVYCPKGQKGEPGEMGLRGQVGPPGDPGLPGRTGAPGPQGPPGSATAKGERGFPGADGRPGSPGRAGNPGTPGAPGLKGSPGLPGPRGDPGERGPRGPKGEPGAPGQVIGGEGPGLPGRKGDPGPSGPPGPRGPLGDPGPRGPPGLPGTAMKGDKGDRGERGPPGPGEGGIAPGEPGLPGLPGSPGPQGPVGPPGKKGEKGDSEDGAPGLPGQPGSPGEQGPRGPPGAIGPKGDRGFPGPLGEAGEKGERGPPGPAGSRGLPGVAGRPGAKGPEGPPGPTGRQGEKGEPGRPGDPAVVGPAVAGPKGEKGDVGPAGPRGATGVQGERGPPGLVLPGDPGPKGDPGDRGPIGLTGRAGPPGDSGPPGEKGDPGRPGPPGPVGPRGRDGEVGEKGDEGPPGDPGLPGKAGERGLRGAPGVRGPVGEKGDQGDPGEDGRNGSPGSSGPKGDRGEPGPPGPPGRLVDTGPGAREKGEPGDRGQEGPRGPKGDPGLPGAPGERGIEGFRGPPGPQGDPGVRGPAGEKGDRGPPGLDGRSGLDGKPGAAGPSGPNGAAGKAGDPGRDGLPGLRGEQGLPGPSGPPGLPGKPGEDGKPGLNGKNGEPGDPGEDGRKGEKGDSGASGREGRDGPKGERGAPGILGPQGPPGLPGPVGPPGQGFPGVPGGTGPKGDRGETGSKGEQGLPGERGLRGEPGSVPNVDRLLETAGIKASALREIVETWDESSGSFLPVPERRRGPKGDSGEQGPPGKEGPIGFPGERGLKGDRGDPGPQGPPGLALGERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEAGRPGERGERGEKGERGEQGRDGPPGLPGTPGPPGPPGPKVSVDEPGPGLSGEQGPPGLKGAKGEPGSNGDQGPKGDRGVPGIKGDRGEPGPRGQDGNPGLPGERGMAGPEGKPGLQGPRGPPGPVGGHGDPGPPGAPGLAGPAGPQGPSGLKGEPGETGPPGRGLTGPTGAVGLPGPPGPSGLVGPQGSPGLPGQVGETGKPGAPGRDGASGKDGDRGSPGVPGSPGLPGPVGPKGEPGPTGAPGQAVVGLPGAKGEKGAPGGLAGDLVGEPGAKGDRGLPGPRGEKGEAGRAGEPGDPGEDGQKGAPGPKGFKGDPGVGVPGSPGPPGPPGVKGDLGLPGLPGAPGVVGFPGQTGPRGEMGQPGPSGERGLAGPPGREGIPGPLGPPGPPGSVGPPGASGLKGDKGDPGVGLPGPRGERGEPGIRGEDGRPGQEGPRGLTGPPGSRGERGEKGDVGSAGLKGDKGDSAVILGPPGPRGAKGDMGERGPRGLDGDKGPRGDNGDPGDKGSKGEPGDKGSAGLPGLRGLLGPQGQPGAAGIPGDPGSPGKDGVPGIRGEKGDVGFMGPRGLKGERGVKGACGLDGEKGDKGEAGPPGRPGLAGHKGEMGEPGVPGQSGAPGKEGLIGPKGDRGFDGQPGPKGDQGEKGERGTPGIGGFPGPSGNDGSAGPPGPPGSVGPRGPEGLQGQKGERGPPGERVVGAPGVPGAPGERGEQGRPGPAGPRGEKGEAALTEDDIRGFVRQEMSQHCACQGQFIASGSRPLPSYAADTAGSQLHAVPVLRVSHAEEEERVPPEDDEYSEYSEYSVEEYQDPEAPWDSDDPCSLPLDEGSCTAYTLRWYHRAVTGSTEACHPFVYGGCGGNANRFGTREACERRCPPRVVQSQGTGTAQD TTBCOKN TT Literature-reported TT3PKZE ID TT3PKZE TT3PKZE TN Corticotropin-releasing factor binding protein (CRHBP) TT3PKZE UP P24387 TT3PKZE UC CRHBP_HUMAN TT3PKZE SN Corticotropin-releasing hormone-binding protein; Corticotropin-releasing factor-binding protein; CRH-BP; CRFBP; CRF-binding protein; CRF-BP TT3PKZE GN CRHBP TT3PKZE FC May prevent inappropriate pituitary-adrenal stimulation in pregnancy. Binds CRF and inactivates it. TT3PKZE SQ MSPNFKLQCHFILIFLTALRGESRYLELREAADYDPFLLFSANLKRELAGEQPYRRALRCLDMLSLQGQFTFTADRPQLHCAAFFISEPEEFITIHYDQVSIDCQGGDFLKVFDGWILKGEKFPSSQDHPLPSAERYIDFCESGLSRRSIRSSQNVAMIFFRVHEPGNGFTLTIKTDPNLFPCNVISQTPNGKFTLVVPHQHRNCSFSIIYPVVIKISDLTLGHVNGLQLKKSSAGCEGIGDFVELLGGTGLDPSKMTPLADLCYPFHGPAQMKVGCDNTVVRMVSSGKHVNRVTFEYRQLEPYELENPNGNSIGEFCLSGL TT3PKZE TT Literature-reported TT3PKZE FM CRF-binding protein family TT4GO0F ID TT4GO0F TT4GO0F TN CREB-regulated transcription coactivator 1 (TORC1) TT4GO0F UP Q6UUV9 TT4GO0F UC CRTC1_HUMAN TT4GO0F SN WAMTP1; Transducer of regulated cAMP response elementbinding protein 1; Transducer of regulated cAMP response element-binding protein 1; Transducer of CREB protein 1; TORC1; TORC-1; Mucoepidermoid carcinoma translocated protein 1; MECT1; KIAA0616; CREBregulated transcription coactivator 1 TT4GO0F GN CRTC1 TT4GO0F FC Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PGC1alpha and inducer of mitochondrial biogenesis in muscle cells. In the hippocampus, involved in late-phase long-term potentiation (L-LTP) maintenance at the Schaffer collateral-CA1 synapses. May be required for dendritic growth of developing cortical neurons. In concert with SIK1, regulates the light-induced entrainment of the circadian clock. In response to light stimulus, coactivates the CREB-mediated transcription of PER1 which plays an important role in the photic entrainment of the circadian clock. Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. TT4GO0F SQ MATSNNPRKFSEKIALHNQKQAEETAAFEEVMKDLSLTRAARLQLQKSQYLQLGPSRGQYYGGSLPNVNQIGSGTMDLPFQTPFQSSGLDTSRTTRHHGLVDRVYRERGRLGSPHRRPLSVDKHGRQADSCPYGTMYLSPPADTSWRRTNSDSALHQSTMTPTQPESFSSGSQDVHQKRVLLLTVPGMEETTSEADKNLSKQAWDTKKTGSRPKSCEVPGINIFPSADQENTTALIPATHNTGGSLPDLTNIHFPSPLPTPLDPEEPTFPALSSSSSTGNLAANLTHLGIGGAGQGMSTPGSSPQHRPAGVSPLSLSTEARRQQASPTLSPLSPITQAVAMDALSLEQQLPYAFFTQAGSQQPPPQPQPPPPPPPASQQPPPPPPPQAPVRLPPGGPLLPSASLTRGPQPPPLAVTVPSSLPQSPPENPGQPSMGIDIASAPALQQYRTSAGSPANQSPTSPVSNQGFSPGSSPQHTSTLGSVFGDAYYEQQMAARQANALSHQLEQFNMMENAISSSSLYSPGSTLNYSQAAMMGLTGSHGSLPDSQQLGYASHSGIPNIILTVTGESPPSLSKELTSSLAGVGDVSFDSDSQFPLDELKIDPLTLDGLHMLNDPDMVLADPATEDTFRMDRL TT4GO0F TT Clinical trial TT4GO0F FM Transducer of regulated CREB TT5MLZR ID TT5MLZR TT5MLZR TN Cryptochrome circadian clock 1 (CRY1) TT5MLZR UP Q16526 TT5MLZR UC CRY1_HUMAN TT5MLZR SN PHLL1; Cryptochrome-1 TT5MLZR GN CRY1 TT5MLZR FC The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. More potent transcriptional repressor in cerebellum and liver than CRY2, though more effective in lengthening the period of the SCN oscillator. On its side, CRY2 seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY2, is dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus. Interacts with CLOCK-ARNTL/BMAL1 independently of PER proteins and is found at CLOCK-ARNTL/BMAL1-bound sites, suggesting that CRY may act as a molecular gatekeeper to maintain CLOCK-ARNTL/BMAL1 in a poised and repressed state until the proper time for transcriptional activation. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1. Represses the CLOCK-ARNTL/BMAL1 induced transcription of ATF4, MTA1, KLF10 and NAMPT. May repress circadian target genes expression in collaboration with HDAC1 and HDAC2 through histone deacetylation. Mediates the clock-control activation of ATR and modulates ATR-mediated DNA damage checkpoint. In liver, mediates circadian regulation of cAMP signaling and gluconeogenesis by binding to membrane-coupled G proteins and blocking glucagon-mediated increases in intracellular cAMP concentrations and CREB1 phosphorylation. Inhibits hepatic gluconeogenesis by decreasing nuclear FOXO1 levels that downregulates gluconeogenic gene expression. Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4. Represses PPARD and its target genes in the skeletal muscle and limits exercise capacity. Plays an essential role in the generation of circadian rhythms in the retina. Represses the transcriptional activity of NR1I2. Transcriptional repressor which forms a core component of the circadian clock. TT5MLZR SQ MGVNAVHWFRKGLRLHDNPALKECIQGADTIRCVYILDPWFAGSSNVGINRWRFLLQCLEDLDANLRKLNSRLFVIRGQPADVFPRLFKEWNITKLSIEYDSEPFGKERDAAIKKLATEAGVEVIVRISHTLYDLDKIIELNGGQPPLTYKRFQTLISKMEPLEIPVETITSEVIEKCTTPLSDDHDEKYGVPSLEELGFDTDGLSSAVWPGGETEALTRLERHLERKAWVANFERPRMNANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYKKVKKNSSPPLSLYGQLLWREFFYTAATNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWISWEEGMKVFEELLLDADWSINAGSWMWLSCSSFFQQFFHCYCPVGFGRRTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPEGIQKVAKCLIGVNYPKPMVNHAEASRLNIERMKQIYQQLSRYRGLGLLASVPSNPNGNGGFMGYSAENIPGCSSSGSCSQGSGILHYAHGDSQQTHLLKQGRSSMGTGLSGGKRPSQEEDTQSIGPKVQRQSTN TT5MLZR TT Preclinical TT1K65C ID TT1K65C TT1K65C TN C-terminal tensin-like protein (Cten) TT1K65C UP Q8IZW8 TT1K65C UC TENS4_HUMAN TT1K65C SN Tensin-4; TNS4 TT1K65C GN TNS4 TT1K65C FC May be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. May promote apoptosis, via its cleavage by caspase-3. TT1K65C SQ MSQVMSSPLLAGGHAVSLAPCDEPRRTLHPAPSPSLPPQCSYYTTEGWGAQALMAPVPCMGPPGRLQQAPQVEAKATCFLPSPGEKALGTPEDLDSYIDFSLESLNQMILELDPTFQLLPPGTGGSQAELAQSTMSMRKKEESEALDIKYIEVTSARSRCHDGPQHCSSPSVTPPFGSLRSGGLLLSRDVPRETRSSSESLIFSGNQGRGHQRPLPPSEGLSPRPPNSPSISIPCMGSKASSPHGLGSPLVASPRLEKRLGGLAPQRGSRISVLSASPVSDVSYMFGSSQSLLHSSNSSHQSSSRSLESPANSSSSLHSLGSVSLCTRPSDFQAPRNPTLTMGQPRTPHSPPLAKEHASSCPPSITNSMVDIPIVLINGCPEPGSSPPQRTPGHQNSVQPGAASPSNPCPATRSNSQTLSDAPFTTCPEGPARDMQPTMKFVMDTSKYWFKPNITREQAIELLRKEEPGAFVIRDSSSYRGSFGLALKVQEVPASAQSRPGEDSNDLIRHFLIESSAKGVHLKGADEEPYFGSLSAFVCQHSIMALALPCKLTIPQRELGGADGASDSTDSPASCQKKSAGCHTLYLSSVSVETLTGALAVQKAISTTFERDILPTPTVVHFKVTEQGITLTDVQRKVFFRRHYPLTTLRFCGMDPEQRKWQKYCKPSWIFGFVAKSQTEPQENVCHLFAEYDMVQPASQVIGLVTALLQDAERM TT1K65C TT Literature-reported TTUTKV4 ID TTUTKV4 TTUTKV4 TN Cytomegalovirus Phosphorylated tegument protein UL51 homolog (CMV pUL71) TTUTKV4 UP F5HEA3 (phosphorylated) TTUTKV4 UC TEG7_HCMVM TTUTKV4 SN Tegument protein UL51 homolog TTUTKV4 GN CMV pUL71 TTUTKV4 FC Plays several roles during the time course of infection, including egress of virus particles from the perinuclear space and secondary envelopment of cytoplasmic capsids that bud into specific trans-Golgi network (TGN)-derived membranes. TTUTKV4 SQ MQLAQRLCELLMCRRKAAPVADYVLLQPSEDVELRELQAFLDENFKQLEITPADLRTFSRDTDVVNHLLKLLPLYRQCQSKCAFLKGYLSEGCLPHTRPAAEVECKKSQRILEALDILILKLVVGEFAMSEADSLEMLLDKFSTDQASLVEVQRVMGLVDMDCEKSAYMLEAGAAATVAPPTPPAVVQGESGVREDGETVAAVSAFACSSVSDSLIPEETGVTRPMMSLAHINTVSCPTVMRFDQRLLEEGDEEDEVTVMSPSPEPVQQQPPVEPVQQQPQGRGSHRRRYKESAPQETLPTNHEREILDLMRHSPDVPREAVMSPTMVTIPPPQIPFVGSARELRGVKKKKPTAAALLSSA TTUTKV4 TT Literature-reported TTB3XAN ID TTB3XAN TTB3XAN TN Decorin (DCN) TTB3XAN UP P07585 TTB3XAN UC PGS2_HUMAN TTB3XAN SN SLRR1B; PGS2; PG40; PG-S2; Bone proteoglycan II TTB3XAN GN DCN TTB3XAN FC May affect the rate of fibrils formation. TTB3XAN SQ MKATIILLLLAQVSWAGPFQQRGLFDFMLEDEASGIGPEVPDDRDFEPSLGPVCPFRCQCHLRVVQCSDLGLDKVPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKVSPGAFTPLVKLERLYLSKNQLKELPEKMPKTLQELRAHENEITKVRKVTFNGLNQMIVIELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITSIPQGLPPSLTELHLDGNKISRVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLDNNKLTRVPGGLAEHKYIQVVYLHNNNISVVGSSDFCPPGHNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRSAIQLGNYK TTB3XAN TT Literature-reported TTN0Z6H ID TTN0Z6H TTN0Z6H TN Disheveled-associated activator of morphogenesis 2 (DAAM2) TTN0Z6H UP Q86T65 TTN0Z6H UC DAAM2_HUMAN TTN0Z6H SN KIAA0381; Disheveledassociated activator of morphogenesis 2 TTN0Z6H GN DAAM2 TTN0Z6H FC Acts downstream of Wnt ligands and upstream of beta-catenin (CTNNB1). Required for canonical Wnt signaling pathway during patterning in the dorsal spinal cord by promoting the aggregation of Disheveled (Dvl) complexes, thereby clustering and formation of Wnt receptor signalosomes and potentiating Wnt activity. During dorsal patterning of the spinal cord, inhibits oligodendrocytes differentiation via interaction with PIP5K1A. Also regulates non-canonical Wnt signaling pathway. Acts downstream of PITX2 in the developing gut and is required for left/right asymmetry within dorsal mesentery: affects mesenchymal condensation by lengthening cadherin-based junctions through WNT5A and non-canonical Wnt signaling, inducing polarized condensation in the left dorsal mesentery necessary to initiate gut rotation. Together with DAAM1, required for myocardial maturation and sarcomere assembly. Key regulator of the Wnt signaling pathway, which is required for various processes during development, such as dorsal patterning, determination of left/right symmetry or myelination in the central nervous system. TTN0Z6H SQ MAPRKRSHHGLGFLCCFGGSDIPEINLRDNHPLQFMEFSSPIPNAEELNIRFAELVDELDLTDKNREAMFALPPEKKWQIYCSKKKEQEDPNKLATSWPDYYIDRINSMAAMQSLYAFDEEETEMRNQVVEDLKTALRTQPMRFVTRFIELEGLTCLLNFLRSMDHATCESRIHTSLIGCIKALMNNSQGRAHVLAQPEAISTIAQSLRTENSKTKVAVLEILGAVCLVPGGHKKVLQAMLHYQVYAAERTRFQTLLNELDRSLGRYRDEVNLKTAIMSFINAVLNAGAGEDNLEFRLHLRYEFLMLGIQPVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKYTEAYPCLLSVLHHCLQMPYKRNGGYFQQWQLLDRILQQIVLQDERGVDPDLAPLENFNVKNIVNMLINENEVKQWRDQAEKFRKEHMELVSRLERKERECETKTLEKEEMMRTLNKMKDKLARESQELRQARGQVAELVAQLSELSTGPVSSPPPPGGPLTLSSSMTTNDLPPPPPPLPFACCPPPPPPPLPPGGPPTPPGAPPCLGMGLPLPQDPYPSSDVPLRKKRVPQPSHPLKSFNWVKLNEERVPGTVWNEIDDMQVFRILDLEDFEKMFSAYQRHQKELGSTEDIYLASRKVKELSVIDGRRAQNCIILLSKLKLSNEEIRQAILKMDEQEDLAKDMLEQLLKFIPEKSDIDLLEEHKHEIERMARADRFLYEMSRIDHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELVRSKRLRQMLEVILAIGNFMNKGQRGGAYGFRVASLNKIADTKSSIDRNISLLHYLIMILEKHFPDILNMPSELQHLPEAAKVNLAELEKEVGNLRRGLRAVEVELEYQRRQVREPSDKFVPVMSDFITVSSFSFSELEDQLNEARDKFAKALMHFGEHDSKMQPDEFFGIFDTFLQAFSEARQDLEAMRRRKEEEERRARMEAMLKEQRERERWQRQRKVLAAGSSLEEGGEFDDLVSALRSGEVFDKDLCKLKRSRKRSGSQALEVTRERAINRLNY TTN0Z6H TT Literature-reported TTN0Z6H FM Formin homology family TTH5GAC ID TTH5GAC TTH5GAC TN DNA-directed RNA polymerase I (RNAP I) TTH5GAC UP O95602; Q9H9Y6 TTH5GAC UC RPA1_HUMAN; RPA2_HUMAN TTH5GAC SN RPA; RNA polymerase I TTH5GAC GN POLR1A; POLR1B TTH5GAC FC DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. Pol I is composed of mobile elements and RPA1/RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft TTH5GAC SQ MLISKNMPWRRLQGISFGMYSAEELKKLSVKSITNPRYLDSLGNPSANGLYDLALGPADSKEVCSTCVQDFSNCSGHLGHIELPLTVYNPLLFDKLYLLLRGSCLNCHMLTCPRAVIHLLLCQLRVLEVGALQAVYELERILNRFLEENPDPSASEIREELEQYTTEIVQNNLLGSQGAHVKNVCESKSKLIALFWKAHMNAKRCPHCKTGRSVVRKEHNSKLTITFPAMVHRTAGQKDSEPLGIEEAQIGKRGYLTPTSAREHLSALWKNEGFFLNYLFSGMDDDGMESRFNPSVFFLDFLVVPPSRYRPVSRLGDQMFTNGQTVNLQAVMKDVVLIRKLLALMAQEQKLPEEVATPTTDEEKDSLIAIDRSFLSTLPGQSLIDKLYNIWIRLQSHVNIVFDSEMDKLMMDKYPGIRQILEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQELRQAVINGPNVHPGASMVINEDGSRTALSAVDMTQREAVAKQLLTPATGAPKPQGTKIVCRHVKNGDILLLNRQPTLHRPSIQAHRARILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQSELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGASMTTRGCFFTREHYMELVYRGLTDKVGRVKLLSPSILKPFPLWTGKQVVSTLLINIIPEDHIPLNLSGKAKITGKAWVKETPRSVPGFNPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGKVLTCLARLFTAYLQLYRGFTLGVEDILVKPKADVKRQRIIEESTHCGPQAVRAALNLPEAASYDEVRGKWQDAHLGKDQRDFNMIDLKFKEEVNHYSNEINKACMPFGLHRQFPENSLQMMVQSGAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIKPPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVVQYDLTVRDSDGSVVQFLYGEDGLDIPKTQFLQPKQFPFLASNYEVIMKSQHLHEVLSRADPKKALHHFRAIKKWQSKHPNTLLRRGAFLSYSQKIQEAVKALKLESENRNGRSPGTQEMLRMWYELDEESRRKYQKKAAACPDPSLSVWRPDIYFASVSETFETKVDDYSQEWAAQTEKSYEKSELSLDRLRTLLQLKWQRSLCEPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIKTPMMSVPVLNTKKALKRVKSLKKQLTRVCLGEVLQKIDVQESFCMEEKQNKFQVYQLRFQFLPHAYYQQEKCLRPEDILRFMETRFFKLLMESIKKKNNKASAFRNVNTRRATQRDLDNAGELGRSRGEQEGDEEEEGHIVDAEAEEGDADASDAKRKEKQEEEVDYESEEEEEREGEENDDEDMQEERNPHREGARKTQEQDEEVGLGTEEDPSLPALLTQPRKPTHSQEPQGPEAMERRVQAVREIHPFIDDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHGAVIYATKGITRCLLNETTNNKNEKELVLNTEGINLPELFKYAEVLDLRRLYSNDIHAIANTYGIEAALRVIEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIRSNSSPLQQMTFETSFQFLKQATMLGSHDELRSPSACLVVGKVVRGGTGLFELKQPLR TTH5GAC TT Literature-reported TTV6BQU ID TTV6BQU TTV6BQU TN Dolichol phosphate mannose synthase (DPMS) TTV6BQU UP O60762; O94777; Q9P2X0 TTV6BQU UC DPM1_HUMAN; DPM2_HUMAN; DPM3_HUMAN TTV6BQU SN Mannose-P-dolichol synthase; MPD synthase; Dolichyl-phosphate beta-D-mannosyltransferase; Dolichol-phosphate mannosyltransferase; Dolichol-phosphate mannose synthase; DPM synthase TTV6BQU GN DPM1; DPM2; DPM3 TTV6BQU FC Synthesize dolichol-phosphate mannose (Dol-P-Man) from GDP-mannose and dolichol-phosphate on the cytosolic side of the ER. Dolichol-phosphate mannose serves as a donor of mannosyl residues on the lumenal side of the endoplasmic reticulum (ER). Lack of Dol-P-Man results in defective surface expression of GPI-anchored proteins. TTV6BQU SQ MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT TTV6BQU TT Literature-reported TT9C46Y ID TT9C46Y TT9C46Y TN Dual specificity phosphatase Cdc25 (CDC25) TT9C46Y UP P30304; P30305; P30307 TT9C46Y UC MPIP1_HUMAN; MPIP2_HUMAN; MPIP3_HUMAN TT9C46Y SN M-phase inducer phosphatase TT9C46Y GN CDC25A; CDC25B; CDC25C TT9C46Y FC A dual-specificity phosphatase first isolated from the yeast Schizosaccharomyces pombe as a cell cycle defective mutant. As with other cell cycle proteins or genes such as Cdc2 and Cdc4, the "cdc" in its name refers to "cell division cycle". Dual-specificity phosphatases are considered a sub-class of protein tyrosine phosphatases. By removing inhibitory phosphate residues from target cyclin-dependent kinases (Cdks), Cdc25 proteins control entry into and progression through various phases of the cell cycle, including mitosis and S ("Synthesis") phase. TT9C46Y SQ MELGPEPPHRRRLLFACSPPPASQPVVKALFGASAAGGLSPVTNLTVTMDQLQGLGSDYEQPLEVKNNSNLQRMGSSESTDSGFCLDSPGPLDSKENLENPMRRIHSLPQKLLGCSPALKRSHSDSLDHDIFQLIDPDENKENEAFEFKKPVRPVSRGCLHSHGLQEGKDLFTQRQNSAPARMLSSNERDSSEPGNFIPLFTPQSPVTATLSDEDDGFVDLLDGENLKNEEETPSCMASLWTAPLVMRTTNLDNRCKLFDSPSLCSSSTRSVLKRPERSQEESPPGSTKRRKSMSGASPKESTNPEKAHETLHQSLSLASSPKGTIENILDNDPRDLIGDFSKGYLFHTVAGKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSERGPRMCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPMHHEDFKEDLKKFRTKSRTWAGEKSKREMYSRLKKL TT9C46Y TT Literature-reported TTCVQYE ID TTCVQYE TTCVQYE TN Dynactin-associated protein (DYNAP) TTCVQYE UP Q8N1N2 TTCVQYE UC DYNAP_HUMAN TTCVQYE SN Full; C18orf26 TTCVQYE GN DYNAP TTCVQYE FC Plays a role in the regulation of cell proliferation. Promotes activation of the AKT1 signaling pathway. Promotes phosphorylation of AKT1 at 'Ser-473'. TTCVQYE SQ MVADIKGNEQIEKYSWREACDTGSSRMDRKHGKYILNVEHSENQPPITHPNDQEAHSSICWCLPSNDITSDVSPNLTGVCVNPGILAHSRCLQSESCNTQVKEYCRNDWSMWKVFLACLLACVIMTAIGVLIICLVNNKGSANSSIVIQLSTNDGECVTVKPGTPSPACPPTMTTTSTVPASTATESTTSTATAATTSTEPITVAPTDHL TTCVQYE TT Literature-reported TTS6VPR ID TTS6VPR TTS6VPR TN Ebola virus VP30-NP interaction (EV VP30-NP PPI) TTS6VPR UP Q05323-P18272 TTS6VPR UC VP30_EBOZM-NCAP_EBOZM TTS6VPR SN Ebola VP30-Nucleocapsid protein interaction TTS6VPR GN EV VP30-NP PPI TTS6VPR FC Plays both essential and inhibitory roles in Ebola virus RNA synthesis. TTS6VPR SQ MEASYERGRPRAARQHSRDGHDHHVRARSSSRENYRGEYRQSRSASQVRVPTVFHKKRVEPLTVPPAPKDICPTLKKGFLCDSSFCKKDHQLESLTDRELLLLIARKTCGSVEQQLNITAPKDSRLANPTADDFQQEEGPKITLLTLIKTAEHWARQDIRTIEDSKLRALLTLCAVMTRKFSKSQLSLLCETHLRREGLGQDQAEPVLEVYQRLHSDKGGSFEAALWQQWDRQSLIMFITAFLNIALQLPCESSAVVVSGLRTLVPQSDNEEASTNPGTCSWSDEGTPMDSRPQKIWMAPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAFEAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEELLPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQARFSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLFPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAESRELDHLGLDDQEKKILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITAASLPKTSGHYDDDDDIPFPGPINDDDNPGHQDDDPTDSQDTTIPDVVVDPDDGSYGEYQSYSENGMNAPDDLVLFDLDEDDEDTKPVPNRSTKGGQQKNSQKGQHIEGRQTQSRPIQNVPGPHRTIHHASAPLTDNDRRNEPSGSTSPRMLTPINEEADPLDDADDETSSLPPLESDDEEQDRDGTSNRTPTVAPPAPVYRDHSEKKELPQDEQQDQDHTQEARNQDSDNTQSEHSFEEMYRHILRSQGPFDAVLYYHMMKDEPVVFSTSDGKEYTYPDSLEEEYPPWLTEKEAMNEENRFVTLDGQQFYWPVMNHKNKFMAILQHHQ TTS6VPR TT Literature-reported TTME5YJ ID TTME5YJ TTME5YJ TN EBV-induced G-protein coupled receptor 2 (GPR183) TTME5YJ UP P32249 TTME5YJ UC GP183_HUMAN TTME5YJ SN hEBI2; G-protein coupled receptor 183; Epstein-Barr virus-induced G-protein coupled receptor 2; EBI2 TTME5YJ GN GPR183 TTME5YJ FC G-protein coupled receptor expressed in lymphocytes that acts as a chemotactic receptor for B-cells, T-cells, splenic dendritic cells, monocytes/macrophages and astrocytes (By similarity). Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols. Mediates cell positioning and movement of a number of cells by binding the 7-alpha,25-OHC ligand that forms a chemotactic gradient (By similarity). Binding of 7-alpha,25-OHC mediates the correct localization of B-cells during humoral immune responses (By similarity). Guides B-cell movement along the B-cell zone-T-cell zone boundary and later to interfollicular and outer follicular regions (By similarity). Its specific expression during B-cell maturation helps position B-cells appropriately for mounting T-dependent antibody responses (By similarity). Collaborates with CXCR5 to mediate B-cell migration; probably by forming a heterodimer with CXCR5 that affects the interaction between of CXCL13 and CXCR5. Also acts as a chemotactic receptor for some T-cells upon binding to 7-alpha,25-OHC ligand (By similarity). Promotes follicular helper T (Tfh) cells differentiation by positioning activated T-cells at the follicle-T-zone interface, promoting contact of newly activated CD4 T-cells with activated dendritic cells and exposing them to Tfh-cell-promoting inducible costimulator (ICOS) ligand (By similarity). Expression in splenic dendritic cells is required for their homeostasis, localization and ability to induce B- and T-cell responses: GPR183 acts as a chemotactic receptor in dendritic cells that mediates the accumulation of CD4(+) dendritic cells in bridging channels (By similarity). Regulates migration of astrocytes and is involved in communication between astrocytes and macrophages. Promotes osteoclast precursor migration to bone surfaces (By similarity). Signals constitutively through G(i)-alpha, but not G(s)-alpha or G(q)-alpha. Signals constitutively also via MAPK1/3 (ERK1/2) (By similarity). TTME5YJ SQ MDIQMANNFTPPSATPQGNDCDLYAHHSTARIVMPLHYSLVFIIGLVGNLLALVVIVQNRKKINSTTLYSTNLVISDILFTTALPTRIAYYAMGFDWRIGDALCRITALVFYINTYAGVNFMTCLSIDRFIAVVHPLRYNKIKRIEHAKGVCIFVWILVFAQTLPLLINPMSKQEAERITCMEYPNFEETKSLPWILLGACFIGYVLPLIIILICYSQICCKLFRTAKQNPLTEKSGVNKKALNTIILIIVVFVLCFTPYHVAIIQHMIKKLRFSNFLECSQRHSFQISLHFTVCLMNFNCCMDPFIYFFACKGYKRKVMRMLKRQVSVSISSAVKSAPEENSREMTETQMMIHSKSSNGK TTME5YJ TT Literature-reported TT8R0BZ ID TT8R0BZ TT8R0BZ TN Elongation factor 1A (EF1A) TT8R0BZ UP P68104; Q05639 TT8R0BZ UC EF1A1_HUMAN; EF1A2_HUMAN TT8R0BZ SN eEF1A; Eukaryotic elongation factor 1 A; Elongation factor 1-alpha; Elongation factor; EF-1-alpha TT8R0BZ GN EEF1A1; EEF1A2 TT8R0BZ FC This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. TT8R0BZ SQ MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK TT8R0BZ TT Literature-reported TTQMNEJ ID TTQMNEJ TTQMNEJ TN Endogenous retrovirus group K Env polyprotein (ENK) TTQMNEJ UP Q9HDB8; Q69384 TTQMNEJ UC ENK5_HUMAN; ENK6_HUMAN TTQMNEJ SN HERV-envelope protein; HERV-K provirus ancestral Env polyprotein; HERV-K envelope protein; Envelope polyprotein; Endogenous retrovirus group K member Env polyprotein; ERVK TTQMNEJ GN ERVK-5; ERVK-6 TTQMNEJ FC Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties. TTQMNEJ SQ MVTPVTWMDNPIEVYVNDSVWVPGPTDDRCPAKPEEEGMMINISIVYRYPPICLGRAPGCLMPAVQNWLVEVPTVSPNSRFTYHMVSGMSLRPRVNYLQDFSYQRSLKFRPKGKPCPKEIPKESKNTEVLVWEECVANSAVILQNNEFGTIIDWAPRGQFYHNCSGQTQSCPSAQVSPAVDSDLTESLDKHKHKKLQSFYPWEWGEKGISTPRPEIISPVSGPEHPELWRLWPDTTLEFGLEIKL TTQMNEJ TT Literature-reported TTOJCQV ID TTOJCQV TTOJCQV TN Epstein-Barr virus Latent membrane protein 2A (EBV LMP2A) TTOJCQV UP Q69133 TTOJCQV UC Q69133_EBVG TTOJCQV SN Latent membrane protein 2A TTOJCQV GN EBV LMP2A TTOJCQV FC A virally encoded membrane protein that is expressed in EBV latent infection and in most of the tumors associated with EBV infection. TTOJCQV SQ PMGAGPPSPGGDPDGDDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDLDWGNGDRHSDYQPLGNQDPSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVC TTOJCQV TT Literature-reported TT0VZF7 ID TT0VZF7 TT0VZF7 TN Epstein-Barr virus Nuclear antigen gene (EBV NA) TT0VZF7 UP Q69128 TT0VZF7 UC Q69128_EBVG TT0VZF7 SN EBV Uncharacterized protein TT0VZF7 GN EBV NA TT0VZF7 FC A multifunctional, dimeric viral protein associated with EpsteinBarr virus (EBV). The only EBV protein found in all EBV-related malignancies. TT0VZF7 SQ MSDEGPGTGPGNGLGEKGDTSGPEGSGGSGPQRRGGDNHGRGRGRGRGRGGGRPGAPG TT0VZF7 TT Literature-reported TT6KMPN ID TT6KMPN TT6KMPN TN Excitatory amino acid transporter 4 (SLC1A6) TT6KMPN UP P48664 TT6KMPN UC EAA4_HUMAN TT6KMPN SN Solute carrier family 1 member 6; Sodium-dependent glutamate/aspartate transporter; EAAT4 TT6KMPN GN SLC1A6 TT6KMPN FC Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (Probable). TT6KMPN SQ MSSHGNSLFLRESGQRLGRVGWLQRLQESLQQRALRTRLRLQTMTLEHVLRFLRRNAFILLTVSAVVIGVSLAFALRPYQLTYRQIKYFSFPGELLMRMLQMLVLPLIVSSLVTGMASLDNKATGRMGMRAAVYYMVTTIIAVFIGILMVTIIHPGKGSKEGLHREGRIETIPTADAFMDLIRNMFPPNLVEACFKQFKTQYSTRVVTRTMVRTENGSEPGASMPPPFSVENGTSFLENVTRALGTLQEMLSFEETVPVPGSANGINALGLVVFSVAFGLVIGGMKHKGRVLRDFFDSLNEAIMRLVGIIIWYAPVGILFLIAGKILEMEDMAVLGGQLGMYTLTVIVGLFLHAGIVLPLIYFLVTHRNPFPFIGGMLQALITAMGTSSSSATLPITFRCLEEGLGVDRRITRFVLPVGATVNMDGTALYEALAAIFIAQVNNYELNLGQITTISITATAASVGAAGIPQAGLVTMVIVLTSVGLPTEDITLIIAVDWFLDRLRTMTNVLGDSIGAAVIEHLSQRELELQEAELTLPSLGKPYKSLMAQEKGASRGRGGNESAM TT6KMPN TT Literature-reported TTK41DM ID TTK41DM TTK41DM TN Excitatory amino acid transporter 5 (SLC1A7) TTK41DM UP O00341 TTK41DM UC EAA5_HUMAN TTK41DM SN Solute carrier family 1 member 7; Retinal glutamate transporter; EAAT5 TTK41DM GN SLC1A7 TTK41DM FC Transports L-glutamate; the L-glutamate uptake is sodium- and voltage-dependent and chloride-independent. Its associated chloride conductance may participate in visual processing. TTK41DM SQ MVPHAILARGRDVCRRNGLLILSVLSVIVGCLLGFFLRTRRLSPQEISYFQFPGELLMRMLKMMILPLVVSSLMSGLASLDAKTSSRLGVLTVAYYLWTTFMAVIVGIFMVSIIHPGSAAQKETTEQSGKPIMSSADALLDLIRNMFPANLVEATFKQYRTKTTPVVKSPKVAPEEAPPRRILIYGVQEENGSHVQNFALDLTPPPEVVYKSEPGTSDGMNVLGIVFFSATMGIMLGRMGDSGAPLVSFCQCLNESVMKIVAVAVWYFPFGIVFLIAGKILEMDDPRAVGKKLGFYSVTVVCGLVLHGLFILPLLYFFITKKNPIVFIRGILQALLIALATSSSSATLPITFKCLLENNHIDRRIARFVLPVGATINMDGTALYEAVAAIFIAQVNNYELDFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWALDRFRTMINVLGDALAAGIMAHICRKDFARDTGTEKLLPCETKPVSLQEIVAAQQNGCVKSVAEASELTLGPTCPHHVPVQVEQDEELPAASLNHCTIQISELETNV TTK41DM TT Literature-reported TTTRULD ID TTTRULD TTTRULD TN Exportin-2 (CSE1L) TTTRULD UP P55060 TTTRULD UC XPO2_HUMAN TTTRULD SN Importin-alpha re-exporter; Exp2; Chromosome segregation 1-like protein; Cellular apoptosis susceptibility protein; CSE1L TTTRULD GN CSE1L TTTRULD FC Export receptor for importin-alpha. Mediates importin- alpha re-export fromthe nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the importin-alpha from the export receptor. CSE1L/XPO2 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasmand nucleus. . TTTRULD SQ MELSDANLQTLTEYLKKTLDPDPAIRRPAEKFLESVEGNQNYPLLLLTLLEKSQDNVIKVCASVTFKNYIKRNWRIVEDEPNKICEADRVAIKANIVHLMLSSPEQIQKQLSDAISIIGREDFPQKWPDLLTEMVNRFQSGDFHVINGVLRTAHSLFKRYRHEFKSNELWTEIKLVLDAFALPLTNLFKATIELCSTHANDASALRILFSSLILISKLFYSLNFQDLPEFFEDNMETWMNNFHTLLTLDNKLLQTDDEEEAGLLELLKSQICDNAALYAQKYDEEFQRYLPRFVTAIWNLLVTTGQEVKYDLLVSNAIQFLASVCERPHYKNLFEDQNTLTSICEKVIVPNMEFRAADEEAFEDNSEEYIRRDLEGSDIDTRRRAACDLVRGLCKFFEGPVTGIFSGYVNSMLQEYAKNPSVNWKHKDAAIYLVTSLASKAQTQKHGITQANELVNLTEFFVNHILPDLKSANVNEFPVLKADGIKYIMIFRNQVPKEHLLVSIPLLINHLQAESIVVHTYAAHALERLFTMRGPNNATLFTAAEIAPFVEILLTNLFKALTLPGSSENEYIMKAIMRSFSLLQEAIIPYIPTLITQLTQKLLAVSKNPSKPHFNHYMFEAICLSIRITCKANPAAVVNFEEALFLVFTEILQNDVQEFIPYVFQVMSLLLETHKNDIPSSYMALFPHLLQPVLWERTGNIPALVRLLQAFLERGSNTIASAAADKIPGLLGVFQKLIASKANDHQGFYLLNSIIEHMPPESVDQYRKQIFILLFQRLQNSKTTKFIKSFLVFINLYCIKYGALALQEIFDGIQPKMFGMVLEKIIIPEIQKVSGNVEKKICAVGITKLLTECPPMMDTEYTKLWTPLLQSLIGLFELPEDDTIPDEEHFIDIEDTPGYQTAFSQLAFAGKKEHDPVGQMVNNPKIHLAQSLHKLSTACPGRVPSMVSTSLNAEALQYLQGYLQAASVTLL TTTRULD TT Literature-reported TTNT3YA ID TTNT3YA TTNT3YA TN Forkhead box protein C1 (FOXC1) TTNT3YA UP Q12948 TTNT3YA UC FOXC1_HUMAN TTNT3YA SN Forkhead-related transcription factor 3; Forkhead-related protein FKHL7; FREAC3; FREAC-3; FKHL7 TTNT3YA GN FOXC1 TTNT3YA FC Acts either as a transcriptional activator or repressor. Binds to the consensus binding site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes. Upon DNA-binding, promotes DNA bending. Acts as a transcriptional coactivator. Stimulates Indian hedgehog (Ihh)-induced target gene expression mediated by the transcription factor GLI2, and hence regulates endochondral ossification. Acts also as a transcriptional coregulator by increasing DNA-binding capacity of GLI2 in breast cancer cells. Regulates FOXO1 through binding to a conserved element, 5'-GTAAACAAA-3' in its promoter region, implicating FOXC1 as an important regulator of cell viability and resistance to oxidative stress in the eye. Cooperates with transcription factor FOXC2 in regulating expression of genes that maintain podocyte integrity. Promotes cell growth inhibition by stopping the cell cycle in the G1 phase through TGFB1-mediated signals. Involved in epithelial-mesenchymal transition (EMT) induction by increasing cell proliferation, migration and invasion. Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression. Plays a role in the gene regulatory network essential for epidermal keratinocyte terminal differentiation. Essential developmental transcriptional factor required for mesoderm-derived tissues, such as the somites, skin, bone and cartilage. Positively regulates CXCL12 and stem cell factor expression in bone marrow mesenchymal progenitor cells, and hence plays a role in the development and maintenance of mesenchymal niches for haematopoietic stem and progenitor cells (HSPC). Plays a role in corneal transparency by preventing both blood vessel and lymphatic vessel growth during embryonic development in a VEGF-dependent manner. Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression. May function as a tumor suppressor. DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as eye, bones, cardiovascular, kidney and skin development. TTNT3YA SQ MQARYSVSSPNSLGVVPYLGGEQSYYRAAAAAAGGGYTAMPAPMSVYSHPAHAEQYPGGMARAYGPYTPQPQPKDMVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMDRFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDAVKDKEEKDRLHLKEPPPPGRQPPPAPPEQADGNAPGPQPPPVRIQDIKTENGTCPSPPQPLSPAAALGSGSAAAVPKIESPDSSSSSLSSGSSPPGSLPSARPLSLDGADSAPPPPAPSAPPPHHSQGFSVDNIMTSLRGSPQSAAAELSSGLLASAAASSRAGIAPPLALGAYSPGQSSLYSSPCSQTSSAGSSGGGGGGAGAAGGAGGAGTYHCNLQAMSLYAAGERGGHLQGAPGGAGGSAVDDPLPDYSLPPVTSSSSSSLSHGGGGGGGGGGQEAGHHPAAHQGRLTSWYLNQAGGDLGHLASAAAAAAAAGYPGQQQNFHSVREMFESQRIGLNNSPVNGNSSCQMAFPSSQSLYRTSGAFVYDCSKF TTNT3YA TT Literature-reported TTV1FDA ID TTV1FDA TTV1FDA TN Forkhead box protein J2 (FOXJ2) TTV1FDA UP Q9P0K8 TTV1FDA UC FOXJ2_HUMAN TTV1FDA SN Fork head homologous X; FHX TTV1FDA GN FOXJ2 TTV1FDA FC Transcriptional activator. Able to bind to two different type of DNA binding sites. Isoform FOXJ2.L behaves as a more potent transactivator than FOXJ2.S. TTV1FDA SQ MASDLESSLTSIDWLPQLTLRATIEKLGSASQAGPPGSSRKCSPGSPTDPNATLSKDEAAVHQDGKPRYSYATLITYAINSSPAKKMTLSEIYRWICDNFPYYKNAGIGWKNSIRHNLSLNKCFRKVPRPRDDPGKGSYWTIDTCPDISRKRRHPPDDDLSQDSPEQEASKSPRGGVAGSGEASLPPEGNPQMSLQSPTSIASYSQGTGSVDGGAVAAGASGRESAEGPPPLYNTNHDFKFSYSEINFQDLSWSFRNLYKSMLEKSSSSSQHGFSSLLGDIPPSNNYYMYQQQQPPPPQQQQQQQQPPQPPPQQSQPQQQQAPAQGPSAVGGAPPLHTPSTDGCTPPGGKQAGAEGYGPPPVMAMHPPPLQHGGYHPHQHHPHSHPAQQPPPPQPQAQGQAPINNTGFAFPSDWCSNIDSLKESFKMVNRLNWSSIEQSQFSELMESLRQAEQKNWTLDQHHIANLCDSLNHFLTQTGHVPPQGGTHRPPAPARIADSCALTSGKQESAMSQVNSYGHPQAPHLYPGPSPMYPIPTQDSAGYNRPAHHMVPRPSVPPPGANEEIPDDFDWDLIT TTV1FDA TT Literature-reported TTEJZOL ID TTEJZOL TTEJZOL TN Forkhead box protein Q1 (FOXQ1) TTEJZOL UP Q9C009 TTEJZOL UC FOXQ1_HUMAN TTEJZOL SN Hepatocyte nuclear factor 3 forkhead homolog 1; HNF3/forkheadlike protein 1; HNF-3/forkhead-like protein 1; HFH1; HFH-1 TTEJZOL GN FOXQ1 TTEJZOL FC Plays a role in hair follicle differentiation. TTEJZOL SQ MKLEVFVPRAAHGDKQGSDLEGAGGSDAPSPLSAAGDDSLGSDGDCAANSPAAGGGARDTQGDGEQSAGGGPGAEEAIPAAAAAAVVAEGAEAGAAGPGAGGAGSGEGARSKPYTRRPKPPYSYIALIAMAIRDSAGGRLTLAEINEYLMGKFPFFRGSYTGWRNSVRHNLSLNDCFVKVLRDPSRPWGKDNYWMLNPNSEYTFADGVFRRRRKRLSHRAPVPAPGLRPEEAPGLPAAPPPAPAAPASPRMRSPARQEERASPAGKFSSSFAIDSILRKPFRSRRLRDTAPGTTLQWGAAPCPPLPAFPALLPAAPCRALLPLCAYGAGEPARLGAREAEVPPTAPPLLLAPLPAAAPAKPLRGPAAGGAHLYCPLRLPAALQAASVRRPGPHLPYPVETLLA TTEJZOL TT Literature-reported TTV4J2X ID TTV4J2X TTV4J2X TN Fungal Plasma membrane H(+)-ATPase (Fung pma) TTV4J2X UP Q01680 TTV4J2X UC Q01680_PNECA TTV4J2X SN Plasma membrane H(+)-ATPase TTV4J2X GN Fung pma TTV4J2X FC Essential to fungal cell physiology, being required for the formation of a large electrochemical proton gradient and the maintenance of intracellular pH. TTV4J2X SQ DDIDALIDDLESQDGDQEDNIEDTEFQSQRQVPEELLATDTRIGLTSQEVINRRKKYGLNKMKEEKENMIIKFLMYFVGPIQFVMEAAAILAAGLQDWVEFGVICALLLLNAFVGFIQEFQAGSIVDELKKTLALKATVLRDGRLIDIEAEEVVPGDILQLEEGSIVPADGRIVTEEAYLQVDQSAITGESLAVDIHKGDSIYSSSVAKPGETFMVVTATGDRT TTV4J2X TT Literature-reported TTQNOPL ID TTQNOPL TTQNOPL TN Fusion protein FIP1L1-PDGFR alpha (FIP1L1-PDGFRA) TTQNOPL UP Q6UN15-P16234 TTQNOPL UC FIP1_HUMAN-PGFRA_HUMAN TTQNOPL SN Fusion protein RHE-CD140a TTQNOPL GN RHE-CD140a TTQNOPL FC Provides a molecular explanation for the pathogenesis of approximately half of the patients with the hypereosinophilic syndrome (HES). TTQNOPL SQ MSAGEVERLVSELSGGTGGDEEEEWLYGGPWDVHVHSDLAKDLDENEVERPEEENASANPPSGIEDETAENGVPKPKVTETEDDSDSDSDDDEDDVHVTIGDIKTGAPQYGSYGTAPVNLNIKTGGRVYGTTGTKVKGVDLDAPGSINGVPLLEVDLDSFEDKPWRKPGADLSDYFNYGFNEDTWKAYCEKQKRIRMGLEVIPVTSTTNKITAEDCTMEVTPGAEIQDGRFNLFKVQQGRTGNSEKETALPSTKAEFTSPPSLFKTGLPPSRNSTSSQSQTSTASRKANSSVGKWQDRYGRAESPDLRRLPGAIDVIGQTITISRVEGRRRANENSNIQVLSERSATEVDNNFSKPPPFFPPGAPPTHLPPPPFLPPPPTVSTAPPLIPPPGFPPPPGAPPPSLIPTIESGHSSGYDSRSARAFPYGNVAFPHLPGSAPSWPSLVDTSKQWDYYARREKDRDRERDRDRERDRDRDRERERTRERERERDHSPTPSVFNSDEERYRYREYAERGYERHRASREKEERHRERRHREKEETRHKSSRSNSRRRHESEEGDSHRRHKHKKSKRSKEGKEAGSEPAPEQESTEATPAEMGTSHPAFLVLGCLLTGLSLILCQLSLPSILPNENEKVVQLNSSFSLRCFGESEVSWQYPMSEEESSDVEIRNEENNSGLFVTVLEVSSASAAHTGLYTCYYNHTQTEENELEGRHIYIYVPDPDVAFVPLGMTDYLVIVEDDDSAIIPCRTTDPETPVTLHNSEGVVPASYDSRQGFNGTFTVGPYICEATVKGKKFQTIPFNVYALKATSELDLEMEALKTVYKSGETIVVTCAVFNNEVVDLQWTYPGEVKGKGITMLEEIKVPSIKLVYTLTVPEATVKDSGDYECAARQATREVKEMKKVTISVHEKGFIEIKPTFSQLEAVNLHEVKHFVVEVRAYPPPRISWLKNNLTLIENLTEITTDVEKIQEIRYRSKLKLIRAKEEDSGHYTIVAQNEDAVKSYTFELLTQVPSSILDLVDDHHGSTGGQTVRCTAEGTPLPDIEWMICKDIKKCNNETSWTILANNVSNIITEIHSRDRSTVEGRVTFAKVEETIAVRCLAKNLLGAENRELKLVAPTLRSELTVAAAVLVLLVIVIISLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRVLGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFLSHHPEKPKKELDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDNSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL TTQNOPL TT Literature-reported TTPNITL ID TTPNITL TTPNITL TN Fusion protein RARS-MAD1L1 (RARS-MAD1L1) TTPNITL UP P54136-Q9Y6D9 TTPNITL UC SYRC_HUMAN-MD1L1_HUMAN TTPNITL SN Fusion protein CArginyl-tRNA synthetase and MAD1-like protein 1 TTPNITL GN RARS-MAD1L1 TTPNITL FC RARS-MAD1L1 overexpression increased cell proliferation, colony formation, and tumorigenicity in vitro, and the silencing of endogenous RARS-MAD1L1 reduced cancer cell growth and colony formation in vitro. In addition, RARS-MAD1L1 increased the side population (SP) ratio and induced chemo- and radioresistance. Furthermore RARS-MAD1L1 interacted with AIMP2, which resulted in activation of FUBP1/c-Myc pathway. TTPNITL SQ MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVAMDVLVSECSARLLQQEEEIKSLTAEIDRLKNCGCLGASPNLEQLQEENLKLKYRLNILRKSLQAERNKPTKNMINIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMGISQMLKTKEQKVNPREIAENITKHLPDNECIEKVEIAGPGFINVHLRKDFVSEQLTSLLVNGVQLPALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGDWGTQFGMLIAHLQDKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKAWKLICDVSRQELNKIYDALDVSLIERGESFYQDRMNDIVKEFEDRGFVQVDDGRKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNGQSVHFQTIFAAAQMIGWYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRSMDKLKEKERDKVLTAEELNAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIARLANIDEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCYCVEKDRQTGKILKVNMWRMLLCEAVAAVMAKGFDILGIKPVQRM TTPNITL TT Literature-reported TTHZVSK ID TTHZVSK TTHZVSK TN G protein-coupled receptor 3 (GPR3) TTHZVSK UP P46089 TTHZVSK UC GPR3_HUMAN TTHZVSK SN G-protein coupled receptor 3; ACCA orphan receptor; ACCA TTHZVSK GN GPR3 TTHZVSK FC Orphan receptor with constitutive G(s) signaling activity that activate cyclic AMP. Has a potential role in modulating a number of brain functions, including behavioral responses to stress (By similarity), amyloid-beta peptide generation in neurons and neurite outgrowth (By similarity). Maintains also meiotic arrest in oocytes (By similarity). TTHZVSK SQ MMWGAGSPLAWLSAGSGNVNVSSVGPAEGPTGPAAPLPSPKAWDVVLCISGTLVSCENALVVAIIVGTPAFRAPMFLLVGSLAVADLLAGLGLVLHFAAVFCIGSAEMSLVLVGVLAMAFTASIGSLLAITVDRYLSLYNALTYYSETTVTRTYVMLALVWGGALGLGLLPVLAWNCLDGLTTCGVVYPLSKNHLVVLAIAFFMVFGIMLQLYAQICRIVCRHAQQIALQRHLLPASHYVATRKGIATLAVVLGAFAACWLPFTVYCLLGDAHSPPLYTYLTLLPATYNSMINPIIYAFRNQDVQKVLWAVCCCCSSSKIPFRSRSPSDV TTHZVSK TT Literature-reported TTLDRGX ID TTLDRGX TTLDRGX TN G1/S-specific cyclin-E2 (CCNE2) TTLDRGX UP O96020 TTLDRGX UC CCNE2_HUMAN TTLDRGX SN G1/Sspecific cyclinE2 TTLDRGX GN CCNE2 TTLDRGX FC Essential for the control of the cell cycle at the late G1 and early S phase. TTLDRGX SQ MSRRSSRLQAKQQPQPSQTESPQEAQIIQAKKRKTTQDVKKRREEVTKKHQYEIRNCWPPVLSGGISPCIIIETPHKEIGTSDFSRFTNYRFKNLFINPSPLPDLSWGCSKEVWLNMLKKESRYVHDKHFEVLHSDLEPQMRSILLDWLLEVCEVYTLHRETFYLAQDFFDRFMLTQKDINKNMLQLIGITSLFIASKLEEIYAPKLQEFAYVTDGACSEEDILRMELIILKALKWELCPVTIISWLNLFLQVDALKDAPKVLLPQYSQETFIQIAQLLDLCILAIDSLEFQYRILTAAALCHFTSIEVVKKASGLEWDSISECVDWMVPFVNVVKSTSPVKLKTFKKIPMEDRHNIQTHTNYLAMLEEVNYINTFRKGGQLSPVCNGGIMTPPKSTEKPPGKH TTLDRGX TT Literature-reported TTNBW4F ID TTNBW4F TTNBW4F TN G2 accumulation protein (GPR132) TTNBW4F UP Q9UNW8 TTNBW4F UC GP132_HUMAN TTNBW4F SN Probable G-protein coupled receptor 132; G2A TTNBW4F GN GPR132 TTNBW4F FC May be a receptor for oxidized free fatty acids derived from linoleic and arachidonic acids such as 9-hydroxyoctadecadienoic acid (9-HODE). Activates a G alpha protein, most likely G alpha(q). May be involved in apoptosis. Functions at the G2/M checkpoint to delay mitosis. May function as a sensor that monitors the oxidative states and mediates appropriate cellular responses such as secretion of paracrine signals and attenuation of proliferation. May mediate ths accumulation of intracellular inositol phosphates at acidic pH through proton-sensing activity. TTNBW4F SQ MCPMLLKNGYNGNATPVTTTAPWASLGLSAKTCNNVSFEESRIVLVVVYSAVCTLGVPANCLTAWLALLQVLQGNVLAVYLLCLALCELLYTGTLPLWVIYIRNQHRWTLGLLACKVTAYIFFCNIYVSILFLCCISCDRFVAVVYALESRGRRRRRTAILISACIFILVGIVHYPVFQTEDKETCFDMLQMDSRIAGYYYARFTVGFAIPLSIIAFTNHRIFRSIKQSMGLSAAQKAKVKHSAIAVVVIFLVCFAPYHLVLLVKAAAFSYYRGDRNAMCGLEERLYTASVVFLCLSTVNGVADPIIYVLATDHSRQEVSRIHKGWKEWSMKTDVTRLTHSRDTEELQSPVALADHYTFSRPVHPPGSPCPAKRLIEESC TTNBW4F TT Literature-reported TTBY4OD ID TTBY4OD TTBY4OD TN GABA(A) receptor epsilon (GABRE) TTBY4OD UP P78334 TTBY4OD UC GBRE_HUMAN TTBY4OD SN Gamma-aminobutyric acid receptor subunit epsilon; GABA(A) receptor subunit epsilon TTBY4OD GN GABRE TTBY4OD FC GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. TTBY4OD SQ MLSKVLPVLLGILLILQSRVEGPQTESKNEASSRDVVYGPQPQPLENQLLSEETKSTETETGSRVGKLPEASRILNTILSNYDHKLRPGIGEKPTVVTVEISVNSLGPLSILDMEYTIDIIFSQTWYDERLCYNDTFESLVLNGNVVSQLWIPDTFFRNSKRTHEHEITMPNQMVRIYKDGKVLYTIRMTIDAGCSLHMLRFPMDSHSCPLSFSSFSYPENEMIYKWENFKLEINEKNSWKLFQFDFTGVSNKTEIITTPVGDFMVMTIFFNVSRRFGYVAFQNYVPSSVTTMLSWVSFWIKTESAPARTSLGITSVLTMTTLGTFSRKNFPRVSYITALDFYIAICFVFCFCALLEFAVLNFLIYNQTKAHASPKLRHPRINSRAHARTRARSRACARQHQEAFVCQIVTTEGSDGEERPSCSAQQPPSPGSPEGPRSLCSKLACCEWCKRFKKYFCMVPDCEGSTWQQGRLCIHVYRLDNYSRVVFPVTFFFFNVLYWLVCLNL TTBY4OD TT Literature-reported TT3E0DI ID TT3E0DI TT3E0DI TN GABA(A) receptor pi (GABRP) TT3E0DI UP O00591 TT3E0DI UC GBRP_HUMAN TT3E0DI SN Gamma-aminobutyric acid receptor subunit pi; GABA(A) receptor subunit pi TT3E0DI GN GABRP TT3E0DI FC GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. In the uterus, the function of the receptor appears to be related to tissue contractility. The binding of this pI subunit with other GABA(A) receptor subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone. TT3E0DI SQ MNYSLHLAFVCLSLFTERMCIQGSQFNVEVGRSDKLSLPGFENLTAGYNKFLRPNFGGEPVQIALTLDIASISSISESNMDYTATIYLRQRWMDQRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVACNMDLSKYPMDTQTCKLQLESWGYDGNDVEFTWLRGNDSVRGLEHLRLAQYTIERYFTLVTRSQQETGNYTRLVLQFELRRNVLYFILETYVPSTFLVVLSWVSFWISLDSVPARTCIGVTTVLSMTTLMIGSRTSLPNTNCFIKAIDVYLGICFSFVFGALLEYAVAHYSSLQQMAAKDRGTTKEVEEVSITNIINSSISSFKRKISFASIEISSDNVDYSDLTMKTSDKFKFVFREKMGRIVDYFTIQNPSNVDHYSKLLFPLIFMLANVFYWAYYMYF TT3E0DI TT Literature-reported TT6XFEU ID TT6XFEU TT6XFEU TN GABA(A) receptor rho1 (GABRR1) TT6XFEU UP P24046 TT6XFEU UC GBRR1_HUMAN TT6XFEU SN Gamma-aminobutyric acid receptor subunit rho-1; GABA(C) receptor1; GABA(A) receptor subunit rho-1 TT6XFEU GN GABRR1 TT6XFEU FC GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-1 GABA receptor could play a role in retinal neurotransmission. TT6XFEU SQ MLAVPNMRFGIFLLWWGWVLATESRMHWPGREVHEMSKKGRPQRQRREVHEDAHKQVSPILRRSPDITKSPLTKSEQLLRIDDHDFSMRPGFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTNNLSMTFDGRLVKKIWVPDMFFVHSKRSFIHDTTTDNVMLRVQPDGKVLYSLRVTVTAMCNMDFSRFPLDTQTCSLEIESYAYTEDDLMLYWKKGNDSLKTDERISLSQFLIQEFHTTTKLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVPLGITTVLTMSTIITGVNASMPRVSYIKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKEQKLREKLPCTSGLPPPRTAMLDGNYSDGEVNDLDNYMPENGEKPDRMMVQLTLASERSSPQRKSQRSSYVSMRIDTHAIDKYSRIIFPAAYILFNLIYWSIFS TT6XFEU TT Literature-reported TTQMXLS ID TTQMXLS TTQMXLS TN GABA(A) receptor rho2 (GABRR2) TTQMXLS UP P28476 TTQMXLS UC GBRR2_HUMAN TTQMXLS SN Gamma-aminobutyric acid receptor subunit rho-2; GABA(C) receptor2; GABA(A) receptor subunit rho-2 TTQMXLS GN GABRR2 TTQMXLS FC GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-2 GABA receptor could play a role in retinal neurotransmission. TTQMXLS SQ MPYFTRLILFLFCLMVLVESRKPKRKRWTGQVEMPKPSHLYKKNLDVTKIRKGKPQQLLRVDEHDFSMRPAFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLAFSSASNKSMTFDGRLVKKIWVPDVFFVHSKRSFTHDTTTDNIMLRVFPDGHVLYSMRITVTAMCNMDFSHFPLDSQTCSLELESYAYTDEDLMLYWKNGDESLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVSLGITTVLTMTTIITGVNASMPRVSYVKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKERKLREKFPCMCGMLHSKTMMLDGSYSESEANSLAGYPRSHILTEEERQDKIVVHLGLSGEANAARKKGLLKGQTGFRIFQNTHAIDKYSRLIFPASYIFFNLIYWSVFS TTQMXLS TT Literature-reported TT4N6D8 ID TT4N6D8 TT4N6D8 TN GABA(A) receptor rho3 (GABRR3) TT4N6D8 UP A8MPY1 TT4N6D8 UC GBRR3_HUMAN TT4N6D8 SN Gamma-aminobutyric acid receptor subunit rho-3; GABA(C) receptor3; GABA(A) receptor subunit rho-3 TT4N6D8 GN GABRR3 TT4N6D8 FC GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. TT4N6D8 SQ MVLAFQLVSFTYIWIILKPNVCAASNIKMTHQRCSSSMKQTCKQETRMKKDDSTKARPQKYEQLLHIEDNDFAMRPGFGGSPVPVGIDVHVESIDSISETNMDFTMTFYLRHYWKDERLSFPSTANKSMTFDHRLTRKIWVPDIFFVHSKRSFIHDTTMENIMLRVHPDGNVLLSLRITVSAMCFMDFSRFPLDTQNCSLELESYAYNEDDLMLYWKHGNKSLNTEEHMSLSQFFIEDFSASSGLAFYSSTGWYNRLFINFVLRRHVFFFVLQTYFPAILMVMLSWVSFWIDRRAVPARVSLGITTVLTMSTIITAVSASMPQVSYLKAVDVYLWVSSLFVFLSVIEYAAVNYLTTVEERKQFKKTGKISRMYNIDAVQAMAFDGCYHDSEIDMDQTSLSLNSEDFMRRKSICSPSTDSSRIKRRKSLGGHVGRIILENNHVIDTYSRILFPIVYILFNLFYWGVYV TT4N6D8 TT Literature-reported TTXDUR9 ID TTXDUR9 TTXDUR9 TN GABA(A) receptor theta (GABRQ) TTXDUR9 UP Q9UN88 TTXDUR9 UC GBRT_HUMAN TTXDUR9 SN Gamma-aminobutyric acid receptor subunit theta; GABA(A) receptor subunit theta TTXDUR9 GN GABRQ TTXDUR9 FC GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. TTXDUR9 SQ MGIRGMLRAAVILLLIRTWLAEGNYPSPIPKFHFEFSSAVPEVVLNLFNCKNCANEAVVQKILDRVLSRYDVRLRPNFGGAPVPVRISIYVTSIEQISEMNMDYTITMFFHQTWKDSRLAYYETTLNLTLDYRMHEKLWVPDCYFLNSKDAFVHDVTVENRVFQLHPDGTVRYGIRLTTTAACSLDLHKFPMDKQACNLVVESYGYTVEDIILFWDDNGNAIHMTEELHIPQFTFLGRTITSKEVYFYTGSYIRLILKFQVQREVNSYLVQVYWPTVLTTITSWISFWMNYDSSAARVTIGLTSMLILTTIDSHLRDKLPNISCIKAIDIYILVCLFFVFLSLLEYVYINYLFYSRGPRRQPRRHRRPRRVIARYRYQQVVVGNVQDGLINVEDGVSSLPITPAQAPLASPESLGSLTSTSEQAQLATSESLSPLTSLSGQAPLATGESLSDLPSTSEQARHSYGVRFNGFQADDSIFPTEIRNRVEAHGHGVTHDHEDSNESLSSDERHGHGPSGKPMLHHGEKGVQEAGWDLDDNNDKSDCLAIKEQFKCDTNSTWGLNDDELMAHGQEKDSSSESEDSCPPSPGCSFTEGFSFDLFNPDYVPKVDKWSRFLFPLAFGLFNIVYWVYHMY TTXDUR9 TT Literature-reported TTFNO7W ID TTFNO7W TTFNO7W TN Gamma glutamyltranspeptidase (GGT) TTFNO7W UP P19440; P36268 TTFNO7W UC GGT1_HUMAN; GGT2_HUMAN TTFNO7W SN Gamma-glutamyltranspeptidase; Gamma-glutamyltransferase; GGT TTFNO7W GN GGT1; GGT2 TTFNO7W FC GGT1 cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, it can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. However GGT2 lack catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer. TTFNO7W SQ MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSRESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY TTFNO7W TT Literature-reported TTNP6O2 ID TTNP6O2 TTNP6O2 TN Glutamate receptor ionotropic kainate 3 (GluK3) TTNP6O2 UP Q13003 TTNP6O2 UC GRIK3_HUMAN TTNP6O2 SN Glutamate receptor ionotropic, kainate 3; Glutamate receptor 7; GluR7; GluR-7; GluK3; Excitatory amino acid receptor 5; EAA5 TTNP6O2 GN GRIK3 TTNP6O2 FC Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA. TTNP6O2 SQ MTAPWRRLRSLVWEYWAGLLVCAFWIPDSRGMPHVIRIGGIFEYADGPNAQVMNAEEHAFRFSANIINRNRTLLPNTTLTYDIQRIHFHDSFEATKKACDQLALGVVAIFGPSQGSCTNAVQSICNALEVPHIQLRWKHHPLDNKDTFYVNLYPDYASLSHAILDLVQYLKWRSATVVYDDSTGLIRLQELIMAPSRYNIRLKIRQLPIDSDDSRPLLKEMKRGREFRIIFDCSHTMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDLEPYRYSGVNLTGFRILNVDNPHVSAIVEKWSMERLQAAPRSESGLLDGVMMTDAALLYDAVHIVSVCYQRAPQMTVNSLQCHRHKAWRFGGRFMNFIKEAQWEGLTGRIVFNKTSGLRTDFDLDIISLKEDGLEKVGVWSPADGLNITEVAKGRGPNVTDSLTNRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSSKPSALVKNNEEGIQRALTADYALLMESTTIEYVTQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWWRGSGCPEEENKEASALGIQKIGGIFIVLAAGLVLSVLVAVGEFVYKLRKTAEREQRSFCSTVADEIRFSLTCQRRVKHKPQPPMMVKTDAVINMHTFNDRRLPGKDSMACSTSLAPVFP TTNP6O2 TT Literature-reported TTQV6BO ID TTQV6BO TTQV6BO TN Glutamate receptor ionotropic kainate 4 (GluK4) TTQV6BO UP Q16099 TTQV6BO UC GRIK4_HUMAN TTQV6BO SN KA1; Glutamate receptor ionotropic, kainate 4; Glutamate receptor KA-1; GluK4; GRIK; Excitatory amino acid receptor 1; EAA1 TTQV6BO GN GRIK4 TTQV6BO FC Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. TTQV6BO SQ MPRVSAPLVLLPAWLVMVACSPHSLRIAAILDDPMECSRGERLSITLAKNRINRAPERLGKAKVEVDIFELLRDSEYETAETMCQILPKGVVAVLGPSSSPASSSIISNICGEKEVPHFKVAPEEFVKFQFQRFTTLNLHPSNTDISVAVAGILNFFNCTTACLICAKAECLLNLEKLLRQFLISKDTLSVRMLDDTRDPTPLLKEIRDDKTATIIIHANASMSHTILLKAAELGMVSAYYTYIFTNLEFSLQRMDSLVDDRVNILGFSIFNQSHAFFQEFAQSLNQSWQENCDHVPFTGPALSSALLFDAVYAVVTAVQELNRSQEIGVKPLSCGSAQIWQHGTSLMNYLRMVELEGLTGHIEFNSKGQRSNYALKILQFTRNGFRQIGQWHVAEGLSMDSHLYASNISDTLFNTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEANGTWTGMVGELIARKADLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWYSPHPCAQGRCNLLVNQYSLGNSLWFPVGGFMQQGSTIAPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMDVPIESVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNSNYAFLLESTMNEYYRQRNCNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWWEGGKCPKEEDHRAKGLGMENIGGIFVVLICGLIVAIFMAMLEFLWTLRHSEATEVSVCQEMVTELRSIILCQDSIHPRRRRAAVPPPRPPIPEERRPRGTATLSNGKLCGAGEPDQLAQRLAQEAALVARGCTHIRVCPECRRFQGLRARPSPARSEESLEWEKTTNSSEPE TTQV6BO TT Literature-reported TT1M8OW ID TT1M8OW TT1M8OW TN Glutamate receptor ionotropic NMDA 2C (GluN2C) TT1M8OW UP Q14957 TT1M8OW UC NMDE3_HUMAN TT1M8OW SN NR2C; NMDAR2C; N-methyl D-aspartate receptor subtype 2C; Glutamate receptor ionotropic, NMDA 2C; Glutamate [NMDA] receptor subunit epsilon-3; GluN2C TT1M8OW GN GRIN2C TT1M8OW FC Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable). Plays a role in regulating the balance between excitatory and inhibitory activity of pyramidal neurons in the prefrontal cortex. Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (By similarity). TT1M8OW SQ MGGALGPALLLTSLFGAWAGLGPGQGEQGMTVAVVFSSSGPPQAQFRARLTPQSFLDLPLEIQPLTVGVNTTNPSSLLTQICGLLGAAHVHGIVFEDNVDTEAVAQILDFISSQTHVPILSISGGSAVVLTPKEPGSAFLQLGVSLEQQLQVLFKVLEEYDWSAFAVITSLHPGHALFLEGVRAVADASHVSWRLLDVVTLELGPGGPRARTQRLLRQLDAPVFVAYCSREEAEVLFAEAAQAGLVGPGHVWLVPNLALGSTDAPPATFPVGLISVVTESWRLSLRQKVRDGVAILALGAHSYWRQHGTLPAPAGDCRVHPGPVSPAREAFYRHLLNVTWEGRDFSFSPGGYLVQPTMVVIALNRHRLWEMVGRWEHGVLYMKYPVWPRYSASLQPVVDSRHLTVATLEERPFVIVESPDPGTGGCVPNTVPCRRQSNHTFSSGDVAPYTKLCCKGFCIDILKKLARVVKFSYDLYLVTNGKHGKRVRGVWNGMIGEVYYKRADMAIGSLTINEERSEIVDFSVPFVETGISVMVARSNGTVSPSAFLEPYSPAVWVMMFVMCLTVVAITVFMFEYFSPVSYNQNLTRGKKSGGPAFTIGKSVWLLWALVFNNSVPIENPRGTTSKIMVLVWAFFAVIFLASYTANLAAFMIQEQYIDTVSGLSDKKFQRPQDQYPPFRFGTVPNGSTERNIRSNYRDMHTHMVKFNQRSVEDALTSLKMGKLDAFIYDAAVLNYMAGKDEGCKLVTIGSGKVFATTGYGIAMQKDSHWKRAIDLALLQFLGDGETQKLETVWLSGICQNEKNEVMSSKLDIDNMAGVFYMLLVAMGLALLVFAWEHLVYWKLRHSVPNSSQLDFLLAFSRGIYSCFSGVQSLASPPRQASPDLTASSAQASVLKMLQAARDMVTTAGVSSSLDRATRTIENWGGGRRAPPPSPCPTPRSGPSPCLPTPDPPPEPSPTGWGPPDGGRAALVRRAPQPPGRPPTPGPPLSDVSRVSRRPAWEARWPVRTGHCGRHLSASERPLSPARCHYSSFPRADRSGRPFLPLFPELEDLPLLGPEQLARREALLHAAWARGSRPRHASLPSSVAEAFARPSSLPAGCTGPACARPDGHSACRRLAQAQSMCLPIYREACQEGEQAGAPAWQHRQHVCLHAHAHLPFCWGAVCPHLPPCASHGSWLSGAWGPLGHRGRTLGLGTGYRDSGGLDEISRVARGTQGFPGPCTWRRISSLESEV TT1M8OW TT Literature-reported TT5POTG ID TT5POTG TT5POTG TN Glutamate receptor ionotropic NMDA 2D (GluN2D) TT5POTG UP O15399 TT5POTG UC NMDE4_HUMAN TT5POTG SN NR2D; NMDAR2D; N-methyl D-aspartate receptor subtype 2D; Glutamate receptor ionotropic, NMDA 2D; Glutamate [NMDA] receptor subunit epsilon-4; GluN2D; EB11 TT5POTG GN GRIN2D TT5POTG FC Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition. TT5POTG SQ MRGAGGPRGPRGPAKMLLLLALACASPFPEEAPGPGGAGGPGGGLGGARPLNVALVFSGPAYAAEAARLGPAVAAAVRSPGLDVRPVALVLNGSDPRSLVLQLCDLLSGLRVHGVVFEDDSRAPAVAPILDFLSAQTSLPIVAVHGGAALVLTPKEKGSTFLQLGSSTEQQLQVIFEVLEEYDWTSFVAVTTRAPGHRAFLSYIEVLTDGSLVGWEHRGALTLDPGAGEAVLSAQLRSVSAQIRLLFCAREEAEPVFRAAEEAGLTGSGYVWFMVGPQLAGGGGSGAPGEPPLLPGGAPLPAGLFAVRSAGWRDDLARRVAAGVAVVARGAQALLRDYGFLPELGHDCRAQNRTHRGESLHRYFMNITWDNRDYSFNEDGFLVNPSLVVISLTRDRTWEVVGSWEQQTLRLKYPLWSRYGRFLQPVDDTQHLTVATLEERPFVIVEPADPISGTCIRDSVPCRSQLNRTHSPPPDAPRPEKRCCKGFCIDILKRLAHTIGFSYDLYLVTNGKHGKKIDGVWNGMIGEVFYQRADMAIGSLTINEERSEIVDFSVPFVETGISVMVARSNGTVSPSAFLEPYSPAVWVMMFVMCLTVVAVTVFIFEYLSPVGYNRSLATGKRPGGSTFTIGKSIWLLWALVFNNSVPVENPRGTTSKIMVLVWAFFAVIFLASYTANLAAFMIQEEYVDTVSGLSDRKFQRPQEQYPPLKFGTVPNGSTEKNIRSNYPDMHSYMVRYNQPRVEEALTQLKAGKLDAFIYDAAVLNYMARKDEGCKLVTIGSGKVFATTGYGIALHKGSRWKRPIDLALLQFLGDDEIEMLERLWLSGICHNDKIEVMSSKLDIDNMAGVFYMLLVAMGLSLLVFAWEHLVYWRLRHCLGPTHRMDFLLAFSRGMYSCCSAEAAPPPAKPPPPPQPLPSPAYPAPRPAPGPAPFVPRERASVDRWRRTKGAGPPGGAGLADGFHRYYGPIEPQGLGLGLGEARAAPRGAAGRPLSPPAAQPPQKPPPSYFAIVRDKEPAEPPAGAFPGFPSPPAPPAAAATAVGPPLCRLAFEDESPPAPARWPRSDPESQPLLGPGAGGAGGTGGAGGGAPAAPPPCRAAPPPCPYLDLEPSPSDSEDSESLGGASLGGLEPWWFADFPYPYAERLGPPPGRYWSVDKLGGWRAGSWDYLPPRSGPAAWHCRHCASLELLPPPRHLSCSHDGLDGGWWAPPPPPWAAGPLPRRRARCGCPRSHPHRPRASHRTPAAAAPHHHRHRRAAGGWDLPPPAPTSRSLEDLSSCPRAAPARRLTGPSRHARRCPHAAHWGPPLPTASHRRHRGGDLGTRRGSAHFSSLESEV TT5POTG TT Literature-reported TTCMBKF ID TTCMBKF TTCMBKF TN GN-binding protein G(I)/G(S)/G(O) gamma-7 (GNG7) TTCMBKF UP O60262 TTCMBKF UC GBG7_HUMAN TTCMBKF SN Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7; GNGT7; G protein gamma 7 TTCMBKF GN GNG7 TTCMBKF FC The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum. Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. TTCMBKF SQ MSATNNIAQARKLVEQLRIEAGIERIKVSKAASDLMSYCEQHARNDPLLVGVPASENPFKDKKPCIIL TTCMBKF TT Literature-reported TT2LHI6 ID TT2LHI6 TT2LHI6 TN GPI transamidase component PIG-U (PIGU) TT2LHI6 UP Q9H490 TT2LHI6 UC PIGU_HUMAN TT2LHI6 SN UNQ3055/PRO9875; Phosphatidylinositol-glycan biosynthesis, class U protein; PIGU; PIG-U; Cell division cycle protein 91-like 1; CDC91L1; CDC91-like 1 protein TT2LHI6 GN PIGU TT2LHI6 FC Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI. TT2LHI6 SQ MAAPLVLVLVVAVTVRAALFRSSLAEFISERVEVVSPLSSWKRVVEGLSLLDLGVSPYSGAVFHETPLIIYLFHFLIDYAELVFMITDALTAIALYFAIQDFNKVVFKKQKLLLELDQYAPDVAELIRTPMEMRYIPLKVALFYLLNPYTILSCVAKSTCAINNTLIAFFILTTIKGSAFLSAIFLALATYQSLYPLTLFVPGLLYLLQRQYIPVKMKSKAFWIFSWEYAMMYVGSLVVIICLSFFLLSSWDFIPAVYGFILSVPDLTPNIGLFWYFFAEMFEHFSLFFVCVFQINVFFYTIPLAIKLKEHPIFFMFIQIAVIAIFKSYPTVGDVALYMAFFPVWNHLYRFLRNIFVLTCIIIVCSLLFPVLWHLWIYAGSANSNFFYAITLTFNVGQILLISDYFYAFLRREYYLTHGLYLTAKDGTEAMLVLK TT2LHI6 TT Literature-reported TT3IPW2 ID TT3IPW2 TT3IPW2 TN G-protein coupled receptor 12 (GPR12) TT3IPW2 UP P47775 TT3IPW2 UC GPR12_HUMAN TT3IPW2 SN G-protein coupled receptor 12 TT3IPW2 GN GPR12 TT3IPW2 FC Promotes neurite outgrowth and blocks myelin inhibition in neurons (By similarity). Receptor with constitutive G(s) signaling activity that stimulates cyclic AMP production. TT3IPW2 SQ MNEDLKVNLSGLPRDYLDAAAAENISAAVSSRVPAVEPEPELVVNPWDIVLCTSGTLISCENAIVVLIIFHNPSLRAPMFLLIGSLALADLLAGIGLITNFVFAYLLQSEATKLVTIGLIVASFSASVCSLLAITVDRYLSLYYALTYHSERTVTFTYVMLVMLWGTSICLGLLPVMGWNCLRDESTCSVVRPLTKNNAAILSVSFLFMFALMLQLYIQICKIVMRHAHQIALQHHFLATSHYVTTRKGVSTLAIILGTFAACWMPFTLYSLIADYTYPSIYTYATLLPATYNSIINPVIYAFRNQEIQKALCLICCGCIPSSLAQRARSPSDV TT3IPW2 TT Literature-reported TTYUB4M ID TTYUB4M TTYUB4M TN G-protein coupled receptor 174 (GPR174) TTYUB4M UP Q9BXC1 TTYUB4M UC GP174_HUMAN TTYUB4M SN Probable G-protein coupled receptor 174 TTYUB4M GN GPR174 TTYUB4M FC Putative receptor for purines coupled to G-proteins. TTYUB4M SQ MPANYTCTRPDGDNTDFRYFIYAVTYTVILVPGLIGNILALWVFYGYMKETKRAVIFMINLAIADLLQVLSLPLRIFYYLNHDWPFGPGLCMFCFYLKYVNMYASIYFLVCISVRRFWFLMYPFRFHDCKQKYDLYISIAGWLIICLACVLFPLLRTSDDTSGNRTKCFVDLPTRNVNLAQSVVMMTIGELIGFVTPLLIVLYCTWKTVLSLQDKYPMAQDLGEKQKALKMILTCAGVFLICFAPYHFSFPLDFLVKSNEIKSCLARRVILIFHSVALCLASLNSCLDPVIYYFSTNEFRRRLSRQDLHDSIQLHAKSFVSNHTASTMTPELC TTYUB4M TT Literature-reported TT71ZLK ID TT71ZLK TT71ZLK TN G-protein coupled receptor 31 (GPR31) TT71ZLK UP O00270 TT71ZLK UC GPR31_HUMAN TT71ZLK SN 12-HETER; 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid receptor; 12-(S)-HETE receptor TT71ZLK GN GPR31 TT71ZLK FC High-affinity receptor for 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12-S-HETE). 12-(S)-HETE is an arachidonic acid metabolite secreted by platelets and tumor cells, and known to induce endothelial cells retraction allowing invasive cell access to the subendothelial matrix, which is a critical step for extravasation or metastasis. Ligand-binding lead to activation of ERK1/2 (MAPK3/MAPK1), MEK, and NF-kappa-B. TT71ZLK SQ MPFPNCSAPSTVVATAVGVLLGLECGLGLLGNAVALWTFLFRVRVWKPYAVYLLNLALADLLLAACLPFLAAFYLSLQAWHLGRVGCWALHFLLDLSRSVGMAFLAAVALDRYLRVVHPRLKVNLLSPQAALGVSGLVWLLMVALTCPGLLISEAAQNSTRCHSFYSRADGSFSIIWQEALSCLQFVLPFGLIVFCNAGIIRALQKRLREPEKQPKLQRAQALVTLVVVLFALCFLPCFLARVLMHIFQNLGSCRALCAVAHTSDVTGSLTYLHSVLNPVVYCFSSPTFRSSYRRVFHTLRGKGQAAEPPDFNPRDSYS TT71ZLK TT Literature-reported TT7OCUB ID TT7OCUB TT7OCUB TN G-protein coupled receptor 32 (GPR32) TT7OCUB UP O75388 TT7OCUB UC GPR32_HUMAN TT7OCUB SN Probable G-protein coupled receptor 32 TT7OCUB GN GPR32 TT7OCUB FC Orphan receptor. TT7OCUB SQ MNGVSEGTRGCSDRQPGVLTRDRSCSRKMNSSGCLSEEVGSLRPLTVVILSASIVVGVLGNGLVLWMTVFRMARTVSTVCFFHLALADFMLSLSLPIAMYYIVSRQWLLGEWACKLYITFVFLSYFASNCLLVFISVDRCISVLYPVWALNHRTVQRASWLAFGVWLLAAALCSAHLKFRTTRKWNGCTHCYLAFNSDNETAQIWIEGVVEGHIIGTIGHFLLGFLGPLAIIGTCAHLIRAKLLREGWVHANRPKRLLLVLVSAFFIFWSPFNVVLLVHLWRRVMLKEIYHPRMLLILQASFALGCVNSSLNPFLYVFVGRDFQEKFFQSLTSALARAFGEEEFLSSCPRGNAPRE TT7OCUB TT Literature-reported TTVXSTQ ID TTVXSTQ TTVXSTQ TN G-protein coupled receptor 34 (GPR34) TTVXSTQ UP Q9UPC5 TTVXSTQ UC GPR34_HUMAN TTVXSTQ SN Probable G-protein coupled receptor 34 TTVXSTQ GN GPR34 TTVXSTQ FC Orphan receptor. TTVXSTQ SQ MRSHTITMTTTSVSSWPYSSHRMRFITNHSDQPPQNFSATPNVTTCPMDEKLLSTVLTTSYSVIFIVGLVGNIIALYVFLGIHRKRNSIQIYLLNVAIADLLLIFCLPFRIMYHINQNKWTLGVILCKVVGTLFYMNMYISIILLGFISLDRYIKINRSIQQRKAITTKQSIYVCCIVWMLALGGFLTMIILTLKKGGHNSTMCFHYRDKHNAKGEAIFNFILVVMFWLIFLLIILSYIKIGKNLLRISKRRSKFPNSGKYATTARNSFIVLIIFTICFVPYHAFRFIYISSQLNVSSCYWKEIVHKTNEIMLVLSSFNSCLDPVMYFLMSSNIRKIMCQLLFRRFQGEPSRSESTSEFKPGYSLHDTSVAVKIQSSSKST TTVXSTQ TT Literature-reported TT2D5VM ID TT2D5VM TT2D5VM TN G-protein coupled receptor 63 (GPR63) TT2D5VM UP Q9BZJ6 TT2D5VM UC GPR63_HUMAN TT2D5VM SN Probable G-protein coupled receptor 63; PSP24B; PSP24-beta; PSP24-2 TT2D5VM GN GPR63 TT2D5VM FC Orphan receptor. May play a role in brain function. TT2D5VM SQ MVFSAVLTAFHTGTSNTTFVVYENTYMNITLPPPFQHPDLSPLLRYSFETMAPTGLSSLTVNSTAVPTTPAAFKSLNLPLQITLSAIMIFILFVSFLGNLVVCLMVYQKAAMRSAINILLASLAFADMLLAVLNMPFALVTILTTRWIFGKFFCRVSAMFFWLFVIEGVAILLIISIDRFLIIVQRQDKLNPYRAKVLIAVSWATSFCVAFPLAVGNPDLQIPSRAPQCVFGYTTNPGYQAYVILISLISFFIPFLVILYSFMGILNTLRHNALRIHSYPEGICLSQASKLGLMSLQRPFQMSIDMGFKTRAFTTILILFAVFIVCWAPFTTYSLVATFSKHFYYQHNFFEISTWLLWLCYLKSALNPLIYYWRIKKFHDACLDMMPKSFKFLPQLPGHTKRRIRPSAVYVCGEHRTVV TT2D5VM TT Literature-reported TTI1PRE ID TTI1PRE TTI1PRE TN G-protein coupled receptor GPCR33 (GPRC6A) TTI1PRE UP Q5T6X5 TTI1PRE UC GPC6A_HUMAN TTI1PRE SN hGPRC6A; hGPCR33; G-protein coupled receptor family C group 6 member A TTI1PRE GN GPRC6A TTI1PRE FC Receptor activated by amino acids with a preference for basic amino acids such as L-Lys, L-Arg and L-ornithine but also by small and polar amino acids. The L-alpha amino acids respond is augmented by divalent cations Ca(2+) and Mg(2+). Activated by extracellular calcium and osteocalcin. Seems to act through a G(q)/G(11) and G(i)-coupled pathway. Mediates the non-genomic effects of androgens in multiple tissue. May coordinate nutritional and hormonal anabolic signals through the sensing of extracellular amino acids, osteocalcin, divalent ions and its responsiveness to anabolic steroids. TTI1PRE SQ MAFLIILITCFVIILATSQPCQTPDDFVAATSPGHIIIGGLFAIHEKMLSSEDSPRRPQIQECVGFEISVFLQTLAMIHSIEMINNSTLLPGVKLGYEIYDTCTEVTVAMAATLRFLSKFNCSRETVEFKCDYSSYMPRVKAVIGSGYSEITMAVSRMLNLQLMPQVGYESTAEILSDKIRFPSFLRTVPSDFHQIKAMAHLIQKSGWNWIGIITTDDDYGRLALNTFIIQAEANNVCIAFKEVLPAFLSDNTIEVRINRTLKKIILEAQVNVIVVFLRQFHVFDLFNKAIEMNINKMWIASDNWSTATKITTIPNVKKIGKVVGFAFRRGNISSFHSFLQNLHLLPSDSHKLLHEYAMHLSACAYVKDTDLSQCIFNHSQRTLAYKANKAIERNFVMRNDFLWDYAEPGLIHSIQLAVFALGYAIRDLCQARDCQNPNAFQPWELLGVLKNVTFTDGWNSFHFDAHGDLNTGYDVVLWKEINGHMTVTKMAEYDLQNDVFIIPDQETKNEFRNLKQIQSKCSKECSPGQMKKTTRSQHICCYECQNCPENHYTNQTDMPHCLLCNNKTHWAPVRSTMCFEKEVEYLNWNDSLAILLLILSLLGIIFVLVVGIIFTRNLNTPVVKSSGGLRVCYVILLCHFLNFASTSFFIGEPQDFTCKTRQTMFGVSFTLCISCILTKSLKILLAFSFDPKLQKFLKCLYRPILIIFTCTGIQVVICTLWLIFAAPTVEVNVSLPRVIILECEEGSILAFGTMLGYIAILAFICFIFAFKGKYENYNEAKFITFGMLIYFIAWITFIPIYATTFGKYVPAVEIIVILISNYGILYCTFIPKCYVIICKQEINTKSAFLKMIYSYSSHSVSSIALSPASLDSMSGNVTMTNPSSSGKSATWQKSKDLQAQAFAHICRENATSVSKTLPRKRMSSI TTI1PRE TT Literature-reported TTFLWN6 ID TTFLWN6 TTFLWN6 TN Growth arrest and DNA-damage-inducible protein (GADD45) TTFLWN6 UP P24522; O75293; O95257 TTFLWN6 UC GA45A_HUMAN; GA45B_HUMAN; GA45G_HUMAN TTFLWN6 SN Growth arrest and DNA damage-inducible protein GADD45; DNA damage-inducible transcript protein; DDIT TTFLWN6 GN GADD45A; GADD45B; GADD45G TTFLWN6 FC Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK. TTFLWN6 SQ MTLEEFSAGEQKTERMDKVGDALEEVLSKALSQRTITVGVYEAAKLLNVDPDNVVLCLLAADEDDDRDVALQIHFTLIQAFCCENDINILRVSNPGRLAELLLLETDAGPAASEGAEQPPDLHCVLVTNPHSSQWKDPALSQLICFCRESRYMDQWVPVINLPER TTFLWN6 TT Literature-reported TTL1SRG ID TTL1SRG TTL1SRG TN Guanine nucleotide-binding alpha-q (GNAQ) TTL1SRG UP P50148 TTL1SRG UC GNAQ_HUMAN TTL1SRG SN GNAQ; G alphaq; G alpha(q) TTL1SRG GN GNAQ TTL1SRG FC Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro). TTL1SRG SQ MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV TTL1SRG TT Literature-reported TT21BYA ID TT21BYA TT21BYA TN HCLS1-associated protein X-1 (HAX1) TT21BYA UP O00165 TT21BYA UC HAX1_HUMAN TT21BYA SN HSP1BP-1; HS1BP1; HS1-binding protein 1; HS1-associating protein X-1; HAX-1 TT21BYA GN HAX1 TT21BYA FC Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools. Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. TT21BYA SQ MSLFDLFRGFFGFPGPRSHRDPFFGGMTRDEDDDEEEEEEGGSWGRGNPRFHSPQHPPEEFGFGFSFSPGGGIRFHDNFGFDDLVRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDWGSQRPFHRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSYFKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSSPRGDPESPRPPALDDAFSILDLFLGRWFRSR TT21BYA TT Literature-reported TTG0RH7 ID TTG0RH7 TTG0RH7 TN Helicobacter pylori Heat shock protein A (HELPY HspA) TTG0RH7 UP P0A0R3 TTG0RH7 UC CH10_HELPY TTG0RH7 SN Protein Cpn10; Heat shock protein 10; HELPY 10 kDa chaperonin; GroES protein TTG0RH7 GN HELPY HspA TTG0RH7 FC Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. TTG0RH7 SQ MKFQPLGERVLVERLEEENKTSSGIIIPDNAKEKPLMGVVKAVSHKISEGCKCVKEGDVIAFGKYKGAEIVLDGTEYMVLELEDILGIVGSGSCCHTGNHDHKHAKEHEACCHDHKKH TTG0RH7 TT Literature-reported TTTZ9DE ID TTTZ9DE TTTZ9DE TN Hemoglobin scavenger receptor (CD163) TTTZ9DE UP Q86VB7 TTTZ9DE UC C163A_HUMAN TTTZ9DE SN sCD163; Soluble CD163; Scavenger receptor cysteine-rich type 1 protein M130; M130 TTTZ9DE GN CD163 TTTZ9DE FC May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Exhibits a higher affinity for complexes of hemoglobin and multimeric haptoglobin of HP*1F phenotype than for complexes of hemoglobin and dimeric haptoglobin of HP*1S phenotype. Induces a cascade of intracellular signals that involves tyrosine kinase-dependent calcium mobilization, inositol triphosphate production and secretion of IL6 and CSF1. Isoform 3 exhibits the higher capacity for ligand endocytosis and the more pronounced surface expression when expressed in cells. Acute phase-regulated receptor involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. TTTZ9DE SQ MSKLRMVLLEDSGSADFRRHFVNLSPFTITVVLLLSACFVTSSLGGTDKELRLVDGENKCSGRVEVKVQEEWGTVCNNGWSMEAVSVICNQLGCPTAIKAPGWANSSAGSGRIWMDHVSCRGNESALWDCKHDGWGKHSNCTHQQDAGVTCSDGSNLEMRLTRGGNMCSGRIEIKFQGRWGTVCDDNFNIDHASVICRQLECGSAVSFSGSSNFGEGSGPIWFDDLICNGNESALWNCKHQGWGKHNCDHAEDAGVICSKGADLSLRLVDGVTECSGRLEVRFQGEWGTICDDGWDSYDAAVACKQLGCPTAVTAIGRVNASKGFGHIWLDSVSCQGHEPAIWQCKHHEWGKHYCNHNEDAGVTCSDGSDLELRLRGGGSRCAGTVEVEIQRLLGKVCDRGWGLKEADVVCRQLGCGSALKTSYQVYSKIQATNTWLFLSSCNGNETSLWDCKNWQWGGLTCDHYEEAKITCSAHREPRLVGGDIPCSGRVEVKHGDTWGSICDSDFSLEAASVLCRELQCGTVVSILGGAHFGEGNGQIWAEEFQCEGHESHLSLCPVAPRPEGTCSHSRDVGVVCSRYTEIRLVNGKTPCEGRVELKTLGAWGSLCNSHWDIEDAHVLCQQLKCGVALSTPGGARFGKGNGQIWRHMFHCTGTEQHMGDCPVTALGASLCPSEQVASVICSGNQSQTLSSCNSSSLGPTRPTIPEESAVACIESGQLRLVNGGGRCAGRVEIYHEGSWGTICDDSWDLSDAHVVCRQLGCGEAINATGSAHFGEGTGPIWLDEMKCNGKESRIWQCHSHGWGQQNCRHKEDAGVICSEFMSLRLTSEASREACAGRLEVFYNGAWGTVGKSSMSETTVGVVCRQLGCADKGKINPASLDKAMSIPMWVDNVQCPKGPDTLWQCPSSPWEKRLASPSEETWITCDNKIRLQEGPTSCSGRVEIWHGGSWGTVCDDSWDLDDAQVVCQQLGCGPALKAFKEAEFGQGTGPIWLNEVKCKGNESSLWDCPARRWGHSECGHKEDAAVNCTDISVQKTPQKATTGRSSRQSSFIAVGILGVVLLAIFVALFFLTKKRRQRQRLAVSSRGENLVHQIQYREMNSCLNADDLDLMNSSENSHESADFSAAELISVSKFLPISGMEKEAILSHTEKENGNL TTTZ9DE TT Literature-reported TTYED1Q ID TTYED1Q TTYED1Q TN Hepatocellular carcinoma-associated protein (HCAP) TTYED1Q UP Q8IXA6 TTYED1Q UC YYAP1_HUMAN TTYED1Q SN YY1AP; YY1-associated protein 1; Hepatocellular carcinoma-associated protein 2; Hepatocellular carcinoma susceptibility protein; HCCA2; HCCA1 TTYED1Q GN YY1AP1 TTYED1Q FC Enhances transcription activation by YY1. Plays a role in cell cycle regulation. Associates with the INO80 chromatin remodeling complex, which is responsible for transcriptional regulation, DNA repair, and replication. TTYED1Q SQ MEEEASRSAAATNPGSRLTRWPPPDKREGSAVDPGKRRSLAATPSSSLPCTLIALGLRHEKEANELMEDLFETFQDEMGFSNMEDDGPEEEERVAEPQANFNTPQALRFEELLANLLNEQHQIAKELFEQLKMKKPSAKQQKEVEKVKPQCKEVHQTLILDPAQRKRLQQQMQQHVQLLTQIHLLATCNPNLNPEASSTRICLKELGTFAQSSIALHHQYNPKFQTLFQPCNLMGAMQLIEDFSTHVSIDCSPHKTVKKTANEFPCLPKQVAWILATSKVFMYPELLPVCSLKAKNPQDKILFTKAEDNKYLLTCKTARQLTVRIKNLNMNRAPDNIIKFYKKTKQLPVLGKCCEEIQPHQWKPPIEREEHRLPFWLKASLPSIQEELRHMADGAREVGNMTGTTEINSDQGLEKDNSELGSETRYPLLLPKGVVLKLKPVADRFPKKAWRQKRSSVLKPLLIQPSPSLQPSFNPGKTPAQSTHSEAPPSKMVLRIPHPIQPATVLQTVPGVPPLGVSGGESFESPAALPAMPPEARTSFPLSESQTLLSSAPVPKVMMPSPASSMFRKPYVRRRPSKRRGARAFRCIKPAPVIHPASVIFTVPATTVKIVSLGGGCNMIQPVNAAVAQSPQTIPIATLLVNPTSFPCPLNQPLVASSVSPLIVSGNSVNLPIPSTPEDKAHMNVDIACAVADGENAFQGLEPKLEPQELSPLSATVFPKVEHSPGPPPVDKQCQEGLSENSAYRWTVVKTEEGRQALEPLPQGIQESLNNSSPGDLEEVVKMEPEDATEEISGFL TTYED1Q TT Literature-reported TT9TENM ID TT9TENM TT9TENM TN Herpesvirus G-protein coupled receptor (KSHV vGPCR) TT9TENM UP Q98146 TT9TENM UC VGPCR_HHV8P TT9TENM SN viral G-protein coupled receptor; vGPCR; Protein ORF74 TT9TENM GN KSHV vGPCR TT9TENM FC Receptor that signals constitutively via several signaling pathways including PI3K/AKT as well as mitogen- and stress-activated/MAP kinases. Promotes host cell proliferation and survival, modulates cell migration, stimulates angiogenesis, and recruits inflammatory cells, both in expressing cells and in neighboring cells. Maintains chronic activation of NF-kappa-B via interaction with host CADM1. TT9TENM SQ MAAEDFLTIFLDDDESWNETLNMSGYDYSGNFSLEVSVCEMTTVVPYTWNVGILSLIFLINVLGNGLVTYIFCKHRSRAGAIDILLLGICLNSLCLSISLLAEVLMFLFPNIISTGLCRLEIFFYYLYVYLDIFSVVCVSLVRYLLVAYSTRSWPKKQSLGWVLTSAALLIALVLSGDACRHRSRVVDPVSKQAMCYENAGNMTADWRLHVRTVSVTAGFLLPLALLILFYALTWCVVRRTKLQARRKVRGVIVAVVLLFFVFCFPYHVLNLLDTLLRRRWIRDSCYTRGLINVGLAVTSLLQALYSAVVPLIYSCLGSLFRQRMYGLFQSLRQSFMSGATT TT9TENM TT Literature-reported TTRV7W3 ID TTRV7W3 TTRV7W3 TN High affinity choline transporter 1 (CHT) TTRV7W3 UP Q9GZV3 TTRV7W3 UC SC5A7_HUMAN TTRV7W3 SN Solute carrier family 5 member 7; Hemicholinium-3-sensitive choline transporter; CHT1; CHT TTRV7W3 GN SLC5A7 TTRV7W3 FC Transmembrane transporter that imports choline from the extracellular space into the neuron with high affinity. Choline uptake is the rate-limiting step in acetylcholine synthesis. Sodium ion- and chloride ion-dependent. TTRV7W3 SQ MAFHVEGLIAIIVFYLLILLVGIWAAWRTKNSGSAEERSEAIIVGGRDIGLLVGGFTMTATWVGGGYINGTAEAVYVPGYGLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQIYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVDMHISVIISALIATLYTLVGGLYSVAYTDVVQLFCIFVGLWISVPFALSHPAVADIGFTAVHAKYQKPWLGTVDSSEVYSWLDSFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMAIPAILIGAIGASTDWNQTAYGLPDPKTTEEADMILPIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFARNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTKTVYGLWYLSSDLVYIVIFPQLLCVLFVKGTNTYGAVAGYVSGLFLRITGGEPYLYLQPLIFYPGYYPDDNGIYNQKFPFKTLAMVTSFLTNICISYLAKYLFESGTLPPKLDVFDAVVARHSEENMDKTILVKNENIKLDELALVKPRQSMTLSSTFTNKEAFLDVDSSPEGSGTEDNLQ TTRV7W3 TT Literature-reported TTSTVM0 ID TTSTVM0 TTSTVM0 TN High mobility group protein HMGI-C (HMGA2) TTSTVM0 UP P52926 TTSTVM0 UC HMGA2_HUMAN TTSTVM0 SN High mobility group AThook protein 2; High mobility group AT-hook protein 2; HMGIC TTSTVM0 GN HMGA2 TTSTVM0 FC Functions in cell cycle regulation through CCNA2. Plays an important role in chromosome condensation during the meiotic G2/M transition of spermatocytes. Plays a role in postnatal myogenesis, is involved in satellite cell activation. Functions as a transcriptional regulator. TTSTVM0 SQ MSARGEGAGQPSTSAQGQPAAPAPQKRGRGRPRKQQQEPTGEPSPKRPRGRPKGSKNKSPSKAAQKKAEATGEKRPRGRPRKWPQQVVQKKPAQEETEETSSQESAEED TTSTVM0 TT Literature-reported TTA78JQ ID TTA78JQ TTA78JQ TN High-mobility group protein B2 (HMGB2) TTA78JQ UP P26583 TTA78JQ UC HMGB2_HUMAN TTA78JQ SN High mobility group protein B2; High mobility group protein 2; HMG2; HMG-2 TTA78JQ GN HMGB2 TTA78JQ FC May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Proposed to be involved in the innate immune response to nucleic acids by acting as a promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. In the extracellular compartment acts as a chemokine. Promotes proliferation and migration of endothelial cells implicating AGER/RAGE. Has antimicrobial activity in gastrointestinal epithelial tissues. Involved in inflammatory response to antigenic stimulus coupled with proinflammatory activity. Involved in modulation of neurogenesis probably by regulation of neural stem proliferation. Involved in articular cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin pathway. Multifunctional protein with various roles in different cellular compartments. TTA78JQ SQ MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSEHRPKIKSEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEDEDEEEEDEDEE TTA78JQ TT Literature-reported TTR4FKD ID TTR4FKD TTR4FKD TN Histidine-rich calcium binding protein (HRC) TTR4FKD UP P23327 TTR4FKD UC SRCH_HUMAN TTR4FKD SN Sarcoplasmic reticulum histidine-rich calcium-binding protein; HRC TTR4FKD GN HRC TTR4FKD FC May play a role in the regulation of calcium sequestration or release in the SR of skeletal and cardiac muscle. TTR4FKD SQ MGHHRPWLHASVLWAGVASLLLPPAMTQQLRGDGLGFRNRNNSTGVAGLSEEASAELRHHLHSPRDHPDENKDVSTENGHHFWSHPDREKEDEDVSKEYGHLLPGHRSQDHKVGDEGVSGEEVFAEHGGQARGHRGHGSEDTEDSAEHRHHLPSHRSHSHQDEDEDEVVSSEHHHHILRHGHRGHDGEDDEGEEEEEEEEEEEEASTEYGHQAHRHRGHGSEEDEDVSDGHHHHGPSHRHQGHEEDDDDDDDDDDDDDDDDVSIEYRHQAHRHQGHGIEEDEDVSDGHHHRDPSHRHRSHEEDDNDDDDVSTEYGHQAHRHQDHRKEEVEAVSGEHHHHVPDHRHQGHRDEEEDEDVSTERWHQGPQHVHHGLVDEEEEEEEITVQFGHYVASHQPRGHKSDEEDFQDEYKTEVPHHHHHRVPREEDEEVSAELGHQAPSHRQSHQDEETGHGQRGSIKEMSHHPPGHTVVKDRSHLRKDDSEEEKEKEEDPGSHEEDDESSEQGEKGTHHGSRDQEDEEDEEEGHGLSLNQEEEEEEDKEEEEEEEDEERREERAEVGAPLSPDHSEEEEEEEEGLEEDEPRFTIIPNPLDRREEAGGASSEEESGEDTGPQDAQEYGNYQPGSLCGYCSFCNRCTECESCHCDEENMGEHCDQCQHCQFCYLCPLVCETVCAPGSYVDYFSSSLYQALADMLETPEP TTR4FKD TT Literature-reported TTBFWZJ ID TTBFWZJ TTBFWZJ TN Histone H1s-2 (H1.3) TTBFWZJ UP P16402 TTBFWZJ UC H13_HUMAN TTBFWZJ SN Histone H1s2; Histone H1c; HIST1H1D TTBFWZJ GN HIST1H1D TTBFWZJ FC Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation. TTBFWZJ SQ MSETAPLAPTIPAPAEKTPVKKKAKKAGATAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEGKPKAKKAGAAKPRKPAGAAKKPKKVAGAATPKKSIKKTPKKVKKPATAAGTKKVAKSAKKVKTPQPKKAAKSPAKAKAPKPKAAKPKSGKPKVTKAKKAAPKKK TTBFWZJ TT Literature-reported TTEX4ZA ID TTEX4ZA TTEX4ZA TN Homeobox protein Hox-A11 (HOXA11) TTEX4ZA UP P31270 TTEX4ZA UC HXA11_HUMAN TTEX4ZA SN Homeobox protein HoxA11; Homeobox protein Hox1I; Homeobox protein Hox-1I; HOX1I TTEX4ZA GN HOXA11 TTEX4ZA FC Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. TTEX4ZA SQ MDFDERGPCSSNMYLPSCTYYVSGPDFSSLPSFLPQTPSSRPMTYSYSSNLPQVQPVREVTFREYAIEPATKWHPRGNLAHCYSAEELVHRDCLQAPSAAGVPGDVLAKSSANVYHHPTPAVSSNFYSTVGRNGVLPQAFDQFFETAYGTPENLASSDYPGDKSAEKGPPAATATSAAAAAAATGAPATSSSDSGGGGGCRETAAAAEEKERRRRPESSSSPESSSGHTEDKAGGSSGQRTRKKRCPYTKYQIRELEREFFFSVYINKEKRLQLSRMLNLTDRQVKIWFQNRRMKEKKINRDRLQYYSANPLL TTEX4ZA TT Literature-reported TT8Z1FE ID TT8Z1FE TT8Z1FE TN Human immunodeficiency virus Tat-TAR RNA interaction (HIV Tat-TAR PPI) TT8Z1FE UP P04608-TAR RNA TT8Z1FE UC TAT_HV1H2-TAR RNA TT8Z1FE SN HIV Protein Tat-TAR RNA interaction TT8Z1FE GN HIV Tat-TAR PPI TT8Z1FE FC Inhibit Tat-dependent transcription of HIV DNA. TT8Z1FE SQ MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAHQNSQTHQASLSKQPTSQPRGDPTGPKE TT8Z1FE TT Literature-reported TTY078U ID TTY078U TTY078U TN IGF-binding protein 3 receptor (TMEM219) TTY078U UP Q86XT9 TTY078U UC TM219_HUMAN TTY078U SN Transmembrane protein 219; Insulin-like growth factor-binding protein 3 receptor; IGFBP-3R TTY078U GN TMEM219 TTY078U FC Cell death receptor specific for IGFBP3, may mediate caspase-8-dependent apoptosis upon ligand binding. TTY078U SQ MGNCQAGHNLHLCLAHHPPLVCATLILLLLGLSGLGLGSFLLTHRTGLRSPDIPQDWVSFLRSFGQLTLCPRNGTVTGKWRGSHVVGLLTTLNFGDGPDRNKTRTFQATVLGSQMGLKGSSAGQLVLITARVTTERTAGTCLYFSAVPGILPSSQPPISCSEEGAGNATLSPRMGEECVSVWSHEGLVLTKLLTSEELALCGSRLLVLGSFLLLFCGLLCCVTAMCFHPRRESHWSRTRL TTY078U TT Literature-reported TTCJ4WY ID TTCJ4WY TTCJ4WY TN Immunoglobulin heavy variable 5 (IGHV5) TTCJ4WY UP A0A0C4DH38; A0A0J9YXX1 TTCJ4WY UC HV551_HUMAN; HV5X1_HUMAN TTCJ4WY SN Immunoglobulin heavy variable 5 TTCJ4WY GN IGHV5-10-1; IGHV5-51 TTCJ4WY FC V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen. TTCJ4WY SQ MGSTAILALLLAVLQGVCAEVQLVQSGAEVKKPGESLKISCKGSGYSFTSYWIGWVRQMPGKGLEWMGIIYPGDSDTRYSPSFQGQVTISADKSISTAYLQWSSLKASDTAMYYCAR TTCJ4WY TT Literature-reported TTG0MQD ID TTG0MQD TTG0MQD TN Inflammation-related GPCR EX33 (GPR84) TTG0MQD UP Q9NQS5 TTG0MQD UC GPR84_HUMAN TTG0MQD SN Inflammation-related G-protein coupled receptor EX33; G-protein coupled receptor 84; EX33 TTG0MQD GN GPR84 TTG0MQD FC Receptor for medium-chain free fatty acid (FFA) with carbon chain lengths of C9 to C14. Capric acid (C10:0), undecanoic acid (C11:0) and lauric acid (C12:0) are the most potent agonists. Not activated by short-chain and long-chain saturated and unsaturated FFAs. Activation by medium-chain free fatty acid is coupled to a pertussis toxin sensitive G(i/o) protein pathway. May have important roles in processes from fatty acid metabolism to regulation of the immune system. TTG0MQD SQ MWNSSDANFSCYHESVLGYRYVAVSWGVVVAVTGTVGNVLTLLALAIQPKLRTRFNLLIANLTLADLLYCTLLQPFSVDTYLHLHWRTGATFCRVFGLLLFASNSVSILTLCLIALGRYLLIAHPKLFPQVFSAKGIVLALVSTWVVGVASFAPLWPIYILVPVVCTCSFDRIRGRPYTTILMGIYFVLGLSSVGIFYCLIHRQVKRAAQALDQYKLRQASIHSNHVARTDEAMPGRFQELDSRLASGGPSEGISSEPVSAATTQTLEGDSSEVGDQINSKRAKQMAEKSPPEASAKAQPIKGARRAPDSSSEFGKVTRMCFAVFLCFALSYIPFLLLNILDARVQAPRVVHMLAANLTWLNGCINPVLYAAMNRQFRQAYGSILKRGPRSFHRLH TTG0MQD TT Clinical trial TTATO6X ID TTATO6X TTATO6X TN Integral membrane protein GPR137 (GPR137) TTATO6X UP Q96N19 TTATO6X UC G137A_HUMAN TTATO6X SN Transmembrane 7 superfamily member 1-like 1 protein; TM7SF1L1; GPR137A; C11orf4 TTATO6X GN GPR137 TTATO6X FC It is a peptide which displays four putative transmembrane domains and is predicted to have a cytoplasmic localization. The receptor is available in the following formats: stable over-expression cell line, membrane preparation, or purified receptor in HEK293 or CHO. TTATO6X SQ MESNLSGLVPAAGLVPALPPAVTLGLTAAYTTLYALLFFSVYAQLWLVLLYGHKRLSYQTVFLALCLLWAALRTTLFSFYFRDTPRANRLGPLPFWLLYCCPVCLQFFTLTLMNLYFAQVVFKAKVKRRPEMSRGLLAVRGAFVGASLLFLLVNVLCAVLSHRRRAQPWALLLVRVLVSDSLFVICALSLAACLCLVARRAPSTSIYLEAKGTSVCQAAAMGGAMVLLYASRACYNLTALALAPQSRLDTFDYDWYNVSDQADLVNDLGNKGYLVFGLILFVWELLPTTLLVGFFRVHRPPQDLSTSHILNGQVFASRSYFFDRAGHCEDEGCSWEHSRGESTRCQDQAATTTVSTPPHRRDPPPSPTEYPGPSPPHPRPLCQVCLPLLAQDPGGRGYPLLWPAPCCSCHSELVPSP TTATO6X TT Literature-reported TTHUBNK ID TTHUBNK TTHUBNK TN Interferon consensus sequence binding protein (IRF8) TTHUBNK UP Q02556 TTHUBNK UC IRF8_HUMAN TTHUBNK SN Interferon regulatory factor 8; Interferon consensus sequence-binding protein; IRF-8; ICSBP1; ICSBP; H-ICSBP TTHUBNK GN IRF8 TTHUBNK FC Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)). Plays a negative regulatory role in cells of the immune system. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF8 and activation of genes. Positively regulates macroautophagy in dendritic cells. Plays a role as a transcriptional activator or repressor. TTHUBNK SQ MCDRNGGRRLRQWLIEQIDSSMYPGLIWENEEKSMFRIPWKHAGKQDYNQEVDASIFKAWAVFKGKFKEGDKAEPATWKTRLRCALNKSPDFEEVTDRSQLDISEPYKVYRIVPEEEQKCKLGVATAGCVNEVTEMECGRSEIDELIKEPSVDDYMGMIKRSPSPPEACRSQLLPDWWAQQPSTGVPLVTGYTTYDAHHSAFSQMVISFYYGGKLVGQATTTCPEGCRLSLSQPGLPGTKLYGPEGLELVRFPPADAIPSERQRQVTRKLFGHLERGVLLHSSRQGVFVKRLCQGRVFCSGNAVVCKGRPNKLERDEVVQVFDTSQFFRELQQFYNSQGRLPDGRVVLCFGEEFPDMAPLRSKLILVQIEQLYVRQLAEEAGKSCGAGSVMQAPEEPPPDQVFRMFPDICASHQRSFFRENQQITV TTHUBNK TT Literature-reported TT4TU3L ID TT4TU3L TT4TU3L TN Interferon regulatory factor 1 (IRF1) TT4TU3L UP P10914 TT4TU3L UC IRF1_HUMAN TT4TU3L SN IRF-1 TT4TU3L GN IRF1 TT4TU3L FC These include the regulation of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, immune responses and cell proliferation and differentiation, regulation of the cell cycle and induction of growth arrest and programmed cell death following DNA damage. Stimulates both innate and acquired immune responses through the activation of specific target genes and can act as a transcriptional activator and repressor regulating target genes by binding to an interferon-stimulated response element (ISRE) in their promoters. Its target genes for transcriptional activation activity include: genes involved in anti-viral response, such as IFN-alpha/beta, DDX58/RIG-I, TNFSF10/TRAIL, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial response, such as NOS2/INOS; anti-proliferative response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II expression, such as CIITA. Represses genes involved in anti-proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and TLR4. Stimulates p53/TP53-dependent transcription through enhanced recruitment of EP300 leading to increased acetylation of p53/TP53. Plays an important role in immune response directly affecting NK maturation and activity, macrophage production of IL12, Th1 development and maturation of CD8+ T-cells. Also implicated in the differentiation and maturation of dendritic cells and in the suppression of regulatory T (Treg) cells development. Acts as a tumor suppressor and plays a role not only in antagonism of tumor cell growth but also in stimulating an immune response against tumor cells. Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses. TT4TU3L SQ MPITRMRMRPWLEMQINSNQIPGLIWINKEEMIFQIPWKHAAKHGWDINKDACLFRSWAIHTGRYKAGEKEPDPKTWKANFRCAMNSLPDIEEVKDQSRNKGSSAVRVYRMLPPLTKNQRKERKSKSSRDAKSKAKRKSCGDSSPDTFSDGLSSSTLPDDHSSYTVPGYMQDLEVEQALTPALSPCAVSSTLPDWHIPVEVVPDSTSDLYNFQVSPMPSTSEATTDEDEEGKLPEDIMKLLEQSEWQPTNVDGKGYLLNEPGVQPTSVYGDFSCKEEPEIDSPGGDIGLSLQRVFTDLKNMDATWLDSLLTPVRLPSIQAIPCAP TT4TU3L TT Literature-reported TTK9OV3 ID TTK9OV3 TTK9OV3 TN IP3 receptor isoform 2 (IP3R2) TTK9OV3 UP Q14571 TTK9OV3 UC ITPR2_HUMAN TTK9OV3 SN Type 2 inositol 1,4,5-trisphosphate receptor; Type 2 InsP3 receptor; InsP3R2; Inositol 1,4,5-trisphosphate receptor type 2; IP3R 2 TTK9OV3 GN ITPR2 TTK9OV3 FC Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of PKA (By similarity). TTK9OV3 SQ MTEKMSSFLYIGDIVSLYAEGSVNGFISTLGLVDDRCVVHPEAGDLANPPKKFRDCLFKVCPMNRYSAQKQYWKAKQAKQGNHTEAALLKKLQHAAELEQKQNESENKKLLGEIVKYSNVIQLLHIKSNKYLTVNKRLPALLEKNAMRVSLDAAGNEGSWFYIHPFWKLRSEGDNIVVGDKVVLMPVNAGQPLHASNIELLDNPGCKEVNAVNCNTSWKITLFMKYSSYREDVLKGGDVVRLFHAEQEKFLTCDEYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLFRFKHLATGNYLAAELNPDYRDAQNEGKNVRDGVPPTSKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPRNSYVRLRHLCTNTWVTSTSIPIDTDEERPVMLKIGTCQTKEDKEAFAIVSVPLSEVRDLDFANDANKVLATTVKKLENGTITQNERRFVTKLLEDLIFFVADVPNNGQEVLDVVITKPNRERQKLMREQNILAQVFGILKAPFKEKAGEGSMLRLEDLGDQRYAPYKYMLRLCYRVLRHSQQDYRKNQEYIAKNFCVMQSQIGYDILAEDTITALLHNNRKLLEKHITAKEIETFVSLLRRNREPRFLDYLSDLCVSNTTAIPVTQELICKFMLSPGNADILIQTKVVSMQADNPMESSILSDDIDDEEVWLYWIDSNKEPHGKAIRHLAQEAKEGTKADLEVLTYYRYQLNLFARMCLDRQYLAINQISTQLSVDLILRCVSDESLPFDLRASFCRLMLHMHVDRDPQESVVPVRYARLWTEIPTKITIHEYDSITDSSRNDMKRKFALTMEFVEEYLKEVVNQPFPFGDKEKNKLTFEVVHLARNLIYFGFYSFSELLRLTRTLLAILDIVQAPMSSYFERLSKFQDGGNNVMRTIHGVGEMMTQMVLSRGSIFPMSVPDVPPSIHPSKQGSPTEHEDVTVMDTKLKIIEILQFILSVRLDYRISYMLSIYKKEFGEDNDNAETSASGSPDTLLPSAIVPDIDEIAAQAETMFAGRKEKNPVQLDDEGGRTFLRVLIHLIMHDYPPLLSGALQLLFKHFSQRAEVLQAFKQVQLLVSNQDVDNYKQIKADLDQLRLTVEKSELWVEKSSNYENGEIGESQVKGGEEPIEESNILSPVQDGTKKPQIDSNKSNNYRIVKEILIRLSKLCVQNKKCRNQHQRLLKNMGAHSVVLDLLQIPYEKNDEKMNEVMNLAHTFLQNFCRGNPQNQVLLHKHLNLFLTPGLLEAETMRHIFMNNYHLCNEISERVVQHFVHCIETHGRHVEYLRFLQTIVKADGKYVKKCQDMVMTELINGGEDVLIFYNDRASFPILLHMMCSERDRGDESGPLAYHITLVELLAACTEGKNVYTEIKCNSLLPLDDIVRVVTHDDCIPEVKIAYVNFVNHCYVDTEVEMKEIYTSNHIWKLFENFLVDMARVCNTTTDRKHADIFLEKCVTESIMNIVSGFFNSPFSDNSTSLQTHQPVFIQLLQSAFRIYNCTWPNPAQKASVESCIRTLAEVAKNRGIAIPVDLDSQVNTLFMKSHSNMVQRAAMGWRLSARSGPRFKEALGGPAWDYRNIIEKLQDVVASLEHQFSPMMQAEFSVLVDVLYSPELLFPEGSDARIRCGAFMSKLINHTKKLMEKEEKLCIKILQTLREMLEKKDSFVEEGNTLRKILLNRYFKGDYSIGVNGHLSGAYSKTAQVGGSFSGQDSDKMGISMSDIQCLLDKEGASELVIDVIVNTKNDRIFSEGIFLGIALLEGGNTQTQYSFYQQLHEQKKSEKFFKVLYDRMKAAQKEIRSTVTVNTIDLGNKKRDDDNELMTSGPRMRVRDSTLHLKEGMKGQLTEASSATSKAYCVYRREMDPEIDIMCTGPEAGNTEEKSAEEVTMSPAIAIMQPILRFLQLLCENHNRELQNFLRNQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALVNQNLESLTEYCQGPCHENQTCIATHESNGIDIIIALILNDINPLGKYRMDLVLQLKNNASKLLLAIMESRHDSENAERILFNMRPRELVDVMKNAYNQGLECDHGDDEGGDDGVSPKDVGHNIYILAHQLARHNKLLQQMLKPGSDPDEGDEALKYYANHTAQIEIVRHDRTMEQIVFPVPNICEYLTRESKCRVFNTTERDEQGSKVNDFFQQTEDLYNEMKWQKKIRNNPALFWFSRHISLWGSISFNLAVFINLAVALFYPFGDDGDEGTLSPLFSVLLWIAVAICTSMLFFFSKPVGIRPFLVSIMLRSIYTIGLGPTLILLGAANLCNKIVFLVSFVGNRGTFTRGYRAVILDMAFLYHVAYVLVCMLGLFVHEFFYSFLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIIGFLFLKDDFTMEVDRLKNRTPVTGSHQVPTMTLTTMMEACAKENCSPTIPASNTADEEYEDGIERTCDTLLMCIVTVLNQGLRNGGGVGDVLRRPSKDEPLFAARVVYDLLFYFIVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVSFEEHIKSEHNMWHYLYFIVLVKVKDPTEYTGPESYVAQMIVEKNLDWFPRMRAMSLVSNEGDSEQNEIRSLQEKLESTMSLVKQLSGQLAELKEQMTEQRKNKQRLGFLGSNTPHVNHHMPPH TTK9OV3 TT Literature-reported TTMX06B ID TTMX06B TTMX06B TN Islet cell autoantigen p69 (ICA1) TTMX06B UP Q05084 TTMX06B UC ICA69_HUMAN TTMX06B SN P69; Islet cell autoantigen 1; ICAp69; ICA69; ICA1 TTMX06B GN ICA1 TTMX06B FC May play a role in neurotransmitter secretion. TTMX06B SQ MSGHKCSYPWDLQDRYAQDKSVVNKMQQKYWETKQAFIKATGKKEDEHVVASDADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKTRAGKMMQATGKALCFSSQQRLALRNPLCRFHQEVETFRHRAISDTWLTVNRMEQCRTEYRGALLWMKDVSQELDPDLYKQMEKFRKVQTQVRLAKKNFDKLKMDVCQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTMAAIHESFKGYQPYEFTTLKSLQDPMKKLVEKEEKKKINQQESTDAAVQEPSQLISLEEENQRKESSSFKTEDGKSILSALDKGSTHTACSGPIDELLDMKSEEGACLGPVAGTPEPEGADKDDLLLLSEIFNASSLEEGEFSKEWAAVFGDGQVKEPVPTMALGEPDPKAQTGSGFLPSQLLDQNMKDLQASLQEPAKAASDLTAWFSLFADLDPLSNPDAVGKTDKEHELLNA TTMX06B TT Literature-reported TTLWKP4 ID TTLWKP4 TTLWKP4 TN Kidney associated antigen 1 (KAAG1) TTLWKP4 UP Q9UBP8 TTLWKP4 UC KAAG1_HUMAN TTLWKP4 SN RU2AS; RU2 antisense gene protein; Kidney-associated antigen 1 TTLWKP4 GN KAAG1 TTLWKP4 FC Invovled in immune response. TTLWKP4 SQ MDDDAAPRVEGVPVAVHKHALHDGLRQVAGPGAAAAHLPRWPPPQLAASRREAPPLSQRPHRTQGAGSPPETNEKLTNPQVKEK TTLWKP4 TT Literature-reported TT3ETNF ID TT3ETNF TT3ETNF TN Leishmania Elongation factor 1-alpha (Leishm EF1A) TT3ETNF UP Q95VF2 TT3ETNF UC Q95VF2_LEIDO TT3ETNF SN Leishmania Elongation factor 1A TT3ETNF GN Leishm EF1A TT3ETNF FC This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. TT3ETNF SQ MGKDKVHMNLVVVGHVDAGKSTATGHLIYKCGGIDKRTIEKFEKEAAEIGKASFKYAWVLDKLKAERERGITIDIALWKFESPKSVFTIIDAPGHRDFIKNMITGTSQADAAILMIDSTHGGFEAGISKDGQTREHALLAFTLGVKQMVVCCNKMDDKTVTYAQSRYDEISKEVGAYLKRVGYNPEKVRFIPISGWQGDNMIERSDNMPWYKGPTLLDALDMLEPPVRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGIMKPGDVVTFAPANVTTEVKSIEMHHEQLAEAQPGDNVGFNVKNVSVKDIRRGNVCGNSKNDPPKEAADFTAQVIVLNHPGQISNGYAPVLDCHTSHIACRFAEIESKIDRRSGKELEKNPKAIKSGDAAIVKMVPQKPMCVEVFNDYAPLGRFAVRDMRQTVAVGIIKGVNKKEGSGGKVTKAAAKAAKK TT3ETNF TT Literature-reported TTOUZG8 ID TTOUZG8 TTOUZG8 TN Leishmania Guanine nucleotide-binding protein (Leishm LACK) TTOUZG8 UP Q25306 TTOUZG8 UC GBLP_LEIMA TTOUZG8 SN Guanine nucleotide-binding protein subunit beta-like protein; Antigen LACK TTOUZG8 GN Leishm LACK TTOUZG8 FC Involved as modulators or transducers in various transmembrane signaling systems. TTOUZG8 SQ MNYEGHLKGHRGWVTSLACPQQAGSYIKVVSTSRDGTVISWKANPDRHSVDSDYGLPNHRLEGHTGFVSCVSLAHATDYALTASWDRSIRMWDLRNGQCQRKFLKHTKDVLAVAFSPDDRLIVSAGRDNVIRVWNVAGECMHEFLRDGHEDWVSSICFSPSLEHPIVVSGSWDNTIKVWNVNGGKCERTLKGHSNYVSTVTVSPDGSLCASGGKDGAALLWDLSTGEQLFKINVESPINQIGFSPNRFWMCVATERSLSVYDLESKAVIAELTPDGAKPSECISIAWSADGNTLYSGHKDNLIRVWSISDAE TTOUZG8 TT Literature-reported TTL7VOU ID TTL7VOU TTL7VOU TN Leukocyte antigen class II (HLA-DQB2) TTL7VOU UP Q29870 TTL7VOU UC DQB2_HUMAN TTL7VOU SN MHC class II antigen DQB2; HLA-DXB; HLA class II histocompatibility antigen, DX beta chain; HLA class II histocompatibility antigen, DQ beta 2 chain TTL7VOU GN HLA-DQB2 TTL7VOU FC Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. TTL7VOU SQ MSWKMALQIPGGFWAAAVTVMLVMLSTPVAEARDFPKDFLVQFKGMCYFTNGTERVRGVARYIYNREEYGRFDSDVGEFQAVTELGRSIEDWNNYKDFLEQERAAVDKVCRHNYEAELRTTLQRQVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTSLIRNGDWTFQILVMLEITPQRGDIYTCQVEHPSLQSPITVEWRAQSESAQSKMLSGIGGFVLGLIFLGLGLIIRHRGQKGPRGPPPAGLLH TTL7VOU TT Literature-reported TTGZN2L ID TTGZN2L TTGZN2L TN Leukocyte Ig-like receptor-3 (LILR3) TTGZN2L UP Q8N6C8; O75022 TTGZN2L UC LIRA3_HUMAN; LIRB3_HUMAN TTGZN2L SN Monocyte inhibitory receptor; Leukocyte immunoglobulin-like receptor; LIR; Immunoglobulin-like transcript; ILT; CD85 antigen-like family member; CD85 TTGZN2L GN LILRA3; LILRB3 TTGZN2L FC Binds with high affinity to the surface of monocytes, leading to abolish LPS-induced TNF-alpha production by monocytes. Acts as soluble receptor for class I MHC antigens. Binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1 or LILRB2. TTGZN2L SQ MTPILTVLICLGLSLDPRTHVQAGPLPKPTLWAEPGSVITQGSPVTLRCQGSLETQEYHLYREKKTALWITRIPQELVKKGQFPILSITWEHAGRYCCIYGSHTAGLSESSDPLELVVTGAYSKPTLSALPSPVVTSGGNVTIQCDSQVAFDGFILCKEGEDEHPQCLNSHSHARGSSRAIFSVGPVSPSRRWSYRCYGYDSRAPYVWSLPSDLLGLLVPGVSKKPSLSVQPGPVVAPGEKLTFQCGSDAGYDRFVLYKEWGRDFLQRPGRQPQAGLSQANFTLGPVSRSYGGQYTCSGAYNLSSEWSAPSDPLDILITGQIRARPFLSVRPGPTVASGENVTLLCQSQGGMHTFLLTKEGAADSPLRLKSKRQSHKYQAEFPMSPVTSAHAGTYRCYGSLSSNPYLLTHPSDPLELVVSGAAETLSPPQNKSDSKAGE TTGZN2L TT Literature-reported TTIVYCQ ID TTIVYCQ TTIVYCQ TN Leukocyte Ig-like receptor-5 (LILR5) TTIVYCQ UP A6NI73; O75023 TTIVYCQ UC LIRA5_HUMAN; LIRB5_HUMAN TTIVYCQ SN ILT-11 TTIVYCQ GN LILRA5; LILRB5 TTIVYCQ FC May play a role in triggering innate immune responses. Does not seem to play a role for any class I MHC antigen recognition. TTIVYCQ SQ MAPWSHPSAQLQPVGGDAVSPALMVLLCLGLSLGPRTHVQAGNLSKATLWAEPGSVISRGNSVTIRCQGTLEAQEYRLVKEGSPEPWDTQNPLEPKNKARFSIPSMTEHHAGRYRCYYYSPAGWSEPSDPLELVVTGFYNKPTLSALPSPVVTSGENVTLQCGSRLRFDRFILTEEGDHKLSWTLDSQLTPSGQFQALFPVGPVTPSHRWMLRCYGSRRHILQVWSEPSDLLEIPVSGAADNLSPSQNKSDSGTASHLQDYAVENLIRMGMAGLILVVLGILIFQDWHSQRSPQAAAGR TTIVYCQ TT Literature-reported TTOZAX0 ID TTOZAX0 TTOZAX0 TN Leukosialin (SPN) TTOZAX0 UP P16150 TTOZAX0 UC LEUK_HUMAN TTOZAX0 SN Sialophorin; Leukocyte sialoglycoprotein; Leucocyte sialoglycoprotein; Galactoglycoprotein; GPL115; GALGP; CD43 antigen; CD43 TTOZAX0 GN SPN TTOZAX0 FC Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN). Negatively regulates Th2 cell differentiation and predisposes the differentiation of T-cells towards a Th1 lineage commitment. Promotes the expression of IFN-gamma by T-cells during T-cell receptor (TCR) activation of naive cells and induces the expression of IFN-gamma by CD4(+) T-cells and to a lesser extent by CD8(+) T-cells. Plays a role in preparing T-cells for cytokine sensing and differentiation into effector cells by inducing the expression of cytokine receptors IFNGR and IL4R, promoting IFNGR and IL4R signaling and by mediating the clustering of IFNGR with TCR. Acts as a major E-selectin ligand responsible for Th17 cell rolling on activated vasculature and recruitment during inflammation. Mediates Th17 cells, but not Th1 cells, adhesion to E-selectin. Acts as a T-cell counter-receptor for SIGLEC1. Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. TTOZAX0 SQ MATLLLLLGVLVVSPDALGSTTAVQTPTSGEPLVSTSEPLSSKMYTTSITSDPKADSTGDQTSALPPSTSINEGSPLWTSIGASTGSPLPEPTTYQEVSIKMSSVPQETPHATSHPAVPITANSLGSHTVTGGTITTNSPETSSRTSGAPVTTAASSLETSRGTSGPPLTMATVSLETSKGTSGPPVTMATDSLETSTGTTGPPVTMTTGSLEPSSGASGPQVSSVKLSTMMSPTTSTNASTVPFRNPDENSRGMLPVAVLVALLAVIVLVALLLLWRRRQKRRTGALVLSRGGKRNGVVDAWAGPAQVPEEGAVTVTVGGSGGDKGSGFPDGEGSSRRPTLTTFFGRRKSRQGSLAMEELKSGSGPSLKGEEEPLVASEDGAVDAPAPDEPEGGDGAAP TTOZAX0 TT Literature-reported TTOZAX0 FM Transmembrane protein TTIV27N ID TTIV27N TTIV27N TN Lipid droplet-associated protein (PLIN1) TTIV27N UP O60240 TTIV27N UC PLIN1_HUMAN TTIV27N SN PLIN1; PERI TTIV27N GN PLIN1 TTIV27N FC Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone- sensitive lipase (HSL). Its absence may result in leanness. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels. TTIV27N SQ MAVNKGLTLLDGDLPEQENVLQRVLQLPVVSGTCECFQKTYTSTKEAHPLVASVCNAYEKGVQSASSLAAWSMEPVVRRLSTQFTAANELACRGLDHLEEKIPALQYPPEKIASELKDTISTRLRSARNSISVPIASTSDKVLGAALAGCELAWGVARDTAEFAANTRAGRLASGGADLALGSIEKVVEYLLPPDKEESAPAPGHQQAQKSPKAKPSLLSRVGALTNTLSRYTVQTMARALEQGHTVAMWIPGVVPLSSLAQWGASVAMQAVSRRRSEVRVPWLHSLAAAQEEDHEDQTDTEGEDTEEEEELETEENKFSEVAALPGPRGLLGGVAHTLQKTLQTTISAVTWAPAAVLGMAGRVLHLTPAPAVSSTKGRAMSLSDALKGVTDNVVDTVVHYVPLPRLSLMEPESEFRDIDNPPAEVERREAERRASGAPSAGPEPAPRLAQPRRSLRSAQSPGAPPGPGLEDEVATPAAPRPGFPAVPREKPKRRVSDSFFRPSVMEPILGRTHYSQLRKKS TTIV27N TT Literature-reported TTU86P0 ID TTU86P0 TTU86P0 TN Liver organic anion transporter 2 (SLCO1B3) TTU86P0 UP Q9NPD5 TTU86P0 UC SO1B3_HUMAN TTU86P0 SN Solute carrier organic anion transporter family member 1B3; Solute carrier family 21 member 8; SLC21A8; Organic anion-transporting polypeptide 8; Organic anion transporter 8; OATP8; OATP1B3; OATP-8; Liver-specific organic anion transporter 2; LST2; LST-2 TTU86P0 GN SLCO1B3 TTU86P0 FC Mediates the Na(+)-independent uptake of organic anions such as 17-beta-glucuronosyl estradiol, taurocholate, triiodothyronine (T3), leukotriene C4, dehydroepiandrosterone sulfate (DHEAS), methotrexate and sulfobromophthalein (BSP). Involved in the clearance of bile acids and organic anions from the liver. TTU86P0 SQ MDQHQHLNKTAESASSEKKKTRRCNGFKMFLAALSFSYIAKALGGIIMKISITQIERRFDISSSLAGLIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCLLMGTGSILTSLPHFFMGYYRYSKETHINPSENSTSSLSTCLINQTLSFNGTSPEIVEKDCVKESGSHMWIYVFMGNMLRGIGETPIVPLGISYIDDFAKEGHSSLYLGSLNAIGMIGPVIGFALGSLFAKMYVDIGYVDLSTIRITPKDSRWVGAWWLGFLVSGLFSIISSIPFFFLPKNPNKPQKERKISLSLHVLKTNDDRNQTANLTNQGKNVTKNVTGFFQSLKSILTNPLYVIFLLLTLLQVSSFIGSFTYVFKYMEQQYGQSASHANFLLGIITIPTVATGMFLGGFIIKKFKLSLVGIAKFSFLTSMISFLFQLLYFPLICESKSVAGLTLTYDGNNSVASHVDVPLSYCNSECNCDESQWEPVCGNNGITYLSPCLAGCKSSSGIKKHTVFYNCSCVEVTGLQNRNYSAHLGECPRDNTCTRKFFIYVAIQVINSLFSATGGTTFILLTVKIVQPELKALAMGFQSMVIRTLGGILAPIYFGALIDKTCMKWSTNSCGAQGACRIYNSVFFGRVYLGLSIALRFPALVLYIVFIFAMKKKFQGKDTKASDNERKVMDEANLEFLNNGEHFVPSAGTDSKTCNLDMQDNAAAN TTU86P0 TT Literature-reported TTINE9B ID TTINE9B TTINE9B TN Lymphocyte antigen 6D (LY6D) TTINE9B UP Q14210 TTINE9B UC LY6D_HUMAN TTINE9B SN LY6D; E48 antigen; Desmoglein III (dg4) TTINE9B GN LY6D TTINE9B FC May act as a specification marker at earliest stage specification of lymphocytes between B- and T-cell development. Marks the earliest stage of B-cell specification. TTINE9B SQ MRTALLLLAALAVATGPALTLRCHVCTSSSNCKHSVVCPASSRFCKTTNTVEPLRGNLVKKDCAESCTPSYTLQGQVSSGTSSTQCCQEDLCNEKLHNAAPTRTALAHSALSLGLALSLLAVILAPSL TTINE9B TT Literature-reported TT5GKHN ID TT5GKHN TT5GKHN TN Lymphocyte antigen 6K (LY6K) TT5GKHN UP Q17RY6 TT5GKHN UC LY6K_HUMAN TT5GKHN SN Ly-6K; CO16 TT5GKHN GN LY6K TT5GKHN FC Required for sperm migration into the oviduct and male fertility by controlling binding of sperm to zona pellucida (By similarity). May play a role in cell growth. TT5GKHN SQ MALLALLLVVALPRVWTDANLTARQRDPEDSQRTDEGDNRVWCHVCERENTFECQNPRRCKWTEPYCVIAAVKIFPRFFMVAKQCSAGCAAMERPKPEEKRFLLEEPMPFFYLKCCKIRYCNLEGPPINSSVFKEYAGSMGESCGGLWLAILLLLASIAAGLSLS TT5GKHN TT Literature-reported TT7ZMY4 ID TT7ZMY4 TT7ZMY4 TN Lysophosphatidic acid receptor 4 (LPAR4) TT7ZMY4 UP Q99677 TT7ZMY4 UC LPAR4_HUMAN TT7ZMY4 SN Purinergic receptor 9; P2Y9; P2Y5-like receptor; P2Y purinoceptor 9; P2RY9; LPA4; LPA-4; LPA receptor 4; GPR23; G-protein coupled receptor 23 TT7ZMY4 GN LPAR4 TT7ZMY4 FC Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Transduces a signal by increasing the intracellular calcium ions and by stimulating adenylyl cyclase activity. The rank order of potency for agonists of this receptor is 1-oleoyl- > 1-stearoyl- > 1-palmitoyl- > 1-myristoyl- > 1-alkyl- > 1-alkenyl-LPA. TT7ZMY4 SQ MGDRRFIDFQFQDSNSSLRPRLGNATANNTCIVDDSFKYNLNGAVYSVVFILGLITNSVSLFVFCFRMKMRSETAIFITNLAVSDLLFVCTLPFKIFYNFNRHWPFGDTLCKISGTAFLTNIYGSMLFLTCISVDRFLAIVYPFRSRTIRTRRNSAIVCAGVWILVLSGGISASLFSTTNVNNATTTCFEGFSKRVWKTYLSKITIFIEVVGFIIPLILNVSCSSVVLRTLRKPATLSQIGTNKKKVLKMITVHMAVFVVCFVPYNSVLFLYALVRSQAITNCFLERFAKIMYPITLCLATLNCCFDPFIYYFTLESFQKSFYINAHIRMESLFKTETPLTTKPSLPAIQEEVSDQTTNNGGELMLESTF TT7ZMY4 TT Literature-reported TTABCJ6 ID TTABCJ6 TTABCJ6 TN Lysophosphatidic acid receptor 5 (LPAR5) TTABCJ6 UP Q9H1C0 TTABCJ6 UC LPAR5_HUMAN TTABCJ6 SN LPA-5; LPA receptor 5; GPR93; GPR92; G-protein coupled receptor 93; G-protein coupled receptor 92 TTABCJ6 GN LPAR5 TTABCJ6 FC Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. TTABCJ6 SQ MLANSSSTNSSVLPCPDYRPTHRLHLVVYSLVLAAGLPLNALALWVFLRALRVHSVVSVYMCNLAASDLLFTLSLPVRLSYYALHHWPFPDLLCQTTGAIFQMNMYGSCIFLMLINVDRYAAIVHPLRLRHLRRPRVARLLCLGVWALILVFAVPAARVHRPSRCRYRDLEVRLCFESFSDELWKGRLLPLVLLAEALGFLLPLAAVVYSSGRVFWTLARPDATQSQRRRKTVRLLLANLVIFLLCFVPYNSTLAVYGLLRSKLVAASVPARDRVRGVLMVMVLLAGANCVLDPLVYYFSAEGFRNTLRGLGTPHRARTSATNGTRAALAQSERSAVTTDATRPDAASQGLLRPSDSHSLSSFTQCPQDSAL TTABCJ6 TT Literature-reported TTZDAGB ID TTZDAGB TTZDAGB TN Lysophosphatidic acid receptor 6 (LPAR6) TTZDAGB UP P43657 TTZDAGB UC LPAR6_HUMAN TTZDAGB SN RB intron encoded G-protein coupled receptor; Purinergic receptor 5; P2Y5; P2Y purinoceptor 5; P2RY5; Oleoyl-L-alpha-lysophosphatidic acid receptor; LPA-6; LPA receptor 6 TTZDAGB GN LPAR6 TTZDAGB FC Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture. TTZDAGB SQ MVSVNSSHCFYNDSFKYTLYGCMFSMVFVLGLISNCVAIYIFICVLKVRNETTTYMINLAMSDLLFVFTLPFRIFYFTTRNWPFGDLLCKISVMLFYTNMYGSILFLTCISVDRFLAIVYPFKSKTLRTKRNAKIVCTGVWLTVIGGSAPAVFVQSTHSQGNNASEACFENFPEATWKTYLSRIVIFIEIVGFFIPLILNVTCSSMVLKTLTKPVTLSRSKINKTKVLKMIFVHLIIFCFCFVPYNINLILYSLVRTQTFVNCSVVAAVRTMYPITLCIAVSNCCFDPIVYYFTSDTIQNSIKMKNWSVRRSDFRFSEVHGAENFIQHNLQTLKSKIFDNESAA TTZDAGB TT Literature-reported TTEJQT0 ID TTEJQT0 TTEJQT0 TN Lysosome-associated transmembrane 4b-35 protein (LAPTM4B) TTEJQT0 UP Q86VI4 TTEJQT0 UC LAP4B_HUMAN TTEJQT0 SN Lysosome-associated transmembrane protein 4-beta; Lysosomal-associated transmembrane protein 4B TTEJQT0 GN LAPTM4B TTEJQT0 FC Required for optimal lysosomal function. Blocks EGF-stimulated EGFR intraluminal sorting and degradation. Conversely by binding with the phosphatidylinositol 4,5-bisphosphate, regulates its PIP5K1C interaction, inhibits HGS ubiquitination and relieves LAPTM4B inhibition of EGFR degradation. Recruits SLC3A2 and SLC7A5 (the Leu transporter) to the lysosome, promoting entry of leucine and other essential amino acid (EAA) into the lysosome, stimulating activation of proton-transporting vacuolar (V)-ATPase protein pump (V-ATPase) and hence mTORC1 activation. Plays a role as negative regulator of TGFB1 production in regulatory T cells. Binds ceramide and facilitates its exit from late endosome in order to control cell death pathways. TTEJQT0 SQ MTSRTRVTWPSPPRPLPVPAAAAVAFGAKGTDPAEARSSRGIEEAGPRAHGRAGREPERRRSRQQRRGGLQARRSTLLKTCARARATAPGAMKMVAPWTRFYSNSCCLCCHVRTGTILLGVWYLIINAVVLLILLSALADPDQYNFSSSELGGDFEFMDDANMCIAIAISLLMILICAMATYGAYKQRAAWIIPFFCYQIFDFALNMLVAITVLIYPNSIQEYIRQLPPNFPYRDDVMSVNPTCLVLIILLFISIILTFKGYLISCVWNCYRYINGRNSSDVLVYVTSNDTTVLLPPYDDATVNGAAKEPPPPYVSA TTEJQT0 TT Literature-reported TTIX6PK ID TTIX6PK TTIX6PK TN Mas-related G protein-coupled receptor X1 (MRGX1) TTIX6PK UP Q96LB2 TTIX6PK UC MRGX1_HUMAN TTIX6PK SN Sensory neuron-specific G-protein coupled receptor 3/4; SNSR4; SNSR3; Mas-related G-protein coupled receptor member X1; MRGX1 TTIX6PK GN MRGPRX1 TTIX6PK FC Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain. Potently activated by enkephalins including BAM22 (bovine adrenal medulla peptide 22) and BAM (8-22). BAM22 is the most potent compound and evoked a large and dose-dependent release of intracellular calcium in stably transfected cells. G(alpha)q proteins are involved in the calcium-signaling pathway. Activated by the antimalarial drug, chloroquine. May mediate chloroquine-induced itch, in a histamine-independent manner. TTIX6PK SQ MDPTISTLDTELTPINGTEETLCYKQTLSLTVLTCIVSLVGLTGNAVVLWLLGCRMRRNAFSIYILNLAAADFLFLSGRLIYSLLSFISIPHTISKILYPVMMFSYFAGLSFLSAVSTERCLSVLWPIWYRCHRPTHLSAVVCVLLWALSLLRSILEWMLCGFLFSGADSAWCQTSDFITVAWLIFLCVVLCGSSLVLLIRILCGSRKIPLTRLYVTILLTVLVFLLCGLPFGIQFFLFLWIHVDREVLFCHVHLVSIFLSALNSSANPIIYFFVGSFRQRQNRQNLKLVLQRALQDASEVDEGGGQLPEEILELSGSRLEQ TTIX6PK TT Literature-reported TTOZT28 ID TTOZT28 TTOZT28 TN Melanoma-associated antigen 2 (MAGEA2) TTOZT28 UP P43356 TTOZT28 UC MAGA2_HUMAN TTOZT28 SN MAGEA2B; MAGEA2A; MAGE2; MAGE-2 antigen; Cancer/testis antigen 1.2; CT1.2 TTOZT28 GN MAGEA2 TTOZT28 FC Represses p73/TP73 activity. Proposed to enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. In vitro enhances ubiquitin ligase activity of TRIM28 and stimulates p53/TP53 ubiquitination by TRIM28 potentially in presence of Ubl-conjugating enzyme UBE2H. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in embryonal development and tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes. Negatively regulates acetylation and sumoylation of PML and represses PML-induced p53/TP53 acetylation and activation. Reduces p53/TP53 transactivation function through recruitment of HDAC3 to p53/TP53 transcription sites. TTOZT28 SQ MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQQTASSSSTLVEVTLGEVPAADSPSPPHSPQGASSFSTTINYTLWRQSDEGSSNQEEEGPRMFPDLESEFQAAISRKMVELVHFLLLKYRAREPVTKAEMLESVLRNCQDFFPVIFSKASEYLQLVFGIEVVEVVPISHLYILVTCLGLSYDGLLGDNQVMPKTGLLIIVLAIIAIEGDCAPEEKIWEELSMLEVFEGREDSVFAHPRKLLMQDLVQENYLEYRQVPGSDPACYEFLWGPRALIETSYVKVLHHTLKIGGEPHISYPPLHERALREGEE TTOZT28 TT Literature-reported TT0VFPN ID TT0VFPN TT0VFPN TN Microtubule-associated protein 4 (MAP4) TT0VFPN UP P27816 TT0VFPN UC MAP4_HUMAN TT0VFPN SN Microtubuleassociated protein 4; MAP4 TT0VFPN GN MAP4 TT0VFPN FC Non-neuronal microtubule-associated protein. Promotes microtubule assembly. TT0VFPN SQ MADLSLADALTEPSPDIEGEIKRDFIATLEAEAFDDVVGETVGKTDYIPLLDVDEKTGNSESKKKPCSETSQIEDTPSSKPTLLANGGHGVEGSDTTGSPTEFLEEKMAYQEYPNSQNWPEDTNFCFQPEQVVDPIQTDPFKMYHDDDLADLVFPSSATADTSIFAGQNDPLKDSYGMSPCNTAVVPQGWSVEALNSPHSESFVSPEAVAEPPQPTAVPLELAKEIEMASEERPPAQALEIMMGLKTTDMAPSKETEMALAKDMALATKTEVALAKDMESPTKLDVTLAKDMQPSMESDMALVKDMELPTEKEVALVKDVRWPTETDVSSAKNVVLPTETEVAPAKDVTLLKETERASPIKMDLAPSKDMGPPKENKKETERASPIKMDLAPSKDMGPPKENKIVPAKDLVLLSEIEVAQANDIISSTEISSAEKVALSSETEVALARDMTLPPETNVILTKDKALPLEAEVAPVKDMAQLPETEIAPAKDVAPSTVKEVGLLKDMSPLSETEMALGKDVTPPPETEVVLIKNVCLPPEMEVALTEDQVPALKTEAPLAKDGVLTLANNVTPAKDVPPLSETEATPVPIKDMEIAQTQKGISEDSHLESLQDVGQSAAPTFMISPETVTGTGKKCSLPAEEDSVLEKLGERKPCNSQPSELSSETSGIARPEEGRPVVSGTGNDITTPPNKELPPSPEKKTKPLATTQPAKTSTSKAKTQPTSLPKQPAPTTIGGLNKKPMSLASGLVPAAPPKRPAVASARPSILPSKDVKPKPIADAKAPEKRASPSKPASAPASRSGSKSTQTVAKTTTAAAVASTGPSSRSPSTLLPKKPTAIKTEGKPAEVKKMTAKSVPADLSRPKSTSTSSMKKTTTLSGTAPAAGVVPSRVKATPMPSRPSTTPFIDKKPTSAKPSSTTPRLSRLATNTSAPDLKNVRSKVGSTENIKHQPGGGRAKVEKKTEAAATTRKPESNAVTKTAGPIASAQKQPAGKVQIVSKKVSYSHIQSKCGSKDNIKHVPGGGNVQIQNKKVDISKVSSKCGSKANIKHKPGGGDVKIESQKLNFKEKAQAKVGSLDNVGHLPAGGAVKTEGGGSEAPLCPGPPAGEEPAISEAAPEAGAPTSASGLNGHPTLSGGGDQREAQTLDSQIQETSI TT0VFPN TT Literature-reported TTTD730 ID TTTD730 TTTD730 TN Mitochondrial citrate transporter (SLC25A1) TTTD730 UP P53007 TTTD730 UC TXTP_HUMAN TTTD730 SN Tricarboxylate transport protein, mitochondrial; Tricarboxylate carrier protein; Solute carrier family 25 member 1; SLC20A3; Citrate transport protein; CTP TTTD730 GN SLC25A1 TTTD730 FC Citrate transporter that mediates the exchange of mitochondrial citrate for cytosolic malate. Also able to mediate the exchange of citrate for isocitrate, phosphoenolpyruvate, cis- but not trans-aconitate and to a lesser extend maleate and succinate. Important for the bioenergetics of hepatic cells as it provides a carbon source for fatty acid and sterol biosyntheses, and NAD(+) for the glycolytic pathway. Required for proper neuromuscular junction formation (Probable). TTTD730 SQ MPAPRAPRALAAAAPASGKAKLTHPGKAILAGGLAGGIEICITFPTEYVKTQLQLDERSHPPRYRGIGDCVRQTVRSHGVLGLYRGLSSLLYGSIPKAAVRFGMFEFLSNHMRDAQGRLDSTRGLLCGLGAGVAEAVVVVCPMETIKVKFIHDQTSPNPKYRGFFHGVREIVREQGLKGTYQGLTATVLKQGSNQAIRFFVMTSLRNWYRGDNPNKPMNPLITGVFGAIAGAASVFGNTPLDVIKTRMQGLEAHKYRNTWDCGLQILKKEGLKAFYKGTVPRLGRVCLDVAIVFVIYDEVVKLLNKVWKTD TTTD730 TT Literature-reported TT7HXSL ID TT7HXSL TT7HXSL TN Multidrug and toxin extrusion protein 2 (MATE2) TT7HXSL UP Q86VL8 TT7HXSL UC S47A2_HUMAN TT7HXSL SN hMATE-2; Solute carrier family 47 member 2; MATE2; MATE-2; Kidney-specific H(+)/organic cation antiporter TT7HXSL GN SLC47A2 TT7HXSL FC Solute transporter for tetraethylammonium (TEA), 1-methyl-4-phenylpyridinium (MPP), cimetidine, N-methylnicotinamide, metformin, creatinine, guanidine, procainamide, topotecan, estrone sulfate, acyclovir, and ganciclovir. Responsible for the secretion of cationic drugs across the brush border membranes. TT7HXSL SQ MDSLQDTVALDHGGCCPALSRLVPRGFGTEMWTLFALSGPLFLFQVLTFMIYIVSTVFCGHLGKVELASVTLAVAFVNVCGVSVGVGLSSACDTLMSQSFGSPNKKHVGVILQRGALVLLLCCLPCWALFLNTQHILLLFRQDPDVSRLTQDYVMIFIPGLPVIFLYNLLAKYLQNQGWLKGQEEESPFQTPGLSILHPSHSHLSRASFHLFQKITWPQVLSGVVGNCVNGVANYALVSVLNLGVRGSAYANIISQFAQTVFLLLYIVLKKLHLETWAGWSSQCLQDWGPFFSLAVPSMLMICVEWWAYEIGSFLMGLLSVVDLSAQAVIYEVATVTYMIPLGLSIGVCVRVGMALGAADTVQAKRSAVSGVLSIVGISLVLGTLISILKNQLGHIFTNDEDVIALVSQVLPVYSVFHVFEAICCVYGGVLRGTGKQAFGAAVNAITYYIIGLPLGILLTFVVRMRIMGLWLGMLACVFLATAAFVAYTARLDWKLAAEEAKKHSGRQQQQRAESTATRPGPEKAVLSSVATGSSPGITLTTYSRSECHVDFFRTPEEAHALSAPTSRLSVKQLVIRRGAALGAASATLMVGLTVRILATRH TT7HXSL TT Literature-reported TTNOTDM ID TTNOTDM TTNOTDM TN Mycobacterium DNA-dependent RNA polymerase beta (MycB rpoB) TTNOTDM UP Q7X2I2 TTNOTDM UC Q7X2I2_MYCTX TTNOTDM SN DNA-dependent RNA polymerase beta subunit TTNOTDM GN MycB rpoB TTNOTDM FC Transcribes the message carried by DNA. Has important implications in transcriptional regulation. TTNOTDM SQ TVPGGVEVPVETDDIDHFGNRRLRTVGELIQNQIRVGMSRMERVVRERMTTQDVEAITPQTLINIRPVVAAIKEFFGTSQLSQFMDQNNPLSGLTHKRRLWALGPGGLSRERAGLEVRDVHPS TTNOTDM TT Literature-reported TT08ESN ID TT08ESN TT08ESN TN Mycobacterium Mycolic acid synthase (MycB cma) TT08ESN UP P9WPB7; P9WPB5; P9WPB3 TT08ESN UC CMAS1_MYCTU; CMAS2_MYCTU; CMAS3_MYCTU TT08ESN SN cma; SAM-MT; S-adenosylmethionine-dependent methyltransferase; Mycolic acid methyltransferase; MA-MT; Cyclopropane-fatty-acyl-phospholipid synthase; Cyclopropane mycolic acid synthase; Cyclopropane fatty acid synthase; CMAS; CFA synthase; AdoMet-MT TT08ESN GN MycB cmaA1; MycB cmaA2; MycB pcaA TT08ESN FC Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. TT08ESN SQ MPDELKPHFANVQAHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVGLTLSKNQANHVQQLVANSENLRSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLLHTITGLHPKEIHERGLPMSFTFARFLKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWSAALQANKGQAIALQSEEVYERYMKYLTGCAEMFRIGYIDVNQFTCQK TT08ESN TT Successful TTUHP04 ID TTUHP04 TTUHP04 TN Mycobacterium Phosphatidyl-myo-inositol mannosyltransferase (MycB pimA) TTUHP04 UP P9WMZ5 TTUHP04 UC PIMA_MYCTU TTUHP04 SN Phosphatidylinositol alpha-mannosyltransferase; Phosphatidyl-myo-inositol mannosyltransferase; PI alpha-mannosyltransferase; Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase; GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferase; Alpha-mannosyltransferase TTUHP04 GN MycB pimA TTUHP04 FC Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). PimA plays an essential role for growth in macrophages and during both the acute and chronic phases of infection. TTUHP04 SQ MRIGMICPYSFDVPGGVQSHVLQLAEVMRTRGHLVSVLAPASPHAALPDYFVSGGRAVPIPYNGSVARLRFGPATHRKVKKWLAHGDFDVLHLHEPNAPSLSMLALNIAEGPIVATFHTSTTKSLTLTVFQGILRPMHEKIVGRIAVSDLARRWQMEALGSDAVEIPNGVDVDSFASAARLDGYPRQGKTVLFLGRYDEPRKGMAVLLDALPKVVQRFPDVQLLIVGHGDADQLRGQAGRLAAHLRFLGQVDDAGKASAMRSADVYCAPNTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVPVDPPDLQAAALADGLIAVLENDVLRERYVAAGNAAVRRYDWSVVASQIMRVYETVAGSGAKVQVAS TTUHP04 TT Literature-reported TTJ4AN0 ID TTJ4AN0 TTJ4AN0 TN Mycobacterium Shikimate kinase (MycB aroK) TTJ4AN0 UP G0TQ18 TTJ4AN0 UC G0TQ18_MYCCP TTJ4AN0 SN Shikimate kinase; MycB SK TTJ4AN0 GN MycB aroK TTJ4AN0 FC Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. TTJ4AN0 SQ MAPKAVLVGLPGSGKSTIGRRLAKALGVSLLDTDVAIEQRTGRSIADIFATDGEQEFRRIEEDVVRAALADHDGVLSLGGGAVTSPGVRAALAGHTVVYLEISAAEGVRRTGGNTVRPLLAGPDRAEKYRALMAKRAPLYRRVATMRVDTNRRNPGAVVRYILSRLQVPSPSEAAT TTJ4AN0 TT Literature-reported TTYUK4F ID TTYUK4F TTYUK4F TN Myelin-associated/oligodendrocyte basic protein (MOBP) TTYUK4F UP Q13875 TTYUK4F UC MOBP_HUMAN TTYUK4F SN Myelin-associated oligodendrocyte basic protein TTYUK4F GN MOBP TTYUK4F FC May play a role in compacting or stabilizing the myelin sheath, possibly by binding the negatively charged acidic phospholipids of the cytoplasmic membrane. TTYUK4F SQ MSQKPAKEGPRLSKNQKYSEHFSIHCCPPFTFLNSKKEIVDRKYSICKSGCFYQKKEEDWICCACQKTRTSRRAKSPQRPKQQPAAPPAVVRAPAKPRSPPRSERQPRSPPRSERQPRSPPRSERQPRSPPRSERQPRPRPEVRPPPAKQRPPQKSKQQPRSSPLRGPGASRGGSPVKASRFW TTYUK4F TT Literature-reported TTQBMPI ID TTQBMPI TTQBMPI TN Na(+)/Cl(-) betaine/GABA transporter (SLC6A12) TTQBMPI UP P48065 TTQBMPI UC S6A12_HUMAN TTQBMPI SN Solute carrier family 6 member 12; Sodium- and chloride-dependent betaine transporter; BGT-1 TTQBMPI GN SLC6A12 TTQBMPI FC Transports betaine and GABA. May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation. TTQBMPI SQ MDGKVAVQECGPPAVSWVPEEGEKLDQEDEDQVKDRGQWTNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYFIFFFVCGIPVFFLEVALGQYTSQGSVTAWRKICPLFQGIGLASVVIESYLNVYYIIILAWALFYLFSSFTSELPWTTCNNFWNTEHCTDFLNHSGAGTVTPFENFTSPVMEFWERRVLGITSGIHDLGSLRWELALCLLLAWVICYFCIWKGVKSTGKVVYFTATFPYLMLVILLIRGVTLPGAYQGIIYYLKPDLFRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYKDCIALCFLNSATSFVAGFVVFSILGFMSQEQGVPISEVAESGPGLAFIAFPKAVTMMPLSQLWSCLFFIMLIFLGLDSQFVCVECLVTASIDMFPRQLRKSGRRELLILTIAVMCYLIGLFLVTEGGMYIFQLFDYYASSGICLLFLSLFEVVCISWVYGADRFYDNIEDMIGYRPWPLVKISWLFLTPGLCLATFLFSLSKYTPLKYNNVYVYPPWGYSIGWFLALSSMVCVPLFVVITLLKTRGPFRKRLRQLITPDSSLPQPKQHPCLDGSAGRNFGPSPTREGLIAGEKETHL TTQBMPI TT Literature-reported TTFZW07 ID TTFZW07 TTFZW07 TN NAD-dependent methylenetetrahydrofolate dehydrogenase (NMD) TTFZW07 UP P13995; Q9H903 TTFZW07 UC MTDC_HUMAN; MTD2L_HUMAN TTFZW07 SN Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase TTFZW07 GN MTHFD2; MTHFD2L TTFZW07 FC Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency. TTFZW07 SQ MAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRNEAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN TTFZW07 TT Literature-reported TTSLJAR ID TTSLJAR TTSLJAR TN N-arachidonyl glycine receptor (GPR18) TTSLJAR UP Q14330 TTSLJAR UC GPR18_HUMAN TTSLJAR SN NAGly receptor; GPCRW; G-protein coupled receptor 18 TTSLJAR GN GPR18 TTSLJAR FC Receptor for endocannabinoid N-arachidonyl glycine (NAGly). However, conflicting results about the role of NAGly as an agonist are reported. Can also be activated by plant-derived and synthetic cannabinoid agonists. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. May contribute to regulation of the immune system. Is required for normal homeostasis of CD8+ subsets of intraepithelial lymphocytes (IELs) (CD8alphaalpha and CD8alphabeta IELs)in small intstine by supporting preferential migration of CD8alphaalpha T-cells to intraepithelial compartment over lamina propria compartment, and by mediating their reconstitution into small intestine after bone marrow transplant (By similarity). Plays a role in hypotensive responses, mediating reduction in intraocular and blood pressure (By similarity). Mediates NAGly-induced process of reorganization of actin filaments and induction of acrosomal exocytosis. TTSLJAR SQ MITLNNQDQPVPFNSSHPDEYKIAALVFYSCIFIIGLFVNITALWVFSCTTKKRTTVTIYMMNVALVDLIFIMTLPFRMFYYAKDEWPFGEYFCQILGALTVFYPSIALWLLAFISADRYMAIVQPKYAKELKNTCKAVLACVGVWIMTLTTTTPLLLLYKDPDKDSTPATCLKISDIIYLKAVNVLNLTRLTFFFLIPLFIMIGCYLVIIHNLLHGRTSKLKPKVKEKSIRIIITLLVQVLVCFMPFHICFAFLMLGTGENSYNPWGAFTTFLMNLSTCLDVILYYIVSKQFQARVISVMLYRNYLRSMRRKSFRSGSLRSLSNINSEML TTSLJAR TT Literature-reported TTOFEAS ID TTOFEAS TTOFEAS TN Natural killer cell receptor BY55 (CD160) TTOFEAS UP O95971 TTOFEAS UC BY55_HUMAN TTOFEAS SN CD160 antigen; BY55 TTOFEAS GN CD160 TTOFEAS FC Exists as a GPI-anchored and as a transmembrane form, each likely initiating distinct signaling pathways via phosphoinositol 3-kinase in activated NK cells and via LCK and CD247/CD3 zeta chain in activated T cells. Receptor for both classical and non-classical MHC class I molecules. In the context of acute viral infection, recognizes HLA-C and triggers NK cell cytotoxic activity, likely playing a role in anti-viral innate immune response. On CD8+ T cells, binds HLA-A2-B2M in complex with a viral peptide and provides a costimulatory signal to activated/memory T cells. Upon persistent antigen stimulation, such as occurs during chronic viral infection, may progressively inhibit TCR signaling in memory CD8+ T cells, contributing to T cell exhaustion. On endothelial cells, recognizes HLA-G and controls angiogenesis in immune privileged sites. Receptor or ligand for TNF superfamily member TNFRSF14, participating in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. Upon ligation of TNFRSF14, provides stimulatory signal to NK cells enhancing IFNG production and anti-tumor immune response. On activated CD4+ T cells, interacts with TNFRSF14 and downregulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response. In the context of bacterial infection, acts as a ligand for TNFRSF14 on epithelial cells, triggering the production of antimicrobial proteins and proinflammatory cytokines. CD160 antigen: Receptor on immune cells capable to deliver stimulatory or inhibitory signals that regulate cell activation and differentiation. TTOFEAS SQ MLLEPGRGCCALAILLAIVDIQSGGCINITSSASQEGTRLNLICTVWHKKEEAEGFVVFLCKDRSGDCSPETSLKQLRLKRDPGIDGVGEISSQLMFTISQVTPLHSGTYQCCARSQKSGIRLQGHFFSILFTETGNYTVTGLKQRQHLEFSHNEGTLSSGFLQEKVWVMLVTSLVALQAL TTOFEAS TT Literature-reported TT7H4BF ID TT7H4BF TT7H4BF TN Nel-related protein 1 (NELL1) TT7H4BF UP Q92832 TT7H4BF UC NELL1_HUMAN TT7H4BF SN NELL1; NEL-like protein 1 TT7H4BF GN NELL1 TT7H4BF FC Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization. TT7H4BF SQ MPMDLILVVWFCVCTARTVVGFGMDPDLQMDIVTELDLVNTTLGVAQVSGMHNASKAFLFQDIEREIHAAPHVSEKLIQLFRNKSEFTILATVQQKPSTSGVILSIRELEHSYFELESSGLRDEIRYHYIHNGKPRTEALPYRMADGQWHKVALSVSASHLLLHVDCNRIYERVIDPPDTNLPPGINLWLGQRNQKHGLFKGIIQDGKIIFMPNGYITQCPNLNHTCPTCSDFLSLVQGIMDLQELLAKMTAKLNYAETRLSQLENCHCEKTCQVSGLLYRDQDSWVDGDHCRNCTCKSGAVECRRMSCPPLNCSPDSLPVHIAGQCCKVCRPKCIYGGKVLAEGQRILTKSCRECRGGVLVKITEMCPPLNCSEKDHILPENQCCRVCRGHNFCAEGPKCGENSECKNWNTKATCECKSGYISVQGDSAYCEDIDECAAKMHYCHANTVCVNLPGLYRCDCVPGYIRVDDFSCTEHDECGSGQHNCDENAICTNTVQGHSCTCKPGYVGNGTICRAFCEEGCRYGGTCVAPNKCVCPSGFTGSHCEKDIDECSEGIIECHNHSRCVNLPGWYHCECRSGFHDDGTYSLSGESCIDIDECALRTHTCWNDSACINLAGGFDCLCPSGPSCSGDCPHEGGLKHNGQVWTLKEDRCSVCSCKDGKIFCRRTACDCQNPSADLFCCPECDTRVTSQCLDQNGHKLYRSGDNWTHSCQQCRCLEGEVDCWPLTCPNLSCEYTAILEGECCPRCVSDPCLADNITYDIRKTCLDSYGVSRLSGSVWTMAGSPCTTCKCKNGRVCCSVDFECLQNN TT7H4BF TT Literature-reported TTHZ752 ID TTHZ752 TTHZ752 TN Nestin (NES) TTHZ752 UP P48681 TTHZ752 UC NEST_HUMAN TTHZ752 SN Nbla00170 TTHZ752 GN NES TTHZ752 FC Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells. Required for brain and eye development. TTHZ752 SQ MEGCMGEESFQMWELNRRLEAYLARVKALEEQNELLSAELGGLRAQSADTSWRAHADDELAALRALVDQRWREKHAAEVARDNLAEELEGVAGRCQQLRLARERTTEEVARNRRAVEAEKCARAWLSSQVAELERELEALRVAHEEERVGLNAQAACAPRCPAPPRGPPAPAPEVEELARRLGEAWRGAVRGYQERVAHMETSLGQARERLGRAVQGAREGRLELQQLQAERGGLLERRAALEQRLEGRWQERLRATEKFQLAVEALEQEKQGLQSQIAQVLEGRQQLAHLKMSLSLEVATYRTLLEAENSRLQTPGGGSKTSLSFQDPKLELQFPRTPEGRRLGSLLPVLSPTSLPSPLPATLETPVPAFLKNQEFLQARTPTLASTPIPPTPQAPSPAVDAEIRAQDAPLSLLQTQGGRKQAPEPLRAEARVAIPASVLPGPEEPGGQRQEASTGQSPEDHASLAPPLSPDHSSLEAKDGESGGSRVFSICRGEGEGQIWGLVEKETAIEGKVVSSLQQEIWEEEDLNRKEIQDSQVPLEKETLKSLGEEIQESLKTLENQSHETLERENQECPRSLEEDLETLKSLEKENKELLKDVEVVRPLEKEAVGQLKPTGKEDTQTLQSLQKENQELMKSLEGNLETFLFPGTENQELVSSLQENLESLTALEKENQEPLRSPEVGDEEALRPLTKENQEPLRSLEDENKEAFRSLEKENQEPLKTLEEEDQSIVRPLETENHKSLRSLEEQDQETLRTLEKETQQRRRSLGEQDQMTLRPPEKVDLEPLKSLDQEIARPLENENQEFLKSLKEESVEAVKSLETEILESLKSAGQENLETLKSPETQAPLWTPEEINQGAMNPLEKEIQEPLESVEVNQETFRLLEEENQESLRSLGAWNLENLRSPEEVDKESQRNLEEEENLGKGEYQESLRSLEEEGQELPQSADVQRWEDTVEKDQELAQESPPGMAGVENEDEAELNLREQDGFTGKEEVVEQGELNATEEVWIPGEGHPESPEPKEQRGLVEGASVKGGAEGLQDPEGQSQQVGAPGLQAPQGLPEAIEPLVEDDVAPGGDQASPEVMLGSEPAMGESAAGAEPGPGQGVGGLGDPGHLTREEVMEPPLEEESLEAKRVQGLEGPRKDLEEAGGLGTEFSELPGKSRDPWEPPREGREESEAEAPRGAEEAFPAETLGHTGSDAPSPWPLGSEEAEEDVPPVLVSPSPTYTPILEDAPGPQPQAEGSQEASWGVQGRAEALGKVESEQEELGSGEIPEGPQEEGEESREESEEDELGETLPDSTPLGFYLRSPTSPRWDPTGEQRPPPQGETGKEGWDPAVLASEGLEAPPSEKEEGEEGEEECGRDSDLSEEFEDLGTEAPFLPGVPGEVAEPLGQVPQLLLDPAAWDRDGESDGFADEEESGEEGEEDQEEGREPGAGRWGPGSSVGSLQALSSSQRGEFLESDSVSVSVPWDDSLRGAVAGAPKTALETESQDSAEPSGSEEESDPVSLEREDKVPGPLEIPSGMEDAGPGADIIGVNGQGPNLEGKSQHVNGGVMNGLEQSEEVGQGMPLVSEGDRGSPFQEEEGSALKTSWAGAPVHLGQGQFLKFTQREGDRESWSSGED TTHZ752 TT Literature-reported TTHZ752 FM Intermediate filament family TTWAGKJ ID TTWAGKJ TTWAGKJ TN Neuregulin 4 (NRG4) TTWAGKJ UP Q8WWG1 TTWAGKJ UC NRG4_HUMAN TTWAGKJ SN Pro-neuregulin-4, membrane-bound isoform; Pro-NRG4 TTWAGKJ GN NRG4 TTWAGKJ FC Low affinity ligand for the ERBB4 tyrosine kinase receptor. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. Does not bind to the ERBB1, ERBB2 and ERBB3 receptors (By similarity). TTWAGKJ SQ MPTDHEEPCGPSHKSFCLNGGLCYVIPTIPSPFCRCVENYTGARCEEVFLPGSSIQTKSNLFEAFVALAVLVTLIIGAFYFLCRKGHFQRASSVQYDINLVETSSTSAHHSHEQH TTWAGKJ TT Literature-reported TTS05MJ ID TTS05MJ TTS05MJ TN Neuritin (NRN1) TTS05MJ UP Q9NPD7 TTS05MJ UC NRN1_HUMAN TTS05MJ SN NRN TTS05MJ GN NRN1 TTS05MJ FC Promotes neurite outgrowth and especially branching of neuritic processes in primary hippocampal and cortical cells. TTS05MJ SQ MGLKLNGRYISLILAVQIAYLVQAVRAAGKCDAVFKGFSDCLLKLGDSMANYPQGLDDKTNIKTVCTYWEDFHSCTVTALTDCQEGAKDMWDKLRKESKNLNIQGSLFELCGSGNGAAGSLLPAFPVLLVSLSAALATWLSF TTS05MJ TT Literature-reported TTS05MJ FM Neuritin family TT3RWZF ID TT3RWZF TT3RWZF TN Neuro/glioblastoma derived oncogene (Herstatin) TT3RWZF UP Q9UK79 TT3RWZF UC Q9UK79_HUMAN TT3RWZF SN V-erb-b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastoma derived oncogene homolog (Avian), isoform CRA_a; Herstatin; ERBB2 TT3RWZF GN HER-2 TT3RWZF FC An autoinhibitor of the ErbB family consisting of subdomains I and II of the human epidermal growth factor receptor 2 (ErbB-2) extracellular domain and a novel C-terminal domain encoded by an intron. Binds to human epidermal growth factor receptor 2 and to the epidermal growth factor receptor (EGFR), blocking receptor oligomerization and tyrosine phosphorylation. TT3RWZF SQ MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARGTHSLPPRPAAVPVPLRMQPGPAHPVLSFLRPSWDLVSAFYSLPLAPLSPTSVPISPVSVGRGPDPDAHVAVDLSRYEG TT3RWZF TT Literature-reported TTI7T1Q ID TTI7T1Q TTI7T1Q TN Neuromedin-U receptor 1 (NMUR1) TTI7T1Q UP Q9HB89 TTI7T1Q UC NMUR1_HUMAN TTI7T1Q SN NMU-R1; GPR66; G-protein coupled receptor FM-3; G-protein coupled receptor 66 TTI7T1Q GN NMUR1 TTI7T1Q FC Receptor for the neuromedin-U and neuromedin-S neuropeptides. TTI7T1Q SQ MTPLCLNCSVLPGDLYPGGARNPMACNGSAARGHFDPEDLNLTDEALRLKYLGPQQTELFMPICATYLLIFVVGAVGNGLTCLVILRHKAMRTPTNYYLFSLAVSDLLVLLVGLPLELYEMWHNYPFLLGVGGCYFRTLLFEMVCLASVLNVTALSVERYVAVVHPLQARSMVTRAHVRRVLGAVWGLAMLCSLPNTSLHGIRQLHVPCRGPVPDSAVCMLVRPRALYNMVVQTTALLFFCLPMAIMSVLYLLIGLRLRRERLLLMQEAKGRGSAAARSRYTCRLQQHDRGRRQVTKMLFVLVVVFGICWAPFHADRVMWSVVSQWTDGLHLAFQHVHVISGIFFYLGSAANPVLYSLMSSRFRETFQEALCLGACCHRLRPRHSSHSLSRMTTGSTLCDVGSLGSWVHPLAGNDGPEAQQETDPS TTI7T1Q TT Literature-reported TT2L6C5 ID TT2L6C5 TT2L6C5 TN Neuromedin-U receptor 2 (NMUR2) TT2L6C5 UP Q9GZQ4 TT2L6C5 UC NMUR2_HUMAN TT2L6C5 SN TGR1; NMU2R; NMU-R2; G-protein coupled receptor TGR-1; G-protein coupled receptor FM-4 TT2L6C5 GN NMUR2 TT2L6C5 FC Receptor for the neuromedin-U and neuromedin-S neuropeptides. TT2L6C5 SQ MSGMEKLQNASWIYQQKLEDPFQKHLNSTEEYLAFLCGPRRSHFFLPVSVVYVPIFVVGVIGNVLVCLVILQHQAMKTPTNYYLFSLAVSDLLVLLLGMPLEVYEMWRNYPFLFGPVGCYFKTALFETVCFASILSITTVSVERYVAILHPFRAKLQSTRRRALRILGIVWGFSVLFSLPNTSIHGIKFHYFPNGSLVPGSATCTVIKPMWIYNFIIQVTSFLFYLLPMTVISVLYYLMALRLKKDKSLEADEGNANIQRPCRKSVNKMLFVLVLVFAICWAPFHIDRLFFSFVEEWSESLAAVFNLVHVVSGVFFYLSSAVNPIIYNLLSRRFQAAFQNVISSFHKQWHSQHDPQLPPAQRNIFLTECHFVELTEDIGPQFPCQSSMHNSHLPAALSSEQMSRTNYQSFHFNKT TT2L6C5 TT Literature-reported TTEP027 ID TTEP027 TTEP027 TN Neuropeptide FF receptor 1 (NPFFR1) TTEP027 UP Q9GZQ6 TTEP027 UC NPFF1_HUMAN TTEP027 SN RFamide-related peptide receptor OT7T022; NPFF1; GPR147; G-protein coupled receptor 147 TTEP027 GN NPFFR1 TTEP027 FC Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. TTEP027 SQ MEGEPSQPPNSSWPLSQNGTNTEATPATNLTFSSYYQHTSPVAAMFIVAYALIFLLCMVGNTLVCFIVLKNRHMHTVTNMFILNLAVSDLLVGIFCMPTTLVDNLITGWPFDNATCKMSGLVQGMSVSASVFTLVAIAVERFRCIVHPFREKLTLRKALVTIAVIWALALLIMCPSAVTLTVTREEHHFMVDARNRSYPLYSCWEAWPEKGMRRVYTTVLFSHIYLAPLALIVVMYARIARKLCQAPGPAPGGEEAADPRASRRRARVVHMLVMVALFFTLSWLPLWALLLLIDYGQLSAPQLHLVTVYAFPFAHWLAFFNSSANPIIYGYFNENFRRGFQAAFRARLCPRPSGSHKEAYSERPGGLLHRRVFVVVRPSDSGLPSESGPSSGAPRPGRLPLRNGRVAHHGLPREGPGCSHLPLTIPAWDI TTEP027 TT Literature-reported TTXYNDJ ID TTXYNDJ TTXYNDJ TN Neuropeptide FF receptor 2 (NPFFR2) TTXYNDJ UP Q9Y5X5 TTXYNDJ UC NPFF2_HUMAN TTXYNDJ SN Neuropeptide G-protein coupled receptor; NPGPR; NPFF2; GPR74; G-protein coupled receptor HLWAR77; G-protein coupled receptor 74 TTXYNDJ GN NPFFR2 TTXYNDJ FC Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. TTXYNDJ SQ MNSFFGTPAASWCLLESDVSSAPDKEAGRERRALSVQQRGGPAWSGSLEWSRQSAGDRRRLGLSRQTAKSSWSRSRDRTCCCRRAWWILVPAADRARRERFIMNEKWDTNSSENWHPIWNVNDTKHHLYSDINITYVNYYLHQPQVAAIFIISYFLIFFLCMMGNTVVCFIVMRNKHMHTVTNLFILNLAISDLLVGIFCMPITLLDNIIAGWPFGNTMCKISGLVQGISVAASVFTLVAIAVDRFQCVVYPFKPKLTIKTAFVIIMIIWVLAITIMSPSAVMLHVQEEKYYRVRLNSQNKTSPVYWCREDWPNQEMRKIYTTVLFANIYLAPLSLIVIMYGRIGISLFRAAVPHTGRKNQEQWHVVSRKKQKIIKMLLIVALLFILSWLPLWTLMMLSDYADLSPNELQIINIYIYPFAHWLAFGNSSVNPIIYGFFNENFRRGFQEAFQLQLCQKRAKPMEAYALKAKSHVLINTSNQLVQESTFQNPHGETLLYRKSAEKPQQELVMEELKETTNSSEI TTXYNDJ TT Literature-reported TT31Q0V ID TT31Q0V TT31Q0V TN Neurotensin receptor type 2 (NTSR2) TT31Q0V UP O95665 TT31Q0V UC NTR2_HUMAN TT31Q0V SN NTR2; NT-R-2; Levocabastine-sensitive neurotensin receptor TT31Q0V GN NTSR2 TT31Q0V FC Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. TT31Q0V SQ METSSPRPPRPSSNPGLSLDARLGVDTRLWAKVLFTALYALIWALGAAGNALSAHVVLKARAGRAGRLRHHVLSLALAGLLLLLVGVPVELYSFVWFHYPWVFGDLGCRGYYFVHELCAYATVLSVAGLSAERCLAVCQPLRARSLLTPRRTRWLVALSWAASLGLALPMAVIMGQKHELETADGEPEPASRVCTVLVSRTALQVFIQVNVLVSFVLPLALTAFLNGVTVSHLLALCSQVPSTSTPGSSTPSRLELLSEEGLLSFIVWKKTFIQGGQVSLVRHKDVRRIRSLQRSVQVLRAIVVMYVICWLPYHARRLMYCYVPDDAWTDPLYNFYHYFYMVTNTLFYVSSAVTPLLYNAVSSSFRKLFLEAVSSLCGEHHPMKRLPPKPQSPTLMDTASGFGDPPETRT TT31Q0V TT Literature-reported TTIMLZ6 ID TTIMLZ6 TTIMLZ6 TN Neurotransmitter transporter NTT4 (SLC6A17) TTIMLZ6 UP Q9H1V8 TTIMLZ6 UC S6A17_HUMAN TTIMLZ6 SN Solute carrier family 6 member 17; Sodium-dependent neutral amino acid transporter SLC6A17; Sodium-dependent neurotransmitter transporter NTT4; NTT4 TTIMLZ6 GN SLC6A17 TTIMLZ6 FC Functions as a sodium-dependent vesicular transporter selective for proline, glycine, leucine and alanine. In contrast to other members of this neurotransmitter transporter family, does not appear to be chloride-dependent (By similarity). TTIMLZ6 SQ MPKNSKVTQREHSSEHVTESVADLLALEEPVDYKQSVLNVAGEAGGKQKAVEEELDAEDRPAWNSKLQYILAQIGFSVGLGNIWRFPYLCQKNGGGAYLVPYLVLLIIIGIPLFFLELAVGQRIRRGSIGVWHYICPRLGGIGFSSCIVCLFVGLYYNVIIGWSIFYFFKSFQYPLPWSECPVVRNGSVAVVEAECEKSSATTYFWYREALDISDSISESGGLNWKMTLCLLVAWSIVGMAVVKGIQSSGKVMYFSSLFPYVVLACFLVRGLLLRGAVDGILHMFTPKLDKMLDPQVWREAATQVFFALGLGFGGVIAFSSYNKQDNNCHFDAALVSFINFFTSVLATLVVFAVLGFKANIMNEKCVVENAEKILGYLNTNVLSRDLIPPHVNFSHLTTKDYMEMYNVIMTVKEDQFSALGLDPCLLEDELDKSVQGTGLAFIAFTEAMTHFPASPFWSVMFFLMLINLGLGSMIGTMAGITTPIIDTFKVPKEMFTVGCCVFAFLVGLLFVQRSGNYFVTMFDDYSATLPLTLIVILENIAVAWIYGTKKFMQELTEMLGFRPYRFYFYMWKFVSPLCMAVLTTASIIQLGVTPPGYSAWIKEEAAERYLYFPNWAMALLITLIVVATLPIPVVFVLRHFHLLSDGSNTLSVSYKKGRMMKDISNLEENDETRFILSKVPSEAPSPMPTHRSYLGPGSTSPLETSGNPNGRYGSGYLLASTPESEL TTIMLZ6 TT Literature-reported TT16TM5 ID TT16TM5 TT16TM5 TN N-formyl peptide receptor 3 (FPR3) TT16TM5 UP P25089 TT16TM5 UC FPR3_HUMAN TT16TM5 SN Formyl peptide receptor-like 2; FPRL2; FPRH1; FMLP-related receptor II; FMLP-R-II TT16TM5 GN FPR3 TT16TM5 FC Low affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophils chemotactic factors. Binding of FMLP to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. TT16TM5 SQ METNFSIPLNETEEVLPEPAGHTVLWIFSLLVHGVTFVFGVLGNGLVIWVAGFRMTRTVNTICYLNLALADFSFSAILPFRMVSVAMREKWPFGSFLCKLVHVMIDINLFVSVYLITIIALDRCICVLHPAWAQNHRTMSLAKRVMTGLWIFTIVLTLPNFIFWTTISTTNGDTYCIFNFAFWGDTAVERLNVFITMAKVFLILHFIIGFSVPMSIITVCYGIIAAKIHRNHMIKSSRPLRVFAAVVASFFICWFPYELIGILMAVWLKEMLLNGKYKIILVLINPTSSLAFFNSCLNPILYVFMGRNFQERLIRSLPTSLERALTEVPDSAQTSNTDTTSASPPEETELQAM TT16TM5 TT Literature-reported TTG53PQ ID TTG53PQ TTG53PQ TN NKG2D-NKG2D ligand interaction (NKG2D-NKG2DL PPI) TTG53PQ UP P26718-Q9BZM6/Q9BZM5/Q9BZM4 TTG53PQ UC NKG2D_HUMAN-ULBP1_HUMAN/ULBP2_HUMAN/ULBP3_HUMAN TTG53PQ SN NK cell receptor D-NKG2D ligand interaction TTG53PQ GN KLRK1-ULBP1/ULBP2/ULBP3 TTG53PQ FC Inhibits the outgrowth of naturally arising low-grade B cell lymphoma In vivo. TTG53PQ SQ MGWIRGRRSRHSWEMSEFHNYNLDLKKSDFSTRWQKQRCPVVKSKCRENASPFFFCCFIAVAMGIRFIIMVAIWSAVFLNSLFNQEVQIPLTESYCGPCPKNWICYKNNCYQFFDESKNWYESQASCMSQNASLLKVYSKEDQDLLKLVKSYHWMGLVHIPTNGSWQWEDGSILSPNLLTIIEMQKGDCALYASSFKGYIENCSTPNTYICMQRTVMAAAASPAFLLCLPLLHLLSGWSRAGWVDTHCLCYDFIITPKSRPEPQWCEVQGLVDERPFLHYDCVNHKAKAFASLGKKVNVTKTWEEQTETLRDVVDFLKGQLLDIQVENLIPIEPLTLQARMSCEHEAHGHGRGSWQFLFNGQKFLLFDSNNRKWTALHPGAKKMTEKWEKNRDVTMFFQKISLGDCKMWLEEFLMYWEQMLDPTKPPSLAPGTTQPKAMATTLSPWSLLIIFLCFILAGR TTG53PQ TT Literature-reported TTK1CX7 ID TTK1CX7 TTK1CX7 TN Olfactomedin 4 (OLFM4) TTK1CX7 UP Q6UX06 TTK1CX7 UC OLFM4_HUMAN TTK1CX7 SN hOLfD; hGC-1; UNQ362/PRO698; Olfactomedin-4; OLM4; GW112; G-CSF-stimulated clone 1 protein; Antiapoptotic protein GW112 TTK1CX7 GN OLFM4 TTK1CX7 FC May promote proliferation of pancreatic cancer cells by favoring the transition from the S to G2/M phase. In myeloid leukemic cell lines, inhibits cell growth and induces cell differentiation and apoptosis. May play a role in the inhibition of EIF4EBP1 phosphorylation/deactivation. Facilitates cell adhesion, most probably through interaction with cell surface lectins and cadherin. TTK1CX7 SQ MRPGLSFLLALLFFLGQAAGDLGDVGPPIPSPGFSSFPGVDSSSSFSSSSRSGSSSSRSLGSGGSVSQLFSNFTGSVDDRGTCQCSVSLPDTTFPVDRVERLEFTAHVLSQKFEKELSKVREYVQLISVYEKKLLNLTVRIDIMEKDTISYTELDFELIKVEVKEMEKLVIQLKESFGGSSEIVDQLEVEIRNMTLLVEKLETLDKNNVLAIRREIVALKTKLKECEASKDQNTPVVHPPPTPGSCGHGGVVNISKPSVVQLNWRGFSYLYGAWGRDYSPQHPNKGLYWVAPLNTDGRLLEYYRLYNTLDDLLLYINARELRITYGQGSGTAVYNNNMYVNMYNTGNIARVNLTTNTIAVTQTLPNAAYNNRFSYANVAWQDIDFAVDENGLWVIYSTEASTGNMVISKLNDTTLQVLNTWYTKQYKPSASNAFMVCGVLYATRTMNTRTEEIFYYYDTNTGKEGKLDIVMHKMQEKVQSINYNPFDQKLYVYNDGYLLNYDLSVLQKPQ TTK1CX7 TT Literature-reported TTU7HRD ID TTU7HRD TTU7HRD TN Oligophrenin-1 (OPHN1) TTU7HRD UP O60890 TTU7HRD UC OPHN1_HUMAN TTU7HRD SN Oligophrenin1; OPHN1 TTU7HRD GN OPHN1 TTU7HRD FC Stimulates GTP hydrolysis of members of the Rho family. Its action on RHOA activity and signaling is implicated in growth and stabilization of dendritic spines, and therefore in synaptic function. Critical for the stabilization of AMPA receptors at postsynaptic sites. Critical for the regulation of synaptic vesicle endocytosis at presynaptic terminals. Required for the localization of NR1D1 to dendrites, can suppress its repressor activity and protect it fromproteasomal degradation. TTU7HRD SQ MGHPPLEFSDCYLDSPDFRERLKCYEQELERTNKFIKDVIKDGNALISAMRNYSSAVQKFSQTLQSFQFDFIGDTLTDDEINIAESFKEFAELLNEVENERMMMVHNASDLLIKPLENFRKEQIGFTKERKKKFEKDGERFYSLLDRHLHLSSKKKESQLQEADLQVDKERHNFFESSLDYVYQIQEVQESKKFNIVEPVLAFLHSLFISNSLTVELTQDFLPYKQQLQLSLQNTRNHFSSTREEMEELKKRMKEAPQTCKLPGQPTIEGYLYTQEKWALGISWVKYYCQYEKETKTLTMTPMEQKPGAKQGPLDLTLKYCVRRKTESIDKRFCFDIETNERPGTITLQALSEANRRLWMEAMDGKEPIYHSPITKQQEMELNEVGFKFVRKCINIIETKGIKTEGLYRTVGSNIQVQKLLNAFFDPKCPGDVDFHNSDWDIKTITSSLKFYLRNLSEPVMTYRLHKELVSAAKSDNLDYRLGAIHSLVYKLPEKNREMLELLIRHLVNVCEHSKENLMTPSNMGVIFGPTLMRAQEDTVAAMMNIKFQNIVVEILIEHFGKIYLGPPEESAAPPVPPPRVTARRHKPITISKRLLRERTVFYTSSLDESEDEIQHQTPNGTITSSIEPPKPPQHPKLPIQRSGETDPGRKSPSRPILDGKLEPCPEVDVGKLVSRLQDGGTKITPKATNGPMPGSGPTKTPSFHIKRPAPRPLAHHKEGDADSFSKVRPPGEKPTIIRPPVRPPDPPCRAATPQKPEPKPDIVAGNAGEITSSVVASRTRFFETASRKTGSSQGRLPGDES TTU7HRD TT Literature-reported TTDL3UZ ID TTDL3UZ TTDL3UZ TN Organic anion transporter B (SLCO2B1) TTDL3UZ UP O94956 TTDL3UZ UC SO2B1_HUMAN TTDL3UZ SN Solute carrier organic anion transporter family member 2B1; Solute carrier family 21 member 9; SLC21A9; Organic anion transporter polypeptide-related protein 2; OATPRP2; OATPB; OATP2B1; OATP-RP2; OATP-B; KIAA0880 TTDL3UZ GN SLCO2B1 TTDL3UZ FC Mediates the Na(+)-independent transport of organic anions such as taurocholate, the prostaglandins PGD2, PGE1, PGE2, leukotriene C4, thromboxane B2 and iloprost. TTDL3UZ SQ MGPRIGPAGEVPQVPDKETKATMGTENTPGGKASPDPQDVRPSVFHNIKLFVLCHSLLQLAQLMISGYLKSSISTVEKRFGLSSQTSGLLASFNEVGNTALIVFVSYFGSRVHRPRMIGYGAILVALAGLLMTLPHFISEPYRYDNTSPEDMPQDFKASLCLPTTSAPASAPSNGNCSSYTETQHLSVVGIMFVAQTLLGVGGVPIQPFGISYIDDFAHNSNSPLYLGILFAVTMMGPGLAFGLGSLMLRLYVDINQMPEGGISLTIKDPRWVGAWWLGFLIAAGAVALAAIPYFFFPKEMPKEKRELQFRRKVLAVTDSPARKGKDSPSKQSPGESTKKQDGLVQIAPNLTVIQFIKVFPRVLLQTLRHPIFLLVVLSQVCLSSMAAGMAIFLPKFLERQFSITASYANLLIGCLSFPSVIVGIVVGGVLVKRLHLGPVGCGALCLLGMLLCLFFSLPLFFIGCSSHQIAGITHQTSAHPGLELSPSCMEACSCPLDGFNPVCDPSTRVEYITPCHAGCSSWVVQDALDNSQVFYTNCSCVVEGNPVLAGSCDSTCSHLVVPFLLLVSLGSALACLTHTPSFMLILRGVKKEDKTLAVGIQFMFLRILAWMPSPVIHGSAIDTTCVHWALSCGRRAVCRYYNNDLLRNRFIGLQFFFKTGSVICFALVLAVLRQQDKEARTKESRSSPAVEQQLLVSGPGKKPEDSRV TTDL3UZ TT Literature-reported TT5CE6L ID TT5CE6L TT5CE6L TN Organic anion transporter D (SLCO3A1) TT5CE6L UP Q9UIG8 TT5CE6L UC SO3A1_HUMAN TT5CE6L SN Solute carrier organic anion transporter family member 3A1; Solute carrier family 21 member 11; Sodium-independent organic anion transporter D; SLC21A11; PGE1 transporter; Organic anion-transporting polypeptide D; Organic anion transporter polypeptide-related protein 3; OATPRP3; OATPD; OATP3A1; OATP-RP3; OATP-D TT5CE6L GN SLCO3A1 TT5CE6L FC Mediates the Na(+)-independent transport of organic anions such as estrone-3-sulfate. Mediates transport of prostaglandins (PG) E1 and E2, thyroxine (T4), deltorphin II, BQ-123 and vasopressin, but not DPDPE (a derivative of enkephalin lacking an N-terminal tyrosine residue), estrone-3-sulfate, taurocholate, digoxin nor DHEAS. TT5CE6L SQ MQGKKPGGSSGGGRSGELQGDEAQRNKKKKKKVSCFSNIKIFLVSECALMLAQGTVGAYLVSVLTTLERRFNLQSADVGVIASSFEIGNLALILFVSYFGARGHRPRLIGCGGIVMALGALLSALPEFLTHQYKYEAGEIRWGAEGRDVCAANGSGGDEGPDPDLICRNRTATNMMYLLLIGAQVLLGIGATPVQPLGVSYIDDHVRRKDSSLYIGILFTMLVFGPACGFILGSFCTKIYVDAVFIDTSNLDITPDDPRWIGAWWGGFLLCGALLFFSSLLMFGFPQSLPPHSEPAMESEQAMLSEREYERPKPSNGVLRHPLEPDSSASCFQQLRVIPKVTKHLLSNPVFTCIILAACMEIAVVAGFAAFLGKYLEQQFNLTTSSANQLLGMTAIPCACLGIFLGGLLVKKLSLSALGAIRMAMLVNLVSTACYVSFLFLGCDTGPVAGVTVPYGNSTAPGSALDPYSPCNNNCECQTDSFTPVCGADGITYLSACFAGCNSTNLTGCACLTTVPAENATVVPGKCPSPGCQEAFLTFLCVMCICSLIGAMAQTPSVIILIRTVSPELKSYALGVLFLLLRLLGFIPPPLIFGAGIDSTCLFWSTFCGEQGACVLYDNVVYRYLYVSIAIALKSFAFILYTTTWQCLRKNYKRYIKNHEGGLSTSEFFASTLTLDNLGRDPVPANQTHRTKFIYNLEDHEWCENMESVL TT5CE6L TT Literature-reported TTV1YIE ID TTV1YIE TTV1YIE TN Organic anion transporter E (SLCO4A1) TTV1YIE UP Q96BD0 TTV1YIE UC SO4A1_HUMAN TTV1YIE SN Solute carrier organic anion transporter family member 4A1; Solute carrier family 21 member 12; Sodium-independent organic anion transporter E; SLC21A12; POAT; Organic anion-transporting polypeptide E; Organic anion transporter polypeptide-related protein 1; OATPRP1; OATPE; OATP4A1; OATP1; OATP-RP1; OATP-E; Colon organic anion transporter TTV1YIE GN SLCO4A1 TTV1YIE FC Mediates the Na(+)-independent transport of organic anions such as the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and of estrone-3-sulfate and taurocholate. TTV1YIE SQ MPLHQLGDKPLTFPSPNSAMENGLDHTPPSRRASPGTPLSPGSLRSAAHSPLDTSKQPLCQLWAEKHGARGTHEVRYVSAGQSVACGWWAFAPPCLQVLNTPKGILFFLCAAAFLQGMTVNGFINTVITSLERRYDLHSYQSGLIASSYDIAACLCLTFVSYFGGSGHKPRWLGWGVLLMGTGSLVFALPHFTAGRYEVELDAGVRTCPANPGAVCADSTSGLSRYQLVFMLGQFLHGVGATPLYTLGVTYLDENVKSSCSPVYIAIFYTAAILGPAAGYLIGGALLNIYTEMGRRTELTTESPLWVGAWWVGFLGSGAAAFFTAVPILGYPRQLPGSQRYAVMRAAEMHQLKDSSRGEASNPDFGKTIRDLPLSIWLLLKNPTFILLCLAGATEATLITGMSTFSPKFLESQFSLSASEAATLFGYLVVPAGGGGTFLGGFFVNKLRLRGSAVIKFCLFCTVVSLLGILVFSLHCPSVPMAGVTASYGGSLLPEGHLNLTAPCNAACSCQPEHYSPVCGSDGLMYFSLCHAGCPAATETNVDGQKVYRDCSCIPQNLSSGFGHATAGKCTSTCQRKPLLLVFIFVVIFFTFLSSIPALTATLRCVRDPQRSFALGIQWIVVRILGGIPGPIAFGWVIDKACLLWQDQCGQQGSCLVYQNSAMSRYILIMGLLYKVLGVLFFAIACFLYKPLSESSDGLETCLPSQSSAPDSATDSQLQSSV TTV1YIE TT Literature-reported TT340CE ID TT340CE TT340CE TN Organic anion transporter F (SLCO1C1) TT340CE UP Q9NYB5 TT340CE UC SO1C1_HUMAN TT340CE SN Thyroxine transporter; Solute carrier organic anion transporter family member 1C1; Solute carrier family 21 member 14; SLC21A14; Organic anion-transporting polypeptide 14; Organic anion transporter polypeptide-related protein 5; OATPRP5; OATPF; OATP1C1; OATP14; OATP-F; OATP-14; OAT-RP-5 TT340CE GN SLCO1C1 TT340CE FC Mediates the Na(+)-independent high affinity transport of organic anions such as the thyroid hormones thyroxine (T4) and rT3. Other potential substrates, such as triiodothyronine (T3), 17-beta-glucuronosyl estradiol, estrone-3-sulfate and sulfobromophthalein (BSP) are transported with much lower efficiency. May play a significant role in regulating T4 flux into and out of the brain (By similarity). TT340CE SQ MDTSSKENIQLFCKTSVQPVGRPSFKTEYPSSEEKQPCCGELKVFLCALSFVYFAKALAEGYLKSTITQIERRFDIPSSLVGVIDGSFEIGNLLVITFVSYFGAKLHRPKIIGAGCVIMGVGTLLIAMPQFFMEQYKYERYSPSSNSTLSISPCLLESSSQLPVSVMEKSKSKISNECEVDTSSSMWIYVFLGNLLRGIGETPIQPLGIAYLDDFASEDNAAFYIGCVQTVAIIGPIFGFLLGSLCAKLYVDIGFVNLDHITITPKDPQWVGAWWLGYLIAGIISLLAAVPFWYLPKSLPRSQSREDSNSSSEKSKFIIDDHTDYQTPQGENAKIMEMARDFLPSLKNLFGNPVYFLYLCTSTVQFNSLFGMVTYKPKYIEQQYGQSSSRANFVIGLINIPAVALGIFSGGIVMKKFRISVCGAAKLYLGSSVFGYLLFLSLFALGCENSDVAGLTVSYQGTKPVSYHERALFSDCNSRCKCSETKWEPMCGENGITYVSACLAGCQTSNRSGKNIIFYNCTCVGIAASKSGNSSGIVGRCQKDNGCPQMFLYFLVISVITSYTLSLGGIPGYILLLRCIKPQLKSFALGIYTLAIRVLAGIPAPVYFGVLIDTSCLKWGFKRCGSRGSCRLYDSNVFRHIYLGLTVILGTVSILLSIAVLFILKKNYVSKHRSFITKRERTMVSTRFQKENYTTSDHLLQPNYWPGKETQL TT340CE TT Literature-reported TTG2UMS ID TTG2UMS TTG2UMS TN Organic cation transporter 3 (OCT3) TTG2UMS UP O75751 TTG2UMS UC S22A3_HUMAN TTG2UMS SN Solute carrier family 22 member 3; Extraneuronal monoamine transporter; EMTH TTG2UMS GN SLC22A3 TTG2UMS FC Mediates potential-dependent transport of a variety of organic cations. May play a significant role in the disposition of cationic neurotoxins and neurotransmitters in the brain. TTG2UMS SQ MPSFDEALQRVGEFGRFQRRVFLLLCLTGVTFAFLFVGVVFLGTQPDHYWCRGPSAAALAERCGWSPEEEWNRTAPASRGPEPPERRGRCQRYLLEAANDSASATSALSCADPLAAFPNRSAPLVPCRGGWRYAQAHSTIVSEFDLVCVNAWMLDLTQAILNLGFLTGAFTLGYAADRYGRIVIYLLSCLGVGVTGVVVAFAPNFPVFVIFRFLQGVFGKGTWMTCYVIVTEIVGSKQRRIVGIVIQMFFTLGIIILPGIAYFIPNWQGIQLAITLPSFLFLLYYWVVPESPRWLITRKKGDKALQILRRIAKCNGKYLSSNYSEITVTDEEVSNPSFLDLVRTPQMRKCTLILMFAWFTSAVVYQGLVMRLGIIGGNLYIDFFISGVVELPGALLILLTIERLGRRLPFAASNIVAGVACLVTAFLPEGIAWLRTTVATLGRLGITMAFEIVYLVNSELYPTTLRNFGVSLCSGLCDFGGIIAPFLLFRLAAVWLELPLIIFGILASICGGLVMLLPETKGIALPETVDDVEKLGSPHSCKCGRNKKTPVSRSHL TTG2UMS TT Literature-reported TT7WBSV ID TT7WBSV TT7WBSV TN Oxoeicosanoid receptor 1 (OXER1) TT7WBSV UP Q8TDS5 TT7WBSV UC OXER1_HUMAN TT7WBSV SN TG1019; GPR170; G-protein coupled receptor TG1019; G-protein coupled receptor R527; G-protein coupled receptor 170; 5-oxo-ETE G-protein coupled receptor TT7WBSV GN OXER1 TT7WBSV FC Receptor for eicosanoids and polyunsaturated fatty acids such as 5-oxo-6E,8Z,11Z,14Z-eicosatetraenoic acid (5-OXO-ETE), 5(S)-hydroperoxy-6E,8Z,11Z,14Z-eicosatetraenoic acid (5(S)-HPETE) and arachidonic acid. Seems to be coupled to the G(i)/G(o), families of heteromeric G proteins. TT7WBSV SQ MLCHRGGQLIVPIIPLCPEHSCRGRRLQNLLSGPWPKQPMELHNLSSPSPSLSSSVLPPSFSPSPSSAPSAFTTVGGSSGGPCHPTSSSLVSAFLAPILALEFVLGLVGNSLALFIFCIHTRPWTSNTVFLVSLVAADFLLISNLPLRVDYYLLHETWRFGAAACKVNLFMLSTNRTASVVFLTAIALNRYLKVVQPHHVLSRASVGAAARVAGGLWVGILLLNGHLLLSTFSGPSCLSYRVGTKPSASLRWHQALYLLEFFLPLALILFAIVSIGLTIRNRGLGGQAGPQRAMRVLAMVVAVYTICFLPSIIFGMASMVAFWLSACRSLDLCTQLFHGSLAFTYLNSVLDPVLYCFSSPNFLHQSRALLGLTRGRQGPVSDESSYQPSRQWRYREASRKAEAIGKLKVQGEVSLEKEGSSQG TT7WBSV TT Literature-reported TTAS1QK ID TTAS1QK TTAS1QK TN Oxoglutarate receptor (OXGR1) TTAS1QK UP Q96P68 TTAS1QK UC OXGR1_HUMAN TTAS1QK SN P2Y15; P2Y-like nucleotide receptor; P2Y-like GPCR; P2Y purinoceptor 15; P2RY15; GPR99; GPR80; G-protein coupled receptor 99; G-protein coupled receptor 80; Alpha-ketoglutarate receptor 1; 2-oxoglutarate receptor 1 TTAS1QK GN OXGR1 TTAS1QK FC Receptor for alpha-ketoglutarate. Seems to act exclusively through a G(q)-mediated pathway (By similarity). TTAS1QK SQ MNEPLDYLANASDFPDYAAAFGNCTDENIPLKMHYLPVIYGIIFLVGFPGNAVVISTYIFKMRPWKSSTIIMLNLACTDLLYLTSLPFLIHYYASGENWIFGDFMCKFIRFSFHFNLYSSILFLTCFSIFRYCVIIHPMSCFSIHKTRCAVVACAVVWIISLVAVIPMTFLITSTNRTNRSACLDLTSSDELNTIKWYNLILTATTFCLPLVIVTLCYTTIIHTLTHGLQTDSCLKQKARRLTILLLLAFYVCFLPFHILRVIRIESRLLSISCSIENQIHEAYIVSRPLAALNTFGNLLLYVVVSDNFQQAVCSTVRCKVSGNLEQAKKISYSNNP TTAS1QK TT Literature-reported TTJW7B3 ID TTJW7B3 TTJW7B3 TN P2X purinoceptor 1 (P2RX1) TTJW7B3 UP P51575 TTJW7B3 UC P2RX1_HUMAN TTJW7B3 SN Purinergic receptor 1; P2X1 TTJW7B3 GN P2RX1 TTJW7B3 FC Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death (By similarity). TTJW7B3 SQ MARRFQEELAAFLFEYDTPRMVLVRNKKVGVIFRLIQLVVLVYVIGWVFLYEKGYQTSSGLISSVSVKLKGLAVTQLPGLGPQVWDVADYVFPAQGDNSFVVMTNFIVTPKQTQGYCAEHPEGGICKEDSGCTPGKAKRKAQGIRTGKCVAFNDTVKTCEIFGWCPVEVDDDIPRPALLREAENFTLFIKNSISFPRFKVNRRNLVEEVNAAHMKTCLFHKTLHPLCPVFQLGYVVQESGQNFSTLAEKGGVVGITIDWHCDLDWHVRHCRPIYEFHGLYEEKNLSPGFNFRFARHFVENGTNYRHLFKVFGIRFDILVDGKAGKFDIIPTMTTIGSGIGIFGVATVLCDLLLLHILPKRHYYKQKKFKYAEDMGPGAAERDLAATSSTLGLQENMRTS TTJW7B3 TT Literature-reported TTMFOU6 ID TTMFOU6 TTMFOU6 TN P2Y purinoceptor 10 (P2RY10) TTMFOU6 UP O00398 TTMFOU6 UC P2Y10_HUMAN TTMFOU6 SN Putative P2Y purinoceptor 10; P2Y10; P2Y-like receptor TTMFOU6 GN P2RY10 TTMFOU6 FC Putative receptor for purines coupled to G-proteins. TTMFOU6 SQ MANLDKYTETFKMGSNSTSTAEIYCNVTNVKFQYSLYATTYILIFIPGLLANSAALWVLCRFISKKNKAIIFMINLSVADLAHVLSLPLRIYYYISHHWPFQRALCLLCFYLKYLNMYASICFLTCISLQRCFFLLKPFRARDWKRRYDVGISAAIWIVVGTACLPFPILRSTDLNNNKSCFADLGYKQMNAVALVGMITVAELAGFVIPVIIIAWCTWKTTISLRQPPMAFQGISERQKALRMVFMCAAVFFICFTPYHINFIFYTMVKETIISSCPVVRIALYFHPFCLCLASLCCLLDPILYYFMASEFRDQLSRHGSSVTRSRLMSKESGSSMIG TTMFOU6 TT Literature-reported TT4FJ3A ID TT4FJ3A TT4FJ3A TN PIN2/TERF1-interacting telomerase inhibitor 1 (PINX1) TT4FJ3A UP Q96BK5 TT4FJ3A UC PINX1_HUMAN TT4FJ3A SN TRF1-interacting protein 1; Protein 67-11-3; Pin2-interacting protein X1; Liver-related putative tumor suppressor; LPTS; LPTL TT4FJ3A GN PINX1 TT4FJ3A FC Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor. Microtubule-binding protein essential for faithful chromosome segregation. TT4FJ3A SQ MSMLAERRRKQKWAVDPQNTAWSNDDSKFGQRMLEKMGWSKGKGLGAQEQGATDHIKVQVKNNHLGLGATINNEDNWIAHQDDFNQLLAELNTCHGQETTDSSDKKEKKSFSLEEKSKISKNRVHYMKFTKGKDLSSRSKTDLDCIFGKRQSKKTPEGDASPSTPEENETTTTSAFTIQEYFAKRMAALKNKPQVPVPGSDISETQVERKRGKKRNKEATGKDVESYLQPKAKRHTEGKPERAEAQERVAKKKSAPAEEQLRGPCWDQSSKASAQDAGDHVQPPEGRDFTLKPKKRRGKKKLQKPVEIAEDATLEETLVKKKKKKDSK TT4FJ3A TT Literature-reported TTM18HX ID TTM18HX TTM18HX TN Placenta specific protein 1 (PLAC1) TTM18HX UP Q9HBJ0 TTM18HX UC PLAC1_HUMAN TTM18HX SN Placentaspecific protein 1; PLAC1 TTM18HX GN PLAC1 TTM18HX FC May play a role in placental development. TTM18HX SQ MKVFKFIGLMILLTSAFSAGSGQSPMTVLCSIDWFMVTVHPFMLNNDVCVHFHELHLGLGCPPNHVQPHAYQFTYRVTECGIRAKAVSQDMVIYSTEIHYSSKGTPSKFVIPVSCAAPQKSPWLTKPCSMRVASKSRATAQKDEKCYEVFSLSQSSQRPNCDCPPCVFSEEEHTQVPCHQAGAQEAQPLQPSHFLDISEDWSLHTDDMIGSM TTM18HX TT Literature-reported TTYXA6Z ID TTYXA6Z TTYXA6Z TN Plasmodium Hexose transporter 1 (Malaria ht1) TTYXA6Z UP O97467 TTYXA6Z UC O97467_PLAFA TTYXA6Z SN ht1; Putative sugar transporter; Hexose transporter TTYXA6Z GN Malaria ht1 TTYXA6Z FC High-affinity glucose transporter. TTYXA6Z SQ MTKSSKDICSENEGKKNGKSGFFSTSFKYVLSACIASFIFGYQVSVLNTIKNFIVVEFEWCKGEKDRLNCSNNTIQSSFLLASVFIGAVLGCGFSGYLVQFGRRLSLLIIYNFFFLVSILTSITHHFHTILFARLLSGFGIGLVTVSVPMYISEMTHKDKKGAYGVMHQLFITFGIFVAVMLGLAMGEGPKADSTEPLTSFAKLWWRLMFLFPSVISLIGILALVVFFKEETPYFLFEKGRIEESKNILKKIYETDNVDEPLNAIKEAVEQNESAKKNSLSLLSALKIPSYRYVIILGCLLSGLQQFTGINVLVSNSNELYKEFLDSHLITILSVVMTAVNFLMTFPAIYIVEKLGRKTLLLWGCVGVLVAYLPTAIANEINRNSNFVKILSIVATFVMIISFAVSYGPVLWIYLHEMFPSEIKDSAASLASLVNWVCAIIVVFPSDIIIKKSPSILFIVFSVMSILTFFFIFFFIKETKGGEIGTSPYITMEERQKHMTKSVV TTYXA6Z TT Literature-reported TT3QW1X ID TT3QW1X TT3QW1X TN Plasmodium Histidine-rich protein II (Malaria HRP II) TT3QW1X UP P90582 TT3QW1X UC P90582_PLAFA TT3QW1X SN Histidine-rich protein II TT3QW1X GN Malaria HRP II TT3QW1X FC Functions as a diagnostic and prognostic marker for falciparum malaria. TT3QW1X SQ MVSFSKNKVLSAAVFASVLLLDNNNSAFNNNLCSKNAKGLNLNKRLLHETQAHVDDAHHAHHVADAHHAHHAADAHHAHHAADAHHAHHAADAHHAHHAADAHHAHHAAYAHHAHHAADAHHAHHASDAHHAADAHHAAYAHHAHHAADAHHAHHASDAHHAADAHHAAYAHHAHHAADAHHAADAHHATDAHHAHHAADARHATDAHHAADAHHATDAHHAADAHHAADAHHATDAHHAADAHHATDAHHAADAHHAADAHHATDAHHAHHAADAHHAAAHHATDAHHATDAHHAAAHHEAATHCLRH TT3QW1X TT Literature-reported TTVF721 ID TTVF721 TTVF721 TN Plasmodium Serine repeat antigen 4 (Malaria PvSERA4) TTVF721 UP Q0PCM2 TTVF721 UC Q0PCM2_PLAVI TTVF721 SN Serine repeat antigen 4 TTVF721 GN Malaria PvSERA4 TTVF721 FC Constitutes major substrates of SUB1, may lead to the identification of parasite and/or host cell substrates and the underlying molecular mechanisms of proteolysis. TTVF721 SQ FNLDMPLATHSINKDPEISDYYLKNSSDYYENLYYKKFQGSGATGGAGKQWVQGASTVYGQEGDPKVADEAGGEAAQSITTHSRAEPAGDAPPSGPLHAGTDSEQGEGTGPTDGEGPTRVVDEKAQAGGPLTSPGTLQDAVAPGGPQGPPEQGSPGPQLPPVQPTAPVPPVLPVPPAAPLPDAPTNSTVPTTESDVKEVLH TTVF721 TT Literature-reported TT1KS9D ID TT1KS9D TT1KS9D TN Pleckstrin homology-like domain B 3 (PHLDB3) TT1KS9D UP Q6NSJ2 TT1KS9D UC PHLB3_HUMAN TT1KS9D SN Pleckstrin homology-like domain family B member 3 TT1KS9D GN PHLDB3 TT1KS9D FC Binds to MDM2 and facilitates MDM2-mediated ubiquitination and degradation of p53. Promotes cell growth and inhibits apoptosis. Plays an oncogenic role by in part inhibiting p53 activity in a feedback fashion. TT1KS9D SQ MGTRSSPEEGTPPPLVPECDVEVQPQGHPEESREQEASEVLAEPSSRGGAEQQAEEEEVGEGSSTESSRDAPEATPPIAMAATPPASTSSREGVRGAARRLQGQQLEALTRVALMEQRVKELQRQRKELRIEMEVEVALLRGELAGERVAARREEEQLRELLEQQAASEQRGRQQREQEQRRLSQERDRLEGLRQRLRKAQGQLDSQPEDQRERLLQGVQEMREQLDVAQRAYEDLEFQQLERESRQEEEDRDSPGPQVPDPKVQELQASMAQHRRGALQHRIRVLEEQLKSLGEQMAAESRGLSRKKEEALQALSQERSRLLELNCLQGTPGGDFSEPNPALTKLLFTQKTDRQLLVLQDAVAHSAATPTSSCLFSVHSSLQGSIGLQRTGSLPRKRGERGSQRGSPRPLSFHCTESLEASALPPAVGDSGRYPLYQLLNCGRGNSCGAIHPDIAHMERLLQQAMAERERLLKAREGTRRGTEGSSGPAVPAITAPPTPPHPPGPRILDLRQHLEGWGHNPENCPHVQVSGCCCRGPLVKMGGRIKTWRKRWFCFDRQARRLAYYADKEETKLKGVIYFQAIEEVYYDHLRCAFKSPNPRLTFCVKTYERLFYMVAPSPEAMRIWMDVIVTAADENHAP TT1KS9D TT Literature-reported TTR16E3 ID TTR16E3 TTR16E3 TN Postmeiotic segregation increased 2-like protein (PMS2L) TTR16E3 UP A4D2B8; O95744; Q13401 TTR16E3 UC PM2P1_HUMAN; PM2P2_HUMAN; PM2P3_HUMAN TTR16E3 SN Putative postmeiotic segregation increased 2-like protein; Putative postmeiotic segregation increased 2 pseudogene; Postmeiotic segregation increased protein; PMS2L; PMS2-related protein; PMS TTR16E3 GN PMS2P1; PMS2P2; PMS2P3 TTR16E3 FC Expressed ubiquitously except in the heart. Analysis of the proteins interacting with PMS2Ls may lead to the elucidation of the function of PMS2Ls or of the downstream pathway in the MMR system. TTR16E3 SQ MVTMCGGHRPENFLHQVLTEFGEELAGEGKSEVGGGAPRSYLQVASAECWAAAPAVHVGEPVHAGGLHTERGADPVIGLYLVHRGGACQTPTVGNRQTPTLGIHARPRRRATTSLLTLLLAFGKNAVRCALIGPGSLTSRTRPLTEPLGEKERREVFFPPRPERVEHNVESSRWEPRRRGACGSRGGNFPSPRGGSGVASLERAESSSTEPAKAIKPIDRKSVHQICSGPVVPSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEENFEGLTLKHHTSKIQEFADLPQVETFGFRGEALSSLCALSDVTISTCHVSAKVGTRLVFDHYGKIIQKTPYPHPRGMTVSVKQLFSTLPVHHKEFQRNIKKKRACFPFAFCRDCQFPEASPAMLPVQPAELTPRSTPPHPCSLEDNVITVFSSVKNGPGSSR TTR16E3 TT Literature-reported TTM67AX ID TTM67AX TTM67AX TN Prokineticin receptor 2 (PKR2) TTM67AX UP Q8NFJ6 TTM67AX UC PKR2_HUMAN TTM67AX SN PKR2; PK-R2; GPRg2; GPR73b; GPR73L1; G-protein coupled receptor I5E; G-protein coupled receptor 73-like 1 TTM67AX GN PROKR2 TTM67AX FC Receptor for prokineticin 2. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase. TTM67AX SQ MAAQNGNTSFTPNFNPPQDHASSLSFNFSYGDYDLPMDEDEDMTKTRTFFAAKIVIGIALAGIMLVCGIGNFVFIAALTRYKKLRNLTNLLIANLAISDFLVAIICCPFEMDYYVVRQLSWEHGHVLCASVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLKPRMNYQTASFLIALVWMVSILIAIPSAYFATETVLFIVKSQEKIFCGQIWPVDQQLYYKSYFLFIFGVEFVGPVVTMTLCYARISRELWFKAVPGFQTEQIRKRLRCRRKTVLVLMCILTAYVLCWAPFYGFTIVRDFFPTVFVKEKHYLTAFYVVECIAMSNSMINTVCFVTVKNNTMKYFKKMMLLHWRPSQRGSKSSADLDLRTNGVPTTEEVDCIRLK TTM67AX TT Literature-reported TT2X79I ID TT2X79I TT2X79I TN Prostate cancer-associated protein 5 (NGEP) TT2X79I UP Q6IWH7 TT2X79I UC ANO7_HUMAN TT2X79I SN Transmembrane protein 16G; TMEM16G; PCANAP5; New gene expressed in prostate; NGEP; IPCA-5; Dresden transmembrane protein of the prostate; D-TMPP; Anoctamin-7 TT2X79I GN ANO7 TT2X79I FC Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Does not exhibit calcium-activated chloride channel (CaCC) activity. May play a role in cell-cell interactions. TT2X79I SQ MRMAATAWAGLQGPPLPTLCPAVRTGLYCRDQAHAERWAMTSETSSGSHCARSRMLRRRAQEEDSTVLIDVSPPEAEKRGSYGSTAHASEPGGQQAAACRAGSPAKPRIADFVLVWEEDLKLDRQQDSAARDRTDMHRTWRETFLDNLRAAGLCVDQQDVQDGNTTVHYALLSASWAVLCYYAEDLRLKLPLQELPNQASNWSAGLLAWLGIPNVLLEVVPDVPPEYYSCRFRVNKLPRFLGSDNQDTFFTSTKRHQILFEILAKTPYGHEKKNLLGIHQLLAEGVLSAAFPLHDGPFKTPPEGPQAPRLNQRQVLFQHWARWGKWNKYQPLDHVRRYFGEKVALYFAWLGFYTGWLLPAAVVGTLVFLVGCFLVFSDIPTQELCGSKDSFEMCPLCLDCPFWLLSSACALAQAGRLFDHGGTVFFSLFMALWAVLLLEYWKRKSATLAYRWDCSDYEDTEERPRPQFAASAPMTAPNPITGEDEPYFPERSRARRMLAGSVVIVVMVAVVVMCLVSIILYRAIMAIVVSRSGNTLLAAWASRIASLTGSVVNLVFILILSKIYVSLAHVLTRWEMHRTQTKFEDAFTLKVFIFQFVNFYSSPVYIAFFKGRFVGYPGNYHTLFGVRNEECAAGGCLIELAQELLVIMVGKQVINNMQEVLIPKLKGWWQKFRLRSKKRKAGASAGASQGPWEDDYELVPCEGLFDEYLEMVLQFGFVTIFVAACPLAPLFALLNNWVEIRLDARKFVCEYRRPVAERAQDIGIWFHILAGLTHLAVISNAFLLAFSSDFLPRAYYRWTRAHDLRGFLNFTLARAPSSFAAAHNRTCRYRAFRDDDGHYSQTYWNLLAIRLAFVIVFEHVVFSVGRLLDLLVPDIPESVEIKVKREYYLAKQALAENEVLFGTNGTKDEQPEGSELSSHWTPFTVPKASQLQQ TT2X79I TT Literature-reported TTNWOIT ID TTNWOIT TTNWOIT TN Prostate-associated gene 5 protein (PAGE5) TTNWOIT UP Q96GU1 TTNWOIT UC PAGE5_HUMAN TTNWOIT SN PAGE-5; P antigen family member 5; GAGEE1; G antigen family E member 1; Cancer/testis antigen 16.1; CT16.1 TTNWOIT GN PAGE5 TTNWOIT FC A member of family of proteins that are expressed in a variety of tumors and in some fetal and reproductive tissues. The encoded protein may protect cells from programmed cell death. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found. TTNWOIT SQ MQAPWAGNRGWAGTREEVRDMSEHVTRSQSSERGNDQESSQPVGPVIVQQPTEEKRQEEEPPTDNQGIAPSGEIKNEGAPAVQGTDVEAFQQELALLKIEDAPGDGPDVREGTLPTFDPTKVLEAGEGQL TTNWOIT TT Literature-reported TT948FC ID TT948FC TT948FC TN Protein unc-13 homolog B (UNC13B) TT948FC UP O14795 TT948FC UC UN13B_HUMAN TT948FC SN UNC13B; Munc13-2; Munc13-1 TT948FC GN UNC13B TT948FC FC Plays a role in vesicle maturation during exocytosis as a target of thediacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity- depending refilling ofreadily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in a subset of excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. TT948FC SQ MSLLCVRVKRAKFQGSPDKFNTYVTLKVQNVKSTTVAVRGDQPSWEQDFMFEISRLDLGLSVEVWNKGLIWDTMVGTVWIALKTIRQSDEEGPGEWSTLEAETLMKDDEICGTRNPTPHKILLDTRFELPFDIPEEEARYWTYKWEQINALGADNEYSSQEESQRKPLPTAAAQCSFEDPDSAVDDRDSDYRSETSNSFPPPYHTASQPNASVHQFPVPVRSPQQLLLQGSSRDSCNDSMQSYDLDYPERRAISPTSSSRYGSSCNVSQGSSQLSELDQYHEQDDDHRETDSIHSCHSSHSLSRDGQAGFGEQEKPLEVTGQAEKEAACEPKEMKEDATTHPPPDLVLQKDHFLGPQESFPEENASSPFTQARAHWIRAVTKVRLQLQEIPDDGDPSLPQWLPEGPAGGLYGIDSMPDLRRKKPLPLVSDLSLVQSRKAGITSAMATRTSLKDEELKSHVYKKTLQALIYPISCTTPHNFEVWTATTPTYCYECEGLLWGIARQGMRCSECGVKCHEKCQDLLNADCLQRAAEKSCKHGAEDRTQNIIMAMKDRMKIRERNKPEIFEVIRDVFTVNKAAHVQQMKTVKQSVLDGTSKWSAKITITVVCAQGLQAKDKTGSSDPYVTVQVSKTKKRTKTIFGNLNPVWEEKFHFECHNSSDRIKVRVWDEDDDIKSRVKQRLKRESDDFLGQTIIEVRTLSGEMDVWYNLEKRTDKSAVSGAIRLQISVEIKGEEKVAPYHVQYTCLHENLFHYLTDIQGSGGVRIPEARGDDAWKVYFDETAQEIVDEFAMRYGIESIYQAMTHFACLSSKYMCPGVPAVMSTLLANINAYYAHTTASTNVSASDRFAASNFGKERFVKLLDQLHNSLRIDLSTYRNNFPAGSPERLQDLKSTVDLLTSITFFRMKVQELQSPPRASQVVKDCVKACLNSTYEYIFNNCHDLYSRQYQLKQELPPEEQGPSIRNLDFWPKLITLIVSIIEEDKNSYTPVLNQFPQELNVGKVSAEVMWHLFAQDMKYALEEHEKDHLCKSADYMNLHFKVKWLHNEYVRDLPVLQGQVPEYPAWFEQFVLQWLDENEDVSLEFLRGALERDKKDGFQQTSEHALFSCSVVDVFTQLNQSFEIIRKLECPDPSILAHYMRRFAKTIGKVLMQYADILSKDFPAYCTKEKLPCILMNNVQQLRVQLEKMFEAMGGKELDLEAADSLKELQVKLNTVLDELSMVFGNSFQVRIDECVRQMADILGQVRGTGNASPDARASAAQDADSVLRPLMDFLDGNLTLFATVCEKTVLKRVLKELWRVVMNTMERMIVLPPLTDQTGTQLIFTAAKELSHLSKLKDHMVREETRNLTPKQCAVLDLALDTIKQYFHAGGNGLKKTFLEKSPDLQSLRYALSLYTQTTDTLIKTFVRSQTTQGSGVDDPVGEVSIQVDLFTHPGTGEHKVTVKVVAANDLKWQTAGMFRPFVEVTMVGPHQSDKKRKFTTKSKSNNWAPKYNETFHFLLGNEEGPESYELQICVKDYCFAREDRVLGLAVMPLRDVTAKGSCACWCPLGRKIHMDETGLTILRILSQRSNDEVAREFVKLKSESRSTEEGS TT948FC TT Literature-reported TTSKF4V ID TTSKF4V TTSKF4V TN Proteoglycan 4 (PRG4) TTSKF4V UP Q92954 TTSKF4V UC PRG4_HUMAN TTSKF4V SN Superficial zone proteoglycan; Proteoglycan 4 C-terminal part; PRG4; Megakaryocyte-stimulating factor; Lubricin TTSKF4V GN PRG4 TTSKF4V FC Isoform F plays a role as a growth factor acting on the primitive cells of both hematopoietic and endothelial cell lineages. TTSKF4V SQ MAWKTLPIYLLLLLSVFVIQQVSSQDLSSCAGRCGEGYSRDATCNCDYNCQHYMECCPDFKRVCTAELSCKGRCFESFERGRECDCDAQCKKYDKCCPDYESFCAEVHNPTSPPSSKKAPPPSGASQTIKSTTKRSPKPPNKKKTKKVIESEEITEEHSVSENQESSSSSSSSSSSSTIRKIKSSKNSAANRELQKKLKVKDNKKNRTKKKPTPKPPVVDEAGSGLDNGDFKVTTPDTSTTQHNKVSTSPKITTAKPINPRPSLPPNSDTSKETSLTVNKETTVETKETTTTNKQTSTDGKEKTTSAKETQSIEKTSAKDLAPTSKVLAKPTPKAETTTKGPALTTPKEPTPTTPKEPASTTPKEPTPTTIKSAPTTPKEPAPTTTKSAPTTPKEPAPTTTKEPAPTTPKEPAPTTTKEPAPTTTKSAPTTPKEPAPTTPKKPAPTTPKEPAPTTPKEPTPTTPKEPAPTTKEPAPTTPKEPAPTAPKKPAPTTPKEPAPTTPKEPAPTTTKEPSPTTPKEPAPTTTKSAPTTTKEPAPTTTKSAPTTPKEPSPTTTKEPAPTTPKEPAPTTPKKPAPTTPKEPAPTTPKEPAPTTTKKPAPTTPKEPAPTTPKETAPTTPKKLTPTTPEKLAPTTPEKPAPTTPEELAPTTPEEPTPTTPEEPAPTTPKAAAPNTPKEPAPTTPKEPAPTTPKEPAPTTPKETAPTTPKGTAPTTLKEPAPTTPKKPAPKELAPTTTKEPTSTTSDKPAPTTPKGTAPTTPKEPAPTTPKEPAPTTPKGTAPTTLKEPAPTTPKKPAPKELAPTTTKGPTSTTSDKPAPTTPKETAPTTPKEPAPTTPKKPAPTTPETPPPTTSEVSTPTTTKEPTTIHKSPDESTPELSAEPTPKALENSPKEPGVPTTKTPAATKPEMTTTAKDKTTERDLRTTPETTTAAPKMTKETATTTEKTTESKITATTTQVTSTTTQDTTPFKITTLKTTTLAPKVTTTKKTITTTEIMNKPEETAKPKDRATNSKATTPKPQKPTKAPKKPTSTKKPKTMPRVRKPKTTPTPRKMTSTMPELNPTSRIAEAMLQTTTRPNQTPNSKLVEVNPKSEDAGGAEGETPHMLLRPHVFMPEVTPDMDYLPRVPNQGIIINPMLSDETNICNGKPVDGLTTLRNGTLVAFRGHYFWMLSPFSPPSPARRITEVWGIPSPIDTVFTRCNCEGKTFFFKDSQYWRFTNDIKDAGYPKPIFKGFGGLTGQIVAALSTAKYKNWPESVYFFKRGGSIQQYIYKQEPVQKCPGRRPALNYPVYGETTQVRRRRFERAIGPSQTHTIRIQYSPARLAYQDKGVLHNEVKVSILWRGLPNVVTSAISLPNIRKPDGYDYYAFSKDQYYNIDVPSRTARAITTRSGQTLSKVWYNCP TTSKF4V TT Literature-reported TTGUJYV ID TTGUJYV TTGUJYV TN Protocadherin Fat 1 (FAT1) TTGUJYV UP Q14517 TTGUJYV UC FAT1_HUMAN TTGUJYV SN Protocadherin Fat 1, nuclear form; Protein fat homolog; Cadherin-related tumor suppressor homolog; Cadherin family member 7; CDHF7 TTGUJYV GN FAT1 TTGUJYV FC Plays an essential role for cellular polarization, directed cell migration and modulating cell-cell contact. TTGUJYV SQ MGRHLALLLLLLLLFQHFGDSDGSQRLEQTPLQFTHLEYNVTVQENSAAKTYVGHPVKMGVYITHPAWEVRYKIVSGDSENLFKAEEYILGDFCFLRIRTKGGNTAILNREVKDHYTLIVKALEKNTNVEARTKVRVQVLDTNDLRPLFSPTSYSVSLPENTAIRTSIARVSATDADIGTNGEFYYSFKDRTDMFAIHPTSGVIVLTGRLDYLETKLYEMEILAADRGMKLYGSSGISSMAKLTVHIEQANECAPVITAVTLSPSELDRDPAYAIVTVDDCDQGANGDIASLSIVAGDLLQQFRTVRSFPGSKEYKVKAIGGIDWDSHPFGYNLTLQAKDKGTPPQFSSVKVIHVTSPQFKAGPVKFEKDVYRAEISEFAPPNTPVVMVKAIPAYSHLRYVFKSTPGKAKFSLNYNTGLISILEPVKRQQAAHFELEVTTSDRKASTKVLVKVLGANSNPPEFTQTAYKAAFDENVPIGTTVMSLSAVDPDEGENGYVTYSIANLNHVPFAIDHFTGAVSTSENLDYELMPRVYTLRIRASDWGLPYRREVEVLATITLNNLNDNTPLFEKINCEGTIPRDLGVGEQITTVSAIDADELQLVQYQIEAGNELDFFSLNPNSGVLSLKRSLMDGLGAKVSFHSLRITATDGENFATPLYINITVAASHKLVNLQCEETGVAKMLAEKLLQANKLHNQGEVEDIFFDSHSVNAHIPQFRSTLPTGIQVKENQPVGSSVIFMNSTDLDTGFNGKLVYAVSGGNEDSCFMIDMETGMLKILSPLDRETTDKYTLNITVYDLGIPQKAAWRLLHVVVVDANDNPPEFLQESYFVEVSEDKEVHSEIIQVEATDKDLGPNGHVTYSIVTDTDTFSIDSVTGVVNIARPLDRELQHEHSLKIEARDQAREEPQLFSTVVVKVSLEDVNDNPPTFIPPNYRVKVREDLPEGTVIMWLEAHDPDLGQSGQVRYSLLDHGEGNFDVDKLSGAVRIVQQLDFEKKQVYNLTVRAKDKGKPVSLSSTCYVEVEVVDVNENLHPPVFSSFVEKGTVKEDAPVGSLVMTVSAHDEDARRDGEIRYSIRDGSGVGVFKIGEETGVIETSDRLDRESTSHYWLTVFATDQGVVPLSSFIEIYIEVEDVNDNAPQTSEPVYYPEIMENSPKDVSVVQIEAFDPDSSSNDKLMYKITSGNPQGFFSIHPKTGLITTTSRKLDREQQDEHILEVTVTDNGSPPKSTIARVIVKILDENDNKPQFLQKFYKIRLPEREKPDRERNARREPLYHVIATDKDEGPNAEISYSIEDGNEHGKFFIEPKTGVVSSKRFSAAGEYDILSIKAVDNGRPQKSSTTRLHIEWISKPKPSLEPISFEESFFTFTVMESDPVAHMIGVISVEPPGIPLWFDITGGNYDSHFDVDKGTGTIIVAKPLDAEQKSNYNLTVEATDGTTTILTQVFIKVIDTNDHRPQFSTSKYEVVIPEDTAPETEILQISAVDQDEKNKLIYTLQSSRDPLSLKKFRLDPATGSLYTSEKLDHEAVHQHTLTVMVRDQDVPVKRNFARIVVNVSDTNDHAPWFTASSYKGRVYESAAVGSVVLQVTALDKDKGKNAEVLYSIESGNIGNSFMIDPVLGSIKTAKELDRSNQAEYDLMVKATDKGSPPMSEITSVRIFVTIADNASPKFTSKEYSVELSETVSIGSFVGMVTAHSQSSVVYEIKDGNTGDAFDINPHSGTIITQKALDFETLPIYTLIIQGTNMAGLSTNTTVLVHLQDENDNAPVFMQAEYTGLISESASINSVVLTDRNVPLVIRAADADKDSNALLVYHIVEPSVHTYFAIDSSTGAIHTVLSLDYEETSIFHFTVQVHDMGTPRLFAEYAANVTVHVIDINDCPPVFAKPLYEASLLLPTYKGVKVITVNATDADSSAFSQLIYSITEGNIGEKFSMDYKTGALTVQNTTQLRSRYELTVRASDGRFAGLTSVKINVKESKESHLKFTQDVYSAVVKENSTEAETLAVITAIGNPINEPLFYHILNPDRRFKISRTSGVLSTTGTPFDREQQEAFDVVVEVTEEHKPSAVAHVVVKVIVEDQNDNAPVFVNLPYYAVVKVDTEVGHVIRYVTAVDRDSGRNGEVHYYLKEHHEHFQIGPLGEISLKKQFELDTLNKEYLVTVVAKDGGNPAFSAEVIVPITVMNKAMPVFEKPFYSAEIAESIQVHSPVVHVQANSPEGLKVFYSITDGDPFSQFTINFNTGVINVIAPLDFEAHPAYKLSIRATDSLTGAHAEVFVDIIVDDINDNPPVFAQQSYAVTLSEASVIGTSVVQVRATDSDSEPNRGISYQMFGNHSKSHDHFHVDSSTGLISLLRTLDYEQSRQHTIFVRAVDGGMPTLSSDVIVTVDVTDLNDNPPLFEQQIYEARISEHAPHGHFVTCVKAYDADSSDIDKLQYSILSGNDHKHFVIDSATGIITLSNLHRHALKPFYSLNLSVSDGVFRSSTQVHVTVIGGNLHSPAFLQNEYEVELAENAPLHTLVMEVKTTDGDSGIYGHVTYHIVNDFAKDRFYINERGQIFTLEKLDRETPAEKVISVRLMAKDAGGKVAFCTVNVILTDDNDNAPQFRATKYEVNIGSSAAKGTSVVKVLASDADEGSNADITYAIEADSESVKENLEINKLSGVITTKESLIGLENEFFTFFVRAVDNGSPSKESVVLVYVKILPPEMQLPKFSEPFYTFTVSEDVPIGTEIDLIRAEHSGTVLYSLVKGNTPESNRDESFVIDRQSGRLKLEKSLDHETTKWYQFSILARCTQDDHEMVASVDVSIQVKDANDNSPVFESSPYEAFIVENLPGGSRVIQIRASDADSGTNGQVMYSLDQSQSVEVIESFAINMETGWITTLKELDHEKRDNYQIKVVASDHGEKIQLSSTAIVDVTVTDVNDSPPRFTAEIYKGTVSEDDPQGGVIAILSTTDADSEEINRQVTYFITGGDPLGQFAVETIQNEWKVYVKKPLDREKRDNYLLTITATDGTFSSKAIVEVKVLDANDNSPVCEKTLYSDTIPEDVLPGKLIMQISATDADIRSNAEITYTLLGSGAEKFKLNPDTGELKTSTPLDREEQAVYHLLVRATDGGGRFCQASIVLTLEDVNDNAPEFSADPYAITVFENTEPGTLLTRVQATDADAGLNRKILYSLIDSADGQFSINELSGIIQLEKPLDRELQAVYTLSLKAVDQGLPRRLTATGTVIVSVLDINDNPPVFEYREYGATVSEDILVGTEVLQVYAASRDIEANAEITYSIISGNEHGKFSIDSKTGAVFIIENLDYESSHEYYLTVEATDGGTPSLSDVATVNVNVTDINDNTPVFSQDTYTTVISEDAVLEQSVITVMADDADGPSNSHIHYSIIDGNQGSSFTIDPVRGEVKVTKLLDRETISGYTLTVQASDNGSPPRVNTTTVNIDVSDVNDNAPVFSRGNYSVIIQENKPVGFSVLQLVVTDEDSSHNGPPFFFTIVTGNDEKAFEVNPQGVLLTSSAIKRKEKDHYLLQVKVADNGKPQLSSLTYIDIRVIEESIYPPAILPLEIFITSSGEEYSGGVIGKIHATDQDVYDTLTYSLDPQMDNLFSVSSTGGKLIAHKKLDIGQYLLNVSVTDGKFTTVADITVHIRQVTQEMLNHTIAIRFANLTPEEFVGDYWRNFQRALRNILGVRRNDIQIVSLQSSEPHPHLDVLLFVEKPGSAQISTKQLLHKINSSVTDIEEIIGVRILNVFQKLCAGLDCPWKFCDEKVSVDESVMSTHSTARLSFVTPRHHRAAVCLCKEGRCPPVHHGCEDDPCPEGSECVSDPWEEKHTCVCPSGRFGQCPGSSSMTLTGNSYVKYRLTENENKLEMKLTMRLRTYSTHAVVMYARGTDYSILEIHHGRLQYKFDCGSGPGIVSVQSIQVNDGQWHAVALEVNGNYARLVLDQVHTASGTAPGTLKTLNLDNYVFFGGHIRQQGTRHGRSPQVGNGFRGCMDSIYLNGQELPLNSKPRSYAHIEESVDVSPGCFLTATEDCASNPCQNGGVCNPSPAGGYYCKCSALYIGTHCEISVNPCSSKPCLYGGTCVVDNGGFVCQCRGLYTGQRCQLSPYCKDEPCKNGGTCFDSLDGAVCQCDSGFRGERCQSDIDECSGNPCLHGALCENTHGSYHCNCSHEYRGRHCEDAAPNQYVSTPWNIGLAEGIGIVVFVAGIFLLVVVFVLCRKMISRKKKHQAEPKDKHLGPATAFLQRPYFDSKLNKNIYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESVHGHRKAVAVCSVAPNLPPPPPSNSPSDSDSIQKPSWDFDYDTKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNGYHWDTSDWMPSVPLPDIQEFPNYEVIDEQTPLYSADPNAIDTDYYPGGYDIESDFPPPPEDFPAADELPPLPPEFSNQFESIHPPRDMPAAGSLGSSSRNRQRFNLNQYLPNFYPLDMSEPQTKGTGENSTCREPHAPYPPGYQRHFEAPAVESMPMSVYASTASCSDVSACCEVESEVMMSDYESGDDGHFEEVTIPPLDSQQHTEV TTGUJYV TT Literature-reported TT1ZCTH ID TT1ZCTH TT1ZCTH TN Proto-oncogene c-Rel (REL) TT1ZCTH UP Q04864 TT1ZCTH UC REL_HUMAN TT1ZCTH SN C-Rel TT1ZCTH GN REL TT1ZCTH FC NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator. Proto-oncogene that may play a role in differentiation and lymphopoiesis. TT1ZCTH SQ MASGAYNPYIEIIEQPRQRGMRFRYKCEGRSAGSIPGEHSTDNNRTYPSIQIMNYYGKGKVRITLVTKNDPYKPHPHDLVGKDCRDGYYEAEFGQERRPLFFQNLGIRCVKKKEVKEAIITRIKAGINPFNVPEKQLNDIEDCDLNVVRLCFQVFLPDEHGNLTTALPPVVSNPIYDNRAPNTAELRICRVNKNCGSVRGGDEIFLLCDKVQKDDIEVRFVLNDWEAKGIFSQADVHRQVAIVFKTPPYCKAITEPVTVKMQLRRPSDQEVSESMDFRYLPDEKDTYGNKAKKQKTTLLFQKLCQDHVETGFRHVDQDGLELLTSGDPPTLASQSAGITVNFPERPRPGLLGSIGEGRYFKKEPNLFSHDAVVREMPTGVSSQAESYYPSPGPISSGLSHHASMAPLPSSSWSSVAHPTPRSGNTNPLSSFSTRTLPSNSQGIPPFLRIPVGNDLNASNACIYNNADDIVGMEASSMPSADLYGISDPNMLSNCSVNMMTTSSDSMGETDNPRLLSMNLENPSCNSVLDPRDLRQLHQMSSSSMSAGANSNTTVFVSQSDAFEGSDFSCADNSMINESGPSNSTNPNSHGFVQDSQYSGIGSMQNEQLSDSFPYEFFQV TT1ZCTH TT Literature-reported TTMADVT ID TTMADVT TTMADVT TN PSD95-nNOS interaction (PSD95-nNOS PPI) TTMADVT UP P78352-P29475 TTMADVT UC DLG4_HUMAN-NOS1_HUMAN TTMADVT SN Disks large homolog 4-Constitutive NOS interaction TTMADVT GN DLG4-NOS1 TTMADVT FC Functions as a novel molecular target to modulate conditioned fear: relevance to PTSD. TTMADVT SQ MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTIRVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAPRPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQVDRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPSKCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCEIFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQEERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGVISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREPDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSSMDCLCIVTTKKYRYQDEDTPPLEHSPAHLPNQANSPPVIVNTDTLEAPGYELQVNGTEGEMEYEEITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFVNEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKVMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVYLKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAKDLLGEEDIPREPRRIVIHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDQILSVNGVDLRNASHEQAAIALKNAGQTVTIIAQYKPEEYSRFEAKIHDLREQLMNSSLGSGTASLRSNPKRGFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDASDEEWWQARRVHSDSETDDIGFIPSKRRVERREWSRLKAKDWGSSSGSQGREDSVLSYETVTQMEVHYARPIIILGPTKDRANDDLLSEFPDKFGSCVPHTTRPKREYEIDGRDYHFVSSREKMEKDIQAHKFIEAGQYNSHLYGTSVQSVREVAEQGKHCILDVSANAVRRLQAAHLHPIAIFIRPRSLENVLEINKRITEEQARKAFDRATKLEQEFTECFSAIVEGDSFEEIYHKVKRVIEDLSGPYIWVPARERL TTMADVT TT Literature-reported TTMU9JB ID TTMU9JB TTMU9JB TN Pseudomonas Protein KerV (Pseudo KerV) TTMU9JB UP A0A1C7BG45 TTMU9JB UC A0A1C7BG45_PSEAI TTMU9JB SN KerV protein TTMU9JB GN Pseudo KerV TTMU9JB FC A methyltransferase, well-conserved across numerous Proteobacteria, including both well-known and emerging pathogens. TTMU9JB SQ MNEPQAFAQTDAEWLASINRARDWFQGPLGSLMLAEERRLLCDELTRYFGGYLVHYGPHAELPPSTGQIQRGVRLGPPLPGVDIACEEGAWPLSEHAADVVLLQHGLDFCLSPHRLLREAARTVRPGGHLLLIGINPWSLWGIRHYFAGDALRQARCIPPSRACDWLNLLGFALEKRRFGCYRPPLASAAWQSRLARLERWGDAWQSSGAGFYLLVARKLVVGLRPLRQSKREPRGQLVPMPVAKVSRRDSEI TTMU9JB TT Literature-reported TTYGK57 ID TTYGK57 TTYGK57 TN Rab-like protein 3 (RABL3) TTYGK57 UP Q5HYI8 TTYGK57 UC RABL3_HUMAN TTYGK57 SN Rab-like protein 3 TTYGK57 GN RABL3 TTYGK57 FC GTPase activity, intracellular protein transport, Rab protein signal transduction TTYGK57 SQ MASLDRVKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRVHDYKEGTPEEKTYYIELWDVGGSVGSASSVKSTRAVFYNSVNGIIFVHDLTNKKSSQNLRRWSLEALNRDLVPTGVLVTNGDYDQEQFADNQIPLLVIGTKLDQIHETKRHEVLTRTAFLAEDFNPEEINLDCTNPRYLAAGSSNAVKLSRFFDKVIEKRYFLREGNQIPGFPDRKRFGAGTLKSLHYD TTYGK57 TT Literature-reported TT9L4J8 ID TT9L4J8 TT9L4J8 TN Rabphilin-3A (RPH3A) TT9L4J8 UP Q9Y2J0 TT9L4J8 UC RP3A_HUMAN TT9L4J8 SN KIAA0985; Exophilin-1 TT9L4J8 GN RPH3A TT9L4J8 FC Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. TT9L4J8 SQ MTDTVFSNSSNRWMYPSDRPLQSNDKEQLQAGWSVHPGGQPDRQRKQEELTDEEKEIINRVIARAEKMEEMEQERIGRLVDRLENMRKNVAGDGVNRCILCGEQLGMLGSACVVCEDCKKNVCTKCGVETNNRLHSVWLCKICIEQREVWKRSGAWFFKGFPKQVLPQPMPIKKTKPQQPVSEPAAPEQPAPEPKHPARAPARGDSEDRRGPGQKTGPDPASAPGRGNYGPPVRRASEARMSSSSRDSESWDHSGGAGDSSRSPAGLRRANSVQASRPAPGSVQSPAPPQPGQPGTPGGSRPGPGPAGRFPDQKPEVAPSDPGTTAPPREERTGGVGGYPAVGAREDRMSHPSGPYSQASAAAPQPAAARQPPPPEEEEEEANSYDSDEATTLGALEFSLLYDQDNSSLQCTIIKAKGLKPMDSNGLADPYVKLHLLPGASKSNKLRTKTLRNTRNPIWNETLVYHGITDEDMQRKTLRISVCDEDKFGHNEFIGETRFSLKKLKPNQRKNFNICLERVIPMKRAGTTGSARGMALYEEEQVERVGDIEERGKILVSLMYSTQQGGLIVGIIRCVHLAAMDANGYSDPFVKLWLKPDMGKKAKHKTQIKKKTLNPEFNEEFFYDIKHSDLAKKSLDISVWDYDIGKSNDYIGGCQLGISAKGERLKHWYECLKNKDKKIERWHQLQNENHVSSD TT9L4J8 TT Literature-reported TTOS63B ID TTOS63B TTOS63B TN Rap guanine nucleotide exchange factor 4 (EPAC2) TTOS63B UP Q8WZA2 TTOS63B UC RPGF4_HUMAN TTOS63B SN cAMP-regulated guanine nucleotide exchange factor II; cAMP-GEFII; Exchange protein directly activated by cAMP 2; Exchange factor directly activated by cAMP 2; EPAC2; EPAC 2; CGEF2 TTOS63B GN RAPGEF4 TTOS63B FC Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA-independent exocytosis through interaction with RIMS2 (By similarity). TTOS63B SQ MVAAHAAHSSSSAEWIACLDKRPLERSSEDVDIIFTRLKEVKAFEKFHPNLLHQICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSLDVKVSETSSHQDAVTICTLGIGTAFGESILDNTPRHATIVTRESSELLRIEQKDFKALWEKYRQYMAGLLAPPYGVMETGSNNDRIPDKENTPLIEPHVPLRPANTITKVPSEKILRAGKILRNAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMMQQTPCVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLFYRFLDDEHEDAPLPTEEEKKECDEELQDTMLLLSQMGPDAHMRMILRKPPGQRTVDDLEIIYEELLHIKALSHLSTTVKRELAGVLIFESHAKGGTVLFNQGEEGTSWYIILKGSVNVVIYGKGVVCTLHEGDDFGKLALVNDAPRAASIVLREDNCHFLRVDKEDFNRILRDVEANTVRLKEHDQDVLVLEKVPAGNRASNQGNSQPQQKYTVMSGTPEKILEHFLETIRLEATLNEATDSVLNDFIMMHCVFMPNTQLCPALVAHYHAQPSQGTEQEKMDYALNNKRRVIRLVLQWAAMYGDLLQEDDVSMAFLEEFYVSVSDDARMIAALKEQLPELEKIVKQISEDAKAPQKKHKVLLQQFNTGDERAQKRQPIRGSDEVLFKVYCMDHTYTTIRVPVATSVKEVISAVADKLGSGEGLIIVKMSSGGEKVVLKPNDVSVFTTLTINGRLFACPREQFDSLTPLPEQEGPTVGTVGTFELMSSKDLAYQMTIYDWELFNCVHELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKKFIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTVAKLEPPLIPFMPLLIKDMTFTHEGNKTFIDNLVNFEKMRMIANTARTVRYYRSQPFNPDAAQANKNHQDVRSYVRQLNVIDNQRTLSQMSHRLEPRRP TTOS63B TT Literature-reported TTGB2LZ ID TTGB2LZ TTGB2LZ TN RAR-related orphan receptor-beta (RORB) TTGB2LZ UP Q92753 TTGB2LZ UC RORB_HUMAN TTGB2LZ SN Retinoid-related orphan receptor-beta; RZRB; Nuclear receptor subfamily 1 group F member 2; Nuclear receptor RZR-beta; Nuclear receptor ROR-beta; NR1F2 TTGB2LZ GN RORB TTGB2LZ FC Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity (By similarity). TTGB2LZ SQ MCENQLKTKADATAQIEVIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQNNASYSCPRQRNCLIDRTNRNRCQHCRLQKCLALGMSRDAVKFGRMSKKQRDSLYAEVQKHQQRLQEQRQQQSGEAEALARVYSSSISNGLSNLNNETSGTYANGHVIDLPKSEGYYNVDSGQPSPDQSGLDMTGIKQIKQEPIYDLTSVPNLFTYSSFNNGQLAPGITMTEIDRIAQNIIKSHLETCQYTMEELHQLAWQTHTYEEIKAYQSKSREALWQQCAIQITHAIQYVVEFAKRITGFMELCQNDQILLLKSGCLEVVLVRMCRAFNPLNNTVLFEGKYGGMQMFKALGSDDLVNEAFDFAKNLCSLQLTEEEIALFSSAVLISPDRAWLIEPRKVQKLQEKIYFALQHVIQKNHLDDETLAKLIAKIPTITAVCNLHGEKLQVFKQSHPEIVNTLFPPLYKELFNPDCATGCK TTGB2LZ TT Patented-recorded TTGTKX9 ID TTGTKX9 TTGTKX9 TN Regulator of G-protein signaling 4 (RGS4) TTGTKX9 UP P49798 TTGTKX9 UC RGS4_HUMAN TTGTKX9 SN RGP4 TTGTKX9 GN RGS4 TTGTKX9 FC Activity on G(z)-alpha is inhibited by phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)-alpha-1 is inhibited by palmitoylation of the G-protein. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. TTGTKX9 SQ MCKGLAGLPASCLRSAKDMKHRLGFLLQKSDSCEHNSSHNKKDKVVICQRVSQEEVKKWAESLENLISHECGLAAFKAFLKSEYSEENIDFWISCEEYKKIKSPSKLSPKAKKIYNEFISVQATKEVNLDSCTREETSRNMLEPTITCFDEAQKKIFNLMEKDSYRRFLKSRFYLDLVNPSSCGAEKQKGAKSSADCASLVPQCA TTGTKX9 TT Literature-reported TT64ZVP ID TT64ZVP TT64ZVP TN Relaxin-3 receptor 1 (RXFP3) TT64ZVP UP Q9NSD7 TT64ZVP UC RL3R1_HUMAN TT64ZVP SN Somatostatin- and angiotensin-like peptide receptor; SALPR; Relaxin family peptide receptor 3; RLN3R1; RLN3 receptor 1; G-protein coupled receptor GPCR135; G protein-coupled receptor SALPR TT64ZVP GN RXFP3 TT64ZVP FC Receptor for RNL3/relaxin-3. Binding of the ligand inhibit cAMP accumulation. TT64ZVP SQ MQMADAATIATMNKAAGGDKLAELFSLVPDLLEAANTSGNASLQLPDLWWELGLELPDGAPPGHPPGSGGAESADTEARVRILISVVYWVVCALGLAGNLLVLYLMKSMQGWRKSSINLFVTNLALTDFQFVLTLPFWAVENALDFKWPFGKAMCKIVSMVTSMNMYASVFFLTAMSVTRYHSVASALKSHRTRGHGRGDCCGRSLGDSCCFSAKALCVWIWALAALASLPSAIFSTTVKVMGEELCLVRFPDKLLGRDRQFWLGLYHSQKVLLGFVLPLGIIILCYLLLVRFIADRRAAGTKGGAAVAGGRPTGASARRLSKVTKSVTIVVLSFFLCWLPNQALTTWSILIKFNAVPFSQEYFLCQVYAFPVSVCLAHSNSCLNPVLYCLVRREFRKALKSLLWRIASPSITSMRPFTATTKPEHEDQGLQAPAPPHAAAEPDLLYYPPGVVVYSGGRYDLLPSSSAY TT64ZVP TT Literature-reported TTMP86V ID TTMP86V TTMP86V TN Remodeling and spacing factor 1 (RSF1) TTMP86V UP Q96T23 TTMP86V UC RSF1_HUMAN TTMP86V SN p325 subunit of RSF chromatin-remodeling complex; XAP8; Rsf-1; Hepatitis B virus X-associated protein; HBXAP; HBV pX-associated protein 8 TTMP86V GN RSF1 TTMP86V FC Required for assembly of regular nucleosome arrays by the RSF chromatin-remodeling complex (PubMed:12972596). Facilitates transcription of hepatitis B virus (HBV) genes by the pX transcription activator. In case of infection by HBV, together with pX, it represses TNF-alpha induced NF-kappa-B transcription activation. Represses transcription when artificially recruited to chromatin by fusion to a heterogeneous DNA binding domain (PubMed:11944984, PubMed:11788598). TTMP86V SQ MATAAAAAAVMAPPGCPGSCPNFAVVCSFLERYGPLLDLPELPFPELERVLQAPPPDVGNGEVPKELVELHLKLMRKIGKSVTADRWEKYLIKICQEFNSTWAWEMEKKGYLEMSVECKLALLKYLCECQFDDNLKFKNIINEEDADTMRLQPIGRDKDGLMYWYQLDQDHNVRMYIEEQDDQDGSSWKCIVRNRNELAETLALLKAQIDPVLLKNSSQQDNSSRESPSLEDEETKKEEETPKQEEQKESEKMKSEEQPMDLENRSTANVLEETTVKKEKEDEKELVKLPVIVKLEKPLPENEEKKIIKEESDSFKENVKPIKVEVKECRADPKDTKSSMEKPVAQEPERIEFGGNIKSSHEITEKSTEETEKLKNDQQAKIPLKKREIKLSDDFDSPVKGPLCKSVTPTKEFLKDEIKQEEETCKRISTITALGHEGKQLVNGEVSDERVAPNFKTEPIETKFYETKEESYSPSKDRNIITEGNGTESLNSVITSMKTGELEKETAPLRKDADSSISVLEIHSQKAQIEEPDPPEMETSLDSSEMAKDLSSKTALSSTESCTMKGEEKSPKTKKDKRPPILECLEKLEKSKKTFLDKDAQRLSPIPEEVPKSTLESEKPGSPEAAETSPPSNIIDHCEKLASEKEVVECQSTSTVGGQSVKKVDLETLKEDSEFTKVEMDNLDNAQTSGIEEPSETKGSMQKSKFKYKLVPEEETTASENTEITSERQKEGIKLTIRISSRKKKPDSPPKVLEPENKQEKTEKEEEKTNVGRTLRRSPRISRPTAKVAEIRDQKADKKRGEGEDEVEEESTALQKTDKKEILKKSEKDTNSKVSKVKPKGKVRWTGSRTRGRWKYSSNDESEGSGSEKSSAASEEEEEKESEEAILADDDEPCKKCGLPNHPELILLCDSCDSGYHTACLRPPLMIIPDGEWFCPPCQHKLLCEKLEEQLQDLDVALKKKERAERRKERLVYVGISIENIIPPQEPDFSEDQEEKKKDSKKSKANLLERRSTRTRKCISYRFDEFDEAIDEAIEDDIKEADGGGVGRGKDISTITGHRGKDISTILDEERKENKRPQRAAAARRKKRRRLNDLDSDSNLDEEESEDEFKISDGSQDEFVVSDENPDESEEDPPSNDDSDTDFCSRRLRRHPSRPMRQSRRLRRKTPKKKYSDDDEEEESEENSRDSESDFSDDFSDDFVETRRRRSRRNQKRQINYKEDSESDGSQKSLRRGKEIRRVHKRRLSSSESEESYLSKNSEDDELAKESKRSVRKRGRSTDEYSEADEEEEEEEGKPSRKRLHRIETDEEESCDNAHGDANQPARDSQPRVLPSEQESTKKPYRIESDEEEDFENVGKVGSPLDYSLVDLPSTNGQSPGKAIENLIGKPTEKSQTPKDNSTASASLASNGTSGGQEAGAPEEEEDELLRVTDLVDYVCNSEQL TTMP86V TT Literature-reported TTXZ7W0 ID TTXZ7W0 TTXZ7W0 TN Rheumatoid arthritis-related antigen RA-A47 (SERPINH1) TTXZ7W0 UP P50454 TTXZ7W0 UC SERPH_HUMAN TTXZ7W0 SN Serpin H1; SERPINH2; PIG14; HSP47; Colligin; Collagen-binding protein; Cell proliferation-inducing gene 14 protein; CBP2; CBP1; AsTP3; Arsenic-transactivated protein 3; 47 kDa heat shock protein TTXZ7W0 GN SERPINH1 TTXZ7W0 FC Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. TTXZ7W0 SQ MRSLLLLSAFCLLEAALAAEVKKPAAAAAPGTAEKLSPKAATLAERSAGLAFSLYQAMAKDQAVENILVSPVVVASSLGLVSLGGKATTASQAKAVLSAEQLRDEEVHAGLGELLRSLSNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVMMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMPHHVEPLERLEKLLTKEQLKIWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFELDTDGNPFDQDIYGREELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRPKGDKMRDEL TTXZ7W0 TT Literature-reported TT1R5DZ ID TT1R5DZ TT1R5DZ TN Rho guanine nucleotide exchange factor 3 (ARHGEF3) TT1R5DZ UP Q9NR81 TT1R5DZ UC ARHG3_HUMAN TT1R5DZ SN XPLN; Exchange factor found in platelets and leukemic and neuronal tissues TT1R5DZ GN ARHGEF3 TT1R5DZ FC Acts as guanine nucleotide exchange factor (GEF) for RhoA and RhoB GTPases. TT1R5DZ SQ MVAKDYPFYLTVKRANCSLELPPASGPAKDAEEPSNKRVKPLSRVTSLANLIPPVKATPLKRFSQTLQRSISFRSESRPDILAPRPWSRNAAPSSTKRRDSKLWSETFDVCVNQMLTSKEIKRQEAIFELSQGEEDLIEDLKLAKKAYHDPMLKLSIMTEQELNQIFGTLDSLIPLHEELLSQLRDVRKPDGSTEHVGPILVGWLPCLSSYDSYCSNQVAAKALLDHKKQDHRVQDFLQRCLESPFSRKLDLWNFLDIPRSRLVKYPLLLREILRHTPNDNPDQQHLEEAINIIQGIVAEINTKTGESECRYYKERLLYLEEGQKDSLIDSSRVLCCHGELKNNRGVKLHVFLFQEVLVITRAVTHNEQLCYQLYRQPIPVKDLLLEDLQDGEVRLGGSLRGAFSNNERIKNFFRVSFKNGSQSQTHSLQANDTFNKQQWLNCIRQAKETVLCAAGQAGVLDSEGSFLNPTTGSRELQGETKLEQMDQSDSESDCSMDTSEVSLDCERMEQTDSSCGNSRHGESNV TT1R5DZ TT Literature-reported TTXGM9Q ID TTXGM9Q TTXGM9Q TN Ribonuclease H2 (RNase H2) TTXGM9Q UP O75792; Q5TBB1; Q8TDP1 TTXGM9Q UC RNH2A_HUMAN; RNH2B_HUMAN; RNH2C_HUMAN TTXGM9Q SN Ribonuclease H; RNase H; Aicardi-Goutieres syndrome protein; AGS TTXGM9Q GN RNASEH2A; RNASEH2B; RNASEH2C TTXGM9Q FC Subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. TTXGM9Q SQ MDLSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPVLGPMVYAICYCPLPRLADLEALKVADSKTLLESERERLFAKMEDTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTATGLIQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGIEVTVKAKADALYPVVSAASICAKVARDQAVKKWQFVEKLQDLDTDYGSGYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTAQTILEKEAEDVIWEDSASENQEGLRKITSYFLNEGSQARPRSSHRYFLERGLESATSL TTXGM9Q TT Literature-reported TTSM4BA ID TTSM4BA TTSM4BA TN RNA-binding protein Musashi-1 (MSI1) TTSM4BA UP O43347 TTSM4BA UC MSI1H_HUMAN TTSM4BA SN RNA-binding protein Musashi homolog 1; Musashi-1 TTSM4BA GN MSI1 TTSM4BA FC Regulates expression of the NOTCH1 antagonist NUMB. Binds RNA containing the sequence 5'-GUUAGUUAGUUAGUU-3' and other sequences containing the pattern 5'-[GA]U(1-3)AGU-3'. May play a role in the proliferation and maintenance of stem cells in the central nervous system. RNA binding protein that regulates the expression of target mRNAs at the translation level. TTSM4BA SQ METDAPQPGLASPDSPHDPCKMFIGGLSWQTTQEGLREYFGQFGEVKECLVMRDPLTKRSRGFGFVTFMDQAGVDKVLAQSRHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSVNTTVEDVKQYFEQFGKVDDAMLMFDKTTNRHRGFGFVTFESEDIVEKVCEIHFHEINNKMVECKKAQPKEVMSPTGSARGRSRVMPYGMDAFMLGIGMLGYPGFQATTYASRSYTGLAPGYTYQFPEFRVERTPLPSAPVLPELTAIPLTAYGPMAAAAAAAAVVRGTGSHPWTMAPPPGSTPSRTGGFLGTTSPGPMAELYGAANQDSGVSSYISAASPAPSTGFGHSLGGPLIATAFTNGYH TTSM4BA TT Literature-reported TTSM4BA FM Musashi family TTD6SZ8 ID TTD6SZ8 TTD6SZ8 TN Runt-related transcription factor 2 (RUNX2) TTD6SZ8 UP Q13950 TTD6SZ8 UC RUNX2_HUMAN TTD6SZ8 SN SL3/AKV core-binding factor alpha A subunit; SL3-3 enhancer factor 1 alpha A subunit; Polyomavirus enhancer-binding protein 2 alpha Asubunit; Polyomavirus enhancer-binding protein 2 alpha A subunit; PEBP2A; PEBP2-alpha A; PEA2-alpha A; Osteoblast-specific transcription factor 2; Oncogene AML-3; OSF2; OSF-2; Core-binding factor subunit alpha-1; CBFA1; CBF-alpha-1; Acute myeloid leukemia 3 protein; AML3 TTD6SZ8 GN RUNX2 TTD6SZ8 FC Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE). Inhibits KAT6B-dependent transcriptional activation. Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. TTD6SZ8 SQ MASNSLFSTVTPCQQNFFWDPSTSRRFSPPSSSLQPGKMSDVSPVVAAQQQQQQQQQQQQQQQQQQQQQQQEAAAAAAAAAAAAAAAAAVPRLRPPHDNRTMVEIIADHPAELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGEVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKVTVDGPREPRRHRQKLDDSKPSLFSDRLSDLGRIPHPSMRVGVPPQNPRPSLNSAPSPFNPQGQSQITDPRQAQSSPPWSYDQSYPSYLSQMTSPSIHSTTPLSSTRGTGLPAITDVPRRISDDDTATSDFCLWPSTLSKKSQAGASELGPFSDPRQFPSISSLTESRFSNPRMHYPATFTYTPPVTSGMSLGMSATTHYHTYLPPPYPGSSQSQSGPFQTSSTPYLYYGTSSGSYQFPMVPGGDRSPSRMLPPCTTTSNGSTLLNPNLPNQNDGVDADGSHSSSPTVLNSSGRMDESVWRPY TTD6SZ8 TT Literature-reported TTQVIA4 ID TTQVIA4 TTQVIA4 TN Salmonella typhi 27-kDa outer membrane protein T2544 (SALTI STY0351) TTQVIA4 UP Q8Z939 TTQVIA4 UC Q8Z939_SALTI TTQVIA4 SN Possible outer membrane adhesin TTQVIA4 GN SALTI STY0351 TTQVIA4 FC Plays a major role in bacterial adhesion to the host through high-affinity binding to laminin. TTQVIA4 SQ MKNFFAVCIIPLVVTWSATASAKEGIYITGKAGTSVVNVYGINSTFSQEEIVNGHATLPDRTKGVFGGGVAIGYDFYDPFQLPVRLELDTTFRGETDAKGGQDIIAFGQPVHINVKNQVRMTTYIVNGYYDFHNSTAFTPYISAGVGLAHVKLSNNTIPVGFGINETLSASKNNFAWGAGIGAKYAVTDNIMIDASYKYINAGKVSISKNHYAGDEHTAYDADTKAASNDFMLGITYAF TTQVIA4 TT Literature-reported TTDR4UA ID TTDR4UA TTDR4UA TN Schistosoma P2X receptor (sch P2X) TTDR4UA UP C4QPC8 TTDR4UA UC C4QPC8_SCHMA TTDR4UA SN p2X receptor subunit (AJ703803) TTDR4UA GN sch P2X TTDR4UA FC A non-vertebrate ATP-gated ion channel. TTDR4UA SQ MYFKGDSEFLGLKQCAREQMVKGIAVLFEYETPKLVQISNIKIGVTQRLLQLVILIYVVCWVMIYEKGYQENDIAKSAVTTKVKGVGFTNFSHIPGIGMRSWDVADYIVPPLENNALFVITNLVKTERQSLSKCQESSWVPEAACYKDSDCKPYFISHLGNGAHTGKCIIKPGNDIGSCEIYSWCPLENDTLPLGRKSFLFPMVYNYTLLIKNDINFEKFGIHRRNIQNWASKKFLRTCLYNKTDPENRFCPIFQFGTIFEEANVDQSIFISGGVIGIDIDWKCDLDWDVQYCNPTYSFRRLDDAHAKIASGFNFR TTDR4UA TT Literature-reported TTX8I1Y ID TTX8I1Y TTX8I1Y TN Secreted frizzled related protein-4 (SFRP4) TTX8I1Y UP Q6FHJ7 TTX8I1Y UC SFRP4_HUMAN TTX8I1Y SN sFRP-4; Secreted frizzled-related protein 4; FrpHE; Frizzled protein, human endometrium TTX8I1Y GN SFRP4 TTX8I1Y FC Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP4 plays a role in bone morphogenesis. May also act as a regulator of adult uterine morphology and function. May also increase apoptosis during ovulation possibly through modulation of FZ1/FZ4/WNT4 signaling. Has phosphaturic effects by specifically inhibiting sodium-dependent phosphate uptake. TTX8I1Y SQ MFLSILVALCLWLHLALGVRGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSAVLRFFLCAMYAPICTLEFLHDPIKPCKSVCQRARDDCEPLMKMYNHSWPESLACDELPVYDRGVCISPEAIVTDLPEDVKWIDITPDMMVQERPLDVDCKRLSPDRCKCKKVKPTLATYLSKNYSYVIHAKIKAVQRSGCNEVTTVVDVKEIFKSSSPIPRTQVPLITNSSCQCPHILPHQDVLIMCYEWRSRMMLLENCLVEKWRDQLSKRSIQWEERLQEQRRTVQDKKKTAGRTSRSNPPKPKGKPPAPKPASPKKNIKTRSAQKRTNPKRV TTX8I1Y TT Literature-reported TTY5R9H ID TTY5R9H TTY5R9H TN Secretogranin-3 (SCG3) TTY5R9H UP Q8WXD2 TTY5R9H UC SCG3_HUMAN TTY5R9H SN SgIII; Secretogranin III TTY5R9H GN SCG3 TTY5R9H FC endoplasmic reticulum lumen, extracellular region, secretory granule lumen, RNA binding, cellular protein metabolic process, platelet degranulation, post-translational protein modification. TTY5R9H SQ MGFLGTGTWILVLVLPIQAFPKPGGSQDKSLHNRELSAERPLNEQIAEAEEDKIKKTYPPENKPGQSNYSFVDNLNLLKAITEKEKIEKERQSIRSSPLDNKLNVEDVDSTKNRKLIDDYDSTKSGLDHKFQDDPDGLHQLDGTPLTAEDIVHKIAARIYEENDRAVFDKIVSKLLNLGLITESQAHTLEDEVAEVLQKLISKEANNYEEDPNKPTSWTENQAGKIPEKVTPMAAIQDGLAKGENDETVSNTLTLTNGLERRTKTYSEDNFEELQYFPNFYALLKSIDSEKEAKEKETLITIMKTLIDFVKMMVKYGTISPEEGVSYLENLDEMIALQTKNKLEKNATDNISKLFPAPSEKSHEETDSTKEEAAKMEKEYGSLKDSTKDDNSNPGGKTDEPKGKTEAYLEAIRKNIEWLKKHDKKGNKEDYDLSKMRDFINKQADAYVEKGILDKEEAEAIKRIYSSL TTY5R9H TT Literature-reported TT059DA ID TT059DA TT059DA TN Serum amyloid A-activating factor-1 (MAZ) TT059DA UP P56270 TT059DA UC MAZ_HUMAN TT059DA SN Zinc finger protein 801; ZNF801; ZF87; Transcription factor Zif87; SAF-1; Purine-binding transcription factor; Pur-1; Myc-associated zinc finger protein; MAZI TT059DA GN MAZ TT059DA FC May function as a transcription factor with dual roles in transcription initiation and termination. Binds to two sites, ME1a1 and ME1a2, within the MYC promoter having greater affinity for the former. Also binds to multiple G/C-rich sites within the promoter of the Sp1 family of transcription factors. Regulates inflammation-induced expression of serum amyloid A proteins. TT059DA SQ MFPVFPCTLLAPPFPVLGLDSRGVGGLMNSFPPPQGHAQNPLQVGAELQSRFFASQGCAQSPFQAAPAPPPTPQAPAAEPLQVDLLPVLAAAQESAAAAAAAAAAAAAVAAAPPAPAAASTVDTAALKQPPAPPPPPPPVSAPAAEAAPPASAATIAAAAATAVVAPTSTVAVAPVASALEKKTKSKGPYICALCAKEFKNGYNLRRHEAIHTGAKAGRVPSGAMKMPTMVPLSLLSVPQLSGAGGGGGEAGAGGGAAAVAAGGVVTTTASGKRIRKNHACEMCGKAFRDVYHLNRHKLSHSDEKPYQCPVCQQRFKRKDRMSYHVRSHDGAVHKPYNCSHCGKSFSRPDHLNSHVRQVHSTERPFKCEKCEAAFATKDRLRAHTVRHEEKVPCHVCGKMLSSAYISDHMKVHSQGPHHVCELCNKGTGEVCPMAAAAAAAAAAAAAAVAAPPTAVGSLSGAEGVPVSSQPLPSQPW TT059DA TT Literature-reported TTZ9WGL ID TTZ9WGL TTZ9WGL TN SHC SH2 domain-binding protein 1 (SHCBP1) TTZ9WGL UP Q8NEM2 TTZ9WGL UC SHCBP_HUMAN TTZ9WGL SN PAL TTZ9WGL GN SHCBP1 TTZ9WGL FC May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc. Acts as a positive regulator of FGF signaling in neural progenitor cells. TTZ9WGL SQ MADGSLTGGGLEAAAMAPERMGWAVEQELASLEKGLFQDEDSCSDCSYRDKPGSSLQSFMPEGKTFFPEIFQTNQLLFYERFRAYQDYILADCKASEVQEFTAEFLEKVLEPSGWRAVWHTNVFKVLVEITDVDFAALKAVVRLAEPYLCDSQVSTFTMECMKELLDLKEHRLPLQELWVVFDDSGVFDQTALAIEHVRFFYQNIWRSWDEEEEDEYDYFVRCVEPRLRLHYDILEDRVPSGLIVDYHNLLSQCEESYRKFLNLRSSLSNCNSDSEQENISMVEGLKLYSEMEQLKQKLKLIENPLLRYVFGYQKNSNIQAKGVRSSGQKITHVVSSTMMAGLLRSLLTDRLCQEPGEEEREIQFHSDPLSAINACFEGDTVIVCPGHYVVHGTFSIADSIELEGYGLPDDIVIEKRGKGDTFVDCTGADIKISGIKFVQHDAVEGILIVHRGKTTLENCVLQCETTGVTVRTSAEFLMKNSDLYGAKGAGIEIYPGSQCTLSDNGIHHCKEGILIKDFLDEHYDIPKISMVNNIIHNNEGYGVVLVKPTIFSDLQENAEDGTEENKALKIQTSGEPDVAERVDLEELIECATGKMELCARTDPSEQVEGNCEIVNELIAASTQKGQIKKKRLSELGITQADDNLMSQEMFVGIVGNQFKWNGKGSFGTFLF TTZ9WGL TT Literature-reported TTWREQP ID TTWREQP TTWREQP TN Signal peptide CUB-EGF-like-domain containing 2 (SCUBE2) TTWREQP UP Q9NQ36 TTWREQP UC SCUB2_HUMAN TTWREQP SN Signal peptide, CUB and EGF-like domain-containing protein 2; Scube/You; Protein CEGP1; CEGP1 TTWREQP GN SCUBE2 TTWREQP FC Lipid-binding protein required for SHH long-range signaling by binding to the dually lipid-modified SHH (ShhNp) and by promoting ShhNp mobilization, solubilization and release from the cell membrane. Acts by enhancing the proteolytic processing (shedding) of the lipid-modified N- and C- terminal of ShhNp at the cell surface. Synergizes with DISP1 to increase SHH secretion. Probable cell surface coreceptor for VEGFR2 involved in VEGFR2-mediated angiogenesis. TTWREQP SQ MGVAGRNRPGAAWAVLLLLLLLPPLLLLAGAVPPGRGRAAGPQEDVDECAQGLDDCHADALCQNTPTSYKCSCKPGYQGEGRQCEDIDECGNELNGGCVHDCLNIPGNYRCTCFDGFMLAHDGHNCLDVDECLENNGGCQHTCVNVMGSYECCCKEGFFLSDNQHTCIHRSEEGLSCMNKDHGCSHICKEAPRGSVACECRPGFELAKNQRDCILTCNHGNGGCQHSCDDTADGPECSCHPQYKMHTDGRSCLEREDTVLEVTESNTTSVVDGDKRVKRRLLMETCAVNNGGCDRTCKDTSTGVHCSCPVGFTLQLDGKTCKDIDECQTRNGGCDHFCKNIVGSFDCGCKKGFKLLTDEKSCQDVDECSLDRTCDHSCINHPGTFACACNRGYTLYGFTHCGDTNECSINNGGCQQVCVNTVGSYECQCHPGYKLHWNKKDCVEVKGLLPTSVSPRVSLHCGKSGGGDGCFLRCHSGIHLSSDVTTIRTSVTFKLNEGKCSLKNAELFPEGLRPALPEKHSSVKESFRYVNLTCSSGKQVPGAPGRPSTPKEMFITVEFELETNQKEVTASCDLSCIVKRTEKRLRKAIRTLRKAVHREQFHLQLSGMNLDVAKKPPRTSERQAESCGVGQGHAENQCVSCRAGTYYDGARERCILCPNGTFQNEEGQMTCEPCPRPGNSGALKTPEAWNMSECGGLCQPGEYSADGFAPCQLCALGTFQPEAGRTSCFPCGGGLATKHQGATSFQDCETRVQCSPGHFYNTTTHRCIRCPVGTYQPEFGKNNCVSCPGNTTTDFDGSTNITQCKNRRCGGELGDFTGYIESPNYPGNYPANTECTWTINPPPKRRILIVVPEIFLPIEDDCGDYLVMRKTSSSNSVTTYETCQTYERPIAFTSRSKKLWIQFKSNEGNSARGFQVPYVTYDEDYQELIEDIVRDGRLYASENHQEILKDKKLIKALFDVLAHPQNYFKYTAQESREMFPRSFIRLLRSKVSRFLRPYK TTWREQP TT Literature-reported TTCTYNP ID TTCTYNP TTCTYNP TN Small cell lung carcinoma cluster 4 antigen (CD24) TTCTYNP UP P25063 TTCTYNP UC CD24_HUMAN TTCTYNP SN Signal transducer CD24; CD24A TTCTYNP GN CD24 TTCTYNP FC Signaling could be triggered by the binding of a lectin-like ligand to the CD24 carbohydrates, and transduced by the release of second messengers derived from the GPI-anchor. Modulates B-cell activation responses. Promotes AG-dependent proliferation of B-cells, and prevents their terminal differentiation into antibody-forming cells. In association with SIGLEC10 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90. Plays a role in the control of autoimmunity. May have a pivotal role in cell differentiation of different cell types. TTCTYNP SQ MGRAMVARLGLGLLLLALLLPTQIYSSETTTGTSSNSSQSTSNSGLAPNPTNATTKAAGGALQSTASLFVVSLSLLHLYS TTCTYNP TT Literature-reported TT2KHSC ID TT2KHSC TT2KHSC TN Small nuclear ribonuclear CaSm (LSM1) TT2KHSC UP O15116 TT2KHSC UC LSM1_HUMAN TT2KHSC SN LSM1; Cancer-associated Sm-like (CaSm) oncogene; Cancer-associated Sm-like; CaSm TT2KHSC GN LSM1 TT2KHSC FC Plays a role in replication-dependenthistone mRNA degradation. Binds specifically to the 3'-terminal U-tract of U6 snRNA. TT2KHSC SQ MNYMPGTASLIEDIDKKHLVLLRDGRTLIGFLRSIDQFANLVLHQTVERIHVGKKYGDIPRGIFVVRGENVVLLGEIDLEKESDTPLQQVSIEEILEEQRVEQQTKLEAEKLKVQALKDRGLSIPRADTLDEY TT2KHSC TT Literature-reported TTW30FR ID TTW30FR TTW30FR TN Small ubiquitin-related modifier (SUMO) TTW30FR UP P63165; P61956; P55854; Q6EEV6; G2XKQ0 TTW30FR UC SUMO1_HUMAN; SUMO2_HUMAN; SUMO3_HUMAN; SUMO4_HUMAN; SUMO5_HUMAN TTW30FR SN Ubiquitin-like protein; SUMO; SMT3 homolog 1 TTW30FR GN SUMO1; SUMO2; SUMO3; SUMO4; SUMO1P1 TTW30FR FC Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3. TTW30FR SQ MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV TTW30FR TT Preclinical TTJN46R ID TTJN46R TTJN46R TN Sodium/potassium/calcium exchanger 6 (SLC8B1) TTJN46R UP Q6J4K2 TTJN46R UC NCLX_HUMAN TTJN46R SN Solute carrier family 8 member B1; Solute carrier family 24 member 6; Sodium/calcium exchanger protein, mitochondrial; Na(+)/K(+)/Ca(2+)-exchange protein 6; NCKX6; Mitochondrial sodium/calcium exchanger protein TTJN46R GN SLC8B1 TTJN46R FC Mitochondrial sodium/calcium antiporter that mediates sodium-dependent calcium efflux from mitochondrion, by mediating the exchange of 3 sodium ions per 1 calcium ion. Plays a central role in mitochondrial calcium homeostasis by mediating mitochondrial calcium extrusion: calcium efflux is essential for mitochondrial function and cell survival, notably in cardiomyocytes (By similarity). Regulates rates of glucose-dependent insulin secretion in pancreatic beta-cells during the first phase of insulin secretion: acts by mediating efflux of calcium from mitochondrion, thereby affecting cytoplasmic calcium responses. Required for store-operated Ca(2+) entry (SOCE) and Ca(2+) release-activated Ca(2+) (CRAC) channel regulation: sodium transport by SLC8B1 leads to promote calcium-shuttling that modulates mitochondrial redox status, thereby regulating SOCE activity. Involved in B-lymphocyte chemotaxis (By similarity). Able to transport Ca(2+) in exchange of either Li(+) or Na(+), explaining how Li(+) catalyzes Ca(2+) exchange. In contrast to other members of the family its function is independent of K(+). TTJN46R SQ MAGRRLNLRWALSVLCVLLMAETVSGTRGSSTGAHISPQFPASGVNQTPVVDCRKVCGLNVSDRCDFIRTNPDCHSDGGYLDYLEGIFCHFPPSLLPLAVTLYVSWLLYLFLILGVTAAKFFCPNLSAISTTLKLSHNVAGVTFLAFGNGAPDIFSALVAFSDPHTAGLALGALFGAGVLVTTVVAGGITILHPFMAASRPFFRDIVFYMVAVFLTFLMLFRGRVTLAWALGYLGLYVFYVVTVILCTWIYQRQRRGSLFCPMPVTPEILSDSEEDRVSSNTNSYDYGDEYRPLFFYQETTAQILVRALNPLDYMKWRRKSAYWKALKVFKLPVEFLLLLTVPVVDPDKDDQNWKRPLNCLHLVISPLVVVLTLQSGTYGVYEIGGLVPVWVVVVIAGTALASVTFFATSDSQPPRLHWLFAFLGFLTSALWINAAATEVVNILRSLGVVFRLSNTVLGLTLLAWGNSIGDAFSDFTLARQGYPRMAFSACFGGIIFNILVGVGLGCLLQISRSHTEVKLEPDGLLVWVLAGALGLSLVFSLVSVPLQCFQLSRVYGFCLLLFYLNFLVVALLTEFGVIHLKSM TTJN46R TT Literature-reported TT9LGO5 ID TT9LGO5 TT9LGO5 TN Sodium-dependent proline transporter (SLC6A7) TT9LGO5 UP Q99884 TT9LGO5 UC SC6A7_HUMAN TT9LGO5 SN Solute carrier family 6 member 7; PROT TT9LGO5 GN SLC6A7 TT9LGO5 FC Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals. TT9LGO5 SQ MKKLQGAHLRKPVTPDLLMTPSDQGDVDLDVDFAAHRGNWTGKLDFLLSCIGYCVGLGNVWRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGAAMLLIVGLVAIYYNMIIAYVLFYLFASLTSDLPWEHCGNWWNTELCLEHRVSKDGNGALPLNLTCTVSPSEEYWSRYVLHIQGSQGIGSPGEIRWNLCLCLLLAWVIVFLCILKGVKSSGKVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLGVGFGGLLTFASYNTFHQNIYRDTFIVTLGNAITSILAGFAIFSVLGYMSQELGVPVDQVAKAGPGLAFVVYPQAMTMLPLSPFWSFLFFFMLLTLGLDSQFAFLETIVTAVTDEFPYYLRPKKAVFSGLICVAMYLMGLILTTDGGMYWLVLLDDYSASFGLMVVVITTCLAVTRVYGIQRFCRDIHMMLGFKPGLYFRACWLFLSPATLLALMVYSIVKYQPSEYGSYRFPPWAELLGILMGLLSCLMIPAGMLVAVLREEGSLWERLQQASRPAMDWGPSLEENRTGMYVATLAGSQSPKPLMVHMRKYGGITSFENTAIEVDREIAEEEESMM TT9LGO5 TT Literature-reported TTUGD21 ID TTUGD21 TTUGD21 TN Sodium-independent organic anion transporter (SLCO1A2) TTUGD21 UP P46721 TTUGD21 UC SO1A2_HUMAN TTUGD21 SN Solute carrier organic anion transporter family member 1A2; Solute carrier family 21 member 3; SLC21A3; Organic anion-transporting polypeptide 1; OATP1A2; OATP-A; OATP-1; OATP TTUGD21 GN SLCO1A2 TTUGD21 FC Mediates the Na(+)-independent transport of organic anions such as sulfobromophthalein (BSP) and conjugated (taurocholate) and unconjugated (cholate) bile acids (By similarity). Selectively inhibited by the grapefruit juice component naringin. TTUGD21 SQ MGETEKRIETHRIRCLSKLKMFLLAITCAFVSKTLSGSYMNSMLTQIERQFNIPTSLVGFINGSFEIGNLLLIIFVSYFGTKLHRPIMIGIGCVVMGLGCFLKSLPHFLMNQYEYESTVSVSGNLSSNSFLCMENGTQILRPTQDPSECTKEVKSLMWVYVLVGNIVRGMGETPILPLGISYIEDFAKFENSPLYIGLVETGAIIGPLIGLLLASFCANVYVDTGFVNTDDLIITPTDTRWVGAWWFGFLICAGVNVLTAIPFFFLPNTLPKEGLETNADIIKNENEDKQKEEVKKEKYGITKDFLPFMKSLSCNPIYMLFILVSVIQFNAFVNMISFMPKYLEQQYGISSSDAIFLMGIYNLPPICIGYIIGGLIMKKFKITVKQAAHIGCWLSLLEYLLYFLSFLMTCENSSVVGINTSYEGIPQDLYVENDIFADCNVDCNCPSKIWDPVCGNNGLSYLSACLAGCETSIGTGINMVFQNCSCIQTSGNSSAVLGLCDKGPDCSLMLQYFLILSAMSSFIYSLAAIPGYMVLLRCMKSEEKSLGVGLHTFCTRVFAGIPAPIYFGALMDSTCLHWGTLKCGESGACRIYDSTTFRYIYLGLPAALRGSSFVPALIILILLRKCHLPGENASSGTELIETKVKGKENECKDIYQKSTVLKDDELKTKL TTUGD21 TT Literature-reported TTJ8C67 ID TTJ8C67 TTJ8C67 TN Solute carrier family 12 member 4 (SLC12A4) TTJ8C67 UP Q9UP95 TTJ8C67 UC S12A4_HUMAN TTJ8C67 SN hKCC1; KCC1; Erythroid K-Cl cotransporter 1; Electroneutral potassium-chloride cotransporter 1 TTJ8C67 GN SLC12A4 TTJ8C67 FC Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May contribute to cell volume homeostasis in single cells. May be involved in the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia (By similarity). Isoform 4 has no transport activity. TTJ8C67 SQ MPHFTVVPVDGPRRGDYDNLEGLSWVDYGERAELDDSDGHGNHRESSPFLSPLEASRGIDYYDRNLALFEEELDIRPKVSSLLGKLVSYTNLTQGAKEHEEAESGEGTRRRAAEAPSMGTLMGVYLPCLQNIFGVILFLRLTWMVGTAGVLQALLIVLICCCCTLLTAISMSAIATNGVVPAGGSYFMISRSLGPEFGGAVGLCFYLGTTFAAAMYILGAIEILLTYIAPPAAIFYPSGAHDTSNATLNNMRVYGTIFLTFMTLVVFVGVKYVNKFASLFLACVIISILSIYAGGIKSIFDPPVFPVCMLGNRTLSRDQFDICAKTAVVDNETVATQLWSFFCHSPNLTTDSCDPYFMLNNVTEIPGIPGAAAGVLQENLWSAYLEKGDIVEKHGLPSADAPSLKESLPLYVVADIATSFTVLVGIFFPSVTGIMAGSNRSGDLRDAQKSIPVGTILAIITTSLVYFSSVVLFGACIEGVVLRDKYGDGVSRNLVVGTLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIAKDNIIPFLRVFGHGKVNGEPTWALLLTALIAELGILIASLDMVAPILSMFFLMCYLFVNLACAVQTLLRTPNWRPRFKYYHWALSFLGMSLCLALMFVSSWYYALVAMLIAGMIYKYIEYQGAEKEWGDGIRGLSLSAARYALLRLEEGPPHTKNWRPQLLVLLKLDEDLHVKYPRLLTFASQLKAGKGLTIVGSVIQGSFLESYGEAQAAEQTIKNMMEIEKVKGFCQVVVASKVREGLAHLIQSCGLGGMRHNSVVLGWPYGWRQSEDPRAWKTFIDTVRCTTAAHLALLVPKNIAFYPSNHERYLEGHIDVWWIVHDGGMLMLLPFLLRQHKVWRKCRMRIFTVAQMDDNSIQMKKDLAVFLYHLRLEAEVEVVEMHNSDISAYTYERTLMMEQRSQMLRQMRLTKTEREREAQLVKDRHSALRLESLYSDEEDESAVGADKIQMTWTRDKYMTETWDPSHAPDNFRELVHIKPDQSNVRRMHTAVKLNEVIVTRSHDARLVLLNMPGPPRNSEGDENYMEFLEVLTEGLERVLLVRGGGREVITIYS TTJ8C67 TT Literature-reported TTU2PCD ID TTU2PCD TTU2PCD TN Solute carrier family 12 member 7 (SLC12A7) TTU2PCD UP Q9Y666 TTU2PCD UC S12A7_HUMAN TTU2PCD SN KCC4; K-Cl cotransporter 4; Electroneutral potassium-chloride cotransporter 4 TTU2PCD GN SLC12A7 TTU2PCD FC Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May mediate K(+) uptake into Deiters' cells in the cochlea and contribute to K(+) recycling in the inner ear. Important for the survival of cochlear outer and inner hair cells and the maintenance of the organ of Corti. May be required for basolateral Cl(-) extrusion in the kidney and contribute to renal acidification (By similarity). TTU2PCD SQ MPTNFTVVPVEAHADGGGDETAERTEAPGTPEGPEPERPSPGDGNPRENSPFLNNVEVEQESFFEGKNMALFEEEMDSNPMVSSLLNKLANYTNLSQGVVEHEEDEESRRREAKAPRMGTFIGVYLPCLQNILGVILFLRLTWIVGVAGVLESFLIVAMCCTCTMLTAISMSAIATNGVVPAGGSYYMISRSLGPEFGGAVGLCFYLGTTFAGAMYILGTIEIFLTYISPGAAIFQAEAAGGEAAAMLHNMRVYGTCTLVLMALVVFVGVKYVNKLALVFLACVVLSILAIYAGVIKSAFDPPDIPVCLLGNRTLSRRSFDACVKAYGIHNNSATSALWGLFCNGSQPSAACDEYFIQNNVTEIQGIPGAASGVFLENLWSTYAHAGAFVEKKGVPSVPVAEESRASALPYVLTDIAASFTLLVGIYFPSVTGIMAGSNRSGDLKDAQKSIPTGTILAIVTTSFIYLSCIVLFGACIEGVVLRDKFGEALQGNLVIGMLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIARDGIVPFLQVFGHGKANGEPTWALLLTVLICETGILIASLDSVAPILSMFFLMCYLFVNLACAVQTLLRTPNWRPRFKFYHWTLSFLGMSLCLALMFICSWYYALSAMLIAGCIYKYIEYRGAEKEWGDGIRGLSLNAARYALLRVEHGPPHTKNWRPQVLVMLNLDAEQAVKHPRLLSFTSQLKAGKGLTIVGSVLEGTYLDKHMEAQRAEENIRSLMSTEKTKGFCQLVVSSSLRDGMSHLIQSAGLGGLKHNTVLMAWPASWKQEDNPFSWKNFVDTVRDTTAAHQALLVAKNVDSFPQNQERFGGGHIDVWWIVHDGGMLMLLPFLLRQHKVWRKCRMRIFTVAQVDDNSIQMKKDLQMFLYHLRISAEVEVVEMVENDISAFTYERTLMMEQRSQMLKQMQLSKNEQEREAQLIHDRNTASHTAAAARTQAPPTPDKVQMTWTREKLIAEKYRSRDTSLSGFKDLFSMKPDQSNVRRMHTAVKLNGVVLNKSQDAQLVLLNMPGPPKNRQGDENYMEFLEVLTEGLNRVLLVRGGGREVITIYS TTU2PCD TT Literature-reported TTFIMH7 ID TTFIMH7 TTFIMH7 TN Solute carrier family 13 member 5 (SLC13A5) TTFIMH7 UP Q86YT5 TTFIMH7 UC S13A5_HUMAN TTFIMH7 SN Sodium-coupled citrate transporter; SLC13A5; NaCT; Na(+)-coupled citrate transporter; Human sodium-coupled citrate transporter TTFIMH7 GN SLC13A5 TTFIMH7 FC High-affinity sodium/citrate cotransporter that mediates citrate entry into cells. The transport process is electrogenic; it is the trivalent form of citrate rather than the divalent form that is recognized as a substrate. May facilitate the utilization of circulating citrate for the generation of metabolic energy and for the synthesis of fatty acids and cholesterol. TTFIMH7 SQ MASALSYVSKFKSFVILFVTPLLLLPLVILMPAKFVRCAYVIILMAIYWCTEVIPLAVTSLMPVLLFPLFQILDSRQVCVQYMKDTNMLFLGGLIVAVAVERWNLHKRIALRTLLWVGAKPARLMLGFMGVTALLSMWISNTATTAMMVPIVEAILQQMEATSAATEAGLELVDKGKAKELPGSQVIFEGPTLGQQEDQERKRLCKAMTLCICYAASIGGTATLTGTGPNVVLLGQMNELFPDSKDLVNFASWFAFAFPNMLVMLLFAWLWLQFVYMRFNFKKSWGCGLESKKNEKAALKVLQEEYRKLGPLSFAEINVLICFFLLVILWFSRDPGFMPGWLTVAWVEGETKYVSDATVAIFVATLLFIVPSQKPKFNFRSQTEEERKTPFYPPPLLDWKVTQEKVPWGIVLLLGGGFALAKGSEASGLSVWMGKQMEPLHAVPPAAITLILSLLVAVFTECTSNVATTTLFLPIFASMSRSIGLNPLYIMLPCTLSASFAFMLPVATPPNAIVFTYGHLKVADMVKTGVIMNIIGVFCVFLAVNTWGRAIFDLDHFPDWANVTHIET TTFIMH7 TT Literature-reported TTAYPWS ID TTAYPWS TTAYPWS TN Solute carrier family 15 member 3 (SLC15A3) TTAYPWS UP Q8IY34 TTAYPWS UC S15A3_HUMAN TTAYPWS SN Peptide/histidine transporter 2; Peptide transporter 3; PTR3; PHT2; Osteoclast transporter; OCTP TTAYPWS GN SLC15A3 TTAYPWS FC Proton oligopeptide cotransporter. Transports free histidine and certain di- and tripeptides (By similarity). TTAYPWS SQ MPAPRAREQPRVPGERQPLLPRGARGPRRWRRAAGAAVLLVEMLERAAFFGVTANLVLYLNSTNFNWTGEQATRAALVFLGASYLLAPVGGWLADVYLGRYRAVALSLLLYLAASGLLPATAFPDGRSSFCGEMPASPLGPACPSAGCPRSSPSPYCAPVLYAGLLLLGLAASSVRSNLTSFGADQVMDLGRDATRRFFNWFYWSINLGAVLSLLVVAFIQQNISFLLGYSIPVGCVGLAFFIFLFATPVFITKPPMGSQVSSMLKLALQNCCPQLWQRHSARDRQCARVLADERSPQPGASPQEDIANFQVLVKILPVMVTLVPYWMVYFQMQSTYVLQGLHLHIPNIFPANPANISVALRAQGSSYTIPEAWLLLANVVVVLILVPLKDRLIDPLLLRCKLLPSALQKMALGMFFGFTSVIVAGVLEMERLHYIHHNETVSQQIGEVLYNAAPLSIWWQIPQYLLIGISEIFASIPGLEFAYSEAPRSMQGAIMGIFFCLSGVGSLLGSSLVALLSLPGGWLHCPKDFGNINNCRMDLYFFLLAGIQAVTALLFVWIAGRYERASQGPASHSRFSRDRG TTAYPWS TT Literature-reported TTG2XRE ID TTG2XRE TTG2XRE TN Solute carrier family 15 member 4 (SLC15A4) TTG2XRE UP Q8N697 TTG2XRE UC S15A4_HUMAN TTG2XRE SN SLC15A4 TTG2XRE GN SLC15A4 TTG2XRE FC Proton oligopeptide cotransporter. Transports free histidine and certain di- and tripeptides. TTG2XRE SQ MEGSGGGAGERAPLLGARRAAAAAAAAGAFAGRRAACGAVLLTELLERAAFYGITSNLVLFLNGAPFCWEGAQASEALLLFMGLTYLGSPFGGWLADARLGRARAILLSLALYLLGMLAFPLLAAPATRAALCGSARLLNCTAPGPDAAARCCSPATFAGLVLVGLGVATVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAILSLGGIAYIQQNVSFVTGYAIPTVCVGLAFVVFLCGQSVFITKPPDGSAFTDMFKILTYSCCSQKRSGERQSNGEGIGVFQQSSKQSLFDSCKMSHGGPFTEEKVEDVKALVKIVPVFLALIPYWTVYFQMQTTYVLQSLHLRIPEISNITTTPHTLPAAWLTMFDAVLILLLIPLKDKLVDPILRRHGLLPSSLKRIAVGMFFVMCSAFAAGILESKRLNLVKEKTINQTIGNVVYHAADLSLWWQVPQYLLIGISEIFASIAGLEFAYSAAPKSMQSAIMGLFFFFSGVGSFVGSGLLALVSIKAIGWMSSHTDFGNINGCYLNYYFFLLAAIQGATLLLFLIISVKYDHHRDHQRSRANGVPTSRRA TTG2XRE TT Literature-reported TT2A1DZ ID TT2A1DZ TT2A1DZ TN Solute carrier family 19 member 2 (SLC19A2) TT2A1DZ UP O60779 TT2A1DZ UC S19A2_HUMAN TT2A1DZ SN Thiamine transporter 1; Thiamine carrier 1; ThTr1; ThTr-1; TRMA; THT1; TC1 TT2A1DZ GN SLC19A2 TT2A1DZ FC High-affinity transporter for the intake of thiamine. TT2A1DZ SQ MDVPGPVSRRAAAAAATVLLRTARVRRECWFLPTALLCAYGFFASLRPSEPFLTPYLLGPDKNLTEREVFNEIYPVWTYSYLVLLFPVFLATDYLRYKPVVLLQGLSLIVTWFMLLYAQGLLAIQFLEFFYGIATATEIAYYSYIYSVVDLGMYQKVTSYCRSATLVGFTVGSVLGQILVSVAGWSLFSLNVISLTCVSVAFAVAWFLPMPQKSLFFHHIPSTCQRVNGIKVQNGGIVTDTPASNHLPGWEDIESKIPLNMEEPPVEEPEPKPDRLLVLKVLWNDFLMCYSSRPLLCWSVWWALSTCGYFQVVNYTQGLWEKVMPSRYAAIYNGGVEAVSTLLGAVAVFAVGYIKISWSTWGEMTLSLFSLLIAAAVYIMDTVGNIWVCYASYVVFRIIYMLLITIATFQIAANLSMERYALVFGVNTFIALALQTLLTLIVVDASGLGLEITTQFLIYASYFALIAVVFLASGAVSVMKKCRKLEDPQSSSQVTTS TT2A1DZ TT Literature-reported TT9BTWM ID TT9BTWM TT9BTWM TN Solute carrier family 19 member 3 (SLC19A3) TT9BTWM UP Q9BZV2 TT9BTWM UC S19A3_HUMAN TT9BTWM SN Thiamine transporter 2; ThTr2; ThTr-2 TT9BTWM GN SLC19A3 TT9BTWM FC Mediates high affinity thiamine uptake, probably via a proton anti-port mechanism. Has no folate transport activity. TT9BTWM SQ MDCYRTSLSSSWIYPTVILCLFGFFSMMRPSEPFLIPYLSGPDKNLTSAEITNEIFPVWTYSYLVLLLPVFVLTDYVRYKPVIILQGISFIITWLLLLFGQGVKTMQVVEFFYGMVTAAEVAYYAYIYSVVSPEHYQRVSGYCRSVTLAAYTAGSVLAQLLVSLANMSYFYLNVISLASVSVAFLFSLFLPMPKKSMFFHAKPSREIKKSSSVNPVLEETHEGEAPGCEEQKPTSEILSTSGKLNKGQLNSLKPSNVTVDVFVQWFQDLKECYSSKRLFYWSLWWAFATAGFNQVLNYVQILWDYKAPSQDSSIYNGAVEAIATFGGAVAAFAVGYVKVNWDLLGELALVVFSVVNAGSLFLMHYTANIWACYAGYLIFKSSYMLLITIAVFQIAVNLNVERYALVFGINTFIALVIQTIMTVIVVDQRGLNLPVSIQFLVYGSYFAVIAGIFLMRSMYITYSTKSQKDVQSPAPSENPDVSHPEEESNIIMSTKL TT9BTWM TT Literature-reported TTITAVR ID TTITAVR TTITAVR TN Solute carrier family 22 member 16 (SLC22A16) TTITAVR UP Q86VW1 TTITAVR UC S22AG_HUMAN TTITAVR SN Organic cation/carnitine transporter 6; Organic cation transporter OKB1; Fly-like putative transporter 2; Flipt 2; FLIPT2; Carnitine transporter 2; CT2 TTITAVR GN SLC22A16 TTITAVR FC High affinity carnitine transporter; the uptake is partially sodium-ion dependent. Thought to mediate the L-carnitine secretion mechanism from testis epididymal epithelium into the lumen which is involved in the maturation of spermatozoa. Also transports organic cations such as tetraethylammonium (TEA) and doxorubicin. The uptake of TEA is inhibited by various organic cations. The uptake of doxorubicin is sodium-independent. TTITAVR SQ MGSRHFEGIYDHVGHFGRFQRVLYFICAFQNISCGIHYLASVFMGVTPHHVCRPPGNVSQVVFHNHSNWSLEDTGALLSSGQKDYVTVQLQNGEIWELSRCSRNKRENTSSLGYEYTGSKKEFPCVDGYIYDQNTWKSTAVTQWNLVCDRKWLAMLIQPLFMFGVLLGSVTFGYFSDRLGRRVVLWATSSSMFLFGIAAAFAVDYYTFMAARFFLAMVASGYLVVGFVYVMEFIGMKSRTWASVHLHSFFAVGTLLVALTGYLVRTWWLYQMILSTVTVPFILCCWVLPETPFWLLSEGRYEEAQKIVDIMAKWNRASSCKLSELLSLDLQGPVSNSPTEVQKHNLSYLFYNWSITKRTLTVWLIWFTGSLGFYSFSLNSVNLGGNEYLNLFLLGVVEIPAYTFVCIAMDKVGRRTVLAYSLFCSALACGVVMVIPQKHYILGVVTAMVGKFAIGAAFGLIYLYTAELYPTIVRSLAVGSGSMVCRLASILAPFSVDLSSIWIFIPQLFVGTMALLSGVLTLKLPETLGKRLATTWEEAAKLESENESKSSKLLLTTNNSGLEKTEAITPRDSGLGE TTITAVR TT Literature-reported TTVP9IQ ID TTVP9IQ TTVP9IQ TN Solute carrier family 28 member 2 (SLC28A2) TTVP9IQ UP O43868 TTVP9IQ UC S28A2_HUMAN TTVP9IQ SN hCNT2; Sodium/purine nucleoside co-transporter; Sodium/nucleoside cotransporter 2; Sodium-coupled nucleoside transporter 2; SPNT; Na(+)/nucleoside cotransporter 2; Concentrative nucleoside transporter 2; CNT2; CNT 2 TTVP9IQ GN SLC28A2 TTVP9IQ FC Sodium-dependent and purine-selective transporter. Exhibits the transport characteristics of the nucleoside transport system cif or N1 subtype (N1/cif) (selective for purine nucleosides and uridine). Plays a critical role in specific uptake and salvage of purine nucleosides in kidney and other tissues. TTVP9IQ SQ MEKASGRQSIALSTVETGTVNPGLELMEKEVEPEGSKRTDAQGHSLGDGLGPSTYQRRSRWPFSKARSFCKTHASLFKKILLGLLCLAYAAYLLAACILNFQRALALFVITCLVIFVLVHSFLKKLLGKKLTRCLKPFENSRLRLWTKWVFAGVSLVGLILWLALDTAQRPEQLIPFAGICMFILILFACSKHHSAVSWRTVFSGLGLQFVFGILVIRTDLGYTVFQWLGEQVQIFLNYTVAGSSFVFGDTLVKDVFAFQALPIIIFFGCVVSILYYLGLVQWVVQKVAWFLQITMGTTATETLAVAGNIFVGMTEAPLLIRPYLGDMTLSEIHAVMTGGFATISGTVLGAFIAFGVDASSLISASVMAAPCALASSKLAYPEVEESKFKSEEGVKLPRGKERNVLEAASNGAVDAIGLATNVAANLIAFLAVLAFINAALSWLGELVDIQGLTFQVICSYLLRPMVFMMGVEWTDCPMVAEMVGIKFFINEFVAYQQLSQYKNKRLSGMEEWIEGEKQWISVRAEIITTFSLCGFANLSSIGITLGGLTSIVPHRKSDLSKVVVRALFTGACVSLISACMAGILYVPRGAEADCVSFPNTSFTNRTYETYMCCRGLFQSTSLNGTNPPSFSGPWEDKEFSAMALTNCCGFYNNTVCA TTVP9IQ TT Literature-reported TTTR957 ID TTTR957 TTTR957 TN Solute carrier family 29 member 4 (SLC29A4) TTTR957 UP Q7RTT9 TTTR957 UC S29A4_HUMAN TTTR957 SN hENT4; Plasma membrane monoamine transporter; PSEC0113; PMAT; Equilibrative nucleoside transporter 4; ENT4 TTTR957 GN SLC29A4 TTTR957 FC Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia. TTTR957 SQ MGSVGSQRLEEPSVAGTPDPGVVMSFTFDSHQLEEAAEAAQGQGLRARGVPAFTDTTLDEPVPDDRYHAIYFAMLLAGVGFLLPYNSFITDVDYLHHKYPGTSIVFDMSLTYILVALAAVLLNNVLVERLTLHTRITAGYLLALGPLLFISICDVWLQLFSRDQAYAINLAAVGTVAFGCTVQQSSFYGYTGMLPKRYTQGVMTGESTAGVMISLSRILTKLLLPDERASTLIFFLVSVALELLCFLLHLLVRRSRFVLFYTTRPRDSHRGRPGLGRGYGYRVHHDVVAGDVHFEHPAPALAPNESPKDSPAHEVTGSGGAYMRFDVPRPRVQRSWPTFRALLLHRYVVARVIWADMLSIAVTYFITLCLFPGLESEIRHCILGEWLPILIMAVFNLSDFVGKILAALPVDWRGTHLLACSCLRVVFIPLFILCVYPSGMPALRHPAWPCIFSLLMGISNGYFGSVPMILAAGKVSPKQRELAGNTMTVSYMSGLTLGSAVAYCTYSLTRDAHGSCLHASTANGSILAGL TTTR957 TT Literature-reported TTUYIZW ID TTUYIZW TTUYIZW TN Solute carrier family 36 member 1 (SLC36A1) TTUYIZW UP Q7Z2H8 TTUYIZW UC S36A1_HUMAN TTUYIZW SN hPAT1; Proton/amino acid transporter 1; Proton-coupled amino acid transporter 1; PAT1 TTUYIZW GN SLC36A1 TTUYIZW FC Neutral amino acid/proton symporter. Has a pH-dependent electrogenic transport activity for small amino acids such as glycine, alanine and proline. Besides small apolar L-amino acids, it also recognizes their D-enantiomers and selected amino acid derivatives such as gamma-aminobutyric acid (By similarity). TTUYIZW SQ MSTQRLRNEDYHDYSSTDVSPEESPSEGLNNLSSPGSYQRFGQSNSTTWFQTLIHLLKGNIGTGLLGLPLAVKNAGIVMGPISLLIIGIVAVHCMGILVKCAHHFCRRLNKSFVDYGDTVMYGLESSPCSWLRNHAHWGRRVVDFFLIVTQLGFCCVYFVFLADNFKQVIEAANGTTNNCHNNETVILTPTMDSRLYMLSFLPFLVLLVFIRNLRALSIFSLLANITMLVSLVMIYQFIVQRIPDPSHLPLVAPWKTYPLFFGTAIFSFEGIGMVLPLENKMKDPRKFPLILYLGMVIVTILYISLGCLGYLQFGANIQGSITLNLPNCWLYQSVKLLYSIGIFFTYALQFYVPAEIIIPFFVSRAPEHCELVVDLFVRTVLVCLTCILAILIPRLDLVISLVGSVSSSALALIIPPLLEVTTFYSEGMSPLTIFKDALISILGFVGFVVGTYEALYELIQPSNAPIFINSTCAFI TTUYIZW TT Literature-reported TT5U0XA ID TT5U0XA TT5U0XA TN Solute carrier family 36 member 2 (SLC36A2) TT5U0XA UP Q495M3 TT5U0XA UC S36A2_HUMAN TT5U0XA SN Tramdorin-1; TRAMD1; Proton/amino acid transporter 2; Proton-coupled amino acid transporter 2; PAT2 TT5U0XA GN SLC36A2 TT5U0XA FC Involved in a pH-dependent electrogenic neuronal transport and sequestration of small amino acids. Transports glycine and proline. Inhibited by sarcosine (By similarity). TT5U0XA SQ MSVTKSTEGPQGAVAIKLDLMSPPESAKKLENKDSTFLDESPSESAGLKKTKGITVFQALIHLVKGNMGTGILGLPLAVKNAGILMGPLSLLVMGFIACHCMHILVKCAQRFCKRLNKPFMDYGDTVMHGLEANPNAWLQNHAHWGRHIVSFFLIITQLGFCCVYIVFLADNLKQVVEAVNSTTNNCYSNETVILTPTMDSRLYMLSFLPFLVLLVLIRNLRILTIFSMLANISMLVSLVIIIQYITQEIPDPSRLPLVASWKTYPLFFGTAIFSFESIGVVLPLENKMKNARHFPAILSLGMSIVTSLYIGMAALGYLRFGDDIKASISLNLPNCWLYQSVKLLYIAGILCTYALQFYVPAEIIIPFAISRVSTRWALPLDLSIRLVMVCLTCLLAILIPRLDLVISLVGSVSGTALALIIPPLLEVTTFYSEGMSPLTIFKDALISILGFVGFVVGTYQALDELLKSEDSHPFSNSTTFVR TT5U0XA TT Literature-reported TT1YE9Z ID TT1YE9Z TT1YE9Z TN Solute carrier family 38 member 1 (SLC38A1) TT1YE9Z UP Q9H2H9 TT1YE9Z UC S38A1_HUMAN TT1YE9Z SN System N amino acid transporter 1; System A amino acid transporter 1; Sodium-coupled neutral amino acid transporter 1; SNAT1; SAT1; NAT2; N-system amino acid transporter 2; Amino acid transporter A1; ATA1 TT1YE9Z GN SLC38A1 TT1YE9Z FC Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of glutamine and sodium ions with a stoichiometry of 1:1. May also transport small zwitterionic and aliphatic amino acids with a lower affinity. May supply glutamatergic and GABAergic neurons with glutamine which is required for the synthesis of the neurotransmitters glutamate and GABA. TT1YE9Z SQ MMHFKSGLELTELQNMTVPEDDNISNDSNDFTEVENGQINSKFISDRESRRSLTNSHLEKKKCDEYIPGTTSLGMSVFNLSNAIMGSGILGLAFALANTGILLFLVLLTSVTLLSIYSINLLLICSKETGCMVYEKLGEQVFGTTGKFVIFGATSLQNTGAMLSYLFIVKNELPSAIKFLMGKEETFSAWYVDGRVLVVIVTFGIILPLCLLKNLGYLGYTSGFSLSCMVFFLIVVIYKKFQIPCIVPELNSTISANSTNADTCTPKYVTFNSKTVYALPTIAFAFVCHPSVLPIYSELKDRSQKKMQMVSNISFFAMFVMYFLTAIFGYLTFYDNVQSDLLHKYQSKDDILILTVRLAVIVAVILTVPVLFFTVRSSLFELAKKTKFNLCRHTVVTCILLVVINLLVIFIPSMKDIFGVVGVTSANMLIFILPSSLYLKITDQDGDKGTQRIWAALFLGLGVLFSLVSIPLVIYDWACSSSSDEGH TT1YE9Z TT Literature-reported TTUSC27 ID TTUSC27 TTUSC27 TN Solute carrier family 38 member 2 (SLC38A2) TTUSC27 UP Q96QD8 TTUSC27 UC S38A2_HUMAN TTUSC27 SN System N amino acid transporter 2; System A transporter 1; System A amino acid transporter 2; Sodium-coupled neutral amino acid transporter 2; SNAT2; SAT2; Protein 40-9-1; KIAA1382; Amino acid transporter A2; ATA2 TTUSC27 GN SLC38A2 TTUSC27 FC Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier and in the supply of maternal nutrients to the fetus through the placenta. TTUSC27 SQ MKKAEMGRFSISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKKKYETEFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGYKAFGLVGKLAASGSITMQNIGAMSSYLFIVKYELPLVIQALTNIEDKTGLWYLNGNYLVLLVSLVVILPLSLFRNLGYLGYTSGLSLLCMVFFLIVVICKKFQVPCPVEAALIINETINTTLTQPTALVPALSHNVTENDSCRPHYFIFNSQTVYAVPILIFSFVCHPAVLPIYEELKDRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYEHVESELLHTYSSILGTDILLLIVRLAVLMAVTLTVPVVIFPIRSSVTHLLCASKDFSWWRHSLITVSILAFTNLLVIFVPTIRDIFGFIGASAASMLIFILPSAFYIKLVKKEPMKSVQKIGALFFLLSGVLVMTGSMALIVLDWVHNAPGGGH TTUSC27 TT Literature-reported TTMAVJQ ID TTMAVJQ TTMAVJQ TN Solute carrier family 38 member 3 (SLC38A3) TTMAVJQ UP Q99624 TTMAVJQ UC S38A3_HUMAN TTMAVJQ SN Sodium-coupled neutral amino acid transporter 3; SNAT3; SN1; Na(+)-coupled neutral amino acid transporter 3; N-system amino acid transporter 1; G17 TTMAVJQ GN SLC38A3 TTMAVJQ FC Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission. TTMAVJQ SQ MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFTDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKSSGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEEKTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPCPLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCHPEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVDPFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINLLVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFLLMTMSLSFIIIDWASGTSRHGGNH TTMAVJQ TT Literature-reported TTJE54U ID TTJE54U TTJE54U TN Solute carrier family 38 member 4 (SLC38A4) TTJE54U UP Q969I6 TTJE54U UC S38A4_HUMAN TTJE54U SN System N amino acid transporter 3; System A amino acid transporter 3; Sodium-coupled neutral amino acid transporter 4; SNAT4; Na(+)-coupled neutral amino acid transporter 4; NAT3; Amino acid transporter A3; ATA3 TTJE54U GN SLC38A4 TTJE54U FC Sodium-dependent amino acid transporter. Mediates electrogenic symport of neutral amino acids and sodium ions. Has a broad specificity, with a preference for Ala, followed by His, Cys, Asn, Ser, Gly, Val, Thr, Gln and Met. May mediate sodium-independent transport of cationic amino acids, such as Arg and Lys. Amino acid uptake is pH-dependent, with low transport activities at pH 6.5, intermediate at pH 7.0 and highest between pH 7.5 and 8.5. TTJE54U SQ MDPMELRNVNIEPDDESSSGESAPDSYIGIGNSEKAAMSSQFANEDTESQKFLTNGFLGKKKLADYADEHHPGTTSFGMSSFNLSNAIMGSGILGLSYAMANTGIILFIIMLLAVAILSLYSVHLLLKTAKEGGSLIYEKLGEKAFGWPGKIGAFVSITMQNIGAMSSYLFIIKYELPEVIRAFMGLEENTGEWYLNGNYLIIFVSVGIILPLSLLKNLGYLGYTSGFSLTCMVFFVSVVIYKKFQIPCPLPVLDHSVGNLSFNNTLPMHVVMLPNNSESSDVNFMMDYTHRNPAGLDENQAKGSLHDSGVEYEAHSDDKCEPKYFVFNSRTAYAIPILVFAFVCHPEVLPIYSELKDRSRRKMQTVSNISITGMLVMYLLAALFGYLTFYGEVEDELLHAYSKVYTLDIPLLMVRLAVLVAVTLTVPIVLFPIRTSVITLLFPKRPFSWIRHFLIAAVLIALNNVLVILVPTIKYIFGFIGASSATMLIFILPAVFYLKLVKKETFRSPQKVGALIFLVVGIFFMIGSMALIIIDWIYDPPNSKHH TTJE54U TT Literature-reported TTC8YPT ID TTC8YPT TTC8YPT TN Solute carrier family 38 member 5 (SLC38A5) TTC8YPT UP Q8WUX1 TTC8YPT UC S38A5_HUMAN TTC8YPT SN System N transporter 2; Sodium-coupled neutral amino acid transporter 5; SNAT5; SN2; PP7194; JM24 TTC8YPT GN SLC38A5 TTC8YPT FC Functions as a sodium-dependent amino acid transporter which countertransport protons. Mediates the saturable, pH-sensitive, and electrogenic cotransport of several neutral amino acids including glycine, asparagine, alanine, serine, glutamine and histidine with sodium. TTC8YPT SQ MELQDPKMNGALPSDAVGYRQEREGFLPSRGPAPGSKPVQFMDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMAHTGVIFFLALLLCIALLSSYSIHLLLTCAGIAGIRAYEQLGQRAFGPAGKVVVATVICLHNVGAMSSYLFIIKSELPLVIGTFLYMDPEGDWFLKGNLLIIIVSVLIILPLALMKHLGYLGYTSGLSLTCMLFFLVSVIYKKFQLGCAIGHNETAMESEALVGLPSQGLNSSCEAQMFTVDSQMSYTVPIMAFAFVCHPEVLPIYTELCRPSKRRMQAVANVSIGAMFCMYGLTATFGYLTFYSSVKAEMLHMYSQKDPLILCVRLAVLLAVTLTVPVVLFPIRRALQQLLFPGKAFSWPRHVAIALILLVLVNVLVICVPTIRDIFGVIGSTSAPSLIFILPSIFYLRIVPSEVEPFLSWPKIQALCFGVLGVLFMAVSLGFMFANWATGQSRMSGH TTC8YPT TT Literature-reported TT7FVLW ID TT7FVLW TT7FVLW TN Son of sevenless (SOS) TT7FVLW UP Q07889; Q07890 TT7FVLW UC SOS1_HUMAN; SOS2_HUMAN TT7FVLW SN Son of sevenless homolog; SOS TT7FVLW GN SOS1; SOS2 TT7FVLW FC Promotes the exchange of Ras-bound GDP by GTP. Probably by promoting Ras activation, regulates phosphorylation of MAP kinase MAPK3 in response to EGF. Catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. TT7FVLW SQ MQAQQLPYEFFSEENAPKWRGLLVPALKKVQGQVHPTLESNDDALQYVEELILQLLNMLCQAQPRSASDVEERVQKSFPHPIDKWAIADAQSAIEKRKRRNPLSLPVEKIHPLLKEVLGYKIDHQVSVYIVAVLEYISADILKLVGNYVRNIRHYEITKQDIKVAMCADKVLMDMFHQDVEDINILSLTDEEPSTSGEQTYYDLVKAFMAEIRQYIRELNLIIKVFREPFVSNSKLFSANDVENIFSRIVDIHELSVKLLGHIEDTVEMTDEGSPHPLVGSCFEDLAEELAFDPYESYARDILRPGFHDRFLSQLSKPGAALYLQSIGEGFKEAVQYVLPRLLLAPVYHCLHYFELLKQLEEKSEDQEDKECLKQAITALLNVQSGMEKICSKSLAKRRLSESACRFYSQQMKGKQLAIKKMNEIQKNIDGWEGKDIGQCCNEFIMEGTLTRVGAKHERHIFLFDGLMICCKSNHGQPRLPGASNAEYRLKEKFFMRKVQINDKDDTNEYKHAFEIILKDENSVIFSAKSAEEKNNWMAALISLQYRSTLERMLDVTMLQEEKEEQMRLPSADVYRFAEPDSEENIIFEENMQPKAGIPIIKAGTVIKLIERLTYHMYADPNFVRTFLTTYRSFCKPQELLSLIIERFEIPEPEPTEADRIAIENGDQPLSAELKRFRKEYIQPVQLRVLNVCRHWVEHHFYDFERDAYLLQRMEEFIGTVRGKAMKKWVESITKIIQRKKIARDNGPGHNITFQSSPPTVEWHISRPGHIETFDLLTLHPIEIARQLTLLESDLYRAVQPSELVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVETENLEERVAVVSRIIEILQVFQELNNFNGVLEVVSAMNSSPVYRLDHTFEQIPSRQKKILEEAHELSEDHYKKYLAKLRSINPPCVPFFGIYLTNILKTEEGNPEVLKRHGKELINFSKRRKVAEITGEIQQYQNQPYCLRVESDIKRFFENLNPMGNSMEKEFTDYLFNKSLEIEPRNPKPLPRFPKKYSYPLKSPGVRPSNPRPGTMRHPTPLQQEPRKISYSRIPESETESTASAPNSPRTPLTPPPASGASSTTDVCSVFDSDHSSPFHSSNDTVFIQVTLPHGPRSASVSSISLTKGTDEVPVPPPVPPRRRPESAPAESSPSKIMSKHLDSPPAIPPRQPTSKAYSPRYSISDRTSISDPPESPPLLPPREPVRTPDVFSSSPLHLQPPPLGKKSDHGNAFFPNSPSPFTPPPPQTPSPHGTRRHLPSPPLTQEVDLHSIAGPPVPPRQSTSQHIPKLPPKTYKREHTHPSMHRDGPPLLENAHSS TT7FVLW TT Literature-reported TTDAKTW ID TTDAKTW TTDAKTW TN Sperm-associated antigen 6 (SPAG6) TTDAKTW UP O75602 TTDAKTW UC SPAG6_HUMAN TTDAKTW SN Sperm flagellar protein; SPAG6; Repro-SA-1; Protein PF16 homolog TTDAKTW GN SPAG6 TTDAKTW FC Important for structural integrity of the central apparatus in the sperm tail andfor flagellar motility. TTDAKTW SQ MSQRQVLQVFEQYQKARTQFVQMVAELATRPQNIETLQNAGVMSLLRTLLLDVVPTIQQTAALALGRLANYNDDLAEAVVKCDILPQLVYSLAEQNRFYKKAAAFVLRAVGKHSPQLAQAIVDCGALDTLVICLEDFDPGVKEAAAWALRYIARHNAELSQAVVDAGAVPLLVLCIQEPEIALKRIAASALSDIAKHSPELAQTVVDAGAVAHLAQMILNPDAKLKHQILSALSQVSKHSVDLAEMVVEAEIFPVVLTCLKDKDEYVKKNASTLIREIAKHTPELSQLVVNAGGVAAVIDCIGSCKGNTRLPGIMMLGYVAAHSENLAMAVIISKGVPQLSVCLSEEPEDHIKAAAAWALGQIGRHTPEHARAVAVTNTLPVLLSLYMSTESSEDLQVKSKKAIKNILQKCTYLPALEPFLYDAPPNILKHVVGQFSKVLPHDSKARRLFVTSGGLKKVQEIKAEPGSLLQEYINSINSCYPEEIVRYYSPGYSDTLLQRVDSYQPLNN TTDAKTW TT Literature-reported TT0PSN6 ID TT0PSN6 TT0PSN6 TN Sprouty homolog 1 (SPRY-1) TT0PSN6 UP O43609 TT0PSN6 UC SPY1_HUMAN TT0PSN6 SN Spry-1; Protein sprouty homolog 1 TT0PSN6 GN SPRY1 TT0PSN6 FC May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis. TT0PSN6 SQ MDPQNQHGSGSSLVVIQQPSLDSRQRLDYEREIQPTAILSLDQIKAIRGSNEYTEGPSVVKRPAPRTAPRQEKHERTHEIIPINVNNNYEHRHTSHLGHAVLPSNARGPILSRSTSTGSAASSGSNSSASSEQGLLGRSPPTRPVPGHRSERAIRTQPKQLIVDDLKGSLKEDLTQHKFICEQCGKCKCGECTAPRTLPSCLACNRQCLCSAESMVEYGTCMCLVKGIFYHCSNDDEGDSYSDNPCSCSQSHCCSRYLCMGAMSLFLPCLLCYPPAKGCLKLCRRCYDWIHRPGCRCKNSNTVYCKLESCPSRGQGKPS TT0PSN6 TT Literature-reported TTL6U2P ID TTL6U2P TTL6U2P TN SREBP cleavage-activating protein (SCAP) TTL6U2P UP Q12770 TTL6U2P UC SCAP_HUMAN TTL6U2P SN SREBPcleavage-activating protein; SREBP-cleavage activating protein; SCAP TTL6U2P GN SCAP TTL6U2P FC Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP/SREBF complex from the ER upon low cholesterol. Formation of a ternary complex with INSIG at high sterol concentrations leads to masking of an ER-export signal in SCAP and retention of the complex in the ER. Low sterol concentrations trigger release of INSIG, a conformational change in the SSC domain of SCAP, unmasking of the ER export signal, recruitment into COPII-coated vesicles, transport to the Golgi complex, proteolytic cleavage of SREBF in the Golgi, release of the transcription factor fragmentof SREBF from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway. TTL6U2P SQ MTLTERLREKISRAFYNHGLLCASYPIPIILFTGFCILACCYPLLKLPLPGTGPVEFTTPVKDYSPPPVDSDRKQGEPTEQPEWYVGAPVAYVQQIFVKSSVFPWHKNLLAVDVFRSPLSRAFQLVEEIRNHVLRDSSGIRSLEELCLQVTDLLPGLRKLRNLLPEHGCLLLSPGNFWQNDWERFHADPDIIGTIHQHEPKTLQTSATLKDLLFGVPGKYSGVSLYTRKRMVSYTITLVFQHYHAKFLGSLRARLMLLHPSPNCSLRAESLVHVHFKEEIGVAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRMELADLNKRLPPEACLPSAKPVGQPTRYERQLAVRPSTPHTITLQPSSFRNLRLPKRLRVVYFLARTRLAQRLIMAGTVVWIGILVYTDPAGLRNYLAAQVTEQSPLGEGALAPMPVPSGMLPPSHPDPAFSIFPPDAPKLPENQTSPGESPERGGPAEVVHDSPVPEVTWGPEDEELWRKLSFRHWPTLFSYYNITLAKRYISLLPVIPVTLRLNPREALEGRHPQDGRSAWPPPGPIPAGHWEAGPKGPGGVQAHGDVTLYKVAALGLATGIVLVLLLLCLYRVLCPRNYGQLGGGPGRRRRGELPCDDYGYAPPETEIVPLVLRGHLMDIECLASDGMLLVSCCLAGHVCVWDAQTGDCLTRIPRPGRQRRDSGVGSGLEAQESWERLSDGGKAGPEEPGDSPPLRHRPRGPPPPSLFGDQPDLTCLIDTNFSAQPRSSQPTQPEPRHRAVCGRSRDSPGYDFSCLVQRVYQEEGLAAVCTPALRPPSPGPVLSQAPEDEGGSPEKGSPSLAWAPSAEGSIWSLELQGNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFLDKRIVAARLNGSLDFFSLETHTALSPLQFRGTPGRGSSPASPVYSSSDTVACHLTHTVPCAHQKPITALKAAAGRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTVYIDQTMVLASGGQDGAICLWDVLTGSRVSHVFAHRGDVTSLTCTTSCVISSGLDDLISIWDRSTGIKFYSIQQDLGCGASLGVISDNLLVTGGQGCVSFWDLNYGDLLQTVYLGKNSEAQPARQILVLDNAAIVCNFGSELSLVYVPSVLEKLD TTL6U2P TT Literature-reported TTZXB07 ID TTZXB07 TTZXB07 TN SSX2-interacting protein (SSX2IP) TTZXB07 UP Q9Y2D8 TTZXB07 UC ADIP_HUMAN TTZXB07 SN KIAA0923; Afadin- and alpha-actinin-binding protein; Afadin DIL domain-interacting protein; ADIP TTZXB07 GN SSX2IP TTZXB07 FC May connect the nectin-afadin and E-cadherin-catenin system through alpha-actinin and may be involved in organization of the actin cytoskeleton at AJs through afadin and alpha-actinin. Involved in cell movement: localizes at the leading edge of moving cells in response to PDGF and is required for the formation of the leading edge and the promotion of cell movement, possibly via activation of Rac signaling. Acts as a centrosome maturation factor, probably by maintaining the integrity of the pericentriolar material and proper microtubule nucleation at mitotic spindle poles. The function seems to implicate at least in part WRAP73; the SSX2IP:WRAP73 complex is proposed to act as regulator of spindle anchoring at the mitotic centrosome. Involved in ciliogenesis. It is required for targeted recruitment of the BBSome, CEP290, RAB8, and SSTR3 to the cilia. Belongs to an adhesion system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). TTZXB07 SQ MGDWMTVTDPGLSSESKTISQYTSETKMSPSSLYSQQVLCSSIPLSKNVHSFFSAFCTEDNIEQSISYLDQELTTFGFPSLYEESKGKETKRELNIVAVLNCMNELLVLQRKNLLAQENVETQNLKLGSDMDHLQSCYSKLKEQLETSRREMIGLQERDRQLQCKNRNLHQLLKNEKDEVQKLQNIIASRATQYNHDMKRKEREYNKLKERLHQLVMNKKDKKIAMDILNYVGRADGKRGSWRTGKTEARNEDEMYKILLNDYEYRQKQILMENAELKKVLQQMKKEMISLLSPQKKKPRERVDDSTGTVISDVEEDAGELSRESMWDLSCETVREQLTNSIRKQWRILKSHVEKLDNQVSKVHLEGFNDEDVISRQDHEQETEKLELEIQQCKEMIKTQQQLLQQQLATAYDDDTTSLLRDCYLLEEKERLKEEWSLFKEQKKNFERERRSFTEAAIRLGLERKAFEEERASWLKQQFLNMTTFDHQNSENVKLFSAFSGSSDWDNLIVHSRQPQKKPHSVSNGSPVCMSKLTKSLPASPSTSDFCQTRSCISEHSSINVLNITAEEIKPNQVGGECTNQKWSVASRPGSQEGCYSGCSLSYTNSHVEKDDLP TTZXB07 TT Literature-reported TTJFEOC ID TTJFEOC TTJFEOC TN Stabilin-1 (STAB1) TTJFEOC UP Q9NY15 TTJFEOC UC STAB1_HUMAN TTJFEOC SN STAB1; MS-1 antigen; Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 1; FEEL-1 TTJFEOC GN STAB1 TTJFEOC FC Acts as a scavenger receptor for acetylated low density lipoprotein. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. When inhibited in endothelial tube formation assays, there is a marked decreasein cell-cell interactions, suggesting a role in angiogenesis. Involved in the delivery of newly synthesized CHID1/SI-CLP from the biosynthetic compartment to the endosomal/lysosomal system. TTJFEOC SQ MAGPRGLLPLCLLAFCLAGFSFVRGQVLFKGCDVKTTFVTHVPCTSCAAIKKQTCPSGWLRELPDQITQDCRYEVQLGGSMVSMSGCRRKCRKQVVQKACCPGYWGSRCHECPGGAETPCNGHGTCLDGMDRNGTCVCQENFRGSACQECQDPNRFGPDCQSVCSCVHGVCNHGPRGDGSCLCFAGYTGPHCDQELPVCQELRCPQNTQCSAEAPSCRCLPGYTQQGSECRAPNPCWPSPCSLLAQCSVSPKGQAQCHCPENYHGDGMVCLPKDPCTDNLGGCPSNSTLCVYQKPGQAFCTCRPGLVSINSNASAGCFAFCSPFSCDRSATCQVTADGKTSCVCRESEVGDGRACYGHLLHEVQKATQTGRVFLQLRVAVAMMDQGCREILTTAGPFTVLVPSVSSFSSRTMNASLAQQLCRQHIIAGQHILEDTRTQQTRRWWTLAGQEITVTFNQFTKYSYKYKDQPQQTFNIYKANNIAANGVFHVVTGLRWQAPSGTPGDPKRTIGQILASTEAFSRFETILENCGLPSILDGPGPFTVFAPSNEAVDSLRDGRLIYLFTAGLSKLQELVRYHIYNHGQLTVEKLISKGRILTMANQVLAVNISEEGRILLGPEGVPLQRVDVMAANGVIHMLDGILLPPTILPILPKHCSEEQHKIVAGSCVDCQALNTSTCPPNSVKLDIFPKECVYIHDPTGLNVLKKGCASYCNQTIMEQGCCKGFFGPDCTQCPGGFSNPCYGKGNCSDGIQGNGACLCFPDYKGIACHICSNPNKHGEQCQEDCGCVHGLCDNRPGSGGVCQQGTCAPGFSGRFCNESMGDCGPTGLAQHCHLHARCVSQEGVARCRCLDGFEGDGFSCTPSNPCSHPDRGGCSENAECVPGSLGTHHCTCHKGWSGDGRVCVAIDECELDMRGGCHTDALCSYVGPGQSRCTCKLGFAGDGYQCSPIDPCRAGNGGCHGLATCRAVGGGQRVCTCPPGFGGDGFSCYGDIFRELEANAHFSIFYQWLKSAGITLPADRRVTALVPSEAAVRQLSPEDRAFWLQPRTLPNLVRAHFLQGALFEEELARLGGQEVATLNPTTRWEIRNISGRVWVQNASVDVADLLATNGVLHILSQVLLPPRGDVPGGQGLLQQLDLVPAFSLFRELLQHHGLVPQIEAATAYTIFVPTNRSLEAQGNSSHLDADTVRHHVVLGEALSMETLRKGGHRNSLLGPAHWIVFYNHSGQPEVNHVPLEGPMLEAPGRSLIGLSGVLTVGSSRCLHSHAEALREKCVNCTRRFRCTQGFQLQDTPRKSCVYRSGFSFSRGCSYTCAKKIQVPDCCPGFFGTLCEPCPGGLGGVCSGHGQCQDRFLGSGECHCHEGFHGTACEVCELGRYGPNCTGVCDCAHGLCQEGLQGDGSCVCNVGWQGLRCDQKITSPQCPRKCDPNANCVQDSAGASTCACAAGYSGNGIFCSEVDPCAHGHGGCSPHANCTKVAPGQRTCTCQDGYMGDGELCQEINSCLIHHGGCHIHAECIPTGPQQVSCSCREGYSGDGIRTCELLDPCSKNNGGCSPYATCKSTGDGQRTCTCDTAHTVGDGLTCRARVGLELLRDKHASFFSLRLLEYKELKGDGPFTIFVPHADLMSNLSQDELARIRAHRQLVFRYHVVGCRRLRSEDLLEQGYATALSGHPLRFSEREGSIYLNDFARVVSSDHEAVNGILHFIDRVLLPPEALHWEPDDAPIPRRNVTAAAQGFGYKIFSGLLKVAGLLPLLREASHRPFTMLWPTDAAFRALPPDRQAWLYHEDHRDKLAAILRGHMIRNVEALASDLPNLGPLRTMHGTPISFSCSRTRAGELMVGEDDARIVQRHLPFEGGLAYGIDQLLEPPGLGARCDHFETRPLRLNTCSICGLEPPCPEGSQEQGSPEACWRFYPKFWTSPPLHSLGLRSVWVHPSLWGRPQGLGRGCHRNCVTTTWKPSCCPGHYGSECQACPGGPSSPCSDRGVCMDGMSGSGQCLCRSGFAGTACELCAPGAFGPHCQACRCTVHGRCDEGLGGSGSCFCDEGWTGPRCEVQLELQPVCTPPCAPEAVCRAGNSCECSLGYEGDGRVCTVADLCQDGHGGCSEHANCSQVGTMVTCTCLPDYEGDGWSCRARNPCTDGHRGGCSEHANCLSTGLNTRRCECHAGYVGDGLQCLEESEPPVDRCLGQPPPCHSDAMCTDLHFQEKRAGVFHLQATSGPYGLNFSEAEAACEAQGAVLASFPQLSAAQQLGFHLCLMGWLANGSTAHPVVFPVADCGNGRVGIVSLGARKNLSERWDAYCFRVQDVACRCRNGFVGDGISTCNGKLLDVLAATANFSTFYGMLLGYANATQRGLDFLDFLDDELTYKTLFVPVNEGFVDNMTLSGPDLELHASNATLLSANASQGKLLPAHSGLSLIISDAGPDNSSWAPVAPGTVVVSRIIVWDIMAFNGIIHALASPLLAPPQPQAVLAPEAPPVAAGVGAVLAAGALLGLVAGALYLRARGKPMGFGFSAFQAEDDADDDFSPWQEGTNPTLVSVPNPVFGSDTFCEPFDDSLLEEDFPDTQRILTVK TTJFEOC TT Literature-reported TT4EFTR ID TT4EFTR TT4EFTR TN Stanniocalcin-2 (STC2) TT4EFTR UP O76061 TT4EFTR UC STC2_HUMAN TT4EFTR SN Stanniocalcin-related protein; STCRP; STC-related protein; STC-2 TT4EFTR GN STC2 TT4EFTR FC Has an anti-hypocalcemic action on calcium and phosphate homeostasis. TT4EFTR SQ MCAERLGQFMTLALVLATFDPARGTDATNPPEGPQDRSSQQKGRLSLQNTAEIQHCLVNAGDVGCGVFECFENNSCEIRGLHGICMTFLHNAGKFDAQGKSFIKDALKCKAHALRHRFGCISRKCPAIREMVSQLQRECYLKHDLCAAAQENTRVIVEMIHFKDLLLHEPYVDLVNLLLTCGEEVKEAITHSVQVQCEQNWGSLCSILSFCTSAIQKPPTAPPERQPQVDRTKLSRAHHGEAGHHLPEPSSRETGRGAKGERGSKSHPNAHARGRVGGLGAQGPSGSSEWEDEQSEYSDIRR TT4EFTR TT Literature-reported TT4EFTR FM Stanniocalcin family TTF3GOT ID TTF3GOT TTF3GOT TN Staphylococcus Pmt ABC transporter (Stap-coc Pmt) TTF3GOT UP A0A2X2N8M2 TTF3GOT UC A0A2X2N8M2_STAAU TTF3GOT SN Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase TTF3GOT GN Stap-coc Pmt TTF3GOT FC A general export system for membrane-damaging peptides, secreting host-derived AMPs in addition to the bacterial PSM cytotoxins. Defends the bacteria from killing by important human AMPs and elimination by human neutrophils. TTF3GOT SQ MTAPVPLLPAPEERSTRYGQLRDRLLRDPDWGRAIRWLAPLVITAIAALLRLINVAHPHQLAFDETYYVKDAWSLWTLGYEGTWGENANDAFITLQQLPLSEQGAFIVHPPLGKWLIALGMAIGGPDNSAGWRLATALLGTASVLLVYLIARRLSGSVVVASVAGTLLAIDGLSIVMSRIALLDGILTFFVLLGVLFVIIDRQRTIPVLERRDPDKPDPFWGPVLWRRPWLIAAGTALGAASAVKWSGLYVLAGFGLYVVVTDALARRRAGVVLWPTGAAFRQGPVSFVLLVFPALAVYLISWTGWLVTAGGYDRQSDPNPLIALWKYHESMLGFHVGLTRGHPYASPAWEWPLLLRPTAVWVDSDPTGCGTDHCIGVISAIPNPLIWYAGVAAAIYLLYRLVRGWITRRPVGPELSIPLVGLAVTYVPWLMFPDRTIFQFYTVVMMPFLVIALAMTLRIIAGTREDPLHRRQSGERTVMIFLAFVVLVSAFFLPLWTGMSVPYEFWLLHNWLPGWV TTF3GOT TT Literature-reported TT369WU ID TT369WU TT369WU TN Stathmin-1 (STMN1) TT369WU UP P16949 TT369WU UC STMN1_HUMAN TT369WU SN pp19; pp17; Stathmin; Protein Pr22; Prosolin; Phosphoprotein p19; Oncoprotein 18; OP18; Metablastin; Leukemia-associated phosphoprotein p18; LAP18; C1orf215 TT369WU GN STMN1 TT369WU FC Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate fear (By similarity). TT369WU SQ MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHIEEVRKNKESKDPADETEAD TT369WU TT Literature-reported TT369WU FM Stathmin family TTOI329 ID TTOI329 TTOI329 TN Stomatin-like protein 2 (STOML2) TTOI329 UP Q9UJZ1 TTOI329 UC STML2_HUMAN TTOI329 SN Stomatin-like protein 2, mitochondrial; SLP2; SLP-2; Paratarg-7; Paraprotein target 7; HSPC108; EPB72-like protein 2 TTOI329 GN STOML2 TTOI329 FC Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation. Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. TTOI329 SQ MLARAARGTGALLLRGSLLASGRAPRRASSGLPRNTVVLFVPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEASAVLAKAKAKAEAIRILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTKAPVPGTPDSLSSGSSRDVQGTDASLDEELDRVKMS TTOI329 TT Literature-reported TTDX1QC ID TTDX1QC TTDX1QC TN Streptococcus Exotoxin type G (Stre-coc speG) TTDX1QC UP Q9X5C7 TTDX1QC UC SPEG_STRP1 TTDX1QC SN SPE G; Pyrogenic exotoxin G; Exotoxin type G TTDX1QC GN Stre-coc speG TTDX1QC FC Mitogenic for human peripheral blood lymphocytes. TTDX1QC SQ MKTNILTIIILSCVFSYGSQLAYADENLKDLKRSLRFAYNITPCDYENVEIAFVTTNSIHINTKQKRSECILYVDSIVSLGITDQFIKGDKVDVFGLPYNFSPPYVDNIYGGIVKHSNQGNKSLQFVGILNQDGKETYLPSEAVRIKKKQFTLQEFDFKIRKFLMEKYNIYDSESRYTSGSLFLATKDSKHYEVDLFNKDDKLLSRDSFFKRYKDNKIFNSEEISHFDIYLKTH TTDX1QC TT Literature-reported TT43K1Z ID TT43K1Z TT43K1Z TN Streptococcus Metal-transporter protein PsaA (Stre-coc psaA) TT43K1Z UP P42363 TT43K1Z UC MTSA_STREE TT43K1Z SN Pneumococcal surface adhesin A TT43K1Z GN Stre-coc psaA TT43K1Z FC Part of an ATP-driven transport system for manganese. Also act as an adhesin which is involved on adherence to extracellular matrix. It is an important factor in pathogenesis and infection. TT43K1Z SQ MKKIASVLALFVALLFGLLACSKGTSSKSSSDKLKVVTTNSILADITKNIAGDKIELHSIVPVGQDPHEYEPLPEDVKKTSQADLIFYNGINLETGGNAWFTKLVKNANKVENKDYFAASDGVEVIYLEGQNQAGKEDPHAWLNLENGIIYAKNIAKQLIAKDPKNKDFYEKNLAAYTEKLSKLDQEAKQAFNNIPAEKKMIVTSEGCFKYFSKAYGVPSAYIWEINTEVEGTPEQIKTLLEKLRQTKVPSLFVESSVDERPMKTVSKDSNIPIFAKIFTDSIAKEGEEGDSYYSMMKWNLEKIAEGLNK TT43K1Z TT Literature-reported TTVARO5 ID TTVARO5 TTVARO5 TN Streptococcus Triosephosphate dehydrogenase (Stre gapN) TTVARO5 UP Q3C1A6 TTVARO5 UC GAPN_STREI TTVARO5 SN Triosephosphate dehydrogenase; Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase; NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]; GAPN TTVARO5 GN Stre gapN TTVARO5 FC Catalyzes the irreversible NADP-dependent oxidation of glyceraldehyde-3-phosphate to 3-phosphoglycerate. Is not able to use NAD instead of NADP. May play an important role in NADPH production in S.equinus. TTVARO5 SQ MTKQYKNYVNGEWKLSKEEIKIYAPATGEELGSVPAMSQEEVDYVYASAKAAQKAWRALSYVERAEYLHKAADILMRDAEKIGAVLSKEIAKGYKSAVGEVIRTAEIINYAAEEGVRLEGEVLEGGSFDPASKKKIAIVRREPVGLVLAISPFNYPINLAGSKIAPALISGNVVALKPPTQGSISGLLLAEAFAEAGLPAGVFNTITGRGSVIGDYIVEHEAVNYINFTGSTPVGEHIGHLAGMRPIMLELGGKDSAIILEDADLDLAAKNIVAGAYGYSGQRCTAVKRVLVMDSIADKLVEKVSALVNNLTVGMPEDNADITPLIDTKAADYVEGLIKDAQEKGAKEVISFKREGNLISPVLFDNVTTDMRLAWEEPFGPVLPFIRVNSVEEAIEISNKSEYGLQASVFTNNFPLAFKIAEQLEVGTVHINNKTQRGTDNFPFLGAKKSGAGVQGVKYSIEAMTTVKSTVFDIAK TTVARO5 TT Literature-reported TTXJKFI ID TTXJKFI TTXJKFI TN Streptomyces Ribosome recycling factor (Stre frr) TTXJKFI UP O86770 TTXJKFI UC RRF_STRCO TTXJKFI SN Ribosome-releasing factor; Ribosome-recycling factor; RRF TTXJKFI GN Stre frr TTXJKFI FC Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another. TTXJKFI SQ MIEETLLEAEEKMEKAVVVAKEDFAAIRTGRAHPAMFNKIVAEYYGAPTPINQLASFSVPEPRMAVVTPFDKTALRNIEQAIRDSDLGVNPSNDGNIIRVTFPELTEERRREYIKVAKAKGEDAKVSIRSVRRKAKDSIDKMVKDGEVGEDEGRRAEKELDDTTAKYVAQVDELLKHKEAELLEV TTXJKFI TT Literature-reported TTMRQY1 ID TTMRQY1 TTMRQY1 TN Striatum-specific G-protein coupled receptor (GPR88) TTMRQY1 UP Q9GZN0 TTMRQY1 UC GPR88_HUMAN TTMRQY1 SN STRG; Probable G-protein coupled receptor 88 TTMRQY1 GN GPR88 TTMRQY1 FC Probable G-protein coupled receptor implicated in a large repertoire of behavioral responses that engage motor activities, spatial learning, and emotional processing. May play a role in the regulation of cognitive and motor function. TTMRQY1 SQ MTNSSSTSTSSTTGGSLLLLCEEEESWAGRRIPVSLLYSGLAIGGTLANGMVIYLVSSFRKLQTTSNAFIVNGCAADLSVCALWMPQEAVLGLLPTGSAEPPADWDGAGGSYRLLRGGLLGLGLTVSLLSHCLVALNRYLLITRAPATYQALYQRRHTAGMLALSWALALGLVLLLPPWAPRPGAAPPRVHYPALLAAAALLAQTALLLHCYLGIVRRVRVSVKRVSVLNFHLLHQLPGCAAAAAAFPGAQHAPGPGGAAHPAQAQPLPPALHPRRAQRRLSGLSVLLLCCVFLLATQPLVWVSLASGFSLPVPWGVQAASWLLCCALSALNPLLYTWRNEEFRRSVRSVLPGVGDAAAAAVAATAVPAVSQAQLGTRAAGQHW TTMRQY1 TT Literature-reported TTVH9W8 ID TTVH9W8 TTVH9W8 TN Succinate dehydrogenase (SDHD) TTVH9W8 UP O14521 TTVH9W8 UC DHSD_HUMAN TTVH9W8 SN Succinate-ubiquinone reductase membrane anchor subunit; Succinate-ubiquinone oxidoreductase cytochrome b small subunit; Succinate dehydrogenase complex subunit D; Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial; SDH4; QPs3; CybS; CII-4 TTVH9W8 GN SDHD TTVH9W8 FC Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). TTVH9W8 SQ MAVLWRLSAVCGALGGRALLLRTPVVRPAHISAFLQDRPIPEWCGVQHIHLSPSHHSGSKAASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGLGQVVTDYVHGDALQKAAKAGLLALSALTFAGLCYFNYHDVGICKAVAMLWKL TTVH9W8 TT Literature-reported TT4FX9Y ID TT4FX9Y TT4FX9Y TN Succinate receptor (SUCNR1) TT4FX9Y UP Q9BXA5 TT4FX9Y UC SUCR1_HUMAN TT4FX9Y SN Succinate receptor 1; P2Y purinoceptor 1-like; GPR91; G-protein coupled receptor 91 TT4FX9Y GN SUCNR1 TT4FX9Y FC Receptor for succinate. TT4FX9Y SQ MLGIMAWNATCKNWLAAEAALEKYYLSIFYGIEFVVGVLGNTIVVYGYIFSLKNWNSSNIYLFNLSVSDLAFLCTLPMLIRSYANGNWIYGDVLCISNRYVLHANLYTSILFLTFISIDRYLIIKYPFREHLLQKKEFAILISLAIWVLVTLELLPILPLINPVITDNGTTCNDFASSGDPNYNLIYSMCLTLLGFLIPLFVMCFFYYKIALFLKQRNRQVATALPLEKPLNLVIMAVVIFSVLFTPYHVMRNVRIASRLGSWKQYQCTQVVINSFYIVTRPLAFLNSVINPVFYFLLGDHFRDMLMNQLRHNFKSLTSFSRWAHELLLSFREK TT4FX9Y TT Literature-reported TT8COJM ID TT8COJM TT8COJM TN Suppressor of cytokine signaling 1 (SOCS1) TT8COJM UP O15524 TT8COJM UC SOCS1_HUMAN TT8COJM SN Tec-interacting protein 3; TIP3; TIP-3; STAT-induced STAT inhibitor 1; STAT induced STAT inhibitor 1; SSI1; SSI-1; SOCS-1; JAK-binding protein; JAB TT8COJM GN SOCS1 TT8COJM FC SOCS1 is involved in negative regulation of cytokines that signal through the JAK/STAT3 pathway. Through binding to JAKs, inhibits their kinase activity. In vitro, also suppresses Tec protein-tyrosine activity. Appears to be a major regulator of signaling by interleukin 6 (IL6) and leukemia inhibitory factor (LIF). Regulates interferon-gamma mediated sensory neuron survival. Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recognize JAK2. SOCS1 appears to be a negative regulator in IGF1R signaling pathway. SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. TT8COJM SQ MVAHNQVAADNAVSTAAEPRRRPEPSSSSSSSPAAPARPRPCPAVPAPAPGDTHFRTFRSHADYRRITRASALLDACGFYWGPLSVHGAHERLRAEPVGTFLVRDSRQRNCFFALSVKMASGPTSIRVHFQAGRFHLDGSRESFDCLFELLEHYVAAPRRMLGAPLRQRRVRPLQELCRQRIVATVGRENLARIPLNPVLRDYLSSFPFQI TT8COJM TT Literature-reported TTI0ME6 ID TTI0ME6 TTI0ME6 TN Suppressor of cytokine signaling 3 (SOCS3) TTI0ME6 UP O14543 TTI0ME6 UC SOCS3_HUMAN TTI0ME6 SN STAT-induced STAT inhibitor 3; STAT induced STAT inhibitor 3; SSI3; SSI-3; SOCS-3; Cytokine-inducible SH2 protein 3; CIS3; CIS-3 TTI0ME6 GN SOCS3 TTI0ME6 FC SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells. Regulates IL-6 signaling in vivo. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recognize IL6ST. SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. TTI0ME6 SQ MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGAPSFPSPPTEPSSEVPEQPSAQPLPGSPPRRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL TTI0ME6 TT Literature-reported TTRZBW7 ID TTRZBW7 TTRZBW7 TN Suppressor of tumorigenicity 15 protein (ST15) TTRZBW7 UP O95980 TTRZBW7 UC RECK_HUMAN TTRZBW7 SN hRECK; Reversion-inducing cysteine-rich protein with Kazal motifs TTRZBW7 GN RECK TTRZBW7 FC Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation. Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7. ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor: negatively regulates matrix metalloproteinase-9 (MMP9) by suppressing MMP9 secretion and by direct inhibition of its enzymatic activity. Also inhibits metalloproteinase activity of MMP2 and MMP14 (MT1-MMP). Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B). TTRZBW7 SQ MATVRASLRGALLLLLAVAGVAEVAGGLAPGSAGALCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLQRAPDYCPETMVEIWNCMNSSLPGVFKKSDGWVGLGCCELAIALECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREYCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQEFDRFCEYNPVEVSMLTCLADVREPCQLGCRNLTYCTNFNNRPTELFRSCNAQSDQGAMNDMKLWEKGSIKMPFINIPVLDIKKCQPEMWKAIACSLQIKPCHSKSRGSIICKSDCVEILKKCGDQNKFPEDHTAESICELLSPTDDLKNCIPLDTYLRPSTLGNIVEEVTHPCNPNPCPANELCEVNRKGCPSGDPCLPYFCVQGCKLGEASDFIVRQGTLIQVPSSAGEVGCYKICSCGQSGLLENCMEMHCIDLQKSCIVGGKRKSHGTSFSIDCNVCSCFAGNLVCSTRLCLSEHSSEDDRRTFTGLPCNCADQFVPVCGQNGRTYPSACIARCVGLQDHQFEFGSCMSKDPCNPNPCQKNQRCIPKPQVCLTTFDKFGCSQYECVPRQLACDQVQDPVCDTDHMEHNNLCTLYQRGKSLSYKGPCQPFCRATEPVCGHNGETYSSVCAAYSDRVAVDYYGDCQAVGVLSEHSSVAECASVKCPSLLAAGCKPIIPPGACCPLCAGMLRVLFDKEKLDTIAKVTNKKPITVLEILQKIRMHVSVPQCDVFGYFSIESEIVILIIPVDHYPKALQIEACNKEAEKIESLINSDSPTLASHVPLSALIISQVQVSSSVPSAGVRARPSCHSLLLPLSLGLALHLLWTYN TTRZBW7 TT Literature-reported TTDN2JG ID TTDN2JG TTDN2JG TN Synapsin (SYN) TTDN2JG UP P17600; Q92777; O14994 TTDN2JG UC SYN1_HUMAN; SYN2_HUMAN; SYN3_HUMAN TTDN2JG SN Synapsin TTDN2JG GN SYN1; SYN2; SYN3 TTDN2JG FC Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level. May be involved in the regulation of noradrenaline secretion, neurotransmitter release and synaptogenesis. TTDN2JG SQ MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPGAHSPGATPGPGTATAERSSGVAPAASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAASRVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMAQALPRQRQRDASPGRGSHGQTPSPGALPLGRQTSQQPAGPPAQQRPPPQGGPPQPGPGPQRQGPPLQQRPPPQGQQHLSGLGPPAGSPLPQRLPSPTSAPQQPASQAAPPTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATRQTSVSGPAPPKASGAPPGGQQRQGPPQKPPGPAGPTRQASQAGPVPRTGPPTTQQPRPSGPGPAGRPKPQLAQKPSQDVPPPATAAAGGPPHPQLNKSQSLTNAFNLPEPAPPRPSLSQDEVKAETIRSLRKSFASLFSD TTDN2JG TT Literature-reported TTNF9PH ID TTNF9PH TTNF9PH TN T-box transcription factor TBX21 (TBX21) TTNF9PH UP Q9UL17 TTNF9PH UC TBX21_HUMAN TTNF9PH SN Transcription factor TBLYM; TBX21; T-cell-specific T-box transcription factor T-bet; T-box protein 21; T-bet TTNF9PH GN TBX21 TTNF9PH FC Transcription factor that controls the expression of the TH1 cytokine, interferon-gamma. Initiates TH1 lineage development from naive TH precursor cells both by activating TH1 genetic programs and by repressing the opposing TH2 programs. TTNF9PH SQ MGIVEPGCGDMLTGTEPMPGSDEGRAPGADPQHRYFYPEPGAQDADERRGGGSLGSPYPGGALVPAPPSRFLGAYAYPPRPQAAGFPGAGESFPPPADAEGYQPGEGYAAPDPRAGLYPGPREDYALPAGLEVSGKLRVALNNHLLWSKFNQHQTEMIITKQGRRMFPFLSFTVAGLEPTSHYRMFVDVVLVDQHHWRYQSGKWVQCGKAEGSMPGNRLYVHPDSPNTGAHWMRQEVSFGKLKLTNNKGASNNVTQMIVLQSLHKYQPRLHIVEVNDGEPEAACNASNTHIFTFQETQFIAVTAYQNAEITQLKIDNNPFAKGFRENFESMYTSVDTSIPSPPGPNCQFLGGDHYSPLLPNQYPVPSRFYPDLPGQAKDVVPQAYWLGAPRDHSYEAEFRAVSMKPAFLPSAPGPTMSYYRGQEVLAPGAGWPVAPQYPPKMGPASWFRPMRTLPMEPGPGGSEGRGPEDQGPPLVWTEIAPIRPESSDSGLGEGDSKRRRVSPYPSSGDSSSPAGAPSPFDKEAEGQFYNYFPN TTNF9PH TT Literature-reported TTVRN05 ID TTVRN05 TTVRN05 TN T-cell immune regulator 1 (TCIRG1) TTVRN05 UP Q13488 TTVRN05 UC VPP3_HUMAN TTVRN05 SN Vacuolar proton translocating ATPase 116 kDa subunit a isoform 3; V-ATPase 116 kDa isoform a3; TIRC7; TCIRG1; T-cell immune response cDNA7 protein; Osteoclastic proton pump 116 kDa subunit; OC116; OC-116 kDa TTVRN05 GN TCIRG1 TTVRN05 FC Part of the proton channel of V-ATPases. Seems to be directly involved in T-cell activation. TTVRN05 SQ MGSMFRSEEVALVQLFLPTAAAYTCVSRLGELGLVEFRDLNASVSAFQRRFVVDVRRCEELEKTFTFLQEEVRRAGLVLPPPKGRLPAPPPRDLLRIQEETERLAQELRDVRGNQQALRAQLHQLQLHAAVLRQGHEPQLAAAHTDGASERTPLLQAPGGPHQDLRVNFVAGAVEPHKAPALERLLWRACRGFLIASFRELEQPLEHPVTGEPATWMTFLISYWGEQIGQKIRKITDCFHCHVFPFLQQEEARLGALQQLQQQSQELQEVLGETERFLSQVLGRVLQLLPPGQVQVHKMKAVYLALNQCSVSTTHKCLIAEAWCSVRDLPALQEALRDSSMEEGVSAVAHRIPCRDMPPTLIRTNRFTASFQGIVDAYGVGRYQEVNPAPYTIITFPFLFAVMFGDVGHGLLMFLFALAMVLAENRPAVKAAQNEIWQTFFRGRYLLLLMGLFSIYTGFIYNECFSRATSIFPSGWSVAAMANQSGWSDAFLAQHTMLTLDPNVTGVFLGPYPFGIDPIWSLAANHLSFLNSFKMKMSVILGVVHMAFGVVLGVFNHVHFGQRHRLLLETLPELTFLLGLFGYLVFLVIYKWLCVWAARAASAPSILIHFINMFLFSHSPSNRLLYPRQEVVQATLVVLALAMVPILLLGTPLHLLHRHRRRLRRRPADRQEENKAGLLDLPDASVNGWSSDEEKAGGLDDEEEAELVPSEVLMHQAIHTIEFCLGCVSNTASYLRLWALSLAHAQLSEVLWAMVMRIGLGLGREVGVAAVVLVPIFAAFAVMTVAILLVMEGLSAFLHALRLHWVEFQNKFYSGTGYKLSPFTFAATDD TTVRN05 TT Literature-reported TTF23RE ID TTF23RE TTF23RE TN Testican-1 (SPOCK1) TTF23RE UP Q08629 TTF23RE UC TICN1_HUMAN TTF23RE SN SPOCK1; Protein SPOCK TTF23RE GN SPOCK1 TTF23RE FC May play a role in cell-cell and cell-matrix interactions. May contribute to various neuronal mechanisms in the central nervous system. TTF23RE SQ MPAIAVLAAAAAAWCFLQVESRHLDALAGGAGPNHGNFLDNDQWLSTVSQYDRDKYWNRFRDDDYFRNWNPNKPFDQALDPSKDPCLKVKCSPHKVCVTQDYQTALCVSRKHLLPRQKKGNVAQKHWVGPSNLVKCKPCPVAQSAMVCGSDGHSYTSKCKLEFHACSTGKSLATLCDGPCPCLPEPEPPKHKAERSACTDKELRNLASRLKDWFGALHEDANRVIKPTSSNTAQGRFDTSILPICKDSLGWMFNKLDMNYDLLLDPSEINAIYLDKYEPCIKPLFNSCDSFKDGKLSNNEWCYCFQKPGGLPCQNEMNRIQKLSKGKSLLGAFIPRCNEEGYYKATQCHGSTGQCWCVDKYGNELAGSRKQGAVSCEEEQETSGDFGSGGSVVLLDDLEYERELGPKDKEGKLRVHTRAVTEDDEDEDDDKEDEVGYIW TTF23RE TT Literature-reported TT7QSMG ID TT7QSMG TT7QSMG TN Testis-enhanced gene transcript protein (TMBIM6) TT7QSMG UP P55061 TT7QSMG UC BI1_HUMAN TT7QSMG SN Testis enhanced gene transcript; TMBIM6; BI-1 TT7QSMG GN TMBIM6 TT7QSMG FC Suppressor of apoptosis. Modulates unfolded protein response signaling. Modulate ER calcium homeostasis by acting as a calcium-leak channel. TT7QSMG SQ MNIFDRKINFDALLKFSHITPSTQQHLKKVYASFALCMFVAAAGAYVHMVTHFIQAGLLSALGSLILMIWLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALEFCIAVNPSILPTAFMGTAMIFTCFTLSALYARRRSYLFLGGILMSALSLLLLSSLGNVFFGSIWLFQANLYVGLVVMCGFVLFDTQLIIEKAEHGDQDYIWHCIDLFLDFITVFRKLMMILAMNEKDKKKEKK TT7QSMG TT Literature-reported TTHSVK0 ID TTHSVK0 TTHSVK0 TN Thioredoxin-like protein 2b (NME9) TTHSVK0 UP Q86XW9 TTHSVK0 UC TXND6_HUMAN TTHSVK0 SN Txl-2; Thioredoxin-like protein 2; Thioredoxin domain-containing protein 6; NME9 TTHSVK0 GN NME9 TTHSVK0 FC May be a regulator of microtubule physiology. TTHSVK0 SQ MGSRKKEIALQVNISTQELWEEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLHFALAEADRLDVLEKYRGKCEPTFLFYAGGELVAVVRGANAPLLQKTILDQLEAEKKVLAEGRERKVIKDEALSDEDECVSHGKNNGEDEDMVSSERTCTLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRTEGFEDVVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFPSLKFSDKDTEAPQGGEAEATAGPTEALCFPEDVD TTHSVK0 TT Literature-reported TTZCL1U ID TTZCL1U TTZCL1U TN T-lymphocyte surface antigen Ly-9 (LY9) TTZCL1U UP Q9HBG7 TTZCL1U UC LY9_HUMAN TTZCL1U SN Signaling lymphocytic activation molecule 3; SLAMF3; SLAM family member 3; Lymphocyte antigen 9; LY9; Cell surface molecule Ly-9 TTZCL1U GN LY9 TTZCL1U FC May participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction. TTZCL1U SQ MVAPKSHTDDWAPGPFSSKPQRSQLQIFSSVLQTSLLFLLMGLRASGKDSAPTVVSGILGGSVTLPLNISVDTEIENVIWIGPKNALAFARPKENVTIMVKSYLGRLDITKWSYSLCISNLTLNDAGSYKAQINQRNFEVTTEEEFTLFVYEQLQEPQVTMKSVKVSENFSCNITLMCSVKGAEKSVLYSWTPREPHASESNGGSILTVSRTPCDPDLPYICTAQNPVSQRSSLPVHVGQFCTDPGASRGGTTGETVVGVLGEPVTLPLALPACRDTEKVVWLFNTSIISKEREEAATADPLIKSRDPYKNRVWVSSQDCSLKISQLKIEDAGPYHAYVCSEASSVTSMTHVTLLIYRRLRKPKITWSLRHSEDGICRISLTCSVEDGGNTVMYTWTPLQKEAVVSQGESHLNVSWRSSENHPNLTCTASNPVSRSSHQFLSENICSGPERNTKLWIGLFLMVCLLCVGIFSWCIWKRKGRCSVPAFCSSQAEAPADTPEPTAGHTLYSVLSQGYEKLDTPLRPARQQPTPTSDSSSDSNLTTEEDEDRPEVHKPISGRYEVFDQVTQEGAGHDPAPEGQADYDPVTPYVTEVESVVGENTMYAQVFNLQGKTPVSQKEESSATIYCSIRKPQVVPPPQQNDLEIPESPTYENFT TTZCL1U TT Literature-reported TTVX9SH ID TTVX9SH TTVX9SH TN Trace amine receptor 3 (TAAR3) TTVX9SH UP Q9P1P4 TTVX9SH UC TAAR3_HUMAN TTVX9SH SN hTaar3; TaR-3; TAAR3; Putative trace amine-associated receptor 3; GPR57; G-protein coupled receptor 57 TTVX9SH GN TAAR3P TTVX9SH FC G protein-coupled receptor activity, trace-amine receptor activity, sensory perception of chemical stimulus TTVX9SH SQ MDLTYIPEDLSSCPKFVNKILSSHQPLFSCPGDNVFGYDWSHDYPLFGNLVIMVSISHFKQLHSPTNFLILSMATTDFLLGFVIMPYSIMRSVESCWYFGDGFCKFHTSFDMMLRLTSIFHLCSIAIDRFYAVCYPLHYTTKMTNSTIKQLLAFCWSVPALFSFGLVLSEADVSGMQSYKILVACFNFCALTFNKFWGTILFTTCFFTPGSIMVGIYGKIFIVSKQHARVISHVPENTKGAVKKHLSKKKDRKAAKTLGIVMGVFLACWLPCFLAVLIDPYLDYSTPILILDLLVWLRYFNSTCNPLIHGFFNPWFQKAFKYIVSGKIFSSHSETANLFPEAH TTVX9SH TT Literature-reported TTCO25G ID TTCO25G TTCO25G TN Trace amine receptor 5 (TAAR5) TTCO25G UP O14804 TTCO25G UC TAAR5_HUMAN TTCO25G SN hTaar5; Trace amine-associated receptor 5; TaR-5; Putative neurotransmitter receptor; PNR TTCO25G GN TAAR5 TTCO25G FC Olfactory receptor specific for trimethylamine, a trace amine. Also activated at lower level by dimethylethylamine. Trimethylamine is a bacterial metabolite found in some animal odors, and to humans it is a repulsive odor associated with bad breath and spoiled food. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase. TTCO25G SQ MRAVFIQGAEEHPAAFCYQVNGSCPRTVHTLGIQLVIYLACAAGMLIIVLGNVFVAFAVSYFKALHTPTNFLLLSLALADMFLGLLVLPLSTIRSVESCWFFGDFLCRLHTYLDTLFCLTSIFHLCFISIDRHCAICDPLLYPSKFTVRVALRYILAGWGVPAAYTSLFLYTDVVETRLSQWLEEMPCVGSCQLLLNKFWGWLNFPLFFVPCLIMISLYVKIFVVATRQAQQITTLSKSLAGAAKHERKAAKTLGIAVGIYLLCWLPFTIDTMVDSLLHFITPPLVFDIFIWFAYFNSACNPIIYVFSYQWFRKALKLTLSQKVFSPQTRTVDLYQE TTCO25G TT Literature-reported TTXHSZK ID TTXHSZK TTXHSZK TN Transcription factor SOX-5 (SOX5) TTXHSZK UP P35711 TTXHSZK UC SOX5_HUMAN TTXHSZK SN SRY-box 5; LAMSHF; L-SOX5F; L-SOX5B; L-SOX5 TTXHSZK GN SOX5 TTXHSZK FC Activates transcription of COL2A1 and AGC1 in vitro. Binds specifically to the DNA sequence 5'-AACAAT-3'. TTXHSZK SQ MLTDPDLPQEFERMSSKRPASPYGEADGEVAMVTSRQKVEEEESDGLPAFHLPLHVSFPNKPHSEEFQPVSLLTQETCGHRTPTSQHNTMEVDGNKVMSSFAPHNSSTSPQKAEEGGRQSGESLSSTALGTPERRKGSLADVVDTLKQRKMEELIKNEPEETPSIEKLLSKDWKDKLLAMGSGNFGEIKGTPESLAEKERQLMGMINQLTSLREQLLAAHDEQKKLAASQIEKQRQQMELAKQQQEQIARQQQQLLQQQHKINLLQQQIQVQGQLPPLMIPVFPPDQRTLAAAAQQGFLLPPGFSYKAGCSDPYPVQLIPTTMAAAAAATPGLGPLQLQQLYAAQLAAMQVSPGGKLPGIPQGNLGAAVSPTSIHTDKSTNSPPPKSKDEVAQPLNLSAKPKTSDGKSPTSPTSPHMPALRINSGAGPLKASVPAALASPSARVSTIGYLNDHDAVTKAIQEARQMKEQLRREQQVLDGKVAVVNSLGLNNCRTEKEKTTLESLTQQLAVKQNEEGKFSHAMMDFNLSGDSDGSAGVSESRIYRESRGRGSNEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKAMTNLEKQPYYEEQARLSKQHLEKYPDYKYKPRPKRTCLVDGKKLRIGEYKAIMRNRRQEMRQYFNVGQQAQIPIATAGVVYPGAIAMAGMPSPHLPSEHSSVSSSPEPGMPVIQSTYGVKGEEPHIKEEIQAEDINGEIYDEYDEEEDDPDVDYGSDSENHIAGQAN TTXHSZK TT Literature-reported TTY85FG ID TTY85FG TTY85FG TN Transcriptional repressor CTCFL (CTCFL) TTY85FG UP Q8NI51 TTY85FG UC CTCFL_HUMAN TTY85FG SN Zinc finger protein CTCF-T; Cancer/testis antigen 27; CTCF-like protein; CTCF paralog; CT27; CCCTC-binding factor; Brother of the regulator of imprinted sites; BORIS TTY85FG GN CTCFL TTY85FG FC Plays a key role in gene imprinting in male germline, by participating in the establishment of differential methylation at the IGF2/H19 imprinted control region (ICR). Directly binds the unmethylated H19 ICR and recruits the PRMT7 methyltransferase, leading to methylate histone H4 'Arg-3' to form H4R3sme2. This probably leads to recruit de novo DNA methyltransferases at these sites. Seems to act as tumor suppressor. In association with DNMT1 and DNMT3B, involved in activation of BAG1 gene expression by binding to its promoter. Required for dimethylation of H3 lysine 4 (H3K4me2) of MYC and BRCA1 promoters. Testis-specific DNA binding protein responsible for insulator function, nuclear architecture and transcriptional control, which probably acts by recruiting epigenetic chromatin modifiers. TTY85FG SQ MAATEISVLSEQFTKIKELELMPEKGLKEEEKDGVCREKDHRSPSELEAERTSGAFQDSVLEEEVELVLAPSEESEKYILTLQTVHFTSEAVELQDMSLLSIQQQEGVQVVVQQPGPGLLWLEEGPRQSLQQCVAISIQQELYSPQEMEVLQFHALEENVMVASEDSKLAVSLAETTGLIKLEEEQEKNQLLAERTKEQLFFVETMSGDERSDEIVLTVSNSNVEEQEDQPTAGQADAEKAKSTKNQRKTKGAKGTFHCDVCMFTSSRMSSFNRHMKTHTSEKPHLCHLCLKTFRTVTLLRNHVNTHTGTRPYKCNDCNMAFVTSGELVRHRRYKHTHEKPFKCSMCKYASVEASKLKRHVRSHTGERPFQCCQCSYASRDTYKLKRHMRTHSGEKPYECHICHTRFTQSGTMKIHILQKHGENVPKYQCPHCATIIARKSDLRVHMRNLHAYSAAELKCRYCSAVFHERYALIQHQKTHKNEKRFKCKHCSYACKQERHMTAHIRTHTGEKPFTCLSCNKCFRQKQLLNAHFRKYHDANFIPTVYKCSKCGKGFSRWINLHRHSEKCGSGEAKSAASGKGRRTRKRKQTILKEATKGQKEAAKGWKEAANGDEAAAEEASTTKGEQFPGEMFPVACRETTARVKEEVDEGVTCEMLLNTMDK TTY85FG TT Literature-reported TTY85FG FM CTCF zinc-finger protein family TT7315J ID TT7315J TT7315J TN Transmembrane glycoprotein NMB (GPNMB) TT7315J UP Q14956 TT7315J UC GPNMB_HUMAN TT7315J SN NMB; Hematopoietic growth factor inducible neurokinin-1 type; HGFIN TT7315J GN GPNMB TT7315J FC Could be a melanogenic enzyme. TT7315J SQ MECLYYFLGFLLLAARLPLDAAKRFHDVLGNERPSAYMREHNQLNGWSSDENDWNEKLYPVWKRGDMRWKNSWKGGRVQAVLTSDSPALVGSNITFAVNLIFPRCQKEDANGNIVYEKNCRNEAGLSADPYVYNWTAWSEDSDGENGTGQSHHNVFPDGKPFPHHPGWRRWNFIYVFHTLGQYFQKLGRCSVRVSVNTANVTLGPQLMEVTVYRRHGRAYVPIAQVKDVYVVTDQIPVFVTMFQKNDRNSSDETFLKDLPIMFDVLIHDPSHFLNYSTINYKWSFGDNTGLFVSTNHTVNHTYVLNGTFSLNLTVKAAAPGPCPPPPPPPRPSKPTPSLATTLKSYDSNTPGPAGDNPLELSRIPDENCQINRYGHFQATITIVEGILEVNIIQMTDVLMPVPWPESSLIDFVVTCQGSIPTEVCTIISDPTCEITQNTVCSPVDVDEMCLLTVRRTFNGSGTYCVNLTLGDDTSLALTSTLISVPDRDPASPLRMANSALISVGCLAIFVTVISLLVYKKHKEYNPIENSPGNVVRSKGLSVFLNRAKAVFFPGNQEKDPLLKNQEFKGVS TT7315J TT Literature-reported TTU6FJG ID TTU6FJG TTU6FJG TN Trichoderma L-Lysine alpha-oxidase (HYPRU LysOX) TTU6FJG UP A0A0G4DCU0 TTU6FJG UC A0A0G4DCU0_HYPRU TTU6FJG SN L-Lysine alpha-oxidase TTU6FJG GN HYPRU LysOX TTU6FJG FC An antitumor enzyme of Trichoderma harzianum. Inhibit highly infectious viruses INSV and TRSV, Mycoplasma hominis, and tick-borne encephalitis virus. TTU6FJG SQ MDNVDFAESVRTRWARRLIREKVAKELNILTERLGEVPGIPPPREGRFLGGGYSHDNLPSDPLYSSIKPALLKEAPRAEEELPPRKVCIVGAGVSGLYIAMILDDLKIPNLTYDIFESSSRTGGRLYTHHFTDAKHDYYDIGAMRYPDIPSMKRTFNLFKRTGMPLIKYYLDGENTPQLYNNHFFAKGVVDPYMVSVANGGTVPDDVVDSVGEKLQQAFGYYKEKLAEDFDKGFDELMLVDDMTTREYLKRGGPKGEAPKYDFFAIQWMETQNTGTNLFDQAFSESVIDSFDFDNPTKPEWYCIEGGTSLLVDAMKETLVHKVQNNKRVEAISIDLDAPDDGNMSVKIGGKDYSGYSTVFNTTALGCLDRMDLRGLNLHPTQADAIRCLHYDNSTKVALKFSYPWWIKDCGITCGGAASTDLPLRTCVYPSYNLGDTGEAVLLASYTWSQDATRIGSLVKDAPPQPPKEDELVELILQNLARLHAEHMTYEKIKEAYTGVYHAYCWANDPNVGGAFALFGPGQFSNLYPYLMRPAAGGKFHIVGEASSVHHAWIIGSLESAYTAVYQFLYKYKMWDYLRLLLERWQYGLQELETGKHGTAHLQFILGSLPKEYQVKI TTU6FJG TT Literature-reported TTHKJPG ID TTHKJPG TTHKJPG TN Troponin I (TNNI) TTHKJPG UP P19237; P48788; P19429 TTHKJPG UC TNNI1_HUMAN; TNNI2_HUMAN; TNNI3_HUMAN TTHKJPG SN Troponin I TTHKJPG GN TNNI1; TNNI2; TNNI3 TTHKJPG FC Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. TTHKJPG SQ MPEVERKPKITASRKLLLKSLMLAKAKECWEQEHEEREAEKVRYLAERIPTLQTRGLSLSALQDLCRELHAKVEVVDEERYDIEAKCLHNTREIKDLKLKVMDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVKKEDTEKERPVEVGDWRKNVEAMSGMEGRKKMFDAAKSPTSQ TTHKJPG TT Literature-reported TT7W0NY ID TT7W0NY TT7W0NY TN Tubulin alpha (TUBA) TT7W0NY UP Q71U36; P68363 TT7W0NY UC TBA1A_HUMAN; TBA1B_HUMAN TT7W0NY SN Tubulin alpha-1 chain; Alpha-tubulin TT7W0NY GN TUBA1A; TUBA1B TT7W0NY FC Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TT7W0NY SQ MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY TT7W0NY TT Literature-reported TTPH7T0 ID TTPH7T0 TTPH7T0 TN Tumor expressed melanoma antigen (PRAME) TTPH7T0 UP P78395 TTPH7T0 UC PRAME_HUMAN TTPH7T0 SN Preferentially expressed antigen of melanoma; Opa-interacting protein 4; OIP-4; Melanoma antigen preferentially expressed in tumors; MAPE TTPH7T0 GN PRAME TTPH7T0 FC Functions as a transcriptional repressor, inhibiting the signaling of retinoic acid through the retinoic acid receptors RARA, RARB and RARG. Prevents retinoic acid-induced cell proliferation arrest, differentiation and apoptosis. TTPH7T0 SQ MERRRLWGSIQSRYISMSVWTSPRRLVELAGQSLLKDEALAIAALELLPRELFPPLFMAAFDGRHSQTLKAMVQAWPFTCLPLGVLMKGQHLHLETFKAVLDGLDVLLAQEVRPRRWKLQVLDLRKNSHQDFWTVWSGNRASLYSFPEPEAAQPMTKKRKVDGLSTEAEQPFIPVEVLVDLFLKEGACDELFSYLIEKVKRKKNVLRLCCKKLKIFAMPMQDIKMILKMVQLDSIEDLEVTCTWKLPTLAKFSPYLGQMINLRRLLLSHIHASSYISPEKEEQYIAQFTSQFLSLQCLQALYVDSLFFLRGRLDQLLRHVMNPLETLSITNCRLSEGDVMHLSQSPSVSQLSVLSLSGVMLTDVSPEPLQALLERASATLQDLVFDECGITDDQLLALLPSLSHCSQLTTLSFYGNSISISALQSLLQHLIGLSNLTHVLYPVPLESYEDIHGTLHLERLAYLHARLRELLCELGRPSMVWLSANPCPHCGDRTFYDPEPILCPCFMPN TTPH7T0 TT Clinical trial TTUJZRL ID TTUJZRL TTUJZRL TN Tumor-associated hydroquinone oxidase (tNOX) TTUJZRL UP Q16206 TTUJZRL UC ENOX2_HUMAN TTUJZRL SN Tumorassociated hydroquinone oxidase; Protein disulfidethiol oxidoreductase; EctoNOX disulfidethiol exchanger 2; Ecto-NOX disulfide-thiol exchanger 2; Cytosolic ovarian carcinoma antigen 1; COVA1; APK1 antigen TTUJZRL GN ENOX2 TTUJZRL FC Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide-thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 22 minutes and play a role in control of the ultradian cellular biological clock. May be involved in cell growth. TTUJZRL SQ MQRDFRWLWVYEIGYAADNSRTLNVDSTAMTLPMSDPTAWATAMNNLGMAPLGIAGQPILPDFDPALGMMTGIPPITPMMPGLGIVPPPIPPDMPVVKEIIHCKSCTLFPPNPNLPPPATRERPPGCKTVFVGGLPENGTEQIIVEVFEQCGEIIAIRKSKKNFCHIRFAEEYMVDKALYLSGYRIRLGSSTDKKDTGRLHVDFAQARDDLYEWECKQRMLAREERHRRRMEEERLRPPSPPPVVHYSDHECSIVAEKLKDDSKFSEAVQTLLTWIERGEVNRRSANNFYSMIQSANSHVRRLVNEKAAHEKDMEEAKEKFKQALSGILIQFEQIVAVYHSASKQKAWDHFTKAQRKNISVWCKQAEEIRNIHNDELMGIRREEEMEMSDDEIEEMTETKETEESALVSQAEALKEENDSLRWQLDAYRNEVELLKQEQGKVHREDDPNKEQQLKLLQQALQGMQQHLLKVQEEYKKKEAELEKLKDDKLQVEKMLENLKEKESCASRLCASNQDSEYPLEKTMNSSPIKSEREALLVGIISTFLHVHPFGASIEYICSYLHRLDNKICTSDVECLMGRLQHTFKQEMTGVGASLEKRWKFCGFEGLKLT TTUJZRL TT Literature-reported TTHT87J ID TTHT87J TTHT87J TN TWIK-related spinal cord potassium channel (TRESK) TTHT87J UP Q7Z418 TTHT87J UC KCNKI_HUMAN TTHT87J SN TWIK-related individual potassium channel; TRIK; TRESK; Potassium channel subfamily K member 18 TTHT87J GN KCNK18 TTHT87J FC Outward rectifying potassium channel. Produces rapidly activating outward rectifier K(+) currents. May function as background potassium channel that sets the resting membrane potential. Channel activity is directly activated by calcium signal. Activated by the G(q)-protein coupled receptor pathway. The calcium signal robustly activates the channel via calcineurin, whereas the anchoring of 14-3-3/YWHAH interferes with the return of the current to the resting state after activation. Inhibited also by arachidonic acid and other naturally occurring unsaturated free fatty acids. Channel activity is also enhanced by volatile anesthetics, such as isoflurane. Appears to be the primary target of hydroxy-alpha-sanshool, an ingredient of Schezuan pepper. May be involved in the somatosensory function with special respect to pain sensation (By similarity). TTHT87J SQ MEVSGHPQARRCCPEALGKLFPGLCFLCFLVTYALVGAVVFSAIEDGQVLVAADDGEFEKFLEELCRILNCSETVVEDRKQDLQGHLQKVKPQWFNRTTHWSFLSSLFFCCTVFSTVGYGYIYPVTRLGKYLCMLYALFGIPLMFLVLTDTGDILATILSTSYNRFRKFPFFTRPLLSKWCPKSLFKKKPDPKPADEAVPQIIISAEELPGPKLGTCPSRPSCSMELFERSHALEKQNTLQLPPQAMERSNSCPELVLGRLSYSIISNLDEVGQQVERLDIPLPIIALIVFAYISCAAAILPFWETQLDFENAFYFCFVTLTTIGFGDTVLEHPNFFLFFSIYIIVGMEIVFIAFKLVQNRLIDIYKNVMLFFAKGKFYHLVKK TTHT87J TT Literature-reported TTODQE2 ID TTODQE2 TTODQE2 TN Two pore calcium channel protein 1 (TPC1) TTODQE2 UP Q9ULQ1 TTODQE2 UC TPC1_HUMAN TTODQE2 SN Voltage-dependent calcium channel protein TPC1; TPC1; KIAA1169 TTODQE2 GN TPCN1 TTODQE2 FC Nicotinic acid adenine dinucleotide phosphate (NAADP) receptor that may function as one of the major voltage-gated Ca(2+) channels (VDCC) across the lysosomal and endosomal membrane. TTODQE2 SQ MAVSLDDDVPLILTLDEGGSAPLAPSNGLGQEELPSKNGGSYAIHDSQAPSLSSGGESSPSSPAHNWEMNYQEAAIYLQEGENNDKFFTHPKDAKALAAYLFAHNHLFYLMELATALLLLLLSLCEAPAVPALRLGIYVHATLELFALMVVVFELCMKLRWLGLHTFIRHKRTMVKTSVLVVQFVEAIVVLVRQMSHVRVTRALRCIFLVDCRYCGGVRRNLRQIFQSLPPFMDILLLLLFFMIIFAILGFYLFSPNPSDPYFSTLENSIVSLFVLLTTANFPDVMMPSYSRNPWSCVFFIVYLSIELYFIMNLLLAVVFDTFNDIEKRKFKSLLLHKRTAIQHAYRLLISQRRPAGISYRQFEGLMRFYKPRMSARERYLTFKALNQNNTPLLSLKDFYDIYEVAALKWKAKKNREHWFDELPRTALLIFKGINILVKSKAFQYFMYLVVAVNGVWILVETFMLKGGNFFSKHVPWSYLVFLTIYGVELFLKVAGLGPVEYLSSGWNLFDFSVTVFAFLGLLALALNMEPFYFIVVLRPLQLLRLFKLKERYRNVLDTMFELLPRMASLGLTLLIFYYSFAIVGMEFFCGIVFPNCCNTSTVADAYRWRNHTVGNRTVVEEGYYYLNNFDNILNSFVTLFELTVVNNWYIIMEGVTSQTSHWSRLYFMTFYIVTMVVMTIIVAFILEAFVFRMNYSRKNQDSEVDGGITLEKEISKEELVAVLELYREARGASSDVTRLLETLSQMERYQQHSMVFLGRRSRTKSDLSLKMYQEEIQEWYEEHAREQEQQRQLSSSAAPAAQQPPGSRQRSQTVT TTODQE2 TT Literature-reported TTMPART ID TTMPART TTMPART TN Uracil nucleotide/cysteinyl leukotriene receptor (GPR17) TTMPART UP Q13304 TTMPART UC GPR17_HUMAN TTMPART SN UDP/CysLT receptor; R12; G-protein coupled receptor 17 TTMPART GN GPR17 TTMPART FC Dual specificity receptor for uracil nucleotides and cysteinyl leukotrienes (CysLTs). Signals through G(i) and inhibition of adenylyl cyclase. May mediate brain damage by nucleotides and CysLTs following ischemia. TTMPART SQ MSKRSWWAGSRKPPREMLKLSGSDSSQSMNGLEVAPPGLITNFSLATAEQCGQETPLENMLFASFYLLDFILALVGNTLALWLFIRDHKSGTPANVFLMHLAVADLSCVLVLPTRLVYHFSGNHWPFGEIACRLTGFLFYLNMYASIYFLTCISADRFLAIVHPVKSLKLRRPLYAHLACAFLWVVVAVAMAPLLVSPQTVQTNHTVVCLQLYREKASHHALVSLAVAFTFPFITTVTCYLLIIRSLRQGLRVEKRLKTKAVRMIAIVLAIFLVCFVPYHVNRSVYVLHYRSHGASCATQRILALANRITSCLTSLNGALDPIMYFFVAEKFRHALCNLLCGKRLKGPPPSFEGKTNESSLSAKSEL TTMPART TT Literature-reported TT18WJB ID TT18WJB TT18WJB TN Vang-like protein 1 (VANGL1) TT18WJB UP Q8TAA9 TT18WJB UC VANG1_HUMAN TT18WJB SN Van Gogh-like protein 1; Strabismus 2; STB2; Loop-tail protein 2 homolog; LPP2 TT18WJB GN VANGL1 TT18WJB FC Invovled in multicellular organism development, Wnt signaling pathway and planar cell polarity pathway. TT18WJB SQ MDTESTYSGYSYYSSHSKKSHRQGERTRERHKSPRNKDGRGSEKSVTIQPPTGEPLLGNDSTRTEEVQDDNWGETTTAITGTSEHSISQEDIARISKDMEDSVGLDCKRYLGLTVASFLGLLVFLTPIAFILLPPILWRDELEPCGTICEGLFISMAFKLLILLIGTWALFFRKRRADMPRVFVFRALLLVLIFLFVVSYWLFYGVRILDSRDRNYQGIVQYAVSLVDALLFIHYLAIVLLELRQLQPMFTLQVVRSTDGESRFYSLGHLSIQRAALVVLENYYKDFTIYNPNLLTASKFRAAKHMAGLKVYNVDGPSNNATGQSRAMIAAAARRRDSSHNELYYEEAEHERRVKKRKARLVVAVEEAFIHIQRLQAEEQQKAPGEVMDPREAAQAIFPSMARALQKYLRITRQQNYHSMESILQHLAFCITNGMTPKAFLERYLSAGPTLQYDKDRWLSTQWRLVSDEAVTNGLRDGIVFVLKCLDFSLVVNVKKIPFIILSEEFIDPKSHKFVLRLQSETSV TT18WJB TT Literature-reported TTN6OKJ ID TTN6OKJ TTN6OKJ TN Virus Capsid glycoprotein VP7 (Viru VP7) TTN6OKJ UP Q8B6C3 TTN6OKJ UC Q8B6C3_9REOV TTN6OKJ SN Outer capsid glycoprotein VP7 TTN6OKJ GN Viru VP7 TTN6OKJ FC Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. TTN6OKJ SQ MVCTTLYTVCAILFILFIYILFFRKMFHLITDTLIVMLILSNCVEWSQCQMFIDDIYYNGNVETIINSTDPFNVESLCIYFPNAVVGSQGPGKSDGHLNDGNYAQTIATLFETKGFPKGSIILKTYTQTSDFINSVEMTCSYNIVIIPDSPNDSESIEQIAEWILNVWKCDDMNLEIYTYEQIGINNLWAAFGSDCDISVCPLDTTSNGIGCSPASTETYEVVSNDTQLALINVVDNVRHRIQMNTAQCKLKNCIKGEARLNTALIRISTSSSFDNSLSPLNNGQTTRSFKINAKKWWTIFYTIIDYINTIVQAMTPRHRAIYPEGWMLRYA TTN6OKJ TT Literature-reported TTQ9HB0 ID TTQ9HB0 TTQ9HB0 TN Virus fusion protein HIV gp41-influenza HA (HIV gp41-Influ HA) TTQ9HB0 UP P04578 (33-511)-P03452 TTQ9HB0 UC ENV_HV1H2-HEMA_I34A1 TTQ9HB0 SN Virus fusion protein Env polyprotein-influenza Hemagglutinin TTQ9HB0 GN HIV gp41-Influ HA TTQ9HB0 FC Functions as a passive -helical anchor of the protein to the virus envelope during its merger with the cell membrane TTQ9HB0 SQ KLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKMKANLLVLLCALAAADADTICIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDSHNGKLCRLKGIAPLQLGKCNIAGWLLGNPECDPLLPVRSWSYIVETPNSENGICYPGDFIDYEELREQLSSVSSFERFEIFPKESSWPNHNTNGVTAACSHEGKSSFYRNLLWLTEKEGSYPKLKNSYVNKKGKEVLVLWGIHHPPNSKEQQNLYQNENAYVSVVTSNYNRRFTPEIAERPKVRDQAGRMNYYWTLLKPGDTIIFEANGNLIAPMYAFALSRGFGSGIITSNASMHECNTKCQTPLGAINSSLPYQNIHPVTIGECPKYVRSAKLRMVTGLRNIPSIQSRGLFGAIAGFIEGGWTGMIDGWYGYHHQNEQGSGYAADQKSTQNAINGITNKVNTVIEKMNIQFTAVGKEFNKLEKRMENLNKKVDDGFLDIWTYNAELLVLLENERTLDFHDSNVKNLYEKVKSQLKNNAKEIGNGCFEFYHKCDNECMESVRNGTYDYPKYSEESKLNREKVDGVKLESMGIYQILAIYSTVASSLVLLVSLGAISFWMCSNGSLQCRICI TTQ9HB0 TT Literature-reported TTD61ET ID TTD61ET TTD61ET TN Western equine encephalitis virus Envelope glycoprotein E1 (WEEV E1) TTD61ET UP Q76SY1 TTD61ET UC Q76SY1_WEEV TTD61ET SN Envelope glycoprotein E1 TTD61ET GN WEEV E1 TTD61ET FC A class II membrane fusion protein, containing a hydrophobic fusion peptide conserved among the alphaviruses. Induced a strong WEEV-specific T cell response. TTD61ET SQ RASNCAYGHIPISIDIPDAAFVRSSESPTILEVSCTVADCIYSADFGGSLTLQYKADREGHCPVHSHSTTAVLKEATTHVTATGSITLHFSTSSPQANFIVSLCGKKTTCNAECKPPADHIIGEPHKVDQEFQAAVSKTSWNWLLALFGGASSLIVVGLIVLVCSSMLINTRR TTD61ET TT Literature-reported TTGTNSL ID TTGTNSL TTGTNSL TN WNT1-inducible-signaling pathway protein 1 (WISP1) TTGTNSL UP O95388 TTGTNSL UC WISP1_HUMAN TTGTNSL SN Wnt-1-induced secreted protein; WISP1; WISP-1; CCN family member 4 TTGTNSL GN WISP1 TTGTNSL FC Downstream regulator in the Wnt/Frizzled-signalingpathway. Associated with cell survival. Attenuates p53-mediated apoptosis in response to DNA damage through activation of AKT kinase. Up-regulates the anti-apoptotic Bcl-X(L) protein. Adheres to skinand melanoma fibroblasts. In vitro binding to skin fibroblasts occurs through the proteoglycans, decorin and biglycan. TTGTNSL SQ MRWFLPWTLAAVTAAAASTVLATALSPAPTTMDFTPAPLEDTSSRPQFCKWPCECPPSPPRCPLGVSLITDGCECCKMCAQQLGDNCTEAAICDPHRGLYCDYSGDRPRYAIGVCAQVVGVGCVLDGVRYNNGQSFQPNCKYNCTCIDGAVGCTPLCLRVRPPRLWCPHPRRVSIPGHCCEQWVCEDDAKRPRKTAPRDTGAFDAVGEVEAWHRNCIAYTSPWSPCSTSCGLGVSTRISNVNAQCWPEQESRLCNLRPCDVDIHTLIKAGKKCLAVYQPEASMNFTLAGCISTRSYQPKYCGVCMDNRCCIPYKSKTIDVSFQCPDGLGFSRQVLWINACFCNLSCRNPNDIFADLESYPDFSEIAN TTGTNSL TT Literature-reported TTKG7F8 ID TTKG7F8 TTKG7F8 TN Wnt-5a protein (WNT5A) TTKG7F8 UP P41221 TTKG7F8 UC WNT5A_HUMAN TTKG7F8 SN Protein Wnt-5a TTKG7F8 GN WNT5A TTKG7F8 FC Can activate or inhibit canonical Wnt signaling, depending on receptor context. In the presence of FZD4, activates beta-catenin signaling. In the presence of ROR2, inhibits the canonical Wnt pathway by promoting beta-catenin degradation through a GSK3-independent pathway which involves down-regulation of beta-catenin-induced reporter gene expression. Suppression of the canonical pathway allows chondrogenesis to occur and inhibits tumor formation. Stimulates cell migration. Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor. Mediates motility of melanoma cells. Required during embryogenesis for extension of the primary anterior-posterior axis and for outgrowth of limbs and the genital tubercle. Inhibits type II collagen expression in chondrocytes. Ligand for members of the frizzled family of seven transmembrane receptors. TTKG7F8 SQ MKKSIGILSPGVALGMAGSAMSSKFFLVALAIFFSFAQVVIEANSWWSLGMNNPVQMSEVYIIGAQPLCSQLAGLSQGQKKLCHLYQDHMQYIGEGAKTGIKECQYQFRHRRWNCSTVDNTSVFGRVMQIGSRETAFTYAVSAAGVVNAMSRACREGELSTCGCSRAARPKDLPRDWLWGGCGDNIDYGYRFAKEFVDARERERIHAKGSYESARILMNLHNNEAGRRTVYNLADVACKCHGVSGSCSLKTCWLQLADFRKVGDALKEKYDSAAAMRLNSRGKLVQVNSRFNSPTTQDLVYIDPSPDYCVRNESTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFKTVQTERCHCKFHWCCYVKCKKCTEIVDQFVCK TTKG7F8 TT Literature-reported TTJ9U4L ID TTJ9U4L TTJ9U4L TN Yellow fever mosquito Eggshell organizing factor 1 (YFM EOF1) TTJ9U4L UP Q16ME2 TTJ9U4L UC Q16ME2_AEDAE TTJ9U4L SN AAEL012336-PA TTJ9U4L GN YFM EOF1 TTJ9U4L FC Plays an essential role in the formation and melanization of the eggshell. TTJ9U4L SQ MEESQQLQFPIRGNNNNKPLNVSGGNDGSGQFTDSGYTSYHSISASGSVARSVLATIEEDNEADSSFEEARSSEDIFQMGGGSNVLTPTTAASIERISNFHLTTPNSTGKPVGQHRGLVRKPTFDNLFEQYTPKKADYGPPCRTTQTPVRSDRKVELGSQTPRKNKASAKRKLGEFREKLYSDGDALELAPSRDLNDSLEGDCKKLDQEDISPIYHTKRRRSSVIDLIRSSTPKTASLRSNFHVEVRENIDWDAVQQGKASGRGGKSRALRKFQSFSPSKMHSYKKRDVLQEKSVIANRRAPFQRQDALRQVSLEQDLSKQSTPQKAQESSLDKSFELPLEGLITPSKQSNLGVLLDAPILVQPSSEADFKESDLEQQISQIPSFEECAYPQTPSKQTLSLDDSGVIRHAPVCTEVNKSIPSILGTESPSFVSLSIPKTPTSTNKSRNRLKRLSSTKKDKPRSKPPSPIHRAQPFIPGTYRRPSYVNVERLNILKWLNEHDKDALGIVLDYLNDSDLVRVVRVSTGWRDIIEHHRPSYRRLRAHFAREKEVKENLSFPSFVSREGSLLGKTGGSLLSSFGDSSKEIAVSLPRQPFSLCNSIDSNQSVGGELRRSGSVQRSPPVSPSKRKFRENQKIASHLKKSERLKPCPRCEKPSRVVLTKSSIKLAMATGSLDSSTTRTVASGKLDRSYTLPDSLMGSSATSMIAAAALDCTSTTIGSPQSPTNPDRIRRNLFSTSLLPRSQSVDARTPVTRSPRRRRSTDVQGSSASLLERKNGKTKSAEAIQCDYAVCSGKNCGFMFCIKCLCEYHPSSVCKDLAPNSPSKEDEPAHNVACSKQSRRSLLRLRK TTJ9U4L TT Literature-reported TTWY768 ID TTWY768 TTWY768 TN ZW10 interactor (ZWINT) TTWY768 UP O95229 TTWY768 UC ZWINT_HUMAN TTWY768 SN Zwint-1; ZW10-interacting protein 1 TTWY768 GN ZWINT TTWY768 FC Part of the MIS12 complex, which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase. TTWY768 SQ MEAAETEAEAAALEVLAEVAGILEPVGLQEEAELPAKILVEFVVDSQKKDKLLCSQLQVADFLQNILAQEDTAKGLDPLASEDTSRQKAIAAKEQWKELKATYREHVEAIKIGLTKALTQMEEAQRKRTQLREAFEQLQAKKQMAMEKRRAVQNQWQLQQEKHLQHLAEVSAEVRERKTGTQQELDRVFQKLGNLKQQAEQERDKLQRYQTFLQLLYTLQGKLLFPEAEAEAENLPDDKPQQPTRPQEQSTGDTMGRDPGVSFKAVGLQPAGDVNLP TTWY768 TT Literature-reported TTDM9GW ID TTDM9GW TTDM9GW TN Hepatitis C virus Nucleoside triphosphatase (HCV NTP) TTDM9GW UP NO-UNIPROT TTDM9GW UC NOUNIPROTAC TTDM9GW SN Nucleoside-triphosphatase; Nucleoside triphosphate phosphohydrolase; NTPase; MJ0226 TTDM9GW GN NO-GeName TTDM9GW FC Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective monophosphate derivatives. Probably excludes non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions. TTDM9GW TT Literature-reported TT9W3FO ID TT9W3FO TT9W3FO TN Monosialic ganglioside 2 (GM2) TT9W3FO UP Other Molecule TT9W3FO UC NOUNIPROTAC TT9W3FO SN Gamma-M2; GM2 TT9W3FO GN NO-GeName TT9W3FO FC Crystallins are the dominant structural components of the vertebrate eye lens. TT9W3FO TT Literature-reported TTVUKJI ID TTVUKJI TTVUKJI TN Cyclic nucleotide (CN) TTVUKJI UP Other Molecule TTVUKJI UC NOUNIPROTAC TTVUKJI SN cNMP TTVUKJI GN NO-GeName TTVUKJI TT Literature-reported TTDCBO2 ID TTDCBO2 TTDCBO2 TN Endotoxin (LPS) TTDCBO2 UP Other Molecule TTDCBO2 UC NOUNIPROTAC TTDCBO2 SN Endotoxin (lipopolysaccharide) TTDCBO2 GN NO-GeName TTDCBO2 TT Literature-reported TT8VA5M ID TT8VA5M TT8VA5M TN Epstein-Barr virus microRNA miR-BART1 (EBV MIRBART1) TT8VA5M UP microRNA/lncRNA TT8VA5M UC NOUNIPROTAC TT8VA5M BC Non-coding RNA target TT8VA5M GN NO-GeName TT8VA5M TT Literature-reported TTMK5ZC ID TTMK5ZC TTMK5ZC TN H19 imprinted maternally expressed transcript (H19) TTMK5ZC UP microRNA/lncRNA TTMK5ZC UC NOUNIPROTAC TTMK5ZC BC Non-coding RNA target TTMK5ZC GN NO-GeName TTMK5ZC TT Literature-reported TTX1CE3 ID TTX1CE3 TTX1CE3 TN High density lipoprotein (HDL) TTX1CE3 UP Other molecule TTX1CE3 UC NOUNIPROTAC TTX1CE3 SN HDL TTX1CE3 GN NO-GeName TTX1CE3 TT Literature-reported TTN4D5H ID TTN4D5H TTN4D5H TN HOXA distal transcript antisense RNA (HOTTIP) TTN4D5H UP microRNA/lncRNA TTN4D5H UC NOUNIPROTAC TTN4D5H BC Non-coding RNA target TTN4D5H GN NO-GeName TTN4D5H TT Literature-reported TTMDPH8 ID TTMDPH8 TTMDPH8 TN Long intergenic noncoding RNA AATBC (lincRNA AATBC) TTMDPH8 UP microRNA/lncRNA TTMDPH8 UC NOUNIPROTAC TTMDPH8 BC Non-coding RNA target TTMDPH8 GN NO-GeName TTMDPH8 TT Literature-reported TTEA4LW ID TTEA4LW TTEA4LW TN Long intergenic noncoding RNA p21 (lincRNA p21) TTEA4LW UP microRNA/lncRNA TTEA4LW UC NOUNIPROTAC TTEA4LW BC Non-coding RNA target TTEA4LW GN NO-GeName TTEA4LW TT Literature-reported TTVPGU3 ID TTVPGU3 TTVPGU3 TN microRNA hsa-miR-100 (MIR100) TTVPGU3 UP microRNA/lncRNA TTVPGU3 UC NOUNIPROTAC TTVPGU3 BC Non-coding RNA target TTVPGU3 GN NO-GeName TTVPGU3 TT Literature-reported TT8LA9O ID TT8LA9O TT8LA9O TN microRNA hsa-miR-101 (MIR101) TT8LA9O UP microRNA/lncRNA TT8LA9O UC NOUNIPROTAC TT8LA9O BC Non-coding RNA target TT8LA9O GN NO-GeName TT8LA9O TT Literature-reported TTQRLOF ID TTQRLOF TTQRLOF TN microRNA hsa-miR-105 (MIR105) TTQRLOF UP microRNA/lncRNA TTQRLOF UC NOUNIPROTAC TTQRLOF BC Non-coding RNA target TTQRLOF GN NO-GeName TTQRLOF TT Literature-reported TTMH5GE ID TTMH5GE TTMH5GE TN microRNA hsa-miR-107 (MIR107) TTMH5GE UP microRNA/lncRNA TTMH5GE UC NOUNIPROTAC TTMH5GE BC Non-coding RNA target TTMH5GE GN NO-GeName TTMH5GE TT Literature-reported TTQYUF5 ID TTQYUF5 TTQYUF5 TN microRNA hsa-miR-10b (MIR10b) TTQYUF5 UP microRNA/lncRNA TTQYUF5 UC NOUNIPROTAC TTQYUF5 BC Non-coding RNA target TTQYUF5 GN NO-GeName TTQYUF5 TT Literature-reported TTY04XD ID TTY04XD TTY04XD TN microRNA hsa-miR-1207-5p (MIR1207-5p) TTY04XD UP microRNA/lncRNA TTY04XD UC NOUNIPROTAC TTY04XD BC Non-coding RNA target TTY04XD GN NO-GeName TTY04XD TT Literature-reported TTJAFT2 ID TTJAFT2 TTJAFT2 TN microRNA hsa-miR-122 (MIR122) TTJAFT2 UP microRNA/lncRNA TTJAFT2 UC NOUNIPROTAC TTJAFT2 BC Non-coding RNA target TTJAFT2 GN NO-GeName TTJAFT2 TT Literature-reported TTJCBTE ID TTJCBTE TTJCBTE TN microRNA hsa-miR-1269a (MIR1269a) TTJCBTE UP microRNA/lncRNA TTJCBTE UC NOUNIPROTAC TTJCBTE BC Non-coding RNA target TTJCBTE GN NO-GeName TTJCBTE TT Literature-reported TTB7DYX ID TTB7DYX TTB7DYX TN microRNA hsa-miR-1271 (MIR1271) TTB7DYX UP microRNA/lncRNA TTB7DYX UC NOUNIPROTAC TTB7DYX BC Non-coding RNA target TTB7DYX GN NO-GeName TTB7DYX TT Literature-reported TTYAR63 ID TTYAR63 TTYAR63 TN microRNA hsa-miR-1280 (MIR1280) TTYAR63 UP microRNA/lncRNA TTYAR63 UC NOUNIPROTAC TTYAR63 BC Non-coding RNA target TTYAR63 GN NO-GeName TTYAR63 TT Literature-reported TT6HUWO ID TT6HUWO TT6HUWO TN microRNA hsa-miR-129-5p (MIR129-5p) TT6HUWO UP microRNA/lncRNA TT6HUWO UC NOUNIPROTAC TT6HUWO BC Non-coding RNA target TT6HUWO GN NO-GeName TT6HUWO TT Literature-reported TTSXL1N ID TTSXL1N TTSXL1N TN microRNA hsa-miR-130b (MIR130b) TTSXL1N UP microRNA/lncRNA TTSXL1N UC NOUNIPROTAC TTSXL1N BC Non-coding RNA target TTSXL1N GN NO-GeName TTSXL1N TT Literature-reported TTBXRSK ID TTBXRSK TTBXRSK TN microRNA hsa-miR-132 (MIR132) TTBXRSK UP microRNA/lncRNA TTBXRSK UC NOUNIPROTAC TTBXRSK BC Non-coding RNA target TTBXRSK GN NO-GeName TTBXRSK TT Literature-reported TTEA1FT ID TTEA1FT TTEA1FT TN microRNA hsa-miR-133a (MIR133a) TTEA1FT UP microRNA/lncRNA TTEA1FT UC NOUNIPROTAC TTEA1FT BC Non-coding RNA target TTEA1FT GN NO-GeName TTEA1FT TT Literature-reported TTG8INV ID TTG8INV TTG8INV TN microRNA hsa-miR-134 (MIR134) TTG8INV UP microRNA/lncRNA TTG8INV UC NOUNIPROTAC TTG8INV BC Non-coding RNA target TTG8INV GN NO-GeName TTG8INV TT Literature-reported TT1W5LN ID TT1W5LN TT1W5LN TN microRNA hsa-miR-143 (MIR143) TT1W5LN UP microRNA/lncRNA TT1W5LN UC NOUNIPROTAC TT1W5LN BC Non-coding RNA target TT1W5LN GN NO-GeName TT1W5LN TT Literature-reported TTQOPIA ID TTQOPIA TTQOPIA TN microRNA hsa-miR-144 (MIR144) TTQOPIA UP microRNA/lncRNA TTQOPIA UC NOUNIPROTAC TTQOPIA BC Non-coding RNA target TTQOPIA GN NO-GeName TTQOPIA TT Literature-reported TT2C5LO ID TT2C5LO TT2C5LO TN microRNA hsa-miR-146a (MIR146a) TT2C5LO UP microRNA/lncRNA TT2C5LO UC NOUNIPROTAC TT2C5LO BC Non-coding RNA target TT2C5LO GN NO-GeName TT2C5LO TT Literature-reported TTOW189 ID TTOW189 TTOW189 TN microRNA hsa-miR-148a (MIR148a) TTOW189 UP microRNA/lncRNA TTOW189 UC NOUNIPROTAC TTOW189 BC Non-coding RNA target TTOW189 GN NO-GeName TTOW189 TT Literature-reported TTD81JK ID TTD81JK TTD81JK TN microRNA hsa-miR-152 (MIR152) TTD81JK UP microRNA/lncRNA TTD81JK UC NOUNIPROTAC TTD81JK BC Non-coding RNA target TTD81JK GN NO-GeName TTD81JK TT Literature-reported TTC3TFX ID TTC3TFX TTC3TFX TN microRNA hsa-miR-181a (MIR181a) TTC3TFX UP microRNA/lncRNA TTC3TFX UC NOUNIPROTAC TTC3TFX BC Non-coding RNA target TTC3TFX GN NO-GeName TTC3TFX TT Literature-reported TTOPT8D ID TTOPT8D TTOPT8D TN microRNA hsa-miR-181c (MIR181c) TTOPT8D UP microRNA/lncRNA TTOPT8D UC NOUNIPROTAC TTOPT8D BC Non-coding RNA target TTOPT8D GN NO-GeName TTOPT8D TT Literature-reported TTJLWTC ID TTJLWTC TTJLWTC TN microRNA hsa-miR-182 (MIR182) TTJLWTC UP microRNA/lncRNA TTJLWTC UC NOUNIPROTAC TTJLWTC BC Non-coding RNA target TTJLWTC GN NO-GeName TTJLWTC TT Literature-reported TTQSK01 ID TTQSK01 TTQSK01 TN microRNA hsa-miR-183 (MIR183) TTQSK01 UP microRNA/lncRNA TTQSK01 UC NOUNIPROTAC TTQSK01 BC Non-coding RNA target TTQSK01 GN NO-GeName TTQSK01 TT Literature-reported TTH12DY ID TTH12DY TTH12DY TN microRNA hsa-miR-185 (MIR185) TTH12DY UP microRNA/lncRNA TTH12DY UC NOUNIPROTAC TTH12DY BC Non-coding RNA target TTH12DY GN NO-GeName TTH12DY TT Literature-reported TT8AJ6S ID TT8AJ6S TT8AJ6S TN microRNA hsa-miR-188 (MIR188) TT8AJ6S UP microRNA/lncRNA TT8AJ6S UC NOUNIPROTAC TT8AJ6S BC Non-coding RNA target TT8AJ6S GN NO-GeName TT8AJ6S TT Literature-reported TT2H4DE ID TT2H4DE TT2H4DE TN microRNA hsa-miR-18a (MIR18a) TT2H4DE UP microRNA/lncRNA TT2H4DE UC NOUNIPROTAC TT2H4DE BC Non-coding RNA target TT2H4DE GN NO-GeName TT2H4DE TT Literature-reported TT3ULBR ID TT3ULBR TT3ULBR TN microRNA hsa-miR-191 (MIR191) TT3ULBR UP microRNA/lncRNA TT3ULBR UC NOUNIPROTAC TT3ULBR BC Non-coding RNA target TT3ULBR GN NO-GeName TT3ULBR TT Literature-reported TT7OE0A ID TT7OE0A TT7OE0A TN microRNA hsa-miR-194 (MIR194) TT7OE0A UP microRNA/lncRNA TT7OE0A UC NOUNIPROTAC TT7OE0A BC Non-coding RNA target TT7OE0A GN NO-GeName TT7OE0A TT Literature-reported TTMRFN9 ID TTMRFN9 TTMRFN9 TN microRNA hsa-miR-197-3p (MIR197-3p) TTMRFN9 UP microRNA/lncRNA TTMRFN9 UC NOUNIPROTAC TTMRFN9 BC Non-coding RNA target TTMRFN9 GN NO-GeName TTMRFN9 TT Literature-reported TTGF64I ID TTGF64I TTGF64I TN microRNA hsa-miR-199a (MIR199a) TTGF64I UP microRNA/lncRNA TTGF64I UC NOUNIPROTAC TTGF64I BC Non-coding RNA target TTGF64I GN NO-GeName TTGF64I TT Literature-reported TTDGEIH ID TTDGEIH TTDGEIH TN microRNA hsa-miR-200c (MIR200c) TTDGEIH UP microRNA/lncRNA TTDGEIH UC NOUNIPROTAC TTDGEIH BC Non-coding RNA target TTDGEIH GN NO-GeName TTDGEIH TT Literature-reported TTI7YU2 ID TTI7YU2 TTI7YU2 TN microRNA hsa-miR-205 (MIR205) TTI7YU2 UP microRNA/lncRNA TTI7YU2 UC NOUNIPROTAC TTI7YU2 BC Non-coding RNA target TTI7YU2 GN NO-GeName TTI7YU2 TT Literature-reported TTZJ0Q6 ID TTZJ0Q6 TTZJ0Q6 TN microRNA hsa-miR-206 (MIR206) TTZJ0Q6 UP microRNA/lncRNA TTZJ0Q6 UC NOUNIPROTAC TTZJ0Q6 BC Non-coding RNA target TTZJ0Q6 GN NO-GeName TTZJ0Q6 TT Literature-reported TTKH1NI ID TTKH1NI TTKH1NI TN microRNA hsa-miR-21 (MIR21) TTKH1NI UP microRNA/lncRNA TTKH1NI UC NOUNIPROTAC TTKH1NI BC Non-coding RNA target TTKH1NI GN NO-GeName TTKH1NI TT Literature-reported TTF5CVU ID TTF5CVU TTF5CVU TN microRNA hsa-miR-210 (MIR210) TTF5CVU UP microRNA/lncRNA TTF5CVU UC NOUNIPROTAC TTF5CVU BC Non-coding RNA target TTF5CVU GN NO-GeName TTF5CVU TT Literature-reported TT2J1RT ID TT2J1RT TT2J1RT TN microRNA hsa-miR-212 (MIR212) TT2J1RT UP microRNA/lncRNA TT2J1RT UC NOUNIPROTAC TT2J1RT BC Non-coding RNA target TT2J1RT GN NO-GeName TT2J1RT TT Literature-reported TTNDIAX ID TTNDIAX TTNDIAX TN microRNA hsa-miR-214 (MIR214) TTNDIAX UP microRNA/lncRNA TTNDIAX UC NOUNIPROTAC TTNDIAX BC Non-coding RNA target TTNDIAX GN NO-GeName TTNDIAX TT Literature-reported TTF7CL8 ID TTF7CL8 TTF7CL8 TN microRNA hsa-miR-218 (MIR218) TTF7CL8 UP microRNA/lncRNA TTF7CL8 UC NOUNIPROTAC TTF7CL8 BC Non-coding RNA target TTF7CL8 GN NO-GeName TTF7CL8 TT Literature-reported TTFWOHQ ID TTFWOHQ TTFWOHQ TN microRNA hsa-miR-22 (MIR22) TTFWOHQ UP microRNA/lncRNA TTFWOHQ UC NOUNIPROTAC TTFWOHQ BC Non-coding RNA target TTFWOHQ GN NO-GeName TTFWOHQ TT Literature-reported TT6ZE4S ID TT6ZE4S TT6ZE4S TN microRNA hsa-miR-223-3p (MIR223-3p) TT6ZE4S UP microRNA/lncRNA TT6ZE4S UC NOUNIPROTAC TT6ZE4S BC Non-coding RNA target TT6ZE4S GN NO-GeName TT6ZE4S TT Literature-reported TTUCLSH ID TTUCLSH TTUCLSH TN microRNA hsa-miR-23a (MIR23a) TTUCLSH UP microRNA/lncRNA TTUCLSH UC NOUNIPROTAC TTUCLSH BC Non-coding RNA target TTUCLSH GN NO-GeName TTUCLSH TT Literature-reported TTJVKAN ID TTJVKAN TTJVKAN TN microRNA hsa-miR-26a (MIR26a) TTJVKAN UP microRNA/lncRNA TTJVKAN UC NOUNIPROTAC TTJVKAN BC Non-coding RNA target TTJVKAN GN NO-GeName TTJVKAN TT Literature-reported TT8EM6Q ID TT8EM6Q TT8EM6Q TN microRNA hsa-miR-296 (MIR296) TT8EM6Q UP microRNA/lncRNA TT8EM6Q UC NOUNIPROTAC TT8EM6Q BC Non-coding RNA target TT8EM6Q GN NO-GeName TT8EM6Q TT Literature-reported TTO60BY ID TTO60BY TTO60BY TN microRNA hsa-miR-29b (MIR29b) TTO60BY UP microRNA/lncRNA TTO60BY UC NOUNIPROTAC TTO60BY BC Non-coding RNA target TTO60BY GN NO-GeName TTO60BY TT Clinical trial TTR7S2C ID TTR7S2C TTR7S2C TN microRNA hsa-miR-29c (MIR29c) TTR7S2C UP microRNA/lncRNA TTR7S2C UC NOUNIPROTAC TTR7S2C BC Non-coding RNA target TTR7S2C GN NO-GeName TTR7S2C TT Literature-reported TT47RZK ID TT47RZK TT47RZK TN microRNA hsa-miR-302a (MIR302a) TT47RZK UP microRNA/lncRNA TT47RZK UC NOUNIPROTAC TT47RZK BC Non-coding RNA target TT47RZK GN NO-GeName TT47RZK TT Literature-reported TTC9EYH ID TTC9EYH TTC9EYH TN microRNA hsa-miR-30a (MIR30a) TTC9EYH UP microRNA/lncRNA TTC9EYH UC NOUNIPROTAC TTC9EYH BC Non-coding RNA target TTC9EYH GN NO-GeName TTC9EYH TT Literature-reported TTEHZXM ID TTEHZXM TTEHZXM TN microRNA hsa-miR-30d (MIR30d) TTEHZXM UP microRNA/lncRNA TTEHZXM UC NOUNIPROTAC TTEHZXM BC Non-coding RNA target TTEHZXM GN NO-GeName TTEHZXM TT Literature-reported TTI4ERV ID TTI4ERV TTI4ERV TN microRNA hsa-miR-30d-5p (MIR30d-5p) TTI4ERV UP microRNA/lncRNA TTI4ERV UC NOUNIPROTAC TTI4ERV BC Non-coding RNA target TTI4ERV GN NO-GeName TTI4ERV TT Literature-reported TT3NJX2 ID TT3NJX2 TT3NJX2 TN microRNA hsa-miR-329 (MIR329) TT3NJX2 UP microRNA/lncRNA TT3NJX2 UC NOUNIPROTAC TT3NJX2 BC Non-coding RNA target TT3NJX2 GN NO-GeName TT3NJX2 TT Literature-reported TTA2G3P ID TTA2G3P TTA2G3P TN microRNA hsa-miR-33 (MIR33) TTA2G3P UP microRNA/lncRNA TTA2G3P UC NOUNIPROTAC TTA2G3P BC Non-coding RNA target TTA2G3P GN NO-GeName TTA2G3P TT Literature-reported TT68KIU ID TT68KIU TT68KIU TN microRNA hsa-miR-371-5p (MIR371-5p) TT68KIU UP microRNA/lncRNA TT68KIU UC NOUNIPROTAC TT68KIU BC Non-coding RNA target TT68KIU GN NO-GeName TT68KIU TT Literature-reported TTZQYV0 ID TTZQYV0 TTZQYV0 TN microRNA hsa-miR-373 (MIR373) TTZQYV0 UP microRNA/lncRNA TTZQYV0 UC NOUNIPROTAC TTZQYV0 BC Non-coding RNA target TTZQYV0 GN NO-GeName TTZQYV0 TT Literature-reported TTIB5L1 ID TTIB5L1 TTIB5L1 TN microRNA hsa-miR-375 (MIR375) TTIB5L1 UP microRNA/lncRNA TTIB5L1 UC NOUNIPROTAC TTIB5L1 BC Non-coding RNA target TTIB5L1 GN NO-GeName TTIB5L1 TT Literature-reported TTYJRBQ ID TTYJRBQ TTYJRBQ TN microRNA hsa-miR-429 (MIR429) TTYJRBQ UP microRNA/lncRNA TTYJRBQ UC NOUNIPROTAC TTYJRBQ BC Non-coding RNA target TTYJRBQ GN NO-GeName TTYJRBQ TT Literature-reported TTIWODE ID TTIWODE TTIWODE TN microRNA hsa-miR-451 (MIR451) TTIWODE UP microRNA/lncRNA TTIWODE UC NOUNIPROTAC TTIWODE BC Non-coding RNA target TTIWODE GN NO-GeName TTIWODE TT Literature-reported TTYJH6B ID TTYJH6B TTYJH6B TN microRNA hsa-miR-455 (MIR455) TTYJH6B UP microRNA/lncRNA TTYJH6B UC NOUNIPROTAC TTYJH6B BC Non-coding RNA target TTYJH6B GN NO-GeName TTYJH6B TT Literature-reported TTFDOTL ID TTFDOTL TTFDOTL TN microRNA hsa-miR-486 (MIR486) TTFDOTL UP microRNA/lncRNA TTFDOTL UC NOUNIPROTAC TTFDOTL BC Non-coding RNA target TTFDOTL GN NO-GeName TTFDOTL TT Literature-reported TTKMAOQ ID TTKMAOQ TTKMAOQ TN microRNA hsa-miR-492 (MIR492) TTKMAOQ UP microRNA/lncRNA TTKMAOQ UC NOUNIPROTAC TTKMAOQ BC Non-coding RNA target TTKMAOQ GN NO-GeName TTKMAOQ TT Literature-reported TT8TPWV ID TT8TPWV TT8TPWV TN microRNA hsa-miR-509 (MIR509) TT8TPWV UP microRNA/lncRNA TT8TPWV UC NOUNIPROTAC TT8TPWV BC Non-coding RNA target TT8TPWV GN NO-GeName TT8TPWV TT Literature-reported TTX2ITC ID TTX2ITC TTX2ITC TN microRNA hsa-miR-572 (MIR572) TTX2ITC UP microRNA/lncRNA TTX2ITC UC NOUNIPROTAC TTX2ITC BC Non-coding RNA target TTX2ITC GN NO-GeName TTX2ITC TT Literature-reported TT9IGC3 ID TT9IGC3 TT9IGC3 TN microRNA hsa-miR-621 (MIR621) TT9IGC3 UP microRNA/lncRNA TT9IGC3 UC NOUNIPROTAC TT9IGC3 BC Non-coding RNA target TT9IGC3 GN NO-GeName TT9IGC3 TT Literature-reported TTQD4FU ID TTQD4FU TTQD4FU TN microRNA hsa-miR-664 (MIR664) TTQD4FU UP microRNA/lncRNA TTQD4FU UC NOUNIPROTAC TTQD4FU BC Non-coding RNA target TTQD4FU GN NO-GeName TTQD4FU TT Literature-reported TTKZVCO ID TTKZVCO TTKZVCO TN microRNA hsa-miR-7 (MIR7) TTKZVCO UP microRNA/lncRNA TTKZVCO UC NOUNIPROTAC TTKZVCO BC Non-coding RNA target TTKZVCO GN NO-GeName TTKZVCO TT Literature-reported TTIWTFQ ID TTIWTFQ TTIWTFQ TN microRNA hsa-miR-709 (MIR709) TTIWTFQ UP microRNA/lncRNA TTIWTFQ UC NOUNIPROTAC TTIWTFQ BC Non-coding RNA target TTIWTFQ GN NO-GeName TTIWTFQ TT Literature-reported TT9ZCFQ ID TT9ZCFQ TT9ZCFQ TN microRNA hsa-miR-9 (MIR9) TT9ZCFQ UP microRNA/lncRNA TT9ZCFQ UC NOUNIPROTAC TT9ZCFQ BC Non-coding RNA target TT9ZCFQ GN NO-GeName TT9ZCFQ TT Literature-reported TT3N0YA ID TT3N0YA TT3N0YA TN microRNA hsa-miR-939 (MIR939) TT3N0YA UP microRNA/lncRNA TT3N0YA UC NOUNIPROTAC TT3N0YA BC Non-coding RNA target TT3N0YA GN NO-GeName TT3N0YA TT Literature-reported TTRZTXD ID TTRZTXD TTRZTXD TN microRNA hsa-miR-96 (MIR96) TTRZTXD UP microRNA/lncRNA TTRZTXD UC NOUNIPROTAC TTRZTXD BC Non-coding RNA target TTRZTXD GN NO-GeName TTRZTXD TT Literature-reported TT27K59 ID TT27K59 TT27K59 TN Platelet activating factor (PAF) TT27K59 UP Other molecule TT27K59 UC NOUNIPROTAC TT27K59 SN PAF TT27K59 GN NO-GeName TT27K59 TT Literature-reported TTL2KO8 ID TTL2KO8 TTL2KO8 TN Small nucleolar RNA 40 (snoRNA40) TTL2KO8 UP microRNA/lncRNA TTL2KO8 UC NOUNIPROTAC TTL2KO8 BC Non-coding RNA target TTL2KO8 GN NO-GeName TTL2KO8 TT Literature-reported TT3STGE ID TT3STGE TT3STGE TN Small nucleolar RNA 78 (snoRNA78) TT3STGE UP microRNA/lncRNA TT3STGE UC NOUNIPROTAC TT3STGE BC Non-coding RNA target TT3STGE GN NO-GeName TT3STGE TT Literature-reported TTHL1EA ID TTHL1EA TTHL1EA TN G-quadruplex DNA (GQDNA) TTHL1EA UP Other molecule TTHL1EA UC NOUNIPROTAC TTHL1EA GN NO-GeName TTHL1EA TT Literature-reported TTPFQ0C ID TTPFQ0C TTPFQ0C TN HOX transcript antisense RNA (HOTAIR) TTPFQ0C UP microRNA/lncRNA TTPFQ0C UC NOUNIPROTAC TTPFQ0C GN NO-GeName TTPFQ0C TT Literature-reported TTQMWCG ID TTQMWCG TTQMWCG TN Human immunodeficiency virus RNA (HIV RNA) TTQMWCG UP microRNA/lncRNA TTQMWCG UC NOUNIPROTAC TTQMWCG GN NO-GeName TTQMWCG TT Literature-reported TTNSXG2 ID TTNSXG2 TTNSXG2 TN Human immunodeficiency virus TAR RNA (HIV TAR-RNA) TTNSXG2 UP microRNA/lncRNA TTNSXG2 UC NOUNIPROTAC TTNSXG2 GN NO-GeName TTNSXG2 TT Literature-reported TTC6RJ7 ID TTC6RJ7 TTC6RJ7 TN Intermediate-density lipoprotein (IDL) TTC6RJ7 UP Other molecule TTC6RJ7 UC NOUNIPROTAC TTC6RJ7 GN NO-GeName TTC6RJ7 TT Literature-reported TTR6NV2 ID TTR6NV2 TTR6NV2 TN Lactobacillus 16S rRNA (Lacto 16RNA) TTR6NV2 UP microRNA/lncRNA TTR6NV2 UC NOUNIPROTAC TTR6NV2 GN NO-GeName TTR6NV2 TT Literature-reported TT4P0T6 ID TT4P0T6 TT4P0T6 TN Potassium-competitive acid (PCA) TT4P0T6 UP Other molecule TT4P0T6 UC NOUNIPROTAC TT4P0T6 GN NO-GeName TT4P0T6 TT Literature-reported TTHF0JV ID TTHF0JV TTHF0JV TN HUMAN alpha-galactosidase A (GLA) TTHF0JV UP P06280 TTHF0JV UC AGAL_HUMAN TTHF0JV BC Glycosylase TTHF0JV SN Melibiase; Agalsidase; Alpha-D-galactoside galactohydrolase; Alpha-D-galactosidase A TTHF0JV GN GLA TTHF0JV FC Human protein galactosidase alpha interacts with SARS-CoV-2 Nsp14 protein with high significance, which indicates GLA as a potential therapeutic target. TTHF0JV EC EC 3.2.1.22 TTHF0JV PD 4NXS; 3TV8; 3S5Z; 3S5Y; 3LXC TTHF0JV SQ MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL TT7GR5W ID TT7GR5W TT7GR5W TN HUMAN casein kinase II alpha prime (CSNK2A2) TT7GR5W UP P19784 TT7GR5W UC CSK22_HUMAN TT7GR5W BC Kinase TT7GR5W SN Casein kinase II subunit alpha'; CK2A2; CK II alpha' TT7GR5W GN CSNK2A2 TT7GR5W FC Human protein casein kinase 2 alpha 2 interacts with SARS-CoV-2 N protein with high significance, which indicates CSNK2A2 as a potential therapeutic target. TT7GR5W EC EC 2.7.11.1 TT7GR5W PD 6QY9; 6HMQ; 6HMD; 6HMC; 6HMB TT7GR5W SQ MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCADNAVLSSGLTAAR TTUJ0G5 ID TTUJ0G5 TTUJ0G5 TN HUMAN catechol-O-methyl-transferase (COMT) TTUJ0G5 UP P21964 TTUJ0G5 UC COMT_HUMAN TTUJ0G5 BC Methyltransferase TTUJ0G5 SN S-COMT; MB-COMT; Catechol-O-methyltransferase; COMT TTUJ0G5 GN COMT TTUJ0G5 FC Human protein catechol-O-methyltransferase interacts with SARS-CoV-2 Nsp7 protein with high significance, which indicates COMT as a potential therapeutic target. TTUJ0G5 EC EC 2.1.1.6 TTUJ0G5 PD 5LSA; 4XUE; 4XUD; 4XUC; 4PYK TTUJ0G5 SQ MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP TTOX4TW ID TTOX4TW TTOX4TW TN HUMAN DNA [cytosine-5]-methyltransferase 1 (DNMT1) TTOX4TW UP P26358 TTOX4TW UC DNMT1_HUMAN TTOX4TW BC Methyltransferase TTOX4TW SN MCMT; M.HsaI; Dnmt1; DNMT; DNA methyltransferase HsaI; DNA MTase HsaI; DNA (cytosine5)methyltransferase 1; DNA (cytosine-5)-methyltransferase 1; CXXCtype zinc finger protein 9; CXXC9; CXXC-type zinc finger protein 9; AIM TTOX4TW GN DNMT1 TTOX4TW FC Human protein DNA methyltransferase 1 interacts with SARS-CoV-2 Orf8 protein with high significance, which indicates DNMT1 as a potential therapeutic target. TTOX4TW EC EC 2.1.1.37 TTOX4TW PD 5YDR; 5WVO; 4Z97; 4Z96; 4YOC TTOX4TW SQ MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQLCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEKEEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD TTCKXRW ID TTCKXRW TTCKXRW TN HUMAN histone deacetylase 2 (HDAC2) TTCKXRW UP Q92769 TTCKXRW UC HDAC2_HUMAN TTCKXRW BC Carbon-nitrogen hydrolase TTCKXRW SN HD2 TTCKXRW GN HDAC2 TTCKXRW FC Human protein histone deacetylase 2 interacts with SARS-CoV-2 Nsp5 protein with high significance, which indicates HDAC2 as a potential therapeutic target. TTCKXRW EC EC 3.5.1.98 TTCKXRW PD 6G3O; 5IX0; 5IWG; 4LY1; 4LXZ TTCKXRW SQ MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP TT3GRLK ID TT3GRLK TT3GRLK TN HUMAN inosine-5'-monophosphate dehydrogenase 1 (IMPDH1) TT3GRLK UP P20839 TT3GRLK UC IMDH1_HUMAN TT3GRLK BC CH-OH donor oxidoreductase TT3GRLK SN Superoxide-inducible protein 12; SOI12; Probable inosine-5'-monophosphate dehydrogenase IMD1; NAD-dependent inosine monophosphate dehydrogenase; Inosine dehydrogenase; IMPDH-I; IMPDH 1; IMPDH; IMPD1; IMPD 1; IMPD; IMP dehydrogenase 1; IMP dehydrogenase TT3GRLK GN IMPDH1 TT3GRLK FC Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors. TT3GRLK EC EC 1.1.1.205 TT3GRLK PD 1JCN TT3GRLK SQ MADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY TTAJ45Y ID TTAJ45Y TTAJ45Y TN HUMAN microtubule affinity regulating kinase 2 (MARK2) TTAJ45Y UP Q7KZI7 TTAJ45Y UC MARK2_HUMAN TTAJ45Y BC Kinase TTAJ45Y SN Par-1b; Par1b; PAR1 homolog b; PAR1 homolog; MAP/microtubule affinity-regulating kinase 2; EMK-1; ELKL motif kinase 1 TTAJ45Y GN MARK2 TTAJ45Y FC Human protein microtubule affinity regulating kinase 2 interacts with SARS-CoV-2 Orf9b protein with high significance, which indicates MARK2 as a potential therapeutic target. TTAJ45Y EC EC 2.7.11.1 TTAJ45Y PD 3IEC; 5EAK; 5KZ7; 5KZ8 TTAJ45Y SQ MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMIRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRFSDQAAGPAIPTSNSYSKKTQSNNAENKRPEEDRESGRKASSTAKVPASPLPGLERKKTTPTPSTNSVLSTSTNRSRNSPLLERASLGQASIQNGKDSLTMPGSRASTASASAAVSAARPRQHQKSMSASVHPNKASGLPPTESNCEVPRPSTAPQRVPVASPSAHNISSSGGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPYGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLSFRFARRNLNEPESKDRVETLRPHVVGSGGNDKEKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHEKYMLLCMHGTPGHEDFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL TT0MFOL ID TT0MFOL TT0MFOL TN HUMAN microtubule affinity regulating kinase 3 (MARK3) TT0MFOL UP P27448 TT0MFOL UC MARK3_HUMAN TT0MFOL BC Kinase TT0MFOL SN cTAK1; Serine/threonine-protein kinase p78; Ser/Thr protein kinase PAR-1; Protein kinase STK10); Protein kinase STK10; Par-1a; MAP/microtubule affinity-regulating kinase 3; EMK2; EMK-2; ELKL motif kinase 2; Cdc25C-associated protein kinase 1; C-TAK1 TT0MFOL GN MARK3 TT0MFOL FC Human protein microtubule affinity regulating kinase 3 interacts with SARS-CoV-2 Orf9b protein with high significance, which indicates MARK3 as a potential therapeutic target. TT0MFOL EC EC 2.7.11.1 TT0MFOL PD 3FE3; 2QNJ TT0MFOL SQ MSTRTPLPTVNERDTENHTSHGDGRQEVTSRTSRSGARCRNSIASCADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLIMEYASGGEVFDYLVAHGRMKEKEARSKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGGKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKRFLVLNPIKRGTLEQIMKDRWINAGHEEDELKPFVEPELDISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLGRKSSELDASDSSSSSNLSLAKVRPSSDLNNSTGQSPHHKVQRSVSSSQKQRRYSDHAGPAIPSVVAYPKRSQTSTADSDLKEDGISSRKSSGSAVGGKGIAPASPMLGNASNPNKADIPERKKSSTVPSSNTASGGMTRRNTYVCSERTTADRHSVIQNGKENSTIPDQRTPVASTHSISSAATPDRIRFPRGTASRSTFHGQPRERRTATYNGPPASPSLSHEATPLSQTRSRGSTNLFSKLTSKLTRRNMSFRFIKRLPTEYERNGRYEGSSRNVSAEQKDENKEAKPRSLRFTWSMKTTSSMDPGDMMREIRKVLDANNCDYEQRERFLLFCVHGDGHAENLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL TTQ79SU ID TTQ79SU TTQ79SU TN HUMAN multidrug resistance-associated protein 1 (ABCC1) TTQ79SU UP P33527 TTQ79SU UC MRP1_HUMAN TTQ79SU BC ABC transporter TTQ79SU SN MRP1; MRP; Leukotriene C(4) transporter; LTC4 transporter; ATP-binding cassette sub-family C member 1 TTQ79SU GN ABCC1 TTQ79SU FC Human protein ATP binding cassette subfamily C member 1 interacts with SARS-CoV-2 Orf9c protein with high significance, which indicates ABCC1 as a potential therapeutic target. TTQ79SU EC EC 7.6.2.2 TTQ79SU PD 4C3Z; 2CBZ TTQ79SU SQ MALRGFCSADGSDPLWDWNVTWNTSNPDFTKCFQNTVLVWVPCFYLWACFPFYFLYLSRHDRGYIQMTPLNKTKTALGFLLWIVCWADLFYSFWERSRGIFLAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMTALKEDAQVDLFRDITFYVYFSLLLIQLVLSCFSDRSPLFSETIHDPNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNKEDTSEQVVPVLVKNWKKECAKTRKQPVKVVYSSKDPAQPKESSKVDANEEVEALIVKSPQKEWNPSLFKVLYKTFGPYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAVYVTIDENNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGGTNSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNDSLRENILFGCQLEEPYYRSVIQACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGVTGVSGPGKEAKQMENGMLVTDSAGKQLQRQLSSSSSYSGDISRHHNSTAELQKAEAKKEETWKLMEADKAQTGQVKLSVYWDYMKAIGLFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSMAKDAGLV TTMP03S ID TTMP03S TTMP03S TN HUMAN NF-kappa-B-activating kinase (TBK1) TTMP03S UP Q9UHD2 TTMP03S UC TBK1_HUMAN TTMP03S BC Kinase TTMP03S SN TANK-binding kinase 1; T2K; Serine/threonine-protein kinase TBK1; NAK TTMP03S GN TBK1 TTMP03S FC Human protein TANK binding kinase 1 interacts with SARS-CoV-2 Nsp13 protein with high significance, which indicates TBK1 as a potential therapeutic target. TTMP03S EC EC 2.7.11.1 TTMP03S PD 6O8B; 6NT9; 6CQ5; 6CQ4; 6CQ0 TTMP03S SQ MQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPVDVQMREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQFFAETSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSREPLNTIGLIYEKISLPKVHPRYDLDGDASMAKAITGVVCYACRIASTLLLYQELMRKGIRWLIELIKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEKLMKINLEAAELGEISDIHTKLLRLSSSQGTIETSLQDIDSRLSPGGSLADAWAHQEGTHPKDRNVEKLQVLLNCMTEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAMTHFTDECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTNELQETLPQKMFTASSGIKHTMTPIYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL TTM57AW ID TTM57AW TTM57AW TN HUMAN NIMA related kinase 9 (NEK9) TTM57AW UP Q8TD19 TTM57AW UC NEK9_HUMAN TTM57AW BC Kinase TTM57AW SN Serine/threonine-protein kinase Nek9; NimA-related protein kinase 9; NimA-related kinase 8; Never in mitosis A-related kinase 9; Nercc1 kinase; Nek8 TTM57AW GN NEK9 TTM57AW FC Human protein NIMA related kinase 9 interacts with SARS-CoV-2 Nsp9 protein with high significance, which indicates NEK9 as a potential therapeutic target. TTM57AW EC EC 2.7.11.1 TTM57AW PD 3ZKE; 3ZKF TTM57AW SQ MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSEKERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTLNIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAMEVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQKLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIRQVSCGDDFTVCVTDEGQLYAFGSDYYGCMGVDKVAGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCGCDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLGVGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHTILIVEKVLNSKTIRSNSSGLSIGTVFQSSSPGGGGGGGGGEEEDSQQESETPDPSGGFRGTMEADRGMEGLISPTEAMGNSNGASSSCPGWLRKELENAEFIPMPDSPSPLSAAFSESEKDTLPYEELQGLKVASEAPLEHKPQVEASSPRLNPAVTCAGKGTPLTPPACACSSLQVEVERLQGLVLKCLAEQQKLQQENLQIFTQLQKLNKKLEGGQQVGMHSKGTQTAKEEMEMDPKPDLDSDSWCLLGTDSCRPSL TTV0HK8 ID TTV0HK8 TTV0HK8 TN HUMAN protein kinase cAMP-activated catalytic subunit alpha (PRKACA) TTV0HK8 UP P17612 TTV0HK8 UC KAPCA_HUMAN TTV0HK8 BC Kinase TTV0HK8 SN PKA C-alpha; cAMP-dependent protein kinase catalytic subunit alpha TTV0HK8 GN PRKACA TTV0HK8 FC Human protein protein kinase cAMP-activated catalytic subunit alpha interacts with SARS-CoV-2 Nsp13 protein with high significance, which indicates PRKACA as a potential therapeutic target. TTV0HK8 EC EC 2.7.11.11 TTV0HK8 PD 2GU8; 3AGL; 3AGM; 3AMA; 3AMB TTV0HK8 SQ MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF TTVJHX8 ID TTVJHX8 TTVJHX8 TN HUMAN receptor-interacting protein 1 (RIPK1) TTVJHX8 UP Q13546 TTVJHX8 UC RIPK1_HUMAN TTVJHX8 BC Kinase TTVJHX8 SN Receptor-interacting serine/threonine-protein kinase 1; RIP1; RIP-1; RIP; Cell death protein RIP TTVJHX8 GN RIPK1 TTVJHX8 FC Human protein receptor interacting serine/threonine kinase 1 interacts with SARS-CoV-2 Nsp12 protein with high significance, which indicates RIPK1 as a potential therapeutic target. TTVJHX8 EC EC 2.7.11.1 TTVJHX8 PD 6R5F; 6OCQ; 6NW2; 6HHO; 6C4D TTVJHX8 SQ MQPDMSLNVIKMKSSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLEESVEEDVKSLKKEYSNENAVVKRMQSLQLDCVAVPSSRSNSATEQPGSLHSSQGLGMGPVEESWFAPSLEHPQEENEPSLQSKLQDEANYHLYGSRMDRQTKQQPRQNVAYNREEERRRRVSHDPFAQQRPYENFQNTEGKGTAYSSAASHGNAVHQPSGLTSQPQVLYQNNGLYSSHGFGTRPLDPGTAGPRVWYRPIPSHMPSLHNIPVPETNYLGNTPTMPFSSLPPTDESIKYTIYNSTGIQIGAYNYMEIGGTSSSLLDSTNTNFKEEPAAKYQAIFDNTTSLTDKHLDPIRENLGKHWKNCARKLGFTQSQIDEIDHDYERDGLKEKVYQMLQKWVMREGIKGATVGKLAQALHQCSRIDLLSSLIYVSQN TTYWTI0 ID TTYWTI0 TTYWTI0 TN HUMAN valosin-containing protein p97 (VCP) TTYWTI0 UP P55072 TTYWTI0 UC TERA_HUMAN TTYWTI0 BC AAA ATPase family TTYWTI0 SN Valosin-containing protein; Transitional endoplasmic reticulum ATPase; TER ATPase; 15S Mg(2+)-ATPase p97 subunit TTYWTI0 GN VCP TTYWTI0 FC Human protein valosin containing protein interacts with SARS-CoV-2 Orf10 protein with high significance, which indicates VCP as a potential therapeutic target. TTYWTI0 EC EC 3.6.4.6 TTYWTI0 PD 6MCK; 6G30; 6G2Z; 6G2Y; 6G2X TTYWTI0 SQ MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGSVYTEDNDDDLYG TTSRAOU ID TTSRAOU TTSRAOU TN HUMAN bromodomain-containing protein 4 (BRD4) TTSRAOU UP O60885 TTSRAOU UC BRD4_HUMAN TTSRAOU BC Bromodomain TTSRAOU SN Protein HUNK1; HUNK1 TTSRAOU GN BRD4 TTSRAOU FC Human protein bromodomain containing 4 interacts with SARS-CoV-2 E protein with high significance, which indicates BRD4 as a potential therapeutic target. TTSRAOU PD 6Q3Z; 6Q3Y; 6MNL; 6MAU; 6HDQ TTSRAOU SQ MSAESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQATPHPFPAVTPDLIVQTPVMTVVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLPPEPKTTKLGQRRESSRPVKPPKKDVPDSQQHPAPEKSSKVSEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLEAREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVAVSSPAVPPPTKVVAPPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKEKDKKEKKKEKHKRKEEVEENKKSKAKEPPPKKTKKNNSSNSNVSKKEPAPMKSKPPPTYESEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESSSESSSSDSEDSETEMAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQQQQQPPPPPPPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPAVSPALTQTPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPPPPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTHIQQPPPPQGQQPPHPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPLMIHSPQMSQFQSLTHQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPFSPSLRPEPPKHPESIKAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKAQAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAAAVAAAATPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF TTCU5EN ID TTCU5EN TTCU5EN TN HUMAN cullin-2 (CUL2) TTCU5EN UP Q13617 TTCU5EN UC CUL2_HUMAN TTCU5EN BC Cullin family TTCU5EN SN cullin 2; CUL-2 TTCU5EN GN cullin 2 TTCU5EN FC Human protein cullin 2 interacts with SARS-CoV-2 Orf10 protein with high significance, which indicates CUL2 as a potential therapeutic target. TTCU5EN PD 4WQO; 5N4W; 6R6H; 6R7F; 6R7H TTCU5EN SQ MSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYTETKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQFIKKNKLTEADLQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQAILIRMLLREIKNDRGGEDPNQKVIHGVINSFVHVEQYKKKFPLKFYQEIFESPFLTETGEYYKQEASNLLQESNCSQYMEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHAECHNIIRQEKKNDMANMYVLLRAVSTGLPHMIQELQNHIHDEGLRATSNLTQENMPTLFVESVLEVHGKFVQLINTVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDRLTSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHRMYTDMSVSADLNNKFNNFIKNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEKSVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMNFSSKRTKFKITTSMQKDTPQEMEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKKCIEVLIDKQYIERSQASADEYSYVA TTNJS0A ID TTNJS0A TTNJS0A TN HUMAN excitatory amino acid transporter 1 (EAAT1) TTNJS0A UP P43003 TTNJS0A UC EAA1_HUMAN TTNJS0A BC SLC1A3 subfamily TTNJS0A SN Solute carrier family 1 member 3; Sodium-dependent glutamate/aspartate transporter 1; GLAST-1 TTNJS0A GN SLC1A3; GLAST, GLAST1 TTNJS0A FC Human protein solute carrier family 1 member 3 interacts with SARS-CoV-2 M protein with high significance, which indicates SLC1A3 as a potential therapeutic target. TTNJS0A PD 5MJU; 5LM4; 5LLU; 5LLM TTNJS0A SQ MTKSNGEEPKMGGRMERFQQGVRKRTLLAKKKVQNITKEDVKSYLFRNAFVLLTVTAVIVGTILGFTLRPYRMSYREVKYFSFPGELLMRMLQMLVLPLIISSLVTGMAALDSKASGKMGMRAVVYYMTTTIIAVVIGIIIVIIIHPGKGTKENMHREGKIVRVTAADAFLDLIRNMFPPNLVEACFKQFKTNYEKRSFKVPIQANETLVGAVINNVSEAMETLTRITEELVPVPGSVNGVNALGLVVFSMCFGFVIGNMKEQGQALREFFDSLNEAIMRLVAVIMWYAPVGILFLIAGKIVEMEDMGVIGGQLAMYTVTVIVGLLIHAVIVLPLLYFLVTRKNPWVFIGGLLQALITALGTSSSSATLPITFKCLEENNGVDKRVTRFVLPVGATINMDGTALYEALAAIFIAQVNNFELNFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWFLDRLRTTTNVLGDSLGAGIVEHLSRHELKNRDVEMGNSVIEENEMKKPYQLIAQDNETEKPIDSETKM TTSN1YP ID TTSN1YP TTSN1YP TN HUMAN la-related protein 1 (LARP1) TTSN1YP UP Q6PKG0 TTSN1YP UC LARP1_HUMAN TTSN1YP BC LARP family TTSN1YP SN La ribonucleoprotein domain family member 1 TTSN1YP GN LARP1 TTSN1YP FC Human protein La ribonucleoprotein domain family member 1 interacts with SARS-CoV-2 N protein with high significance, which indicates LARP1 as a potential therapeutic target. TTSN1YP PD 4ZC4; 5C0V; 5V4R; 5V7C; 5V87 TTSN1YP SQ MATQVEPLLPGGATLLQAEEHGGLVRKKPPPAPEGKGEPGPNDVRGGEPDGSARRPRPPCAKPHKEGTGQQERESPRPLQLPGAEGPAISDGEEGGGEPGAGGGAAGAAGAGRRDFVEAPPPKVNPWTKNALPPVLTTVNGQSPPEHSAPAKVVRAAVPKQRKGSKVGDFGDAINWPTPGEIAHKSVQPQSHKPQPTRKLPPKKDMKEQEKGEGSDSKESPKTKSDESGEEKNGDEDCQRGGQKKKGNKHKWVPLQIDMKPEVPREKLASRPTRPPEPRHIPANRGEIKGSESATYVPVAPPTPAWQPEIKPEPAWHDQDETSSVKSDGAGGARASFRGRGRGRGRGRGRGRGGTRTHFDYQFGYRKFDGVEGPRTPKYMNNITYYFDNVSSTELYSVDQELLKDYIKRQIEYYFSVDNLERDFFLRRKMDADGFLPITLIASFHRVQALTTDISLIFAALKDSKVVEIVDEKVRRREEPEKWPLPPIVDYSQTDFSQLLNCPEFVPRQHYQKETESAPGSPRAVTPVPTKTEEVSNLKTLPKGLSASLPDLDSENWIEVKKRPRPSPARPKKSEESRFSHLTSLPQQLPSQQLMSKDQDEQEELDFLFDEEMEQMDGRKNTFTAWSDEESDYEIDDRDVNKILIVTQTPHYMRRHPGGDRTGNHTSRAKMSAELAKVINDGLFYYEQDLWAEKFEPEYSQIKQEVENFKKVNMISREQFDTLTPEPPVDPNQEVPPGPPRFQQVPTDALANKLFGAPEPSTIARSLPTTVPESPNYRNTRTPRTPRTPQLKDSSQTSRFYPVVKEGRTLDAKMPRKRKTRHSSNPPLESHVGWVMDSREHRPRTASISSSPSEGTPTVGSYGCTPQSLPKFQHPSHELLKENGFTQHVYHKYRRRCLNERKRLGIGQSQEMNTLFRFWSFFLRDHFNKKMYEEFKQLALEDAKEGYRYGLECLFRYYSYGLEKKFRLDIFKDFQEETVKDYEAGQLYGLEKFWAFLKYSKAKNLDIDPKLQEYLGKFRRLEDFRVDPPMGEEGNHKRHSVVAGGGGGEGRKRCPSQSSSRPAAMISQPPTPPTGQPVREDAKWTSQHSNTQTLGK TTQHNAM ID TTQHNAM TTQHNAM TN HUMAN lysyl oxidase (LOX) TTQHNAM UP P28300 TTQHNAM UC LYOX_HUMAN TTQHNAM BC CH-NH(2) donor oxidoreductase TTQHNAM SN Protein-lysine 6-oxidase TTQHNAM GN LOX TTQHNAM FC Human protein lysyl oxidase interacts with SARS-CoV-2 Orf8 protein with high significance, which indicates LOX as a potential therapeutic target. TTQHNAM EC EC 1.4.3.13 TTQHNAM SQ MRFAWTVLLLGPLQLCALVHCAPPAAGQQQPPREPPAAPGAWRQQIQWENNGQVFSLLSLGSQYQPQRRRDPGAAVPGAANASAQQPRTPILLIRDNRTAAARTRTAGSSGVTAGRPRPTARHWFQAGYSTSRAREAGASRAENQTAPGEVPALSNLRPPSRVDGMVGDDPYNPYKYSDDNPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAAEENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY TTBYJ39 ID TTBYJ39 TTBYJ39 TN HUMAN NADH:ubiquinone oxidoreductase subunit B9 (NDUFB9) TTBYJ39 UP Q9Y6M9 TTBYJ39 UC NDUB9_HUMAN TTBYJ39 BC Complex I LYR family TTBYJ39 SN NADH-ubiquinone oxidoreductase B22 subunit; NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9; LYR motif-containing protein 3; Complex I-B22; CI-B22 TTBYJ39 GN NDUFB9 TTBYJ39 FC Human protein NADH:ubiquinone oxidoreductase subunit B9 interacts with SARS-CoV-2 Orf9c protein with high significance, which indicates NDUFB9 as a potential therapeutic target. TTBYJ39 PD 5XTC; 5XTD; 5XTH; 5XTI TTBYJ39 SQ MAFLASGPYLTHQQKVLRLYKRALRHLESWCVQRDKYRYFACLMRARFEEHKNEKDMAKATQLLKEAEEEFWYRQHPQPYIFPDSPGGTSYERYDCYKVPEWCLDDWHPSEKAMYPDYFAKREQWKKLRRESWEREVKQLQEETPPGGPLTEALPPARKEGDLPPLWWYIVTRPRERPM TTWU04I ID TTWU04I TTWU04I TN HUMAN prostaglandin E synthase 2 (PTGES2) TTWU04I UP Q9H7Z7 TTWU04I UC PGES2_HUMAN TTWU04I BC GST superfamily TTWU04I SN Prostaglandin-H(2) E-isomerase; mPGES-2; mPGE synthase-2 ; Microsomal prostaglandin E synthase 2; Membrane-associated prostaglandin E synthase-2 TTWU04I GN PTGES2 TTWU04I FC Human protein prostaglandin E synthase 2 interacts with SARS-CoV-2 Nsp7 protein with high significance, which indicates PTGES2 as a potential therapeutic target. TTWU04I EC EC 5.3.99.3 TTWU04I SQ MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLGAAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRAFLDFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQPLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADDWLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAITEASPAH TTD3TZ2 ID TTD3TZ2 TTD3TZ2 TN HUMAN proteinase activated receptor 2 (PAR2) TTD3TZ2 UP P55085 TTD3TZ2 UC PAR2_HUMAN TTD3TZ2 BC GPCR rhodopsin TTD3TZ2 SN Thrombin receptor-like 1; Proteinase-activated receptor-2; Proteinase-activated receptor 2; Protease activated receptor 2; PAR-2; GPR11; G-protein coupled receptor 11; Coagulation factor II receptor-like 1 TTD3TZ2 GN F2RL1 TTD3TZ2 FC Human protein F2R like trypsin receptor 1 interacts with SARS-CoV-2 Orf9c protein with high significance, which indicates F2RL1 as a potential therapeutic target. TTD3TZ2 PD 5NJ6; 5NDZ; 5NDD TTD3TZ2 SQ MRSPSAAWLLGAAILLAASLSCSGTIQGTNRSSKGRSLIGKVDGTSHVTGKGVTVETVFSVDEFSASVLTGKLTTVFLPIVYTIVFVVGLPSNGMALWVFLFRTKKKHPAVIYMANLALADLLSVIWFPLKIAYHIHGNNWIYGEALCNVLIGFFYGNMYCSILFMTCLSVQRYWVIVNPMGHSRKKANIAIGISLAIWLLILLVTIPLYVVKQTIFIPALNITTCHDVLPEQLLVGDMFNYFLSLAIGVFLFPAFLTASAYVLMIRMLRSSAMDENSEKKRKRAIKLIVTVLAMYLICFTPSNLLLVVHYFLIKSQGQSHVYALYIVALCLSTLNSCIDPFVYYFVSHDFRDHAKNALLCRSVRTVKQMQVSLTSKKHSRKSSSYSSSSTTVKTSY TT2Q719 ID TT2Q719 TT2Q719 TN HUMAN vacuolar-type proton ATPase catalytic A (v-ATPase-A) TT2Q719 UP P38606 TT2Q719 UC VATA_HUMAN TT2Q719 BC Acid anhydrides hydrolase TT2Q719 SN Vacuolar proton pump subunit alpha; Vacuolar ATPase isoform VA68; VPP2; V-ATPase subunit A; V-ATPase 69 kDa subunit; ATP6V1A1; ATP6V1A; ATP6A1 TT2Q719 GN ATP6V1A TT2Q719 FC Human protein ATPase H+ transporting V1 subunit A interacts with SARS-CoV-2 M protein with high significance, which indicates ATP6V1A as a potential therapeutic target. TT2Q719 EC EC 7.1.2.2 TT2Q719 SQ MDFSKLPKILDEDKESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWDFTPCKNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTYIAPPGNYDTSDVVLELEFEGVKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDNKITWSIIREHMGDILYKLSSMKFKDPLKDGEAKIKSDYAQLLEDMQNAFRSLED TTWDM4U ID TTWDM4U TTWDM4U TN HUMAN ATPase H+ transporting accessory protein 1 (ATP6AP1) TTWDM4U UP Q15904 TTWDM4U UC VAS1_HUMAN TTWDM4U BC Vacuolar ATPase subunit S1 family TTWDM4U SN V-type proton ATPase subunit S1; V-ATPase subunit S1; V-ATPase S1 accessory protein; V-ATPase Ac45 subunit; Vacuolar proton pump subunit S1; Protein XAP-3 TTWDM4U GN ATP6AP1 TTWDM4U FC Human protein ATPase H+ transporting accessory protein 1 interacts with SARS-CoV-2 Nsp6 protein with high significance, which indicates ATP6AP1 as a potential therapeutic target. TTWDM4U SQ MMAAMATARVRMGPRCAQALWRMPWLPVFLSLAAAAAAAAAEQQVPLVLWSSDRDLWAPAADTHEGHITSDLQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAVSTLTTYLQEKLGASPLHVDLATLRELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLKSEDVPYTAALTAVRPSRVARDVAVVAGGLGRQLLQKQPVSPVIHPPVSYNDTAPRILFWAQNFSVAYKDQWEDLTPLTFGVQELNLTGSFWNDSFARLSLTYERLFGTTVTFKFILANRLYPVSARHWFTMERLEVHSNGSVAYFNASQVTGPSIYSFHCEYVSSLSKKGSLLVARTQPSPWQMMLQDFQIQAFNVMGEQFSYASDCASFFSPGIWMGLLTSLFMLFIFTYGLHMILSLKTMDRFDDHKGPTISLTQIV TTZ1YIS ID TTZ1YIS TTZ1YIS TN HUMAN dCTP pyrophosphatase 1 TTZ1YIS UP Q9H773 TTZ1YIS UC DCTP1_HUMAN TTZ1YIS SN XTP3-transactivated gene A protein ; RS21C6 ; Deoxycytidine-triphosphatase 1; dCTPase 1 TTZ1YIS GN DCTPP1 TTZ1YIS FC Human protein dCTP pyrophosphatase 1 interacts with SARS-CoV-2 Orf9b protein with high significance, which indicates DCTPP1 as a potential therapeutic target. TTZ1YIS EC EC 3.6.1.12 TTZ1YIS SQ MSVAGGEIRGDTGGEDTAAPGRFSFSPEPTLEDIRRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGPQGWSPRERAALQEELSDVLIYLVALAARCRVDLPLAVLSKMDINRRRYPAHLARSSSRKYTELPHGAISEDQAVGPADIPCDSTGQTST TT2ZSKV ID TT2ZSKV TT2ZSKV TN HUMAN eukaryotic translation initiation factor 4E family member 2 (EIF4E2) TT2ZSKV UP Q53RG0 TT2ZSKV UC Q53RG0_HUMAN TT2ZSKV BC Eukaryotic initiation factor 4E family TT2ZSKV SN 4EHP; IF4e; 4E-LP; h4EHP; EIF4EL3 TT2ZSKV GN EIF4E2 TT2ZSKV FC Human protein eukaryotic translation initiation factor 4E family member 2 interacts with SARS-CoV-2 Nsp2? protein with high significance, which indicates EIF4E2 as a potential therapeutic target. TT2ZSKV SQ MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP TT4P8O2 ID TT4P8O2 TT4P8O2 TN HUMAN FK506 binding protein 10 (FKBP10) TT4P8O2 UP Q96AY3 TT4P8O2 UC FKB10_HUMAN TT4P8O2 SN Rotamase; PPIase FKBP10; Peptidyl-prolyl cis-trans isomerase FKBP10; Immunophilin FKBP65; FKBP-65; FKBP-10; FK506-binding protein 10; 65 kDa FKBP; 65 kDa FK506-binding protein TT4P8O2 GN FKBP10 TT4P8O2 FC Human protein FK506 binding protein 10 interacts with SARS-CoV-2 Orf8 protein with high significance, which indicates FKBP10 as a potential therapeutic target. TT4P8O2 EC EC 5.2.1.8 TT4P8O2 SQ MFPAGPPSHSLLRLPLLQLLLLVVQAVGRGLGRASPAGGPLEDVVIERYHIPRACPREVQMGDFVRYHYNGTFEDGKKFDSSYDRNTLVAIVVGVGRLITGMDRGLMGMCVNERRRLIVPPHLGYGSIGLAGLIPPDATLYFDVVLLDVWNKEDTVQVSTLLRPPHCPRMVQDGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSGWLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGYGTVIPPQASLVFHVLLIDVHNPKDAVQLETLELPPGCVRRAGAGDFMRYHYNGSLMDGTLFDSSYSRNHTYNTYIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENGTGDKIPGSAVLIFNVHVIDFHNPADVVEIRTLSRPSETCNETTKLGDFVRYHYNCSLLDGTQLFTSHDYGAPQEATLGANKVIEGLDTGLQGMCVGERRQLIVPPHLAHGESGARGVPGSAVLLFEVELVSREDGLPTGYLFVWHKDPPANLFEDMDLNKDGEVPPEEFSTFIKAQVSEGKGRLMPGQDPEKTIGDMFQNQDRNQDGKITVDELKLKSDEDEERVHEEL TT1XEQO ID TT1XEQO TT1XEQO TN HUMAN FK506 binding protein 15 (FKBP15) TT1XEQO UP Q5T1M5 TT1XEQO UC FKB15_HUMAN TT1XEQO BC FKBP-type PPIase family TT1XEQO SN WASP- and FKBP-like protein; WAFL; FKBP-15; FKBP-133; FK506-binding protein 15; 133 kDa FKBP; 133 kDa FK506-binding protein TT1XEQO GN FKBP15 TT1XEQO FC Human protein FK506 binding protein 15 interacts with SARS-CoV-2 Nsp2 protein with high significance, which indicates FKBP15 as a potential therapeutic target. TT1XEQO SQ MFGAGDEDDTDFLSPSGGARLASLFGLDQAAAGHGNEFFQYTAPKQPKKGQGTAATGNQATPKTAPATMSTPTILVATAVHAYRYTNGQYVKQGKFGAAVLGNHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQRQNWSIMFESEKAAVEFNKQVCIAKCNSTSSLDAVLSQDLIVADGPAVEVGDSLEVAYTGWLFQNHVLGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGWTQATDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSNSLSEQLAINTSPDAVKAKLISRMAKMGQPMLPILPPQLDSNDSEIEDVNTLQGGGQPVVTPSVQPSLHPAHPALPQMTSQAPQPSVTGLQAPSAALMQVSSLDSHSAVSGNAQSFQPYAGMQAYAYPQASAVTSQLQPVRPLYPAPLSQPPHFQGSGDMASFLMTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRTILGTIMNTIKMVTLQLLNQQEQEKEESSSEEEEEKAEERPRRPSQEQSASASSGQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGHRRKGDSEAEALSEIKDGSLPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPDGPLQESSTRLSLTSDPEEGDPLALGPESPGEPQPPQLKKDDVTSSTGPHKELSSTEAGSTVAGAALRPSHHSQRSSLSGDEEDELFKGATLKALRPKAQPEEEDEDEVSMKGRPPPTPLFGDDDDDDDIDWLG TTO1ENI ID TTO1ENI TTO1ENI TN HUMAN FK506 binding protein 7 (FKBP7) TTO1ENI UP Q9Y680 TTO1ENI UC FKBP7_HUMAN TTO1ENI SN Rotamase; PPIase FKBP7; Peptidyl-prolyl cis-trans isomerase FKBP7; FKBP-7; FKBP-23; FK506-binding protein 7; 23 kDa FKBP; 23 kDa FK506-binding protein TTO1ENI GN FKBP7 TTO1ENI FC Human protein FK506 binding protein 7 interacts with SARS-CoV-2 Orf8 protein with high significance, which indicates FKBP7 as a potential therapeutic target. TTO1ENI EC EC 5.2.1.8 TTO1ENI SQ MPKTMHFLFRFIVFFYLWGLFTAQRQKKEESTEEVKIEVLHRPENCSKTSKKGDLLNAHYDGYLAKDGSKFYCSRTQNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYAEGKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLQREFEKDEKPRDKSYQDAVLEDIFKKNDHDGDGFISPKEYNVYQHDEL TT8MEUD ID TT8MEUD TT8MEUD TN HUMAN lysyl hydroxylase 2 (LH2) TT8MEUD UP O00469 TT8MEUD UC PLOD2_HUMAN TT8MEUD SN Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 TT8MEUD GN PLOD2 TT8MEUD FC Human protein procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 interacts with SARS-CoV-2 Orf8 protein with high significance, which indicates PLOD2 as a potential therapeutic target. TT8MEUD EC EC 1.14.11.4 TT8MEUD SQ MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPTDKLLVITVATKESDGFHRFMQSAKYFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGYAPYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAINGNGPTKILLNYFGNYVPNSWTQDNGCTLCEFDTVDLSAVDVHPNVSIGVFIEQPTPFLPRFLDILLTLDYPKEALKLFIHNKEVYHEKDIKVFFDKAKHEIKTIKIVGPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTRHGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGVWNVPYMANVYLIKGKTLRSEMNERNYFVRDKLDPDMALCRNAREMGVFMYISNRHEFGRLLSTANYNTSHYNNDLWQIFENPVDWKEKYINRDYSKIFTENIVEQPCPDVFWFPIFSEKACDELVEEMEHYGKWSGGKHHDSRISGGYENVPTDDIHMKQVDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQRSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEGLPVKNGTRYIAVSFIDP TTCHGVF ID TTCHGVF TTCHGVF TN HUMAN NADH:ubiquinone oxidoreductase complex assembly factor 2 (NDUFAF2) TTCHGVF UP Q8N183 TTCHGVF UC NDUF2_HUMAN TTCHGVF BC Complex I NDUFA12 subunit family TTCHGVF SN NDUFA12-like protein; NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2; Myc-induced mitochondrial protein ; MMTN ; Mimitin ; B17.2-like; B17.2L TTCHGVF GN NDUFAF2 TTCHGVF FC Human protein NADH:ubiquinone oxidoreductase complex assembly factor 2 interacts with SARS-CoV-2 Nsp7 protein with high significance, which indicates NDUFAF2 as a potential therapeutic target. TTCHGVF SQ MGWSQDLFRALWRSLSREVKEHVGTDQFGNKYYYIPQYKNWRGQTIREKRIVEAANKKEVDYEAGDIPTEWEAWIRRTRKTPPTMEEILKNEKHREEIKIKSQDFYEKEKLLSKETSEELLPPPVQTQIKGHASAPYFGKEEPSVAPSSTGKTFQPGSWMPRDGKSHNQ TT4LRUE ID TT4LRUE TT4LRUE TN HUMAN solute carrier family 6 member 15 (SLC6A15) TT4LRUE UP Q9H2J7 TT4LRUE UC S6A15_HUMAN TT4LRUE BC SLC6A15 subfamily TT4LRUE SN Transporter v7-3; Sodium-dependent neutral amino acid transporter B(0)AT2; Sodium-coupled branched-chain amino-acid transporter 1; Sodium- and chloride-dependent neurotransmitter transporter NTT73 TT4LRUE GN SLC6A15 TT4LRUE FC Human protein solute carrier family 6 member 15 interacts with SARS-CoV-2 Nsp6 protein with high significance, which indicates SLC6A15 as a potential therapeutic target. TT4LRUE SQ MPKNSKVVKRELDDDVTESVKDLLSNEDAADDAFKTSELIVDGQEEKDTDVEEGSEVEDERPAWNSKLQYILAQVGFSVGLGNVWRFPYLCQKNGGGAYLLPYLILLMVIGIPLFFLELSVGQRIRRGSIGVWNYISPKLGGIGFASCVVCYFVALYYNVIIGWSLFYFSQSFQQPLPWDQCPLVKNASHTFVEPECEQSSATTYYWYREALNISSSISESGGLNWKMTICLLAAWVMVCLAMIKGIQSSGKIIYFSSLFPYVVLICFLIRAFLLNGSIDGIRHMFTPKLEIMLEPKVWREAATQVFFALGLGFGGVIAFSSYNKRDNNCHFDAVLVSFINFFTSVLATLVVFAVLGFKANVINEKCITQNSETIMKFLKMGNISQDIIPHHINLSTVTAEDYHLVYDIIQKVKEEEFPALHLNSCKIEEELNKAVQGTGLAFIAFTEAMTHFPASPFWSVMFFLMLVNLGLGSMFGTIEGIVTPIVDTFKVRKEILTVICCLLAFCIGLIFVQRSGNYFVTMFDDYSATLPLLIVVILENIAVCFVYGIDKFMEDLKDMLGFAPSRYYYYMWKYISPLMLLSLLIASVVNMGLSPPGYNAWIEDKASEEFLSYPTWGLVVCVSLVVFAILPVPVVFIVRRFNLIDDSSGNLASVTYKRGRVLKEPVNLEGDDTSLIHGKIPSEMPSPNFGKNIYRKQSGSPTLDTAPNGRYGIGYLMADIMPDMPESDL TTPOA6U ID TTPOA6U TTPOA6U TN HUMAN centrosomal protein 250 (Cep250) TTPOA6U UP Q9BV73 TTPOA6U UC CP250_HUMAN TTPOA6U SN C-Nap1; Centrosome-associated protein CEP250; Centrosomal protein 2; Centrosomal Nek2-associated protein 1; 250 kDa centrosomal protein TTPOA6U GN CEP250 TTPOA6U FC Human protein centrosomal protein 250 interacts with SARS-CoV-2 Nsp13 protein with high significance, which indicates CEP250 as a potential therapeutic target. TTPOA6U SQ METRSPGLNNMKPQSLQLVLEEQVLALQQQMAENQAASWRKLKNSQEAQQRQATLVRKLQAKVLQYRSWCQELEKRLEATGGPIPQRWENVEEPNLDELLVRLEEEQQRCESLAEVNTQLRLHMEKADVVNKALREDVEKLTVDWSRARDELMRKESQWQMEQEFFKGYLKGEHGRLLSLWREVVTFRRHFLEMKSATDRDLMELKAEHVRLSGSLLTCCLRLTVGAQSREPNGSGRMDGREPAQLLLLLAKTQELEKEAHERSQELIQLKSQGDLEKAELQDRVTELSALLTQSQKQNEDYEKMIKALRETVEILETNHTELMEHEASLSRNAQEEKLSLQQVIKDITQVMVEEGDNIAQGSGHENSLELDSSIFSQFDYQDADKALTLVRSVLTRRRQAVQDLRQQLAGCQEAVNLLQQQHDQWEEEGKALRQRLQKLTGERDTLAGQTVDLQGEVDSLSKERELLQKAREELRQQLEVLEQEAWRLRRVNVELQLQGDSAQGQKEEQQEELHLAVRERERLQEMLMGLEAKQSESLSELITLREALESSHLEGELLRQEQTEVTAALARAEQSIAELSSSENTLKTEVADLRAAAVKLSALNEALALDKVGLNQQLLQLEEENQSVCSRMEAAEQARNALQVDLAEAEKRREALWEKNTHLEAQLQKAEEAGAELQADLRDIQEEKEEIQKKLSESRHQQEAATTQLEQLHQEAKRQEEVLARAVQEKEALVREKAALEVRLQAVERDRQDLAEQLQGLSSAKELLESSLFEAQQQNSVIEVTKGQLEVQIQTVTQAKEVIQGEVRCLKLELDTERSQAEQERDAAARQLAQAEQEGKTALEQQKAAHEKEVNQLREKWEKERSWHQQELAKALESLEREKMELEMRLKEQQTEMEAIQAQREEERTQAESALCQMQLETEKERVSLLETLLQTQKELADASQQLERLRQDMKVQKLKEQETTGILQTQLQEAQRELKEAARQHRDDLAALQEESSSLLQDKMDLQKQVEDLKSQLVAQDDSQRLVEQEVQEKLRETQEYNRIQKELEREKASLTLSLMEKEQRLLVLQEADSIRQQELSALRQDMQEAQGEQKELSAQMELLRQEVKEKEADFLAQEAQLLEELEASHITEQQLRASLWAQEAKAAQLQLRLRSTESQLEALAAEQQPGNQAQAQAQLASLYSALQQALGSVCESRPELSGGGDSAPSVWGLEPDQNGARSLFKRGPLLTALSAEAVASALHKLHQDLWKTQQTRDVLRDQVQKLEERLTDTEAEKSQVHTELQDLQRQLSQNQEEKSKWEGKQNSLESELMELHETMASLQSRLRRAELQRMEAQGERELLQAAKENLTAQVEHLQAAVVEARAQASAAGILEEDLRTARSALKLKNEEVESERERAQALQEQGELKVAQGKALQENLALLTQTLAEREEEVETLRGQIQELEKQREMQKAALELLSLDLKKRNQEVDLQQEQIQELEKCRSVLEHLPMAVQEREQKLTVQREQIRELEKDRETQRNVLEHQLLELEKKDQMIESQRGQVQDLKKQLVTLECLALELEENHHKMECQQKLIKELEGQRETQRVALTHLTLDLEERSQELQAQSSQIHDLESHSTVLARELQERDQEVKSQREQIEELQRQKEHLTQDLERRDQELMLQKERIQVLEDQRTRQTKILEEDLEQIKLSLRERGRELTTQRQLMQERAEEGKGPSKAQRGSLEHMKLILRDKEKEVECQQEHIHELQELKDQLEQQLQGLHRKVGETSLLLSQREQEIVVLQQQLQEAREQGELKEQSLQSQLDEAQRALAQRDQELEALQQEQQQAQGQEERVKEKADALQGALEQAHMTLKERHGELQDHKEQARRLEEELAVEGRRVQALEEVLGDLRAESREQEKALLALQQQCAEQAQEHEVETRALQDSWLQAQAVLKERDQELEALRAESQSSRHQEEAARARAEALQEALGKAHAALQGKEQHLLEQAELSRSLEASTATLQASLDACQAHSRQLEEALRIQEGEIQDQDLRYQEDVQQLQQALAQRDEELRHQQEREQLLEKSLAQRVQENMIQEKQNLGQEREEEEIRGLHQSVRELQLTLAQKEQEILELRETQQRNNLEALPHSHKTSPMEEQSLKLDSLEPRLQRELERLQAALRQTEAREIEWREKAQDLALSLAQTKASVSSLQEVAMFLQASVLERDSEQQRLQDELELTRRALEKERLHSPGATSTAELGSRGEQGVQLGEVSGVEAEPSPDGMEKQSWRQRLEHLQQAVARLEIDRSRLQRHNVQLRSTLEQVERERRKLKREAMRAAQAGSLEISKATASSPTQQDGRGQKNSDAKCVAELQKEVVLLQAQLTLERKQKQDYITRSAQTSRELAGLHHSLSHSLLAVAQAPEATVLEAETRRLDESLTQSLTSPGPVLLHPSPSTTQAASR TTJSZTB ID TTJSZTB TTJSZTB TN Nicotinic acetylcholine receptor (nAChR) TTJSZTB UP Family TTJSZTB UC NOUNIPROTAC TTJSZTB BC Ion transport TTJSZTB SN nAChR; Nicotinergic acetylcholine receptor TTJSZTB GN NO-GeName TTJSZTB FC After binding acetylcholine, the AChRresponds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. TTJSZTB TT Successful TTJSZTB KE hsa04080:Neuroactive ligand-receptor interaction TTJSZTB RC R-HSA-629587:Highly sodium permeable acetylcholine nicotinic receptors; R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors TTDP1UC ID TTDP1UC TTDP1UC TN Fatty acid amide hydrolase (FAAH) TTDP1UC UP Family TTDP1UC UC NOUNIPROTAC TTDP1UC SN Oleamidehydrolase; Anandamide amidohydrolase TTDP1UC GN NO-GeName TTDP1UC FC Degradesbioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates. TTDP1UC TT Successful TTDP1UC FM Carbon nitrogen hydrolase TTDP1UC KE hsa04723:Retrograde endocannabinoid signaling TTAN6JD ID TTAN6JD TTAN6JD TN Glutamate receptor AMPA (GRIA) TTAN6JD UP Family TTAN6JD UC NOUNIPROTAC TTAN6JD BC Chloride channel TTAN6JD SN Glutamate receptor ionotropic, AMPA; Glutamate receptor; AMPA selective glutamate receptor; AMPA receptor TTAN6JD GN NO-GeName TTAN6JD TT Successful TTAJU0S ID TTAJU0S TTAJU0S TN Interleukin 2 receptor (IL2R) TTAJU0S UP Family TTAJU0S UC NOUNIPROTAC TTAJU0S BC Cytokine receptor TTAJU0S SN p64; gammaC; Interleukin2 receptor subunit gamma; Interleukin-2 receptor subunit gamma; IL2R subunit gamma; IL2 receptor subunit gamma; IL-2RG; IL-2R subunit gamma; IL-2R; IL-2 receptor subunit gamma; Cytokine receptor common subunit gamma; CD132 TTAJU0S GN NO-GeName TTAJU0S FC Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15. Common subunit for the receptors for a variety of interleukins. TTAJU0S TT Successful TTAJU0S KE hsa04060:Cytokine-cytokine receptor interaction; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05162:Measles; hsa05166:HTLV-I infection TTAJU0S RC R-HSA-114604:GPVI-mediated activation cascade; R-HSA-1266695:Interleukin-7 signaling; R-HSA-392451:G beta:gamma signalling through PI3Kgamma; R-HSA-451927:Interleukin-2 signaling; R-HSA-5673001:RAF/MAP kinase cascade; R-HSA-912526:Interleukin receptor SHC signaling TTRK8B9 ID TTRK8B9 TTRK8B9 TN Sodium channel unspecific (NaC) TTRK8B9 UP Family TTRK8B9 UC NOUNIPROTAC TTRK8B9 GN NO-GeName TTRK8B9 FC Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. TTRK8B9 TT Successful TTRK8B9 KE hsa04728:Dopaminergic synapse TTRK8B9 RC R-HSA-445095:Interaction between L1 and Ankyrins TTYFKSZ ID TTYFKSZ TTYFKSZ TN Tubulin beta (TUBB) TTYFKSZ UP Family TTYFKSZ UC NOUNIPROTAC TTYFKSZ BC Tubulin family TTYFKSZ SN Major cysteine proteinase; Cysteine proteinase cruzipain; Cruzaine; Congopain; Beta-tubulin TTYFKSZ GN NO-GeName TTYFKSZ FC Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TTYFKSZ TT Successful TTYFKSZ KE hsa04145:Phagosome; hsa04540:Gap junction; hsa05130:Pathogenic Escherichia coli infection TTYFKSZ RC R-HSA-2565942:Regulation of PLK1 Activity at G2/M Transition; R-HSA-380259:Loss of Nlp from mitotic centrosomes; R-HSA-380270:Recruitment of mitotic centrosome proteins and complexes; R-HSA-380284:Loss of proteins required for interphase microtubule organization?from the centrosome; R-HSA-5620912:Anchoring of the basal body to the plasma membrane TTYSN63 ID TTYSN63 TTYSN63 TN 5-HT 2 receptor (5HT2R) TTYSN63 UP Family TTYSN63 UC NOUNIPROTAC TTYSN63 BC GPCR rhodopsin TTYSN63 SN Serotonin receptor 2; 5-hydroxytryptamine receptor 2; 5-HT2 receptor TTYSN63 GN NO-GeName TTYSN63 FC G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5- dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions from intracellular stores. Affects neural activity, perception, cognition and mood. Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction. TTYSN63 TT Successful TTYSN63 KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04726:Serotonergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels TTNXLKE ID TTNXLKE TTNXLKE TN 5-HT 3 receptor (5HT3R) TTNXLKE UP Family TTNXLKE UC NOUNIPROTAC TTNXLKE BC GPCR rhodopsin TTNXLKE SN 5-hydroxytryptamine receptor type 3; 5-hydroxytryptamine receptor 3; 5-HT3R; 5-HT3 receptor; 5-HT-3 TTNXLKE GN NO-GeName TTNXLKE FC This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel. TTNXLKE TT Successful TTG28O6 ID TTG28O6 TTG28O6 TN Adrenergic receptor Alpha-1 (ADRA1) TTG28O6 UP Family TTG28O6 UC NOUNIPROTAC TTG28O6 BC GPCR rhodopsin TTG28O6 SN Alpha1-adrenoceptor; Alpha(1)-adrenoceptor TTG28O6 GN NO-GeName TTG28O6 TT Successful TTMNI76 ID TTMNI76 TTMNI76 TN Calcium-activated potassium channel (KCN) TTMNI76 UP Family TTMNI76 UC NOUNIPROTAC TTMNI76 SN Ca-activated K channel TTMNI76 GN NO-GeName TTMNI76 FC Forms a voltage-independent potassium channel that is activated by intracellular calcium. activation is followed by membrane hyperpolarization which promotes calcium influx. The channel is blocked by clotrimazole and charybdotoxin. TTMNI76 TT Successful TTHQENC ID TTHQENC TTHQENC TN Phosphodiesterase 1 (PDE1) TTHQENC UP Family TTHQENC UC NOUNIPROTAC TTHQENC BC Phosphoric diester hydrolase TTHQENC SN PDE-I; Cam-PDE 1 TTHQENC GN NO-GeName TTHQENC FC Has a higher affinity for cgmp than for camp. TTHQENC TT Successful TTV5CGO ID TTV5CGO TTV5CGO TN Phosphodiesterase 4 (PDE4) TTV5CGO UP Family TTV5CGO UC NOUNIPROTAC TTV5CGO BC Phosphoric diester hydrolase TTV5CGO SN PDE-4 TTV5CGO GN NO-GeName TTV5CGO FC Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes||Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents TTV5CGO TT Successful TTML2WA ID TTML2WA TTML2WA TN Tubulin (TUB) TTML2WA UP Family TTML2WA UC NOUNIPROTAC TTML2WA SN Human tubulin TTML2WA GN NO-GeName TTML2WA FC Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TUBB3 plays a critical role in proper axon guidance and mantainance. TTML2WA TT Successful TTML2WA FM Tubulin TT85JO3 ID TT85JO3 TT85JO3 TN 5-HT receptor (5HTR) TT85JO3 UP Family TT85JO3 UC NOUNIPROTAC TT85JO3 BC GPCR rhodopsin TT85JO3 SN 5-Hydroxytryptamine receptor TT85JO3 GN NO-GeName TT85JO3 TT Successful TTSLI08 ID TTSLI08 TTSLI08 TN Adenosine receptor (ADOR) TTSLI08 UP Family TTSLI08 UC NOUNIPROTAC TTSLI08 BC GPCR rhodopsin TTSLI08 SN P1 receptor TTSLI08 GN NO-GeName TTSLI08 TT Successful TTQ8AFT ID TTQ8AFT TTQ8AFT TN Adrenergic receptor Alpha-2 (ADRA2) TTQ8AFT UP Family TTQ8AFT UC NOUNIPROTAC TTQ8AFT BC GPCR rhodopsin TTQ8AFT SN Alpha-2 adrenergic receptor; Alpha(2)-adrenoceptor TTQ8AFT GN NO-GeName TTQ8AFT TT Successful TTUNARX ID TTUNARX TTUNARX TN Carbonic anhydrase (CA) TTUNARX UP Family TTUNARX UC NOUNIPROTAC TTUNARX SN Carbonate dehydratase TTUNARX GN NO-GeName TTUNARX TT Successful TTUNARX FM Carbon-oxygen lyases TTHVCUP ID TTHVCUP TTHVCUP TN DNA [cytosine-5]-methyltransferase (DNMT) TTHVCUP UP Family TTHVCUP UC NOUNIPROTAC TTHVCUP SN DNA MTase TTHVCUP GN NO-GeName TTHVCUP FC This methylase recognizes the double-stranded sequence ccwgg, causes specific methylation on c-2 on both strands. TTHVCUP TT Successful TTHVCUP FM Class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family TTQOD3G ID TTQOD3G TTQOD3G TN Folate receptor (FOLR) TTQOD3G UP Family TTQOD3G UC NOUNIPROTAC TTQOD3G BC Folate receptor TTQOD3G SN FR; FOLR TTQOD3G GN NO-GeName TTQOD3G FC Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate to the interior of cells. Isoform short does not bind folate. TTQOD3G TT Successful TT6HPVC ID TT6HPVC TT6HPVC TN Guanylate cyclase (GC) TT6HPVC UP Family TT6HPVC UC NOUNIPROTAC TT6HPVC BC Phosphorus-oxygen lyase TT6HPVC SN Guanylyl Cyclase TT6HPVC GN NO-GeName TT6HPVC TT Successful TTBH0VX ID TTBH0VX TTBH0VX TN Histone deacetylase (HDAC) TTBH0VX UP Family TTBH0VX UC NOUNIPROTAC TTBH0VX SN Human histone deacetylase TTBH0VX GN NO-GeName TTBH0VX FC Responsible for the deacetylation of lysine residues on the n-terminal part of the core histones (H2a, H2b, H3 and H4). Histone deacetylation givesa tag for epigenetic repression and plays an important role in transcriptional regulation. TTBH0VX TT Successful TTBH0VX FM Histone deacetylase family TT95SOA ID TT95SOA TT95SOA TN Interferon alpha (IFNA) TT95SOA UP Family TT95SOA UC NOUNIPROTAC TT95SOA SN IFN-A TT95SOA GN NO-GeName TT95SOA FC Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. TT95SOA TT Successful TT95SOA KE hsa04060:Cytokine-cytokine receptor interaction; hsa04140:Regulation of autophagy; hsa04151:PI3K-Akt signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04630:Jak-STAT signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05168:Herpes simplex infection; hsa05320:Autoimmune thyroid disease TT95SOA RC R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912694:Regulation of IFNA signaling; R-HSA-933541:TRAF6 mediated IRF7 activation; R-HSA-983231:Factors involved in megakaryocyte development and platelet production TT5L2VC ID TT5L2VC TT5L2VC TN Kallikrein-related peptidase (KLK) TT5L2VC UP Family TT5L2VC UC NOUNIPROTAC TT5L2VC BC Peptidase TT5L2VC SN Human kallikrein TT5L2VC GN NO-GeName TT5L2VC TT Successful TT5L2VC FM Peptidase S1 family TTROQ37 ID TTROQ37 TTROQ37 TN MAPK/ERK kinase kinase (MAP3K) TTROQ37 UP Family TTROQ37 UC NOUNIPROTAC TTROQ37 BC Kinase TTROQ37 GN NO-GeName TTROQ37 FC Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leadingto their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator- activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis. TTROQ37 TT Successful TTROQ37 KE hsa04010:MAPK signaling pathway; hsa04012:ErbB signaling pathway; hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04068:FoxO signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04114:Oocyte meiosis; hsa04151:PI3K-Akt signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04320:Dorso-ventral axis formation; hsa04370:VEGF signaling pathway; hsa04380:Osteoclast differentiation; hsa04510:Focal adhesion; hsa04540:Gap junction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04620:Toll-like receptor signaling pathway; hsa04650:Natural killer cell mediated cytotoxicity; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa04666:Fc gamma R-mediated phagocytosis; hsa04668:TNF signaling pathway; hsa04720:Long-term potentiation; hsa04722:Neurotrophin signaling pathway; hsa04725:Cholinergic synapse; hsa04726:Serotonergic synapse; hsa04730:Long-term depression; hsa04810:Regulation of actin cytoskeleton; hsa04910:Insulin signaling pathway; hsa04912:GnRH signaling pathway; hsa04914:Progesterone-mediated oocyte maturation; hsa04915:Estrogen signaling pathway; hsa04916:Melanogenesis; hsa04917:Prolactin signaling pathway; hsa04919:Thyroid hormone signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05020:Prion diseases; hsa05034:Alcoholism; hsa05161:Hepatitis B; hsa05164:Influenza A; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer; hsa05210:Colorectal cancer; hsa05211:Renal cell carcinoma; hsa05212:Pancreatic cancer; hsa05213:Endometrial cancer; hsa05214:Glioma; hsa05215:Prostate cancer; hsa05216:Thyroid cancer; hsa05218:Melanoma; hsa05219:Bladder cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05223:Non-small cell lung cancer; hsa05230:Central carbon metabolism in cancer; hsa05231:Choline metabolism in cancer TTROQ37 RC R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-5210891:Uptake and function of anthrax toxins; R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5674499:Negative feedback regulation of MAPK pathway; R-HSA-5684264:MAP3K8 (TPL2)-dependent MAPK1/3 activation TTZCG4L ID TTZCG4L TTZCG4L TN Phosphodiesterase 3 (PDE3) TTZCG4L UP Family TTZCG4L UC NOUNIPROTAC TTZCG4L BC Phosphoric diester hydrolase TTZCG4L SN Phosphodiesterase III; PDE3; Cyclic GMP inhibited phosphodiesterase; Cyclic AMP phosphodiesterase III; CGI-PDE; CAMP phosphodiesterase III TTZCG4L GN NO-GeName TTZCG4L TT Successful TTI2WET ID TTI2WET TTI2WET TN Platelet-derived growth factor receptor (PDGFR) TTI2WET UP Family TTI2WET UC NOUNIPROTAC TTI2WET SN Platelet-derived growth factor receptor tyrosine kinase; PDGFR kinase; PDGF-R TTI2WET GN NO-GeName TTI2WET TT Successful TTI2WET FM Protein kinase superfamily. Tyr protein kinase family TTZVSJ2 ID TTZVSJ2 TTZVSJ2 TN Sarcoplasmic/endoplasmic reticulum calcium ATPase (ATP2A) TTZVSJ2 UP Family TTZVSJ2 UC NOUNIPROTAC TTZVSJ2 BC Acid anhydrides hydrolase TTZVSJ2 SN SERCA pump; SERCA; Calcium-transporting ATPase; Calcium pump; Ca2+-ATPase; Ca(2+)-ATPase; ATP4 TTZVSJ2 GN NO-GeName TTZVSJ2 TT Successful TT9HKJA ID TT9HKJA TT9HKJA TN Vascular endothelial growth factor (VEGF) TT9HKJA UP P15692; P49765; P49767; O43915 TT9HKJA UC VEGFA_HUMAN; VEGFB_HUMAN; VEGFC_HUMAN; VEGFD_HUMAN TT9HKJA BC Growth factor TT9HKJA SN Vascular endothelial cell growth factor TT9HKJA GN NO-GeName TT9HKJA TT Successful TTXHYV6 ID TTXHYV6 TTXHYV6 TN Voltage-gated L-type calcium channel (L-CaC) TTXHYV6 UP Family TTXHYV6 UC NOUNIPROTAC TTXHYV6 BC Voltage-gated ion channel TTXHYV6 SN L-type voltage-dependent Ca(2+) channel; L-type Ca2+ channel; L-type Ca(2+) channel TTXHYV6 GN NO-GeName TTXHYV6 TT Successful TTVIREA ID TTVIREA TTVIREA TN Adrenergic receptor (ADR) TTVIREA UP Family TTVIREA UC NOUNIPROTAC TTVIREA BC GPCR rhodopsin TTVIREA SN Adrenoceptor TTVIREA GN NO-GeName TTVIREA TT Successful TTJP4SM ID TTJP4SM TTJP4SM TN Bacterial Penicillin binding protein (Bact PBP) TTJP4SM UP Family TTJP4SM UC NOUNIPROTAC TTJP4SM GN NO-GeName TTJP4SM FC Cell wall formation. TTJP4SM TT Successful TT5HONZ ID TT5HONZ TT5HONZ TN Calcium channel unspecific (CaC) TT5HONZ UP Family TT5HONZ UC NOUNIPROTAC TT5HONZ GN NO-GeName TT5HONZ TT Successful TTZCRP3 ID TTZCRP3 TTZCRP3 TN ERK activator kinase (MEK) TTZCRP3 UP Family TTZCRP3 UC NOUNIPROTAC TTZCRP3 SN MEK; MAPKK; MAP kinase kinase TTZCRP3 GN NO-GeName TTZCRP3 TT Successful TTZCRP3 FM Protein kinase superfamily. STE Ser/Thr protein kinase family TTV9MQG ID TTV9MQG TTV9MQG TN Gamma-aminobutyric acid uptake (GABAU) TTV9MQG UP Pathway/Process TTV9MQG UC NOUNIPROTAC TTV9MQG SN GABA uptake TTV9MQG GN NO-GeName TTV9MQG TT Successful TTKLW9S ID TTKLW9S TTKLW9S TN Hyperpolarization cyclic nucleotide-gated channel (HCN) TTKLW9S UP Family TTKLW9S UC NOUNIPROTAC TTKLW9S BC Voltage-gated ion channel TTKLW9S GN NO-GeName TTKLW9S FC Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). May mediate responses to sour stimuli. TTKLW9S TT Successful TTCAQMW ID TTCAQMW TTCAQMW TN Inosine-5'-monophosphate dehydrogenase (IMPDH) TTCAQMW UP Family TTCAQMW UC NOUNIPROTAC TTCAQMW BC Short-chain dehydrogenases reductase TTCAQMW GN NO-GeName TTCAQMW TT Successful TTCAQMW KE hsa00230:Purine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways TTCAQMW RC R-HSA-73817:Purine ribonucleoside monophosphate biosynthesis TT0JLSD ID TT0JLSD TT0JLSD TN Multidrug resistance protein (MDR) TT0JLSD UP Family TT0JLSD UC NOUNIPROTAC TT0JLSD BC ABC transporter TT0JLSD SN P-glycoprotein TT0JLSD GN NO-GeName TT0JLSD TT Successful TTOXS3C ID TTOXS3C TTOXS3C TN Muscarinic acetylcholine receptor (CHRM) TTOXS3C UP Family TTOXS3C UC NOUNIPROTAC TTOXS3C GN NO-GeName TTOXS3C FC The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through theaction of G proteins. Primary transducing effect is Pi turnover. TTOXS3C TT Successful TTOXS3C KE hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04725:Cholinergic synapse; hsa04810:Regulation of actin cytoskeleton TTOXS3C RC R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-399997:Acetylcholine regulates insulin secretion; R-HSA-416476:G alpha (q) signalling events TT9IK2Z ID TT9IK2Z TT9IK2Z TN N-methyl-D-aspartate receptor (NMDAR) TT9IK2Z UP Family TT9IK2Z UC NOUNIPROTAC TT9IK2Z SN NMDA-R TT9IK2Z GN NO-GeName TT9IK2Z TT Successful TT9IK2Z FM Glutamate-gated ion channel family TTN4QDT ID TTN4QDT TTN4QDT TN Opioid receptor (OPR) TTN4QDT UP Family TTN4QDT UC NOUNIPROTAC TTN4QDT SN Opioid receptor TTN4QDT GN NO-GeName TTN4QDT TT Successful TTOD7B3 ID TTOD7B3 TTOD7B3 TN Retinoic acid receptor (RAR) TTOD7B3 UP Family TTOD7B3 UC NOUNIPROTAC TTOD7B3 SN Retinoic acid receptor TTOD7B3 GN NO-GeName TTOD7B3 TT Successful TTOD7B3 FM Nuclear hormone receptor family TTJSQEF ID TTJSQEF TTJSQEF TN Tyrosine-protein kinase (PTK) TTJSQEF UP Family TTJSQEF UC NOUNIPROTAC TTJSQEF SN Protein-tyrosine kinase; PTK TTJSQEF GN NO-GeName TTJSQEF TT Successful TTJSQEF FM Protein kinase superfamily. Tyr protein kinase family TTVJ1D8 ID TTVJ1D8 TTVJ1D8 TN Vascular endothelial growth factor receptor (VEGFR) TTVJ1D8 UP Family TTVJ1D8 UC NOUNIPROTAC TTVJ1D8 BC Kinase TTVJ1D8 GN NO-GeName TTVJ1D8 TT Successful TTVJ1D8 KE hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04144:Endocytosis; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa05202:Transcriptional misregulation in cancer; hsa05323:Rheumatoid arthritis TTIJ5EB ID TTIJ5EB TTIJ5EB TN Bacterial RNA polymerase switch region (Bact RNAP-SR) TTIJ5EB UP NO-UNIPROT TTIJ5EB UC NOUNIPROTAC TTIJ5EB GN NO-GeName TTIJ5EB TT Successful TT2SUAQ ID TT2SUAQ TT2SUAQ TN Cysteine protease (CYP) TT2SUAQ UP Family TT2SUAQ UC NOUNIPROTAC TT2SUAQ GN NO-GeName TT2SUAQ TT Successful TTT6K3S ID TTT6K3S TTT6K3S TN Endothelium of blood vessels (Endothelium) TTT6K3S UP Organelle/Cell TTT6K3S UC NOUNIPROTAC TTT6K3S SN Endothelium of blood vessels TTT6K3S GN NO-GeName TTT6K3S TT Successful TT7PBUD ID TT7PBUD TT7PBUD TN Fungal Microtubule (Fung MicroTU) TT7PBUD UP Family TT7PBUD UC NOUNIPROTAC TT7PBUD SN Keratin TT7PBUD GN NO-GeName TT7PBUD TT Successful TTNJYV2 ID TTNJYV2 TTNJYV2 TN Gamma-aminobutyric acid receptor (GAR) TTNJYV2 UP Family TTNJYV2 UC NOUNIPROTAC TTNJYV2 GN NO-GeName TTNJYV2 TT Successful TTJQFBG ID TTJQFBG TTJQFBG TN HIF-prolyl hydroxylase (HPH) TTJQFBG UP Family TTJQFBG UC NOUNIPROTAC TTJQFBG GN NO-GeName TTJQFBG TT Successful TT7CXIM ID TT7CXIM TT7CXIM TN Histamine receptor (HR) TT7CXIM UP Family TT7CXIM UC NOUNIPROTAC TT7CXIM BC GPCR rhodopsin TT7CXIM GN NO-GeName TT7CXIM TT Successful TTXFI1K ID TTXFI1K TTXFI1K TN Hyaluronidase (HYAL) TTXFI1K UP Family TTXFI1K UC NOUNIPROTAC TTXFI1K BC Glycosylase TTXFI1K GN NO-GeName TTXFI1K TT Successful TT1WB5A ID TT1WB5A TT1WB5A TN Immunoglobulin G (IgG) TT1WB5A UP Family TT1WB5A UC NOUNIPROTAC TT1WB5A BC Immunoglobulin TT1WB5A GN NO-GeName TT1WB5A TT Successful TT32XQJ ID TT32XQJ TT32XQJ TN Monoamine oxidase (MAO) TT32XQJ UP Family TT32XQJ UC NOUNIPROTAC TT32XQJ SN Human monoamine oxidase TT32XQJ GN NO-GeName TT32XQJ TT Successful TTEBCY8 ID TTEBCY8 TTEBCY8 TN Poly [ADP-ribose] polymerase (PARP) TTEBCY8 UP Family TTEBCY8 UC NOUNIPROTAC TTEBCY8 SN Poly-ADP-ribose polymerase TTEBCY8 GN NO-GeName TTEBCY8 TT Successful TT1VOHK ID TT1VOHK TT1VOHK TN Potassium channel unspecific (KC) TT1VOHK UP Family TT1VOHK UC NOUNIPROTAC TT1VOHK GN NO-GeName TT1VOHK TT Successful TTMQO60 ID TTMQO60 TTMQO60 TN Rho-associated protein kinase (ROCK) TTMQO60 UP Family TTMQO60 UC NOUNIPROTAC TTMQO60 SN Rho-associated, coiled-coil-containing protein kinase; Rho associated protein kinase TTMQO60 GN NO-GeName TTMQO60 TT Successful TTEMV5X ID TTEMV5X TTEMV5X TN Serine protease unspecific (SP) TTEMV5X UP Family TTEMV5X UC NOUNIPROTAC TTEMV5X GN NO-GeName TTEMV5X TT Successful TTUN7MC ID TTUN7MC TTUN7MC TN T-cell surface glycoprotein CD3 (CD3) TTUN7MC UP Family TTUN7MC UC NOUNIPROTAC TTUN7MC SN Cluster of differentiation 3 TTUN7MC GN NO-GeName TTUN7MC TT Successful TTYCILE ID TTYCILE TTYCILE TN Vasopressin receptor (VR) TTYCILE UP Family TTYCILE UC NOUNIPROTAC TTYCILE SN Human vasopressin receptor TTYCILE GN NO-GeName TTYCILE TT Successful TTPFZJ1 ID TTPFZJ1 TTPFZJ1 TN Vasopressin V1 receptor (V1R) TTPFZJ1 UP Family TTPFZJ1 UC NOUNIPROTAC TTPFZJ1 SN Vasopressin receptor 1; ADH V1 receptor TTPFZJ1 GN NO-GeName TTPFZJ1 TT Successful TTCRJKY ID TTCRJKY TTCRJKY TN Voltage-gated calcium channel (Cav) TTCRJKY UP Family TTCRJKY UC NOUNIPROTAC TTCRJKY BC Voltage-gated ion channel TTCRJKY GN NO-GeName TTCRJKY TT Successful TTIG65Q ID TTIG65Q TTIG65Q TN Voltage-gated sodium channel (Nav) TTIG65Q UP Family TTIG65Q UC NOUNIPROTAC TTIG65Q BC Voltage-gated ion channel TTIG65Q GN NO-GeName TTIG65Q TT Successful TTZJD1B ID TTZJD1B TTZJD1B TN Acetylcholine release (Ach rele) TTZJD1B UP Pathway/Process TTZJD1B UC NOUNIPROTAC TTZJD1B GN NO-GeName TTZJD1B TT Successful TTT04VN ID TTT04VN TTT04VN TN Adrenergic neuron (AD neuro) TTT04VN UP Organelle/Cell TTT04VN UC NOUNIPROTAC TTT04VN GN NO-GeName TTT04VN TT Successful TTDIBYJ ID TTDIBYJ TTDIBYJ TN Angiogenesis/myeloma cell growth (AMCG) TTDIBYJ UP Pathway/Process TTDIBYJ UC NOUNIPROTAC TTDIBYJ GN NO-GeName TTDIBYJ TT Successful TTXT4D5 ID TTXT4D5 TTXT4D5 TN Bacterial Cell membrane (Bact CM) TTXT4D5 UP Organelle/Cell TTXT4D5 UC NOUNIPROTAC TTXT4D5 GN NO-GeName TTXT4D5 TT Successful TTND3XS ID TTND3XS TTND3XS TN Bacterial Ribosome (Bact RIBS) TTND3XS UP Family TTND3XS UC NOUNIPROTAC TTND3XS GN NO-GeName TTND3XS TT Successful TT9X7H4 ID TT9X7H4 TT9X7H4 TN Beta-hematin formation (BHF) TT9X7H4 UP Pathway/Process TT9X7H4 UC NOUNIPROTAC TT9X7H4 GN NO-GeName TT9X7H4 TT Successful TT94IAG ID TT94IAG TT94IAG TN Cannabinoid receptor (CB) TT94IAG UP Family TT94IAG UC NOUNIPROTAC TT94IAG GN NO-GeName TT94IAG TT Successful TT3J5ZI ID TT3J5ZI TT3J5ZI TN Cell mediated immunity response (CMIR) TT3J5ZI UP Pathway/Process TT3J5ZI UC NOUNIPROTAC TT3J5ZI GN NO-GeName TT3J5ZI TT Successful TTCYAXN ID TTCYAXN TTCYAXN TN Chloride channel unspecific (ClC) TTCYAXN UP Family TTCYAXN UC NOUNIPROTAC TTCYAXN GN NO-GeName TTCYAXN TT Successful TTUPDWN ID TTUPDWN TTUPDWN TN Cholinergic receptor unspecific (CHR) TTUPDWN UP Family TTUPDWN UC NOUNIPROTAC TTUPDWN GN NO-GeName TTUPDWN TT Successful TTK982E ID TTK982E TTK982E TN Collagen (CO) TTK982E UP Family TTK982E UC NOUNIPROTAC TTK982E GN NO-GeName TTK982E TT Successful TTIJQ3O ID TTIJQ3O TTIJQ3O TN Cytochrome P450 3A (CYP3A) TTIJQ3O UP Family TTIJQ3O UC NOUNIPROTAC TTIJQ3O GN NO-GeName TTIJQ3O TT Successful TTZHSBO ID TTZHSBO TTZHSBO TN Cytomegalovirus Terminase (CMV TRM) TTZHSBO UP Family TTZHSBO UC NOUNIPROTAC TTZHSBO GN NO-GeName TTZHSBO TT Successful TTABD5E ID TTABD5E TTABD5E TN DNA replication (DNA repli) TTABD5E UP Pathway/Process TTABD5E UC NOUNIPROTAC TTABD5E GN NO-GeName TTABD5E TT Successful TTUBNVO ID TTUBNVO TTUBNVO TN DNA synthesis (DNA synth) TTUBNVO UP Pathway/Process TTUBNVO UC NOUNIPROTAC TTUBNVO GN NO-GeName TTUBNVO TT Successful TTHKJLN ID TTHKJLN TTHKJLN TN DNA-directed RNA polymerase (RNAP) TTHKJLN UP Family TTHKJLN UC NOUNIPROTAC TTHKJLN GN NO-GeName TTHKJLN TT Successful TT8CYO4 ID TT8CYO4 TT8CYO4 TN Endopeptidase (ENP) TT8CYO4 UP Family TT8CYO4 UC NOUNIPROTAC TT8CYO4 GN NO-GeName TT8CYO4 TT Successful TT3C1VN ID TT3C1VN TT3C1VN TN Enzyme unspecific (Enz) TT3C1VN UP Family TT3C1VN UC NOUNIPROTAC TT3C1VN GN NO-GeName TT3C1VN TT Successful TTSBFYK ID TTSBFYK TTSBFYK TN Estramustine binding protein (EMBP) TTSBFYK UP NO-UNIPROT TTSBFYK UC NOUNIPROTAC TTSBFYK GN NO-GeName TTSBFYK TT Successful TTAH0B3 ID TTAH0B3 TTAH0B3 TN Fungal Cell membrane (Fung CM) TTAH0B3 UP Organelle/Cell TTAH0B3 UC NOUNIPROTAC TTAH0B3 GN NO-GeName TTAH0B3 TT Successful TTG5TOX ID TTG5TOX TTG5TOX TN Fungal Proton pump (FPPCM) TTG5TOX UP Family TTG5TOX UC NOUNIPROTAC TTG5TOX GN NO-GeName TTG5TOX TT Successful TTI7S12 ID TTI7S12 TTI7S12 TN Glutamine receptor (GluR) TTI7S12 UP Family TTI7S12 UC NOUNIPROTAC TTI7S12 GN NO-GeName TTI7S12 TT Successful TT4LXBC ID TT4LXBC TT4LXBC TN Hedgehog signaling pathway (HS pathway) TT4LXBC UP Pathway/Process TT4LXBC UC NOUNIPROTAC TT4LXBC GN NO-GeName TT4LXBC TT Successful TTKA5LP ID TTKA5LP TTKA5LP TN HGF/Met signaling pathway (HGF/Met pathway) TTKA5LP UP Pathway/Process TTKA5LP UC NOUNIPROTAC TTKA5LP GN NO-GeName TTKA5LP TT Successful TTOP3CH ID TTOP3CH TTOP3CH TN Immunoglobulin unspecific (Ig) TTOP3CH UP Family TTOP3CH UC NOUNIPROTAC TTOP3CH GN NO-GeName TTOP3CH TT Successful TTXL3MF ID TTXL3MF TTXL3MF TN Lymphoid cell adhesion molecule expression (LCDME) TTXL3MF UP Pathway/Process TTXL3MF UC NOUNIPROTAC TTXL3MF GN NO-GeName TTXL3MF TT Successful TTD2MLN ID TTD2MLN TTD2MLN TN Natural killer cell activation (NKA) TTD2MLN UP Pathway/Process TTD2MLN UC NOUNIPROTAC TTD2MLN GN NO-GeName TTD2MLN TT Successful TTS5WZF ID TTS5WZF TTS5WZF TN Neuronal acetylcholine receptor alpha (NACHRA) TTS5WZF UP Family TTS5WZF UC NOUNIPROTAC TTS5WZF GN NO-GeName TTS5WZF TT Successful TTK3Q4W ID TTK3Q4W TTK3Q4W TN NFE2-related factor 2 pathway (Nrf2 pathway) TTK3Q4W UP Pathway/Process TTK3Q4W UC NOUNIPROTAC TTK3Q4W GN NO-GeName TTK3Q4W TT Successful TTPZ7AG ID TTPZ7AG TTPZ7AG TN Oxidoreductase unspecific (OR) TTPZ7AG UP Family TTPZ7AG UC NOUNIPROTAC TTPZ7AG GN NO-GeName TTPZ7AG TT Successful TT6EYVN ID TT6EYVN TT6EYVN TN Peripheral carotid chemoreceptor (PCC) TT6EYVN UP NO-UNIPROT TT6EYVN UC NOUNIPROTAC TT6EYVN GN NO-GeName TT6EYVN TT Successful TTGQUFK ID TTGQUFK TTGQUFK TN PI3K/AKT/mTOR pathway (PAm pathway) TTGQUFK UP Pathway/Process TTGQUFK UC NOUNIPROTAC TTGQUFK GN NO-GeName TTGQUFK TT Successful TT9B4N3 ID TT9B4N3 TT9B4N3 TN Prostaglandin receptor (PTGR) TT9B4N3 UP Family TT9B4N3 UC NOUNIPROTAC TT9B4N3 GN NO-GeName TT9B4N3 TT Successful TTZBFA0 ID TTZBFA0 TTZBFA0 TN Protease unspecific (PRO) TTZBFA0 UP Family TTZBFA0 UC NOUNIPROTAC TTZBFA0 GN NO-GeName TTZBFA0 TT Successful TTU7ZMG ID TTU7ZMG TTU7ZMG TN Proteasome (PS) TTU7ZMG UP Family TTU7ZMG UC NOUNIPROTAC TTU7ZMG GN NO-GeName TTU7ZMG TT Successful TTA4FIU ID TTA4FIU TTA4FIU TN Ribosome A (hRA) TTA4FIU UP Family TTA4FIU UC NOUNIPROTAC TTA4FIU GN NO-GeName TTA4FIU TT Successful TTX2AYW ID TTX2AYW TTX2AYW TN RNA synthesis (hRNA synth) TTX2AYW UP Pathway/Process TTX2AYW UC NOUNIPROTAC TTX2AYW GN NO-GeName TTX2AYW TT Successful TT9YXM1 ID TT9YXM1 TT9YXM1 TN Ryanodine receptor (RYR) TT9YXM1 UP Family TT9YXM1 UC NOUNIPROTAC TT9YXM1 GN NO-GeName TT9YXM1 TT Successful TT8G3Z7 ID TT8G3Z7 TT8G3Z7 TN Serotoninnorepinephrinedopamine reuptake (SNDR) TT8G3Z7 UP Pathway/Process TT8G3Z7 UC NOUNIPROTAC TT8G3Z7 GN NO-GeName TT8G3Z7 TT Successful TTFCQYU ID TTFCQYU TTFCQYU TN Sinus node I(f) channel (SA node IfC) TTFCQYU UP NO-UNIPROT TTFCQYU UC NOUNIPROTAC TTFCQYU GN NO-GeName TTFCQYU TT Successful TTYHPRQ ID TTYHPRQ TTYHPRQ TN Sodium pump (NaP) TTYHPRQ UP Family TTYHPRQ UC NOUNIPROTAC TTYHPRQ GN NO-GeName TTYHPRQ TT Successful TT9GOIR ID TT9GOIR TT9GOIR TN Streptococcus Diphtheria protein (Stre DIPP) TT9GOIR UP NO-UNIPROT TT9GOIR UC NOUNIPROTAC TT9GOIR GN NO-GeName TT9GOIR TT Successful TTGPK5Y ID TTGPK5Y TTGPK5Y TN T(H2) cytokine production (TH2 produ) TTGPK5Y UP Pathway/Process TTGPK5Y UC NOUNIPROTAC TTGPK5Y GN NO-GeName TTGPK5Y TT Successful TTTEJMY ID TTTEJMY TTTEJMY TN Tromboxane A2 synthesis (TA2 synth) TTTEJMY UP Pathway/Process TTTEJMY UC NOUNIPROTAC TTTEJMY GN NO-GeName TTTEJMY TT Successful TTX35ZM ID TTX35ZM TTX35ZM TN Tumor-associated glycoprotein 72 (TAG-72) TTX35ZM UP NO-UNIPROT TTX35ZM UC NOUNIPROTAC TTX35ZM GN NO-GeName TTX35ZM TT Successful TT8JRS7 ID TT8JRS7 TT8JRS7 TN Beta-secretase (BACE) TT8JRS7 UP Family TT8JRS7 UC NOUNIPROTAC TT8JRS7 BC Peptidase TT8JRS7 SN Transmembrane aspartic protease; Beta-site amyloid precursor protein cleaving enzyme; Beta-site AbetaPP-cleaving enzyme; BACE1 TT8JRS7 GN NO-GeName TT8JRS7 FC Responsible for the proteolytic processing of the amyloid precursor protein (app). Cleaves at the amino terminus of the a-beta peptide sequence, between residues 671 and 672 of app, leads to the generation and extracellular release of beta-cleaved soluble liquid. TT8JRS7 TT Clinical trial TTKIAM5 ID TTKIAM5 TTKIAM5 TN NF-kappa-B messenger RNA (NFKB mRNA) TTKIAM5 UP Family TTKIAM5 UC NOUNIPROTAC TTKIAM5 BC mRNA target TTKIAM5 SN mRNA of NF-kappaB; NF-kappaB mRNA TTKIAM5 GN NO-GeName TTKIAM5 FC NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65,RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. TTKIAM5 TT Clinical trial TTKIAM5 KE hsa04010:MAPK signaling pathway; hsa04014:Ras signaling pathway; hsa04024:cAMP signaling pathway; hsa04062:Chemokine signaling pathway; hsa04064:NF-kappa B signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa04621:NOD-like receptor signaling pathway; hsa04622:RIG-I-like receptor signaling pathway; hsa04623:Cytosolic DNA-sensing pathway; hsa04660:T cell receptor signaling pathway; hsa04662:B cell receptor signaling pathway; hsa04668:TNF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04917:Prolactin signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04932:Non-alcoholic fatty liver disease (NAFLD); hsa05030:Cocaine addiction; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05131:Shigellosis; hsa05132:Salmonella infection; hsa05133:Pertussis; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05142:Chagas disease (American trypanosomiasis); hsa05145:Toxoplasmosis; hsa05146:Amoebiasis; hsa05152:Tuberculosis; hsa05160:Hepatitis C; hsa05161:Hepatitis B; hsa05162:Measles; hsa05164:Influenza A; hsa05166:HTLV-I infection; hsa05168:Herpes simplex infection; hsa05169:Epstein-Barr virus infection; hsa05200:Pathways in cancer; hsa05202:Transcriptional misregulation in cancer; hsa05203:Viral carcinogenesis; hsa05206:MicroRNAs in cancer; hsa05212:Pancreatic cancer; hsa05215:Prostate cancer; hsa05220:Chronic myeloid leukemia; hsa05221:Acute myeloid leukemia; hsa05222:Small cell lung cancer; hsa05321:Inflammatory bowel disease (IBD) TTUST1O ID TTUST1O TTUST1O TN Phosphodiesterase (PDE) TTUST1O UP Family TTUST1O UC NOUNIPROTAC TTUST1O BC Phosphoric diester hydrolase TTUST1O SN Human phosphodiesterase TTUST1O GN NO-GeName TTUST1O FC Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones. TTUST1O TT Clinical trial TTQ29KF ID TTQ29KF TTQ29KF TN Voltage-gated potassium channel Kv7 (KCNQ) TTQ29KF UP Family TTQ29KF UC NOUNIPROTAC TTQ29KF BC Voltage-gated ion channel TTQ29KF SN Voltage-gated potassium channel subunit Kv7; Potassium voltage-gated channel subfamily KQT; Kv7; KVLQT; KQT-like; IKs producing slow voltage-gated potassium channel subunit alpha KvLQT; IKs producing slow voltage-gated potassium channel alpha subunit KvLQT TTQ29KF GN NO-GeName TTQ29KF TT Clinical trial TTQ29KF KE hsa04261:Adrenergic signaling in cardiomyocytes; hsa04725:Cholinergic synapse; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04974:Protein digestion and absorption; hsa05110:Vibrio cholerae infection TT6S84O ID TT6S84O TT6S84O TN Human immunodeficiency virus Trans-activation response element (HIV TAR RNA element) TT6S84O UP NO-UNIPROT TT6S84O UC NOUNIPROTAC TT6S84O BC mRNA target TT6S84O SN HIV TAR element TT6S84O GN NO-GeName TT6S84O TT Clinical trial TT9K83W ID TT9K83W TT9K83W TN Tubulin receptor (TUBR) TT9K83W UP NO-UNIPROT TT9K83W UC NOUNIPROTAC TT9K83W SN Tubulin protein TT9K83W GN NO-GeName TT9K83W FC Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TT9K83W TT Clinical trial TT9K83W FM Tubulin family TT9K83W KE hsa04145:Phagosome; hsa04540:Gap junction; hsa05130:Pathogenic Escherichia coli infection TT9K83W RC R-HSA-1445148:Translocation of GLUT4 to the plasma membrane; R-HSA-190840:Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane; R-HSA-190861:Gap junction assembly; R-HSA-2132295:MHC class II antigen presentation; R-HSA-2467813:Separation of Sister Chromatids; R-HSA-2500257:Resolution of Sister Chromatid Cohesion; R-HSA-380320:Recruitment of NuMA to mitotic centrosomes; R-HSA-389977:Post-chaperonin tubulin folding pathway; R-HSA-437239:Recycling pathway of L1; R-HSA-5610787:Hedgehog 'off' state; R-HSA-5617833:Assembly of the primary cilium; R-HSA-5626467:RHO GTPases activate IQGAPs; R-HSA-5663220:RHO GTPases Activate Formins; R-HSA-68877:Mitotic Prometaphase; R-HSA-983189:Kinesins TTRG4QN ID TTRG4QN TTRG4QN TN Activin receptor type II (ACVR2) TTRG4QN UP P27037; Q13705 TTRG4QN UC AVR2A_HUMAN; AVR2B_HUMAN TTRG4QN GN NO-GeName TTRG4QN TT Clinical trial TT0IUKX ID TT0IUKX TT0IUKX TN Alpha-L-iduronidase (IDUA) TT0IUKX UP P35475 TT0IUKX UC IDUA_HUMAN TT0IUKX GN IDUA TT0IUKX FC extracellular exosome, lysosomal lumen, hydrolase activity, hydrolyzing O-glycosyl compounds, L-iduronidase activity, chondroitin sulfate catabolic process, dermatan sulfate catabolic process, disaccharide metabolic process, glycosaminoglycan catabolic process, heparin catabolic process TT0IUKX EC EC 3.2.1.76 TT0IUKX SQ MRPLRPRAALLALLASLLAAPPVAPAEAPHLVHVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP TT0IUKX TT Clinical trial TTGN1ZA ID TTGN1ZA TTGN1ZA TN Angiotensin II receptor (AGTR) TTGN1ZA UP Family TTGN1ZA UC NOUNIPROTAC TTGN1ZA GN NO-GeName TTGN1ZA FC Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. TTGN1ZA TT Clinical trial TTGN1ZA KE hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04270:Vascular smooth muscle contraction; hsa04614:Renin-angiotensin system; hsa04924:Renin secretion; hsa05200:Pathways in cancer TTQ57WJ ID TTQ57WJ TTQ57WJ TN Apoptosis regulator BAX (BAX) TTQ57WJ UP Q07812 TTQ57WJ UC BAX_HUMAN TTQ57WJ SN Bcl-2-like protein 4; Bcl2-L-4 TTQ57WJ GN BAX TTQ57WJ FC Plays a role in the mitochondrial apoptotic process. Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM). Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. TTQ57WJ SQ MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG TTQ57WJ TT Clinical trial TTTSUI2 ID TTTSUI2 TTTSUI2 TN Aspergillus Dihydroorotate dehydrogenase (Aspergillus DHODH) TTTSUI2 UP G5EB61 TTTSUI2 UC G5EB61_EMENI TTTSUI2 SN Dihydroorotate oxidase TTTSUI2 GN NOUNIPROTAC TTTSUI2 EC EC 1.3.5.2 TTTSUI2 SQ MATNSFRKLTFSGASRLGGCRRLPLTCRQLRFASDSGAAAATTKATAESAAESASINVKEAPKKAGRGLRRTVLGTSLALTLLVGYVYGTDTRASVHRYGVVPLIRALYPDAEDAHHIGVDTLKMLYKYGLHPRERGDPDGDGALATEVFGYTLSNPIGISGGLDKHAEIPDPLFAIGPAIVEVGGTTPLPQDGNPRPRVFRLPSQRAMINRYGLNSKGADHMAAILEQRVRDFAYANGFGAYDAAKQRVLDGEAGVPPGSLQPGKLLAVQVAKNKATPDGDIEAIKRDYVYCVDRVAKYADILVVNVSSPNTPGLRDLQATAPLTAILSAVVGAAKSVNRKTKPYVMVKVSPDEDSDEQVSGICDAVRASGVDGVIVGNTTNRRPDPIPQGYTLPAKEQATLKETGGYSGPQLFDRTVALVARYRSMLDAESETAGSAKDSAATIAQTEPGSENVPPVEAPSGLPRKVIFASGGITNGKQAHAVLDTGASVAMMYTGVVYGGVGTVTRVKQELRTAKKE TTTSUI2 TT Clinical trial TTR61MW ID TTR61MW TTR61MW TN B-cell lymphoma/leukemia 11A (BCL11A) TTR61MW UP Q9H165 TTR61MW UC BC11A_HUMAN TTR61MW SN BCL-11A; B-cell CLL/lymphoma 11A; COUP-TF-interacting protein 1; Ecotropic viral integration site 9 protein homolog; EVI-9; Zinc finger protein 856; BCL-11A; B-cell CLL/lymphoma 11A; COUP-TF-interacting protein 1; Ecotropic viral integration site 9 protein homolog; EVI-9; Zinc finger protein 856 TTR61MW GN BCL11A TTR61MW FC Transcription factor associated with the BAF SWI/SNF chromatin remodeling complex (By similarity). Repressor of fetal hemoglobin (HbF) level. Involved in brain development. May play a role in hematopoiesis. Essential factor in lymphopoiesis required for B-cell formation in fetal liver. May function as a modulator of the transcriptional repression activity of ARP1 (By similarity). TTR61MW SQ MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLRELAGNTSSPPLSPGRPSPMQRLLQPFQPGSKPPFLATPPLPPLQSAPPPSQPPVKSKSCEFCGKTFKFQSNLVVHRRSHTGEKPYKCNLCDHACTQASKLKRHMKTHMHKSSPMTVKSDDGLSTASSPEPGTSDLVGSASSALKSVVAKFKSENDPNLIPENGDEEEEEDDEEEEEEEEEEEEELTESERVDYGFGLSLEAARHHENSSRGAVVGVGDESRALPDVMQGMVLSSMQHFSEAFHQVLGEKHKRGHLAEAEGHRDTCDEDSVAGESDRIDDGTVNGRGCSPGESASGGLSKKLLLGSPSSLSPFSKRIKLEKEFDLPPAAMPNTENVYSQWLAGYAASRQLKDPFLSFGDSRQSPFASSSEHSSENGSLRFSTPPGELDGGISGRSGTGSGGSTPHISGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQVGKDVYKCEICKMPFSVYSTLEKHMKKWHSDRVLNNDIKTE TTR61MW TT Clinical trial TTPLHYK ID TTPLHYK TTPLHYK TN BCL11A messenger RNA (BCL11A mRNA) TTPLHYK UP Q9H165 TTPLHYK UC BC11A_HUMAN TTPLHYK SN BCL-11A; B-cell CLL/lymphoma 11A; COUP-TF-interacting protein 1; Ecotropic viral integration site 9 protein homolog; EVI-9; Zinc finger protein 856; BCL-11A; B-cell CLL/lymphoma 11A; COUP-TF-interacting protein 1; Ecotropic viral integration site 9 protein homolog; EVI-9; Zinc finger protein 856 TTPLHYK GN BCL11A TTPLHYK FC Transcription factor associated with the BAF SWI/SNF chromatin remodeling complex (By similarity). Repressor of fetal hemoglobin (HbF) level. Involved in brain development. May play a role in hematopoiesis. Essential factor in lymphopoiesis required for B-cell formation in fetal liver. May function as a modulator of the transcriptional repression activity of ARP1 (By similarity). TTPLHYK SQ MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLRELAGNTSSPPLSPGRPSPMQRLLQPFQPGSKPPFLATPPLPPLQSAPPPSQPPVKSKSCEFCGKTFKFQSNLVVHRRSHTGEKPYKCNLCDHACTQASKLKRHMKTHMHKSSPMTVKSDDGLSTASSPEPGTSDLVGSASSALKSVVAKFKSENDPNLIPENGDEEEEEDDEEEEEEEEEEEEELTESERVDYGFGLSLEAARHHENSSRGAVVGVGDESRALPDVMQGMVLSSMQHFSEAFHQVLGEKHKRGHLAEAEGHRDTCDEDSVAGESDRIDDGTVNGRGCSPGESASGGLSKKLLLGSPSSLSPFSKRIKLEKEFDLPPAAMPNTENVYSQWLAGYAASRQLKDPFLSFGDSRQSPFASSSEHSSENGSLRFSTPPGELDGGISGRSGTGSGGSTPHISGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQVGKDVYKCEICKMPFSVYSTLEKHMKKWHSDRVLNNDIKTE TTPLHYK TT Clinical trial TTEDCQ0 ID TTEDCQ0 TTEDCQ0 TN Beta-sarcoglycan (SGCB) TTEDCQ0 UP Q16585 TTEDCQ0 UC SGCB_HUMAN TTEDCQ0 SN Beta-SG; 43 kDa dystrophin-associated glycoprotein; 43DAG; A3b TTEDCQ0 GN SGCB TTEDCQ0 FC Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. TTEDCQ0 SQ MAAAAAAAAEQQSSNGPVKKSMREKAVERRSVNKEHNSNFKAGYIPIDEDRLHKTGLRGRKGNLAICVIILLFILAVINLIITLVIWAVIRIGPNGCDSMEFHESGLLRFKQVSDMGVIHPLYKSTVGGRRNENLVITGNNQPIVFQQGTTKLSVENNKTSITSDIGMQFFDPRTQNILFSTDYETHEFHLPSGVKSLNVQKASTERITSNATSDLNIKVDGRAIVRGNEGVFIMGKTIEFHMGGNMELKAENSIILNGSVMVSTTRLPSSSSGDQLGSGDWVRYKLCMCADGTLFKVQVTSQNMGCQISDNPCGNTH TTEDCQ0 TT Clinical trial TTA9CK4 ID TTA9CK4 TTA9CK4 TN Biliary glycoprotein 1 (CEACAM1) TTA9CK4 UP P13688 TTA9CK4 UC CEAM1_HUMAN TTA9CK4 SN Biliary glycoprotein 1; BGP-1; DE AltName: CD_antigen=CD66a TTA9CK4 GN CEACAM1 TTA9CK4 FC Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis. Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors. Plays a role in immune response, of T cells, natural killer (NK) and neutrophils. Upon TCR/CD3 complex stimulation, inhibits TCR-mediated cytotoxicity by blocking granule exocytosis by mediating homophilic binding to adjacent cells, allowing interaction with and phosphorylation by LCK and interaction with the TCR/CD3 complex which recruits PTPN6 resulting in dephosphorylation of CD247 and ZAP70. Also inhibits T cell proliferation and cytokine production through inhibition of JNK cascade and plays a crucial role in regulating autoimmunity and anti-tumor immunity by inhibiting T cell through its interaction with HAVCR2. Upon natural killer (NK) cells activation, inhibit KLRK1-mediated cytolysis of CEACAM1-bearing tumor cells by trans-homophilic interactions with CEACAM1 on the target cell and lead to cis-interaction between CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1 dephosphorylation. Upon neutrophils activation negatively regulates IL1B production by recruiting PTPN6 to a SYK-TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome. Downregulates neutrophil production by acting as a coinhibitory receptor for CSF3R by downregulating the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (By similarity). Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (By similarity). Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis. This inernalization promotes interaction with FASN leading to receptor-mediated insulin degradation and to reduction of FASN activity leading to negative regulation of fatty acid synthesis. INSR-mediated phosphorylation also provokes a down-regulation of cell proliferation through SHC1 interaction resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways (By similarity). Functions as activator in angiogenesis by promoting blood vessel remodeling through endothelial cell differentiation and migration and in arteriogenesis by increasing the number of collateral arteries and collateral vessel calibers after ischemia. Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (By similarity). Downregulates cell growth in response to EGF through its interaction with SHC1 that mediates interaction with EGFR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (By similarity). Negatively regulates platelet aggregation by decreasing platelet adhesion on type I collagen through the GPVI-FcRgamma complex (By similarity). Inhibits cell migration and cell scattering through interaction with FLNA; interfers with the interaction of FLNA with RALA. Mediates bile acid transport activity in a phosphorylation dependent manner (By similarity). Negatively regulates osteoclastogenesis (By similarity). TTA9CK4 SQ MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWINNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPGAIAGIVIGVVALVALIAVALACFLHFGKTGRASDQRDLTEHKPSVSNHTQDHSNDPPNKMNEVTYSTLNFEAQQPTQPTSASPSLTATEIIYSEVKKQ TTA9CK4 TT Clinical trial TT07RIB ID TT07RIB TT07RIB TN Bone morphogenetic protein 6 (BMP6) TT07RIB UP P22004 TT07RIB UC BMP6_HUMAN TT07RIB SN BMP-6; VG-1-related protein; VG-1-R; VGR-1 TT07RIB GN BMP6 TT07RIB FC Induces cartilage and bone formation. TT07RIB SQ MPGLGRRAQWLCWWWGLLCSCCGPPPLRPPLPAAAAAAAGGQLLGDGGSPGRTEQPPPSPQSSSGFLYRRLKTQEKREMQKEILSVLGLPHRPRPLHGLQQPQPPALRQQEEQQQQQQLPRGEPPPGRLKSAPLFMLDLYNALSADNDEDGASEGERQQSWPHEAASSSQRRQPPPGAAHPLNRKSLLAPGSGSGGASPLTSAQDSAFLNDADMVMSFVNLVEYDKEFSPRQRHHKEFKFNLSQIPEGEVVTAAEFRIYKDCVMGSFKNQTFLISIYQVLQEHQHRDSDLFLLDTRVVWASEEGWLEFDITATSNLWVVTPQHNMGLQLSVVTRDGVHVHPRAAGLVGRDGPYDKQPFMVAFFKVSEVHVRTTRSASSRRRQQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH TT07RIB TT Clinical trial TTKOBRA ID TTKOBRA TTKOBRA TN Bone morphogenetic protein 7 (BMP7) TTKOBRA UP P18075 TTKOBRA UC BMP7_HUMAN TTKOBRA SN BMP-7; Osteogenic protein 1; OP-1; Eptotermin alfa TTKOBRA GN BMP7 TTKOBRA FC Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis. Promotes brown adipocyte differentiation by P38 MAPK pathway-mediated activation of target genes, including members of the SOX family of transcription factors. TTKOBRA SQ MHVRSLRAAAPHSFVALWAPLFLLRSALADFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAMAVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPRYHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLLDSRTLWASEEGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKATEVHFRSIRSTGSKQRSQNRSKTPKNQEALRMANVAENSSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAYYCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKPCCAPTQLNAISVLYFDDSSNVILKKYRNMVVRACGCH TTKOBRA TT Clinical trial TTE4BSY ID TTE4BSY TTE4BSY TN Bromodomain and extraterminal domain protein (BET) TTE4BSY UP Family TTE4BSY UC NOUNIPROTAC TTE4BSY SN Bromodomain and Extra Terminal protein TTE4BSY GN NO-GeName TTE4BSY TT Clinical trial TTE4BSY KE hsa04130:SNARE interactions in vesicular transport TTE4BSY RC R-HSA-204005:COPII (Coat Protein 2) Mediated Vesicle Transport TT09JLE ID TT09JLE TT09JLE TN BV virus Major capsid protein VP1 (BKV VP1) TT09JLE UP P03088 TT09JLE UC VP1_POVBK TT09JLE SN Major structural protein VP1 TT09JLE GN BKV VP1 TT09JLE FC Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA. TT09JLE SQ MAPTKRKGECPGAAPKKPKEPVQVPKLLIKGGVEVLEVKTGVDAITEVECFLNPEMGDPDENLRGFSLKLSAENDFSSDSPERKMLPCYSTARIPLPNLNEDLTCGNLLMWEAVTVQTEVIGITSMLNLHAGSQKVHEHGGGKPIQGSNFHFFAVGGEPLEMQGVLMNYRSKYPDGTITPKNPTAQSQVMNTDHKAYLDKNNAYPVECWVPDPSRNENARYFGTFTGGENVPPVLHVTNTATTVLLDEQGVGPLCKADSLYVSAADICGLFTNSSGTQQWRGLARYFKIRLRKRSVKNPYPISFLLSDLINRRTQRVDGQPMYGMESQVEEVRVFDGTERLPGDPDMIRYIDKQGQLQTKML TT09JLE TT Clinical trial TT2LJRF ID TT2LJRF TT2LJRF TN C5 messenger RNA (C5 mRNA) TT2LJRF UP P01031 TT2LJRF UC CO5_HUMAN TT2LJRF SN C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4 TT2LJRF GN C5 TT2LJRF FC Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled. TT2LJRF SQ MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC TT2LJRF TT Clinical trial TTA4SHR ID TTA4SHR TTA4SHR TN C9orf72 messenger RNA (C9orf72 mRNA) TTA4SHR UP Q96LT7 TTA4SHR UC CI072_HUMAN TTA4SHR GN C9orf72 TTA4SHR FC Component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy. In the complex, C9orf72 and SMCR8 probably constitute the catalytic subunits that promote the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation. The C9orf72-SMCR8 complex also acts as a regulator of autophagy initiation by interacting with the ATG1/ULK1 kinase complex and modulating its protein kinase activity. Positively regulates initiation of autophagy by regulating the RAB1A-dependent trafficking of the ATG1/ULK1 kinase complex to the phagophore which leads to autophagosome formation. Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates. Plays a role in endosomal trafficking. May be involved in regulating the maturation of phagosomes to lysosomes (By similarity). Regulates actin dynamics in motor neurons by inhibiting the GTP-binding activity of ARF6, leading to ARF6 inactivation. This reduces the activity of the LIMK1 and LIMK2 kinases which are responsible for phosphorylation and inactivation of cofilin, leading to cofilin activation. Positively regulates axon extension and axon growth cone size in spinal motor neurons. Plays a role within the hematopoietic system in restricting inflammation and the development of autoimmunity (By similarity). TTA4SHR SQ MSTLCPPPSPAVAKTEIALSGKSPLLAATFAYWDNILGPRVRHIWAPKTEQVLLSDGEITFLANHTLNGEILRNAESGAIDVKFFVLSEKGVIIVSLIFDGNWNGDRSTYGLSIILPQTELSFYLPLHRVCVDRLTHIIRKGRIWMHKERQENVQKIILEGTERMEDQGQSIIPMLTGEVIPVMELLSSMKSHSVPEEIDIADTVLNDDDIGDSCHEGFLLNAISSHLQTCGCSVVVGSSAEKVNKIVRTLCLFLTPAERKCSRLCEAESSFKYESGLFVQGLLKDSTGSFVLPFRQVMYAPYPTTHIDVDVNTVKQMPPCHEHIYNQRRYMRSELTAFWRATSEEDMAQDTIIYTDESFTPDLNIFQDVLHRDTLVKAFLDQVFQLKPGLSLRSTFLAQFLLVLHRKALTLIKYIEDDTQKGKKPFKSLRNLKIDLDLTAEGDLNIIMALAEKIKPGLHSFIFGRPFYTSVQERDVLMTF TTA4SHR TT Clinical trial TTKU9YD ID TTKU9YD TTKU9YD TN Calcium-activated potassium channel KCa2 (KCNN) TTKU9YD UP Family TTKU9YD UC NOUNIPROTAC TTKU9YD BC Voltage-gated ion channel TTKU9YD GN NO-GeName TTKU9YD FC Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blockedby apamin. TTKU9YD TT Clinical trial TTZY5KP ID TTZY5KP TTZY5KP TN Caspase (CASP) TTZY5KP UP Family TTZY5KP UC NOUNIPROTAC TTZY5KP BC Peptidase TTZY5KP GN NO-GeName TTZY5KP TT Clinical trial TTHRAIJ ID TTHRAIJ TTHRAIJ TN CBLB messenger RNA (CBLB mRNA) TTHRAIJ UP Q13191 TTHRAIJ UC CBLB_HUMAN TTHRAIJ SN Casitas B-lineage lymphoma proto-oncogene b; RING finger protein 56; RING-type E3 ubiquitin transferase CBL-B; SH3-binding protein CBL-B; Signal transduction protein CBL-B TTHRAIJ GN CBLB TTHRAIJ FC E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBL, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity). TTHRAIJ EC EC 2.3.2.27 TTHRAIJ SQ MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFGMPMLDLDDDDDREESLMMNRLANVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPPERPPPIPPDNRLSRHIHHVESVPSRDPPMPLEAWCPRDVFGTNQLVGCRLLGEGSPKPGITASSNVNGRHSRVGSDPVLMRKHRRHDLPLEGAKVFSNGHLGSEEYDVPPRLSPPPPVTTLLPSIKCTGPLANSLSEKTRDPVEEDDDEYKIPSSHPVSLNSQPSHCHNVKPPVRSCDNGHCMLNGTHGPSSEKKSNIPDLSIYLKGDVFDSASDPVPLPPARPPTRDNPKHGSSLNRTPSDYDLLIPPLGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFVDLASGQVPLPPARRLPGENVKTNRTSQDYDQLPSCSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL TTHRAIJ TT Clinical trial TTIL516 ID TTIL516 TTIL516 TN CCN2 messenger RNA (CCN2 mRNA) TTIL516 UP P29279 TTIL516 UC CCN2_HUMAN TTIL516 SN Cellular communication network factor 2; Connective tissue growth factor; Hypertrophic chondrocyte-specific protein 24; Insulin-like growth factor-binding protein 8; IBP-8; IGF-binding protein 8; IGFBP-8 TTIL516 GN CCN2 TTIL516 FC Major connective tissue mitoattractant secreted by vascular endothelial cells. Promotes proliferation and differentiation of chondrocytes. Mediates heparin- and divalent cation-dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells. Enhances fibroblast growth factor-induced DNA synthesis. TTIL516 SQ MTAASMGPVRVAFVVLLALCSRPAVGQNCSGPCRCPDEPAPRCPAGVSLVLDGCGCCRVCAKQLGELCTERDPCDPHKGLFCHFGSPANRKIGVCTAKDGAPCIFGGTVYRSGESFQSSCKYQCTCLDGAVGCMPLCSMDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKDQTVVGPALAAYRLEDTFGPDPTMIRANCLVQTTEWSACSKTCGMGISTRVTNDNASCRLEKQSRLCMVRPCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSMKTYRAKFCGVCTDGRCCTPHRTTTLPVEFKCPDGEVMKKNMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA TTIL516 TT Clinical trial TTFAOU7 ID TTFAOU7 TTFAOU7 TN CD274 messenger RNA (CD274 mRNA) TTFAOU7 UP Q9NZQ7 TTFAOU7 UC PD1L1_HUMAN TTFAOU7 SN PD-L1; PDCD1 ligand 1; Programmed death ligand 1; hPD-L1; B7 homolog 1; B7-H1; DE AltName: CD_antigen=CD274 TTFAOU7 GN CD274 TTFAOU7 FC Plays a critical role in induction and maintenance of immune tolerance to self. As a ligand for the inhibitory receptor PDCD1/PD-1, modulates the activation threshold of T-cells and limits T-cell effector response. Through a yet unknown activating receptor, may costimulate T-cell subsets that predominantly produce interleukin-10 (IL10). TTFAOU7 SQ MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET TTFAOU7 TT Clinical trial TT6K9BV ID TT6K9BV TT6K9BV TN Cdc-like kinase (CLK) TT6K9BV UP P49759; P49760; P49761; Q9HAZ1 TT6K9BV UC CLK1_HUMAN; CLK2_HUMAN; CLK3_HUMAN; CLK4_HUMAN TT6K9BV GN NO-GeName TT6K9BV TT Clinical trial TT5LWG1 ID TT5LWG1 TT5LWG1 TN CEBPA messenger RNA (CEBPA mRNA) TT5LWG1 UP P49715 TT5LWG1 UC CEBPA_HUMAN TT5LWG1 SN C/EBP alpha TT5LWG1 GN CEBPA TT5LWG1 FC Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta. Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes. During early embryogenesis, plays essential and redundant functions with CEBPB. Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP). Critical for the proper development of the liver and the lung (By similarity). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (By similarity). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Downregulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters. Proliferation arrest also depends on a functional binding to SWI/SNF complex. In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC1. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity). TT5LWG1 SQ MESADFYEAEPRPPMSSHLQSPPHAPSSAAFGFPRGAGPAQPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAVGPTGGGGGGDFDYPGAPAGPGGAVMPGGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPSHPHPHPPPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHPAPALGAAGLPGPGSALKGLGAAHPDLRASGGSGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELDTLRGIFRQLPESSLVKAMGNCA TT5LWG1 TT Clinical trial TTTYQNS ID TTTYQNS TTTYQNS TN Cellular disintegrin-related protein (ADAM9) TTTYQNS UP Q13443 TTTYQNS UC ADAM9_HUMAN TTTYQNS SN ADAM 9; Cellular disintegrin-related protein; Meltrin-gamma; Metalloprotease/disintegrin/cysteine-rich protein 9; Myeloma cell metalloproteinase TTTYQNS GN ADAM9 TTTYQNS FC Cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5. May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins. TTTYQNS EC EC 3.4.24.- TTTYQNS SQ MGSGARFPSGTLRVRWLLLLGLVGPVLGAARPGFQQTSHLSSYEIITPWRLTRERREAPRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGYVEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQNSSHFEHIIYRMDDVYKEPLKCGVSNKDIEKETAKDEEEEPPSMTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKFLITRRRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRDCSCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGNCLLNIPKPDEAYSAPSCGNKLVDAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPDVFIQNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQEIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCGAGKICRNFQCVDASVLNYDCDVQKKCHGHGVCNSNKNCHCENGWAPPNCETKGYGGSVDSGPTYNEMNTALRDGLLVFFFLIVPLIVCAIFIFIKRDQLWRSYFRKKRSQTYESDGKNQANPSRQPGSVPRHVSPVTPPREVPIYANRFAVPTYAAKQPQQFPSRPPPPQPKVSSQGNLIPARPAPAPPLYSSLT TTTYQNS TT Clinical trial TT3XBOV ID TT3XBOV TT3XBOV TN CEP290 messenger RNA (CEP290 mRNA) TT3XBOV UP O15078 TT3XBOV UC CE290_HUMAN TT3XBOV SN Cep290; Bardet-Biedl syndrome 14 protein; Cancer/testis antigen 87; CT87; Nephrocystin-6; Tumor antigen se2-2 TT3XBOV GN CEP290 TT3XBOV FC Involved in early and late steps in cilia formation. Its association with CCP110 is required for inhibition of primary cilia formation by CCP110. May play a role in early ciliogenesis in the disappearance of centriolar satellites and in the transition of primary ciliar vesicles (PCVs) to capped ciliary vesicles (CCVs). Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1. Required for the correct localization of ciliary and phototransduction proteins in retinal photoreceptor cells; may play a role in ciliary transport processes (By similarity). Required for efficient recruitment of RAB8A to primary cilium. In the ciliary transition zone is part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). Involved in regulation of the BBSome complex integrity, specifically for presence of BBS2, BBS5 and BBS8/TTC8 in the complex, and in ciliary targeting of selected BBSome cargos. May play a role in controlling entry of the BBSome complex to cilia possibly implicating IQCB1/NPHP5. Activates ATF4-mediated transcription. TT3XBOV SQ MPPNINWKEIMKVDPDDLPRQEELADNLLISLSKVEVNELKSEKQENVIHLFRITQSLMKMKAQEVELALEEVEKAGEEQAKFENQLKTKVMKLENELEMAQQSAGGRDTRFLRNEICQLEKQLEQKDRELEDMEKELEKEKKVNEQLALRNEEAENENSKLRRENKRLKKKNEQLCQDIIDYQKQIDSQKETLLSRRGEDSDYRSQLSKKNYELIQYLDEIQTLTEANEKIEVQNQEMRKNLEESVQEMEKMTDEYNRMKAIVHQTDNVIDQLKKENDHYQLQVQELTDLLKSKNEEDDPIMVAVNAKVEEWKLILSSKDDEIIEYQQMLHNLREKLKNAQLDADKSNVMALQQGIQERDSQIKMLTEQVEQYTKEMEKNTCIIEDLKNELQRNKGASTLSQQTHMKIQSTLDILKEKTKEAERTAELAEADAREKDKELVEALKRLKDYESGVYGLEDAVVEIKNCKNQIKIRDREIEILTKEINKLELKISDFLDENEALRERVGLEPKTMIDLTEFRNSKHLKQQQYRAENQILLKEIESLEEERLDLKKKIRQMAQERGKRSATSGLTTEDLNLTENISQGDRISERKLDLLSLKNMSEAQSKNEFLSRELIEKERDLERSRTVIAKFQNKLKELVEENKQLEEGMKEILQAIKEMQKDPDVKGGETSLIIPSLERLVNAIESKNAEGIFDASLHLKAQVDQLTGRNEELRQELRESRKEAINYSQQLAKANLKIDHLEKETSLLRQSEGSNVVFKGIDLPDGIAPSSASIINSQNEYLIHLLQELENKEKKLKNLEDSLEDYNRKFAVIRHQQSLLYKEYLSEKETWKTESKTIKEEKRKLEDQVQQDAIKVKEYNNLLNALQMDSDEMKKILAENSRKITVLQVNEKSLIRQYTTLVELERQLRKENEKQKNELLSMEAEVCEKIGCLQRFKEMAIFKIAALQKVVDNSVSLSELELANKQYNELTAKYRDILQKDNMLVQRTSNLEHLECENISLKEQVESINKELEITKEKLHTIEQAWEQETKLGNESSMDKAKKSITNSDIVSISKKITMLEMKELNERQRAEHCQKMYEHLRTSLKQMEERNFELETKFAELTKINLDAQKVEQMLRDELADSVSKAVSDADRQRILELEKNEMELKVEVSKLREISDIARRQVEILNAQQQSRDKEVESLRMQLLDYQAQSDEKSLIAKLHQHNVSLQLSEATALGKLESITSKLQKMEAYNLRLEQKLDEKEQALYYARLEGRNRAKHLRQTIQSLRRQFSGALPLAQQEKFSKTMIQLQNDKLKIMQEMKNSQQEHRNMENKTLEMELKLKGLEELISTLKDTKGAQKVINWHMKIEELRLQELKLNRELVKDKEEIKYLNNIISEYERTISSLEEEIVQQNKFHEERQMAWDQREVDLERQLDIFDRQQNEILNAAQKFEEATGSIPDPSLPLPNQLEIALRKIKENIRIILETRATCKSLEEKLKEKESALRLAEQNILSRDKVINELRLRLPATAEREKLIAELGRKEMEPKSHHTLKIAHQTIANMQARLNQKEEVLKKYQRLLEKAREEQREIVKKHEEDLHILHHRLELQADSSLNKFKQTAWDLMKQSPTPVPTNKHFIRLAEMEQTVAEQDDSLSSLLVKLKKVSQDLERQREITELKVKEFENIKLQLQENHEDEVKKVKAEVEDLKYLLDQSQKESQCLKSELQAQKEANSRAPTTTMRNLVERLKSQLALKEKQQKALSRALLELRAEMTAAAEERIISATSQKEAHLNVQQIVDRHTRELKTQVEDLNENLLKLKEALKTSKNRENSLTDNLNDLNNELQKKQKAYNKILREKEEIDQENDELKRQIKRLTSGLQGKPLTDNKQSLIEELQRKVKKLENQLEGKVEEVDLKPMKEKNAKEELIRWEEGKKWQAKIEGIRNKLKEKEGEVFTLTKQLNTLKDLFAKADKEKLTLQRKLKTTGMTVDQVLGIRALESEKELEELKKRNLDLENDILYMRAHQALPRDSVVEDLHLQNRYLQEKLHALEKQFSKDTYSKPSISGIESDDHCQREQELQKENLKLSSENIELKFQLEQANKDLPRLKNQVRDLKEMCEFLKKEKAEVQRKLGHVRGSGRSGKTIPELEKTIGLMKKVVEKVQRENEQLKKASGILTSEKMANIEQENEKLKAELEKLKAHLGHQLSMHYESKTKGTEKIIAENERLRKELKKETDAAEKLRIAKNNLEILNEKMTVQLEETGKRLQFAESRGPQLEGADSKSWKSIVVTRMYETKLKELETDIAKKNQSITDLKQLVKEATEREQKVNKYNEDLEQQIKILKHVPEGAETEQGLKRELQVLRLANHQLDKEKAELIHQIEANKDQSGAESTIPDADQLKEKIKDLETQLKMSDLEKQHLKEEIKKLKKELENFDPSFFEEIEDLKYNYKEEVKKNILLEEKVKKLSEQLGVELTSPVAASEEFEDEEESPVNFPIY TT3XBOV TT Clinical trial TTEZQ39 ID TTEZQ39 TTEZQ39 TN Cerebron E3 ubiquitin ligase complex (CRL4-CRBN E3 ubiquitin ligase) TTEZQ39 UP Q13619/Q13620-Q16531-Q96SW2 TTEZQ39 UC CUL4A_HUMAN/CUL4B_HUMAN-DDB1_HUMAN-CRBN_HUMAN TTEZQ39 GN CUL4A/CUL4B-DDB1-CRBN TTEZQ39 TT Clinical trial TT3SGK7 ID TT3SGK7 TT3SGK7 TN CFB messenger RNA (CFB mRNA) TT3SGK7 UP P00751 TT3SGK7 UC CFAB_HUMAN TT3SGK7 SN C3/C5 convertase; Glycine-rich beta glycoprotein; GBG; PBF2; Properdin factor B TT3SGK7 GN CFB TT3SGK7 FC Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B-lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes. TT3SGK7 EC EC 3.4.21.47 TT3SGK7 SQ MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL TT3SGK7 TT Clinical trial TTPBZUO ID TTPBZUO TTPBZUO TN Clostridium difficile DNA gyrase (CD gyr) TTPBZUO UP P94605; P94604 TTPBZUO UC GYRA_CLOAB; GYRB_CLOAB TTPBZUO GN CD gyrA; CD gyrB TTPBZUO TT Clinical trial TTMXD0O ID TTMXD0O TTMXD0O TN Coagulation factor XII (F12) TTMXD0O UP P00748 TTMXD0O UC FA12_HUMAN TTMXD0O SN Hageman factor; HAF TTMXD0O GN F12 TTMXD0O EC EC 3.4.21.38 TTMXD0O SQ MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS TTMXD0O TT Clinical trial TTWE5PB ID TTWE5PB TTWE5PB TN C-X-C motif chemokine 9 (CXCL9) TTWE5PB UP Q07325 TTWE5PB UC CXCL9_HUMAN TTWE5PB SN Gamma-interferon-induced monokine; Monokine induced by interferon-gamma; HuMIG; MIG; Small-inducible cytokine B9 TTWE5PB GN CXCL9 TTWE5PB FC Cytokine that affects the growth, movement, or activation state of cells that participate in immune and inflammatory response. Chemotactic for activated T-cells. Binds to CXCR3. TTWE5PB SQ MKKSGVLFLLGIILLVLIGVQGTPVVRKGRCSCISTNQGTIHLQSLKDLKQFAPSPSCEKIEIIATLKNGVQTCLNPDSADVKELIKKWEKQVSQKKKQKNGKKHQKKKVLKVRKSQRSRQKKTT TTWE5PB TT Clinical trial TTJ21A9 ID TTJ21A9 TTJ21A9 TN Cyclin-dependent kinase 12 (CDK12) TTJ21A9 UP Q9NYV4 TTJ21A9 UC CDK12_HUMAN TTJ21A9 SN Cdc2-related kinase, arginine/serine-rich; CrkRS; Cell division cycle 2-related protein kinase 7; CDC2-related protein kinase 7; Cell division protein kinase 12; hCDK12 TTJ21A9 GN CDK12 TTJ21A9 FC Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors. TTJ21A9 EC EC 2.7.11.22 TTJ21A9 SQ MPNSERHGGKKDGSGGASGTLQPSSGGGSSNSRERHRLVSKHKRHKSKHSKDMGLVTPEAASLGTVIKPLVEYDDISSDSDTFSDDMAFKLDRRENDERRGSDRSDRLHKHRHHQHRRSRDLLKAKQTEKEKSQEVSSKSGSMKDRISGSSKRSNEETDDYGKAQVAKSSSKESRSSKLHKEKTRKERELKSGHKDRSKSHRKRETPKSYKTVDSPKRRSRSPHRKWSDSSKQDDSPSGASYGQDYDLSPSRSHTSSNYDSYKKSPGSTSRRQSVSPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSYSGRSPSPYGRRRSSSPFLSKRSLSRSPLPSRKSMKSRSRSPAYSRHSSSHSKKKRSSSRSRHSSISPVRLPLNSSLGAELSRKKKERAAAAAAAKMDGKESKGSPVFLPRKENSSVEAKDSGLESKKLPRSVKLEKSAPDTELVNVTHLNTEVKNSSDTGKVKLDENSEKHLVKDLKAQGTRDSKPIALKEEIVTPKETETSEKETPPPLPTIASPPPPLPTTTPPPQTPPLPPLPPIPALPQQPPLPPSQPAFSQVPASSTSTLPPSTHSKTSAVSSQANSQPPVQVSVKTQVSVTAAIPHLKTSTLPPLPLPPLLPGDDDMDSPKETLPSKPVKKEKEQRTRHLLTDLPLPPELPGGDLSPPDSPEPKAITPPQQPYKKRPKICCPRYGERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLIHRSVVNMKEIVTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLEYCHKKNFLHRDIKCSNILLNNSGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMAPPDLPHWQDCHELWSKKRRRQRQSGVVVEEPPPSKTSRKETTSGTSTEPVKNSSPAPPQPAPGKVESGAGDAIGLADITQQLNQSELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTEATSQQQDSETMAPEESLKEAPSAPVILPSAEQTTLEASSTPADMQNILAVLLSQLMKTQEPAGSLEENNSDKNSGPQGPRRTPTMPQEEAAACPPHILPPEKRPPEPPGPPPPPPPPPLVEGDLSSAPQELNPAVTAALLQLLSQPEAEPPGHLPHEHQALRPMEYSTRPRPNRTYGNTDGPETGFSAIDTDERNSGPALTESLVQTLVKNRTFSGSLSHLGESSSYQGTGSVQFPGDQDLRFARVPLALHPVVGQPFLKAEGSSNSVVHAETKLQNYGELGPGTTGASSSGAGLHWGGPTQSSAYGKLYRGPTRVPPRGGRGRGVPY TTJ21A9 TT Clinical trial TTNABU9 ID TTNABU9 TTNABU9 TN Cyclin-dependent kinase 19 (CDK19) TTNABU9 UP Q9BWU1 TTNABU9 UC CDK19_HUMAN TTNABU9 SN CDC2-related protein kinase 6; Cell division cycle 2-like protein kinase 6; Cell division protein kinase 19; Cyclin-dependent kinase 11; Death-preventing kinase TTNABU9 GN CDK19 TTNABU9 FC cytosol, mediator complex, nucleus, cyclin-dependent protein serine/threonine kinase activity, RNA polymerase II CTD heptapeptide repeat kinase activity, protein phosphorylation TTNABU9 EC EC 2.7.11.22 TTNABU9 SQ MDYDFKAKLAAERERVEDLFEYEGCKVGRGTYGHVYKARRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQEDPLPTLDVFAGCQIPYPKREFLNEDDPEEKGDKNQQQQQNQHQQPTAPPQQAAAPPQAPPPQQNSTQTNGTAGGAGAGVGGTGAGLQHSQDSSLNQVPPNKKPRLGPSGANSGGPVMPSDYQHSSSRLNYQSSVQGSSQSQSTLGYSSSSQQSSQYHPSHQAHRY TTNABU9 TT Clinical trial TT8N5V1 ID TT8N5V1 TT8N5V1 TN DGAT2 messenger RNA (DGAT2 mRNA) TT8N5V1 UP Q96PD7 TT8N5V1 UC DGAT2_HUMAN TT8N5V1 SN Acyl-CoA retinol O-fatty-acyltransferase; ARAT; Retinol O-fatty-acyltransferase; Diglyceride acyltransferase 2 TT8N5V1 GN DGAT2 TT8N5V1 FC Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides (By similarity). Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG). TT8N5V1 EC EC 2.3.1.20 TT8N5V1 SQ MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHTMYMEALVKLFDKHKTKFGLPETEVLEVN TT8N5V1 TT Clinical trial TTA0XPV ID TTA0XPV TTA0XPV TN DNA polymerase beta (POLB) TTA0XPV UP P06746 TTA0XPV UC DPOLB_HUMAN TTA0XPV GN POLB TTA0XPV FC Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. TTA0XPV EC EC 2.7.7.7 TTA0XPV SQ MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE TTA0XPV TT Clinical trial TTVRA5G ID TTVRA5G TTVRA5G TN DNM2 messenger RNA (DNM2 mRNA) TTVRA5G UP P50570 TTVRA5G UC DYN2_HUMAN TTVRA5G GN DNM2 TTVRA5G FC Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Plays an important role in vesicular trafficking processes, in particular endocytosis. Involved in cytokinesis. Regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (By similarity). TTVRA5G EC EC 3.6.5.5 TTVRA5G SQ MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEHAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDLFPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD TTVRA5G TT Clinical trial TT2M7YX ID TT2M7YX TT2M7YX TN EGFR Exon20ins mutant (EGFR Exon20ins) TT2M7YX UP P00533 TT2M7YX UC EGFR_HUMAN TT2M7YX GN EGFR TT2M7YX SQ MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA TT2M7YX TT Clinical trial TTE8LGD ID TTE8LGD TTE8LGD TN EGR1 messenger RNA (EGR1 mRNA) TTE8LGD UP P18146 TTE8LGD UC EGR1_HUMAN TTE8LGD SN EGR-1; AT225; Nerve growth factor-induced protein A; NGFI-A; Transcription factor ETR103; Transcription factor Zif268; Zinc finger protein 225; Zinc finger protein Krox-24 TTE8LGD GN EGR1 TTE8LGD FC Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (By similarity). Binds double-stranded target DNA, irrespective of the cytosine methylation status. Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia. Plays a role in the regulation of cell survival, proliferation and cell death. Activates expression of p53/TP53 and TGFB1, and thereby helps prevent tumor formation. Required for normal progress through mitosis and normal proliferation of hepatocytes after partial hepatectomy. Mediates responses to ischemia and hypoxia; regulates the expression of proteins such as IL1B and CXCL2 that are involved in inflammatory processes and development of tissue damage after ischemia. Regulates biosynthesis of luteinizing hormone (LHB) in the pituitary (By similarity). Regulates the amplitude of the expression rhythms of clock genes: ARNTL/BMAL1, PER2 and NR1D1 in the liver via the activation of PER1 (clock repressor) transcription. Regulates the rhythmic expression of core-clock gene ARNTL/BMAL1 in the suprachiasmatic nucleus (SCN) (By similarity). TTE8LGD SQ MAAAKAEMQLMSPLQISDPFGSFPHSPTMDNYPKLEEMMLLSNGAPQFLGAAGAPEGSGSNSSSSSSGGGGGGGGGSNSSSSSSTFNPQADTGEQPYEHLTAESFPDISLNNEKVLVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPASSSSAPSPAASSASASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPAAKGGFQVPMIPDYLFPQQQGDLGLGTPDQKPFQGLESRTQQPSLTPLSTIKAFATQSGSQDLKALNTSYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKADKSVVASSATSSLSSYPSPVATSYPSPVTTSYPSPATTSYPSPVPTSFSSPGSSTYPSPVHSGFPSPSVATTYSSVPPAFPAQVSSFPSSAVTNSFSASTGLSDMTATFSPRTIEIC TTE8LGD TT Clinical trial TTHOM2S ID TTHOM2S TTHOM2S TN EWS-FLI1 fusion gene mRNA (EWS-FLI1 mRNA) TTHOM2S UP Q01844-Q01543 TTHOM2S UC EWS_HUMAN-FLI1_HUMAN TTHOM2S GN EWS-FLI1 TTHOM2S TT Clinical trial TTLQTHB ID TTLQTHB TTLQTHB TN Extracellular sulfatase Sulf-2 (SULF2) TTLQTHB UP Q8IWU5 TTLQTHB UC SULF2_HUMAN TTLQTHB SN hSulf-2 TTLQTHB GN SULF2 TTLQTHB FC Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin. TTLQTHB EC EC 3.1.6.- TTLQTHB SQ MGPPSLVLCLLSATVFSLLGGSSAFLSHHRLKGRFQRDRRNIRPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHGSDYSKDYLTDLITNDSVSFFRTSKKMYPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPVNRFHLKKKMRVWRDSFLVERGKLLHKRDNDKVDAQEENFLPKYQRVKDLCQRAEYQTACEQLGQKWQCVEDATGKLKLHKCKGPMRLGGSRALSNLVPKYYGQGSEACTCDSGDYKLSLAGRRKKLFKKKYKASYVRSRSIRSVAIEVDGRVYHVGLGDAAQPRNLTKRHWPGAPEDQDDKDGGDFSGTGGLPDYSAANPIKVTHRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHKISYHTQHKGRLKHRGSSLHPFRKGLQEKDKVWLLREQKRKKKLRKLLKRLQNNDTCSMPGLTCFTHDNQHWQTAPFWTLGPFCACTSANNNTYWCMRTINETHNFLFCEFATGFLEYFDLNTDPYQLMNAVNTLDRDVLNQLHVQLMELRSCKGYKQCNPRTRNMDLGLKDGGSYEQYRQFQRRKWPEMKRPSSKSLGQLWEGWEG TTLQTHB TT Clinical trial TTV5HJS ID TTV5HJS TTV5HJS TN Fanconi anemia group A protein (FANCA) TTV5HJS UP O15360 TTV5HJS UC FANCA_HUMAN TTV5HJS SN Protein FACA TTV5HJS GN FANCA TTV5HJS FC DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be involved in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. TTV5HJS SQ MSDSWVPNSASGQDPGGRRRAWAELLAGRVKREKYNPERAQKLKESAVRLLRSHQDLNALLLEVEGPLCKKLSLSKVIDCDSSEAYANHSSSFIGSALQDQASRLGVPVGILSAGMVASSVGQICTAPAETSHPVLLTVEQRKKLSSLLEFAQYLLAHSMFSRLSFCQELWKIQSSLLLEAVWHLHVQGIVSLQELLESHPDMHAVGSWLFRNLCCLCEQMEASCQHADVARAMLSDFVQMFVLRGFQKNSDLRRTVEPEKMPQVTVDVLQRMLIFALDALAAGVQEESSTHKIVRCWFGVFSGHTLGSVISTDPLKRFFSHTLTQILTHSPVLKASDAVQMQREWSFARTHPLLTSLYRRLFVMLSAEELVGHLQEVLETQEVHWQRVLSFVSALVVCFPEAQQLLEDWVARLMAQAFESCQLDSMVTAFLVVRQAALEGPSAFLSYADWFKASFGSTRGYHGCSKKALVFLFTFLSELVPFESPRYLQVHILHPPLVPGKYRSLLTDYISLAKTRLADLKVSIENMGLYEDLSSAGDITEPHSQALQDVEKAIMVFEHTGNIPVTVMEASIFRRPYYVSHFLPALLTPRVLPKVPDSRVAFIESLKRADKIPPSLYSTYCQACSAAEEKPEDAALGVRAEPNSAEEPLGQLTAALGELRASMTDPSQRDVISAQVAVISERLRAVLGHNEDDSSVEISKIQLSINTPRLEPREHMAVDLLLTSFCQNLMAASSVAPPERQGPWAALFVRTMCGRVLPAVLTRLCQLLRHQGPSLSAPHVLGLAALAVHLGESRSALPEVDVGPPAPGAGLPVPALFDSLLTCRTRDSLFFCLKFCTAAISYSLCKFSSQSRDTLCSCLSPGLIKKFQFLMFRLFSEARQPLSEEDVASLSWRPLHLPSADWQRAALSLWTHRTFREVLKEEDVHLTYQDWLHLELEIQPEADALSDTERQDFHQWAIHEHFLPESSASGGCDGDLQAACTILVNALMDFHQSSRSYDHSENSDLVFGGRTGNEDIISRLQEMVADLELQQDLIVPLGHTPSQEHFLFEIFRRRLQALTSGWSVAASLQRQRELLMYKRILLRLPSSVLCGSSFQAEQPITARCEQFFHLVNSEMRNFCSHGGALTQDITAHFFRGLLNACLRSRDPSLMVDFILAKCQTKCPLILTSALVWWPSLEPVLLCRWRRHCQSPLPRELQKLQEGRQFASDFLSPEAASPAPNPDWLSAAALHFAIQQVREENIRKQLKKLDCEREELLVFLFFFSLMGLLSSHLTSNSTTDLPKAFHVCAAILECLEKRKISWLALFQLTESDLRLGRLLLRVAPDQHTRLLPFAFYSLLSYFHEDAAIREEAFLHVAVDMYLKLVQLFVAGDTSTVSPPAGRSLELKGQGNPVELITKARLFLLQLIPRCPKKSFSHVAELLADRGDCDPEVSAALQSRQQAAPDADLSQEPHLF TTV5HJS TT Clinical trial TTSKL3G ID TTSKL3G TTSKL3G TN FAS-associated factor 1 (FAF1) TTSKL3G UP Q9UNN5 TTSKL3G UC FAF1_HUMAN TTSKL3G SN hFAF1; UBX domain-containing protein 12; UBX domain-containing protein 3A TTSKL3G GN FAF1 TTSKL3G FC Ubiquitin-binding protein. Required for the progression of DNA replication forks by targeting DNA replication licensing factor CDT1 for degradation. Potentiates but cannot initiate FAS-induced apoptosis (By similarity). TTSKL3G SQ MASNMDREMILADFQACTGIENIDEAITLLEQNNWDLVAAINGVIPQENGILQSEYGGETIPGPAFNPASHPASAPTSSSSSAFRPVMPSRQIVERQPRMLDFRVEYRDRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVLKSLHLPKNNSLYVLTPDLPPPSSSSHAGALQESLNQNFMLIITHREVQREYNLNFSGSSTIQEVKRNVYDLTSIPVRHQLWEGWPTSATDDSMCLAESGLSYPCHRLTVGRRSSPAQTREQSEEQITDVHMVSDSDGDDFEDATEFGVDDGEVFGMASSALRKSPMMPENAENEGDALLQFTAEFSSRYGDCHPVFFIGSLEAAFQEAFYVKARDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDSNRARFLTMCNRHFGSVVAQTIRTQKTDQFPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIFTAQQQEDIKDEDEREARENVKREQDEAYRLSLEADRAKREAHEREMAEQFRLEQIRKEQEEEREAIRLSLEQALPPEPKEENAEPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLEAKE TTSKL3G TT Clinical trial TT1X3QF ID TT1X3QF TT1X3QF TN FOXP3 messenger RNA (FOXP3 mRNA) TT1X3QF UP Q9BZS1 TT1X3QF UC FOXP3_HUMAN TT1X3QF SN Scurfin TT1X3QF GN FOXP3 TT1X3QF FC Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells. Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases. The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon-gamma (IFNG). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2. Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7. Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1. Inhibits the differentiation of IL17 producing helper T-cells (Th17) by antagonizing RORC function, leading to down-regulation of IL17 expression, favoring Treg development. Inhibits the transcriptional activator activity of RORA. Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4 (By similarity). TT1X3QF SQ MPNPRPGKPSAPSLALGPSPGASPSWRAAPKASDLLGARGPGGTFQGRDLRGGAHASSSSLNPMPPSQLQLPTLPLVMVAPSGARLGPLPHLQALLQDRPHFMHQLSTVDAHARTPVLQVHPLESPAMISLTPPTTATGVFSLKARPGLPPGINVASLEWVSREPALLCTFPNPSAPRKDSTLSAVPQSSYPLLANGVCKWPGCEKVFEEPEDFLKHCQADHLLDEKGRAQCLLQREMVQSLEQQLVLEKEKLSAMQAHLAGKMALTKASSVASSDKGSCCIVAAGSQGPVVPAWSGPREAPDSLFAVRRHLWGSHGNSTFPEFLHNMDYFKFHNMRPPFTYATLIRWAILEAPEKQRTLNEIYHWFTRMFAFFRNHPATWKNAIRHNLSLHKCFVRVESEKGAVWTVDELEFRKKRSQRPSRCSNPTPGP TT1X3QF TT Clinical trial TTP1S2F ID TTP1S2F TTP1S2F TN Frizzled-10 (FZD10) TTP1S2F UP Q9ULW2 TTP1S2F UC FZD10_HUMAN TTP1S2F SN Fz-10; hFz10; FzE7; DE AltName: CD_antigen=CD350 TTP1S2F GN FZD10 TTP1S2F FC Receptor for Wnt proteins. Functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable). TTP1S2F SQ MQRPGPRLWLVLQVMGSCAAISSMDMERPGDGKCQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHGHLRFFLCSLYAPMCTEQVSTPIPACRVMCEQARLKCSPIMEQFNFKWPDSLDCRKLPNKNDPNYLCMEAPNNGSDEPTRGSGLFPPLFRPQRPHSAQEHPLKDGGPGRGGCDNPGKFHHVEKSASCAPLCTPGVDVYWSREDKRFAVVWLAIWAVLCFFSSAFTVLTFLIDPARFRYPERPIIFLSMCYCVYSVGYLIRLFAGAESIACDRDSGQLYVIQEGLESTGCTLVFLVLYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIEANSSYFHLAAWAIPAVKTILILVMRRVAGDELTGVCYVGSMDVNALTGFVLIPLACYLVIGTSFILSGFVALFHIRRVMKTGGENTDKLEKLMVRIGLFSVLYTVPATCVIACYFYERLNMDYWKILAAQHKCKMNNQTKTLDCLMAASIPAVEIFMVKIFMLLVVGITSGMWIWTSKTLQSWQQVCSRRLKKKSRRKPASVITSGGIYKKAQHPQKTHHGKYEIPAQSPTCV TTP1S2F TT Clinical trial TTVO9RI ID TTVO9RI TTVO9RI TN Fungal Probable histone deacetylase HOS2 (Fung HOS2) TTVO9RI UP P53096 TTVO9RI UC HOS2_YEAST TTVO9RI GN Fung HOS2 TTVO9RI FC Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). It is apparently involved in transcriptional activation. TTVO9RI EC EC 3.5.1.98 TTVO9RI SQ MSGTFSYDVKTKENEPLFEFNSAYSPRVSYHFNSKVSHYHYGVKHPMKPFRLMLTDHLVSSYGLHKIMDLYETRSATRDELLQFHSEDYVNFLSKVSPENANKLPRGTLENFNIGDDCPIFQNLYDYTTLYTGASLDATRKLINNQSDIAINWSGGLHHAKKNSPSGFCYVNDIVLSILNLLRYHPRILYIDIDLHHGDGVQEAFYTTDRVFTLSFHKYNGEFFPGTGDLTEIGCDKGKHFALNVPLEDGIDDDSYINLFKSIVDPLIMTFKPTLIVQQCGADSLGHDRLGCFNLNIKAHGECVKFVKSFGLPMLVVGGGGYTPRNVSRLWTYETGILNDVLLPEDIPEDIPFRDSFGPDYSLYPMLDDLYENKNSKKLLEDIRIRCLENIRYLQGAPSVRMDAECIPTQDISALTEEEDKIIQEMNEETEADSSNRLEEMEKENSGLIAFS TTVO9RI TT Clinical trial TTE61UB ID TTE61UB TTE61UB TN GDNF family receptor alpha-like (GFRAL) TTE61UB UP Q6UXV0 TTE61UB UC GFRAL_HUMAN TTE61UB GN GFRAL TTE61UB FC Brainstem-restricted receptor for GDF15 which regulates food intake, energy expenditure and body weight in response to metabolic and toxin-induced stresses. Upon interaction with its ligand, GDF15, interacts with RET and induces cellular signaling through activation of MAPK- and AKT- signaling pathways. TTE61UB SQ MIVFIFLAMGLSLENEYTSQTNNCTYLREQCLRDANGCKHAWRVMEDACNDSDPGDPCKMRNSSYCNLSIQYLVESNFQFKECLCTDDFYCTVNKLLGKKCINKSDNVKEDKFKWNLTTRSHHGFKGMWSCLEVAEACVGDVVCNAQLASYLKACSANGNPCDLKQCQAAIRFFYQNIPFNIAQMLAFCDCAQSDIPCQQSKEALHSKTCAVNMVPPPTCLSVIRSCQNDELCRRHYRTFQSKCWQRVTRKCHEDENCISTLSKQDLTCSGSDDCKAAYIDILGTVLQVQCTCRTITQSEESLCKIFQHMLHRKSCFNYPTLSNVKGMALYTRKHANKITLTGFHSPFNGEVIYAAMCMTVTCGILLLVMVKLRTSRISSKARDPSSIQIPGEL TTE61UB TT Clinical trial TT26C7Z ID TT26C7Z TT26C7Z TN G-protein coupled receptor 20 (GPR20) TT26C7Z UP Q99678 TT26C7Z UC GPR20_HUMAN TT26C7Z GN GPR20 TT26C7Z FC Orphan receptor with constitutive G(i) signaling activity that activate cyclic AMP. TT26C7Z SQ MPSVSPAGPSAGAVPNATAVTTVRTNASGLEVPLFHLFARLDEELHGTFPGLWLALMAVHGAIFLAGLVLNGLALYVFCCRTRAKTPSVIYTINLVVTDLLVGLSLPTRFAVYYGARGCLRCAFPHVLGYFLNMHCSILFLTCICVDRYLAIVRPEGSRRCRQPACARAVCAFVWLAAGAVTLSVLGVTGSRPCCRVFALTVLEFLLPLLVISVFTGRIMCALSRPGLLHQGRQRRVRAMQLLLTVLIIFLVCFTPFHARQVAVALWPDMPHHTSLVVYHVAVTLSSLNSCMDPIVYCFVTSGFQATVRGLFGQHGEREPSSGDVVSMHRSSKGSGRHHILSAGPHALTQALANGPEA TT26C7Z TT Clinical trial TTHRAPJ ID TTHRAPJ TTHRAPJ TN G-protein coupled receptor C 5D (GPRC5D) TTHRAPJ UP Q9NZD1 TTHRAPJ UC GPC5D_HUMAN TTHRAPJ GN GPRC5D TTHRAPJ FC extracellular exosome, intracellular membrane-bounded organelle, plasma membrane, receptor complex, protein kinase activator activity TTHRAPJ SQ MYKDCIESTGDYFLLCDAEGPWGIILESLAILGIVVTILLLLAFLFLMRKIQDCSQWNVLPTQLLFLLSVLGLFGLAFAFIIELNQQTAPVRYFLFGVLFALCFSCLLAHASNLVKLVRGCVSFSWTTILCIAIGCSLLQIIIATEYVTLIMTRGMMFVNMTPCQLNVDFVVLLVYVLFLMALTFFVSKATFCGPCENWKQHGRLIFITVLFSIIIWVVWISMLLRGNPQFQRQPQWDDPVVCIALVTNAWVFLLLYIVPELCILYRSCRQECPLQGNACPVTAYQHSFQVENQELSRARDSDGAEEDVALTSYGTPIQPQTVDPTQECFIPQAKLSPQQDAGGV TTHRAPJ TT Clinical trial TT48Z3K ID TT48Z3K TT48Z3K TN GSTP1 messenger RNA (GSTP1 mRNA) TT48Z3K UP P09211 TT48Z3K UC GSTP1_HUMAN TT48Z3K SN GST class-pi; GSTP1-1 TT48Z3K GN GSTP1 TT48Z3K FC Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. TT48Z3K EC EC 2.5.1.18 TT48Z3K SQ MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ TT48Z3K TT Clinical trial TTS58YO ID TTS58YO TTS58YO TN HAO1 messenger RNA (HAO1 mRNA) TTS58YO UP Q9UJM8 TTS58YO UC HAOX1_HUMAN TTS58YO SN HAOX1; Glycolate oxidase; GOX TTS58YO GN HAO1 TTS58YO FC Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate. TTS58YO EC EC 1.1.3.15 TTS58YO SQ MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQLRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLAVSKI TTS58YO TT Clinical trial TTM42UJ ID TTM42UJ TTM42UJ TN Hepatitis B virus Capsid protein (HBV C) TTM42UJ UP P03146 TTM42UJ UC CAPSD_HBVD3 TTM42UJ SN Core antigen; Core protein; HBcAg; p21.5 TTM42UJ GN HBV C TTM42UJ FC Self assembles to form an icosahedral capsid. Most capsid appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsid are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stucked in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genome for transcription, or bud through the endoplasmic reticulum to provide new virions. TTM42UJ SQ MDIDPYKEFGATVELLSFLPSDFFPSVRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMTLATWVGVNLEDPASRDLVVSYVNTNMGLKFRQLLWFHISCLTFGRETVIEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC TTM42UJ TT Clinical trial TTINUYD ID TTINUYD TTINUYD TN Hepatitis B virus Large envelope protein (HBV S) TTINUYD UP P03138 TTINUYD UC HBSAG_HBVD3 TTINUYD SN L glycoprotein; L-HBsAg; LHB; Large S protein; Large surface protein; Major surface antigen; L glycoprotein; L-HBsAg; LHB; Large S protein; Large surface protein; Major surface antigen TTINUYD GN HBV S TTINUYD FC The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. TTINUYD SQ MGQNLSTSNPLGFFPDHQLDPAFRANTANPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGILQTLPANPPPASTNRQSGRQPTPLSPPLRNTHPQAMQWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVLTTASPLSSIFSRIGDPALNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPTSNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCMTTAQGTSMYPSCCCTKPSDGNCTCIPIPSSWAFGKFLWEWASARFSWLSLLVPFVQWFVGLSPTVWLSVIWMMWYWGPSLYSILSPFLPLLPIFFCLWVYI TTINUYD TT Clinical trial TTSJVOI ID TTSJVOI TTSJVOI TN Hepatitis B virus Large envelope protein messenger RNA (HBV S mRNA) TTSJVOI UP P03138 TTSJVOI UC HBSAG_HBVD3 TTSJVOI SN L glycoprotein; L-HBsAg; LHB; Large S protein; Large surface protein; Major surface antigen; L glycoprotein; L-HBsAg; LHB; Large S protein; Large surface protein; Major surface antigen TTSJVOI GN HBV S mRNA TTSJVOI FC The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. TTSJVOI SQ MGQNLSTSNPLGFFPDHQLDPAFRANTANPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGILQTLPANPPPASTNRQSGRQPTPLSPPLRNTHPQAMQWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVLTTASPLSSIFSRIGDPALNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPTSNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCMTTAQGTSMYPSCCCTKPSDGNCTCIPIPSSWAFGKFLWEWASARFSWLSLLVPFVQWFVGLSPTVWLSVIWMMWYWGPSLYSILSPFLPLLPIFFCLWVYI TTSJVOI TT Clinical trial TT43YWN ID TT43YWN TT43YWN TN Hepatitis B virus messenger RNA (HBV mRNA) TT43YWN UP Family TT43YWN UC NOUNIPROTAC TT43YWN BC mRNA target TT43YWN SN mRNA of HBV protein TT43YWN GN NO-GeName TT43YWN TT Clinical trial TTWSF5D ID TTWSF5D TTWSF5D TN HRSV Nucleoprotein messenger RNA (HRSV N mRNA) TTWSF5D UP P03418 TTWSF5D UC NCAP_HRSVA TTWSF5D SN Protein N; Nucleocapsid protein TTWSF5D GN HRSV N mRNA TTWSF5D FC Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases. RNA replication depends on the availability of soluble nucleoprotein. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Together with the phosphoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway. May also act as a modulator of the innate immune response by sequestration of host IFIH1/MDA5 and MAVS into IBs. TTWSF5D SQ MALSKVKLNDTLNKDQLLSSSKYTIQRSTGDSIDTPNYDVQKHINKLCGMLLITEDANHKFTGLIGMLYAMSRLGREDTIKILRDAGYHVKANGVDVTTHRQDINGKEMKFEVLTLASLTTEIQINIEIESRKSYKKMLKEMGEVAPEYRHDSPDCGMIILCIAALVITKLAAGDRSGLTAVIRRANNVLKNEMKRYKGLLPKDIANSFYEVFEKHPHFIDVFVHFGIAQSSTRGGSRVEGIFAGLFMNAYGAGQVMLRWGVLAKSVKNIMLGHASVQAEMEQVVEVYEYAQKLGGEAGFYHILNNPKASLLSLTQFPHFSSVVLGNAAGLGIMGEYRGTPRNQDLYDAAKAYAEQLKENGVINYSVLDLTAEELEAIKHQLNPKDNDVEL TTWSF5D TT Clinical trial TT6275O ID TT6275O TT6275O TN HRSV RNA-directed RNA polymerase L (HRSV L) TT6275O UP P28887 TT6275O UC L_HRSVA TT6275O SN Protein L; Large structural protein; Replicase; Transcriptase TT6275O GN HRSV L TT6275O FC Responsible for RNA synthesis (replicase and transcriptase), cap addition, and cap methylation. Performs also the polyadenylation of subgenomic mRNAs by a stuttering mechanism at a slipery stop site present at the end of viral genes. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N) (Probable). The viral polymerase binds to the genomic RNA at two differents sites in the 3' leader promoter thereby initiating either genome replication or mRNA transcription. In the transcription mode, the polymerase performs the sequential transcription of all mRNAs using a termination-reinitiation mechanism responding to gene start and gene end signals. Some polymerase disengage from the template at each gene junction, resulting in a decreasing abundance of transcripts from the 3' to the 5' end of the genome (Probable). The first gene is the most transcribed, and the last the least transcribed (Probable). Needs as cofactors the phosphoprotein for processivity and the M2-1 anti-termination protein. Polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation (By similarity). In the replication mode, the polymerase replicates the whole viral genome without recognizing the gene end transcriptional signals. The ability of the polymerase to override the gene end signals as it is producing the antigenome is probably due to replicative RNA becoming encapsidated with nucleoprotein as it is synthesized. TT6275O SQ MDPIINGNSANVYLTDSYLKGVISFSECNALGSYIFNGPYLKNDYTNLISRQNPLIEHMNLKKLNITQSLISKYHKGEIKLEEPTYFQSLLMTYKSMTSSEQIATTNLLKKIIRRAIEISDVKVYAILNKLGLKEKDKIKSNNGQDEDNSVITTIIKDDILSAVKDNQSHLKADKNHSTKQKDTIKTTLLKKLMCSMQHPPSWLIHWFNLYTKLNNILTQYRSNEVKNHGFTLIDNQTLSGFQFILNQYGCIVYHKELKRITVTTYNQFLTWKDISLSRLNVCLITWISNCLNTLNKSLGLRCGFNNVILTQLFLYGDCILKLFHNEGFYIIKEVEGFIMSLILNITEEDQFRKRFYNSMLNNITDAANKAQKNLLSRVCHTLLDKTVSDNIINGRWIILLSKFLKLIKLAGDNNLNNLSELYFLFRIFGHPMVDERQAMDAVKINCNETKFYLLSSLSMLRGAFIYRIIKGFVNNYNRWPTLRNAIVLPLRWLTYYKLNTYPSLLELTERDLIVLSGLRFYREFRLPKKVDLEMIINDKAISPPKNLIWTSFPRNYMPSHIQNYIEHEKLKFSESDKSRRVLEYYLRDNKFNECDLYNCVVNQSYLNNPNHVVSLTGKERELSVGRMFAMQPGMFRQVQILAEKMIAENILQFFPESLTRYGDLELQKILELKAGISNKSNRYNDNYNNYISKCSIITDLSKFNQAFRYETSCICSDVLDELHGVQSLFSWLHLTIPHVTIICTYRHAPPYIGDHIVDLNNVDEQSGLYRYHMGGIEGWCQKLWTIEAISLLDLISLKGKFSITALINGDNQSIDISKPIRLMEGQTHAQADYLLALNSLKLLYKEYAGIGHKLKGTETYISRDMQFMSKTIQHNGVYYPASIKKVLRVGPWINTILDDFKVSLESIGSLTQELEYRGESLLCSLIFRNVWLYNQIALQLKNHALCNNKLYLDILKVLKHLKTFFNLDNIDTALTLYMNLPMLFGGGDPNLLYRSFYRRTPDFLTEAIVHSVFILSYYTNHDLKDKLQDLSDDRLNKFLTCIITFDKNPNAEFVTLMRDPQALGSERQAKITSEINRLAVTEVLSTAPNKIFSKSAQHYTTTEIDLNDIMQNIEPTYPHGLRVVYESLPFYKAEKIVNLISGTKSITNILEKTSAIDLTDIDRATEMMRKNITLLIRILPLDCNRDKREILSMENLSITELSKYVRERSWSLSNIVGVTSPSIMYTMDIKYTTSTISSGIIIEKYNVNSLTRGERGPTKPWVGSSTQEKKTMPVYNRQVLTKKQRDQIDLLAKLDWVYASIDNKDEFMEELSIGTLGLTYEKAKKLFPQYLSVNYLHRLTVSSRPCEFPASIPAYRTTNYHFDTSPINRILTEKYGDEDIDIVFQNCISFGLSLMSVVEQFTNVCPNRIILIPKLNEIHLMKPPIFTGDVDIHKLKQVIQKQHMFLPDKISLTQYVELFLSNKTLKSGSHVNSNLILAHKISDYFHNTYILSTNLAGHWILIIQLMKDSKGIFEKDWGEGYITDHMFINLKVFFNAYKTYLLCFHKGYGKAKLECDMNTSDLLCVLELIDSSYWKSMSKVFLEQKVIKYILSQDASLHRVKGCHSFKLWFLKRLNVAEFTVCPWVVNIDYHPTHMKAILTYIDLVRMGLINIDRIHIKNKHKFNDEFYTSNLFYINYNFSDNTHLLTKHIRIANSELENNYNKLYHPTPETLENILANPIKSNDKKTLNDYCIGKNVDSIMLPLLSNKKLIKSSAMIRTNYSKQDLYNLFPMVVIDRIIDHSGNTAKSNQLYTTTSHQISLVHNSTSLYCMLPWHHINRFNFVFSSTGCKISIEYILKDLKIKDPNCIAFIGEGAGNLLLRTVVELHPDIRYIYRSLKDCNDHSLPIEFLRLYNGHINIDYGENLTIPATDATNNIHWSYLHIKFAEPISLFVCDAELSVTVNWSKIIIEWSKHVRKCKYCSSVNKCMLIVKYHAQDDIDFKLDNITILKTYVCLGSKLKGSEVYLVLTIGPANIFPVFNVVQNAKLILSRTKNFIMPKKADKESIDANIKSLIPFLCYPITKKGINTALSKLKSVVSGDILSYSIAGRNEVFSNKLINHKHMNILKWFNHVLNFRSTELNYNHLYMVESTYPYLSELLNSLTTNELKKLIKITGSLLYNFHNE TT6275O TT Clinical trial TT0R2QD ID TT0R2QD TT0R2QD TN Ig-like domain-containing receptor 2 (ILDR2) TT0R2QD UP Q71H61 TT0R2QD UC ILDR2_HUMAN TT0R2QD GN ILDR2 TT0R2QD FC May be involved in lipid homeostasis and ER stress pathways. TT0R2QD SQ MDRVLLRWISLFWLTAMVEGLQVTVPDKKKVAMLFQPTVLRCHFSTSSHQPAVVQWKFKSYCQDRMGESLGMSSTRAQSLSKRNLEWDPYLDCLDSRRTVRVVASKQGSTVTLGDFYRGREITIVHDADLQIGKLMWGDSGLYYCIITTPDDLEGKNEDSVELLVLGRTGLLADLLPSFAVEIMPEWVFVGLVLLGVFLFFVLVGICWCQCCPHSCCCYVRCPCCPDSCCCPQALYEAGKAAKAGYPPSVSGVPGPYSIPSVPLGGAPSSGMLMDKPHPPPLAPSDSTGGSHSVRKGYRIQADKERDSMKVLYYVEKELAQFDPARRMRGRYNNTISELSSLHEEDSNFRQSFHQMRSKQFPVSGDLESNPDYWSGVMGGSSGASRGPSAMEYNKEDRESFRHSQPRSKSEMLSRKNFATGVPAVSMDELAAFADSYGQRPRRADGNSHEARGGSRFERSESRAHSGFYQDDSLEEYYGQRSRSREPLTDADRGWAFSPARRRPAEDAHLPRLVSRTPGTAPKYDHSYLGSARERQARPEGASRGGSLETPSKRSAQLGPRSASYYAWSPPGTYKAGSSQDDQEDASDDALPPYSELELTRGPSYRGRDLPYHSNSEKKRKKEPAKKTNDFPTRMSLVV TT0R2QD TT Clinical trial TTBRJS9 ID TTBRJS9 TTBRJS9 TN Inhibitory receptor SHPS-1 (SIRPA) TTBRJS9 UP P78324 TTBRJS9 UC SHPS1_HUMAN TTBRJS9 SN SHP substrate 1; SHPS-1; Brain Ig-like molecule with tyrosine-based activation motifs; Bit; CD172 antigen-like family member A; Macrophage fusion receptor; MyD-1 antigen; Signal-regulatory protein alpha-1; Sirp-alpha-1; Signal-regulatory protein alpha-2; Sirp-alpha-2; Signal-regulatory protein alpha-3; Sirp-alpha-3; p84; DE AltName: CD_antigen=CD172a TTBRJS9 GN SIRPA TTBRJS9 FC Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function (By similarity). Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. TTBRJS9 SQ MEPAGPAPGRLGPLLCLLLAASCAWSGVAGEEELQVIQPDKSVLVAAGETATLRCTATSLIPVGPIQWFRGAGPGRELIYNQKEGHFPRVTTVSDLTKRNNMDFSIRIGNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVRAKPSAPVVSGPAARATPQHTVSFTCESHGFSPRDITLKWFKNGNELSDFQTNVDPVGESVSYSIHSTAKVVLTREDVHSQVICEVAHVTLQGDPLRGTANLSETIRVPPTLEVTQQPVRAENQVNVTCQVRKFYPQRLQLTWLENGNVSRTETASTVTENKDGTYNWMSWLLVNVSAHRDDVKLTCQVEHDGQPAVSKSHDLKVSAHPKEQGSNTAAENTGSNERNIYIVVGVVCTLLVALLMAALYLVRIRQKKAQGSTSSTRLHEPEKNAREITQDTNDITYADLNLPKGKKPAPQAAEPNNHTEYASIQTSPQPASEDTLTYADLDMVHLNRTPKQPAPKPEPSFSEYASVQVPRK TTBRJS9 TT Clinical trial TTF95B8 ID TTF95B8 TTF95B8 TN Insulin receptor substrate 2 (IRS2) TTF95B8 UP Q9Y4H2 TTF95B8 UC IRS2_HUMAN TTF95B8 SN IRS-2 TTF95B8 GN IRS2 TTF95B8 FC May mediate the control of various cellular processes by insulin. TTF95B8 SQ MASPPRHGPPGPASGDGPNLNNNNNNNNHSVRKCGYLRKQKHGHKRFFVLRGPGAGGDEATAGGGSAPQPPRLEYYESEKKWRSKAGAPKRVIALDCCLNINKRADAKHKYLIALYTKDEYFAVAAENEQEQEGWYRALTDLVSEGRAAAGDAPPAAAPAASCSASLPGALGGSAGAAGAEDSYGLVAPATAAYREVWQVNLKPKGLGQSKNLTGVYRLCLSARTIGFVKLNCEQPSVTLQLMNIRRCGHSDSFFFIEVGRSAVTGPGELWMQADDSVVAQNIHETILEAMKALKELFEFRPRSKSQSSGSSATHPISVPGARRHHHLVNLPPSQTGLVRRSRTDSLAATPPAAKCSSCRVRTASEGDGGAAAGAAAAGARPVSVAGSPLSPGPVRAPLSRSHTLSGGCGGRGSKVALLPAGGALQHSRSMSMPVAHSPPAATSPGSLSSSSGHGSGSYPPPPGPHPPLPHPLHHGPGQRPSSGSASASGSPSDPGFMSLDEYGSSPGDLRAFCSHRSNTPESIAETPPARDGGGGGEFYGYMTMDRPLSHCGRSYRRVSGDAAQDLDRGLRKRTYSLTTPARQRPVPQPSSASLDEYTLMRATFSGSAGRLCPSCPASSPKVAYHPYPEDYGDIEIGSHRSSSSNLGADDGYMPMTPGAALAGSGSGSCRSDDYMPMSPASVSAPKQILQPRAAAAAAAAVPSAGPAGPAPTSAAGRTFPASGGGYKASSPAESSPEDSGYMRMWCGSKLSMEHADGKLLPNGDYLNVSPSDAVTTGTPPDFFSAALHPGGEPLRGVPGCCYSSLPRSYKAPYTCGGDSDQYVLMSSPVGRILEEERLEPQATPGPSQAASAFGAGPTQPPHPVVPSPVRPSGGRPEGFLGQRGRAVRPTRLSLEGLPSLPSMHEYPLPPEPKSPGEYINIDFGEPGARLSPPAPPLLASAASSSSLLSASSPASSLGSGTPGTSSDSRQRSPLSDYMNLDFSSPKSPKPGAPSGHPVGSLDGLLSPEASSPYPPLPPRPSASPSSSLQPPPPPPAPGELYRLPPASAVATAQGPGAASSLSSDTGDNGDYTEMAFGVAATPPQPIAAPPKPEAARVASPTSGVKRLSLMEQVSGVEAFLQASQPPDPHRGAKVIRADPQGGRRRHSSETFSSTTTVTPVSPSFAHNPKRHNSASVENVSLRKSSEGGVGVGPGGGDEPPTSPRQLQPAPPLAPQGRPWTPGQPGGLVGCPGSGGSPMRRETSAGFQNGLNYIAIDVREEPGLPPQPQPPPPPLPQPGDKSSWGRTRSLGGLISAVGVGSTGGGCGGPGPGALPPANTYASIDFLSHHLKEATIVKE TTF95B8 TT Clinical trial TT7B3HE ID TT7B3HE TT7B3HE TN Integrin alpha-V/beta-8 (ITGAV/B8) TT7B3HE UP P06756-P26012 TT7B3HE UC ITAV_HUMAN-ITB8_HUMAN TT7B3HE GN ITGAV-ITGB8 TT7B3HE TT Clinical trial TTKQSXZ ID TTKQSXZ TTKQSXZ TN Integrin beta-6 (ITGB6) TTKQSXZ UP P18564 TTKQSXZ UC ITB6_HUMAN TTKQSXZ GN ITGB6 TTKQSXZ FC Integrin alpha-V:beta-6 (ITGAV:ITGB6) is a receptor for fibronectin and cytotactin. It recognizes the sequence R-G-D in its ligands. Internalisation of integrin alpha-V/beta-6 via clathrin-mediated endocytosis promotes carcinoma cell invasion. ITGAV:ITGB6 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation. TTKQSXZ SQ MGIELLCLFFLFLGRNDHVQGGCALGGAETCEDCLLIGPQCAWCAQENFTHPSGVGERCDTPANLLAKGCQLNFIENPVSQVEILKNKPLSVGRQKNSSDIVQIAPQSLILKLRPGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTVNIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCECGEDMLSTDSCKEAPDHPSCSGRGDCYCGQCICHLSPYGNIYGPYCQCDNFSCVRHKGLLCGGNGDCDCGECVCRSGWTGEYCNCTTSTDSCVSEDGVLCSGRGDCVCGKCVCTNPGASGPTCERCPTCGDPCNSKRSCIECHLSAAGQAREECVDKCKLAGATISEEEDFSKDGSVSCSLQGENECLITFLITTDNEGKTIIHSINEKDCPKPPNIPMIMLGVSLAILLIGVVLLCIWKLLVSFHDRKEVAKFEAERSKAKWQTGTNPLYRGSTSTFKNVTYKHREKQKVDLSTDC TTKQSXZ TT Clinical trial TTSD92E ID TTSD92E TTSD92E TN Interleukin-1 (IL1) TTSD92E UP Family TTSD92E UC NOUNIPROTAC TTSD92E SN IL-1 TTSD92E GN NO-GeName TTSD92E TT Clinical trial TT5BFT0 ID TT5BFT0 TT5BFT0 TN Interleukin-1 receptor (IL1R) TT5BFT0 UP P14778; P27930 TT5BFT0 UC IL1R1_HUMAN; IL1R2_HUMAN TT5BFT0 GN IL1R1; IL1R2 TT5BFT0 TT Clinical trial TT8SLDN ID TT8SLDN TT8SLDN TN Interleukin-36 gamma (IL36G) TT8SLDN UP Q9NZH8 TT8SLDN UC IL36G_HUMAN TT8SLDN SN IL-1-related protein 2; IL-1RP2; Interleukin-1 epsilon; IL-1 epsilon; Interleukin-1 family member 9; IL-1F9; Interleukin-1 homolog 1; IL-1H1 TT8SLDN GN IL36G TT8SLDN FC Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. In cultured keratinocytes induces the expression of macrophage, T-cell, and neutrophil chemokines, such as CCL3, CCL4, CCL5, CCL2, CCL17, CCL22, CL20, CCL5, CCL2, CCL17, CCL22, CXCL8, CCL20 and CXCL1; also stimulates its own expression and that of the prototypic cutaneous proinflammatory parameters TNF-alpha, S100A7/psoriasin and inducible NOS. May play a role in proinflammatory responses during particular neutrophilic airway inflammation: activates mitogen-activated protein kinases and NF-kappa B in primary lung fibroblasts, and stimulates the expression of IL-8 and CXCL3 and Th17 chemokine CCL20 in lung fibroblasts. May be involved in the innate immune response to fungal pathogens, such as Aspergillus fumigatus. TT8SLDN SQ MRGTPGDADGGGRAVYQSMCKPITGTINDLNQQVWTLQGQNLVAVPRSDSVTPVTVAVITCKYPEALEQGRGDPIYLGIQNPEMCLYCEKVGEQPTLQLKEQKIMDLYGQPEPVKPFLFYRAKTGRTSTLESVAFPDWFIASSKRDQPIILTSELGKSYNTAFELNIND TT8SLDN TT Clinical trial TTG68FB ID TTG68FB TTG68FB TN Interleukine 12 (IL-12) TTG68FB UP P29459; P29460 TTG68FB UC IL12A_HUMAN; IL12B_HUMAN TTG68FB GN NO-GeName TTG68FB TT Clinical trial TT3LH46 ID TT3LH46 TT3LH46 TN KRAS G12C mutant (KRAS G12C) TT3LH46 UP P01116 TT3LH46 UC RASK_HUMAN TT3LH46 GN KRAS TT3LH46 SQ MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM TT3LH46 TT Clinical trial TT9TVNM ID TT9TVNM TT9TVNM TN KRAS G12D mutant messenger RNA (KRAS mRNA) TT9TVNM UP P01116 TT9TVNM UC RASK_HUMAN TT9TVNM SN K-Ras 2; Ki-Ras; c-K-ras; c-Ki-ras TT9TVNM GN KRAS TT9TVNM FC Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the regulation of cell proliferation. Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner. TT9TVNM EC EC 3.6.5.2 TT9TVNM SQ MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM TT9TVNM TT Clinical trial TTD2IK3 ID TTD2IK3 TTD2IK3 TN Lassa virus Pre-glycoprotein polyprotein GP complex (LASV GPC) TTD2IK3 UP P17332 TTD2IK3 UC GLYC_LASSG TTD2IK3 SN Pre-GP-C TTD2IK3 GN LASV GPC TTD2IK3 SQ MGQIVTFFQEVPHVIEEVMNIVLIALSILAILKGLYNVATCGLIGLVTFLLLSGRSCSLIYKGTYELQTLELNMETLNMTMPLSCTKNNSHHYIRVGNETGLELTLTNTSILNHKFCNLSDAHKRNLYDHSLMSIISTFHLSIPNFNQYEAMSCDFNGGKITVQYNLSHSFAVDAAGHCGTLANGVLQTFMRMAWGGSYIALDSGRGNWDCIMTSYQYLIIQNTTWDDHCQFSRPSPIGYLGLLSQRTRDIYISRRLLGTFTWTLSDSEGNETPGGYCLTRWMLIEAELKCFGNTAVAKCNEKHDEEFCDMLRLFDFNKQAIRRLKTEAQMSIQLINKAVNALINDQLIMKNHLRDIMGIPYCNYSRYWYLNHTSTGKTSLPRCWLISNGSYLNETKFSDDIEQQADNMITEMLQKEYIDRQGKTPLGLVDLFVFSTSFYLISIFLHLVKIPTHRHIVGKPCPKPHRLNHMGICSCGLYKQPGVPVRWKR TTD2IK3 TT Clinical trial TTW76JE ID TTW76JE TTW76JE TN LDHA messenger RNA (LDHA mRNA) TTW76JE UP P00338 TTW76JE UC LDHA_HUMAN TTW76JE SN LDH-A; Cell proliferation-inducing gene 19 protein; LDH muscle subunit; LDH-M; Renal carcinoma antigen NY-REN-59 TTW76JE GN LDHA TTW76JE EC EC 1.1.1.27 TTW76JE SQ MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF TTW76JE TT Clinical trial TTSVQWU ID TTSVQWU TTSVQWU TN Leishmania major Proteasome (Leishm Proteasome) TTSVQWU UP Q4QH56; Q4Q1Q9 TTSVQWU UC Q4QH56_LEIMA; Q4Q1Q9_LEIMA TTSVQWU GN NOUNIPROTAC TTSVQWU TT Clinical trial TTHC6XU ID TTHC6XU TTHC6XU TN Leukocyte immunoglobulin-like receptor B2 (LILRB2) TTHC6XU UP Q8N423 TTHC6XU UC LIRB2_HUMAN TTHC6XU SN LIR-2; Leukocyte immunoglobulin-like receptor 2; CD85 antigen-like family member D; Immunoglobulin-like transcript 4; ILT-4; Monocyte/macrophage immunoglobulin-like receptor 10; MIR-10; DE AltName: CD_antigen=CD85d TTHC6XU GN LILRB2 TTHC6XU FC Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles. Involved in the down-regulation of the immune response and the development of tolerance. Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide (peptide-bound HLA-G-B2M) triggering differentiation of type 1 regulatory T cells and myeloid-derived suppressor cells, both of which actively maintain maternal-fetal tolerance. Competes with CD8A for binding to class I MHC antigens. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions. TTHC6XU SQ MTPIVTVLICLGLSLGPRTHVQTGTIPKPTLWAEPDSVITQGSPVTLSCQGSLEAQEYRLYREKKSASWITRIRPELVKNGQFHIPSITWEHTGRYGCQYYSRARWSELSDPLVLVMTGAYPKPTLSAQPSPVVTSGGRVTLQCESQVAFGGFILCKEGEEEHPQCLNSQPHARGSSRAIFSVGPVSPNRRWSHRCYGYDLNSPYVWSSPSDLLELLVPGVSKKPSLSVQPGPVVAPGESLTLQCVSDVGYDRFVLYKEGERDLRQLPGRQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSECSAPSDPLDILITGQIRGTPFISVQPGPTVASGENVTLLCQSWRQFHTFLLTKAGAADAPLRLRSIHEYPKYQAEFPMSPVTSAHAGTYRCYGSLNSDPYLLSHPSEPLELVVSGPSMGSSPPPTGPISTPAGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVVLLLLLLLLLFLILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKDTQPEDGVEMDTRAAASEAPQDVTYAQLHSLTLRRKATEPPPSQEREPPAEPSIYATLAIH TTHC6XU TT Clinical trial TTREOKA ID TTREOKA TTREOKA TN Leukocyte immunoglobulin-like receptor B4 (LILRB4) TTREOKA UP Q8NHJ6 TTREOKA UC LIRB4_HUMAN TTREOKA SN CD85 antigen-like family member K; Immunoglobulin-like transcript 3; ILT-3; Leukocyte immunoglobulin-like receptor 5; LIR-5; Monocyte inhibitory receptor HM18; DE AltName: CD_antigen=CD85k TTREOKA GN LILRB4 TTREOKA FC Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Involved in the down-regulation of the immune response and the development of tolerance, e.g. towards transplants. Interferes with TNFRSF5-signaling and NF-kappa-B up-regulation. Inhibits receptor-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions. TTREOKA SQ MIPTFTALLCLGLSLGPRTHMQAGPLPKPTLWAEPGSVISWGNSVTIWCQGTLEAREYRLDKEESPAPWDRQNPLEPKNKARFSIPSMTEDYAGRYRCYYRSPVGWSQPSDPLELVMTGAYSKPTLSALPSPLVTSGKSVTLLCQSRSPMDTFLLIKERAAHPLLHLRSEHGAQQHQAEFPMSPVTSVHGGTYRCFSSHGFSHYLLSHPSDPLELIVSGSLEDPRPSPTRSVSTAAGPEDQPLMPTGSVPHSGLRRHWEVLIGVLVVSILLLSLLLFLLLQHWRQGKHRTLAQRQADFQRPPGAAEPEPKDGGLQRRSSPAADVQGENFCAAVKNTQPEDGVEMDTRQSPHDEDPQAVTYAKVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSFTLRQKATEPPPSQEGASPAEPSVYATLAIH TTREOKA TT Clinical trial TTSI7A8 ID TTSI7A8 TTSI7A8 TN Leukocyte-associated Ig-like receptor 1 (LAIR1) TTSI7A8 UP Q6GTX8 TTSI7A8 UC LAIR1_HUMAN TTSI7A8 SN LAIR-1; hLAIR1; DE AltName: CD_antigen=CD305 TTSI7A8 GN LAIR1 TTSI7A8 FC Functions as an inhibitory receptor that plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation. May also play its inhibitory role independently of SH2-containing phosphatases. Modulates cytokine production in CD4+ T-cells, down-regulating IL2 and IFNG production while inducing secretion of transforming growth factor beta. Down-regulates also IgG and IgE production in B-cells as well as IL8, IL10 and TNF secretion. Inhibits proliferation and induces apoptosis in myeloid leukemia cell lines as well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA and phosphorylation of I-kappa-B alpha/CHUK in these cells. Inhibits the differentiation of peripheral blood precursors towards dendritic cells. TTSI7A8 SQ MSPHPTALLGLVLCLAQTIHTQEEDLPRPSISAEPGTVIPLGSHVTFVCRGPVGVQTFRLERESRSTYNDTEDVSQASPSESEARFRIDSVSEGNAGPYRCIYYKPPKWSEQSDYLELLVKETSGGPDSPDTEPGSSAGPTQRPSDNSHNEHAPASQGLKAEHLYILIGVSVVFLFCLLLLVLFCLHRQNQIKQGPPRSKDEEQKPQQRPDLAVDVLERTADKATVNGLPEKDRETDTSALAAGSSQEVTYAQLDHWALTQRTARAVSPQSTKPMAESITYAAVARH TTSI7A8 TT Clinical trial TT3GKN5 ID TT3GKN5 TT3GKN5 TN Lipase unspecific (LIP) TT3GKN5 UP Family TT3GKN5 UC NOUNIPROTAC TT3GKN5 BC Ester hydrolase TT3GKN5 GN NO-GeName TT3GKN5 TT Clinical trial TT7VMG4 ID TT7VMG4 TT7VMG4 TN Low-density lipoprotein receptor-related protein 5 (LRP5) TT7VMG4 UP O75197 TT7VMG4 UC LRP5_HUMAN TT7VMG4 SN LRP-5; Low-density lipoprotein receptor-related protein 7; LRP-7 TT7VMG4 GN LRP5 TT7VMG4 FC Acts as a coreceptor with members of the frizzled family of seven-transmembrane spanning receptors to transduce signal by Wnt proteins. Activates the canonical Wnt signaling pathway that controls cell fate determination and self-renewal during embryonic development and adult tissue regeneration. In particular, may play an important role in the development of the posterior patterning of the epiblast during gastrulation (By similarity). During bone development, regulates osteoblast proliferation and differentiation thus determining bone mass. Mechanistically, the formation of the signaling complex between Wnt ligand, frizzled receptor and LRP5 coreceptor promotes the recruitment of AXIN1 to LRP5, stabilizing beta-catenin/CTNNB1 and activating TCF/LEF-mediated transcriptional programs. Acts as a coreceptor for non-Wnt proteins, such as norrin/NDP. Binding of norrin/NDP to frizzled 4/FZD4-LRP5 receptor complex triggers beta-catenin/CTNNB1-dependent signaling known to be required for retinal vascular development. Plays a role in controlling postnatal vascular regression in retina via macrophage-induced endothelial cell apoptosis (By similarity). TT7VMG4 SQ MEAAPPGPPWPLLLLLLLLLALCGCPAPAAASPLLLFANRRDVRLVDAGGVKLESTIVVSGLEDAAAVDFQFSKGAVYWTDVSEEAIKQTYLNQTGAAVQNVVISGLVSPDGLACDWVGKKLYWTDSETNRIEVANLNGTSRKVLFWQDLDQPRAIALDPAHGYMYWTDWGETPRIERAGMDGSTRKIIVDSDIYWPNGLTIDLEEQKLYWADAKLSFIHRANLDGSFRQKVVEGSLTHPFALTLSGDTLYWTDWQTRSIHACNKRTGGKRKEILSALYSPMDIQVLSQERQPFFHTRCEEDNGGCSHLCLLSPSEPFYTCACPTGVQLQDNGRTCKAGAEEVLLLARRTDLRRISLDTPDFTDIVLQVDDIRHAIAIDYDPLEGYVYWTDDEVRAIRRAYLDGSGAQTLVNTEINDPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTSRKILVSEDLDEPRAIALHPVMGLMYWTDWGENPKIECANLDGQERRVLVNASLGWPNGLALDLQEGKLYWGDAKTDKIEVINVDGTKRRTLLEDKLPHIFGFTLLGDFIYWTDWQRRSIERVHKVKASRDVIIDQLPDLMGLKAVNVAKVVGTNPCADRNGGCSHLCFFTPHATRCGCPIGLELLSDMKTCIVPEAFLVFTSRAAIHRISLETNNNDVAIPLTGVKEASALDFDVSNNHIYWTDVSLKTISRAFMNGSSVEHVVEFGLDYPEGMAVDWMGKNLYWADTGTNRIEVARLDGQFRQVLVWRDLDNPRSLALDPTKGYIYWTEWGGKPRIVRAFMDGTNCMTLVDKVGRANDLTIDYADQRLYWTDLDTNMIESSNMLGQERVVIADDLPHPFGLTQYSDYIYWTDWNLHSIERADKTSGRNRTLIQGHLDFVMDILVFHSSRQDGLNDCMHNNGQCGQLCLAIPGGHRCGCASHYTLDPSSRNCSPPTTFLLFSQKSAISRMIPDDQHSPDLILPLHGLRNVKAIDYDPLDKFIYWVDGRQNIKRAKDDGTQPFVLTSLSQGQNPDRQPHDLSIDIYSRTLFWTCEATNTINVHRLSGEAMGVVLRGDRDKPRAIVVNAERGYLYFTNMQDRAAKIERAALDGTEREVLFTTGLIRPVALVVDNTLGKLFWVDADLKRIESCDLSGANRLTLEDANIVQPLGLTILGKHLYWIDRQQQMIERVEKTTGDKRTRIQGRVAHLTGIHAVEEVSLEEFSAHPCARDNGGCSHICIAKGDGTPRCSCPVHLVLLQNLLTCGEPPTCSPDQFACATGEIDCIPGAWRCDGFPECDDQSDEEGCPVCSAAQFPCARGQCVDLRLRCDGEADCQDRSDEADCDAICLPNQFRCASGQCVLIKQQCDSFPDCIDGSDELMCEITKPPSDDSPAHSSAIGPVIGIILSLFVMGGVYFVCQRVVCQRYAGANGPFPHEYVSGTPHVPLNFIAPGGSQHGPFTGIACGKSMMSSVSLMGGRGGVPLYDRNHVTGASSSSSSSTKATLYPPILNPPPSPATDPSLYNMDMFYSSNIPATARPYRPYIIRGMAPPTTPCSTDVCDSDYSASRWKASKYYLDLNSDSDPYPPPPTPHSQYLSAEDSCPPSPATERSYFHLFPPPPSPCTDSS TT7VMG4 TT Clinical trial TTULDG7 ID TTULDG7 TTULDG7 TN Lysosome-associated membrane glycoprotein 2 (LAMP2) TTULDG7 UP P13473 TTULDG7 UC LAMP2_HUMAN TTULDG7 SN LAMP-2; Lysosome-associated membrane protein 2; CD107 antigen-like family member B; LGP-96; DE AltName: CD_antigen=CD107b TTULDG7 GN LAMP2 TTULDG7 FC Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live. Functions by binding target proteins, such as GAPDH and MLLT11, and targeting them for lysosomal degradation. Plays a role in lysosomal protein degradation in response to starvation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy. Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes. Required for normal degradation of the contents of autophagosomes. Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits. Is not required for efficient MHCII-mediated presentation of endogenous antigens. TTULDG7 SQ MVCFRLFPVPGSGLVLVCLVLGAVRSYALELNLTDSENATCLYAKWQMNFTVRYETTNKTYKTVTISDHGTVTYNGSICGDDQNGPKIAVQFGPGFSWIANFTKAASTYSIDSVSFSYNTGDNTTFPDAEDKGILTVDELLAIRIPLNDLFRCNSLSTLEKNDVVQHYWDVLVQAFVQNGTVSTNEFLCDKDKTSTVAPTIHTTVPSPTTTPTPKEKPEAGTYSVNNGNDTCLLATMGLQLNITQDKVASVININPNTTHSTGSCRSHTALLRLNSSTIKYLDFVFAVKNENRFYLKEVNISMYLVNGSVFSIANNNLSYWDAPLGSSYMCNKEQTVSVSGAFQINTFDLRVQPFNVTQGKYSTAQDCSADDDNFLVPIAVGAALAGVLILVLLAYFIGLKHHHAGYEQF TTULDG7 TT Clinical trial TTCI81G ID TTCI81G TTCI81G TN MALT lymphoma-associated translocation (MALT1) TTCI81G UP Q9UDY8 TTCI81G UC MALT1_HUMAN TTCI81G SN MALT lymphoma-associated translocation; Paracaspase TTCI81G GN MALT1 TTCI81G FC Protease that enhances BCL10-induced activation of NF-kappa-B by mediating its cleavage. MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion. Involved in the induction of T helper 17 cells (Th17) differentiation. Cleaves RC3H1 and ZC3H12A in response to T-cell receptor (TCR) stimulation which releases their cooperatively repressed targets to promote Th17 cell differentiation (By similarity). Also mediates cleavage of N4BP1 in T-cells following TCR-mediated activation, leading to N4BP1 inactivation. Also has ubiquitin ligase activity: binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. TTCI81G EC EC 3.4.22.- TTCI81G SQ MSLLGDPLQALPPSAAPTGPLLAPPAGATLNRLREPLLRRLSELLDQAPEGRGWRRLAELAGSRGRLRLSCLDLEQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDFLQAMEHTEVLQLLSPPGIKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPNGNTSELIFNAVHVKDAGFYVCRVNNNFTFEFSQWSQLDVCDIPESFQRSVDGVSESKLQICVEPTSQKLMPGSTLVLQCVAVGSPIPHYQWFKNELPLTHETKKLYMVPYVDLEHQGTYWCHVYNDRDSQDSKKVEIIIGRTDEAVECTEDELNNLGHPDNKEQTTDQPLAKDKVALLIGNMNYREHPKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMRNAVDEFLLLLDKGVYGLLYYAGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCRKRNDYDDTIPILDALKVTANIVFGYATCQGAEAFEIQHSGLANGIFMKFLKDRLLEDKKITVLLDEVAEDMGKCHLTKGKQALEIRSSLSEKRALTDPIQGTEYSAESLVRNLQWAKAHELPESMCLKFDCGVQIQLGFAAEFSNVMIIYTSIVYKPPEIIMCDAYVTDFPLDLDIDPKDANKGTPEETGSYLVSKDLPKHCLYTRLSSLQKLKEHLVFTVCLSYQYSGLEDTVEDKQEVNVGKPLIAKLDMHRGLGRKTCFQTCLMSNGPYQSSAATSGGAGHYHSLQDPFHGVYHSHPGNPSNVTPADSCHCSRTPDAFISSFAHHASCHFSRSNVPVETTDEIPFSFSDRLRISEK TTCI81G TT Clinical trial TTEOSZT ID TTEOSZT TTEOSZT TN Melanocortin receptor (MCR) TTEOSZT UP Family TTEOSZT UC NOUNIPROTAC TTEOSZT SN Melanocortin receptor TTEOSZT GN NO-GeName TTEOSZT TT Clinical trial TTJIWMO ID TTJIWMO TTJIWMO TN Melanoma-associated antigen 6 (MAGEA6) TTJIWMO UP P43360 TTJIWMO UC MAGA6_HUMAN TTJIWMO SN Cancer/testis antigen 1.6; CT1.6; MAGE-6 antigen; MAGE3B antigen TTJIWMO GN MAGEA6 TTJIWMO FC Proposed to enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. May enhance ubiquitin ligase activity of TRIM28 and stimulate p53/TP53 ubiquitination by TRIM28. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. TTJIWMO SQ MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQEAASSSSTLVEVTLGEVPAAESPDPPQSPQGASSLPTTMNYPLWSQSYEDSSNQEEEGPSTFPDLESEFQAALSRKVAKLVHFLLLKYRAREPVTKAEMLGSVVGNWQYFFPVIFSKASDSLQLVFGIELMEVDPIGHVYIFATCLGLSYDGLLGDNQIMPKTGFLIIILAIIAKEGDCAPEEKIWEELSVLEVFEGREDSIFGDPKKLLTQYFVQENYLEYRQVPGSDPACYEFLWGPRALIETSYVKVLHHMVKISGGPRISYPLLHEWALREGEE TTJIWMO TT Clinical trial TT8OBT3 ID TT8OBT3 TT8OBT3 TN Melanotransferrin (MELTF) TT8OBT3 UP P08582 TT8OBT3 UC TRFM_HUMAN TT8OBT3 SN Melanoma-associated antigen p97; DE AltName: CD_antigen=CD228 TT8OBT3 GN MELTF TT8OBT3 FC Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc. TT8OBT3 SQ MRGPSGALWLLLALRTVLGGMEVRWCATSDPEQHKCGNMSEAFREAGIQPSLLCVRGTSADHCVQLIAAQEADAITLDGGAIYEAGKEHGLKPVVGEVYDQEVGTSYYAVAVVRRSSHVTIDTLKGVKSCHTGINRTVGWNVPVGYLVESGRLSVMGCDVLKAVSDYFGGSCVPGAGETSYSESLCRLCRGDSSGEGVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGKTLPSWGQALLSQDFELLCRDGSRADVTEWRQCHLARVPAHAVVVRADTDGGLIFRLLNEGQRLFSHEGSSFQMFSSEAYGQKDLLFKDSTSELVPIATQTYEAWLGHEYLHAMKGLLCDPNRLPPYLRWCVLSTPEIQKCGDMAVAFRRQRLKPEIQCVSAKSPQHCMERIQAEQVDAVTLSGEDIYTAGKTYGLVPAAGEHYAPEDSSNSYYVVAVVRRDSSHAFTLDELRGKRSCHAGFGSPAGWDVPVGALIQRGFIRPKDCDVLTAVSEFFNASCVPVNNPKNYPSSLCALCVGDEQGRNKCVGNSQERYYGYRGAFRCLVENAGDVAFVRHTTVFDNTNGHNSEPWAAELRSEDYELLCPNGARAEVSQFAACNLAQIPPHAVMVRPDTNIFTVYGLLDKAQDLFGDDHNKNGFKMFDSSNYHGQDLLFKDATVRAVPVGEKTTYRGWLGLDYVAALEGMSSQQCSGAAAPAPGAPLLPLLLPALAARLLPPAL TT8OBT3 TT Clinical trial TT0CZBQ ID TT0CZBQ TT0CZBQ TN Menin-MLL1 interaction (MEN1-KMT2A PPI) TT0CZBQ UP MEN1-KMT2A TT0CZBQ UC MEN1_HUMAN-KMT2A_HUMAN TT0CZBQ GN MEN1-KMT2A TT0CZBQ TT Clinical trial TTLKFB3 ID TTLKFB3 TTLKFB3 TN MHC class I antigen G (HLA-G) TTLKFB3 UP P17693 TTLKFB3 UC HLAG_HUMAN TTLKFB3 SN HLA G antigen; MHC class I antigen G TTLKFB3 GN HLA-G TTLKFB3 FC Non-classical major histocompatibility class Ib molecule involved in immune regulatory processes at the maternal-fetal interface. In complex with B2M/beta-2 microglobulin binds a limited repertoire of nonamer self-peptides derived from intracellular proteins including histones and ribosomal proteins. Peptide-bound HLA-G-B2M complex acts as a ligand for inhibitory/activating KIR2DL4, LILRB1 and LILRB2 receptors on uterine immune cells to promote fetal development while maintaining maternal-fetal tolerance. Upon interaction with KIR2DL4 and LILRB1 receptors on decidual NK cells, it triggers NK cell senescence-associated secretory phenotype as a molecular switch to promote vascular remodeling and fetal growth in early pregnancy. Through interaction with KIR2DL4 receptor on decidual macrophages induces proinflammatory cytokine production mainly associated with tissue remodeling. Through interaction with LILRB2 receptor triggers differentiation of type 1 regulatory T cells and myeloid-derived suppressor cells, both of which actively maintain maternal-fetal tolerance. May play a role in balancing tolerance and antiviral-immunity at maternal-fetal interface by keeping in check the effector functions of NK, CD8+ T cells and B cells. Reprograms B cells toward an immune suppressive phenotype via LILRB1. May induce immune activation/suppression via intercellular membrane transfer (trogocytosis), likely enabling interaction with KIR2DL4, which resides mostly in endosomes. Through interaction with the inhibitory receptor CD160 on endothelial cells may control angiogenesis in immune privileged sites. TTLKFB3 SQ MVVMAPRTLFLLLSGALTLTETWAGSHSMRYFSAAVSRPGRGEPRFIAMGYVDDTQFVRFDSDSACPRMEPRAPWVEQEGPEYWEEETRNTKAHAQTDRMNLQTLRGYYNQSEASSHTLQWMIGCDLGSDGRLLRGYEQYAYDGKDYLALNEDLRSWTAADTAAQISKRKCEAANVAEQRRAYLEGTCVEWLHRYLENGKEMLQRADPPKTHVTHHPVFDYEATLRCWALGFYPAEIILTWQRDGEDQTQDVELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLMLRWKQSSLPTIPIMGIVAGLVVLAAVVTGAAVAAVLWRKKSSD TTLKFB3 TT Clinical trial TTVOE6D ID TTVOE6D TTVOE6D TN Mitogen-activated protein kinase (MAPK) TTVOE6D UP Family TTVOE6D UC NOUNIPROTAC TTVOE6D BC Kinase TTVOE6D SN MAPK; Extracellular signal-regulated kinase; ERK TTVOE6D GN NO-GeName TTVOE6D TT Clinical trial TTVO0JU ID TTVO0JU TTVO0JU TN Mucin-17 (MUC17) TTVO0JU UP Q685J3 TTVO0JU UC MUC17_HUMAN TTVO0JU SN MUC-17; Small intestinal mucin-3; MUC-3 TTVO0JU GN MUC17 TTVO0JU FC Probably plays a role in maintaining homeostasis on mucosal surfaces. TTVO0JU SQ MPRPGTMALCLLTLVLSLLPPQAAAEQDLSVNRAVWDGGGCISQGDVLNRQCQQLSQHVRTGSAANTATGTTSTNVVEPRMYLSCSTNPEMTSIESSVTSDTPGVSSTRMTPTESRTTSESTSDSTTLFPSSTEDTSSPTTPEGTDVPMSTPSEESISSTMAFVSTAPLPSFEAYTSLTYKVDMSTPLTTSTQASSSPTTPESTTIPKSTNSEGSTPLTSMPASTMKVASSEAITLLTTPVEISTPVTISAQASSSPTTAEGPSLSNSAPSGGSTPLTRMPLSVMLVVSSEASTLSTTPAATNIPVITSTEASSSPTTAEGTSIPTSTYTEGSTPLTSTPASTMPVATSEMSTLSITPVDTSTLVTTSTEPSSLPTTAEATSMLTSTLSEGSTPLTNMPVSTILVASSEASTTSTIPVDSKTFVTTASEASSSPTTAEDTSIATSTPSEGSTPLTSMPVSTTPVASSEASNLSTTPVDSKTQVTTSTEASSSPPTAEVNSMPTSTPSEGSTPLTSMSVSTMPVASSEASTLSTTPVDTSTPVTTSSEASSSSTTPEGTSIPTSTPSEGSTPLTNMPVSTRLVVSSEASTTSTTPADSNTFVTTSSEASSSSTTAEGTSMPTSTYSERGTTITSMSVSTTLVASSEASTLSTTPVDSNTPVTTSTEATSSSTTAEGTSMPTSTYTEGSTPLTSMPVNTTLVASSEASTLSTTPVDTSTPVTTSTEASSSPTTADGASMPTSTPSEGSTPLTSMPVSKTLLTSSEASTLSTTPLDTSTHITTSTEASCSPTTTEGTSMPISTPSEGSPLLTSIPVSITPVTSPEASTLSTTPVDSNSPVTTSTEVSSSPTPAEGTSMPTSTYSEGRTPLTSMPVSTTLVATSAISTLSTTPVDTSTPVTNSTEARSSPTTSEGTSMPTSTPGEGSTPLTSMPDSTTPVVSSEARTLSATPVDTSTPVTTSTEATSSPTTAEGTSIPTSTPSEGTTPLTSTPVSHTLVANSEASTLSTTPVDSNTPLTTSTEASSPPPTAEGTSMPTSTPSEGSTPLTRMPVSTTMVASSETSTLSTTPADTSTPVTTYSQASSSSTTADGTSMPTSTYSEGSTPLTSVPVSTRLVVSSEASTLSTTPVDTSIPVTTSTEASSSPTTAEGTSIPTSPPSEGTTPLASMPVSTTLVVSSEANTLSTTPVDSKTQVATSTEASSPPPTAEVTSMPTSTPGERSTPLTSMPVRHTPVASSEASTLSTSPVDTSTPVTTSAETSSSPTTAEGTSLPTSTTSEGSTLLTSIPVSTTLVTSPEASTLLTTPVDTKGPVVTSNEVSSSPTPAEGTSMPTSTYSEGRTPLTSIPVNTTLVASSAISILSTTPVDNSTPVTTSTEACSSPTTSEGTSMPNSNPSEGTTPLTSIPVSTTPVVSSEASTLSATPVDTSTPGTTSAEATSSPTTAEGISIPTSTPSEGKTPLKSIPVSNTPVANSEASTLSTTPVDSNSPVVTSTAVSSSPTPAEGTSIAISTPSEGSTALTSIPVSTTTVASSEINSLSTTPAVTSTPVTTYSQASSSPTTADGTSMQTSTYSEGSTPLTSLPVSTMLVVSSEANTLSTTPIDSKTQVTASTEASSSTTAEGSSMTISTPSEGSPLLTSIPVSTTPVASPEASTLSTTPVDSNSPVITSTEVSSSPTPAEGTSMPTSTYTEGRTPLTSITVRTTPVASSAISTLSTTPVDNSTPVTTSTEARSSPTTSEGTSMPNSTPSEGTTPLTSIPVSTTPVLSSEASTLSATPIDTSTPVTTSTEATSSPTTAEGTSIPTSTLSEGMTPLTSTPVSHTLVANSEASTLSTTPVDSNSPVVTSTAVSSSPTPAEGTSIATSTPSEGSTALTSIPVSTTTVASSETNTLSTTPAVTSTPVTTYAQVSSSPTTADGSSMPTSTPREGRPPLTSIPVSTTTVASSEINTLSTTLADTRTPVTTYSQASSSPTTADGTSMPTPAYSEGSTPLTSMPLSTTLVVSSEASTLSTTPVDTSTPATTSTEGSSSPTTAGGTSIQTSTPSERTTPLAGMPVSTTLVVSSEGNTLSTTPVDSKTQVTNSTEASSSATAEGSSMTISAPSEGSPLLTSIPLSTTPVASPEASTLSTTPVDSNSPVITSTEVSSSPIPTEGTSMQTSTYSDRRTPLTSMPVSTTVVASSAISTLSTTPVDTSTPVTNSTEARSSPTTSEGTSMPTSTPSEGSTPFTSMPVSTMPVVTSEASTLSATPVDTSTPVTTSTEATSSPTTAEGTSIPTSTLSEGTTPLTSIPVSHTLVANSEVSTLSTTPVDSNTPFTTSTEASSPPPTAEGTSMPTSTSSEGNTPLTRMPVSTTMVASFETSTLSTTPADTSTPVTTYSQAGSSPTTADDTSMPTSTYSEGSTPLTSVPVSTMPVVSSEASTHSTTPVDTSTPVTTSTEASSSPTTAEGTSIPTSPPSEGTTPLASMPVSTTPVVSSEAGTLSTTPVDTSTPMTTSTEASSSPTTAEDIVVPISTASEGSTLLTSIPVSTTPVASPEASTLSTTPVDSNSPVVTSTEISSSATSAEGTSMPTSTYSEGSTPLRSMPVSTKPLASSEASTLSTTPVDTSIPVTTSTETSSSPTTAKDTSMPISTPSEVSTSLTSILVSTMPVASSEASTLSTTPVDTRTLVTTSTGTSSSPTTAEGSSMPTSTPGERSTPLTNILVSTTLLANSEASTLSTTPVDTSTPVTTSAEASSSPTTAEGTSMRISTPSDGSTPLTSILVSTLPVASSEASTVSTTAVDTSIPVTTSTEASSSPTTAEVTSMPTSTPSETSTPLTSMPVNHTPVASSEAGTLSTTPVDTSTPVTTSTKASSSPTTAEGIVVPISTASEGSTLLTSIPVSTTPVASSEASTLSTTPVDTSIPVTTSTEGSSSPTTAEGTSMPISTPSEVSTPLTSILVSTVPVAGSEASTLSTTPVDTRTPVTTSAEASSSPTTAEGTSMPISTPGERRTPLTSMSVSTMPVASSEASTLSRTPADTSTPVTTSTEASSSPTTAEGTGIPISTPSEGSTPLTSIPVSTTPVAIPEASTLSTTPVDSNSPVVTSTEVSSSPTPAEGTSMPISTYSEGSTPLTGVPVSTTPVTSSAISTLSTTPVDTSTPVTTSTEAHSSPTTSEGTSMPTSTPSEGSTPLTYMPVSTMLVVSSEDSTLSATPVDTSTPVTTSTEATSSTTAEGTSIPTSTPSEGMTPLTSVPVSNTPVASSEASILSTTPVDSNTPLTTSTEASSSPPTAEGTSMPTSTPSEGSTPLTSMPVSTTTVASSETSTLSTTPADTSTPVTTYSQASSSPPIADGTSMPTSTYSEGSTPLTNMSFSTTPVVSSEASTLSTTPVDTSTPVTTSTEASLSPTTAEGTSIPTSSPSEGTTPLASMPVSTTPVVSSEVNTLSTTPVDSNTLVTTSTEASSSPTIAEGTSLPTSTTSEGSTPLSIMPLSTTPVASSEASTLSTTPVDTSTPVTTSSPTNSSPTTAEVTSMPTSTAGEGSTPLTNMPVSTTPVASSEASTLSTTPVDSNTFVTSSSQASSSPATLQVTTMRMSTPSEGSSSLTTMLLSSTYVTSSEASTPSTPSVDRSTPVTTSTQSNSTPTPPEVITLPMSTPSEVSTPLTIMPVSTTSVTISEAGTASTLPVDTSTPVITSTQVSSSPVTPEGTTMPIWTPSEGSTPLTTMPVSTTRVTSSEGSTLSTPSVVTSTPVTTSTEAISSSATLDSTTMSVSMPMEISTLGTTILVSTTPVTRFPESSTPSIPSVYTSMSMTTASEGSSSPTTLEGTTTMPMSTTSERSTLLTTVLISPISVMSPSEASTLSTPPGDTSTPLLTSTKAGSFSIPAEVTTIRISITSERSTPLTTLLVSTTLPTSFPGASIASTPPLDTSTTFTPSTDTASTPTIPVATTISVSVITEGSTPGTTIFIPSTPVTSSTADVFPATTGAVSTPVITSTELNTPSTSSSSTTTSFSTTKEFTTPAMTTAAPLTYVTMSTAPSTPRTTSRGCTTSASTLSATSTPHTSTSVTTRPVTPSSESSRPSTITSHTIPPTFPPAHSSTPPTTSASSTTVNPEAVTTMTTRTKPSTRTTSFPTVTTTAVPTNTTIKSNPTSTPTVPRTTTCFGDGCQNTASRCKNGGTWDGLKCQCPNLYYGELCEEVVSSIDIGPPETISAQMELTVTVTSVKFTEELKNHSSQEFQEFKQTFTEQMNIVYSGIPEYVGVNITKLRLGSVVVEHDVLLRTKYTPEYKTVLDNATEVVKEKITKVTTQQIMINDICSDMMCFNTTGTQVQNITVTQYDPEEDCRKMAKEYGDYFVVEYRDQKPYCISPCEPGFSVSKNCNLGKCQMSLSGPQCLCVTTETHWYSGETCNQGTQKSLVYGLVGAGVVLMLIILVALLMLVFRSKREVKRQKYRLSQLYKWQEEDSGPAPGTFQNIGFDICQDDDSIHLESIYSNFQPSLRHIDPETKIRIQRPQVMTTSF TTVO0JU TT Clinical trial TT46T5G ID TT46T5G TT46T5G TN Mycobacterium Leucine-tRNA ligase (MycB leuS) TT46T5G UP P9WFV1 TT46T5G UC SYL_MYCTU TT46T5G SN Leucyl-tRNA synthetase; LeuRS TT46T5G GN MycB leuS TT46T5G EC EC 6.1.1.4 TT46T5G SQ MTESPTAGPGGVPRADDADSDVPRYRYTAELAARLERTWQENWARLGTFNVPNPVGSLAPPDGAAVPDDKLFVQDMFPYPSGEGLHVGHPLGYIATDVYARYFRMVGRNVLHALGFDAFGLPAEQYAVQTGTHPRTRTEANVVNFRRQLGRLGFGHDSRRSFSTTDVDFYRWTQWIFLQIYNAWFDTTANKARPISELVAEFESGARCLDGGRDWAKLTAGERADVIDEYRLVYRADSLVNWCPGLGTVLANEEVTADGRSDRGNFPVFRKRLRQWMMRITAYADRLLDDLDVLDWPEQVKTMQRNWIGRSTGAVALFSARAASDDGFEVDIEVFTTRPDTLFGATYLVLAPEHDLVDELVAASWPAGVNPLWTYGGGTPGEAIAAYRRAIAAKSDLERQESREKTGVFLGSYAINPANGEPVPIFIADYVLAGYGTGAIMAVPGHDQRDWDFARAFGLPIVEVIAGGNISESAYTGDGILVNSDYLNGMSVPAAKRAIVDRLESAGRGRARIEFKLRDWLFARQRYWGEPFPIVYDSDGRPHALDEAALPVELPDVPDYSPVLFDPDDADSEPSPPLAKATEWVHVDLDLGDGLKPYSRDTNVMPQWAGSSWYELRYTDPHNSERFCAKENEAYWMGPRPAEHGPDDPGGVDLYVGGAEHAVLHLLYSRFWHKVLYDLGHVSSREPYRRLVNQGYIQAYAYTDARGSYVPAEQVIERGDRFVYPGPDGEVEVFQEFGKIGKSLKNSVSPDEICDAYGADTLRVYEMSMGPLEASRPWATKDVVGAYRFLQRVWRLVVDEHTGETRVADGVELDIDTLRALHRTIVGVSEDFAALRNNTATAKLIEYTNHLTKKHRDAVPRAAVEPLVQMLAPLAPHIAEELWLRLGNTTSLAHGPFPKADAAYLVDETVEYPVQVNGKVRGRVVVAADTDEETLKAAVLTDEKVQAFLAGATPRKVIVVAGRLVNLVI TT46T5G TT Clinical trial TTFQVUT ID TTFQVUT TTFQVUT TN NADPH oxidase (NOX) TTFQVUT UP Family TTFQVUT UC NOUNIPROTAC TTFQVUT GN NO-GeName TTFQVUT FC NOH-1S is a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues. It participates in the regulation of cellular pH and is blocked by zinc. NOH-1L is a pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H(+) ions as part of its electron transport mechanism, whereas NOH-1S does not contain an electron transport chain. TTFQVUT TT Clinical trial TTFQVUT KE hsa04066:HIF-1 signaling pathway; hsa04145:Phagosome; hsa04380:Osteoclast differentiation; hsa04670:Leukocyte transendothelial migration TTUBJQ3 ID TTUBJQ3 TTUBJQ3 TN Neural cell adhesion molecule (NCAM) TTUBJQ3 UP Family TTUBJQ3 UC NOUNIPROTAC TTUBJQ3 BC Immunoglobulin TTUBJQ3 GN NO-GeName TTUBJQ3 TT Clinical trial TTUBJQ3 KE hsa04514:Cell adhesion molecules (CAMs); hsa05020:Prion diseases TTSHAEB ID TTSHAEB TTSHAEB TN NF-kappa-B inhibitor alpha (NFKBIA) TTSHAEB UP P25963 TTSHAEB UC IKBA_HUMAN TTSHAEB SN I-kappa-B-alpha; IkB-alpha; IkappaBalpha; Major histocompatibility complex enhancer-binding protein MAD3 TTSHAEB GN NFKBIA TTSHAEB FC Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription. TTSHAEB SQ MFQAAERPQEWAMEGPRDGLKKERLLDDRHDSGLDSMKDEEYEQMVKELQEIRLEPQEVPRGSEPWKQQLTEDGDSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSILKATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDTESEFTEFTEDELPYDDCVFGGQRLTL TTSHAEB TT Clinical trial TT5KIO9 ID TT5KIO9 TT5KIO9 TN Ornithine transcarbamylase (OTC) TT5KIO9 UP P00480 TT5KIO9 UC OTC_HUMAN TT5KIO9 SN OTCase; Ornithine carbamoyltransferase, mitochondrial TT5KIO9 GN OTC TT5KIO9 FC Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion. TT5KIO9 EC EC 2.1.3.3 TT5KIO9 SQ MLFNLRILLNNAAFRNGHNFMVRNFRCGQPLQNKVQLKGRDLLTLKNFTGEEIKYMLWLSADLKFRIKQKGEYLPLLQGKSLGMIFEKRSTRTRLSTETGFALLGGHPCFLTTQDIHLGVNESLTDTARVLSSMADAVLARVYKQSDLDTLAKEASIPIINGLSDLYHPIQILADYLTLQEHYSSLKGLTLSWIGDGNNILHSIMMSAAKFGMHLQAATPKGYEPDASVTKLAEQYAKENGTKLLLTNDPLEAAHGGNVLITDTWISMGQEEEKKKRLQAFQGYQVTMKTAKVAASDWTFLHCLPRKPEEVDDEVFYSPRSLVFPEAENRKWTIMAVMVSLLTDYSPQLQKPKF TT5KIO9 TT Clinical trial TTJC50M ID TTJC50M TTJC50M TN P53 Y220C mutant (TP53 Y220C) TTJC50M UP P04637 TTJC50M UC P53_HUMAN TTJC50M GN TP53 TTJC50M SQ MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD TTJC50M TT Clinical trial TTRMIZ7 ID TTRMIZ7 TTRMIZ7 TN Peroxisome proliferator-activated receptor (PPAR) TTRMIZ7 UP Q07869; Q03181; P37231 TTRMIZ7 UC PPARA_HUMAN; PPARD_HUMAN; PPARG_HUMAN TTRMIZ7 GN NO-GeName TTRMIZ7 TT Clinical trial TT1APCZ ID TT1APCZ TT1APCZ TN Phosphodiesterase 7 (PDE7) TT1APCZ UP Q13946; Q9NP56 TT1APCZ UC PDE7A_HUMAN; PDE7B_HUMAN TT1APCZ GN NO-GeName TT1APCZ TT Clinical trial TTSG7Q5 ID TTSG7Q5 TTSG7Q5 TN Platelet factor 4 (PF4) TTSG7Q5 UP P02776 TTSG7Q5 UC PLF4_HUMAN TTSG7Q5 SN PF-4; C-X-C motif chemokine 4; Iroplact; Oncostatin-A TTSG7Q5 GN PF4 TTSG7Q5 FC Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form. TTSG7Q5 SQ MSSAAGFCASRPGLLFLGLLLLPLVVAFASAEAEEDGDLQCLCVKTTSQVRPRHITSLEVIKAGPHCPTAQLIATLKNGRKICLDLQAPLYKKIIKKLLES TTSG7Q5 TT Clinical trial TTHC8EF ID TTHC8EF TTHC8EF TN Polyadenylate-binding protein 1 (PABPC1) TTHC8EF UP P11940 TTHC8EF UC PABP1_HUMAN TTHC8EF SN PABP-1; Poly(A)-binding protein 1 TTHC8EF GN PABPC1 TTHC8EF FC Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability. TTHC8EF SQ MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV TTHC8EF TT Clinical trial TTYVX59 ID TTYVX59 TTYVX59 TN Protein kinase C (PRKC) TTYVX59 UP Family TTYVX59 UC NOUNIPROTAC TTYVX59 BC Kinase TTYVX59 GN NO-GeName TTYVX59 TT Clinical trial TT2FRAN ID TT2FRAN TT2FRAN TN Protein mono-ADP-ribosyltransferase TIPARP (TIPARP) TT2FRAN UP Q7Z3E1 TT2FRAN UC PARPT_HUMAN TT2FRAN SN ADP-ribosyltransferase diphtheria toxin-like 14; ARTD14; Poly [ADP-ribose] polymerase 7; PARP-7; TCDD-inducible poly [ADP-ribose] polymerase TT2FRAN GN TIPARP TT2FRAN FC ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate, aspartate and cysteine residues on target proteins. Acts as a negative regulator of AHR by mediating mono-ADP-ribosylation of AHR, leading to inhibit transcription activator activity of AHR. TT2FRAN EC EC 2.4.2.- TT2FRAN SQ MEMETTEPEPDCVVQPPSPPDDFSCQMRLSEKITPLKTCFKKKDQKRLGTGTLRSLRPILNTLLESGSLDGVFRSRNQSTDENSLHEPMMKKAMEINSSCPPAENNMSVLIPDRTNVGDQIPEAHPSTEAPERVVPIQDHSFPSETLSGTVADSTPAHFQTDLLHPVSSDVPTSPDCLDKVIDYVPGIFQENSFTIQYILDTSDKLSTELFQDKSEEASLDLVFELVNQLQYHTHQENGIEICMDFLQGTCIYGRDCLKHHTVLPYHWQIKRTTTQKWQSVFNDSQEHLERFYCNPENDRMRMKYGGQEFWADLNAMNVYETTEFDQLRRLSTPPSSNVNSIYHTVWKFFCRDHFGWREYPESVIRLIEEANSRGLKEVRFMMWNNHYILHNSFFRREIKRRPLFRSCFILLPYLQTLGGVPTQAPPPLEATSSSQIICPDGVTSANFYPETWVYMHPSQDFIQVPVSAEDKSYRIIYNLFHKTVPEFKYRILQILRVQNQFLWEKYKRKKEYMNRKMFGRDRIINERHLFHGTSQDVVDGICKHNFDPRVCGKHATMFGQGSYFAKKASYSHNFSKKSSKGVHFMFLAKVLTGRYTMGSHGMRRPPPVNPGSVTSDLYDSCVDNFFEPQIFVIFNDDQSYPYFVIQYEEVSNTVSI TT2FRAN TT Clinical trial TTWC6MY ID TTWC6MY TTWC6MY TN Protein tyrosine phosphatase (PTP) TTWC6MY UP Family TTWC6MY UC NOUNIPROTAC TTWC6MY BC Phosphoric monoester hydrolase TTWC6MY SN PTPase; PTPN TTWC6MY GN NO-GeName TTWC6MY TT Clinical trial TT3UNDH ID TT3UNDH TT3UNDH TN Pyruvate dehydrogenase kinase (PDHK) TT3UNDH UP Family TT3UNDH UC NOUNIPROTAC TT3UNDH BC Kinase TT3UNDH SN PDH kinase TT3UNDH GN NO-GeName TT3UNDH TT Clinical trial TTOA18V ID TTOA18V TTOA18V TN Rab proteins geranylgeranyltransferase component A 1 (CHM) TTOA18V UP P24386 TTOA18V UC RAE1_HUMAN TTOA18V SN Choroideremia protein; Rab escort protein 1; REP-1; TCD protein TTOA18V GN CHM TTOA18V FC Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation. TTOA18V SQ MADTLPSEFDVIVIGTGLPESIIAAACSRSGRRVLHVDSRSYYGGNWASFSFSGLLSWLKEYQENSDIVSDSPVWQDQILENEEAIALSRKDKTIQHVEVFCYASQDLHEDVEEAGALQKNHALVTSANSTEAADSAFLPTEDESLSTMSCEMLTEQTPSSDPENALEVNGAEVTGEKENHCDDKTCVPSTSAEDMSENVPIAEDTTEQPKKNRITYSQIIKEGRRFNIDLVSKLLYSRGLLIDLLIKSNVSRYAEFKNITRILAFREGRVEQVPCSRADVFNSKQLTMVEKRMLMKFLTFCMEYEKYPDEYKGYEEITFYEYLKTQKLTPNLQYIVMHSIAMTSETASSTIDGLKATKNFLHCLGRYGNTPFLFPLYGQGELPQCFCRMCAVFGGIYCLRHSVQCLVVDKESRKCKAIIDQFGQRIISEHFLVEDSYFPENMCSRVQYRQISRAVLITDRSVLKTDSDQQISILTVPAEEPGTFAVRVIELCSSTMTCMKGTYLVHLTCTSSKTAREDLESVVQKLFVPYTEMEIENEQVEKPRILWALYFNMRDSSDISRSCYNDLPSNVYVCSGPDCGLGNDNAVKQAETLFQEICPNEDFCPPPPNPEDIILDGDSLQPEASESSAIPEANSETFKESTNLGNLEESSE TTOA18V TT Clinical trial TTQ7UAP ID TTQ7UAP TTQ7UAP TN RAC serine/threonine-protein kinase (AKT) TTQ7UAP UP P31749; P31751; Q9Y243 TTQ7UAP UC AKT1_HUMAN; AKT2_HUMAN; AKT3_HUMAN TTQ7UAP GN NO-GeName TTQ7UAP TT Clinical trial TTOE7I0 ID TTOE7I0 TTOE7I0 TN Rap guanine nucleotide exchange factor 3 (RAPGEF3) TTOE7I0 UP O95398 TTOE7I0 UC RPGF3_HUMAN TTOE7I0 SN Exchange factor directly activated by cAMP 1; Exchange protein directly activated by cAMP 1; EPAC 1; Rap1 guanine-nucleotide-exchange factor directly activated by cAMP; cAMP-regulated guanine nucleotide exchange factor I; cAMP-GEFI TTOE7I0 GN RAPGEF3 TTOE7I0 FC Guanine nucleotide exchange factor (GEF) for RAP1A and RAP2A small GTPases that is activated by binding cAMP. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which it activates the PI3K gamma complex and which is involved in angiogenesis. Plays a role in the modulation of the cAMP-induced dynamic control of endothelial barrier function through a pathway that is independent on Rho-mediated signaling. Required for the actin rearrangement at cell-cell junctions, such as stress fibers and junctional actin. TTOE7I0 SQ MKVGWPGESCWQVGLAVEDSPALGAPRVGALPDVVPEGTLLNMVLRRMHRPRSCSYQLLLEHQRPSCIQGLRWTPLTNSEESLDFSESLEQASTERVLRAGRQLHRHLLATCPNLIRDRKYHLRLYRQCCSGRELVDGILALGLGVHSRSQVVGICQVLLDEGALCHVKHDWAFQDRDAQFYRFPGPEPEPVRTHEMEEELAEAVALLSQRGPDALLTVALRKPPGQRTDEELDLIFEELLHIKAVAHLSNSVKRELAAVLLFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKGLVTTLHEGDDFGQLALVNDAPRAATIILREDNCHFLRVDKQDFNRIIKDVEAKTMRLEEHGKVVLVLERASQGAGPSRPPTPGRNRYTVMSGTPEKILELLLEAMGPDSSAHDPTETFLSDFLLTHRVFMPSAQLCAALLHHFHVEPAGGSEQERSTYVCNKRQQILRLVSQWVALYGSMLHTDPVATSFLQKLSDLVGRDTRLSNLLREQWPERRRCHRLENGCGNASPQMKARNLPVWLPNQDEPLPGSSCAIQVGDKVPYDICRPDHSVLTLQLPVTASVREVMAALAQEDGWTKGQVLVKVNSAGDAIGLQPDARGVATSLGLNERLFVVNPQEVHELIPHPDQLGPTVGSAEGLDLVSAKDLAGQLTDHDWSLFNSIHQVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGPRAQLLRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALAKLSPPVIPFMPLLLKDMTFIHEGNHTLVENLINFEKMRMMARAARMLHHCRSHNPVPLSPLRSRVSHLHEDSQVARISTCSEQSLSTRSPASTWAYVQQLKVIDNQRELSRLSRELEP TTOE7I0 TT Clinical trial TT7M3PI ID TT7M3PI TT7M3PI TN Ribosomal protein S6 kinase (S6K) TT7M3PI UP Family TT7M3PI UC NOUNIPROTAC TT7M3PI BC Kinase TT7M3PI SN Ribosomal s6 kinase TT7M3PI GN NO-GeName TT7M3PI TT Clinical trial TTMVQXO ID TTMVQXO TTMVQXO TN Ribosomal protein S6 kinase beta-2 (RPS6KB2) TTMVQXO UP Q9UBS0 TTMVQXO UC KS6B2_HUMAN TTMVQXO SN S6K-beta-2; S6K2; 70 kDa ribosomal protein S6 kinase 2; P70S6K2; p70-S6K 2; S6 kinase-related kinase; SRK; Serine/threonine-protein kinase 14B; p70 ribosomal S6 kinase beta; S6K-beta; p70 S6 kinase beta; p70 S6K-beta; p70 S6KB; p70-beta TTMVQXO GN RPS6KB2 TTMVQXO FC Phosphorylates specifically ribosomal protein S6. Seems to act downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression in an alternative pathway regulated by MEAK7. TTMVQXO EC EC 2.7.11.1 TTMVQXO SQ MAAVFDLDLETEEGSEGEGEPELSPADACPLAELRAAGLEPVGHYEEVELTETSVNVGPERIGPHCFELLRVLGKGGYGKVFQVRKVQGTNLGKIYAMKVLRKAKIVRNAKDTAHTRAERNILESVKHPFIVELAYAFQTGGKLYLILECLSGGELFTHLEREGIFLEDTACFYLAEITLALGHLHSQGIIYRDLKPENIMLSSQGHIKLTDFGLCKESIHEGAVTHTFCGTIEYMAPEILVRSGHNRAVDWWSLGALMYDMLTGSPPFTAENRKKTMDKIIRGKLALPPYLTPDARDLVKKFLKRNPSQRIGGGPGDAADVQRHPFFRHMNWDDLLAWRVDPPFRPCLQSEEDVSQFDTRFTRQTPVDSPDDTALSESANQAFLGFTYVAPSVLDSIKEGFSFQPKLRSPRRLNSSPRAPVSPLKFSPFEGFRPSPSLPEPTELPLPPLLPPPPPSTTAPLPIRPPSGTKKSKRGRGRPGR TTMVQXO TT Clinical trial TTA7WGU ID TTA7WGU TTA7WGU TN Serine/threonine-protein kinase pim (PIM) TTA7WGU UP Family TTA7WGU UC NOUNIPROTAC TTA7WGU BC Kinase TTA7WGU GN NO-GeName TTA7WGU FC Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling throughphosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl- X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A proteinstability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post- translational levels. Phosphorylation of CDKN1B,induces 14-3-3- proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Actsalso as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis. TTA7WGU TT Clinical trial TT2L4TV ID TT2L4TV TT2L4TV TN SERPINA1 messenger RNA (SERPINA1 mRNA) TT2L4TV UP P01009 TT2L4TV UC A1AT_HUMAN TT2L4TV SN Alpha-1 protease inhibitor; Alpha-1-antiproteinase; Serpin A1 TT2L4TV GN SERPINA1 TT2L4TV FC Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin. TT2L4TV SQ MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK TT2L4TV TT Clinical trial TTZ4MD5 ID TTZ4MD5 TTZ4MD5 TN SERPINC1 messenger RNA (SERPINC1 mRNA) TTZ4MD5 UP P01008 TTZ4MD5 UC ANT3_HUMAN TTZ4MD5 SN ATIII; Serpin C1 TTZ4MD5 GN SERPINC1 TTZ4MD5 FC Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin. TTZ4MD5 SQ MYSNVIGTVTSGKRKVYLLSLLLIGFWDCVTCHGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANPCVK TTZ4MD5 TT Clinical trial TTPSWQG ID TTPSWQG TTPSWQG TN SERPINH1 messenger RNA (SERPINH1 mRNA) TTPSWQG UP P50454 TTPSWQG UC SERPH_HUMAN TTPSWQG SN 47 kDa heat shock protein; Arsenic-transactivated protein 3; AsTP3; Cell proliferation-inducing gene 14 protein; Collagen-binding protein; Colligin; Rheumatoid arthritis-related antigen RA-A47 TTPSWQG GN SERPINH1 TTPSWQG FC Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. TTPSWQG SQ MRSLLLLSAFCLLEAALAAEVKKPAAAAAPGTAEKLSPKAATLAERSAGLAFSLYQAMAKDQAVENILVSPVVVASSLGLVSLGGKATTASQAKAVLSAEQLRDEEVHAGLGELLRSLSNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVMMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMPHHVEPLERLEKLLTKEQLKIWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFELDTDGNPFDQDIYGREELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRPKGDKMRDEL TTPSWQG TT Clinical trial TTXR78S ID TTXR78S TTXR78S TN SF3b complex (SF3b) TTXR78S UP O75533-Q13435-Q15393-Q15427-Q9BWJ5-Q9Y3B4 TTXR78S UC SF3B1_HUMAN-SF3B2_HUMAN-SF3B3_HUMAN-SF3B4_HUMAN-SF3B5_HUMAN-SF3B6_HUMAN TTXR78S GN SF3B1-SF3B2-SF3B3-SF3B4-SF3B5-SF3B6 TTXR78S TT Clinical trial TT619TC ID TT619TC TT619TC TN Sodium/calcium exchanger (SLC) TT619TC UP Family TT619TC UC NOUNIPROTAC TT619TC SN NaCaX; Na(+)/Ca(2+) exchanger; Mitochondrial sodium-calcium exchanger TT619TC GN NO-GeName TT619TC TT Clinical trial TTYUHB5 ID TTYUHB5 TTYUHB5 TN Solute carrier family 6 member 8 (SLC6A8) TTYUHB5 UP P48029 TTYUHB5 UC SC6A8_HUMAN TTYUHB5 SN CT1; Creatine transporter 1; Solute carrier family 6 member 8 TTYUHB5 GN SLC6A8 TTYUHB5 FC Required for the uptake of creatine in muscles and brain. TTYUHB5 SQ MAKKSAENGIYSVSGDEKKGPLIAPGPDGAPAKGDGPVGLGTPGGRLAVPPRETWTRQMDFIMSCVGFAVGLGNVWRFPYLCYKNGGGVFLIPYVLIALVGGIPIFFLEISLGQFMKAGSINVWNICPLFKGLGYASMVIVFYCNTYYIMVLAWGFYYLVKSFTTTLPWATCGHTWNTPDCVEIFRHEDCANASLANLTCDQLADRRSPVIEFWENKVLRLSGGLEVPGALNWEVTLCLLACWVLVYFCVWKGVKSTGKIVYFTATFPYVVLVVLLVRGVLLPGALDGIIYYLKPDWSKLGSPQVWIDAGTQIFFSYAIGLGALTALGSYNRFNNNCYKDAIILALINSGTSFFAGFVVFSILGFMAAEQGVHISKVAESGPGLAFIAYPRAVTLMPVAPLWAALFFFMLLLLGLDSQFVGVEGFITGLLDLLPASYYFRFQREISVALCCALCFVIDLSMVTDGGMYVFQLFDYYSASGTTLLWQAFWECVVVAWVYGADRFMDDIACMIGYRPCPWMKWCWSFFTPLVCMGIFIFNVVYYEPLVYNNTYVYPWWGEAMGWAFALSSMLCVPLHLLGCLLRAKGTMAERWQHLTQPIWGLHHLEYRAQDADVRGLTTLTPVSESSKVVVVESVM TTYUHB5 TT Clinical trial TTOWKQ9 ID TTOWKQ9 TTOWKQ9 TN Staphylococcus IgG binding protein A (Stap-coc SpA) TTOWKQ9 UP P02976 TTOWKQ9 UC SPA_STAA8 TTOWKQ9 SN IgG-binding protein A; Staphylococcal protein A; SpA TTOWKQ9 GN Stap-coc SpA TTOWKQ9 FC Plays a role in the inhibition of the host innate and adaptive immune responses. Possesses five immunoglobulin-binding domains that capture both the fragment crystallizable region (Fc region) and the Fab region (part of Ig that identifies antigen) of immunoglobulins. In turn, Staphylococcus aureus is protected from phagocytic killing via inhibition of Ig Fc region. In addition, the host elicited B-cell response is prevented due to a decrease of antibody-secreting cell proliferation that enter the bone marrow, thereby decreasing long-term antibody production. Inhibits osteogenesis by preventing osteoblast proliferation and expression of alkaline phosphatase, type I collagen, osteopontin and osteocalcin. Acts directly as a proinflammatory factor in the lung through its ability to bind and activate tumor necrosis factor alpha receptor 1/TNFRSF1A (By similarity). TTOWKQ9 SQ MKKKNIYSIRKLGVGIASVTLGTLLISGGVTPAANAAQHDEAQQNAFYQVLNMPNLNADQRNGFIQSLKDDPSQSANVLGEAQKLNDSQAPKADAQQNNFNKDQQSAFYEILNMPNLNEAQRNGFIQSLKDDPSQSTNVLGEAKKLNESQAPKADNNFNKEQQNAFYEILNMPNLNEEQRNGFIQSLKDDPSQSANLLSEAKKLNESQAPKADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKADNKFNKEQQNAFYEILHLPNLTEEQRNGFIQSLKDDPSVSKEILAEAKKLNDAQAPKEEDNNKPGKEDNNKPGKEDNNKPGKEDNNKPGKEDNNKPGKEDGNKPGKEDNKKPGKEDGNKPGKEDNKKPGKEDGNKPGKEDGNKPGKEDGNGVHVVKPGDTVNDIAKANGTTADKIAADNKLADKNMIKPGQELVVDKKQPANHADANKAQALPETGEENPFIGTTVFGGLSLALGAALLAGRRREL TTOWKQ9 TT Clinical trial TTWELHI ID TTWELHI TTWELHI TN Stress-activated protein kinase (p38) TTWELHI UP Family TTWELHI UC NOUNIPROTAC TTWELHI BC Kinase TTWELHI SN p38) Stress-activated protein kinase; P38 MAPK; P38 MAP kinase; Mitogen-activated protein kinase p38 TTWELHI GN NO-GeName TTWELHI TT Clinical trial TTKSAQZ ID TTKSAQZ TTKSAQZ TN Tankyrase (TNKS) TTKSAQZ UP Family TTKSAQZ UC NOUNIPROTAC TTKSAQZ BC Glycosyltransferases TTKSAQZ GN NO-GeName TTKSAQZ FC Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Stimulates 26S proteasome activity. TTKSAQZ TT Clinical trial TT83C4X ID TT83C4X TT83C4X TN T-cell surface protein tactile (CD96) TT83C4X UP P40200 TT83C4X UC TACT_HUMAN TT83C4X SN Cell surface antigen CD96; T cell-activated increased late expression protein; DE AltName: CD_antigen=CD96 TT83C4X GN CD96 TT83C4X FC May be involved in adhesive interactions of activated T and NK cells during the late phase of the immune response. Promotes NK cell-target adhesion by interacting with PVR present on target cells. May function at a time after T and NK cells have penetrated the endothelium using integrins and selectins, when they are actively engaging diseased cells and moving within areas of inflammation. TT83C4X SQ MEKKWKYCAVYYIIQIHFVKGVWEKTVNTEENVYATLGSDVNLTCQTQTVGFFVQMQWSKVTNKIDLIAVYHPQYGFYCAYGRPCESLVTFTETPENGSKWTLHLRNMSCSVSGRYECMLVLYPEGIQTKIYNLLIQTHVTADEWNSNHTIEIEINQTLEIPCFQNSSSKISSEFTYAWSVENSSTDSWVLLSKGIKEDNGTQETLISQNHLISNSTLLKDRVKLGTDYRLHLSPVQIFDDGRKFSCHIRVGPNKILRSSTTVKVFAKPEIPVIVENNSTDVLVERRFTCLLKNVFPKANITWFIDGSFLHDEKEGIYITNEERKGKDGFLELKSVLTRVHSNKPAQSDNLTIWCMALSPVPGNKVWNISSEKITFLLGSEISSTDPPLSVTESTLDTQPSPASSVSPARYPATSSVTLVDVSALRPNTTPQPSNSSMTTRGFNYPWTSSGTDTKKSVSRIPSETYSSSPSGAGSTLHDNVFTSTARAFSEVPTTANGSTKTNHVHITGIVVNKPKDGMSWPVIVAALLFCCMILFGLGVRKWCQYQKEIMERPPPFKPPPPPIKYTCIQEPNESDLPYHEMETL TT83C4X TT Clinical trial TTNIUKC ID TTNIUKC TTNIUKC TN TMPRSS6 messenger RNA (TMPRSS6 mRNA) TTNIUKC UP Q8IU80 TTNIUKC UC TMPS6_HUMAN TTNIUKC SN Matriptase-2 TTNIUKC GN TMPRSS6 TTNIUKC FC Serine protease which hydrolyzes a range of proteins including type I collagen, fibronectin and fibrinogen. Can also activate urokinase-type plasminogen activator with low efficiency. May play a specialized role in matrix remodeling processes in liver. Through the cleavage of HJV, a regulator of the expression of the iron absorption-regulating hormone hepicidin/HAMP, plays a role in iron homeostasis. TTNIUKC EC EC 3.4.21.- TTNIUKC SQ MLLLFHSKRMPVAEAPQVAGGQGDGGDGEEAEPEGMFKACEDSKRKARGYLRLVPLFVLLALLVLASAGVLLWYFLGYKAEVMVSQVYSGSLRVLNRHFSQDLTRRESSAFRSETAKAQKMLKELITSTRLGTYYNSSSVYSFGEGPLTCFFWFILQIPEHRRLMLSPEVVQALLVEELLSTVNSSAAVPYRAEYEVDPEGLVILEASVKDIAALNSTLGCYRYSYVGQGQVLRLKGPDHLASSCLWHLQGPKDLMLKLRLEWTLAECRDRLAMYDVAGPLEKRLITSVYGCSRQEPVVEVLASGAIMAVVWKKGLHSYYDPFVLSVQPVVFQACEVNLTLDNRLDSQGVLSTPYFPSYYSPQTHCSWHLTVPSLDYGLALWFDAYALRRQKYDLPCTQGQWTIQNRRLCGLRILQPYAERIPVVATAGITINFTSQISLTGPGVRVHYGLYNQSDPCPGEFLCSVNGLCVPACDGVKDCPNGLDERNCVCRATFQCKEDSTCISLPKVCDGQPDCLNGSDEEQCQEGVPCGTFTFQCEDRSCVKKPNPQCDGRPDCRDGSDEEHCDCGLQGPSSRIVGGAVSSEGEWPWQASLQVRGRHICGGALIADRWVITAAHCFQEDSMASTVLWTVFLGKVWQNSRWPGEVSFKVSRLLLHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPISNALQKVDVQLIPQDLCSEVYRYQVTPRMLCAGYRKGKKDACQGDSGGPLVCKALSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVISWIQQVVT TTNIUKC TT Clinical trial TTO3HT7 ID TTO3HT7 TTO3HT7 TN Transforming growth factor beta (TGFB) TTO3HT7 UP Family TTO3HT7 UC NOUNIPROTAC TTO3HT7 SN TGF-beta TTO3HT7 GN NO-GeName TTO3HT7 TT Clinical trial TT0FAYT ID TT0FAYT TT0FAYT TN Transforming growth factor beta activator LRRC32 (LRRC32) TT0FAYT UP Q14392 TT0FAYT UC LRC32_HUMAN TT0FAYT SN Garpin; Glycoprotein A repetitions predominant; GARP; Leucine-rich repeat-containing protein 32 TT0FAYT GN LRRC32 TT0FAYT FC Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta. Able to outcompete LTBP1 for binding to LAP regulatory chain of TGF-beta. Controls activation of TGF-beta-1 (TGFB1) on the surface of activated regulatory T-cells (Tregs). Required for epithelial fusion during palate development by regulating activation of TGF-beta-3 (TGFB3) (By similarity). TT0FAYT SQ MRPQILLLLALLTLGLAAQHQDKVPCKMVDKKVSCQVLGLLQVPSVLPPDTETLDLSGNQLRSILASPLGFYTALRHLDLSTNEISFLQPGAFQALTHLEHLSLAHNRLAMATALSAGGLGPLPRVTSLDLSGNSLYSGLLERLLGEAPSLHTLSLAENSLTRLTRHTFRDMPALEQLDLHSNVLMDIEDGAFEGLPRLTHLNLSRNSLTCISDFSLQQLRVLDLSCNSIEAFQTASQPQAEFQLTWLDLRENKLLHFPDLAALPRLIYLNLSNNLIRLPTGPPQDSKGIHAPSEGWSALPLSAPSGNASGRPLSQLLNLDLSYNEIELIPDSFLEHLTSLCFLNLSRNCLRTFEARRLGSLPCLMLLDLSHNALETLELGARALGSLRTLLLQGNALRDLPPYTFANLASLQRLNLQGNRVSPCGGPDEPGPSGCVAFSGITSLRSLSLVDNEIELLRAGAFLHTPLTELDLSSNPGLEVATGALGGLEASLEVLALQGNGLMVLQVDLPCFICLKRLNLAENRLSHLPAWTQAVSLEVLDLRNNSFSLLPGSAMGGLETSLRRLYLQGNPLSCCGNGWLAAQLHQGRVDVDATQDLICRFSSQEEVSLSHVRPEDCEKGGLKNINLIIILTFILVSAILLTTLAACCCVRRQKFNQQYKA TT0FAYT TT Clinical trial TTOGCNT ID TTOGCNT TTOGCNT TN Transmembrane protein PVRIG (PVRIG) TTOGCNT UP Q6DKI7 TTOGCNT UC PVRIG_HUMAN TTOGCNT SN CD112 receptor; CD112R; Poliovirus receptor-related immunoglobulin domain-containing protein TTOGCNT GN PVRIG TTOGCNT FC Cell surface receptor for NECTIN2. May act as a coinhibitory receptor that suppresses T-cell receptor-mediated signals. Following interaction with NECTIN2, inhibits T-cell proliferation. Competes with CD226 for NECTIN2-binding. TTOGCNT SQ MRTEAQVPALQPPEPGLEGAMGHRTLVLPWVLLTLCVTAGTPEVWVQVRMEATELSSFTIRCGFLGSGSISLVTVSWGGPNGAGGTTLAVLHPERGIRQWAPARQARWETQSSISLILEGSGASSPCANTTFCCKFASFPEGSWEACGSLPPSSDPGLSAPPTPAPILRADLAGILGVSGVLLFGCVYLLHLLRRHKHRPAPRLQPSRTSPQAPRARAWAPSQASQAALHVPYATINTSCRPATLDTAHPHGGPSWWASLPTHAAHRPQGPAAWASTPIPARGSFVSVENGLYAQAGERPPHTGPGLTLFPDPRGPRAMEGPLGVR TTOGCNT TT Clinical trial TTJOCTY ID TTJOCTY TTJOCTY TN Tropomyosin receptor kinase (Trk) TTJOCTY UP P04629; Q16620; Q16288 TTJOCTY UC NTRK1_HUMAN; NTRK2_HUMAN; NTRK3_HUMAN TTJOCTY GN NO-GeName TTJOCTY TT Clinical trial TTP2HE5 ID TTP2HE5 TTP2HE5 TN Tumor associated calcium signal transducer 2 (TACSTD2) TTP2HE5 UP P09758 TTP2HE5 UC TACD2_HUMAN TTP2HE5 SN Cell surface glycoprotein Trop-2; Membrane component chromosome 1 surface marker 1; Pancreatic carcinoma marker protein GA733-1 TTP2HE5 GN TACSTD2 TTP2HE5 FC May function as a growth factor receptor. TTP2HE5 SQ MARGPGLAPPPLRLPLLLLVLAAVTGHTAAQDNCTCPTNKMTVCSPDGPGGRCQCRALGSGMAVDCSTLTSKCLLLKARMSAPKNARTLVRPSEHALVDNDGLYDPDCDPEGRFKARQCNQTSVCWCVNSVGVRRTDKGDLSLRCDELVRTHHILIDLRHRPTAGAFNHSDLDAELRRLFRERYRLHPKFVAAVHYEQPTIQIELRQNTSQKAAGDVDIGDAAYYFERDIKGESLFQGRGGLDLRVRGEPLQVERTLIYYLDEIPPKFSMKRLTAGLIAVIVVVVVALVAGMAVLVITNRRKSGKYKKVEIKELGELRKEPSL TTP2HE5 TT Clinical trial TTDV6BQ ID TTDV6BQ TTDV6BQ TN Tumor necrosis factor receptor member 25 (TNFRSF25) TTDV6BQ UP Q93038 TTDV6BQ UC TNR25_HUMAN TTDV6BQ SN Apo-3; Apoptosis-inducing receptor AIR; Apoptosis-mediating receptor DR3; Apoptosis-mediating receptor TRAMP; Death receptor 3; Lymphocyte-associated receptor of death; LARD; Protein WSL; Protein WSL-1 TTDV6BQ GN TNFRSF25 TTDV6BQ FC Receptor for TNFSF12/APO3L/TWEAK. Interacts directly with the adapter TRADD. Mediates activation of NF-kappa-B and induces apoptosis. May play a role in regulating lymphocyte homeostasis. TTDV6BQ SQ MEQRPRGCAAVAAALLLVLLGARAQGGTRSPRCDCAGDFHKKIGLFCCRGCPAGHYLKAPCTEPCGNSTCLVCPQDTFLAWENHHNSECARCQACDEQASQVALENCSAVADTRCGCKPGWFVECQVSQCVSSSPFYCQPCLDCGALHRHTRLLCSRRDTDCGTCLPGFYEHGDGCVSCPTSTLGSCPERCAAVCGWRQMFWVQVLLAGLVVPLLLGATLTYTYRHCWPHKPLVTADEAGMEALTPPPATHLSPLDSAHTLLAPPDSSEKICTVQLVGNSWTPGYPETQEALCPQVTWSWDQLPSRALGPAAAPTLSPESPAGSPAMMLQPGPQLYDVMDAVPARRWKEFVRTLGLREAEIEAVEVEIGRFRDQQYEMLKRWRQQQPAGLGAVYAALERMGLDGCVEDLRSRLQRGP TTDV6BQ TT Clinical trial TTY8PUS ID TTY8PUS TTY8PUS TN Tyrosine-protein phosphatase non-receptor type 2 (PTPN2) TTY8PUS UP P17706 TTY8PUS UC PTN2_HUMAN TTY8PUS SN T-cell protein-tyrosine phosphatase; TCPTP TTY8PUS GN PTPN2 TTY8PUS FC Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3 and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T-cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. In addition to the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Plays also an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. May also bind DNA. TTY8PUS EC EC 3.1.3.48 TTY8PUS SQ MPTTIEREFEELDTQRRWQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKCIKGDSSIQKRWKELSKEDLSPAFDHSPNKIMTEKYNGNRIGLEEEKLTGDRCTGLSSKMQDTMEENSESALRKRIREDRKATTAQKVQQMKQRLNENERKRKRWLYWQPILTKMGFMSVILVGAFVGWTLFFQQNAL TTY8PUS TT Clinical trial TT34ZAF ID TT34ZAF TT34ZAF TN UDP-glucuronosyltransferase 1A1 (UGT1A1) TT34ZAF UP P22309 TT34ZAF UC UD11_HUMAN TT34ZAF SN UGT1A1; Bilirubin-specific UDPGT isozyme 1; hUG-BR1; UDP-glucuronosyltransferase 1-1; UDPGT 1-1; UGT1*1; UGT1-01; UGT1.1; UDP-glucuronosyltransferase 1A isoform 1 TT34ZAF GN UGT1A1 TT34ZAF FC UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol, estrone and estriol. Involved in the glucuronidation of bilirubin, a degradation product occurring in the normal catabolic pathway that breaks down heme in vertebrates. Also catalyzes the glucuronidation the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties. Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, a drug which can inhibit the effect of angiotensin II. Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan. TT34ZAF EC EC 2.4.1.17 TT34ZAF SQ MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVLAPDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDSAMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLEFEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQREVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH TT34ZAF TT Clinical trial TTHBDA9 ID TTHBDA9 TTHBDA9 TN X-linked retinitis pigmentosa GTPase regulator (RPGR) TTHBDA9 UP Q92834 TTHBDA9 UC RPGR_HUMAN TTHBDA9 GN RPGR TTHBDA9 FC Could be a guanine-nucleotide releasing factor. Plays a role in ciliogenesis. Probably regulates cilia formation by regulating actin stress filaments and cell contractility. Plays an important role in photoreceptor integrity. May play a critical role in spermatogenesis and in intraflagellar transport processes (By similarity). May be involved in microtubule organization and regulation of transport in primary cilia. TTHBDA9 SQ MREPEELMPDSGAVFTFGKSKFAENNPGKFWFKNDVPVHLSCGDEHSAVVTGNNKLYMFGSNNWGQLGLGSKSAISKPTCVKALKPEKVKLAACGRNHTLVSTEGGNVYATGGNNEGQLGLGDTEERNTFHVISFFTSEHKIKQLSAGSNTSAALTEDGRLFMWGDNSEGQIGLKNVSNVCVPQQVTIGKPVSWISCGYYHSAFVTTDGELYVFGEPENGKLGLPNQLLGNHRTPQLVSEIPEKVIQVACGGEHTVVLTENAVYTFGLGQFGQLGLGTFLFETSEPKVIENIRDQTISYISCGENHTALITDIGLMYTFGDGRHGKLGLGLENFTNHFIPTLCSNFLRFIVKLVACGGCHMVVFAAPHRGVAKEIEFDEINDTCLSVATFLPYSSLTSGNVLQRTLSARMRRRERERSPDSFSMRRTLPPIEGTLGLSACFLPNSVFPRCSERNLQESVLSEQDLMQPEEPDYLLDEMTKEAEIDNSSTVESLGETTDILNMTHIMSLNSNEKSLKLSPVQKQKKQQTIGELTQDTALTENDDSDEYEEMSEMKEGKACKQHVSQGIFMTQPATTIEAFSDEEVGNDTGQVGPQADTDGEGLQKEVYRHENNNGVDQLDAKEIEKESDGGHSQKESEAEEIDSEKETKLAEIAGMKDLREREKSTKKMSPFFGNLPDRGMNTESEENKDFVKKRESCKQDVIFDSERESVEKPDSYMEGASESQQGIADGFQQPEAIEFSSGEKEDDEVETDQNIRYGRKLIEQGNEKETKPIISKSMAKYDFKCDRLSEIPEEKEGAEDSKGNGIEEQEVEANEENVKVHGGRKEKTEILSDDLTDKAEDHEFSKTEELKLEDVDEEINAENVESKKKTVGDDESVPTGYHSKTEGAERTNDDSSAETIEKKEKANLEERAICEYNENPKGYMLDDADSSSLEILENSETTPSKDMKKTKKIFLFKRVPSINQKIVKNNNEPLPEIKSIGDQIILKSDNKDADQNHMSQNHQNIPPTNTERRSKSCTIL TTHBDA9 TT Clinical trial TTKT5NV ID TTKT5NV TTKT5NV TN Zinc finger protein Helios (IKZF2) TTKT5NV UP Q9UKS7 TTKT5NV UC IKZF2_HUMAN TTKT5NV SN Ikaros family zinc finger protein 2 TTKT5NV GN IKZF2 TTKT5NV FC Associates with Ikaros at centromeric heterochromatin. TTKT5NV SQ METEAIDGYITCDNELSPEREHSNMAIDLTSSTPNGQHASPSHMTSTNSVKLEMQSDEECDRKPLSREDEIRGHDEGSSLEEPLIESSEVADNRKVQELQGEGGIRLPNGKLKCDVCGMVCIGPNVLMVHKRSHTGERPFHCNQCGASFTQKGNLLRHIKLHSGEKPFKCPFCSYACRRRDALTGHLRTHSVGKPHKCNYCGRSYKQRSSLEEHKERCHNYLQNVSMEAAGQVMSHHVPPMEDCKEQEPIMDNNISLVPFERPAVIEKLTGNMGKRKSSTPQKFVGEKLMRFSYPDIHFDMNLTYEKEAELMQSHMMDQAINNAITYLGAEALHPLMQHPPSTIAEVAPVISSAYSQVYHPNRIERPISRETADSHENNMDGPISLIRPKSRPQEREASPSNSCLDSTDSESSHDDHQSYQGHPALNPKRKQSPAYMKEDVKALDTTKAPKGSLKDIYKVFNGEGEQIRAFKCEHCRVLFLDHVMYTIHMGCHGYRDPLECNICGYRSQDRYEFSSHIVRGEHTFH TTKT5NV TT Clinical trial TTK8XD6 ID TTK8XD6 TTK8XD6 TN ATP-binding cassette transporter (ABCA) TTK8XD6 UP Family TTK8XD6 UC NOUNIPROTAC TTK8XD6 BC ABC transporter TTK8XD6 GN NO-GeName TTK8XD6 TT Clinical trial TTV75BJ ID TTV75BJ TTV75BJ TN Carbohydrate antigen Lewis-Y (Lewis-Y) TTV75BJ UP NO-UNIPROT TTV75BJ UC NOUNIPROTAC TTV75BJ SN Lewis-Y carbohydrate antigen; Lewis-Y TTV75BJ GN NO-GeName TTV75BJ TT Clinical trial TT7MRGU ID TT7MRGU TT7MRGU TN Chymotrypsin (CTR) TT7MRGU UP Family TT7MRGU UC NOUNIPROTAC TT7MRGU BC Peptidase TT7MRGU GN NO-GeName TT7MRGU TT Clinical trial TTLK6DR ID TTLK6DR TTLK6DR TN Cyclin D1 synthesis (CCND1 synthesis) TTLK6DR UP Pathway/Process TTLK6DR UC NOUNIPROTAC TTLK6DR SN Cyclin D1 biosynthesis TTLK6DR GN NO-GeName TTLK6DR TT Clinical trial TTMBO1Z ID TTMBO1Z TTMBO1Z TN Cyclin-dependent kinase (CDK) TTMBO1Z UP Family TTMBO1Z UC NOUNIPROTAC TTMBO1Z SN Cyclin dependent kinase TTMBO1Z GN NO-GeName TTMBO1Z TT Clinical trial TT2GPK3 ID TT2GPK3 TT2GPK3 TN DNA topoisomerase (TOP) TT2GPK3 UP Family TT2GPK3 UC NOUNIPROTAC TT2GPK3 GN NO-GeName TT2GPK3 TT Clinical trial TTWFZ1N ID TTWFZ1N TTWFZ1N TN Dopamine receptor (DR) TTWFZ1N UP Family TTWFZ1N UC NOUNIPROTAC TTWFZ1N SN Human dopamine receptor TTWFZ1N GN NO-GeName TTWFZ1N TT Clinical trial TTWFZ1N FM G-protein coupled receptor 1 family TTCV6O0 ID TTCV6O0 TTCV6O0 TN Endothelin receptor (EDNR) TTCV6O0 UP Family TTCV6O0 UC NOUNIPROTAC TTCV6O0 SN Human endothelin receptor TTCV6O0 GN NO-GeName TTCV6O0 TT Clinical trial TT1BGDH ID TT1BGDH TT1BGDH TN Endothelin-converting enzyme (ECE) TT1BGDH UP Family TT1BGDH UC NOUNIPROTAC TT1BGDH SN Endothelin converting enzyme TT1BGDH GN NO-GeName TT1BGDH TT Clinical trial TT0LF7H ID TT0LF7H TT0LF7H TN Fibroblast growth factor receptor (FGFR) TT0LF7H UP Family TT0LF7H UC NOUNIPROTAC TT0LF7H SN FGF receptor TT0LF7H GN NO-GeName TT0LF7H TT Successful TTPXOQN ID TTPXOQN TTPXOQN TN Gastric carcinoma-associated antigen MG7 (MG7) TTPXOQN UP NO-UNIPROT TTPXOQN UC NOUNIPROTAC TTPXOQN SN MG7-Ag TTPXOQN GN NO-GeName TTPXOQN TT Clinical trial TT4P2VW ID TT4P2VW TT4P2VW TN Geranylgeranyl transferase (GGTase) TT4P2VW UP Family TT4P2VW UC NOUNIPROTAC TT4P2VW SN Geranylgeranyltransferase TT4P2VW GN NO-GeName TT4P2VW TT Clinical trial TTO7FVG ID TTO7FVG TTO7FVG TN Heat shock protein 90 (HSP90) TTO7FVG UP Family TTO7FVG UC NOUNIPROTAC TTO7FVG BC Heat shock protein TTO7FVG GN NO-GeName TTO7FVG TT Clinical trial TT3WAD0 ID TT3WAD0 TT3WAD0 TN HLA-A02/AFP complex (HLA-A02/AFP) TT3WAD0 UP NO-UNIPROT TT3WAD0 UC NOUNIPROTAC TT3WAD0 SN HLA-A2/AFP complex TT3WAD0 GN NO-GeName TT3WAD0 TT Clinical trial TTYJQTF ID TTYJQTF TTYJQTF TN Immunoglobulin E (IgE) TTYJQTF UP Family TTYJQTF UC NOUNIPROTAC TTYJQTF SN IgE TTYJQTF GN NO-GeName TTYJQTF TT Clinical trial TTPY4SE ID TTPY4SE TTPY4SE TN Immunoglobulin Fc receptor (FCR) TTPY4SE UP Family TTPY4SE UC NOUNIPROTAC TTPY4SE BC Immunoglobulin TTPY4SE GN NO-GeName TTPY4SE TT Clinical trial TT6ONYI ID TT6ONYI TT6ONYI TN Interferon (IFN) TT6ONYI UP Family TT6ONYI UC NOUNIPROTAC TT6ONYI SN Interferon protein TT6ONYI GN NO-GeName TT6ONYI TT Clinical trial TTV2CN0 ID TTV2CN0 TTV2CN0 TN Interferon receptor (IFNR) TTV2CN0 UP Family TTV2CN0 UC NOUNIPROTAC TTV2CN0 SN Interferon receptor TTV2CN0 GN NO-GeName TTV2CN0 TT Clinical trial TTF6I40 ID TTF6I40 TTF6I40 TN Interleukin (IL) TTF6I40 UP Family TTF6I40 UC NOUNIPROTAC TTF6I40 SN Interleukin TTF6I40 GN NO-GeName TTF6I40 TT Clinical trial TT1HM0R ID TT1HM0R TT1HM0R TN Kappa myeloma antigen (KMA) TT1HM0R UP NO-UNIPROT TT1HM0R UC NOUNIPROTAC TT1HM0R BC Kappa myeloma antigen TT1HM0R GN NO-GeName TT1HM0R TT Clinical trial TTO0YVN ID TTO0YVN TTO0YVN TN Leukocyte (WBC) TTO0YVN UP Organelle/Cell TTO0YVN UC NOUNIPROTAC TTO0YVN SN Human leukocyte TTO0YVN GN NO-GeName TTO0YVN TT Clinical trial TTTWGIX ID TTTWGIX TTTWGIX TN Leukotriene receptor (LTR) TTTWGIX UP Family TTTWGIX UC NOUNIPROTAC TTTWGIX SN Human leukotriene receptor TTTWGIX GN NO-GeName TTTWGIX TT Clinical trial TT1GHVO ID TT1GHVO TT1GHVO TN Matrix metalloproteinase (MMP) TT1GHVO UP Family TT1GHVO UC NOUNIPROTAC TT1GHVO SN Matrix metalloproteinase TT1GHVO GN NO-GeName TT1GHVO TT Successful TTM1EQF ID TTM1EQF TTM1EQF TN Oxysterols receptor LXR (NR1H) TTM1EQF UP Family TTM1EQF UC NOUNIPROTAC TTM1EQF BC Nuclear hormone receptor TTM1EQF GN NO-GeName TTM1EQF TT Clinical trial TT1UZQH ID TT1UZQH TT1UZQH TN Phospholipase C (PLC) TT1UZQH UP Family TT1UZQH UC NOUNIPROTAC TT1UZQH BC Phosphoric diester hydrolase TT1UZQH GN NO-GeName TT1UZQH TT Clinical trial TTU8W4S ID TTU8W4S TTU8W4S TN Protein kinase (PK) TTU8W4S UP Family TTU8W4S UC NOUNIPROTAC TTU8W4S BC Kinase TTU8W4S GN NO-GeName TTU8W4S TT Clinical trial TTABNSJ ID TTABNSJ TTABNSJ TN Pyruvate kinase (PK) TTABNSJ UP Family TTABNSJ UC NOUNIPROTAC TTABNSJ BC Kinase TTABNSJ GN NO-GeName TTABNSJ TT Clinical trial TTP7WQM ID TTP7WQM TTP7WQM TN Retinoic acid receptor RXR (RXR) TTP7WQM UP Family TTP7WQM UC NOUNIPROTAC TTP7WQM SN RXR TTP7WQM GN NO-GeName TTP7WQM TT Clinical trial TTRKDL6 ID TTRKDL6 TTRKDL6 TN Serine/threonine PP2A (PP2A) TTRKDL6 UP Family TTRKDL6 UC NOUNIPROTAC TTRKDL6 SN PP2A TTRKDL6 GN NO-GeName TTRKDL6 TT Clinical trial TT7BQRM ID TT7BQRM TT7BQRM TN Sphingosine-1 phosphate receptor (S1PR) TT7BQRM UP Family TT7BQRM UC NOUNIPROTAC TT7BQRM BC GPCR rhodopsin TT7BQRM GN NO-GeName TT7BQRM TT Successful TTXQYT6 ID TTXQYT6 TTXQYT6 TN T-cells (T-cells) TTXQYT6 UP Organelle/Cell TTXQYT6 UC NOUNIPROTAC TTXQYT6 SN T cells TTXQYT6 GN NO-GeName TTXQYT6 TT Clinical trial TT470F3 ID TT470F3 TT470F3 TN TNF alpha production (TNFA produ) TT470F3 UP Pathway/Process TT470F3 UC NOUNIPROTAC TT470F3 SN Tumor necrosis factor alpha production TT470F3 GN NO-GeName TT470F3 TT Clinical trial TTZXH48 ID TTZXH48 TTZXH48 TN TNF receptor (TNFR) TTZXH48 UP Family TTZXH48 UC NOUNIPROTAC TTZXH48 SN TNFR TTZXH48 GN NO-GeName TTZXH48 TT Clinical trial TTRPO9Z ID TTRPO9Z TTRPO9Z TN TNF-alpha signaling pathway (TNFA pathway) TTRPO9Z UP Pathway/Process TTRPO9Z UC NOUNIPROTAC TTRPO9Z BC Viral DNA polymerase TTRPO9Z GN NO-GeName TTRPO9Z TT Clinical trial TTOK0LR ID TTOK0LR TTOK0LR TN Toll-like receptor (TLR) TTOK0LR UP Family TTOK0LR UC NOUNIPROTAC TTOK0LR SN Toll-like receptor TTOK0LR GN NO-GeName TTOK0LR TT Clinical trial TTOK0LR FM Toll-like receptor family TT9PNO1 ID TT9PNO1 TT9PNO1 TN TRAIL receptor (TRAIL-R) TT9PNO1 UP Family TT9PNO1 UC NOUNIPROTAC TT9PNO1 GN NO-GeName TT9PNO1 FC Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADDrecruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF- kappa-B. TT9PNO1 TT Clinical trial TT7ZK9C ID TT7ZK9C TT7ZK9C TN Tryptophan 5-hydroxylase (TPH) TT7ZK9C UP Family TT7ZK9C UC NOUNIPROTAC TT7ZK9C BC Paired donor oxygen oxidoreductase TT7ZK9C GN NO-GeName TT7ZK9C TT Clinical trial TTSFNKW ID TTSFNKW TTSFNKW TN Tumor antigen NGcGM3 (NGcGM3) TTSFNKW UP NO-UNIPROT TTSFNKW UC NOUNIPROTAC TTSFNKW SN Tumor antigen N-glycolyl-GM3 TTSFNKW GN NO-GeName TTSFNKW TT Clinical trial TTT6NKW ID TTT6NKW TTT6NKW TN Voltage-gated T-type calcium channel (T-CaC) TTT6NKW UP Family TTT6NKW UC NOUNIPROTAC TTT6NKW BC Voltage-gated ion channel TTT6NKW GN NO-GeName TTT6NKW TT Clinical trial TTH5WZF ID TTH5WZF TTH5WZF TN Actin (ACT) TTH5WZF UP Family TTH5WZF UC NOUNIPROTAC TTH5WZF GN NO-GeName TTH5WZF TT Clinical trial TTU5CF1 ID TTU5CF1 TTU5CF1 TN Actin polymerization (Actin poly) TTU5CF1 UP Pathway/Process TTU5CF1 UC NOUNIPROTAC TTU5CF1 GN NO-GeName TTU5CF1 TT Clinical trial TTEWTCR ID TTEWTCR TTEWTCR TN Adenine synthesis (Adeni synth) TTEWTCR UP Pathway/Process TTEWTCR UC NOUNIPROTAC TTEWTCR GN NO-GeName TTEWTCR TT Clinical trial TTWLEZV ID TTWLEZV TTWLEZV TN Aminopeptidase (AMP) TTWLEZV UP Family TTWLEZV UC NOUNIPROTAC TTWLEZV GN NO-GeName TTWLEZV TT Clinical trial TTRAXK5 ID TTRAXK5 TTRAXK5 TN Aminotransferase (AT) TTRAXK5 UP Family TTRAXK5 UC NOUNIPROTAC TTRAXK5 GN NO-GeName TTRAXK5 TT Clinical trial TTB8Y9K ID TTB8Y9K TTB8Y9K TN Angiogenesis (AGG) TTB8Y9K UP Pathway/Process TTB8Y9K UC NOUNIPROTAC TTB8Y9K GN NO-GeName TTB8Y9K TT Clinical trial TT2QPV9 ID TT2QPV9 TT2QPV9 TN Aryl hydrocarbon receptor signaling pathway (AhR pathway) TT2QPV9 UP Pathway/Process TT2QPV9 UC NOUNIPROTAC TT2QPV9 GN NO-GeName TT2QPV9 TT Clinical trial TT5WKM8 ID TT5WKM8 TT5WKM8 TN ATP phosphatase (ATPase) TT5WKM8 UP Family TT5WKM8 UC NOUNIPROTAC TT5WKM8 GN NO-GeName TT5WKM8 TT Clinical trial TT2VX74 ID TT2VX74 TT2VX74 TN Bacterial Protein synthesis (Bact PROS) TT2VX74 UP Pathway/Process TT2VX74 UC NOUNIPROTAC TT2VX74 GN NO-GeName TT2VX74 TT Clinical trial TTAFORY ID TTAFORY TTAFORY TN Calcitonin gene-related peptide (CALC) TTAFORY UP Family TTAFORY UC NOUNIPROTAC TTAFORY GN NO-GeName TTAFORY TT Successful TTW6MKR ID TTW6MKR TTW6MKR TN Calcium release (Ca rele) TTW6MKR UP Pathway/Process TTW6MKR UC NOUNIPROTAC TTW6MKR GN NO-GeName TTW6MKR TT Clinical trial TTATDGJ ID TTATDGJ TTATDGJ TN Calcium signal-modulating cyclophilin ligand (CAML) TTATDGJ UP P49069 TTATDGJ UC CAMLG_HUMAN TTATDGJ SN cyclophilin TTATDGJ GN CAMLG; CAML TTATDGJ FC Likely involved in the mobilization of calcium as a result of the TCR/CD3 complex interaction. Binds to cyclophilin B. TTATDGJ SQ MESMAVATDGGERPGVPAGSGLSASQRRAELRRRKLLMNSEQRINRIMGFHRPGSGAEEESQTKSKQQDSDKLNSLSVPSVSKRVVLGDSVSTGTTDQQGGVAEVKGTQLGDKLDSFIKPPECSSDVNLELRQRNRGDLTADSVQRGSRHGLEQYLSRFEEAMKLRKQLISEKPSQEDGNTTEEFDSFRIFRLVGCALLALGVRAFVCKYLSIFAPFLTLQLAYMGLYKYFPKSEKKIKTTVLTAALLLSGIPAEVINRSMDTYSKMGEVFTDLCVYFFTFIFCHELLDYWGSEVP TTATDGJ TT Clinical trial TT0QZ8R ID TT0QZ8R TT0QZ8R TN cAMP formation (cAMP form) TT0QZ8R UP Pathway/Process TT0QZ8R UC NOUNIPROTAC TT0QZ8R GN NO-GeName TT0QZ8R TT Clinical trial TTPV9O1 ID TTPV9O1 TTPV9O1 TN Cancer stemness kinase (CSK) TTPV9O1 UP NO-UNIPROT TTPV9O1 UC NOUNIPROTAC TTPV9O1 GN NO-GeName TTPV9O1 TT Clinical trial TTZ5NI7 ID TTZ5NI7 TTZ5NI7 TN Casein kinase II (CSNK2) TTZ5NI7 UP Family TTZ5NI7 UC NOUNIPROTAC TTZ5NI7 GN NO-GeName TTZ5NI7 TT Clinical trial TTD26RC ID TTD26RC TTD26RC TN Cell adhesion molecule (CADM) TTD26RC UP Family TTD26RC UC NOUNIPROTAC TTD26RC GN NO-GeName TTD26RC TT Clinical trial TT34ECM ID TT34ECM TT34ECM TN Cell cycle (CC) TT34ECM UP Pathway/Process TT34ECM UC NOUNIPROTAC TT34ECM GN NO-GeName TT34ECM TT Clinical trial TTF63Z1 ID TTF63Z1 TTF63Z1 TN Cell differentiation (CD) TTF63Z1 UP Pathway/Process TTF63Z1 UC NOUNIPROTAC TTF63Z1 GN NO-GeName TTF63Z1 TT Clinical trial TT3FOGT ID TT3FOGT TT3FOGT TN Chemosensory receptor (CheR) TT3FOGT UP Family TT3FOGT UC NOUNIPROTAC TT3FOGT GN NO-GeName TT3FOGT TT Clinical trial TTNA5ZS ID TTNA5ZS TTNA5ZS TN Cholesterol absorption (Chole absorp) TTNA5ZS UP Pathway/Process TTNA5ZS UC NOUNIPROTAC TTNA5ZS GN NO-GeName TTNA5ZS TT Clinical trial TTRA79S ID TTRA79S TTRA79S TN Cholesterol synthesis (Chole synth) TTRA79S UP Pathway/Process TTRA79S UC NOUNIPROTAC TTRA79S GN NO-GeName TTRA79S TT Successful TT61VTP ID TT61VTP TT61VTP TN Cholesterol uptake (Chole uptake) TT61VTP UP Pathway/Process TT61VTP UC NOUNIPROTAC TT61VTP GN NO-GeName TT61VTP TT Clinical trial TTTMZSG ID TTTMZSG TTTMZSG TN Clostridium difficile Toxin (CD tox) TTTMZSG UP Family TTTMZSG UC NOUNIPROTAC TTTMZSG GN NO-GeName TTTMZSG TT Clinical trial TTXM6JN ID TTXM6JN TTXM6JN TN Cytokine receptor unspecific (CRF) TTXM6JN UP Family TTXM6JN UC NOUNIPROTAC TTXM6JN GN NO-GeName TTXM6JN TT Clinical trial TTFTSHD ID TTFTSHD TTFTSHD TN Cytokine unspecific (CYK) TTFTSHD UP Family TTFTSHD UC NOUNIPROTAC TTFTSHD GN NO-GeName TTFTSHD TT Clinical trial TTF5WCR ID TTF5WCR TTF5WCR TN Endogenous gut peptide (EGP) TTF5WCR UP NO-UNIPROT TTF5WCR UC NOUNIPROTAC TTF5WCR GN NO-GeName TTF5WCR TT Clinical trial TT26HJ8 ID TT26HJ8 TT26HJ8 TN Eosinophil/lymphocyte-rich accumulation (ELR accum) TT26HJ8 UP Pathway/Process TT26HJ8 UC NOUNIPROTAC TT26HJ8 GN NO-GeName TT26HJ8 TT Clinical trial TT5HU6Z ID TT5HU6Z TT5HU6Z TN Fibroblast growth factor (FGF) TT5HU6Z UP Family TT5HU6Z UC NOUNIPROTAC TT5HU6Z GN NO-GeName TT5HU6Z TT Clinical trial TTFH2RS ID TTFH2RS TTFH2RS TN FK506-binding protein (FKBP) TTFH2RS UP Family TTFH2RS UC NOUNIPROTAC TTFH2RS GN NO-GeName TTFH2RS TT Clinical trial TTCI43M ID TTCI43M TTCI43M TN GABA(A) receptor (GABAR) TTCI43M UP Family TTCI43M UC NOUNIPROTAC TTCI43M GN NO-GeName TTCI43M TT Clinical trial TTPJ1I3 ID TTPJ1I3 TTPJ1I3 TN Galactosyltransferase (GALT) TTPJ1I3 UP Family TTPJ1I3 UC NOUNIPROTAC TTPJ1I3 GN NO-GeName TTPJ1I3 TT Clinical trial TTX1OI0 ID TTX1OI0 TTX1OI0 TN Galectin (LGALS) TTX1OI0 UP Family TTX1OI0 UC NOUNIPROTAC TTX1OI0 GN NO-GeName TTX1OI0 TT Clinical trial TTJO6E9 ID TTJO6E9 TTJO6E9 TN Gap junction protein (GJP) TTJO6E9 UP Family TTJO6E9 UC NOUNIPROTAC TTJO6E9 GN NO-GeName TTJO6E9 TT Clinical trial TTZ7WFL ID TTZ7WFL TTZ7WFL TN Glucose metabolism (Glucose metab) TTZ7WFL UP Pathway/Process TTZ7WFL UC NOUNIPROTAC TTZ7WFL GN NO-GeName TTZ7WFL TT Clinical trial TTDXZ24 ID TTDXZ24 TTDXZ24 TN Glutamate receptor ionotropic (GRI) TTDXZ24 UP Family TTDXZ24 UC NOUNIPROTAC TTDXZ24 GN NO-GeName TTDXZ24 TT Clinical trial TTSTYLU ID TTSTYLU TTSTYLU TN Growth hormone secretion (GH secr) TTSTYLU UP Pathway/Process TTSTYLU UC NOUNIPROTAC TTSTYLU GN NO-GeName TTSTYLU TT Clinical trial TTC6JZQ ID TTC6JZQ TTC6JZQ TN Haemophilus influenzae CRM197 (Hae-influ CRM197) TTC6JZQ UP NO-UNIPROT TTC6JZQ UC NOUNIPROTAC TTC6JZQ GN NO-GeName TTC6JZQ TT Clinical trial TTPTJUM ID TTPTJUM TTPTJUM TN Haemophilus influenzae Outer membrane protein (Hae-influ OMP) TTPTJUM UP Family TTPTJUM UC NOUNIPROTAC TTPTJUM GN NO-GeName TTPTJUM TT Clinical trial TTG91S4 ID TTG91S4 TTG91S4 TN Heat shock protein (HSP) TTG91S4 UP Family TTG91S4 UC NOUNIPROTAC TTG91S4 GN NO-GeName TTG91S4 TT Clinical trial TTIEJ8U ID TTIEJ8U TTIEJ8U TN Helper-inducer T-lymphocyte (HITL) TTIEJ8U UP Organelle/Cell TTIEJ8U UC NOUNIPROTAC TTIEJ8U GN NO-GeName TTIEJ8U TT Clinical trial TTMR83K ID TTMR83K TTMR83K TN Hepatitis B virus Reverse transcriptase priming/DNA synthesis (HBV RTP/DS) TTMR83K UP Pathway/Process TTMR83K UC NOUNIPROTAC TTMR83K GN NO-GeName TTMR83K TT Clinical trial TTE3PC9 ID TTE3PC9 TTE3PC9 TN Hepatitis C virus Non-structural 5 (HCV NS5) TTE3PC9 UP Family TTE3PC9 UC NOUNIPROTAC TTE3PC9 GN NO-GeName TTE3PC9 TT Clinical trial TT4IN7L ID TT4IN7L TT4IN7L TN Histamine release (His rele) TT4IN7L UP Pathway/Process TT4IN7L UC NOUNIPROTAC TT4IN7L GN NO-GeName TT4IN7L TT Clinical trial TT7KY5U ID TT7KY5U TT7KY5U TN Histamine/peptide leukotriene release (His/p-LT rele) TT7KY5U UP Pathway/Process TT7KY5U UC NOUNIPROTAC TT7KY5U GN NO-GeName TT7KY5U TT Clinical trial TTUIFO6 ID TTUIFO6 TTUIFO6 TN Human immunodeficiency virus Adenovector Ad35 (HIV Ad35) TTUIFO6 UP NO-UNIPROT TTUIFO6 UC NOUNIPROTAC TTUIFO6 GN NO-GeName TTUIFO6 TT Clinical trial TT5TOX7 ID TT5TOX7 TT5TOX7 TN Human immunodeficiency virus Maturation (HIV Mat) TT5TOX7 UP Pathway/Process TT5TOX7 UC NOUNIPROTAC TT5TOX7 GN NO-GeName TT5TOX7 TT Clinical trial TTAUG8D ID TTAUG8D TTAUG8D TN Human immunodeficiency virus Transmission (HIV Tran) TTAUG8D UP Pathway/Process TTAUG8D UC NOUNIPROTAC TTAUG8D GN NO-GeName TTAUG8D TT Clinical trial TT20DOQ ID TT20DOQ TT20DOQ TN Hydroxy radical elimination (HYRE) TT20DOQ UP Pathway/Process TT20DOQ UC NOUNIPROTAC TT20DOQ GN NO-GeName TT20DOQ TT Clinical trial TTEWNM1 ID TTEWNM1 TTEWNM1 TN IL-1 synthesis/release (IL-1 synth/rele) TTEWNM1 UP Pathway/Process TTEWNM1 UC NOUNIPROTAC TTEWNM1 GN NO-GeName TTEWNM1 TT Clinical trial TTV8N19 ID TTV8N19 TTV8N19 TN Immune checkpoint (ICH) TTV8N19 UP Pathway/Process TTV8N19 UC NOUNIPROTAC TTV8N19 GN NO-GeName TTV8N19 TT Clinical trial TTA6ZER ID TTA6ZER TTA6ZER TN Immunoglobulin G1k (IgG1k) TTA6ZER UP Family TTA6ZER UC NOUNIPROTAC TTA6ZER GN NO-GeName TTA6ZER TT Clinical trial TTBD054 ID TTBD054 TTBD054 TN Inflammation pathogenesis (IP) TTBD054 UP Pathway/Process TTBD054 UC NOUNIPROTAC TTBD054 GN NO-GeName TTBD054 TT Clinical trial TT5XVD6 ID TT5XVD6 TT5XVD6 TN Intracellular nitroreductase (INR) TT5XVD6 UP NO-UNIPROT TT5XVD6 UC NOUNIPROTAC TT5XVD6 GN NO-GeName TT5XVD6 TT Clinical trial TTM7WCE ID TTM7WCE TTM7WCE TN Ion channel unspecific (IC) TTM7WCE UP Family TTM7WCE UC NOUNIPROTAC TTM7WCE GN NO-GeName TTM7WCE TT Clinical trial TTKAWRQ ID TTKAWRQ TTKAWRQ TN JAK-STAT signaling pathway (JAK-STAT pathway) TTKAWRQ UP Pathway/Process TTKAWRQ UC NOUNIPROTAC TTKAWRQ GN NO-GeName TTKAWRQ TT Clinical trial TTX1JEN ID TTX1JEN TTX1JEN TN JNK signaling pathway (JNK pathway) TTX1JEN UP Pathway/Process TTX1JEN UC NOUNIPROTAC TTX1JEN GN NO-GeName TTX1JEN TT Clinical trial TTNHYJL ID TTNHYJL TTNHYJL TN Ketogenesis (KG) TTNHYJL UP Pathway/Process TTNHYJL UC NOUNIPROTAC TTNHYJL GN NO-GeName TTNHYJL TT Clinical trial TT40BO8 ID TT40BO8 TT40BO8 TN Late inward sodium current (LISC) TT40BO8 UP Pathway/Process TT40BO8 UC NOUNIPROTAC TT40BO8 GN NO-GeName TT40BO8 TT Clinical trial TTV0YFR ID TTV0YFR TTV0YFR TN Lipid peroxidation (LPO) TTV0YFR UP Pathway/Process TTV0YFR UC NOUNIPROTAC TTV0YFR GN NO-GeName TTV0YFR TT Clinical trial TTG3K2U ID TTG3K2U TTG3K2U TN Lipoxygenase (ALOX) TTG3K2U UP Family TTG3K2U UC NOUNIPROTAC TTG3K2U GN NO-GeName TTG3K2U TT Clinical trial TTC8NQ2 ID TTC8NQ2 TTC8NQ2 TN Lyase unspecific (LYA) TTC8NQ2 UP Family TTC8NQ2 UC NOUNIPROTAC TTC8NQ2 GN NO-GeName TTC8NQ2 TT Clinical trial TT2DLFI ID TT2DLFI TT2DLFI TN Lysosphingolipid receptor (LSPR) TT2DLFI UP Family TT2DLFI UC NOUNIPROTAC TT2DLFI GN NO-GeName TT2DLFI TT Clinical trial TTA5LWY ID TTA5LWY TTA5LWY TN M1-prime segment of membrane-expressed IgE (M1 IgE) TTA5LWY UP NO-UNIPROT TTA5LWY UC NOUNIPROTAC TTA5LWY GN NO-GeName TTA5LWY TT Clinical trial TT7KPH1 ID TT7KPH1 TT7KPH1 TN MAPK/ERK signaling pathway (MAPK pathway) TT7KPH1 UP Pathway/Process TT7KPH1 UC NOUNIPROTAC TT7KPH1 GN NO-GeName TT7KPH1 TT Clinical trial TTZ1DV7 ID TTZ1DV7 TTZ1DV7 TN Mitochondrial function (MF) TTZ1DV7 UP Pathway/Process TTZ1DV7 UC NOUNIPROTAC TTZ1DV7 GN NO-GeName TTZ1DV7 TT Clinical trial TTSJH2W ID TTSJH2W TTSJH2W TN Mitochondrial protein unspecific (MP) TTSJH2W UP Family TTSJH2W UC NOUNIPROTAC TTSJH2W GN NO-GeName TTSJH2W TT Clinical trial TTHBUXE ID TTHBUXE TTHBUXE TN Mucin (MUC) TTHBUXE UP Family TTHBUXE UC NOUNIPROTAC TTHBUXE GN NO-GeName TTHBUXE TT Clinical trial TTITSMB ID TTITSMB TTITSMB TN Myosin (MYO) TTITSMB UP Family TTITSMB UC NOUNIPROTAC TTITSMB GN NO-GeName TTITSMB TT Clinical trial TTRF7Q8 ID TTRF7Q8 TTRF7Q8 TN Natural killer cell receptor (NKCR) TTRF7Q8 UP Family TTRF7Q8 UC NOUNIPROTAC TTRF7Q8 GN NO-GeName TTRF7Q8 TT Clinical trial TT34I9F ID TT34I9F TT34I9F TN Neoplasm antigen (NA) TT34I9F UP Family TT34I9F UC NOUNIPROTAC TT34I9F GN NO-GeName TT34I9F TT Clinical trial TTWFC4G ID TTWFC4G TTWFC4G TN Netrin (NET) TTWFC4G UP Family TTWFC4G UC NOUNIPROTAC TTWFC4G GN NO-GeName TTWFC4G TT Clinical trial TTOASGR ID TTOASGR TTOASGR TN Neuroepithelial receptor (NR) TTOASGR UP NO-UNIPROT TTOASGR UC NOUNIPROTAC TTOASGR GN NO-GeName TTOASGR TT Clinical trial TT9RTYG ID TT9RTYG TT9RTYG TN Neuropeptide receptor (NPR) TT9RTYG UP Family TT9RTYG UC NOUNIPROTAC TT9RTYG GN NO-GeName TT9RTYG TT Clinical trial TTTD45S ID TTTD45S TTTD45S TN Neurotransmitter release (NT rele) TTTD45S UP Pathway/Process TTTD45S UC NOUNIPROTAC TTTD45S GN NO-GeName TTTD45S TT Clinical trial TTXT2VN ID TTXT2VN TTXT2VN TN NF-kappa-B-p38 signaling pathway (NFKB-p38 pathway) TTXT2VN UP Pathway/Process TTXT2VN UC NOUNIPROTAC TTXT2VN GN NO-GeName TTXT2VN TT Clinical trial TTUO9SZ ID TTUO9SZ TTUO9SZ TN Nitric oxide elimination (NOE) TTUO9SZ UP Pathway/Process TTUO9SZ UC NOUNIPROTAC TTUO9SZ GN NO-GeName TTUO9SZ TT Clinical trial TT3V81G ID TT3V81G TT3V81G TN Nuclear receptor unspecific (NR) TT3V81G UP Family TT3V81G UC NOUNIPROTAC TT3V81G GN NO-GeName TT3V81G TT Clinical trial TTUS05D ID TTUS05D TTUS05D TN Nucleoside DNA polymerase (DPOL) TTUS05D UP Family TTUS05D UC NOUNIPROTAC TTUS05D GN NO-GeName TTUS05D TT Clinical trial TTC0BEN ID TTC0BEN TTC0BEN TN Oxidative stress (OS) TTC0BEN UP Pathway/Process TTC0BEN UC NOUNIPROTAC TTC0BEN GN NO-GeName TTC0BEN TT Clinical trial TTGMYVE ID TTGMYVE TTGMYVE TN Phosphofructokinase 2 (PFK2) TTGMYVE UP Family TTGMYVE UC NOUNIPROTAC TTGMYVE GN NO-GeName TTGMYVE TT Clinical trial TTWR6YK ID TTWR6YK TTWR6YK TN PI3-kinase (PIK3C) TTWR6YK UP NOUNIPROTAC TTWR6YK UC Family TTWR6YK GN NO-GeName TTWR6YK TT Literature-reported TTQ2GJ0 ID TTQ2GJ0 TTQ2GJ0 TN Plasmodial phospholipid metabolism (PPP metab) TTQ2GJ0 UP Pathway/Process TTQ2GJ0 UC NOUNIPROTAC TTQ2GJ0 GN NO-GeName TTQ2GJ0 TT Clinical trial TTHQGFL ID TTHQGFL TTHQGFL TN PMN apoptosis and chemotaxis (PMNAC) TTHQGFL UP Pathway/Process TTHQGFL UC NOUNIPROTAC TTHQGFL GN NO-GeName TTHQGFL TT Clinical trial TTYA7V2 ID TTYA7V2 TTYA7V2 TN Prostate cance cell (PCC) TTYA7V2 UP Organelle/Cell TTYA7V2 UC NOUNIPROTAC TTYA7V2 GN NO-GeName TTYA7V2 TT Clinical trial TTGFK5X ID TTGFK5X TTGFK5X TN Protein kinase unspecific (PK) TTGFK5X UP Family TTGFK5X UC NOUNIPROTAC TTGFK5X GN NO-GeName TTGFK5X TT Clinical trial TTLIZBJ ID TTLIZBJ TTLIZBJ TN Protein synthesis (hPRO synth) TTLIZBJ UP Pathway/Process TTLIZBJ UC NOUNIPROTAC TTLIZBJ GN NO-GeName TTLIZBJ TT Clinical trial TTIB5LO ID TTIB5LO TTIB5LO TN Quinone reductase (NQO) TTIB5LO UP Family TTIB5LO UC NOUNIPROTAC TTIB5LO GN NO-GeName TTIB5LO TT Clinical trial TTDB5IS ID TTDB5IS TTDB5IS TN Receptor unspecific (Rec) TTDB5IS UP Family TTDB5IS UC NOUNIPROTAC TTDB5IS GN NO-GeName TTDB5IS TT Clinical trial TTBMAOZ ID TTBMAOZ TTBMAOZ TN Regulatory protein unspecific (RGP) TTBMAOZ UP Family TTBMAOZ UC NOUNIPROTAC TTBMAOZ GN NO-GeName TTBMAOZ TT Clinical trial TTRBUYN ID TTRBUYN TTRBUYN TN Ribonuclease (RNase) TTRBUYN UP Family TTRBUYN UC NOUNIPROTAC TTRBUYN GN NO-GeName TTRBUYN TT Clinical trial TTJ073B ID TTJ073B TTJ073B TN Ribosome (hRBS) TTJ073B UP Organelle/Cell TTJ073B UC NOUNIPROTAC TTJ073B GN NO-GeName TTJ073B TT Clinical trial TT1AVS7 ID TT1AVS7 TT1AVS7 TN Second phase insulin secretion (SPI secr) TT1AVS7 UP Pathway/Process TT1AVS7 UC NOUNIPROTAC TT1AVS7 GN NO-GeName TT1AVS7 TT Clinical trial TT2XHSJ ID TT2XHSJ TT2XHSJ TN Secretory phospholipase A2 (sPLA2) TT2XHSJ UP Family TT2XHSJ UC NOUNIPROTAC TT2XHSJ GN NO-GeName TT2XHSJ TT Clinical trial TTBGONL ID TTBGONL TTBGONL TN Selectin (SEL) TTBGONL UP Family TTBGONL UC NOUNIPROTAC TTBGONL GN NO-GeName TTBGONL TT Clinical trial TTPMIQ9 ID TTPMIQ9 TTPMIQ9 TN Serine/threonine-protein kinase (STK) TTPMIQ9 UP Family TTPMIQ9 UC NOUNIPROTAC TTPMIQ9 GN NO-GeName TTPMIQ9 TT Clinical trial TTPVYKI ID TTPVYKI TTPVYKI TN Signal transduction unspecific (ST) TTPVYKI UP Pathway/Process TTPVYKI UC NOUNIPROTAC TTPVYKI GN NO-GeName TTPVYKI TT Clinical trial TTYJL7K ID TTYJL7K TTYJL7K TN Sodium/potassium transport (Na/K trans) TTYJL7K UP Pathway/Process TTYJL7K UC NOUNIPROTAC TTYJL7K GN NO-GeName TTYJL7K TT Clinical trial TTOMNR9 ID TTOMNR9 TTOMNR9 TN Somatostatin receptor (SSTR) TTOMNR9 UP Family TTOMNR9 UC NOUNIPROTAC TTOMNR9 GN NO-GeName TTOMNR9 TT Clinical trial TTV4B1Y ID TTV4B1Y TTV4B1Y TN Src tyrosine kinase signaling pathway (Src pathway) TTV4B1Y UP Pathway/Process TTV4B1Y UC NOUNIPROTAC TTV4B1Y GN NO-GeName TTV4B1Y TT Literature-reported TT3BLGR ID TT3BLGR TT3BLGR TN STAT3-Beta-catenin pathway (SBC pathway) TT3BLGR UP Pathway/Process TT3BLGR UC NOUNIPROTAC TT3BLGR GN NO-GeName TT3BLGR TT Clinical trial TTPW8EF ID TTPW8EF TTPW8EF TN Synaptic transmission (ST) TTPW8EF UP Pathway/Process TTPW8EF UC NOUNIPROTAC TTPW8EF GN NO-GeName TTPW8EF TT Clinical trial TTZGF8B ID TTZGF8B TTZGF8B TN Tau protein aggregation (TauA) TTZGF8B UP Pathway/Process TTZGF8B UC NOUNIPROTAC TTZGF8B GN NO-GeName TTZGF8B TT Clinical trial TT7AKW1 ID TT7AKW1 TT7AKW1 TN T-cell receptor (TCR) TT7AKW1 UP Family TT7AKW1 UC NOUNIPROTAC TT7AKW1 GN NO-GeName TT7AKW1 TT Clinical trial TT5BDCY ID TT5BDCY TT5BDCY TN TGF-beta receptor (TGFBR) TT5BDCY UP Family TT5BDCY UC NOUNIPROTAC TT5BDCY GN NO-GeName TT5BDCY TT Clinical trial TTQWUPT ID TTQWUPT TTQWUPT TN Thyroid hormone receptor (THR) TTQWUPT UP Family TTQWUPT UC NOUNIPROTAC TTQWUPT GN NO-GeName TTQWUPT TT Clinical trial TT4EWFY ID TT4EWFY TT4EWFY TN TNF/IL-10 release (TNF/IL10 rele) TT4EWFY UP Pathway/Process TT4EWFY UC NOUNIPROTAC TT4EWFY GN NO-GeName TT4EWFY TT Clinical trial TTGD6BY ID TTGD6BY TTGD6BY TN TNF-alpha/IL-1 beta production (TNFA/IL1B produ) TTGD6BY UP Pathway/Process TTGD6BY UC NOUNIPROTAC TTGD6BY GN NO-GeName TTGD6BY TT Clinical trial TTRX125 ID TTRX125 TTRX125 TN Transcription factor unspecific (TF) TTRX125 UP Family TTRX125 UC NOUNIPROTAC TTRX125 GN NO-GeName TTRX125 TT Clinical trial TTX2N1T ID TTX2N1T TTX2N1T TN Transferase unspecific (TF) TTX2N1T UP Family TTX2N1T UC NOUNIPROTAC TTX2N1T GN NO-GeName TTX2N1T TT Successful TTXEVN8 ID TTXEVN8 TTXEVN8 TN Transforming protein Rho (RHO) TTXEVN8 UP Family TTXEVN8 UC NOUNIPROTAC TTXEVN8 GN NO-GeName TTXEVN8 TT Clinical trial TT79AOF ID TT79AOF TT79AOF TN Transient receptor potential channel (TRP channel) TT79AOF UP Family TT79AOF UC NOUNIPROTAC TT79AOF GN NO-GeName TT79AOF TT Clinical trial TTSB7ZR ID TTSB7ZR TTSB7ZR TN Trigeminal ganglion stimulation-induced response (TGSR) TTSB7ZR UP Pathway/Process TTSB7ZR UC NOUNIPROTAC TTSB7ZR GN NO-GeName TTSB7ZR TT Clinical trial TTHVQ4N ID TTHVQ4N TTHVQ4N TN Tubulin polymerization (TubP) TTHVQ4N UP Pathway/Process TTHVQ4N UC NOUNIPROTAC TTHVQ4N GN NO-GeName TTHVQ4N TT Successful TTYG378 ID TTYG378 TTYG378 TN Tuftsin receptor (TR) TTYG378 UP NO-UNIPROT TTYG378 UC NOUNIPROTAC TTYG378 GN NO-GeName TTYG378 TT Clinical trial TTU8HT1 ID TTU8HT1 TTU8HT1 TN Ubiquitin-activating enzyme (UBA) TTU8HT1 UP Family TTU8HT1 UC NOUNIPROTAC TTU8HT1 GN NO-GeName TTU8HT1 TT Clinical trial TTMCA52 ID TTMCA52 TTMCA52 TN Viral Maturation (VM) TTMCA52 UP Pathway/Process TTMCA52 UC NOUNIPROTAC TTMCA52 GN NO-GeName TTMCA52 TT Clinical trial TTL3N71 ID TTL3N71 TTL3N71 TN Virus Replication (Viru Repli) TTL3N71 UP Pathway/Process TTL3N71 UC NOUNIPROTAC TTL3N71 GN NO-GeName TTL3N71 TT Clinical trial TTE5Q4N ID TTE5Q4N TTE5Q4N TN VWF-dependent platelet-collagen conversion (VDDPCC) TTE5Q4N UP Pathway/Process TTE5Q4N UC NOUNIPROTAC TTE5Q4N GN NO-GeName TTE5Q4N TT Clinical trial TTVZ87F ID TTVZ87F TTVZ87F TN Wnt protein (WNT) TTVZ87F UP Family TTVZ87F UC NOUNIPROTAC TTVZ87F GN NO-GeName TTVZ87F TT Clinical trial TTFPSHI ID TTFPSHI TTFPSHI TN Wnt signaling pathway (Wnt pathway) TTFPSHI UP Pathway/Process TTFPSHI UC NOUNIPROTAC TTFPSHI GN NO-GeName TTFPSHI TT Clinical trial TT3J1EK ID TT3J1EK TT3J1EK TN Zinc finger protein (ZNF) TT3J1EK UP Family TT3J1EK UC NOUNIPROTAC TT3J1EK GN NO-GeName TT3J1EK TT Clinical trial TTRPDBG ID TTRPDBG TTRPDBG TN Inhibitor of nuclear factor kappa-B kinase (IKK) TTRPDBG UP Family TTRPDBG UC NOUNIPROTAC TTRPDBG SN IB kinase; IkappaB kinase; IKK TTRPDBG GN NO-GeName TTRPDBG FC Serine kinase that plays an essential role in the NF- kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators sincethey exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation. TTRPDBG TT Patented-recorded TTRPDBG FM Protein kinase superfamily. Ser/Thr protein kinase family TTRPDBG RC R-HSA-1169091:Activation of NF-kappaB in B cells; R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-1810476:RIP-mediated NFkB activation via ZBP1; R-HSA-198323:AKT phosphorylates targets in the cytosol; R-HSA-209543:p75NTR recruits signalling complexes; R-HSA-209560:NF-kB is activated and signals survival; R-HSA-2871837:FCERI mediated NF-kB activation; R-HSA-446652:Interleukin-1 signaling; R-HSA-5357905:Regulation of TNFR1 signaling; R-HSA-5357956:TNFR1-induced NFkappaB signaling pathway; R-HSA-5602636:IKBKB deficiency causes SCID; R-HSA-5603027:IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR); R-HSA-5603029:IkBA variant leads to EDA-ID; R-HSA-5607761:Dectin-1 mediated noncanonical NF-kB signaling; R-HSA-5607764:CLEC7A (Dectin-1) signaling; R-HSA-5674400:Constitutive Signaling by AKT1 E17K in Cancer; R-HSA-5676590:NIK-->noncanonical NF-kB signaling; R-HSA-5684264:MAP3K8 (TPL2)-dependent MAPK1/3 activation; R-HSA-933541:TRAF6 mediated IRF7 activation; R-HSA-933542:TRAF6 mediated NF-kB activation; R-HSA-933543:NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10; R-HSA-936440:Negative regulators of RIG-I/MDA5 signaling; R-HSA-936964:Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon; R-HSA-937039:IRAK1 recruits IKK complex; R-HSA-937041:IKK complex recruitment mediated by RIP1; R-HSA-975144:IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation TTWT5K7 ID TTWT5K7 TTWT5K7 TN 5-HT 1 receptor (5HT1R) TTWT5K7 UP Family TTWT5K7 UC NOUNIPROTAC TTWT5K7 BC GPCR rhodopsin TTWT5K7 SN Serotonin receptor 1; 5-hydroxytryptamine receptor 1; 5-HT1 receptor TTWT5K7 GN NO-GeName TTWT5K7 TT Patented-recorded TTMY6L1 ID TTMY6L1 TTMY6L1 TN Fatty acid-binding protein (FABP) TTMY6L1 UP Family TTMY6L1 UC NOUNIPROTAC TTMY6L1 SN Fatty acid binding protein TTMY6L1 GN NO-GeName TTMY6L1 TT Patented-recorded TTMY6L1 FM Calycin superfamily TTMY6L1 KE hsa00250:Alanine, aspartate and glutamate metabolism; hsa00270:Cysteine and methionine metabolism; hsa00330:Arginine and proline metabolism; hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism; hsa00400:Phenylalanine, tyrosine and tryptophan biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa01210:2-Oxocarboxylic acid metabolism; hsa01230:Biosynthesis of amino acids; hsa04975:Fat digestion and absorption TTMY6L1 RC R-HSA-70263:Gluconeogenesis; R-HSA-70614:Amino acid synthesis and interconversion (transamination) TT9BPT3 ID TT9BPT3 TT9BPT3 TN Orexin receptor (HCRTR) TT9BPT3 UP Family TT9BPT3 UC NOUNIPROTAC TT9BPT3 SN Hypocretin receptor TT9BPT3 GN NO-GeName TT9BPT3 FC Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide. Seems to be exclusively coupled to the G(q) subclass of heteromeric G proteins, which activates the phospholipase C mediated signaling cascade. TT9BPT3 TT Patented-recorded TT53E8H ID TT53E8H TT53E8H TN Amine oxidase (AO) TT53E8H UP Family TT53E8H UC NOUNIPROTAC TT53E8H SN Amine oxidase (copper-containing); AOC TT53E8H GN NO-GeName TT53E8H TT Literature-reported TTCY4SB ID TTCY4SB TTCY4SB TN Aurora kinase (AURK) TTCY4SB UP Family TTCY4SB UC NOUNIPROTAC TTCY4SB SN Serine/threonine kinase TTCY4SB GN NO-GeName TTCY4SB TT Clinical trial TTCY4SB FM Protein kinase superfamily. Ser/Thr protein kinase family TTUX68I ID TTUX68I TTUX68I TN Hypoxia-inducible factor 1 (HIF-1) TTUX68I UP Family TTUX68I UC NOUNIPROTAC TTUX68I SN HIF-1 TTUX68I GN NO-GeName TTUX68I TT Patented-recorded TTSJMN8 ID TTSJMN8 TTSJMN8 TN Immunoproteasome complex (IP) TTSJMN8 UP NO-UNIPROT TTSJMN8 UC NOUNIPROTAC TTSJMN8 SN i-proteasome complex TTSJMN8 GN NO-GeName TTSJMN8 TT Patented-recorded TT3ZIJL ID TT3ZIJL TT3ZIJL TN JNK-interacting protein peptide (pepJIP) TT3ZIJL UP Family TT3ZIJL UC NOUNIPROTAC TT3ZIJL SN pepJIP TT3ZIJL GN NO-GeName TT3ZIJL TT Patented-recorded TT3ZIJL FM JIP scaffold family TT0RGE9 ID TT0RGE9 TT0RGE9 TN Lysine-specific demethylase 4 (KDM4) TT0RGE9 UP Family TT0RGE9 UC NOUNIPROTAC TT0RGE9 SN KDM4 TT0RGE9 GN NO-GeName TT0RGE9 TT Patented-recorded TT0RGE9 FM JHDM3 histone demethylase family TTSCO7R ID TTSCO7R TTSCO7R TN NAD-dependent deacetylase sirtuin (SIRT) TTSCO7R UP Family TTSCO7R UC NOUNIPROTAC TTSCO7R SN NAD+-dependent deacetylase SIRT TTSCO7R GN NO-GeName TTSCO7R TT Patented-recorded TTSCO7R FM Sirtuin family TTQSFTZ ID TTQSFTZ TTQSFTZ TN Phosphoprotein phosphatases 1 (PP1) TTQSFTZ UP Family TTQSFTZ UC NOUNIPROTAC TTQSFTZ SN Protein phosphatase 1 TTQSFTZ GN NO-GeName TTQSFTZ TT Patented-recorded TTQSFTZ FM PPP phosphatase family TT5SZDC ID TT5SZDC TT5SZDC TN Serine/threonine-protein phosphatase (PSP) TT5SZDC UP Family TT5SZDC UC NOUNIPROTAC TT5SZDC SN Protein serine/threonine phosphatase TT5SZDC GN NO-GeName TT5SZDC TT Patented-recorded TT5SZDC FM PPP phosphatase family TT3M2WO ID TT3M2WO TT3M2WO TN Sphingosine kinase (SphK) TT3M2WO UP Family TT3M2WO UC NOUNIPROTAC TT3M2WO SN SphK TT3M2WO GN NO-GeName TT3M2WO TT Patented-recorded TTXWCK2 ID TTXWCK2 TTXWCK2 TN Hepatitis C virus Internal ribosome entry site messenger RNA (HCV IRES mRNA) TTXWCK2 UP NO-UNIPROT TTXWCK2 UC NOUNIPROTAC TTXWCK2 BC mRNA target TTXWCK2 SN mRNA of HCV IRES TTXWCK2 GN NO-GeName TTXWCK2 TT Discontinued TTZC9FV ID TTZC9FV TTZC9FV TN Vasoactive intestinal polypeptide receptor (VIPR) TTZC9FV UP Family TTZC9FV UC NOUNIPROTAC TTZC9FV BC GPCR secretin TTZC9FV SN VIP-R; VIP receptor TTZC9FV GN NO-GeName TTZC9FV TT Discontinued TT7OGZP ID TT7OGZP TT7OGZP TN Casein kinase 1 (CK1) TT7OGZP UP P48729; P48730; P49674; Q9HCP0; P78368; Q9Y6M4 TT7OGZP UC KC1A_HUMAN; KC1D_HUMAN; KC1E_HUMAN; KC1G1_HUMAN; KC1G2_HUMAN; KC1G3_HUMAN TT7OGZP GN NO-GeName TT7OGZP TT Preclinical TTKW9CI ID TTKW9CI TTKW9CI TN FOXO4-P53 interaction (FOXO4-P53 PPI) TTKW9CI UP P98177-P04637 TTKW9CI UC FOXO4_HUMAN-P53_HUMAN TTKW9CI GN FOXO4-TP53 TTKW9CI TT Preclinical TTDW3Z2 ID TTDW3Z2 TTDW3Z2 TN Telomerase messenger RNA (Telomerase mRNA) TTDW3Z2 UP Family TTDW3Z2 UC NOUNIPROTAC TTDW3Z2 BC mRNA target TTDW3Z2 SN mRNA of Terminal transferase TTDW3Z2 GN NO-GeName TTDW3Z2 TT Discontinued TTTK3BH ID TTTK3BH TTTK3BH TN Vacuolar-type proton ATPase (v-ATPase) TTTK3BH UP Family TTTK3BH UC NOUNIPROTAC TTTK3BH BC Acid anhydrides hydrolase TTTK3BH SN Vacuolar-ATPase; Vacuolar ATPase; V-ATPase TTTK3BH GN NO-GeName TTTK3BH TT Preclinical TT438XZ ID TT438XZ TT438XZ TN Cyclin D1/E2F pathway (CCND1/E2F pathway) TT438XZ UP Pathway/Process TT438XZ UC NOUNIPROTAC TT438XZ SN Cyclin D1/E2F pathway signalling TT438XZ GN NO-GeName TT438XZ TT Discontinued TTKG67B ID TTKG67B TTKG67B TN Neuropeptide Y receptor (NPYR) TTKG67B UP Family TTKG67B UC NOUNIPROTAC TTKG67B SN NPY receptor TTKG67B GN NO-GeName TTKG67B TT Discontinued TTOV74C ID TTOV74C TTOV74C TN Bone metabolism (Bone metab) TTOV74C UP Pathway/Process TTOV74C UC NOUNIPROTAC TTOV74C GN NO-GeName TTOV74C TT Discontinued TTTG60L ID TTTG60L TTTG60L TN CAP-dependent endonuclease (CDE) TTTG60L UP NO-UNIPROT TTTG60L UC NOUNIPROTAC TTTG60L GN NO-GeName TTTG60L TT Discontinued TTD9I12 ID TTD9I12 TTD9I12 TN Carbohydrate antigen 19-9 (CA 19-9) TTD9I12 UP Other Molecule TTD9I12 UC NOUNIPROTAC TTD9I12 GN NOUNIPROTAC TTD9I12 TT Clinical trial TTQR8Z6 ID TTQR8Z6 TTQR8Z6 TN Chemokine receptor (CHR) TTQR8Z6 UP Family TTQR8Z6 UC NOUNIPROTAC TTQR8Z6 GN NO-GeName TTQR8Z6 TT Discontinued TTX7ZJ3 ID TTX7ZJ3 TTX7ZJ3 TN Cocaine (Coca) TTX7ZJ3 UP Other molecule TTX7ZJ3 UC NOUNIPROTAC TTX7ZJ3 GN NOUNIPROTAC TTX7ZJ3 TT Clinical trial TT01UPE ID TT01UPE TT01UPE TN Cytomegalovirus Replication (CMV replication) TT01UPE UP Pathway/Process TT01UPE UC NOUNIPROTAC TT01UPE GN NO-GeName TT01UPE TT Discontinued TT63CB1 ID TT63CB1 TT63CB1 TN Food intake (FI) TT63CB1 UP Pathway/Process TT63CB1 UC NOUNIPROTAC TT63CB1 GN NO-GeName TT63CB1 TT Discontinued TTW7KYV ID TTW7KYV TTW7KYV TN Fucosyl GM1 (FucGM1) TTW7KYV UP Other Molecule TTW7KYV UC NOUNIPROTAC TTW7KYV GN NOUNIPROTAC TTW7KYV TT Clinical trial TT4UXTG ID TT4UXTG TT4UXTG TN Globohexaosylceramide (Globo H) TT4UXTG UP Other Molecule TT4UXTG UC NOUNIPROTAC TT4UXTG GN NOUNIPROTAC TT4UXTG TT Clinical trial TTQRL1H ID TTQRL1H TTQRL1H TN Glucosidase unspecific (GAN) TTQRL1H UP Family TTQRL1H UC NOUNIPROTAC TTQRL1H GN NO-GeName TTQRL1H TT Discontinued TTR8XOH ID TTR8XOH TTR8XOH TN GPCR secretin protein unspecific (GPCRB) TTR8XOH UP Family TTR8XOH UC NOUNIPROTAC TTR8XOH GN NO-GeName TTR8XOH TT Discontinued TTXEU7H ID TTXEU7H TTXEU7H TN GPCR unspecific (GPCR) TTXEU7H UP Family TTXEU7H UC NOUNIPROTAC TTXEU7H GN NO-GeName TTXEU7H TT Discontinued TTF1HYB ID TTF1HYB TTF1HYB TN Herpesvirus DNA polymerase (KSHV DNAP) TTF1HYB UP Family TTF1HYB UC NOUNIPROTAC TTF1HYB GN NO-GeName TTF1HYB TT Discontinued TTNRF4L ID TTNRF4L TTNRF4L TN Histone synthesis (Histone synth) TTNRF4L UP Pathway/Process TTNRF4L UC NOUNIPROTAC TTNRF4L GN NO-GeName TTNRF4L TT Discontinued TT2ISQT ID TT2ISQT TT2ISQT TN Human immunodeficiency virus Attachment (HIV att) TT2ISQT UP Pathway/Process TT2ISQT UC NOUNIPROTAC TT2ISQT GN NOUNIPROTAC TT2ISQT TT Clinical trial TTGUHMF ID TTGUHMF TTGUHMF TN Hydroxyapatite (HA) TTGUHMF UP Other molecule TTGUHMF UC NOUNIPROTAC TTGUHMF GN NOUNIPROTAC TTGUHMF TT Clinical trial TT2GVH5 ID TT2GVH5 TT2GVH5 TN Isomerase unspecific (IsoM) TT2GVH5 UP Family TT2GVH5 UC NOUNIPROTAC TT2GVH5 GN NO-GeName TT2GVH5 TT Discontinued TTZTEFH ID TTZTEFH TTZTEFH TN Major histocompatibility complex (MHC) TTZTEFH UP Family TTZTEFH UC NOUNIPROTAC TTZTEFH GN NO-GeName TTZTEFH TT Discontinued TT3UEY0 ID TT3UEY0 TT3UEY0 TN Methamphetamine (Meth) TT3UEY0 UP Other molecule TT3UEY0 UC NOUNIPROTAC TT3UEY0 GN NOUNIPROTAC TT3UEY0 TT Clinical trial TTMGJ19 ID TTMGJ19 TTMGJ19 TN microRNA hsa-miR-17 (MIR17) TTMGJ19 UP microRNA/lncRNA TTMGJ19 UC NOUNIPROTAC TTMGJ19 GN NO-GeName TTMGJ19 TT Clinical trial TTIXJ2S ID TTIXJ2S TTIXJ2S TN microRNA hsa-miR-92 (MIR92) TTIXJ2S UP microRNA/lncRNA TTIXJ2S UC NOUNIPROTAC TTIXJ2S GN NO-GeName TTIXJ2S TT Clinical trial TT1WDO0 ID TT1WDO0 TT1WDO0 TN Microtubule (MicroTu) TT1WDO0 UP Other Molecule TT1WDO0 UC NOUNIPROTAC TT1WDO0 GN NOUNIPROTAC TT1WDO0 TT Clinical trial TTU1SOM ID TTU1SOM TTU1SOM TN Microtubule polymerization (MicroTu poly) TTU1SOM UP Pathway/Process TTU1SOM UC NOUNIPROTAC TTU1SOM GN NOUNIPROTAC TTU1SOM TT Clinical trial TT8WZ3Q ID TT8WZ3Q TT8WZ3Q TN Mitochondrial gene transcription (MGT) TT8WZ3Q UP Pathway/Process TT8WZ3Q UC NOUNIPROTAC TT8WZ3Q GN NO-GeName TT8WZ3Q TT Discontinued TT5BN70 ID TT5BN70 TT5BN70 TN Nucleoside transporter (SLC) TT5BN70 UP Family TT5BN70 UC NOUNIPROTAC TT5BN70 GN NO-GeName TT5BN70 TT Discontinued TTMDQIJ ID TTMDQIJ TTMDQIJ TN Oxalate absorption (Oxalate absor) TTMDQIJ UP Pathway/Process TTMDQIJ UC NOUNIPROTAC TTMDQIJ GN NO-GeName TTMDQIJ TT Clinical trial TT8YUAD ID TT8YUAD TT8YUAD TN P450-dependent ergosterol synthesis (PDE synth) TT8YUAD UP Pathway/Process TT8YUAD UC NOUNIPROTAC TT8YUAD GN NO-GeName TT8YUAD TT Discontinued TTO32GK ID TTO32GK TTO32GK TN P-glycoprotein (P-GP) TTO32GK UP Family TTO32GK UC NOUNIPROTAC TTO32GK GN NO-GeName TTO32GK TT Discontinued TTW1KTD ID TTW1KTD TTW1KTD TN Phosphoric monoester hydrolase (PMH) TTW1KTD UP Family TTW1KTD UC NOUNIPROTAC TTW1KTD GN NO-GeName TTW1KTD TT Discontinued TTJR4Z5 ID TTJR4Z5 TTJR4Z5 TN Polyamine transport (Poly trans) TTJR4Z5 UP Pathway/Process TTJR4Z5 UC NOUNIPROTAC TTJR4Z5 GN NOUNIPROTAC TTJR4Z5 TT Clinical trial TTORYTW ID TTORYTW TTORYTW TN Polymerase unspecific (POL) TTORYTW UP Family TTORYTW UC NOUNIPROTAC TTORYTW GN NO-GeName TTORYTW TT Discontinued TTJAY96 ID TTJAY96 TTJAY96 TN Polymorphonuclear neutrophil adhesion (PMNA) TTJAY96 UP Pathway/Process TTJAY96 UC NOUNIPROTAC TTJAY96 GN NO-GeName TTJAY96 TT Discontinued TTNSUK0 ID TTNSUK0 TTNSUK0 TN Protein thiol group (PTG) TTNSUK0 UP NO-UNIPROT TTNSUK0 UC NOUNIPROTAC TTNSUK0 GN NO-GeName TTNSUK0 TT Discontinued TTZUFEL ID TTZUFEL TTZUFEL TN Tumor-associated glycan antigen (TAGA) TTZUFEL UP Other Molecule TTZUFEL UC NOUNIPROTAC TTZUFEL GN NOUNIPROTAC TTZUFEL TT Clinical trial TT2QM9D ID TT2QM9D TT2QM9D TN Adenylate cyclase (ADCY) TT2QM9D UP Family TT2QM9D UC NOUNIPROTAC TT2QM9D BC Phosphorus-oxygen lyase TT2QM9D SN Adenylyl cyclase; ATP pyrophosphate-lyase TT2QM9D GN NO-GeName TT2QM9D FC Catalyzes the formation of the second messenger cAMP from ATP. Its transcript is probably degraded by endoribonuclease LS (rnlA), decreasing cAMP levels and the negative regulator Crp- cAMP, which then induces its own transcription again. TT2QM9D TT Literature-reported TTAVH2G ID TTAVH2G TTAVH2G TN Cytochrome P450 2B2 (CYP2B2) TTAVH2G UP NO-UNIPROT TTAVH2G UC NOUNIPROTAC TTAVH2G BC Paired donor oxygen oxidoreductase TTAVH2G SN Cytochrome P450E; Cytochrome P450 PB4; Cyp2b2; Cyp2b-2; CYPIIB2 TTAVH2G GN NO-GeName TTAVH2G FC Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. TTAVH2G TT Literature-reported TTWOCZI ID TTWOCZI TTWOCZI TN Cation channel sperm-associated protein (CatSper) TTWOCZI UP Family TTWOCZI UC NOUNIPROTAC TTWOCZI SN Chemokine (C-C motif) receptor TTWOCZI GN NO-GeName TTWOCZI FC Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte. Activated by extracellular progesterone and prostaglandins following the sequence: progesterone > PGF1-alpha = PGE1 > PGA1 > PGE2 >> PGD2. The primary effect of progesterone activation is to shift voltage dependence towards more physiological, negative membrane potentials; it is not mediated by metabotropic receptors and second messengers. Sperm capacitation enhances the effect of progesterone by providing additional negative shift. Also activated by the elevation of intracellular pH. TTWOCZI TT Literature-reported TT8KLPT ID TT8KLPT TT8KLPT TN C-C chemokine receptor (CCR) TT8KLPT UP Family TT8KLPT UC NOUNIPROTAC TT8KLPT SN Chemokine (C-C motif) receptor TT8KLPT GN NO-GeName TT8KLPT FC Receptor for a C-C type chemokine. Binds to MIP-1-alpha, MIP-1-delta, RANTES, and MCP-3 and, less efficiently, to MIP-1- beta or MCP-1 and subsequently transduces a signal by increasing the intracellular calcium ions level. Responsible for affecting stem cell proliferation. TT8KLPT TT Literature-reported TT8KLPT KE hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway TT8KLPT RC R-HSA-1461957:Beta defensins; R-HSA-173107:Binding and entry of HIV virion; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events TTC50YZ ID TTC50YZ TTC50YZ TN Inflammatory cytokine messenger RNA (Cytokine mRNA) TTC50YZ UP Family TTC50YZ UC NOUNIPROTAC TTC50YZ BC mRNA target TTC50YZ SN mRNA of Inflammatory cytokine TTC50YZ GN NO-GeName TTC50YZ TT Literature-reported TTQW170 ID TTQW170 TTQW170 TN Phospholipase D (PLD) TTQW170 UP Family TTQW170 UC NOUNIPROTAC TTQW170 BC Phosphoric diester hydrolase TTQW170 SN PLD-A; PLD; Choline phosphatase TTQW170 GN NO-GeName TTQW170 TT Literature-reported TTX7HPM ID TTX7HPM TTX7HPM TN Prolyl hydroxylase (PH) TTX7HPM UP Family TTX7HPM UC NOUNIPROTAC TTX7HPM BC Paired donor oxygen oxidoreductase TTX7HPM SN Procollagen-proline,2-oxoglutarate-4-dioxygenase alpha; 4-PH alpha TTX7HPM GN NO-GeName TTX7HPM TT Literature-reported TTZ13BD ID TTZ13BD TTZ13BD TN Anandamide amidase (ANA) TTZ13BD UP Family TTZ13BD UC NOUNIPROTAC TTZ13BD BC Carbon-nitrogen hydrolase TTZ13BD SN Arachidonylethanolamide synthase; Anandamide synthase TTZ13BD GN NO-GeName TTZ13BD TT Literature-reported TTG712R ID TTG712R TTG712R TN Calprotectin (CP) TTG712R UP Family TTG712R UC NOUNIPROTAC TTG712R SN S100A9/S100A8; MRP8/MRP14 complex; MRP-8/MRP-14; Leucocyte protein L1; L1 protein; L1 antigen; Cytosolic protein complex L1 TTG712R GN NO-GeName TTG712R FC Expressed by macrophages in chronic inflammations. Also expressed in epithelial cells constitutively or induced during dermatoses. May interact with components of the intermediate filaments in monocytes and epithelial cells. TTG712R TT Literature-reported TTQ1DP3 ID TTQ1DP3 TTQ1DP3 TN CoA-independent transacylase (CIT) TTQ1DP3 UP NO-UNIPROT TTQ1DP3 UC NOUNIPROTAC TTQ1DP3 BC Acyltransferase TTQ1DP3 SN Glycerophospholipid arachidonoyl-transferase(CoA-independent); Coenzyme A-independent transacylase; CoA-IT; 1-alkylglycerophosphocholine Acyltransferase TTQ1DP3 GN NO-GeName TTQ1DP3 TT Literature-reported TTOCKIN ID TTOCKIN TTOCKIN TN Homocitrate synthase (HCS) TTOCKIN UP Family TTOCKIN UC NOUNIPROTAC TTOCKIN BC Acyltransferase TTOCKIN SN Homocitrate synthetase; Acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase; 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating) TTOCKIN GN NO-GeName TTOCKIN TT Literature-reported TTH754E ID TTH754E TTH754E TN Lentivirus messenger RNA (Lentivirus mRNA) TTH754E UP Family TTH754E UC NOUNIPROTAC TTH754E BC mRNA target TTH754E SN mRNA of Lentivirus TTH754E GN NO-GeName TTH754E TT Literature-reported TTU593I ID TTU593I TTU593I TN Neurokinin receptor (NKR) TTU593I UP Family TTU593I UC NOUNIPROTAC TTU593I GN NO-GeName TTU593I FC This is a receptor for the tachykinin neuropeptide substance P. It is probably associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance P > substance K > neuromedin-K. TTU593I TT Literature-reported TTU593I KE hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa05162:Measles TTQD1SA ID TTQD1SA TTQD1SA TN P2Y purinoceptor (P2RY) TTQD1SA UP Family TTQD1SA UC NOUNIPROTAC TTQD1SA BC GPCR rhodopsin TTQD1SA SN Platelet adenosine diphosphatereceptor; P2Y receptor; Adenosine diphosphate (ADP) receptor; Adenosine 5'-Diphosphate Receptor; ADP receptor TTQD1SA GN NO-GeName TTQD1SA TT Literature-reported TTUZ196 ID TTUZ196 TTUZ196 TN Phosphodiesterase 5 (PDE5) TTUZ196 UP Family TTUZ196 UC NOUNIPROTAC TTUZ196 BC Phosphoric diester hydrolase TTUZ196 SN Phosphosdiesterase-5; PDE5; PDE-V; PDE-5 TTUZ196 GN NO-GeName TTUZ196 TT Literature-reported TTSXP1G ID TTSXP1G TTSXP1G TN Protein kinase A alpha messenger RNA (PKA-alpha mRNA) TTSXP1G UP Family TTSXP1G UC NOUNIPROTAC TTSXP1G BC mRNA target TTSXP1G SN mRNA of PKA alpha TTSXP1G GN NO-GeName TTSXP1G TT Literature-reported TTXQFV2 ID TTXQFV2 TTXQFV2 TN Protein kinase A Ri alpha messenger RNA (PKA-Ri-alpha mRNA) TTXQFV2 UP Family TTXQFV2 UC NOUNIPROTAC TTXQFV2 BC mRNA target TTXQFV2 SN mRNA of PKA Ri alpha TTXQFV2 GN NO-GeName TTXQFV2 TT Literature-reported TTMQ2WK ID TTMQ2WK TTMQ2WK TN Protein kinase A1 messenger RNA (PKA mRNA) TTMQ2WK UP Family TTMQ2WK UC NOUNIPROTAC TTMQ2WK BC mRNA target TTMQ2WK SN mRNA of PKA TTMQ2WK GN NO-GeName TTMQ2WK TT Literature-reported TTZALHD ID TTZALHD TTZALHD TN Protein kinase C messenger RNA (PKC mRNA) TTZALHD UP Family TTZALHD UC NOUNIPROTAC TTZALHD BC mRNA target TTZALHD SN mRNA of PKC TTZALHD GN NO-GeName TTZALHD TT Literature-reported TT70SZ3 ID TT70SZ3 TT70SZ3 TN Sodium/hydrogen exchanger (SLC) TT70SZ3 UP Family TT70SZ3 UC NOUNIPROTAC TT70SZ3 GN NO-GeName TT70SZ3 FC Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. TT70SZ3 TT Literature-reported TT70SZ3 KE hsa04024:cAMP signaling pathway; hsa04260:Cardiac muscle contraction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04810:Regulation of actin cytoskeleton; hsa04919:Thyroid hormone signaling pathway; hsa04970:Salivary secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04976:Bile secretion; hsa05205:Proteoglycans in cancer TTPZI04 ID TTPZI04 TTPZI04 TN Voltage-dependent anion channel (VDAC) TTPZI04 UP Family TTPZI04 UC NOUNIPROTAC TTPZI04 BC Eukaryotic mitochondrial porin TTPZI04 GN NO-GeName TTPZI04 FC Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. TTPZI04 TT Clinical trial TTYOMFZ ID TTYOMFZ TTYOMFZ TN Voltage-gated potassium channel (VGKC) TTYOMFZ UP Family TTYOMFZ UC NOUNIPROTAC TTYOMFZ BC Voltage-gated ion channel TTYOMFZ GN NO-GeName TTYOMFZ TT Literature-reported TTQJBF8 ID TTQJBF8 TTQJBF8 TN Acid-sensing ion channel (ASIC) TTQJBF8 UP Family TTQJBF8 UC NOUNIPROTAC TTQJBF8 BC Amiloride-sensitive sodium channel TTQJBF8 GN NO-GeName TTQJBF8 TT Literature-reported TTANY71 ID TTANY71 TTANY71 TN AdoHcy hydrolase (SAHase) TTANY71 UP Family TTANY71 UC NOUNIPROTAC TTANY71 SN AdoHcyase TTANY71 GN NO-GeName TTANY71 TT Literature-reported TTW4DUY ID TTW4DUY TTW4DUY TN Beta-lactoglobulin 1 (BetaL1) TTW4DUY UP Family TTW4DUY UC NOUNIPROTAC TTW4DUY GN NO-GeName TTW4DUY FC Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. TTW4DUY TT Literature-reported TTZSDKE ID TTZSDKE TTZSDKE TN Carcinogenesis (Tumorigenesis) TTZSDKE UP Pathway/Process TTZSDKE UC NOUNIPROTAC TTZSDKE SN Biogenesis of tumor TTZSDKE GN NO-GeName TTZSDKE TT Literature-reported TTLYHN8 ID TTLYHN8 TTLYHN8 TN CXCL5/CXCR2 axis (CXCL5/CXCR2 axis) TTLYHN8 UP Pathway/Process TTLYHN8 UC NOUNIPROTAC TTLYHN8 SN C-X-C motif chemokine 5/C-X-C motif chemokine receptor 2 axis TTLYHN8 GN NO-GeName TTLYHN8 TT Literature-reported TT14TBN ID TT14TBN TT14TBN TN Cyclin E/cdk2 pathway (CCNE2/CDK2 pathway) TT14TBN UP Pathway/Process TT14TBN UC NOUNIPROTAC TT14TBN SN Cyclin E/CDK2 pathway signalling TT14TBN GN NO-GeName TT14TBN TT Literature-reported TT7FTES ID TT7FTES TT7FTES TN Endothelium-derived hyperpolarizing factor (EDHF) TT7FTES UP NO-UNIPROT TT7FTES UC NOUNIPROTAC TT7FTES SN EDHF TT7FTES GN NO-GeName TT7FTES TT Literature-reported TTL86IU ID TTL86IU TTL86IU TN Estrogen-related receptor (ESRR) TTL86IU UP Family TTL86IU UC NOUNIPROTAC TTL86IU GN NO-GeName TTL86IU FC Binds to an ERR-alpha response element (ERRE) containinga single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism. Induces theexpression of PERM1 in the skeletal muscle. TTL86IU TT Literature-reported TT5JCZL ID TT5JCZL TT5JCZL TN GDNF receptor complexes (GDNFR) TT5JCZL UP Family TT5JCZL UC NOUNIPROTAC TT5JCZL GN NO-GeName TT5JCZL FC Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor. TT5JCZL TT Literature-reported TTQ5XI3 ID TTQ5XI3 TTQ5XI3 TN Glycoprotein Ib-IX-V receptor (GPIbIXV) TTQ5XI3 UP NO-UNIPROT TTQ5XI3 UC NOUNIPROTAC TTQ5XI3 SN Glycoprotein Ib-IX-V; Glycoprotein (GP) Ib-IX-V; GP Ib-IX-V TTQ5XI3 GN NO-GeName TTQ5XI3 TT Literature-reported TTQFP08 ID TTQFP08 TTQFP08 TN Integrin (ITG) TTQFP08 UP Family TTQFP08 UC NOUNIPROTAC TTQFP08 SN Integrin protein TTQFP08 GN NO-GeName TTQFP08 TT Clinical trial TTV57E8 ID TTV57E8 TTV57E8 TN Interleukin receptor (ILR) TTV57E8 UP Family TTV57E8 UC NOUNIPROTAC TTV57E8 SN Interleukin receptor TTV57E8 GN NO-GeName TTV57E8 TT Literature-reported TTE8XGQ ID TTE8XGQ TTE8XGQ TN Large subunit Cp complex Cdc68p (CDC68) TTE8XGQ UP Family TTE8XGQ UC NOUNIPROTAC TTE8XGQ SN Cdc68p; CDC68 TTE8XGQ GN NO-GeName TTE8XGQ TT Literature-reported TTMPGNS ID TTMPGNS TTMPGNS TN Leukotriene biosynthesis (LT synth) TTMPGNS UP Pathway/Process TTMPGNS UC NOUNIPROTAC TTMPGNS SN Leukotriene synthesis TTMPGNS GN NO-GeName TTMPGNS TT Literature-reported TTGFDOM ID TTGFDOM TTGFDOM TN Leukotriene E4 receptor (LTE4R) TTGFDOM UP NO-UNIPROT TTGFDOM UC NOUNIPROTAC TTGFDOM SN LTE4 receptor TTGFDOM GN NO-GeName TTGFDOM TT Literature-reported TTTM6W8 ID TTTM6W8 TTTM6W8 TN Melanin-concentrating hormone receptor (MCHR) TTTM6W8 UP Family TTTM6W8 UC NOUNIPROTAC TTTM6W8 SN MCH receptor TTTM6W8 GN NO-GeName TTTM6W8 TT Literature-reported TTCZO0Q ID TTCZO0Q TTCZO0Q TN Mitogen-activated protein kinase kinase (MAPKK) TTCZO0Q UP Family TTCZO0Q UC NOUNIPROTAC TTCZO0Q BC Kinase TTCZO0Q GN NO-GeName TTCZO0Q TT Literature-reported TTJXYQ6 ID TTJXYQ6 TTJXYQ6 TN Monoamine uptake (MA uptake) TTJXYQ6 UP Pathway/Process TTJXYQ6 UC NOUNIPROTAC TTJXYQ6 SN Monoamine(MA) uptake TTJXYQ6 GN NO-GeName TTJXYQ6 TT Literature-reported TTYHBSN ID TTYHBSN TTYHBSN TN Nerve/glial antigen-2 (NG2) TTYHBSN UP NO-UNIPROT TTYHBSN UC NOUNIPROTAC TTYHBSN SN Tubulin protein TTYHBSN GN NO-GeName TTYHBSN TT Literature-reported TTT1MCF ID TTT1MCF TTT1MCF TN Permeability pathway (NP pathway) TTT1MCF UP Pathway/Process TTT1MCF UC NOUNIPROTAC TTT1MCF SN NPPs TTT1MCF GN NO-GeName TTT1MCF TT Literature-reported TT5TFXR ID TT5TFXR TT5TFXR TN Relaxin receptor (RXFP) TT5TFXR UP Family TT5TFXR UC NOUNIPROTAC TT5TFXR GN NO-GeName TT5TFXR FC Receptor for relaxins. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. Binding of the ligand may also activate a tyrosine kinase pathway that inhibits the activity of a phosphodiesterase that degrades cAMP. TT5TFXR TT Literature-reported TTC3JYS ID TTC3JYS TTC3JYS TN TNF alpha synthesis (TNFA synthesis) TTC3JYS UP Pathway/Process TTC3JYS UC NOUNIPROTAC TTC3JYS SN Tumor necrosis factor alpha synthesis TTC3JYS GN NO-GeName TTC3JYS TT Literature-reported TTVBH9I ID TTVBH9I TTVBH9I TN TNF receptor-associated factor (TRAF) TTVBH9I UP Family TTVBH9I UC NOUNIPROTAC TTVBH9I SN TRAF; TNF-receptor-associated factor TTVBH9I GN NO-GeName TTVBH9I TT Literature-reported TTKURIS ID TTKURIS TTKURIS TN Tumor suppressor candidate (TUSC) TTKURIS UP Family TTKURIS UC NOUNIPROTAC TTKURIS SN Candidate tumor suppressor protein TTKURIS GN NO-GeName TTKURIS TT Literature-reported TTH7Z83 ID TTH7Z83 TTH7Z83 TN Tumor-associated carbohydrate antigen KH-1 (KH-1) TTH7Z83 UP NO-UNIPROT TTH7Z83 UC NOUNIPROTAC TTH7Z83 SN Antigen KH-1 TTH7Z83 GN NO-GeName TTH7Z83 TT Literature-reported TTMYPOH ID TTMYPOH TTMYPOH TN Tumor-associated peptide (TAP) TTMYPOH UP Family TTMYPOH UC NOUNIPROTAC TTMYPOH SN Tumor associated peptide TTMYPOH GN NO-GeName TTMYPOH TT Literature-reported TT0DWYQ ID TT0DWYQ TT0DWYQ TN Tumour metastasis (Tmet) TT0DWYQ UP Pathway/Process TT0DWYQ UC NOUNIPROTAC TT0DWYQ SN Metastasis; Cancer metastasis TT0DWYQ GN NO-GeName TT0DWYQ TT Literature-reported TT0JUOH ID TT0JUOH TT0JUOH TN Voltage-gated potassium channel Kv1 (KCNA) TT0JUOH UP Family TT0JUOH UC NOUNIPROTAC TT0JUOH BC Voltage-gated ion channel TT0JUOH GN NO-GeName TT0JUOH TT Literature-reported TT0FC1V ID TT0FC1V TT0FC1V TN Volume regulated chloride channel (VRAC) TT0FC1V UP Family TT0FC1V UC NOUNIPROTAC TT0FC1V BC Chloride channel TT0FC1V GN NO-GeName TT0FC1V TT Literature-reported TTM2AGN ID TTM2AGN TTM2AGN TN 3-oxo-dodecanoyl-homoserine lactone (C12) TTM2AGN UP Other molecule TTM2AGN UC NOUNIPROTAC TTM2AGN GN NOUNIPROTAC TTM2AGN TT Preclinical TTWYIT3 ID TTWYIT3 TTWYIT3 TN Acetaminophen binding protein 58kDa (ABP58) TTWYIT3 UP NO-UNIPROT TTWYIT3 UC NOUNIPROTAC TTWYIT3 GN NO-GeName TTWYIT3 TT Literature-reported TTB094Z ID TTB094Z TTB094Z TN Adrenomedullin receptor (AMR) TTB094Z UP Family TTB094Z UC NOUNIPROTAC TTB094Z GN NO-GeName TTB094Z TT Literature-reported TTNDGAR ID TTNDGAR TTNDGAR TN Advanced glycation end-product pathway (AGE pathway) TTNDGAR UP Pathway/Process TTNDGAR UC NOUNIPROTAC TTNDGAR GN NO-GeName TTNDGAR TT Literature-reported TTTB3L1 ID TTTB3L1 TTTB3L1 TN Alpha-crystallin (CRYA) TTTB3L1 UP Family TTTB3L1 UC NOUNIPROTAC TTTB3L1 GN NO-GeName TTTB3L1 TT Preclinical TTBH0LA ID TTBH0LA TTBH0LA TN Alpha-secretase (ASE) TTBH0LA UP Family TTBH0LA UC NOUNIPROTAC TTBH0LA GN NO-GeName TTBH0LA TT Literature-reported TTZWSN5 ID TTZWSN5 TTZWSN5 TN Amyloid precursor protein (APP) TTZWSN5 UP Family TTZWSN5 UC NOUNIPROTAC TTZWSN5 GN NO-GeName TTZWSN5 TT Literature-reported TTVXDU9 ID TTVXDU9 TTVXDU9 TN Anaphase-promoting complex (APC/C) TTVXDU9 UP Family TTVXDU9 UC NOUNIPROTAC TTVXDU9 GN NO-GeName TTVXDU9 TT Literature-reported TTPHW9Y ID TTPHW9Y TTPHW9Y TN Ascaris NADH-fumarate reductase (Asc OSM) TTPHW9Y UP NO-UNIPROT TTPHW9Y UC NOUNIPROTAC TTPHW9Y GN NO-GeName TTPHW9Y TT Literature-reported TTD0CAZ ID TTD0CAZ TTD0CAZ TN Aspartic protease (ASPP) TTD0CAZ UP Family TTD0CAZ UC NOUNIPROTAC TTD0CAZ GN NO-GeName TTD0CAZ TT Literature-reported TTX1KNQ ID TTX1KNQ TTX1KNQ TN ATP synthase (ATPS) TTX1KNQ UP Family TTX1KNQ UC NOUNIPROTAC TTX1KNQ GN NO-GeName TTX1KNQ TT Literature-reported TT92RXQ ID TT92RXQ TT92RXQ TN ATP-sensitive potassium channel (KATP channel) TT92RXQ UP Family TT92RXQ UC NOUNIPROTAC TT92RXQ GN NO-GeName TT92RXQ TT Literature-reported TTYIJX1 ID TTYIJX1 TTYIJX1 TN Autophagy (AUT) TTYIJX1 UP Pathway/Process TTYIJX1 UC NOUNIPROTAC TTYIJX1 GN NO-GeName TTYIJX1 TT Literature-reported TTD3BVN ID TTD3BVN TTD3BVN TN Axon loss (AXL) TTD3BVN UP Pathway/Process TTD3BVN UC NOUNIPROTAC TTD3BVN GN NO-GeName TTD3BVN TT Literature-reported TTM0O8B ID TTM0O8B TTM0O8B TN Bacillus poly-gamma-d-glutamic acid (Bacillus PGA) TTM0O8B UP Other molecule TTM0O8B UC NOUNIPROTAC TTM0O8B GN NOUNIPROTAC TTM0O8B TT Preclinical TT1EAC9 ID TT1EAC9 TT1EAC9 TN Bacterial ATP synthase (Bact atps) TT1EAC9 UP Family TT1EAC9 UC NOUNIPROTAC TT1EAC9 GN NO-GeName TT1EAC9 TT Literature-reported TTQALFH ID TTQALFH TTQALFH TN Bacterial Beta-glucuronidase (Bact uidA) TTQALFH UP P05804 TTQALFH UC BGLR_ECOLI TTQALFH SN GUS; Beta-D-glucuronoside glucuronosohydrolase TTQALFH GN Bact uidA TTQALFH FC cytosol, protein-containing complex, beta-glucuronidase activity, carbohydrate binding, identical protein binding, glucuronoside catabolic process TTQALFH EC EC 3.2.1.31 TTQALFH SQ MLRPVETPTREIKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADIRNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTPYVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTPNTWVDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPHLWQPGEGYLYELCVTAKSQTECDIYPLRVGIRSVAVKGEQFLINHKPFYFTGFGRHEDADLRGKGFDNVLMVHDHALMDWIGANSYRTSHYPYAEEMLDWADEHGIVVIDETAAVGFNLSLGIGFEAGNKPKELYSEEAVNGETQQAHLQAIKELIARDKNHPSVVMWSIANEPDTRPQGAREYFAPLAEATRKLDPTRPITCVNVMFCDAHTDTISDLFDVLCLNRYYGWYVQSGDLETAEKVLEKELLAWQEKLHQPIIITEYGVDTLAGLHSMYTDMWSEEYQCAWLDMYHRVFDRVSAVVGEQVWNFADFATSQGILRVGGNKKGIFTRDRKPKSAAFLLQKRWTGMNFGEKPQQGGKQ TTQALFH TT Preclinical TT0AD7X ID TT0AD7X TT0AD7X TN Bacterial Quorum sensing (Bact BQS) TT0AD7X UP Pathway/Process TT0AD7X UC NOUNIPROTAC TT0AD7X GN NO-GeName TT0AD7X TT Literature-reported TTGWSKE ID TTGWSKE TTGWSKE TN Bacterial Transpeptidase (Bact TPP) TTGWSKE UP Family TTGWSKE UC NOUNIPROTAC TTGWSKE GN NO-GeName TTGWSKE TT Literature-reported TTNLDC4 ID TTNLDC4 TTNLDC4 TN Bilophila glycyl radical enzyme (GRE) TTNLDC4 UP Family TTNLDC4 UC NOUNIPROTAC TTNLDC4 GN NO-GeName TTNLDC4 TT Literature-reported TTJ6ESR ID TTJ6ESR TTJ6ESR TN Catecholamine uptake (CA uptake) TTJ6ESR UP Pathway/Process TTJ6ESR UC NOUNIPROTAC TTJ6ESR GN NO-GeName TTJ6ESR TT Literature-reported TTKA1M6 ID TTKA1M6 TTKA1M6 TN Catenin (CTNN) TTKA1M6 UP Family TTKA1M6 UC NOUNIPROTAC TTKA1M6 GN NO-GeName TTKA1M6 TT Literature-reported TTKAPQ1 ID TTKAPQ1 TTKAPQ1 TN Cholecystokinin receptor (CCKR) TTKAPQ1 UP Family TTKAPQ1 UC NOUNIPROTAC TTKAPQ1 GN NO-GeName TTKAPQ1 TT Literature-reported TTSXM8W ID TTSXM8W TTSXM8W TN Corticosteroid receptor (CCR) TTSXM8W UP Family TTSXM8W UC NOUNIPROTAC TTSXM8W GN NO-GeName TTSXM8W TT Literature-reported TTA6KF7 ID TTA6KF7 TTA6KF7 TN C-X-C chemokine receptor (CXCR) TTA6KF7 UP Family TTA6KF7 UC NOUNIPROTAC TTA6KF7 GN NO-GeName TTA6KF7 TT Literature-reported TTH6N8T ID TTH6N8T TTH6N8T TN Cytochrome P450 3 (CYP3) TTH6N8T UP Family TTH6N8T UC NOUNIPROTAC TTH6N8T GN NO-GeName TTH6N8T TT Literature-reported TTXRADL ID TTXRADL TTXRADL TN Death associated protein kinase (DAPK) TTXRADL UP Family TTXRADL UC NOUNIPROTAC TTXRADL GN NO-GeName TTXRADL TT Literature-reported TTR1XF8 ID TTR1XF8 TTR1XF8 TN Deoxyribonuclease (DNASE) TTR1XF8 UP Family TTR1XF8 UC NOUNIPROTAC TTR1XF8 GN NO-GeName TTR1XF8 TT Literature-reported TTTLEHG ID TTTLEHG TTTLEHG TN DNA methyltransferase (DNMT) TTTLEHG UP Family TTTLEHG UC NOUNIPROTAC TTTLEHG GN NO-GeName TTTLEHG TT Literature-reported TTRBPLN ID TTRBPLN TTRBPLN TN DNA-binding protein inhibitor (ID) TTRBPLN UP Family TTRBPLN UC NOUNIPROTAC TTRBPLN GN NO-GeName TTRBPLN TT Literature-reported TTXKQIV ID TTXKQIV TTXKQIV TN Energy metabolism (Energy metab) TTXKQIV UP Pathway/Process TTXKQIV UC NOUNIPROTAC TTXKQIV GN NO-GeName TTXKQIV TT Literature-reported TTZXI0P ID TTZXI0P TTZXI0P TN Enterococcus fsrC (Ente-cocc fsrC) TTZXI0P UP C3VD18 TTZXI0P UC C3VD18_ENTFC TTZXI0P GN Ente-cocc fsrC TTZXI0P SQ MILSLLATNVLLVSSFIVFVFLRVTLIKIECKIPLLSLLIVINLCSFAALMLGYSWLIYALTVVVFTGFLLIHKKRFSIFKAIFLSVFTLLMVSFINYTEQTILSVFFQQIYQNKLLWIASNVLLLLINIWIALKIPNSVFLRLNRVLENSRIFFGCLLLLLILLLLFVFLISPEISPDFMRGFVTVNSSKLELLISVGLFLILIGLVIEAYLEEQRINTQLLNNLTIYTEKIESINEELAMFRHDYKNLLYSLQIAISYEDILEIKRIYEETIAPTKKIIDNEEFELMKLNRLKNMELKALISMKINTAKQAKLKVIVDVPEVFILDTSIDLVVVIRLLAILLDNAIENSAKSELKMFAISIFNKNETQEFVITNSVQAEFDFKVMKKTKFSSKSNPEEHGWGLLYVKEIVDFSDQFDLQTSFNEGAVTQHLIIEKNHNSKKVVNE TTZXI0P TT Preclinical TTF1HJC ID TTF1HJC TTF1HJC TN Ergosterol synthesis (EG synth) TTF1HJC UP Pathway/Process TTF1HJC UC NOUNIPROTAC TTF1HJC GN NO-GeName TTF1HJC TT Literature-reported TTVC5K6 ID TTVC5K6 TTVC5K6 TN Estradiol 17 beta-dehydrogenase (17-beta-HSD) TTVC5K6 UP Family TTVC5K6 UC NOUNIPROTAC TTVC5K6 GN NO-GeName TTVC5K6 TT Literature-reported TTBFHXC ID TTBFHXC TTBFHXC TN Feto-acinar pancreatic protein (FAPP) TTBFHXC UP NO-UNIPROT TTBFHXC UC NOUNIPROTAC TTBFHXC GN NO-GeName TTBFHXC TT Literature-reported TT7GJ9D ID TT7GJ9D TT7GJ9D TN Glutamate release (GLU rele) TT7GJ9D UP Pathway/Process TT7GJ9D UC NOUNIPROTAC TT7GJ9D GN NO-GeName TT7GJ9D TT Literature-reported TTZH7FT ID TTZH7FT TTZH7FT TN Gluten (GLEN) TTZH7FT UP Family TTZH7FT UC NOUNIPROTAC TTZH7FT GN NO-GeName TTZH7FT TT Literature-reported TTSI7BV ID TTSI7BV TTSI7BV TN Glycolysis (GLYS) TTSI7BV UP Pathway/Process TTSI7BV UC NOUNIPROTAC TTSI7BV GN NO-GeName TTSI7BV TT Literature-reported TTZ7HX8 ID TTZ7HX8 TTZ7HX8 TN Glycoside hydrolase (GlyH) TTZ7HX8 UP Family TTZ7HX8 UC NOUNIPROTAC TTZ7HX8 GN NO-GeName TTZ7HX8 TT Literature-reported TTSBIMH ID TTSBIMH TTSBIMH TN GPCR frizzled protein unspecific (GPCRF) TTSBIMH UP Family TTSBIMH UC NOUNIPROTAC TTSBIMH GN NO-GeName TTSBIMH TT Literature-reported TT60D9N ID TT60D9N TT60D9N TN GPCR rhodopsin protein unspecific (GPCRA) TT60D9N UP Family TT60D9N UC NOUNIPROTAC TT60D9N GN NO-GeName TT60D9N TT Literature-reported TT2QROC ID TT2QROC TT2QROC TN Guanosine phosphotransferase (GPTase) TT2QROC UP Family TT2QROC UC NOUNIPROTAC TT2QROC GN NO-GeName TT2QROC TT Literature-reported TTBA9I1 ID TTBA9I1 TTBA9I1 TN Hematopoietic protein-tyrosine phosphatase (PTPN) TTBA9I1 UP Family TTBA9I1 UC NOUNIPROTAC TTBA9I1 GN NO-GeName TTBA9I1 TT Literature-reported TTYNBIE ID TTYNBIE TTYNBIE TN Hepatic oligosaccharide/glycolipid storage (HOGS) TTYNBIE UP Pathway/Process TTYNBIE UC NOUNIPROTAC TTYNBIE GN NO-GeName TTYNBIE TT Literature-reported TTXAKVF ID TTXAKVF TTXAKVF TN Hepatitis C virus Envelope glycoprotein (HCV Env) TTXAKVF UP Family TTXAKVF UC NOUNIPROTAC TTXAKVF GN NO-GeName TTXAKVF TT Literature-reported TTS3GIJ ID TTS3GIJ TTS3GIJ TN Heterotrimeric G-protein signaling pathway (HGP pathway) TTS3GIJ UP Pathway/Process TTS3GIJ UC NOUNIPROTAC TTS3GIJ GN NO-GeName TTS3GIJ TT Literature-reported TTR3ZY2 ID TTR3ZY2 TTR3ZY2 TN Human immunodeficiency virus Cell fusion (HIV CF) TTR3ZY2 UP Pathway/Process TTR3ZY2 UC NOUNIPROTAC TTR3ZY2 GN NO-GeName TTR3ZY2 TT Literature-reported TTWH7FA ID TTWH7FA TTWH7FA TN Hydroxylase (HYL) TTWH7FA UP Family TTWH7FA UC NOUNIPROTAC TTWH7FA GN NO-GeName TTWH7FA TT Literature-reported TTEI6SF ID TTEI6SF TTEI6SF TN IKB-beta-NFKB signaling pathway (IKBB-NFKB pathway) TTEI6SF UP Pathway/Process TTEI6SF UC NOUNIPROTAC TTEI6SF GN NO-GeName TTEI6SF TT Literature-reported TTR6P2Z ID TTR6P2Z TTR6P2Z TN Imidazoline I2 receptor (I2R) TTR6P2Z UP NO-UNIPROT TTR6P2Z UC NOUNIPROTAC TTR6P2Z GN NO-GeName TTR6P2Z TT Literature-reported TT0YOTH ID TT0YOTH TT0YOTH TN Immunoglobulin gamma Fc receptor (FCGR) TT0YOTH UP Family TT0YOTH UC NOUNIPROTAC TT0YOTH GN NO-GeName TT0YOTH TT Literature-reported TT5WF6D ID TT5WF6D TT5WF6D TN Inflammatory cytokine (IC) TT5WF6D UP Family TT5WF6D UC NOUNIPROTAC TT5WF6D GN NO-GeName TT5WF6D TT Literature-reported TT15T2Q ID TT15T2Q TT15T2Q TN Inflammatory mediator release (IM rele) TT15T2Q UP Pathway/Process TT15T2Q UC NOUNIPROTAC TT15T2Q GN NO-GeName TT15T2Q TT Literature-reported TTDLJ0S ID TTDLJ0S TTDLJ0S TN Interleukin-12 signaling pathway (IL12 pathway) TTDLJ0S UP Pathway/Process TTDLJ0S UC NOUNIPROTAC TTDLJ0S GN NO-GeName TTDLJ0S TT Literature-reported TTDEGJQ ID TTDEGJQ TTDEGJQ TN Ligand-gated ion channel (LGIC) TTDEGJQ UP Family TTDEGJQ UC NOUNIPROTAC TTDEGJQ GN NO-GeName TTDEGJQ TT Literature-reported TTE6DMK ID TTE6DMK TTE6DMK TN Ligand-nuclear hormone receptor interaction (LNHRI) TTE6DMK UP Pathway/Process TTE6DMK UC NOUNIPROTAC TTE6DMK GN NO-GeName TTE6DMK TT Literature-reported TT62Q7D ID TT62Q7D TT62Q7D TN LPS-miR-34a-CCL22 axis (LmCa) TT62Q7D UP Pathway/Process TT62Q7D UC NOUNIPROTAC TT62Q7D GN NO-GeName TT62Q7D TT Literature-reported TTZC3G5 ID TTZC3G5 TTZC3G5 TN Lysine-specific histone demethylase (LSD) TTZC3G5 UP Family TTZC3G5 UC NOUNIPROTAC TTZC3G5 GN NO-GeName TTZC3G5 TT Literature-reported TTUPO71 ID TTUPO71 TTUPO71 TN Mast cell degranulation pathway (MCD pathway) TTUPO71 UP Pathway/Process TTUPO71 UC NOUNIPROTAC TTUPO71 GN NO-GeName TTUPO71 TT Literature-reported TTFNSPC ID TTFNSPC TTFNSPC TN Mechanistic target of rapamycin complex 3 (mTORC3) TTFNSPC UP NO-UNIPROT TTFNSPC UC NOUNIPROTAC TTFNSPC GN NO-GeName TTFNSPC TT Literature-reported TT2AMHT ID TT2AMHT TT2AMHT TN Mitochondrial membrane (MIM) TT2AMHT UP Organelle/Cell TT2AMHT UC NOUNIPROTAC TT2AMHT GN NO-GeName TT2AMHT TT Literature-reported TTZRQHU ID TTZRQHU TTZRQHU TN Monocyte derived cytokine (MDC) TTZRQHU UP Family TTZRQHU UC NOUNIPROTAC TTZRQHU GN NO-GeName TTZRQHU TT Literature-reported TT9LCI1 ID TT9LCI1 TT9LCI1 TN Mothers against decapentaplegic homolog (SMAD) TT9LCI1 UP Family TT9LCI1 UC NOUNIPROTAC TT9LCI1 GN NO-GeName TT9LCI1 TT Literature-reported TTDPZCU ID TTDPZCU TTDPZCU TN Motoneuronotrophic factor (MNTF) TTDPZCU UP Family TTDPZCU UC NOUNIPROTAC TTDPZCU GN NO-GeName TTDPZCU TT Literature-reported TT5WVU2 ID TT5WVU2 TT5WVU2 TN mRNA-decapping enzyme (DCP) TT5WVU2 UP Family TT5WVU2 UC NOUNIPROTAC TT5WVU2 GN NO-GeName TT5WVU2 TT Literature-reported TT3V4L8 ID TT3V4L8 TT3V4L8 TN Mycobacterial lipoarabinomannan (MycB LAM) TT3V4L8 UP Other molecule TT3V4L8 UC NOUNIPROTAC TT3V4L8 GN NOUNIPROTAC TT3V4L8 TT Preclinical TT1OQ4F ID TT1OQ4F TT1OQ4F TN NEDD4-like E3 ubiquitin-protein ligase WWP (WWP) TT1OQ4F UP Family TT1OQ4F UC NOUNIPROTAC TT1OQ4F GN NO-GeName TT1OQ4F TT Literature-reported TT9142J ID TT9142J TT9142J TN Neisseria gonorrhoeae Enoyl-[acyl-carrier-protein] reductase (Neisseria fabI) TT9142J UP D6H5M4 TT9142J UC D6H5M4_NEIGO TT9142J GN NOUNIPROTAC TT9142J EC EC 1.3.1.9 TT9142J SQ MGFLQGKKILITGMISERSIAYGIAKACREQGAELAFTYVVDKLEERVRKMAAELDSELVFRCDVASDDEINQVFADLGKHWDGLDGLVHSIGFAPKEALSGDFLDSISREAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSYLGAVRAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIADFGKLLGHVAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDGGYSINALSTEG TT9142J TT Preclinical TTCDKBP ID TTCDKBP TTCDKBP TN Non-steroidal androgen synthesis (NSAD synth) TTCDKBP UP Pathway/Process TTCDKBP UC NOUNIPROTAC TTCDKBP GN NO-GeName TTCDKBP TT Literature-reported TTVH35R ID TTVH35R TTVH35R TN Opsin (OP) TTVH35R UP Family TTVH35R UC NOUNIPROTAC TTVH35R GN NO-GeName TTVH35R TT Literature-reported TTJNPTK ID TTJNPTK TTJNPTK TN Plasmodium Cysteine protease falcipain (Malaria CPF) TTJNPTK UP Family TTJNPTK UC NOUNIPROTAC TTJNPTK GN NO-GeName TTJNPTK TT Literature-reported TTU8Q3Y ID TTU8Q3Y TTU8Q3Y TN Plasmodium Gametocytogenesis (Plasm Gamet) TTU8Q3Y UP Pathway/Process TTU8Q3Y UC NOUNIPROTAC TTU8Q3Y GN NO-GeName TTU8Q3Y TT Literature-reported TTXLO8T ID TTXLO8T TTXLO8T TN Potential penetration (PP) TTXLO8T UP Pathway/Process TTXLO8T UC NOUNIPROTAC TTXLO8T GN NO-GeName TTXLO8T TT Literature-reported TTC4QIX ID TTC4QIX TTC4QIX TN Pro-inflammatory autologous messenger (PAM) TTC4QIX UP Pathway/Process TTC4QIX UC NOUNIPROTAC TTC4QIX GN NO-GeName TTC4QIX TT Literature-reported TTX1Z4P ID TTX1Z4P TTX1Z4P TN Prostaglandin metabolism (PG metab) TTX1Z4P UP Pathway/Process TTX1Z4P UC NOUNIPROTAC TTX1Z4P GN NO-GeName TTX1Z4P TT Literature-reported TTGSRBC ID TTGSRBC TTGSRBC TN Prostaglandin synthetase (PGS) TTGSRBC UP Family TTGSRBC UC NOUNIPROTAC TTGSRBC GN NO-GeName TTGSRBC TT Literature-reported TT6AS9F ID TT6AS9F TT6AS9F TN Protein phosphorylation (PP) TT6AS9F UP Pathway/Process TT6AS9F UC NOUNIPROTAC TT6AS9F GN NO-GeName TT6AS9F TT Literature-reported TTV8ETH ID TTV8ETH TTV8ETH TN Protein prenyl transferase (PPTF) TTV8ETH UP Family TTV8ETH UC NOUNIPROTAC TTV8ETH GN NO-GeName TTV8ETH TT Literature-reported TTVX670 ID TTVX670 TTVX670 TN Protein translation (hPT) TTVX670 UP Pathway/Process TTVX670 UC NOUNIPROTAC TTVX670 GN NO-GeName TTVX670 TT Literature-reported TTM852O ID TTM852O TTM852O TN S100A6/p38/MAPK signaling pathway (SpM pathway) TTM852O UP Pathway/Process TTM852O UC NOUNIPROTAC TTM852O GN NO-GeName TTM852O TT Literature-reported TTBC12P ID TTBC12P TTBC12P TN Sonic hedgehog pathway (Shh pathway) TTBC12P UP Pathway/Process TTBC12P UC NOUNIPROTAC TTBC12P GN NO-GeName TTBC12P TT Literature-reported TTWPX3M ID TTWPX3M TTWPX3M TN Staphylococcus Accessory gene regulator protein A (Stap-coc agrA) TTWPX3M UP P0A0I7 TTWPX3M UC AGRA_STAAU TTWPX3M GN Stap-coc agrA TTWPX3M FC Required for high-level post-exponential phase expression of a series of secreted proteins. TTWPX3M SQ MKIFICEDDPKQRENMVTIIKNYIMIEEKPMEIALATDNPYEVLEQAKNMNDIGCYFLDIQLSTDINGIKLGSEIRKHDPVGNIIFVTSHSELTYLTFVYKVAAMDFIFKDDPAELRTRIIDCLETAHTRLQLLSKDNSVETIELKRGSNSVYVQYDDIMFFESSTKSHRLIAHLDNRQIEFYGNLKELSQLDDRFFRCHNSFVVNRHNIESIDSKERIVYFKNKEHCYASVRNVKKI TTWPX3M TT Preclinical TTQDJCS ID TTQDJCS TTQDJCS TN Streptococcus Capsular antigen (Stre CA) TTQDJCS UP NO-UNIPROT TTQDJCS UC NOUNIPROTAC TTQDJCS GN NO-GeName TTQDJCS TT Literature-reported TT6HNB8 ID TT6HNB8 TT6HNB8 TN Stretch-gated ion channel (MSC) TT6HNB8 UP Family TT6HNB8 UC NOUNIPROTAC TT6HNB8 GN NO-GeName TT6HNB8 TT Literature-reported TTBLN9S ID TTBLN9S TTBLN9S TN Sulfur mustard-stimulated protease (SMSP) TTBLN9S UP Family TTBLN9S UC NOUNIPROTAC TTBLN9S GN NO-GeName TTBLN9S TT Literature-reported TTTPKA5 ID TTTPKA5 TTTPKA5 TN Thyroid hormone synthesis (TH synth) TTTPKA5 UP Pathway/Process TTTPKA5 UC NOUNIPROTAC TTTPKA5 GN NO-GeName TTTPKA5 TT Literature-reported TTAXYDF ID TTAXYDF TTAXYDF TN TLR signaling pathway (TLR pathway) TTAXYDF UP Pathway/Process TTAXYDF UC NOUNIPROTAC TTAXYDF GN NO-GeName TTAXYDF TT Literature-reported TTU81IF ID TTU81IF TTU81IF TN Transporter unspecfic (TP) TTU81IF UP Family TTU81IF UC NOUNIPROTAC TTU81IF GN NO-GeName TTU81IF TT Literature-reported TT8579I ID TT8579I TT8579I TN Tumor necrosis factor synthesis (TNF synth) TT8579I UP Pathway/Process TT8579I UC NOUNIPROTAC TT8579I GN NO-GeName TT8579I TT Literature-reported TTCLA5K ID TTCLA5K TTCLA5K TN Type II transmembrane serine proteases (TTSP) TTCLA5K UP Family TTCLA5K UC NOUNIPROTAC TTCLA5K GN NO-GeName TTCLA5K TT Literature-reported TT3KL5X ID TT3KL5X TT3KL5X TN Ubiquitin-proteasome pathway (UP pathway) TT3KL5X UP Pathway/Process TT3KL5X UC NOUNIPROTAC TT3KL5X GN NO-GeName TT3KL5X TT Literature-reported TT3MSAO ID TT3MSAO TT3MSAO TN HUMAN cholinesterase (BCHE) TT3MSAO UP P06276 TT3MSAO UC CHLE_HUMAN TT3MSAO BC Type-B carboxylesterase/lipase TT3MSAO SN Pseudocholinesterase; Choline esterase II; CHE1; Butyrylcholine esterase; Acylcholine acylhydrolase TT3MSAO GN BCHE TT3MSAO FC Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. TT3MSAO EC EC 3.1.1.8 TT3MSAO PD 6QAE; 6QAD; 6QAC; 6QAB; 6QAA TT3MSAO SQ MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCVGL TTG01U6 ID TTG01U6 TTG01U6 TN HUMAN c-reactive protein (CRP) TTG01U6 UP P02741 TTG01U6 UC CRP_HUMAN TTG01U6 BC Pentraxin family TTG01U6 SN C reactive protein TTG01U6 GN CRP; PTX1 TTG01U6 FC Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. TTG01U6 PD 1B09; 1GNH; 1LJ7; 3L2Y; 3PVN TTG01U6 SQ MEKLLCFLVLTSLSHAFGQTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP TTBJZ7D ID TTBJZ7D TTBJZ7D TN HUMAN interleukin-1 beta (IL1B) TTBJZ7D UP P01584 TTBJZ7D UC IL1B_HUMAN TTBJZ7D BC Cytokine: interleukin TTBJZ7D SN IL1F2; IL-1beta; IL-1 beta; Catabolin TTBJZ7D GN IL1B TTBJZ7D FC Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. Potent proinflammatory cytokine. TTBJZ7D PD 9ILB; 7I1B; 6I1B; 5MVZ; 5I1B TTBJZ7D SQ MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS TTBJZ7D FM Interleukin TT4NHTB ID TT4NHTB TT4NHTB TN HUMAN interleukin-10 (IL10) TT4NHTB UP P22301 TT4NHTB UC IL10_HUMAN TT4NHTB BC Cytokine: interleukin TT4NHTB SN IL-10; Cytokine synthesis inhibitory factor; CSIF TT4NHTB GN IL10 TT4NHTB FC Mechanistically, IL10 binds to its heterotetrameric receptor comprising IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of STAT3. In turn, STAT3 translocates to the nucleus where it drives expression of anti-inflammatory mediators. Targets antigen-presenting cells (APCs) such as macrophages and monocytes and inhibits their release of pro-inflammatory cytokines including granulocyte-macrophage colony-stimulating factor /GM-CSF, granulocyte colony-stimulating factor/G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha. Interferes also with antigen presentation by reducing the expression of MHC-class II and co-stimulatory molecules, thereby inhibiting their ability to induce T cell activation. In addition, controls the inflammatory response of macrophages by reprogramming essential metabolic pathways including mTOR signaling. Major immune regulatory cytokine that acts on many cells of the immune system where it has profound anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. TT4NHTB PD 2ILK; 2H24; 1Y6K; 1LK3; 1J7V TT4NHTB SQ MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN TTW86QI ID TTW86QI TTW86QI TN HUMAN tumor necrosis factor (TNF) TTW86QI UP P01375 TTW86QI UC TNFA_HUMAN TTW86QI BC Cytokine: tumor necrosis factor TTW86QI SN Tumour necrosis factor alpha; Tumour necrosis factor; Tumor necrosis factor ligand superfamily member 2; TNFalpha; TNFSF2; TNFA; TNF-alpha; TNF-a; TNF alpha; Cachectin TTW86QI GN TNF TTW86QI FC It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Upregulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective. Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line. Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance. Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. TTW86QI PD 5YOY; 5WUX; 5UUI; 5TSW; 5MU8 TTW86QI SQ MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL TTQTSFR ID TTQTSFR TTQTSFR TN HUMAN l-lactate dehydrogenase (LDH) TTQTSFR UP P00338; P07195; P07864 TTQTSFR UC LDHA_HUMAN; LDHB_HUMAN; LDHC_HUMAN TTQTSFR BC Short-chain dehydrogenases reductase TTQTSFR SN Renal carcinoma antigen NY-REN; LDH TTQTSFR GN LDHA; LDHB; LDHC TTQTSFR FC Catalyzes the conversion of lactate to pyruvate and back, as it converts NAD+ to NADH and back. Expressed extensively in body tissues, such as blood cells and heart muscle. Functions asa marker of common injuries and disease such as heart failure because it is released during tissue damage TTQTSFR SQ MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF TTC2DS7 ID TTC2DS7 TTC2DS7 TN COVID-19 non-structural protein 14 (nsp14) TTC2DS7 UP P0DTD1 (59266452) TTC2DS7 UC R1AB_SARS2 TTC2DS7 BC Coronaviruses polyprotein 1ab family TTC2DS7 SN COVID-19 Proofreading exoribonuclease; COVID-19 ExoN; COVID-19 Guanine-N7 methyltransferase TTC2DS7 GN COVID-19 rep TTC2DS7 FC Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens. TTC2DS7 EC EC 3.1.13.- TTC2DS7 SQ AENVTGLFKDCSKVITGLHPTQAPTHLSVDTKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFITREEAIRHVRAWIGFDVEGCHATREAVGTNLPLQLGFSTGVNLVAVPTGYVDTPNNTDFSRVSAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSDTLKNLSDRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDRRATCFSTASDTYACWHHSIGFDYVYNPFMIDVQQWGFTGNLQSNHDLYCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWTIEYPIIGDELKINAACRKVQHMVVKAALLADKFPVLHDIGNPKAIKCVPQADVEWKFYDAQPCSDKAYKIEELFYSYATHSDKFTDGVCLFWNCNVDRYPANSIVCRFDTRVLSNLNLPGCDGGSLYVNKHAFHTPAFDKSAFVNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRHHANEYRLYLDAYNMMISAGFSLWVYKQFDTYNLWNTFTRLQ TTS824E ID TTS824E TTS824E TN COVID-19 replicase polyprotein 1ab (pp1ab) TTS824E UP P0DTD1 TTS824E UC R1AB_SARS2 TTS824E BC Coronaviruses polyprotein 1ab family TTS824E SN ORF1ab polyprotein; pp1ab TTS824E GN COVID-19 rep TTS824E FC Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. TTGL3J0 ID TTGL3J0 TTGL3J0 TN COVID-19 ribonucleic acid (RNA) TTGL3J0 UP Other molecule TTDBOI7 ID TTDBOI7 TTDBOI7 TN HUAMN alpha-1 adrenergic receptor (ADRA1) TTDBOI7 UP P35348; P35368; P25100 TTDBOI7 UC ADA1A_HUMAN; ADA1B_HUMAN; ADA1D_HUMAN TTDBOI7 BC Adrenergic receptor subfamily TTDBOI7 SN Alpha-1 adrenoreceptor TTDBOI7 GN ADRA1A; ADRA1B; ADRA1D TTDBOI7 FC This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes. TTDBOI7 SQ MVFLSGNASDSSNCTQPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV TTXQ1JS ID TTXQ1JS TTXQ1JS TN HUAMN eIF4E-eIF4G interaction (eIF4E-eIF4G) TTXQ1JS UP Pathway/Process TTCLGZ8 ID TTCLGZ8 TTCLGZ8 TN HUAMN monocyte differentiation antigen CD14 (CD14) TTCLGZ8 UP P08571 TTCLGZ8 UC CD14_HUMAN TTCLGZ8 SN Myeloid cell-specific leucine-rich glycoprotein TTCLGZ8 GN CD14 TTCLGZ8 FC In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-). Coreceptor for bacterial lipopolysaccharide. TTCLGZ8 PD 4GLP TTCLGZ8 SQ MERASCLLLLLLPLVHVSATTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVDADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKITGTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAFSCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCAALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKLRVLDLSCNRLNRAPQPDELPEVDNLTLDGNPFLVPGTALPHEGSMNSGVVPACARSTLSVGVSGTLVLLQGARGFA TTK9LUQ ID TTK9LUQ TTK9LUQ TN HUAMN serine protease factor Xa (SERPINA5) TTK9LUQ UP P05154 TTK9LUQ UC IPSP_HUMAN TTK9LUQ BC Serpin family TTK9LUQ SN Plasma serine protease inhibitor; Acrosomal serine protease inhibitor; Plasminogen activator inhibitor 3; PAI-3; PAI3; Protein C inhibitor; PCI; Serpin A5 TTK9LUQ GN SERPINA5; PCI; PLANH3; PROCI TTK9LUQ FC Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and proinflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. TTK9LUQ PD 1LQ8; 2HI9; 2OL2 TTK9LUQ SQ MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRP TT67OLB ID TT67OLB TT67OLB TN HUMAN calcitonin gene-related peptide type 1 receptor (CALCRL) TT67OLB UP Q16602 TT67OLB UC CALRL_HUMAN TT67OLB BC GPCR secretin TT67OLB SN Calcitonin receptor-like receptor; Calcitonin gene-related peptide type 1 receptor; CGRPR; CGRP type 1 receptor TT67OLB GN CALCRL TT67OLB FC Receptor for calcitonin-gene-related peptide (CGRP) together with RAMP1 and receptor for adrenomedullin together with RAMP3 (By similarity). Receptor for adrenomedullin together with RAMP2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. TT67OLB PD 6E3Y; 6D1U; 5V6Y; 4RWG; 4RWF TT67OLB SQ MEKKCTLNFLVLLPFFMILVTAELEESPEDSIQLGVTRNKIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLTIIGHGLSIASLLISLGIFFYFKSLSCQRITLHKNLFFSFVCNSVVTIIHLTAVANNQALVATNPVSCKVSQFIHLYLMGCNYFWMLCEGIYLHTLIVVAVFAEKQHLMWYYFLGWGFPLIPACIHAIARSLYYNDNCWISSDTHLLYIIHGPICAALLVNLFFLLNIVRVLITKLKVTHQAESNLYMKAVRATLILVPLLGIEFVLIPWRPEGKIAEEVYDYIMHILMHFQGLLVSTIFCFFNGEVQAILRRNWNQYKIQFGNSFSNSEALRSASYTVSTISDGPGYSHDCPSEHLNGKSIHDIENVLLKPENLYN TTJQV83 ID TTJQV83 TTJQV83 TN HUMAN creatinine (CREA) TTJQV83 UP Other molecule TTM6Z3L ID TTM6Z3L TTM6Z3L TN HUMAN cystatin C (CysC) TTM6Z3L UP Other molecule TTSB6CA ID TTSB6CA TTSB6CA TN HUMAN cysteinyl leukotriene receptor (CysLTR) TTSB6CA UP Q9Y271; Q9NS75 TTSB6CA UC CLTR1_HUMAN; CLTR2_HUMAN TTSB6CA BC G-protein coupled receptor 1 family TTSB6CA GN CYSLTR1; CYSLTR2 TTSB6CA FC Receptor for cysteinyl leukotrienes mediating bronchoconstriction of individuals with and without asthma. Stimulation by LTD4 results in the contraction and proliferation of smooth muscle, edema, eosinophil migration and damage to the mucus layer in the lung. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. TTSB6CA SQ MDETGNLTVSSATCHDTIDDFRNQVYSTLYSMISVVGFFGNGFVLYVLIKTYHKKSAFQVYMINLAVADLLCVCTLPLRVVYYVHKGIWLFGDFLCRLSTYALYVNLYCSIFFMTAMSFFRCIAIVFPVQNINLVTQKKARFVCVGIWIFVILTSSPFLMAKPQKDEKNNTKCFEPPQDNQTKNHVLVLHYVSLFVGFIIPFVIIIVCYTMIILTLLKKSMKKNLSSHKKAIGMIMVVTAAFLVSFMPYHIQRTIHLHFLHNETKPCDSVLRMQKSVVITLSLAASNCCFDPLLYFFSGGNFRKRLSTFRKHSLSSVTYVPRKKASLPEKGEEICKV TTQ9J6R ID TTQ9J6R TTQ9J6R TN HUMAN dipeptidyl peptidase 1 (CTSC) TTQ9J6R UP P53634 TTQ9J6R UC CATC_HUMAN TTQ9J6R BC Peptidase TTQ9J6R SN Dipeptidyl transferase; Dipeptidyl peptidase 1; DPPI; DPP-I; Cysteine protease dipeptidyl peptidase I; Cathepsin J; Cathepsin C; CPPI TTQ9J6R GN CTSC TTQ9J6R FC Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII. Thiol protease. TTQ9J6R EC EC 3.4.14.1 TTQ9J6R PD 4OEM; 4OEL; 4CDF; 4CDE; 4CDD TTQ9J6R SQ MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL TTAHMI6 ID TTAHMI6 TTAHMI6 TN HUMAN estrogen receptor (ESR1) TTAHMI6 UP P03372 TTAHMI6 UC ESR1_HUMAN TTAHMI6 BC Nuclear hormone receptor TTAHMI6 SN Nuclear receptor subfamily 3 group A member 1; NR3A1; Estradiol receptor; ESR; ER-alpha; ER TTAHMI6 GN ESR1 TTAHMI6 FC Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full-length receptor. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3. Isoform 3 can bind to ERE and inhibit isoform 1. TTAHMI6 PD 6IAR; 6HMU; 6HKF; 6HKB; 6HHP TTAHMI6 SQ MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV TT9P1CK ID TT9P1CK TT9P1CK TN HUMAN mineralocorticoid receptor (MR) TT9P1CK UP P08235 TT9P1CK UC MCR_HUMAN TT9P1CK BC Nuclear hormone receptor TT9P1CK SN Nuclear receptor subfamily 3 group C member 2; Mineralocorticoid receptor; MLR; MCR; Inner ear mineralocorticoid receptor; Delta TT9P1CK GN NR3C2 TT9P1CK FC Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels. Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. TT9P1CK PD 6GGG; 6GG8; 6GEV; 5MWY; 5MWP TT9P1CK SQ METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNSTQGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYEQQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAVVKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPNVENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSPANINNSRCSVSSPSNTNNRSTLSSPAASTVGSICSPVNNAFSYTASGTSAGSSTLRDVVPSPDTQEKGAQEVPFPKTEEVESAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNSKINSDSSFSVPIKQESTKHSCSGTSFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGFDGNCEGSGFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSARDQSFQHLSSFPPVNTLVESWKSHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPSKICLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRLQKCLQAGMNLGARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEEGTTYIAPAKEPSVNTALVPQLSTISRALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKCPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAMLVEIISDQLPKVESGNAKPLYFHRK TT0S3MP ID TT0S3MP TT0S3MP TN HUMAN phosphatidylinositol 3-phosphate 5-kinase (PIKfyve) TT0S3MP UP Q9Y2I7 TT0S3MP UC FYV1_HUMAN TT0S3MP SN Type III PIP kinase; Phosphatidylinositol 3-phosphate 5-kinase type III; PIPkin-III; PIKfyve; FYVE finger-containing phosphoinositide kinase TT0S3MP GN PIKFYVE TT0S3MP FC The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. Plays a role in the biogenesis of endosome carrier vesicles (ECV)/ multivesicular bodies (MVB) transport intermediates from early endosomes. TT0S3MP EC EC 2.7.1.150 TT0S3MP SQ MATDDKTSPTLDSANDLPRSPTSPSHLTHFKPLTPDQDEPPFKSAYSSFVNLFRFNKERAEGGQGEQQPLSGSWTSPQLPSRTQSVRSPTPYKKQLNEELQRRSSALDTRRKAEPTFGGHDPRTAVQLRSLSTVLKRLKEIMEGKSQDSDLKQYWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRKIALSYAHSTDSNSIGEDLNALSDSACSVSVLDPSEPRTPVGSRKASRNIFLEDDLAWQSLIHPDSSNTPLSTRLVSVQEDAGKSPARNRSASITNLSLDRSGSPMVPSYETSVSPQANRTYVRTETTEDERKILLDSVQLKDLWKKICHHSSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDQLFRDEYALYRPLQSTEFSETPSPDSDSVNSVEGHSEPSWFKDIKFDDSDTEQIAEEGDDNLANSASPSKRTSVSSFQSTVDSDSAASISLNVELDNVNFHIKKPSKYPHVPPHPADQKEYLISDTGGQQLSISDAFIKESLFNRRVEEKSKELPFTPLGWHHNNLELLREENGEKQAMERLLSANHNHMMALLQQLLHSDSLSSSWRDIIVSLVCQVVQTVRPDVKNQDDDMDIRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIEYLYREETKFTCIDPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVMSMDQLLTKPHLGTCHKFYMQIFQLPNEQTKTLMFFEGCPQHLGCTIKLRGGSDYELARVKEILIFMICVAYHSQLEISFLMDEFAMPPTLMQNPSFHSLIEGRGHEGAVQEQYGGGSIPWDPDIPPESLPCDDSSLLELRIVFEKGEQENKNLPQAVASVKHQEHSTTACPAGLPCAFFAPVPESLLPLPVDDQQDALGSEQPETLQQTVVLQDPKSQIRAFRDPLQDDTGLYVTEEVTSSEDKRKTYSLAFKQELKDVILCISPVITFREPFLLTEKGMRCSTRDYFAEQVYWSPLLNKEFKEMENRRKKQLLRDLSGLQGMNGSIQAKSIQVLPSHELVSTRIAEHLGDSQSLGRMLADYRARGGRIQPKNSDPFAHSKDASSTSSGQSGSKNEGDEERGLILSDAVWSTKVDCLNPINHQRLCVLFSSSSAQSSNAPSACVSPWIVTMEFYGKNDLTLGIFLERYCFRPSYQCPSMFCDTPMVHHIRRFVHGQGCVQIILKELDSPVPGYQHTILTYSWCRICKQVTPVVALSNESWSMSFAKYLELRFYGHQYTRRANAEPCGHSIHHDYHQYFSYNQMVASFSYSPIRLLEVCVPLPKIFIKRQAPLKVSLLQDLKDFFQKVSQVYVAIDERLASLKTDTFSKTREEKMEDIFAQKEMEEGEFKNWIEKMQARLMSSSVDTPQQLQSVFESLIAKKQSLCEVLQAWNNRLQDLFQQEKGRKRPSVPPSPGRLRQGEESKISAMDASPRNISPGLQNGEKEDRFLTTLSSQSSTSSTHLQLPTPPEVMSEQSVGGPPELDTASSSEDVFDGHLLGSTDSQVKEKSTMKAIFANLLPGNSYNPIPFPFDPDKHYLMYEHERVPIAVCEKEPSSIIAFALSCKEYRNALEELSKATQWNSAEEGLPTNSTSDSRPKSSSPIRLPEMSGGQTNRTTETEPQPTKKASGMLSFFRGTAGKSPDLSSQKRETLRGADSAYYQVGQTGKEGTENQGVEPQDEVDGGDTQKKQLINPHVELQFSDANAKFYCRLYYAGEFHKMREVILDSSEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYITNAVQQKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENLLKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTFTWDKKLEMVVKSTGILGGQGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTGLGLNC TTVLU5N ID TTVLU5N TTVLU5N TN HUMAN programmed cell death protein 1 (PD-1) TTVLU5N UP Q15116 TTVLU5N UC PDCD1_HUMAN TTVLU5N BC Immunoglobulin TTVLU5N SN hPD1; hPD-1; Protein PD1; Protein PD-1; PD1; CD279 TTVLU5N GN PDCD1 TTVLU5N FC Delivers inhibitory signals upon binding to ligands CD274/PDCD1L1 and CD273/PDCD1LG2. Following T-cell receptor (TCR) engagement, PDCD1 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation. Suppresses T-cell activation through the recruitment of PTPN11/SHP-2: following ligand-binding, PDCD1 is phosphorylated within the ITSM motif, leading to the recruitment of the protein tyrosine phosphatase PTPN11/SHP-2 that mediates dephosphorylation of key TCR proximal signaling molecules, such as ZAP70, PRKCQ/PKCtheta and CD247/CD3zeta. Inhibitory receptor on antigen activated T-cells that plays a critical role in induction and maintenance of immune tolerance to self. TTVLU5N PD 5WT9; 5JXE; 5IUS; 5GGS; 5GGR TTVLU5N SQ MQIPQAPWPVVWAVLQLGWRPGWFLDSPDRPWNPPTFSPALLVVTEGDNATFTCSFSNTSESFVLNWYRMSPSNQTDKLAAFPEDRSQPGQDCRFRVTQLPNGRDFHMSVVRARRNDSGTYLCGAISLAPKAQIKESLRAELRVTERRAEVPTAHPSPSPRPAGQFQTLVVGVVGGLLGSLVLLVWVLAVICSRAARGTIGARRTGQPLKEDPSAVPVFSVDYGELDFQWREKTPEPPVPCVPEQTEYATIVFPSGMGTSSPARRGSADGPRSAQPLRPEDGHCSWPL TTV50LE ID TTV50LE TTV50LE TN HUMAN serum direct bilirubin (DBIL) TTV50LE UP Other molecule TTEKDU8 ID TTEKDU8 TTEKDU8 TN HUMAN serum urea (SeU) TTEKDU8 UP Other molecule